data_4QIY
# 
_entry.id   4QIY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.381 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
RCSB  RCSB086113   ?            ?                   
PDB   4QIY         pdb_00004qiy 10.2210/pdb4qiy/pdb 
WWPDB D_1000086113 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4QIZ . unspecified 
PDB 4QJ0 . unspecified 
PDB 4QJM . unspecified 
PDB 4QJO . unspecified 
PDB 4QJP . unspecified 
PDB 4QJW . unspecified 
PDB 4QJX . unspecified 
PDB 4QTL . unspecified 
# 
_pdbx_database_status.entry_id                        4QIY 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2014-06-03 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Manakova, E.' 1 
'Smirnov, A.'  2 
'Grazulis, S.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties toward Carbonic Anhydrases' 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_volume            10 
_citation.page_first                662 
_citation.page_last                 687 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   DE 
_citation.journal_id_ISSN           1860-7179 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25758852 
_citation.pdbx_database_id_DOI      10.1002/cmdc.201402490 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dudutiene, V.'     1  ? 
primary 'Zubriene, A.'      2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Timm, D.D.'        4  ? 
primary 'Smirnoviene, J.'   5  ? 
primary 'Kazokaite, J.'     6  ? 
primary 'Michailoviene, V.' 7  ? 
primary 'Zaksauskas, A.'    8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
_cell.entry_id           4QIY 
_cell.length_a           73.594 
_cell.length_b           41.206 
_cell.length_c           84.047 
_cell.angle_alpha        90.000 
_cell.angle_beta         109.300 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              4 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4QIY 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.Int_Tables_number                1 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                                                          
29289.062 4    4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                                                                      
65.409    4    ?       ? ? ? 
3 non-polymer syn '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' 
530.537   4    ?       ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                            
78.133    4    ?       ? ? ? 
5 non-polymer syn BICINE                                                                                                          
163.172   4    ?       ? ? ? 
6 water       nat water                                                                                                           
18.015    1013 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4QIY A 1 ? 260 ? P00918 1 ? 260 ? 1 261 
2 1 4QIY B 1 ? 260 ? P00918 1 ? 260 ? 1 261 
3 1 4QIY C 1 ? 260 ? P00918 1 ? 260 ? 1 261 
4 1 4QIY D 1 ? 260 ? P00918 1 ? 260 ? 1 261 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'          133.103 
BCN non-polymer         . BICINE ? 'C6 H13 N O4'         163.172 
CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'           78.133  
GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER ? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'         117.146 
WWX non-polymer         . 
'2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' ? 
'C22 H21 F3 N2 O6 S2' 530.537 
ZN  non-polymer         . 'ZINC ION' ? 'Zn 2'                65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          4QIY 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   38.2 
_exptl_crystal.density_Matthews      2.0 
_exptl_crystal.pdbx_mosaicity        0.19 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium BICINE, pH 9, 0.2M ammonium sulfate, 2M sodium malonate pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 291K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS 6M' 
_diffrn_detector.pdbx_collection_date   2012-12-02 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    
;High Heat Load (HHL) Monochromator: Si 111; Large Offset Monochromator (LOM) 
: Si 311, Si 511
;
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
# 
_reflns.entry_id                     4QIY 
_reflns.d_resolution_high            1.300 
_reflns.d_resolution_low             79.324 
_reflns.pdbx_number_measured_all     786555 
_reflns.number_all                   ? 
_reflns.number_obs                   206964 
_reflns.pdbx_netI_over_av_sigmaI     10.792 
_reflns.pdbx_netI_over_sigmaI        13.000 
_reflns.pdbx_Rsym_value              0.032 
_reflns.pdbx_redundancy              3.800 
_reflns.percent_possible_obs         90.300 
_reflns.pdbx_Rrim_I_all              0.044 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_CC_half                 ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
1.30 1.37  ? 114646 ? ? 0.286 2.7  0.286 ? 3.80 ? 3.40  ? 30039 ? ? 0.402 ? 89.60 0.40 0.20 1  1 ? 
1.37 1.45  ? 102653 ? ? 0.198 3.9  0.198 ? 3.70 ? 4.40  ? 27678 ? ? 0.278 ? 87.20 0.28 0.14 2  1 ? 
1.45 1.55  ? 101661 ? ? 0.129 6.0  0.129 ? 3.80 ? 6.30  ? 26658 ? ? 0.182 ? 89.70 0.18 0.09 3  1 ? 
1.55 1.68  ? 97059  ? ? 0.085 8.9  0.085 ? 3.80 ? 8.80  ? 25269 ? ? 0.121 ? 91.20 0.12 0.06 4  1 ? 
1.68 1.84  ? 84925  ? ? 0.055 13.1 0.055 ? 3.70 ? 12.00 ? 22703 ? ? 0.079 ? 88.70 0.08 0.04 5  1 ? 
1.84 2.06  ? 81957  ? ? 0.037 17.3 0.037 ? 3.80 ? 17.50 ? 21321 ? ? 0.053 ? 92.40 0.05 0.03 6  1 ? 
2.06 2.37  ? 72463  ? ? 0.030 19.6 0.030 ? 3.90 ? 22.80 ? 18768 ? ? 0.042 ? 92.50 0.04 0.02 7  1 ? 
2.37 2.91  ? 57534  ? ? 0.026 20.4 0.026 ? 3.70 ? 25.30 ? 15367 ? ? 0.036 ? 89.50 0.04 0.02 8  1 ? 
2.91 4.11  ? 48315  ? ? 0.021 21.9 0.021 ? 3.90 ? 32.50 ? 12451 ? ? 0.028 ? 93.70 0.03 0.01 9  1 ? 
4.11 79.32 ? 25342  ? ? 0.018 22.3 0.018 ? 3.80 ? 29.90 ? 6710  ? ? 0.025 ? 92.70 0.03 0.01 10 1 ? 
# 
_refine.entry_id                                 4QIY 
_refine.ls_d_res_high                            1.300 
_refine.ls_d_res_low                             69.460 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    90.240 
_refine.ls_number_reflns_obs                     206936 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES' 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.155 
_refine.ls_R_factor_R_work                       0.151 
_refine.ls_wR_factor_R_work                      0.156 
_refine.ls_R_factor_R_free                       0.192 
_refine.ls_wR_factor_R_free                      0.199 
_refine.ls_percent_reflns_R_free                 9.900 
_refine.ls_number_reflns_R_free                  20560 
_refine.ls_number_reflns_R_work                  186376 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               16.645 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.350 
_refine.aniso_B[2][2]                            -0.420 
_refine.aniso_B[3][3]                            0.140 
_refine.aniso_B[1][2]                            -0.060 
_refine.aniso_B[1][3]                            0.110 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.981 
_refine.correlation_coeff_Fo_to_Fc_free          0.972 
_refine.overall_SU_R_Cruickshank_DPI             0.066 
_refine.overall_SU_R_free                        0.061 
_refine.pdbx_overall_ESU_R                       0.066 
_refine.pdbx_overall_ESU_R_Free                  0.061 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.833 
_refine.B_iso_max                                85.73 
_refine.B_iso_min                                4.53 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.50 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      3HLJ 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8191 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         204 
_refine_hist.number_atoms_solvent             1013 
_refine_hist.number_atoms_total               9408 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        69.460 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' r_bond_refined_d       8981  0.023  0.020  ? ? 
'X-RAY DIFFRACTION' r_angle_refined_deg    12252 2.286  1.968  ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 1101  7.195  5.000  ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 411   36.231 24.720 ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 1451  12.922 15.000 ? ? 
'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 31    21.390 15.000 ? ? 
'X-RAY DIFFRACTION' r_chiral_restr         1269  0.182  0.200  ? ? 
'X-RAY DIFFRACTION' r_gen_planes_refined   7005  0.017  0.021  ? ? 
'X-RAY DIFFRACTION' r_rigid_bond_restr     8981  9.493  3.000  ? ? 
'X-RAY DIFFRACTION' r_sphericity_free      1017  17.064 5.000  ? ? 
'X-RAY DIFFRACTION' r_sphericity_bonded    8699  9.743  5.000  ? ? 
# 
_refine_ls_shell.d_res_high                       1.300 
_refine_ls_shell.d_res_low                        1.334 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               89.680 
_refine_ls_shell.number_reflns_R_work             13719 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.238 
_refine_ls_shell.R_factor_R_free                  0.285 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             1481 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                15200 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  4QIY 
_struct.title                     'Crystal structure of human carbonic anhydrase isozyme II with inhibitor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QIY 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, LYASE-LYASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'LYASE/LYASE INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 5 ? 
M N N 2 ? 
N N N 3 ? 
O N N 4 ? 
P N N 5 ? 
Q N N 2 ? 
R N N 3 ? 
S N N 4 ? 
T N N 5 ? 
U N N 6 ? 
V N N 6 ? 
W N N 6 ? 
X N N 6 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  GLY A 12  ? TRP A 16  ? GLY A 12  TRP A 16  5 ? 5 
HELX_P HELX_P2  2  PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3  3  LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4  4  ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5  5  LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6  6  LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7  7  ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8  8  ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9  9  SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
HELX_P HELX_P10 10 GLY B 12  ? ASP B 19  ? GLY B 12  ASP B 19  5 ? 8 
HELX_P HELX_P11 11 PHE B 20  ? GLY B 25  ? PHE B 20  GLY B 25  5 ? 6 
HELX_P HELX_P12 12 LYS B 126 ? GLY B 128 ? LYS B 127 GLY B 129 5 ? 3 
HELX_P HELX_P13 13 ASP B 129 ? VAL B 134 ? ASP B 130 VAL B 135 1 ? 6 
HELX_P HELX_P14 14 LYS B 153 ? GLY B 155 ? LYS B 154 GLY B 156 5 ? 3 
HELX_P HELX_P15 15 LEU B 156 ? LEU B 163 ? LEU B 157 LEU B 164 1 ? 8 
HELX_P HELX_P16 16 ASP B 164 ? LYS B 167 ? ASP B 165 LYS B 168 5 ? 4 
HELX_P HELX_P17 17 ASP B 179 ? LEU B 184 ? ASP B 180 LEU B 185 5 ? 6 
HELX_P HELX_P18 18 SER B 218 ? ARG B 226 ? SER B 219 ARG B 227 1 ? 9 
HELX_P HELX_P19 19 GLY C 12  ? ASP C 19  ? GLY C 12  ASP C 19  5 ? 8 
HELX_P HELX_P20 20 PHE C 20  ? GLY C 25  ? PHE C 20  GLY C 25  5 ? 6 
HELX_P HELX_P21 21 LYS C 126 ? GLY C 128 ? LYS C 127 GLY C 129 5 ? 3 
HELX_P HELX_P22 22 ASP C 129 ? VAL C 134 ? ASP C 130 VAL C 135 1 ? 6 
HELX_P HELX_P23 23 LYS C 153 ? GLY C 155 ? LYS C 154 GLY C 156 5 ? 3 
HELX_P HELX_P24 24 LEU C 156 ? LEU C 163 ? LEU C 157 LEU C 164 1 ? 8 
HELX_P HELX_P25 25 ASP C 164 ? LYS C 167 ? ASP C 165 LYS C 168 5 ? 4 
HELX_P HELX_P26 26 ASP C 179 ? LEU C 184 ? ASP C 180 LEU C 185 5 ? 6 
HELX_P HELX_P27 27 SER C 218 ? ARG C 226 ? SER C 219 ARG C 227 1 ? 9 
HELX_P HELX_P28 28 PHE D 20  ? GLY D 25  ? PHE D 20  GLY D 25  5 ? 6 
HELX_P HELX_P29 29 LYS D 126 ? GLY D 128 ? LYS D 127 GLY D 129 5 ? 3 
HELX_P HELX_P30 30 ASP D 129 ? VAL D 134 ? ASP D 130 VAL D 135 1 ? 6 
HELX_P HELX_P31 31 LYS D 153 ? GLY D 155 ? LYS D 154 GLY D 156 5 ? 3 
HELX_P HELX_P32 32 LEU D 156 ? LEU D 163 ? LEU D 157 LEU D 164 1 ? 8 
HELX_P HELX_P33 33 ASP D 164 ? LYS D 167 ? ASP D 165 LYS D 168 5 ? 4 
HELX_P HELX_P34 34 ASP D 179 ? LEU D 184 ? ASP D 180 LEU D 185 5 ? 6 
HELX_P HELX_P35 35 SER D 218 ? ARG D 226 ? SER D 219 ARG D 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc2  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc3  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 E ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F WWX . N4 ? ? A ZN  301 A WWX 302 1_555 ? ? ? ? ? ? ? 1.930 ? ? 
metalc5  metalc ? ? B HIS 94  NE2 ? ? ? 1_555 I ZN  . ZN ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc6  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 I ZN  . ZN ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc7  metalc ? ? B HIS 119 ND1 ? ? ? 1_555 I ZN  . ZN ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc8  metalc ? ? I ZN  .   ZN  ? ? ? 1_555 J WWX . N4 ? ? B ZN  301 B WWX 302 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
metalc9  metalc ? ? C HIS 94  NE2 ? ? ? 1_555 M ZN  . ZN ? ? C HIS 94  C ZN  301 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc10 metalc ? ? C HIS 96  NE2 ? ? ? 1_555 M ZN  . ZN ? ? C HIS 96  C ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc11 metalc ? ? C HIS 119 ND1 ? ? ? 1_555 M ZN  . ZN ? ? C HIS 119 C ZN  301 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc12 metalc ? ? M ZN  .   ZN  ? ? ? 1_555 N WWX . N4 ? ? C ZN  301 C WWX 302 1_555 ? ? ? ? ? ? ? 1.962 ? ? 
metalc13 metalc ? ? D HIS 94  NE2 ? ? ? 1_555 Q ZN  . ZN ? ? D HIS 94  D ZN  301 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc14 metalc ? ? D HIS 96  NE2 ? ? ? 1_555 Q ZN  . ZN ? ? D HIS 96  D ZN  301 1_555 ? ? ? ? ? ? ? 2.023 ? ? 
metalc15 metalc ? ? D HIS 119 ND1 ? ? ? 1_555 Q ZN  . ZN ? ? D HIS 119 D ZN  301 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc16 metalc ? ? Q ZN  .   ZN  ? ? ? 1_555 R WWX . N4 ? ? D ZN  301 D WWX 302 1_555 ? ? ? ? ? ? ? 1.933 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -2.69 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.42 
3 SER 29  B . ? SER 29  B PRO 30  B ? PRO 30  B 1 -2.40 
4 PRO 200 B . ? PRO 201 B PRO 201 B ? PRO 202 B 1 8.12  
5 SER 29  C . ? SER 29  C PRO 30  C ? PRO 30  C 1 -4.11 
6 PRO 200 C . ? PRO 201 C PRO 201 C ? PRO 202 C 1 12.93 
7 SER 29  D . ? SER 29  D PRO 30  D ? PRO 30  D 1 -3.66 
8 PRO 200 D . ? PRO 201 D PRO 201 D ? PRO 202 D 1 12.62 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 6  ? 
D ? 2  ? 
E ? 10 ? 
F ? 6  ? 
G ? 2  ? 
H ? 10 ? 
I ? 6  ? 
J ? 2  ? 
K ? 10 ? 
L ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2  ? parallel      
B 1 2  ? parallel      
B 2 3  ? anti-parallel 
B 3 4  ? anti-parallel 
B 4 5  ? parallel      
B 5 6  ? anti-parallel 
B 6 7  ? anti-parallel 
B 7 8  ? anti-parallel 
B 8 9  ? anti-parallel 
B 9 10 ? anti-parallel 
C 1 2  ? anti-parallel 
C 2 3  ? anti-parallel 
C 3 4  ? anti-parallel 
C 4 5  ? anti-parallel 
C 5 6  ? parallel      
D 1 2  ? parallel      
E 1 2  ? parallel      
E 2 3  ? anti-parallel 
E 3 4  ? anti-parallel 
E 4 5  ? parallel      
E 5 6  ? anti-parallel 
E 6 7  ? anti-parallel 
E 7 8  ? anti-parallel 
E 8 9  ? anti-parallel 
E 9 10 ? anti-parallel 
F 1 2  ? anti-parallel 
F 2 3  ? anti-parallel 
F 3 4  ? anti-parallel 
F 4 5  ? anti-parallel 
F 5 6  ? parallel      
G 1 2  ? parallel      
H 1 2  ? parallel      
H 2 3  ? anti-parallel 
H 3 4  ? anti-parallel 
H 4 5  ? parallel      
H 5 6  ? anti-parallel 
H 6 7  ? anti-parallel 
H 7 8  ? anti-parallel 
H 8 9  ? anti-parallel 
H 9 10 ? anti-parallel 
I 1 2  ? anti-parallel 
I 2 3  ? anti-parallel 
I 3 4  ? anti-parallel 
I 4 5  ? anti-parallel 
I 5 6  ? parallel      
J 1 2  ? parallel      
K 1 2  ? parallel      
K 2 3  ? anti-parallel 
K 3 4  ? anti-parallel 
K 4 5  ? parallel      
K 5 6  ? anti-parallel 
K 6 7  ? anti-parallel 
K 7 8  ? anti-parallel 
K 8 9  ? anti-parallel 
K 9 10 ? anti-parallel 
L 1 2  ? anti-parallel 
L 2 3  ? anti-parallel 
L 3 4  ? anti-parallel 
L 4 5  ? anti-parallel 
L 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
A 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
B 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
B 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
B 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
B 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
B 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
B 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
B 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
B 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
B 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
B 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
C 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
C 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
C 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
C 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
C 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
C 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
D 1  ASP B 32  ? ILE B 33  ? ASP B 32  ILE B 33  
D 2  THR B 108 ? VAL B 109 ? THR B 108 VAL B 109 
E 1  LYS B 39  ? TYR B 40  ? LYS B 39  TYR B 40  
E 2  LYS B 256 ? ALA B 257 ? LYS B 257 ALA B 258 
E 3  TYR B 190 ? GLY B 195 ? TYR B 191 GLY B 196 
E 4  VAL B 206 ? LEU B 211 ? VAL B 207 LEU B 212 
E 5  LEU B 140 ? VAL B 149 ? LEU B 141 VAL B 150 
E 6  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
E 7  THR B 87  ? TRP B 97  ? THR B 87  TRP B 97  
E 8  PHE B 66  ? PHE B 70  ? PHE B 66  PHE B 70  
E 9  SER B 56  ? ASN B 61  ? SER B 56  ASN B 61  
E 10 SER B 172 ? ASP B 174 ? SER B 173 ASP B 175 
F 1  LEU B 47  ? SER B 50  ? LEU B 47  SER B 50  
F 2  VAL B 78  ? GLY B 81  ? VAL B 78  GLY B 81  
F 3  THR B 87  ? TRP B 97  ? THR B 87  TRP B 97  
F 4  ALA B 116 ? ASN B 124 ? ALA B 116 ASN B 124 
F 5  LEU B 140 ? VAL B 149 ? LEU B 141 VAL B 150 
F 6  ILE B 215 ? VAL B 217 ? ILE B 216 VAL B 218 
G 1  ASP C 32  ? ILE C 33  ? ASP C 32  ILE C 33  
G 2  THR C 108 ? VAL C 109 ? THR C 108 VAL C 109 
H 1  LYS C 39  ? TYR C 40  ? LYS C 39  TYR C 40  
H 2  LYS C 256 ? ALA C 257 ? LYS C 257 ALA C 258 
H 3  TYR C 190 ? GLY C 195 ? TYR C 191 GLY C 196 
H 4  VAL C 206 ? LEU C 211 ? VAL C 207 LEU C 212 
H 5  LEU C 140 ? VAL C 149 ? LEU C 141 VAL C 150 
H 6  ALA C 116 ? ASN C 124 ? ALA C 116 ASN C 124 
H 7  THR C 87  ? TRP C 97  ? THR C 87  TRP C 97  
H 8  PHE C 66  ? PHE C 70  ? PHE C 66  PHE C 70  
H 9  SER C 56  ? ASN C 61  ? SER C 56  ASN C 61  
H 10 SER C 172 ? ASP C 174 ? SER C 173 ASP C 175 
I 1  LEU C 47  ? SER C 50  ? LEU C 47  SER C 50  
I 2  VAL C 78  ? GLY C 81  ? VAL C 78  GLY C 81  
I 3  THR C 87  ? TRP C 97  ? THR C 87  TRP C 97  
I 4  ALA C 116 ? ASN C 124 ? ALA C 116 ASN C 124 
I 5  LEU C 140 ? VAL C 149 ? LEU C 141 VAL C 150 
I 6  ILE C 215 ? VAL C 217 ? ILE C 216 VAL C 218 
J 1  ASP D 32  ? ILE D 33  ? ASP D 32  ILE D 33  
J 2  THR D 108 ? VAL D 109 ? THR D 108 VAL D 109 
K 1  LYS D 39  ? TYR D 40  ? LYS D 39  TYR D 40  
K 2  LYS D 256 ? ALA D 257 ? LYS D 257 ALA D 258 
K 3  TYR D 190 ? GLY D 195 ? TYR D 191 GLY D 196 
K 4  VAL D 206 ? LEU D 211 ? VAL D 207 LEU D 212 
K 5  LEU D 140 ? VAL D 149 ? LEU D 141 VAL D 150 
K 6  ALA D 116 ? ASN D 124 ? ALA D 116 ASN D 124 
K 7  TYR D 88  ? TRP D 97  ? TYR D 88  TRP D 97  
K 8  PHE D 66  ? PHE D 70  ? PHE D 66  PHE D 70  
K 9  SER D 56  ? ASN D 61  ? SER D 56  ASN D 61  
K 10 SER D 172 ? ASP D 174 ? SER D 173 ASP D 175 
L 1  LEU D 47  ? SER D 50  ? LEU D 47  SER D 50  
L 2  VAL D 78  ? GLY D 81  ? VAL D 78  GLY D 81  
L 3  TYR D 88  ? TRP D 97  ? TYR D 88  TRP D 97  
L 4  ALA D 116 ? ASN D 124 ? ALA D 116 ASN D 124 
L 5  LEU D 140 ? VAL D 149 ? LEU D 141 VAL D 150 
L 6  ILE D 215 ? VAL D 217 ? ILE D 216 VAL D 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
B 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
B 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
B 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
B 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
B 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
B 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
B 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
B 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
D 1 2  N ILE B 33  ? N ILE B 33  O THR B 108 ? O THR B 108 
E 1 2  N LYS B 39  ? N LYS B 39  O ALA B 257 ? O ALA B 258 
E 2 3  O LYS B 256 ? O LYS B 257 N THR B 192 ? N THR B 193 
E 3 4  N GLY B 195 ? N GLY B 196 O VAL B 206 ? O VAL B 207 
E 4 5  O ILE B 209 ? O ILE B 210 N GLY B 144 ? N GLY B 145 
E 5 6  O ILE B 145 ? O ILE B 146 N LEU B 118 ? N LEU B 118 
E 6 7  O HIS B 119 ? O HIS B 119 N HIS B 94  ? N HIS B 94  
E 7 8  O PHE B 93  ? O PHE B 93  N VAL B 68  ? N VAL B 68  
E 8 9  O GLU B 69  ? O GLU B 69  N LEU B 57  ? N LEU B 57  
E 9 10 N ILE B 59  ? N ILE B 59  O ALA B 173 ? O ALA B 174 
F 1 2  N SER B 48  ? N SER B 48  O LYS B 80  ? O LYS B 80  
F 2 3  N LEU B 79  ? N LEU B 79  O TYR B 88  ? O TYR B 88  
F 3 4  N HIS B 94  ? N HIS B 94  O HIS B 119 ? O HIS B 119 
F 4 5  N LEU B 118 ? N LEU B 118 O ILE B 145 ? O ILE B 146 
F 5 6  N PHE B 146 ? N PHE B 147 O ILE B 215 ? O ILE B 216 
G 1 2  N ILE C 33  ? N ILE C 33  O THR C 108 ? O THR C 108 
H 1 2  N LYS C 39  ? N LYS C 39  O ALA C 257 ? O ALA C 258 
H 2 3  O LYS C 256 ? O LYS C 257 N THR C 192 ? N THR C 193 
H 3 4  N GLY C 195 ? N GLY C 196 O VAL C 206 ? O VAL C 207 
H 4 5  O ILE C 209 ? O ILE C 210 N GLY C 144 ? N GLY C 145 
H 5 6  O ILE C 145 ? O ILE C 146 N LEU C 118 ? N LEU C 118 
H 6 7  O HIS C 119 ? O HIS C 119 N HIS C 94  ? N HIS C 94  
H 7 8  O PHE C 93  ? O PHE C 93  N VAL C 68  ? N VAL C 68  
H 8 9  O GLU C 69  ? O GLU C 69  N LEU C 57  ? N LEU C 57  
H 9 10 N ILE C 59  ? N ILE C 59  O ALA C 173 ? O ALA C 174 
I 1 2  N SER C 48  ? N SER C 48  O LYS C 80  ? O LYS C 80  
I 2 3  N LEU C 79  ? N LEU C 79  O TYR C 88  ? O TYR C 88  
I 3 4  N HIS C 94  ? N HIS C 94  O HIS C 119 ? O HIS C 119 
I 4 5  N LEU C 118 ? N LEU C 118 O ILE C 145 ? O ILE C 146 
I 5 6  N PHE C 146 ? N PHE C 147 O ILE C 215 ? O ILE C 216 
J 1 2  N ILE D 33  ? N ILE D 33  O THR D 108 ? O THR D 108 
K 1 2  N LYS D 39  ? N LYS D 39  O ALA D 257 ? O ALA D 258 
K 2 3  O LYS D 256 ? O LYS D 257 N THR D 192 ? N THR D 193 
K 3 4  N GLY D 195 ? N GLY D 196 O VAL D 206 ? O VAL D 207 
K 4 5  O ILE D 209 ? O ILE D 210 N GLY D 144 ? N GLY D 145 
K 5 6  O ILE D 145 ? O ILE D 146 N LEU D 118 ? N LEU D 118 
K 6 7  O HIS D 119 ? O HIS D 119 N HIS D 94  ? N HIS D 94  
K 7 8  O ILE D 91  ? O ILE D 91  N PHE D 70  ? N PHE D 70  
K 8 9  O GLU D 69  ? O GLU D 69  N LEU D 57  ? N LEU D 57  
K 9 10 N ILE D 59  ? N ILE D 59  O ALA D 173 ? O ALA D 174 
L 1 2  N SER D 48  ? N SER D 48  O LYS D 80  ? O LYS D 80  
L 2 3  N LEU D 79  ? N LEU D 79  O TYR D 88  ? O TYR D 88  
L 3 4  N HIS D 94  ? N HIS D 94  O HIS D 119 ? O HIS D 119 
L 4 5  N LEU D 118 ? N LEU D 118 O ILE D 145 ? O ILE D 146 
L 5 6  N PHE D 146 ? N PHE D 147 O ILE D 215 ? O ILE D 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN A 301'  
AC2 Software A WWX 302 ? 12 'BINDING SITE FOR RESIDUE WWX A 302' 
AC3 Software A DMS 303 ? 5  'BINDING SITE FOR RESIDUE DMS A 303' 
AC4 Software A BCN 304 ? 6  'BINDING SITE FOR RESIDUE BCN A 304' 
AC5 Software B ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN B 301'  
AC6 Software B WWX 302 ? 12 'BINDING SITE FOR RESIDUE WWX B 302' 
AC7 Software B DMS 303 ? 4  'BINDING SITE FOR RESIDUE DMS B 303' 
AC8 Software B BCN 304 ? 6  'BINDING SITE FOR RESIDUE BCN B 304' 
AC9 Software C ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN C 301'  
BC1 Software C WWX 302 ? 11 'BINDING SITE FOR RESIDUE WWX C 302' 
BC2 Software C DMS 303 ? 3  'BINDING SITE FOR RESIDUE DMS C 303' 
BC3 Software C BCN 304 ? 7  'BINDING SITE FOR RESIDUE BCN C 304' 
BC4 Software D ZN  301 ? 4  'BINDING SITE FOR RESIDUE ZN D 301'  
BC5 Software D WWX 302 ? 12 'BINDING SITE FOR RESIDUE WWX D 302' 
BC6 Software D DMS 303 ? 4  'BINDING SITE FOR RESIDUE DMS D 303' 
BC7 Software D BCN 304 ? 6  'BINDING SITE FOR RESIDUE BCN D 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2   AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3   AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4   AC1 4  WWX F .   ? WWX A 302 . ? 1_555 ? 
5   AC2 12 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6   AC2 12 ASN A 67  ? ASN A 67  . ? 1_555 ? 
7   AC2 12 GLN A 92  ? GLN A 92  . ? 1_555 ? 
8   AC2 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
9   AC2 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
10  AC2 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
11  AC2 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
12  AC2 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
13  AC2 12 THR A 198 ? THR A 199 . ? 1_555 ? 
14  AC2 12 THR A 199 ? THR A 200 . ? 1_555 ? 
15  AC2 12 PRO A 201 ? PRO A 202 . ? 1_555 ? 
16  AC2 12 ZN  E .   ? ZN  A 301 . ? 1_555 ? 
17  AC3 5  TYR A 7   ? TYR A 7   . ? 1_555 ? 
18  AC3 5  ASP A 242 ? ASP A 243 . ? 1_555 ? 
19  AC3 5  TRP A 244 ? TRP A 245 . ? 1_555 ? 
20  AC3 5  PRO A 246 ? PRO A 247 . ? 1_555 ? 
21  AC3 5  HOH U .   ? HOH A 616 . ? 1_555 ? 
22  AC4 6  LYS A 148 ? LYS A 149 . ? 1_555 ? 
23  AC4 6  LYS A 212 ? LYS A 213 . ? 1_555 ? 
24  AC4 6  GLU A 213 ? GLU A 214 . ? 1_555 ? 
25  AC4 6  PRO A 214 ? PRO A 215 . ? 1_555 ? 
26  AC4 6  HOH U .   ? HOH A 440 . ? 1_555 ? 
27  AC4 6  HOH U .   ? HOH A 639 . ? 1_555 ? 
28  AC5 4  HIS B 94  ? HIS B 94  . ? 1_555 ? 
29  AC5 4  HIS B 96  ? HIS B 96  . ? 1_555 ? 
30  AC5 4  HIS B 119 ? HIS B 119 . ? 1_555 ? 
31  AC5 4  WWX J .   ? WWX B 302 . ? 1_555 ? 
32  AC6 12 ASN B 62  ? ASN B 62  . ? 1_555 ? 
33  AC6 12 ASN B 67  ? ASN B 67  . ? 1_555 ? 
34  AC6 12 GLN B 92  ? GLN B 92  . ? 1_555 ? 
35  AC6 12 HIS B 94  ? HIS B 94  . ? 1_555 ? 
36  AC6 12 HIS B 96  ? HIS B 96  . ? 1_555 ? 
37  AC6 12 HIS B 119 ? HIS B 119 . ? 1_555 ? 
38  AC6 12 PHE B 130 ? PHE B 131 . ? 1_555 ? 
39  AC6 12 LEU B 197 ? LEU B 198 . ? 1_555 ? 
40  AC6 12 THR B 198 ? THR B 199 . ? 1_555 ? 
41  AC6 12 THR B 199 ? THR B 200 . ? 1_555 ? 
42  AC6 12 PRO B 201 ? PRO B 202 . ? 1_555 ? 
43  AC6 12 ZN  I .   ? ZN  B 301 . ? 1_555 ? 
44  AC7 4  TYR B 7   ? TYR B 7   . ? 1_555 ? 
45  AC7 4  ASP B 242 ? ASP B 243 . ? 1_555 ? 
46  AC7 4  TRP B 244 ? TRP B 245 . ? 1_555 ? 
47  AC7 4  HOH V .   ? HOH B 631 . ? 1_555 ? 
48  AC8 6  LYS B 148 ? LYS B 149 . ? 1_555 ? 
49  AC8 6  LYS B 212 ? LYS B 213 . ? 1_555 ? 
50  AC8 6  GLU B 213 ? GLU B 214 . ? 1_555 ? 
51  AC8 6  PRO B 214 ? PRO B 215 . ? 1_555 ? 
52  AC8 6  HOH V .   ? HOH B 440 . ? 1_555 ? 
53  AC8 6  HOH V .   ? HOH B 461 . ? 1_555 ? 
54  AC9 4  HIS C 94  ? HIS C 94  . ? 1_555 ? 
55  AC9 4  HIS C 96  ? HIS C 96  . ? 1_555 ? 
56  AC9 4  HIS C 119 ? HIS C 119 . ? 1_555 ? 
57  AC9 4  WWX N .   ? WWX C 302 . ? 1_555 ? 
58  BC1 11 ASN C 62  ? ASN C 62  . ? 1_555 ? 
59  BC1 11 ASN C 67  ? ASN C 67  . ? 1_555 ? 
60  BC1 11 GLN C 92  ? GLN C 92  . ? 1_555 ? 
61  BC1 11 HIS C 94  ? HIS C 94  . ? 1_555 ? 
62  BC1 11 HIS C 96  ? HIS C 96  . ? 1_555 ? 
63  BC1 11 HIS C 119 ? HIS C 119 . ? 1_555 ? 
64  BC1 11 LEU C 197 ? LEU C 198 . ? 1_555 ? 
65  BC1 11 THR C 198 ? THR C 199 . ? 1_555 ? 
66  BC1 11 THR C 199 ? THR C 200 . ? 1_555 ? 
67  BC1 11 PRO C 201 ? PRO C 202 . ? 1_555 ? 
68  BC1 11 ZN  M .   ? ZN  C 301 . ? 1_555 ? 
69  BC2 3  ASP C 242 ? ASP C 243 . ? 1_555 ? 
70  BC2 3  TRP C 244 ? TRP C 245 . ? 1_555 ? 
71  BC2 3  HOH W .   ? HOH C 639 . ? 1_555 ? 
72  BC3 7  LYS C 148 ? LYS C 149 . ? 1_555 ? 
73  BC3 7  LYS C 212 ? LYS C 213 . ? 1_555 ? 
74  BC3 7  GLU C 213 ? GLU C 214 . ? 1_555 ? 
75  BC3 7  PRO C 214 ? PRO C 215 . ? 1_555 ? 
76  BC3 7  HOH W .   ? HOH C 440 . ? 1_555 ? 
77  BC3 7  HOH W .   ? HOH C 587 . ? 1_555 ? 
78  BC3 7  HOH W .   ? HOH C 640 . ? 1_555 ? 
79  BC4 4  HIS D 94  ? HIS D 94  . ? 1_555 ? 
80  BC4 4  HIS D 96  ? HIS D 96  . ? 1_555 ? 
81  BC4 4  HIS D 119 ? HIS D 119 . ? 1_555 ? 
82  BC4 4  WWX R .   ? WWX D 302 . ? 1_555 ? 
83  BC5 12 ASN D 62  ? ASN D 62  . ? 1_555 ? 
84  BC5 12 ASN D 67  ? ASN D 67  . ? 1_555 ? 
85  BC5 12 GLN D 92  ? GLN D 92  . ? 1_555 ? 
86  BC5 12 HIS D 94  ? HIS D 94  . ? 1_555 ? 
87  BC5 12 HIS D 96  ? HIS D 96  . ? 1_555 ? 
88  BC5 12 HIS D 119 ? HIS D 119 . ? 1_555 ? 
89  BC5 12 LEU D 140 ? LEU D 141 . ? 1_555 ? 
90  BC5 12 LEU D 197 ? LEU D 198 . ? 1_555 ? 
91  BC5 12 THR D 198 ? THR D 199 . ? 1_555 ? 
92  BC5 12 THR D 199 ? THR D 200 . ? 1_555 ? 
93  BC5 12 PRO D 201 ? PRO D 202 . ? 1_555 ? 
94  BC5 12 ZN  Q .   ? ZN  D 301 . ? 1_555 ? 
95  BC6 4  TYR D 7   ? TYR D 7   . ? 1_555 ? 
96  BC6 4  ASP D 242 ? ASP D 243 . ? 1_555 ? 
97  BC6 4  TRP D 244 ? TRP D 245 . ? 1_555 ? 
98  BC6 4  HOH X .   ? HOH D 637 . ? 1_555 ? 
99  BC7 6  LYS D 148 ? LYS D 149 . ? 1_555 ? 
100 BC7 6  LYS D 212 ? LYS D 213 . ? 1_555 ? 
101 BC7 6  GLU D 213 ? GLU D 214 . ? 1_555 ? 
102 BC7 6  PRO D 214 ? PRO D 215 . ? 1_555 ? 
103 BC7 6  HOH X .   ? HOH D 440 . ? 1_555 ? 
104 BC7 6  HOH X .   ? HOH D 613 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4QIY 
_atom_sites.fract_transf_matrix[1][1]   0.013588 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004758 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024268 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.012607 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 0.214   3.253   20.919  1.00 35.47 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? -0.343  2.046   21.608  1.00 29.52 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? -0.721  0.952   20.624  1.00 20.64 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? -0.447  -0.238  20.852  1.00 21.69 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? -1.534  2.403   22.514  1.00 29.55 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? -1.925  1.287   23.474  1.00 36.40 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? -1.231  1.033   24.625  1.00 43.10 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? -2.982  0.340   23.416  1.00 38.21 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? -1.798  -0.043  25.261  1.00 47.25 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? -2.892  -0.451  24.527  1.00 35.39 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? -1.341  1.330   19.508  1.00 18.80 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? -1.870  0.413   18.547  1.00 16.50 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? -0.810  -0.389  17.850  1.00 15.24 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 0.332   0.006   17.677  1.00 15.93 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? -2.789  1.117   17.528  1.00 16.85 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? -2.075  1.915   16.507  1.00 16.00 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? -1.763  3.283   16.551  1.00 16.39 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? -1.567  1.426   15.213  1.00 16.84 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? -1.057  3.646   15.416  1.00 16.11 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? -0.931  2.575   14.568  1.00 17.09 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? -1.568  0.174   14.565  1.00 13.99 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? -0.350  2.496   13.333  1.00 17.56 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? -0.932  0.129   13.280  1.00 12.69 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? -0.401  1.261   12.684  1.00 15.50 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? -1.249  -1.597  17.479  1.00 13.69 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? -0.341  -2.432  16.704  1.00 15.84 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? -1.145  -3.544  16.063  1.00 12.49 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? -2.298  -3.378  15.680  1.00 12.89 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? -0.543  -4.714  15.977  1.00 14.27 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? -1.146  -5.840  15.256  1.00 14.68 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? -1.346  -7.092  16.128  1.00 18.08 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? -1.907  -8.123  15.666  1.00 18.99 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? -0.299  -6.197  14.020  1.00 14.93 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? -0.420  -5.115  12.956  1.00 12.38 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? -1.568  -5.114  12.103  1.00 12.15 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 0.550   -4.100  12.759  1.00 14.14 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? -1.732  -4.116  11.102  1.00 11.52 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.373   -3.119  11.754  1.00 12.37 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? -0.778  -3.171  10.960  1.00 11.61 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.882  -2.194  9.976   1.00 12.81 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? -0.994  -6.969  17.417  1.00 17.28 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? -1.140  -8.141  18.340  1.00 16.75 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? -2.526  -8.383  18.913  1.00 16.99 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? -3.530  -7.673  18.655  1.00 17.10 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? -2.602  -9.338  19.874  1.00 17.90 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? -3.857  -9.751  20.471  1.00 19.10 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? -4.502  -8.619  21.268  1.00 16.23 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? -5.738  -8.453  21.266  1.00 18.32 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? -3.544  -10.889 21.447  1.00 21.80 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? -4.757  -11.412 22.135  1.00 24.47 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? -3.659  -7.881  21.959  1.00 17.64 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? -4.198  -6.824  22.877  1.00 16.32 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? -4.233  -5.438  22.330  1.00 15.38 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? -4.857  -4.565  22.924  1.00 16.73 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? -3.367  -6.826  24.172  1.00 16.83 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? -3.360  -8.160  24.808  1.00 15.12 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? -4.459  -8.674  25.453  1.00 17.50 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? -2.419  -9.146  24.748  1.00 16.28 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? -4.171  -9.934  25.875  1.00 17.13 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? -2.900  -10.236 25.432  1.00 17.65 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? -3.695  -5.268  21.113  1.00 14.84 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? -3.641  -3.913  20.549  1.00 13.75 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? -3.961  -3.894  19.027  1.00 14.25 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? -3.784  -2.818  18.416  1.00 14.88 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? -2.272  -3.203  20.760  1.00 13.81 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? -1.135  -3.875  20.059  1.00 15.97 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? -1.312  -4.930  19.445  1.00 19.02 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 0.042   -3.315  20.175  1.00 17.98 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? -4.412  -5.028  18.483  1.00 13.63 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? -4.570  -5.135  16.992  1.00 12.95 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? -5.850  -4.615  16.533  1.00 13.05 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? -6.597  -3.945  17.205  1.00 13.69 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? -6.154  -5.011  15.244  1.00 11.98 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? -7.340  -4.493  14.604  1.00 13.23 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? -8.602  -4.454  15.357  1.00 13.82 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? -9.415  -3.528  15.166  1.00 13.98 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? -7.419  -5.276  13.287  1.00 13.28 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? -5.990  -5.552  12.992  1.00 13.52 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? -5.246  -5.777  14.339  1.00 14.14 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? -8.860  -5.480  16.182  1.00 13.10 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? -10.166 -5.537  16.896  1.00 16.52 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? -10.224 -4.517  18.009  1.00 13.28 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? -11.336 -4.309  18.556  1.00 15.83 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? -10.469 -6.964  17.438  1.00 18.34 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? -10.375 -8.069  16.378  1.00 23.67 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? -11.127 -7.743  15.097  1.00 36.48 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? -12.311 -7.349  15.170  1.00 38.55 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? -10.531 -7.892  14.009  1.00 37.78 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? -9.090  -3.908  18.322  1.00 13.05 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? -9.062  -2.912  19.376  1.00 13.56 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? -9.064  -1.488  18.895  1.00 13.62 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? -9.315  -0.560  19.693  1.00 12.90 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? -7.785  -3.085  20.200  1.00 14.02 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? -7.788  -4.344  21.026  1.00 14.81 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? -8.325  -4.376  22.344  1.00 14.19 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? -7.349  -5.607  20.735  1.00 18.47 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? -8.171  -5.627  22.828  1.00 16.82 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? -7.576  -6.387  21.878  1.00 16.25 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? -8.751  -1.264  17.597  1.00 12.11 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? -8.462  0.073   17.135  1.00 12.01 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? -9.635  1.034   17.297  1.00 10.73 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? -9.435  2.253   17.448  1.00 11.56 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? -8.060  0.023   15.661  1.00 12.82 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? -6.789  -0.690  15.462  1.00 12.22 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? -5.828  -1.069  16.358  1.00 11.35 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? -6.224  -1.030  14.122  1.00 12.23 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? -4.745  -1.665  15.718  1.00 10.88 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? -4.932  -1.628  14.337  1.00 11.47 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? -6.714  -0.892  12.808  1.00 11.13 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? -4.155  -2.108  13.265  1.00 12.53 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? -5.960  -1.375  11.771  1.00 12.01 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? -4.713  -1.924  11.969  1.00 12.54 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? -10.850 0.535   17.278  1.00 12.06 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? -12.063 1.377   17.347  1.00 13.11 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? -12.096 2.207   18.673  1.00 14.20 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? -12.740 3.228   18.690  1.00 13.85 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? -13.363 0.598   17.164  1.00 14.21 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? -13.709 -0.255  18.359  1.00 14.09 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? -14.607 0.137   19.314  1.00 18.45 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? -13.174 -1.435  18.761  1.00 14.22 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? -14.658 -0.785  20.256  1.00 18.02 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? -13.776 -1.742  19.962  1.00 15.55 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? -11.389 1.745   19.736  1.00 14.10 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? -11.513 2.485   21.011  1.00 14.49 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? -10.793 3.837   20.891  1.00 17.94 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? -11.359 4.900   21.271  1.00 21.59 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? -10.956 1.641   22.147  1.00 15.42 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? -11.899 0.481   22.443  1.00 17.97 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? -11.253 -0.451  23.465  1.00 15.56 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? -10.312 -1.441  22.847  1.00 16.50 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? -9.427  -2.230  23.729  1.00 14.90 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? -9.621  3.827   20.264  1.00 17.11 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? -8.944  5.102   20.038  1.00 17.83 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? -9.432  5.813   18.769  1.00 17.61 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? -9.347  7.020   18.696  1.00 17.97 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? -7.424  4.879   19.948  1.00 22.07 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? -6.679  4.914   21.314  1.00 25.20 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? -7.111  5.593   22.285  1.00 28.90 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? -5.625  4.268   21.356  1.00 43.92 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? -9.968  5.061   17.789  1.00 13.66 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? -10.282 5.631   16.475  1.00 14.56 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? -11.664 5.117   16.101  1.00 13.00 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? -11.777 4.068   15.399  1.00 14.14 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? -9.198  5.235   15.460  1.00 14.71 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? -7.775  5.597   15.909  1.00 14.57 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? -7.306  6.897   15.717  1.00 19.24 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? -6.985  4.689   16.592  1.00 18.70 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? -6.054  7.273   16.183  1.00 20.47 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? -5.734  5.027   17.049  1.00 19.32 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? -5.267  6.328   16.813  1.00 17.99 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? -12.759 5.704   16.617  1.00 15.58 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? -14.069 5.135   16.430  1.00 16.86 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? -14.511 5.005   14.934  1.00 13.97 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? -15.398 4.241   14.649  1.00 14.47 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? -15.015 6.094   17.220  1.00 19.50 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? -14.184 7.299   17.388  1.00 24.63 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? -12.782 6.801   17.601  1.00 17.84 ? 21  PRO A CD  1 
ATOM   158  N  N   A ILE A 1 22  ? -13.859 5.773   14.015  0.50 13.26 ? 22  ILE A N   1 
ATOM   159  N  N   B ILE A 1 22  ? -13.837 5.773   14.042  0.50 13.68 ? 22  ILE A N   1 
ATOM   160  C  CA  A ILE A 1 22  ? -14.147 5.657   12.556  0.50 13.90 ? 22  ILE A CA  1 
ATOM   161  C  CA  B ILE A 1 22  ? -14.059 5.685   12.593  0.50 14.89 ? 22  ILE A CA  1 
ATOM   162  C  C   A ILE A 1 22  ? -13.861 4.222   12.086  0.50 11.79 ? 22  ILE A C   1 
ATOM   163  C  C   B ILE A 1 22  ? -13.676 4.302   12.080  0.50 11.61 ? 22  ILE A C   1 
ATOM   164  O  O   A ILE A 1 22  ? -14.435 3.807   11.007  0.50 10.78 ? 22  ILE A O   1 
ATOM   165  O  O   B ILE A 1 22  ? -13.908 4.008   10.944  0.50 11.98 ? 22  ILE A O   1 
ATOM   166  C  CB  A ILE A 1 22  ? -13.407 6.766   11.737  0.50 13.09 ? 22  ILE A CB  1 
ATOM   167  C  CB  B ILE A 1 22  ? -13.210 6.758   11.881  0.50 14.56 ? 22  ILE A CB  1 
ATOM   168  C  CG1 A ILE A 1 22  ? -14.053 6.963   10.368  0.50 15.31 ? 22  ILE A CG1 1 
ATOM   169  C  CG1 B ILE A 1 22  ? -13.794 7.099   10.519  0.50 14.16 ? 22  ILE A CG1 1 
ATOM   170  C  CG2 A ILE A 1 22  ? -11.887 6.527   11.636  0.50 14.88 ? 22  ILE A CG2 1 
ATOM   171  C  CG2 B ILE A 1 22  ? -11.748 6.311   11.780  0.50 16.34 ? 22  ILE A CG2 1 
ATOM   172  C  CD1 A ILE A 1 22  ? -15.278 7.857   10.389  0.50 16.70 ? 22  ILE A CD1 1 
ATOM   173  C  CD1 B ILE A 1 22  ? -13.121 8.259   9.839   0.50 17.52 ? 22  ILE A CD1 1 
ATOM   174  N  N   . ALA A 1 23  ? -13.049 3.450   12.903  1.00 12.99 ? 23  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 23  ? -12.805 2.063   12.545  1.00 13.11 ? 23  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 23  ? -14.041 1.328   12.217  1.00 13.19 ? 23  ALA A C   1 
ATOM   177  O  O   . ALA A 1 23  ? -13.976 0.300   11.513  1.00 13.39 ? 23  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 23  ? -12.057 1.348   13.637  1.00 11.61 ? 23  ALA A CB  1 
ATOM   179  N  N   . LYS A 1 24  ? -15.187 1.739   12.782  1.00 14.11 ? 24  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 24  ? -16.484 1.110   12.487  1.00 13.82 ? 24  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 24  ? -17.303 1.973   11.517  1.00 16.60 ? 24  LYS A C   1 
ATOM   182  O  O   . LYS A 1 24  ? -18.540 1.846   11.463  1.00 18.72 ? 24  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 24  ? -17.335 0.881   13.755  1.00 15.98 ? 24  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 24  ? -16.624 -0.015  14.720  1.00 18.03 ? 24  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 24  ? -17.547 -0.297  15.915  1.00 26.40 ? 24  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 24  ? -16.868 -1.151  16.955  1.00 22.62 ? 24  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 24  ? -16.865 -2.543  16.464  1.00 31.72 ? 24  LYS A NZ  1 
ATOM   188  N  N   . GLY A 1 25  ? -16.614 2.841   10.733  1.00 14.46 ? 25  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 25  ? -17.325 3.790   9.804   1.00 15.44 ? 25  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 25  ? -17.841 3.120   8.568   1.00 13.65 ? 25  GLY A C   1 
ATOM   191  O  O   . GLY A 1 25  ? -17.906 1.889   8.386   1.00 14.69 ? 25  GLY A O   1 
ATOM   192  N  N   . GLU A 1 26  ? -18.341 3.993   7.718   1.00 14.99 ? 26  GLU A N   1 
ATOM   193  C  CA  . GLU A 1 26  ? -18.971 3.587   6.531   1.00 15.98 ? 26  GLU A CA  1 
ATOM   194  C  C   . GLU A 1 26  ? -18.111 3.331   5.270   1.00 12.06 ? 26  GLU A C   1 
ATOM   195  O  O   . GLU A 1 26  ? -18.649 2.831   4.267   1.00 13.75 ? 26  GLU A O   1 
ATOM   196  C  CB  . GLU A 1 26  ? -20.012 4.673   6.182   1.00 20.08 ? 26  GLU A CB  1 
ATOM   197  C  CG  . GLU A 1 26  ? -21.096 4.906   7.269   1.00 26.98 ? 26  GLU A CG  1 
ATOM   198  C  CD  . GLU A 1 26  ? -21.840 3.585   7.678   1.00 27.92 ? 26  GLU A CD  1 
ATOM   199  O  OE1 . GLU A 1 26  ? -22.356 2.795   6.821   1.00 31.57 ? 26  GLU A OE1 1 
ATOM   200  O  OE2 . GLU A 1 26  ? -21.856 3.261   8.891   1.00 40.22 ? 26  GLU A OE2 1 
ATOM   201  N  N   . ARG A 1 27  ? -16.802 3.698   5.316   1.00 11.16 ? 27  ARG A N   1 
ATOM   202  C  CA  . ARG A 1 27  ? -15.983 3.518   4.154   1.00 9.86  ? 27  ARG A CA  1 
ATOM   203  C  C   . ARG A 1 27  ? -14.628 3.029   4.579   1.00 9.57  ? 27  ARG A C   1 
ATOM   204  O  O   . ARG A 1 27  ? -13.606 3.612   4.178   1.00 10.46 ? 27  ARG A O   1 
ATOM   205  C  CB  . ARG A 1 27  ? -15.946 4.785   3.260   1.00 13.52 ? 27  ARG A CB  1 
ATOM   206  C  CG  . ARG A 1 27  ? -15.525 6.073   3.876   1.00 16.83 ? 27  ARG A CG  1 
ATOM   207  C  CD  . ARG A 1 27  ? -15.377 7.261   2.863   1.00 19.39 ? 27  ARG A CD  1 
ATOM   208  N  NE  . ARG A 1 27  ? -14.183 7.156   2.027   1.00 19.53 ? 27  ARG A NE  1 
ATOM   209  C  CZ  . ARG A 1 27  ? -13.715 8.144   1.270   1.00 16.25 ? 27  ARG A CZ  1 
ATOM   210  N  NH1 . ARG A 1 27  ? -14.338 9.314   1.242   1.00 14.46 ? 27  ARG A NH1 1 
ATOM   211  N  NH2 . ARG A 1 27  ? -12.624 7.962   0.538   1.00 15.78 ? 27  ARG A NH2 1 
ATOM   212  N  N   . GLN A 1 28  ? -14.610 1.960   5.397   1.00 9.63  ? 28  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 28  ? -13.323 1.465   5.911   1.00 9.47  ? 28  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 28  ? -12.692 0.468   4.887   1.00 7.99  ? 28  GLN A C   1 
ATOM   215  O  O   . GLN A 1 28  ? -13.352 -0.201  4.119   1.00 9.32  ? 28  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 28  ? -13.614 0.754   7.275   1.00 10.07 ? 28  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 28  ? -13.876 1.825   8.334   1.00 10.43 ? 28  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 28  ? -12.629 2.617   8.645   1.00 9.67  ? 28  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 28  ? -11.681 2.100   9.176   1.00 10.92 ? 28  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 28  ? -12.605 3.955   8.278   1.00 9.93  ? 28  GLN A NE2 1 
ATOM   221  N  N   . SER A 1 29  ? -11.388 0.418   4.981   1.00 8.25  ? 29  SER A N   1 
ATOM   222  C  CA  . SER A 1 29  ? -10.532 -0.460  4.115   1.00 8.24  ? 29  SER A CA  1 
ATOM   223  C  C   . SER A 1 29  ? -9.675  -1.330  5.019   1.00 8.71  ? 29  SER A C   1 
ATOM   224  O  O   . SER A 1 29  ? -9.364  -0.981  6.153   1.00 8.67  ? 29  SER A O   1 
ATOM   225  C  CB  . SER A 1 29  ? -9.613  0.400   3.251   1.00 9.60  ? 29  SER A CB  1 
ATOM   226  O  OG  . SER A 1 29  ? -10.434 1.130   2.308   1.00 8.56  ? 29  SER A OG  1 
ATOM   227  N  N   . PRO A 1 30  ? -9.196  -2.472  4.495   1.00 8.51  ? 30  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 30  ? -9.465  -3.014  3.115   1.00 8.05  ? 30  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 30  ? -10.830 -3.692  3.066   1.00 7.63  ? 30  PRO A C   1 
ATOM   230  O  O   . PRO A 1 30  ? -11.579 -3.719  4.068   1.00 8.44  ? 30  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 30  ? -8.340  -4.005  2.969   1.00 7.52  ? 30  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 30  ? -8.231  -4.640  4.368   1.00 9.40  ? 30  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 30  ? -8.342  -3.388  5.292   1.00 9.01  ? 30  PRO A CD  1 
ATOM   234  N  N   . VAL A 1 31  ? -11.140 -4.238  1.904   1.00 8.00  ? 31  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 31  ? -12.336 -4.997  1.645   1.00 8.24  ? 31  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 31  ? -12.011 -6.228  0.847   1.00 8.16  ? 31  VAL A C   1 
ATOM   237  O  O   . VAL A 1 31  ? -10.934 -6.269  0.196   1.00 9.09  ? 31  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 31  ? -13.428 -4.159  0.897   1.00 8.07  ? 31  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 31  ? -13.833 -2.964  1.750   1.00 10.22 ? 31  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 31  ? -12.979 -3.760  -0.506  1.00 9.43  ? 31  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 32  ? -12.909 -7.213  0.845   1.00 9.40  ? 32  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 32  ? -12.853 -8.278  -0.127  1.00 8.56  ? 32  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 32  ? -13.411 -7.759  -1.459  1.00 7.95  ? 32  ASP A C   1 
ATOM   244  O  O   . ASP A 1 32  ? -14.520 -7.140  -1.519  1.00 10.72 ? 32  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 32  ? -13.690 -9.452  0.368   1.00 10.96 ? 32  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 32  ? -13.654 -10.631 -0.646  1.00 11.66 ? 32  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 32  ? -12.532 -11.073 -0.968  1.00 9.64  ? 32  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 32  ? -14.777 -11.058 -1.092  1.00 14.00 ? 32  ASP A OD2 1 
ATOM   249  N  N   . ILE A 1 33  ? -12.709 -8.071  -2.542  1.00 8.53  ? 33  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 33  ? -13.110 -7.654  -3.871  1.00 10.37 ? 33  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 33  ? -13.786 -8.902  -4.422  1.00 10.67 ? 33  ILE A C   1 
ATOM   252  O  O   . ILE A 1 33  ? -13.156 -9.902  -4.792  1.00 11.25 ? 33  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 33  ? -11.906 -7.241  -4.732  1.00 9.86  ? 33  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 33  ? -11.243 -5.990  -4.082  1.00 9.46  ? 33  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 33  ? -12.371 -6.930  -6.158  1.00 10.98 ? 33  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 33  ? -9.858  -5.691  -4.706  1.00 11.93 ? 33  ILE A CD1 1 
ATOM   257  N  N   . ASP A 1 34  ? -15.118 -8.833  -4.522  1.00 11.49 ? 34  ASP A N   1 
ATOM   258  C  CA  . ASP A 1 34  ? -15.918 -9.936  -5.103  1.00 12.45 ? 34  ASP A CA  1 
ATOM   259  C  C   . ASP A 1 34  ? -15.903 -9.649  -6.630  1.00 12.64 ? 34  ASP A C   1 
ATOM   260  O  O   . ASP A 1 34  ? -16.579 -8.646  -7.073  1.00 13.91 ? 34  ASP A O   1 
ATOM   261  C  CB  . ASP A 1 34  ? -17.309 -9.923  -4.485  1.00 15.08 ? 34  ASP A CB  1 
ATOM   262  C  CG  . ASP A 1 34  ? -18.296 -10.885 -5.121  1.00 19.87 ? 34  ASP A CG  1 
ATOM   263  O  OD1 . ASP A 1 34  ? -18.106 -11.287 -6.285  1.00 21.42 ? 34  ASP A OD1 1 
ATOM   264  O  OD2 . ASP A 1 34  ? -19.304 -11.192 -4.448  1.00 33.81 ? 34  ASP A OD2 1 
ATOM   265  N  N   . THR A 1 35  ? -15.183 -10.419 -7.398  1.00 12.52 ? 35  THR A N   1 
ATOM   266  C  CA  . THR A 1 35  ? -14.870 -10.039 -8.791  1.00 14.17 ? 35  THR A CA  1 
ATOM   267  C  C   . THR A 1 35  ? -16.059 -10.197 -9.677  1.00 14.90 ? 35  THR A C   1 
ATOM   268  O  O   . THR A 1 35  ? -16.136 -9.483  -10.702 1.00 17.44 ? 35  THR A O   1 
ATOM   269  C  CB  . THR A 1 35  ? -13.782 -10.959 -9.356  1.00 14.34 ? 35  THR A CB  1 
ATOM   270  O  OG1 . THR A 1 35  ? -14.279 -12.328 -9.397  1.00 16.67 ? 35  THR A OG1 1 
ATOM   271  C  CG2 . THR A 1 35  ? -12.473 -10.842 -8.538  1.00 15.21 ? 35  THR A CG2 1 
ATOM   272  N  N   . HIS A 1 36  ? -16.996 -11.052 -9.280  1.00 16.42 ? 36  HIS A N   1 
ATOM   273  C  CA  . HIS A 1 36  ? -18.287 -11.246 -10.002 1.00 16.30 ? 36  HIS A CA  1 
ATOM   274  C  C   . HIS A 1 36  ? -19.276 -10.132 -9.806  1.00 17.59 ? 36  HIS A C   1 
ATOM   275  O  O   . HIS A 1 36  ? -19.959 -9.771  -10.814 1.00 18.27 ? 36  HIS A O   1 
ATOM   276  C  CB  . HIS A 1 36  ? -18.791 -12.681 -9.746  1.00 17.73 ? 36  HIS A CB  1 
ATOM   277  C  CG  . HIS A 1 36  ? -17.975 -13.697 -10.567 1.00 17.92 ? 36  HIS A CG  1 
ATOM   278  N  ND1 . HIS A 1 36  ? -17.149 -14.684 -10.039 1.00 21.05 ? 36  HIS A ND1 1 
ATOM   279  C  CD2 . HIS A 1 36  ? -17.852 -13.784 -11.960 1.00 20.89 ? 36  HIS A CD2 1 
ATOM   280  C  CE1 . HIS A 1 36  ? -16.568 -15.357 -11.073 1.00 26.70 ? 36  HIS A CE1 1 
ATOM   281  N  NE2 . HIS A 1 36  ? -17.012 -14.833 -12.238 1.00 31.50 ? 36  HIS A NE2 1 
ATOM   282  N  N   . THR A 1 37  ? -19.230 -9.445  -8.641  1.00 17.95 ? 37  THR A N   1 
ATOM   283  C  CA  . THR A 1 37  ? -20.052 -8.326  -8.271  1.00 15.74 ? 37  THR A CA  1 
ATOM   284  C  C   . THR A 1 37  ? -19.492 -6.921  -8.645  1.00 15.85 ? 37  THR A C   1 
ATOM   285  O  O   . THR A 1 37  ? -20.240 -5.916  -8.672  1.00 21.27 ? 37  THR A O   1 
ATOM   286  C  CB  . THR A 1 37  ? -20.365 -8.442  -6.748  1.00 23.27 ? 37  THR A CB  1 
ATOM   287  O  OG1 . THR A 1 37  ? -21.171 -9.604  -6.597  1.00 28.26 ? 37  THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 37  ? -21.107 -7.194  -6.196  1.00 22.62 ? 37  THR A CG2 1 
ATOM   289  N  N   . ALA A 1 38  ? -18.196 -6.878  -8.956  1.00 12.83 ? 38  ALA A N   1 
ATOM   290  C  CA  . ALA A 1 38  ? -17.597 -5.611  -9.325  1.00 14.02 ? 38  ALA A CA  1 
ATOM   291  C  C   . ALA A 1 38  ? -18.207 -5.263  -10.684 1.00 16.36 ? 38  ALA A C   1 
ATOM   292  O  O   . ALA A 1 38  ? -18.425 -6.068  -11.522 1.00 21.69 ? 38  ALA A O   1 
ATOM   293  C  CB  . ALA A 1 38  ? -16.110 -5.731  -9.355  1.00 14.28 ? 38  ALA A CB  1 
ATOM   294  N  N   . LYS A 1 39  ? -18.546 -4.005  -10.808 1.00 14.55 ? 39  LYS A N   1 
ATOM   295  C  CA  . LYS A 1 39  ? -19.148 -3.485  -12.045 1.00 17.93 ? 39  LYS A CA  1 
ATOM   296  C  C   . LYS A 1 39  ? -18.089 -2.978  -13.048 1.00 14.85 ? 39  LYS A C   1 
ATOM   297  O  O   . LYS A 1 39  ? -17.425 -1.987  -12.761 1.00 12.81 ? 39  LYS A O   1 
ATOM   298  C  CB  . LYS A 1 39  ? -20.110 -2.350  -11.611 1.00 22.52 ? 39  LYS A CB  1 
ATOM   299  C  CG  . LYS A 1 39  ? -20.787 -1.517  -12.702 1.00 28.46 ? 39  LYS A CG  1 
ATOM   300  C  CD  . LYS A 1 39  ? -21.912 -2.269  -13.414 1.00 22.43 ? 39  LYS A CD  1 
ATOM   301  C  CE  . LYS A 1 39  ? -22.571 -1.331  -14.362 1.00 25.13 ? 39  LYS A CE  1 
ATOM   302  N  NZ  . LYS A 1 39  ? -23.654 -2.042  -15.042 1.00 28.09 ? 39  LYS A NZ  1 
ATOM   303  N  N   . TYR A 1 40  ? -18.038 -3.551  -14.257 1.00 16.13 ? 40  TYR A N   1 
ATOM   304  C  CA  . TYR A 1 40  ? -17.238 -2.952  -15.294 1.00 15.37 ? 40  TYR A CA  1 
ATOM   305  C  C   . TYR A 1 40  ? -17.757 -1.566  -15.618 1.00 15.01 ? 40  TYR A C   1 
ATOM   306  O  O   . TYR A 1 40  ? -18.965 -1.417  -15.910 1.00 17.45 ? 40  TYR A O   1 
ATOM   307  C  CB  . TYR A 1 40  ? -17.219 -3.816  -16.590 1.00 18.20 ? 40  TYR A CB  1 
ATOM   308  C  CG  . TYR A 1 40  ? -16.621 -3.105  -17.767 1.00 20.95 ? 40  TYR A CG  1 
ATOM   309  C  CD1 . TYR A 1 40  ? -15.291 -2.659  -17.750 1.00 19.85 ? 40  TYR A CD1 1 
ATOM   310  C  CD2 . TYR A 1 40  ? -17.383 -2.885  -18.935 1.00 29.84 ? 40  TYR A CD2 1 
ATOM   311  C  CE1 . TYR A 1 40  ? -14.713 -2.016  -18.826 1.00 22.52 ? 40  TYR A CE1 1 
ATOM   312  C  CE2 . TYR A 1 40  ? -16.813 -2.244  -20.021 1.00 25.80 ? 40  TYR A CE2 1 
ATOM   313  C  CZ  . TYR A 1 40  ? -15.495 -1.794  -19.970 1.00 28.32 ? 40  TYR A CZ  1 
ATOM   314  O  OH  . TYR A 1 40  ? -14.967 -1.155  -21.068 1.00 28.42 ? 40  TYR A OH  1 
ATOM   315  N  N   . ASP A 1 41  ? -16.900 -0.575  -15.571 1.00 15.40 ? 41  ASP A N   1 
ATOM   316  C  CA  . ASP A 1 41  ? -17.317 0.801   -15.858 1.00 15.75 ? 41  ASP A CA  1 
ATOM   317  C  C   . ASP A 1 41  ? -16.614 1.338   -17.075 1.00 18.37 ? 41  ASP A C   1 
ATOM   318  O  O   . ASP A 1 41  ? -15.443 1.724   -16.941 1.00 17.33 ? 41  ASP A O   1 
ATOM   319  C  CB  . ASP A 1 41  ? -17.070 1.692   -14.624 1.00 18.69 ? 41  ASP A CB  1 
ATOM   320  C  CG  . ASP A 1 41  ? -17.590 3.079   -14.798 1.00 21.08 ? 41  ASP A CG  1 
ATOM   321  O  OD1 . ASP A 1 41  ? -18.002 3.484   -15.917 1.00 23.39 ? 41  ASP A OD1 1 
ATOM   322  O  OD2 . ASP A 1 41  ? -17.552 3.802   -13.783 1.00 24.11 ? 41  ASP A OD2 1 
ATOM   323  N  N   . PRO A 1 42  ? -17.319 1.343   -18.260 1.00 19.28 ? 42  PRO A N   1 
ATOM   324  C  CA  . PRO A 1 42  ? -16.681 1.717   -19.528 1.00 23.99 ? 42  PRO A CA  1 
ATOM   325  C  C   . PRO A 1 42  ? -16.207 3.173   -19.473 1.00 24.31 ? 42  PRO A C   1 
ATOM   326  O  O   . PRO A 1 42  ? -15.376 3.592   -20.298 1.00 31.73 ? 42  PRO A O   1 
ATOM   327  C  CB  . PRO A 1 42  ? -17.841 1.527   -20.582 1.00 28.25 ? 42  PRO A CB  1 
ATOM   328  C  CG  . PRO A 1 42  ? -19.088 1.717   -19.744 1.00 29.19 ? 42  PRO A CG  1 
ATOM   329  C  CD  . PRO A 1 42  ? -18.741 0.945   -18.497 1.00 21.96 ? 42  PRO A CD  1 
ATOM   330  N  N   . SER A 1 43  ? -16.765 3.962   -18.547 1.00 21.63 ? 43  SER A N   1 
ATOM   331  C  CA  . SER A 1 43  ? -16.385 5.375   -18.430 1.00 25.79 ? 43  SER A CA  1 
ATOM   332  C  C   . SER A 1 43  ? -15.052 5.650   -17.631 1.00 26.43 ? 43  SER A C   1 
ATOM   333  O  O   . SER A 1 43  ? -14.538 6.812   -17.616 1.00 30.01 ? 43  SER A O   1 
ATOM   334  C  CB  . SER A 1 43  ? -17.516 6.172   -17.798 1.00 34.73 ? 43  SER A CB  1 
ATOM   335  O  OG  . SER A 1 43  ? -17.463 6.080   -16.404 1.00 31.04 ? 43  SER A OG  1 
ATOM   336  N  N   . LEU A 1 44  ? -14.554 4.631   -16.922 1.00 19.53 ? 44  LEU A N   1 
ATOM   337  C  CA  . LEU A 1 44  ? -13.221 4.682   -16.203 1.00 19.25 ? 44  LEU A CA  1 
ATOM   338  C  C   . LEU A 1 44  ? -12.107 4.857   -17.229 1.00 24.11 ? 44  LEU A C   1 
ATOM   339  O  O   . LEU A 1 44  ? -12.129 4.249   -18.300 1.00 24.94 ? 44  LEU A O   1 
ATOM   340  C  CB  . LEU A 1 44  ? -12.975 3.410   -15.361 1.00 16.94 ? 44  LEU A CB  1 
ATOM   341  C  CG  . LEU A 1 44  ? -13.689 3.377   -14.035 1.00 15.53 ? 44  LEU A CG  1 
ATOM   342  C  CD1 . LEU A 1 44  ? -13.456 1.984   -13.442 1.00 19.84 ? 44  LEU A CD1 1 
ATOM   343  C  CD2 . LEU A 1 44  ? -13.219 4.504   -13.123 1.00 16.87 ? 44  LEU A CD2 1 
ATOM   344  N  N   . LYS A 1 45  ? -11.130 5.693   -16.901 1.00 20.91 ? 45  LYS A N   1 
ATOM   345  C  CA  . LYS A 1 45  ? -10.007 5.891   -17.810 1.00 21.83 ? 45  LYS A CA  1 
ATOM   346  C  C   . LYS A 1 45  ? -8.835  4.995   -17.472 1.00 19.22 ? 45  LYS A C   1 
ATOM   347  O  O   . LYS A 1 45  ? -8.789  4.357   -16.359 1.00 20.47 ? 45  LYS A O   1 
ATOM   348  C  CB  . LYS A 1 45  ? -9.548  7.291   -17.735 1.00 23.17 ? 45  LYS A CB  1 
ATOM   349  C  CG  . LYS A 1 45  ? -10.571 8.321   -18.063 1.00 32.01 ? 45  LYS A CG  1 
ATOM   350  C  CD  . LYS A 1 45  ? -9.964  9.685   -17.785 1.00 41.45 ? 45  LYS A CD  1 
ATOM   351  C  CE  . LYS A 1 45  ? -10.478 10.706  -18.795 1.00 57.75 ? 45  LYS A CE  1 
ATOM   352  N  NZ  . LYS A 1 45  ? -9.964  12.084  -18.521 1.00 64.49 ? 45  LYS A NZ  1 
ATOM   353  N  N   . PRO A 1 46  ? -7.948  4.780   -18.491 1.00 20.38 ? 46  PRO A N   1 
ATOM   354  C  CA  . PRO A 1 46  ? -6.732  4.049   -18.127 1.00 17.40 ? 46  PRO A CA  1 
ATOM   355  C  C   . PRO A 1 46  ? -6.040  4.810   -17.000 1.00 13.35 ? 46  PRO A C   1 
ATOM   356  O  O   . PRO A 1 46  ? -6.112  6.050   -16.969 1.00 15.80 ? 46  PRO A O   1 
ATOM   357  C  CB  . PRO A 1 46  ? -5.886  4.111   -19.420 1.00 18.96 ? 46  PRO A CB  1 
ATOM   358  C  CG  . PRO A 1 46  ? -6.931  4.333   -20.525 1.00 21.98 ? 46  PRO A CG  1 
ATOM   359  C  CD  . PRO A 1 46  ? -7.995  5.193   -19.920 1.00 22.11 ? 46  PRO A CD  1 
ATOM   360  N  N   . LEU A 1 47  ? -5.388  4.096   -16.085 1.00 17.65 ? 47  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 47  ? -4.660  4.736   -15.086 1.00 15.64 ? 47  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 47  ? -3.403  5.342   -15.730 1.00 17.59 ? 47  LEU A C   1 
ATOM   363  O  O   . LEU A 1 47  ? -2.749  4.624   -16.529 1.00 21.71 ? 47  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 47  ? -4.345  3.634   -14.095 1.00 20.69 ? 47  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 47  ? -3.771  4.009   -12.828 1.00 19.53 ? 47  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 47  ? -4.789  4.858   -12.017 1.00 23.32 ? 47  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 47  ? -3.366  2.766   -12.004 1.00 20.97 ? 47  LEU A CD2 1 
ATOM   368  N  N   . SER A 1 48  ? -2.988  6.558   -15.334 1.00 15.11 ? 48  SER A N   1 
ATOM   369  C  CA  . SER A 1 48  ? -1.706  7.140   -15.777 1.00 14.42 ? 48  SER A CA  1 
ATOM   370  C  C   . SER A 1 48  ? -0.760  7.121   -14.564 1.00 12.82 ? 48  SER A C   1 
ATOM   371  O  O   . SER A 1 48  ? -1.011  7.847   -13.588 1.00 14.80 ? 48  SER A O   1 
ATOM   372  C  CB  . SER A 1 48  ? -2.010  8.550   -16.235 1.00 17.92 ? 48  SER A CB  1 
ATOM   373  O  OG  . SER A 1 48  ? -0.846  9.330   -16.391 1.00 20.04 ? 48  SER A OG  1 
ATOM   374  N  N   . VAL A 1 49  ? 0.266   6.341   -14.647 1.00 15.00 ? 49  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 49  ? 1.310   6.269   -13.658 1.00 15.83 ? 49  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 49  ? 2.566   6.882   -14.240 1.00 16.44 ? 49  VAL A C   1 
ATOM   377  O  O   . VAL A 1 49  ? 3.117   6.274   -15.146 1.00 21.98 ? 49  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 49  ? 1.571   4.813   -13.271 1.00 18.77 ? 49  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 49  ? 2.609   4.753   -12.159 1.00 24.11 ? 49  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 49  ? 0.297   4.078   -12.894 1.00 19.22 ? 49  VAL A CG2 1 
ATOM   381  N  N   . SER A 1 50  ? 3.048   8.035   -13.738 1.00 16.73 ? 50  SER A N   1 
ATOM   382  C  CA  . SER A 1 50  ? 4.261   8.659   -14.302 1.00 16.04 ? 50  SER A CA  1 
ATOM   383  C  C   . SER A 1 50  ? 5.265   8.773   -13.234 1.00 14.69 ? 50  SER A C   1 
ATOM   384  O  O   . SER A 1 50  ? 5.309   9.789   -12.519 1.00 17.72 ? 50  SER A O   1 
ATOM   385  C  CB  . SER A 1 50  ? 3.952   10.023  -14.925 1.00 22.31 ? 50  SER A CB  1 
ATOM   386  O  OG  . SER A 1 50  ? 2.847   9.883   -15.800 1.00 28.25 ? 50  SER A OG  1 
ATOM   387  N  N   . TYR A 1 51  ? 6.142   7.782   -13.131 1.00 18.26 ? 51  TYR A N   1 
ATOM   388  C  CA  . TYR A 1 51  ? 7.168   7.642   -12.081 1.00 16.98 ? 51  TYR A CA  1 
ATOM   389  C  C   . TYR A 1 51  ? 8.580   7.853   -12.612 1.00 19.44 ? 51  TYR A C   1 
ATOM   390  O  O   . TYR A 1 51  ? 9.526   7.686   -11.834 1.00 20.16 ? 51  TYR A O   1 
ATOM   391  C  CB  . TYR A 1 51  ? 7.085   6.247   -11.445 1.00 16.79 ? 51  TYR A CB  1 
ATOM   392  C  CG  . TYR A 1 51  ? 5.892   5.979   -10.529 1.00 12.63 ? 51  TYR A CG  1 
ATOM   393  C  CD1 . TYR A 1 51  ? 5.038   6.993   -10.093 1.00 13.59 ? 51  TYR A CD1 1 
ATOM   394  C  CD2 . TYR A 1 51  ? 5.632   4.680   -10.121 1.00 14.46 ? 51  TYR A CD2 1 
ATOM   395  C  CE1 . TYR A 1 51  ? 3.955   6.710   -9.241  1.00 13.95 ? 51  TYR A CE1 1 
ATOM   396  C  CE2 . TYR A 1 51  ? 4.598   4.352   -9.225  1.00 13.96 ? 51  TYR A CE2 1 
ATOM   397  C  CZ  . TYR A 1 51  ? 3.725   5.375   -8.828  1.00 12.68 ? 51  TYR A CZ  1 
ATOM   398  O  OH  . TYR A 1 51  ? 2.720   5.029   -7.957  1.00 12.38 ? 51  TYR A OH  1 
ATOM   399  N  N   . ASP A 1 52  ? 8.733   8.276   -13.889 1.00 18.84 ? 52  ASP A N   1 
ATOM   400  C  CA  . ASP A 1 52  ? 10.098  8.470   -14.424 1.00 22.26 ? 52  ASP A CA  1 
ATOM   401  C  C   . ASP A 1 52  ? 10.976  9.458   -13.631 1.00 24.59 ? 52  ASP A C   1 
ATOM   402  O  O   . ASP A 1 52  ? 12.184  9.264   -13.537 1.00 28.42 ? 52  ASP A O   1 
ATOM   403  C  CB  . ASP A 1 52  ? 10.077  8.839   -15.927 1.00 24.54 ? 52  ASP A CB  1 
ATOM   404  C  CG  . ASP A 1 52  ? 9.250   10.045  -16.229 1.00 40.52 ? 52  ASP A CG  1 
ATOM   405  O  OD1 . ASP A 1 52  ? 7.991   9.961   -16.196 1.00 54.28 ? 52  ASP A OD1 1 
ATOM   406  O  OD2 . ASP A 1 52  ? 9.881   11.081  -16.546 1.00 60.32 ? 52  ASP A OD2 1 
ATOM   407  N  N   . GLN A 1 53  ? 10.389  10.472  -13.009 1.00 21.57 ? 53  GLN A N   1 
ATOM   408  C  CA  . GLN A 1 53  ? 11.286  11.392  -12.231 1.00 23.37 ? 53  GLN A CA  1 
ATOM   409  C  C   . GLN A 1 53  ? 11.200  11.207  -10.739 1.00 16.05 ? 53  GLN A C   1 
ATOM   410  O  O   . GLN A 1 53  ? 11.583  12.110  -9.997  1.00 21.03 ? 53  GLN A O   1 
ATOM   411  C  CB  . GLN A 1 53  ? 11.010  12.885  -12.564 1.00 26.49 ? 53  GLN A CB  1 
ATOM   412  C  CG  . GLN A 1 53  ? 10.657  13.188  -13.987 1.00 34.51 ? 53  GLN A CG  1 
ATOM   413  C  CD  . GLN A 1 53  ? 11.906  13.338  -14.813 1.00 53.05 ? 53  GLN A CD  1 
ATOM   414  O  OE1 . GLN A 1 53  ? 13.012  12.944  -14.389 1.00 65.36 ? 53  GLN A OE1 1 
ATOM   415  N  NE2 . GLN A 1 53  ? 11.748  13.899  -16.001 1.00 80.15 ? 53  GLN A NE2 1 
ATOM   416  N  N   . ALA A 1 54  ? 10.670  10.044  -10.279 1.00 15.64 ? 54  ALA A N   1 
ATOM   417  C  CA  . ALA A 1 54  ? 10.505  9.899   -8.853  1.00 14.78 ? 54  ALA A CA  1 
ATOM   418  C  C   . ALA A 1 54  ? 11.895  9.993   -8.181  1.00 15.33 ? 54  ALA A C   1 
ATOM   419  O  O   . ALA A 1 54  ? 12.885  9.382   -8.661  1.00 19.54 ? 54  ALA A O   1 
ATOM   420  C  CB  . ALA A 1 54  ? 9.863   8.526   -8.499  1.00 15.65 ? 54  ALA A CB  1 
ATOM   421  N  N   . THR A 1 55  ? 11.937  10.696  -7.059  1.00 14.30 ? 55  THR A N   1 
ATOM   422  C  CA  . THR A 1 55  ? 13.150  10.830  -6.210  1.00 15.25 ? 55  THR A CA  1 
ATOM   423  C  C   . THR A 1 55  ? 12.959  10.259  -4.787  1.00 12.17 ? 55  THR A C   1 
ATOM   424  O  O   . THR A 1 55  ? 12.405  10.942  -3.957  1.00 14.90 ? 55  THR A O   1 
ATOM   425  C  CB  . THR A 1 55  ? 13.653  12.267  -6.057  1.00 20.08 ? 55  THR A CB  1 
ATOM   426  O  OG1 . THR A 1 55  ? 13.411  12.995  -7.262  1.00 28.95 ? 55  THR A OG1 1 
ATOM   427  C  CG2 . THR A 1 55  ? 15.153  12.259  -5.751  1.00 19.25 ? 55  THR A CG2 1 
ATOM   428  N  N   . SER A 1 56  ? 13.419  9.029   -4.547  1.00 12.21 ? 56  SER A N   1 
ATOM   429  C  CA  . SER A 1 56  ? 13.297  8.478   -3.189  1.00 12.57 ? 56  SER A CA  1 
ATOM   430  C  C   . SER A 1 56  ? 14.293  9.169   -2.231  1.00 10.61 ? 56  SER A C   1 
ATOM   431  O  O   . SER A 1 56  ? 15.360  9.686   -2.635  1.00 13.85 ? 56  SER A O   1 
ATOM   432  C  CB  . SER A 1 56  ? 13.496  6.955   -3.191  1.00 12.85 ? 56  SER A CB  1 
ATOM   433  O  OG  . SER A 1 56  ? 14.854  6.633   -3.595  1.00 13.31 ? 56  SER A OG  1 
ATOM   434  N  N   . LEU A 1 57  ? 13.950  9.259   -0.963  1.00 12.47 ? 57  LEU A N   1 
ATOM   435  C  CA  . LEU A 1 57  ? 14.819  9.921   0.053   1.00 12.84 ? 57  LEU A CA  1 
ATOM   436  C  C   . LEU A 1 57  ? 15.377  8.973   1.119   1.00 13.27 ? 57  LEU A C   1 
ATOM   437  O  O   . LEU A 1 57  ? 16.608  8.917   1.351   1.00 14.00 ? 57  LEU A O   1 
ATOM   438  C  CB  . LEU A 1 57  ? 14.094  11.095  0.768   1.00 16.12 ? 57  LEU A CB  1 
ATOM   439  C  CG  . LEU A 1 57  ? 13.879  12.350  -0.133  1.00 17.18 ? 57  LEU A CG  1 
ATOM   440  C  CD1 . LEU A 1 57  ? 12.889  13.224  0.636   1.00 18.00 ? 57  LEU A CD1 1 
ATOM   441  C  CD2 . LEU A 1 57  ? 15.193  13.107  -0.309  1.00 26.45 ? 57  LEU A CD2 1 
ATOM   442  N  N   A ARG A 1 58  ? 14.515  8.205   1.776   0.50 14.33 ? 58  ARG A N   1 
ATOM   443  N  N   B ARG A 1 58  ? 14.473  8.277   1.817   0.50 12.65 ? 58  ARG A N   1 
ATOM   444  C  CA  A ARG A 1 58  ? 14.958  7.401   2.901   0.50 14.05 ? 58  ARG A CA  1 
ATOM   445  C  CA  B ARG A 1 58  ? 14.798  7.614   3.085   0.50 12.02 ? 58  ARG A CA  1 
ATOM   446  C  C   A ARG A 1 58  ? 14.044  6.183   2.984   0.50 13.01 ? 58  ARG A C   1 
ATOM   447  C  C   B ARG A 1 58  ? 13.894  6.366   3.289   0.50 12.03 ? 58  ARG A C   1 
ATOM   448  O  O   A ARG A 1 58  ? 13.017  6.114   2.282   0.50 12.65 ? 58  ARG A O   1 
ATOM   449  O  O   B ARG A 1 58  ? 12.757  6.396   2.856   0.50 9.96  ? 58  ARG A O   1 
ATOM   450  C  CB  A ARG A 1 58  ? 14.814  8.160   4.237   0.50 17.14 ? 58  ARG A CB  1 
ATOM   451  C  CB  B ARG A 1 58  ? 14.646  8.607   4.271   0.50 12.03 ? 58  ARG A CB  1 
ATOM   452  C  CG  A ARG A 1 58  ? 15.493  9.490   4.367   0.50 20.22 ? 58  ARG A CG  1 
ATOM   453  C  CG  B ARG A 1 58  ? 15.803  9.623   4.355   0.50 12.01 ? 58  ARG A CG  1 
ATOM   454  C  CD  A ARG A 1 58  ? 15.129  9.927   5.756   0.50 21.11 ? 58  ARG A CD  1 
ATOM   455  C  CD  B ARG A 1 58  ? 15.913  10.355  5.699   0.50 11.79 ? 58  ARG A CD  1 
ATOM   456  N  NE  A ARG A 1 58  ? 13.983  9.148   6.145   0.50 18.98 ? 58  ARG A NE  1 
ATOM   457  N  NE  B ARG A 1 58  ? 16.338  9.403   6.727   0.50 10.49 ? 58  ARG A NE  1 
ATOM   458  C  CZ  A ARG A 1 58  ? 13.747  8.835   7.405   0.50 13.49 ? 58  ARG A CZ  1 
ATOM   459  C  CZ  B ARG A 1 58  ? 17.614  9.097   6.893   0.50 10.75 ? 58  ARG A CZ  1 
ATOM   460  N  NH1 A ARG A 1 58  ? 14.482  9.401   8.369   0.50 25.41 ? 58  ARG A NH1 1 
ATOM   461  N  NH1 B ARG A 1 58  ? 18.059  8.281   7.784   0.50 11.14 ? 58  ARG A NH1 1 
ATOM   462  N  NH2 A ARG A 1 58  ? 12.673  8.184   7.704   0.50 26.90 ? 58  ARG A NH2 1 
ATOM   463  N  NH2 B ARG A 1 58  ? 18.489  9.699   6.109   0.50 12.61 ? 58  ARG A NH2 1 
ATOM   464  N  N   . ILE A 1 59  ? 14.430  5.291   3.921   1.00 13.08 ? 59  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 59  ? 13.675  4.140   4.317   1.00 12.38 ? 59  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 59  ? 13.645  4.077   5.818   1.00 13.86 ? 59  ILE A C   1 
ATOM   467  O  O   . ILE A 1 59  ? 14.699  4.307   6.427   1.00 13.54 ? 59  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 59  ? 14.184  2.865   3.629   1.00 14.71 ? 59  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 59  ? 13.168  1.706   3.826   1.00 14.14 ? 59  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 59  ? 15.628  2.505   4.070   1.00 14.02 ? 59  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 59  ? 13.540  0.437   3.034   1.00 15.44 ? 59  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 60  ? 12.513  3.778   6.447   1.00 12.06 ? 60  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 60  ? 12.379  3.835   7.863   1.00 13.39 ? 60  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 60  ? 11.610  2.580   8.301   1.00 12.31 ? 60  LEU A C   1 
ATOM   475  O  O   . LEU A 1 60  ? 10.564  2.250   7.668   1.00 13.70 ? 60  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 60  ? 11.553  5.145   8.340   1.00 14.71 ? 60  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 60  ? 10.952  5.219   9.739   1.00 16.68 ? 60  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 60  ? 12.076  5.392   10.724  1.00 21.20 ? 60  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 60  ? 9.968   6.364   9.862   1.00 18.86 ? 60  LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 61  ? 12.006  1.943   9.385   1.00 11.36 ? 61  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 61  ? 11.207  0.987   10.134  1.00 11.83 ? 61  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 61  ? 10.403  1.774   11.169  1.00 13.60 ? 61  ASN A C   1 
ATOM   483  O  O   . ASN A 1 61  ? 11.037  2.304   12.163  1.00 13.89 ? 61  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 61  ? 12.102  -0.050  10.801  1.00 13.14 ? 61  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 61  ? 11.325  -1.037  11.592  1.00 12.40 ? 61  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 61  ? 10.224  -0.757  12.108  1.00 14.10 ? 61  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 61  ? 11.942  -2.241  11.750  1.00 12.64 ? 61  ASN A ND2 1 
ATOM   488  N  N   . ASN A 1 62  ? 9.115   1.884   10.988  1.00 13.39 ? 62  ASN A N   1 
ATOM   489  C  CA  . ASN A 1 62  ? 8.290   2.696   11.932  1.00 13.46 ? 62  ASN A CA  1 
ATOM   490  C  C   . ASN A 1 62  ? 7.647   1.863   13.027  1.00 14.87 ? 62  ASN A C   1 
ATOM   491  O  O   . ASN A 1 62  ? 6.805   2.346   13.847  1.00 18.81 ? 62  ASN A O   1 
ATOM   492  C  CB  . ASN A 1 62  ? 7.290   3.538   11.114  1.00 17.44 ? 62  ASN A CB  1 
ATOM   493  C  CG  . ASN A 1 62  ? 6.441   2.650   10.217  1.00 19.65 ? 62  ASN A CG  1 
ATOM   494  O  OD1 . ASN A 1 62  ? 5.927   1.663   10.710  1.00 17.08 ? 62  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A 1 62  ? 6.426   2.906   8.899   1.00 20.54 ? 62  ASN A ND2 1 
ATOM   496  N  N   . GLY A 1 63  ? 8.027   0.599   13.146  1.00 13.58 ? 63  GLY A N   1 
ATOM   497  C  CA  . GLY A 1 63  ? 7.487   -0.298  14.172  1.00 16.16 ? 63  GLY A CA  1 
ATOM   498  C  C   . GLY A 1 63  ? 6.211   -0.983  13.730  1.00 12.25 ? 63  GLY A C   1 
ATOM   499  O  O   . GLY A 1 63  ? 5.714   -1.864  14.437  1.00 16.84 ? 63  GLY A O   1 
ATOM   500  N  N   . HIS A 1 64  ? 5.635   -0.505  12.589  1.00 14.02 ? 64  HIS A N   1 
ATOM   501  C  CA  . HIS A 1 64  ? 4.409   -1.155  11.976  1.00 13.85 ? 64  HIS A CA  1 
ATOM   502  C  C   . HIS A 1 64  ? 4.757   -1.828  10.668  1.00 13.80 ? 64  HIS A C   1 
ATOM   503  O  O   . HIS A 1 64  ? 4.358   -2.981  10.426  1.00 16.54 ? 64  HIS A O   1 
ATOM   504  C  CB  . HIS A 1 64  ? 3.226   -0.181  11.786  1.00 13.21 ? 64  HIS A CB  1 
ATOM   505  C  CG  . HIS A 1 64  ? 2.909   0.571   13.074  1.00 14.83 ? 64  HIS A CG  1 
ATOM   506  N  ND1 . HIS A 1 64  ? 2.381   -0.048  14.174  1.00 18.12 ? 64  HIS A ND1 1 
ATOM   507  C  CD2 . HIS A 1 64  ? 3.047   1.881   13.389  1.00 17.21 ? 64  HIS A CD2 1 
ATOM   508  C  CE1 . HIS A 1 64  ? 2.196   0.844   15.149  1.00 19.63 ? 64  HIS A CE1 1 
ATOM   509  N  NE2 . HIS A 1 64  ? 2.620   2.026   14.688  1.00 17.72 ? 64  HIS A NE2 1 
ATOM   510  N  N   . ALA A 1 65  ? 5.513   -1.136  9.825   1.00 12.55 ? 65  ALA A N   1 
ATOM   511  C  CA  . ALA A 1 65  ? 5.989   -1.603  8.515   1.00 12.11 ? 65  ALA A CA  1 
ATOM   512  C  C   . ALA A 1 65  ? 7.292   -0.846  8.289   1.00 12.91 ? 65  ALA A C   1 
ATOM   513  O  O   . ALA A 1 65  ? 7.848   -0.220  9.205   1.00 13.32 ? 65  ALA A O   1 
ATOM   514  C  CB  . ALA A 1 65  ? 4.897   -1.358  7.431   1.00 14.32 ? 65  ALA A CB  1 
ATOM   515  N  N   . PHE A 1 66  ? 7.818   -0.937  7.083   1.00 10.85 ? 66  PHE A N   1 
ATOM   516  C  CA  . PHE A 1 66  ? 8.810   -0.009  6.644   1.00 12.20 ? 66  PHE A CA  1 
ATOM   517  C  C   . PHE A 1 66  ? 8.277   0.849   5.531   1.00 11.76 ? 66  PHE A C   1 
ATOM   518  O  O   . PHE A 1 66  ? 7.411   0.379   4.728   1.00 13.34 ? 66  PHE A O   1 
ATOM   519  C  CB  . PHE A 1 66  ? 10.156  -0.729  6.244   1.00 12.68 ? 66  PHE A CB  1 
ATOM   520  C  CG  . PHE A 1 66  ? 10.019  -1.579  4.996   1.00 11.13 ? 66  PHE A CG  1 
ATOM   521  C  CD1 . PHE A 1 66  ? 10.214  -1.064  3.713   1.00 11.27 ? 66  PHE A CD1 1 
ATOM   522  C  CD2 . PHE A 1 66  ? 9.753   -2.917  5.064   1.00 12.63 ? 66  PHE A CD2 1 
ATOM   523  C  CE1 . PHE A 1 66  ? 10.097  -1.795  2.546   1.00 11.69 ? 66  PHE A CE1 1 
ATOM   524  C  CE2 . PHE A 1 66  ? 9.643   -3.727  3.898   1.00 13.43 ? 66  PHE A CE2 1 
ATOM   525  C  CZ  . PHE A 1 66  ? 9.812   -3.175  2.612   1.00 11.05 ? 66  PHE A CZ  1 
ATOM   526  N  N   A ASN A 1 67  ? 8.679   2.131   5.576   0.50 12.21 ? 67  ASN A N   1 
ATOM   527  N  N   B ASN A 1 67  ? 8.778   2.056   5.407   0.50 11.92 ? 67  ASN A N   1 
ATOM   528  C  CA  A ASN A 1 67  ? 8.332   3.103   4.539   0.50 13.74 ? 67  ASN A CA  1 
ATOM   529  C  CA  B ASN A 1 67  ? 8.234   2.879   4.378   0.50 12.65 ? 67  ASN A CA  1 
ATOM   530  C  C   A ASN A 1 67  ? 9.535   3.481   3.692   0.50 12.89 ? 67  ASN A C   1 
ATOM   531  C  C   B ASN A 1 67  ? 9.337   3.697   3.762   0.50 12.77 ? 67  ASN A C   1 
ATOM   532  O  O   A ASN A 1 67  ? 10.627  3.652   4.174   0.50 12.78 ? 67  ASN A O   1 
ATOM   533  O  O   B ASN A 1 67  ? 10.188  4.311   4.509   0.50 11.04 ? 67  ASN A O   1 
ATOM   534  C  CB  A ASN A 1 67  ? 7.751   4.442   5.082   0.50 17.14 ? 67  ASN A CB  1 
ATOM   535  C  CB  B ASN A 1 67  ? 7.138   3.830   4.899   0.50 13.96 ? 67  ASN A CB  1 
ATOM   536  C  CG  A ASN A 1 67  ? 6.617   4.225   5.993   0.50 19.42 ? 67  ASN A CG  1 
ATOM   537  C  CG  B ASN A 1 67  ? 7.700   4.914   5.778   0.50 14.93 ? 67  ASN A CG  1 
ATOM   538  O  OD1 A ASN A 1 67  ? 6.430   4.943   6.994   0.50 23.88 ? 67  ASN A OD1 1 
ATOM   539  O  OD1 B ASN A 1 67  ? 7.847   4.726   6.982   0.50 17.95 ? 67  ASN A OD1 1 
ATOM   540  N  ND2 A ASN A 1 67  ? 5.831   3.183   5.671   0.50 16.61 ? 67  ASN A ND2 1 
ATOM   541  N  ND2 B ASN A 1 67  ? 7.994   6.076   5.200   0.50 20.72 ? 67  ASN A ND2 1 
ATOM   542  N  N   . VAL A 1 68  ? 9.305   3.670   2.425   1.00 10.70 ? 68  VAL A N   1 
ATOM   543  C  CA  . VAL A 1 68  ? 10.208  4.419   1.572   1.00 12.01 ? 68  VAL A CA  1 
ATOM   544  C  C   . VAL A 1 68  ? 9.519   5.743   1.268   1.00 13.11 ? 68  VAL A C   1 
ATOM   545  O  O   . VAL A 1 68  ? 8.448   5.750   0.625   1.00 13.13 ? 68  VAL A O   1 
ATOM   546  C  CB  . VAL A 1 68  ? 10.524  3.672   0.277   1.00 11.44 ? 68  VAL A CB  1 
ATOM   547  C  CG1 . VAL A 1 68  ? 11.331  4.535   -0.678  1.00 14.77 ? 68  VAL A CG1 1 
ATOM   548  C  CG2 . VAL A 1 68  ? 11.293  2.387   0.634   1.00 14.09 ? 68  VAL A CG2 1 
ATOM   549  N  N   A GLU A 1 69  ? 10.043  6.866   1.799   0.50 10.18 ? 69  GLU A N   1 
ATOM   550  N  N   B GLU A 1 69  ? 10.245  6.801   1.607   0.50 13.68 ? 69  GLU A N   1 
ATOM   551  C  CA  A GLU A 1 69  ? 9.515   8.220   1.494   0.50 10.59 ? 69  GLU A CA  1 
ATOM   552  C  CA  B GLU A 1 69  ? 9.853   8.161   1.453   0.50 12.55 ? 69  GLU A CA  1 
ATOM   553  C  C   A GLU A 1 69  ? 10.281  8.907   0.373   0.50 10.29 ? 69  GLU A C   1 
ATOM   554  C  C   B GLU A 1 69  ? 10.333  8.750   0.118   0.50 12.77 ? 69  GLU A C   1 
ATOM   555  O  O   A GLU A 1 69  ? 11.555  8.840   0.305   0.50 7.58  ? 69  GLU A O   1 
ATOM   556  O  O   B GLU A 1 69  ? 11.428  8.419   -0.436  0.50 14.49 ? 69  GLU A O   1 
ATOM   557  C  CB  A GLU A 1 69  ? 9.449   9.125   2.787   0.50 9.41  ? 69  GLU A CB  1 
ATOM   558  C  CB  B GLU A 1 69  ? 10.363  8.889   2.720   0.50 16.29 ? 69  GLU A CB  1 
ATOM   559  C  CG  A GLU A 1 69  ? 8.574   10.385  2.608   0.50 12.63 ? 69  GLU A CG  1 
ATOM   560  C  CG  B GLU A 1 69  ? 9.671   8.306   3.974   0.50 24.93 ? 69  GLU A CG  1 
ATOM   561  C  CD  A GLU A 1 69  ? 8.148   11.082  3.899   0.50 16.00 ? 69  GLU A CD  1 
ATOM   562  C  CD  B GLU A 1 69  ? 10.389  8.296   5.348   0.50 18.69 ? 69  GLU A CD  1 
ATOM   563  O  OE1 A GLU A 1 69  ? 8.161   12.345  3.864   0.50 18.18 ? 69  GLU A OE1 1 
ATOM   564  O  OE1 B GLU A 1 69  ? 11.476  7.584   5.582   0.50 15.69 ? 69  GLU A OE1 1 
ATOM   565  O  OE2 A GLU A 1 69  ? 7.796   10.408  4.915   0.50 20.57 ? 69  GLU A OE2 1 
ATOM   566  O  OE2 B GLU A 1 69  ? 9.686   8.920   6.243   0.50 20.67 ? 69  GLU A OE2 1 
ATOM   567  N  N   . PHE A 1 70  ? 9.499   9.609   -0.443  1.00 12.54 ? 70  PHE A N   1 
ATOM   568  C  CA  . PHE A 1 70  ? 9.960   10.332  -1.676  1.00 11.96 ? 70  PHE A CA  1 
ATOM   569  C  C   . PHE A 1 70  ? 9.924   11.881  -1.445  1.00 11.74 ? 70  PHE A C   1 
ATOM   570  O  O   . PHE A 1 70  ? 9.183   12.369  -0.635  1.00 14.60 ? 70  PHE A O   1 
ATOM   571  C  CB  . PHE A 1 70  ? 9.058   10.045  -2.889  1.00 11.98 ? 70  PHE A CB  1 
ATOM   572  C  CG  . PHE A 1 70  ? 9.214   8.640   -3.349  1.00 11.74 ? 70  PHE A CG  1 
ATOM   573  C  CD1 . PHE A 1 70  ? 8.689   7.550   -2.642  1.00 13.65 ? 70  PHE A CD1 1 
ATOM   574  C  CD2 . PHE A 1 70  ? 9.993   8.408   -4.465  1.00 12.54 ? 70  PHE A CD2 1 
ATOM   575  C  CE1 . PHE A 1 70  ? 8.935   6.222   -3.050  1.00 12.85 ? 70  PHE A CE1 1 
ATOM   576  C  CE2 . PHE A 1 70  ? 10.243  7.095   -4.914  1.00 12.61 ? 70  PHE A CE2 1 
ATOM   577  C  CZ  . PHE A 1 70  ? 9.693   6.004   -4.214  1.00 11.23 ? 70  PHE A CZ  1 
ATOM   578  N  N   . ASP A 1 71  ? 10.717  12.572  -2.260  1.00 15.12 ? 71  ASP A N   1 
ATOM   579  C  CA  . ASP A 1 71  ? 10.661  14.020  -2.276  1.00 14.36 ? 71  ASP A CA  1 
ATOM   580  C  C   . ASP A 1 71  ? 9.502   14.386  -3.181  1.00 16.09 ? 71  ASP A C   1 
ATOM   581  O  O   . ASP A 1 71  ? 9.568   14.192  -4.400  1.00 20.29 ? 71  ASP A O   1 
ATOM   582  C  CB  . ASP A 1 71  ? 11.976  14.568  -2.805  1.00 19.30 ? 71  ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 71  ? 11.929  16.089  -3.101  1.00 23.95 ? 71  ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 71  ? 11.000  16.724  -2.710  1.00 23.10 ? 71  ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 71  ? 12.797  16.583  -3.828  1.00 37.43 ? 71  ASP A OD2 1 
ATOM   586  N  N   . ASP A 1 72  ? 8.479   14.947  -2.598  1.00 15.16 ? 72  ASP A N   1 
ATOM   587  C  CA  . ASP A 1 72  ? 7.207   15.281  -3.246  1.00 16.00 ? 72  ASP A CA  1 
ATOM   588  C  C   . ASP A 1 72  ? 7.027   16.818  -3.326  1.00 21.23 ? 72  ASP A C   1 
ATOM   589  O  O   . ASP A 1 72  ? 5.896   17.331  -3.259  1.00 22.42 ? 72  ASP A O   1 
ATOM   590  C  CB  . ASP A 1 72  ? 6.035   14.656  -2.420  1.00 17.35 ? 72  ASP A CB  1 
ATOM   591  C  CG  . ASP A 1 72  ? 5.856   15.245  -1.004  1.00 18.20 ? 72  ASP A CG  1 
ATOM   592  O  OD1 . ASP A 1 72  ? 6.785   15.931  -0.464  1.00 18.10 ? 72  ASP A OD1 1 
ATOM   593  O  OD2 . ASP A 1 72  ? 4.831   15.032  -0.358  1.00 20.63 ? 72  ASP A OD2 1 
ATOM   594  N  N   . SER A 1 73  ? 8.157   17.509  -3.323  1.00 19.21 ? 73  SER A N   1 
ATOM   595  C  CA  . SER A 1 73  ? 8.117   19.009  -3.323  1.00 21.99 ? 73  SER A CA  1 
ATOM   596  C  C   . SER A 1 73  ? 8.032   19.557  -4.782  1.00 25.54 ? 73  SER A C   1 
ATOM   597  O  O   . SER A 1 73  ? 7.890   20.780  -4.964  1.00 21.71 ? 73  SER A O   1 
ATOM   598  C  CB  . SER A 1 73  ? 9.340   19.523  -2.596  1.00 27.28 ? 73  SER A CB  1 
ATOM   599  O  OG  . SER A 1 73  ? 10.488  19.374  -3.431  1.00 25.04 ? 73  SER A OG  1 
ATOM   600  N  N   . GLN A 1 74  ? 8.128   18.679  -5.784  1.00 25.69 ? 74  GLN A N   1 
ATOM   601  C  CA  . GLN A 1 74  ? 7.920   19.063  -7.179  1.00 24.78 ? 74  GLN A CA  1 
ATOM   602  C  C   . GLN A 1 74  ? 6.946   18.093  -7.736  1.00 26.83 ? 74  GLN A C   1 
ATOM   603  O  O   . GLN A 1 74  ? 6.701   17.004  -7.140  1.00 21.75 ? 74  GLN A O   1 
ATOM   604  C  CB  . GLN A 1 74  ? 9.218   19.052  -8.005  1.00 24.73 ? 74  GLN A CB  1 
ATOM   605  C  CG  . GLN A 1 74  ? 10.153  20.178  -7.532  1.00 29.64 ? 74  GLN A CG  1 
ATOM   606  C  CD  . GLN A 1 74  ? 11.463  20.124  -8.250  1.00 31.37 ? 74  GLN A CD  1 
ATOM   607  O  OE1 . GLN A 1 74  ? 11.496  20.106  -9.476  1.00 47.38 ? 74  GLN A OE1 1 
ATOM   608  N  NE2 . GLN A 1 74  ? 12.559  20.063  -7.494  1.00 36.12 ? 74  GLN A NE2 1 
ATOM   609  N  N   . ASP A 1 75  ? 6.476   18.500  -8.906  1.00 25.63 ? 75  ASP A N   1 
ATOM   610  C  CA  . ASP A 1 75  ? 5.553   17.811  -9.737  1.00 24.18 ? 75  ASP A CA  1 
ATOM   611  C  C   . ASP A 1 75  ? 6.327   16.680  -10.478 1.00 27.54 ? 75  ASP A C   1 
ATOM   612  O  O   . ASP A 1 75  ? 6.805   16.884  -11.605 1.00 29.72 ? 75  ASP A O   1 
ATOM   613  C  CB  . ASP A 1 75  ? 5.047   18.886  -10.756 1.00 25.32 ? 75  ASP A CB  1 
ATOM   614  C  CG  . ASP A 1 75  ? 4.048   18.336  -11.726 1.00 27.70 ? 75  ASP A CG  1 
ATOM   615  O  OD1 . ASP A 1 75  ? 3.659   17.144  -11.504 1.00 31.63 ? 75  ASP A OD1 1 
ATOM   616  O  OD2 . ASP A 1 75  ? 3.680   19.074  -12.716 1.00 41.20 ? 75  ASP A OD2 1 
ATOM   617  N  N   . LYS A 1 76  ? 6.527   15.526  -9.862  1.00 21.13 ? 76  LYS A N   1 
ATOM   618  C  CA  . LYS A 1 76  ? 7.335   14.478  -10.476 1.00 27.11 ? 76  LYS A CA  1 
ATOM   619  C  C   . LYS A 1 76  ? 6.581   13.206  -10.590 1.00 37.07 ? 76  LYS A C   1 
ATOM   620  O  O   . LYS A 1 76  ? 5.951   12.970  -11.625 1.00 43.12 ? 76  LYS A O   1 
ATOM   621  C  CB  . LYS A 1 76  ? 8.686   14.362  -9.679  1.00 25.99 ? 76  LYS A CB  1 
ATOM   622  C  CG  . LYS A 1 76  ? 9.539   15.637  -9.812  1.00 32.38 ? 76  LYS A CG  1 
ATOM   623  C  CD  . LYS A 1 76  ? 10.820  15.566  -8.997  1.00 35.16 ? 76  LYS A CD  1 
ATOM   624  C  CE  . LYS A 1 76  ? 10.675  15.296  -7.501  1.00 36.00 ? 76  LYS A CE  1 
ATOM   625  N  NZ  . LYS A 1 76  ? 9.615   16.061  -6.781  1.00 27.39 ? 76  LYS A NZ  1 
ATOM   626  N  N   . ALA A 1 77  ? 6.619   12.399  -9.558  1.00 26.63 ? 77  ALA A N   1 
ATOM   627  C  CA  . ALA A 1 77  ? 6.004   11.061  -9.576  1.00 20.04 ? 77  ALA A CA  1 
ATOM   628  C  C   . ALA A 1 77  ? 4.494   11.242  -9.349  1.00 16.25 ? 77  ALA A C   1 
ATOM   629  O  O   . ALA A 1 77  ? 4.080   11.460  -8.249  1.00 21.02 ? 77  ALA A O   1 
ATOM   630  C  CB  . ALA A 1 77  ? 6.634   10.267  -8.410  1.00 22.28 ? 77  ALA A CB  1 
ATOM   631  N  N   . VAL A 1 78  ? 3.685   11.145  -10.394 1.00 14.86 ? 78  VAL A N   1 
ATOM   632  C  CA  . VAL A 1 78  ? 2.238   11.409  -10.245 1.00 15.68 ? 78  VAL A CA  1 
ATOM   633  C  C   . VAL A 1 78  ? 1.287   10.340  -10.802 1.00 15.89 ? 78  VAL A C   1 
ATOM   634  O  O   . VAL A 1 78  ? 1.599   9.669   -11.761 1.00 16.14 ? 78  VAL A O   1 
ATOM   635  C  CB  . VAL A 1 78  ? 1.804   12.750  -10.845 1.00 20.90 ? 78  VAL A CB  1 
ATOM   636  C  CG1 . VAL A 1 78  ? 2.666   13.916  -10.426 1.00 24.31 ? 78  VAL A CG1 1 
ATOM   637  C  CG2 . VAL A 1 78  ? 1.894   12.709  -12.281 1.00 22.16 ? 78  VAL A CG2 1 
ATOM   638  N  N   . LEU A 1 79  ? 0.178   10.148  -10.096 1.00 12.38 ? 79  LEU A N   1 
ATOM   639  C  CA  . LEU A 1 79  ? -0.863  9.266   -10.530 1.00 13.54 ? 79  LEU A CA  1 
ATOM   640  C  C   . LEU A 1 79  ? -2.003  10.163  -10.982 1.00 13.03 ? 79  LEU A C   1 
ATOM   641  O  O   . LEU A 1 79  ? -2.391  11.115  -10.223 1.00 15.00 ? 79  LEU A O   1 
ATOM   642  C  CB  . LEU A 1 79  ? -1.206  8.359   -9.325  1.00 15.89 ? 79  LEU A CB  1 
ATOM   643  C  CG  . LEU A 1 79  ? -2.198  7.287   -9.531  1.00 15.05 ? 79  LEU A CG  1 
ATOM   644  C  CD1 . LEU A 1 79  ? -1.620  6.225   -10.446 1.00 17.66 ? 79  LEU A CD1 1 
ATOM   645  C  CD2 . LEU A 1 79  ? -2.450  6.625   -8.208  1.00 14.23 ? 79  LEU A CD2 1 
ATOM   646  N  N   . LYS A 1 80  ? -2.626  9.872   -12.113 1.00 14.36 ? 80  LYS A N   1 
ATOM   647  C  CA  . LYS A 1 80  ? -3.847  10.531  -12.483 1.00 15.42 ? 80  LYS A CA  1 
ATOM   648  C  C   . LYS A 1 80  ? -4.632  9.597   -13.405 1.00 13.86 ? 80  LYS A C   1 
ATOM   649  O  O   . LYS A 1 80  ? -4.239  8.457   -13.629 1.00 15.34 ? 80  LYS A O   1 
ATOM   650  C  CB  . LYS A 1 80  ? -3.626  11.845  -13.212 1.00 19.69 ? 80  LYS A CB  1 
ATOM   651  C  CG  . LYS A 1 80  ? -2.799  11.676  -14.441 1.00 20.63 ? 80  LYS A CG  1 
ATOM   652  C  CD  . LYS A 1 80  ? -2.579  13.036  -15.170 1.00 28.43 ? 80  LYS A CD  1 
ATOM   653  N  N   . GLY A 1 81  ? -5.750  10.121  -13.957 1.00 13.88 ? 81  GLY A N   1 
ATOM   654  C  CA  . GLY A 1 81  ? -6.579  9.289   -14.816 1.00 15.88 ? 81  GLY A CA  1 
ATOM   655  C  C   . GLY A 1 81  ? -7.253  8.237   -13.991 1.00 14.78 ? 81  GLY A C   1 
ATOM   656  O  O   . GLY A 1 81  ? -7.485  8.431   -12.756 1.00 15.21 ? 81  GLY A O   1 
ATOM   657  N  N   . GLY A 1 82  ? -7.560  7.105   -14.599 1.00 17.85 ? 82  GLY A N   1 
ATOM   658  C  CA  . GLY A 1 82  ? -8.331  6.103   -13.866 1.00 20.84 ? 82  GLY A CA  1 
ATOM   659  C  C   . GLY A 1 82  ? -9.616  6.717   -13.376 1.00 17.04 ? 82  GLY A C   1 
ATOM   660  O  O   . GLY A 1 82  ? -10.331 7.460   -14.104 1.00 21.74 ? 82  GLY A O   1 
ATOM   661  N  N   . PRO A 1 83  ? -9.952  6.508   -12.068 1.00 15.59 ? 83  PRO A N   1 
ATOM   662  C  CA  . PRO A 1 83  ? -11.135 7.109   -11.474 1.00 14.17 ? 83  PRO A CA  1 
ATOM   663  C  C   . PRO A 1 83  ? -10.890 8.544   -10.957 1.00 16.54 ? 83  PRO A C   1 
ATOM   664  O  O   . PRO A 1 83  ? -11.793 9.135   -10.441 1.00 18.29 ? 83  PRO A O   1 
ATOM   665  C  CB  . PRO A 1 83  ? -11.414 6.193   -10.266 1.00 14.96 ? 83  PRO A CB  1 
ATOM   666  C  CG  . PRO A 1 83  ? -10.064 5.786   -9.866  1.00 13.16 ? 83  PRO A CG  1 
ATOM   667  C  CD  . PRO A 1 83  ? -9.247  5.614   -11.132 1.00 14.54 ? 83  PRO A CD  1 
ATOM   668  N  N   . LEU A 1 84  ? -9.667  9.039   -11.041 1.00 12.05 ? 84  LEU A N   1 
ATOM   669  C  CA  . LEU A 1 84  ? -9.267  10.245  -10.305 1.00 12.79 ? 84  LEU A CA  1 
ATOM   670  C  C   . LEU A 1 84  ? -9.590  11.497  -11.084 1.00 14.30 ? 84  LEU A C   1 
ATOM   671  O  O   . LEU A 1 84  ? -9.476  11.511  -12.302 1.00 14.29 ? 84  LEU A O   1 
ATOM   672  C  CB  . LEU A 1 84  ? -7.769  10.192  -10.052 1.00 12.50 ? 84  LEU A CB  1 
ATOM   673  C  CG  . LEU A 1 84  ? -7.296  8.916   -9.269  1.00 12.01 ? 84  LEU A CG  1 
ATOM   674  C  CD1 . LEU A 1 84  ? -5.776  8.890   -9.296  1.00 13.75 ? 84  LEU A CD1 1 
ATOM   675  C  CD2 . LEU A 1 84  ? -7.909  8.902   -7.858  1.00 11.83 ? 84  LEU A CD2 1 
ATOM   676  N  N   . ASP A 1 85  ? -9.933  12.532  -10.335 1.00 14.41 ? 85  ASP A N   1 
ATOM   677  C  CA  . ASP A 1 85  ? -10.025 13.890  -10.851 1.00 16.48 ? 85  ASP A CA  1 
ATOM   678  C  C   . ASP A 1 85  ? -8.771  14.556  -10.412 1.00 17.73 ? 85  ASP A C   1 
ATOM   679  O  O   . ASP A 1 85  ? -8.410  14.530  -9.248  1.00 21.67 ? 85  ASP A O   1 
ATOM   680  C  CB  . ASP A 1 85  ? -11.277 14.633  -10.343 1.00 21.14 ? 85  ASP A CB  1 
ATOM   681  C  CG  . ASP A 1 85  ? -12.554 14.121  -10.990 1.00 27.29 ? 85  ASP A CG  1 
ATOM   682  O  OD1 . ASP A 1 85  ? -12.519 13.574  -12.105 1.00 29.87 ? 85  ASP A OD1 1 
ATOM   683  O  OD2 . ASP A 1 85  ? -13.644 14.235  -10.393 1.00 28.71 ? 85  ASP A OD2 1 
ATOM   684  N  N   . GLY A 1 86  ? -8.107  15.271  -11.314 1.00 21.48 ? 86  GLY A N   1 
ATOM   685  C  CA  . GLY A 1 86  ? -6.878  15.967  -10.882 1.00 17.72 ? 86  GLY A CA  1 
ATOM   686  C  C   . GLY A 1 86  ? -5.618  15.095  -10.802 1.00 17.80 ? 86  GLY A C   1 
ATOM   687  O  O   . GLY A 1 86  ? -5.521  14.085  -11.491 1.00 22.39 ? 86  GLY A O   1 
ATOM   688  N  N   A THR A 1 87  ? -4.665  15.523  -9.983  0.50 16.55 ? 87  THR A N   1 
ATOM   689  N  N   B THR A 1 87  ? -4.664  15.486  -9.968  0.50 15.57 ? 87  THR A N   1 
ATOM   690  C  CA  A THR A 1 87  ? -3.304  14.988  -9.989  0.50 17.30 ? 87  THR A CA  1 
ATOM   691  C  CA  B THR A 1 87  ? -3.344  14.858  -9.992  0.50 15.20 ? 87  THR A CA  1 
ATOM   692  C  C   A THR A 1 87  ? -3.001  14.569  -8.568  0.50 13.27 ? 87  THR A C   1 
ATOM   693  C  C   B THR A 1 87  ? -2.834  14.611  -8.583  0.50 13.00 ? 87  THR A C   1 
ATOM   694  O  O   A THR A 1 87  ? -3.393  15.285  -7.620  0.50 11.18 ? 87  THR A O   1 
ATOM   695  O  O   B THR A 1 87  ? -2.865  15.467  -7.673  0.50 11.01 ? 87  THR A O   1 
ATOM   696  C  CB  A THR A 1 87  ? -2.295  16.092  -10.448 0.50 19.88 ? 87  THR A CB  1 
ATOM   697  C  CB  B THR A 1 87  ? -2.320  15.748  -10.725 0.50 15.90 ? 87  THR A CB  1 
ATOM   698  O  OG1 A THR A 1 87  ? -2.619  16.508  -11.778 0.50 18.82 ? 87  THR A OG1 1 
ATOM   699  O  OG1 B THR A 1 87  ? -2.440  17.055  -10.157 0.50 15.93 ? 87  THR A OG1 1 
ATOM   700  C  CG2 A THR A 1 87  ? -0.805  15.615  -10.358 0.50 17.40 ? 87  THR A CG2 1 
ATOM   701  C  CG2 B THR A 1 87  ? -2.601  15.805  -12.204 0.50 15.08 ? 87  THR A CG2 1 
ATOM   702  N  N   . TYR A 1 88  ? -2.378  13.405  -8.418  1.00 11.40 ? 88  TYR A N   1 
ATOM   703  C  CA  . TYR A 1 88  ? -1.962  12.960  -7.067  1.00 11.64 ? 88  TYR A CA  1 
ATOM   704  C  C   . TYR A 1 88  ? -0.480  12.653  -7.087  1.00 12.14 ? 88  TYR A C   1 
ATOM   705  O  O   . TYR A 1 88  ? 0.023   11.983  -8.011  1.00 15.59 ? 88  TYR A O   1 
ATOM   706  C  CB  . TYR A 1 88  ? -2.759  11.714  -6.696  1.00 11.33 ? 88  TYR A CB  1 
ATOM   707  C  CG  . TYR A 1 88  ? -4.206  11.952  -6.385  1.00 9.80  ? 88  TYR A CG  1 
ATOM   708  C  CD1 . TYR A 1 88  ? -5.133  12.248  -7.393  1.00 11.09 ? 88  TYR A CD1 1 
ATOM   709  C  CD2 . TYR A 1 88  ? -4.694  11.772  -5.103  1.00 9.86  ? 88  TYR A CD2 1 
ATOM   710  C  CE1 . TYR A 1 88  ? -6.495  12.390  -7.143  1.00 12.01 ? 88  TYR A CE1 1 
ATOM   711  C  CE2 . TYR A 1 88  ? -6.038  11.910  -4.812  1.00 9.73  ? 88  TYR A CE2 1 
ATOM   712  C  CZ  . TYR A 1 88  ? -6.957  12.199  -5.823  1.00 9.75  ? 88  TYR A CZ  1 
ATOM   713  O  OH  . TYR A 1 88  ? -8.267  12.293  -5.566  1.00 10.96 ? 88  TYR A OH  1 
ATOM   714  N  N   A ARG A 1 89  ? 0.240   13.143  -6.078  0.50 10.89 ? 89  ARG A N   1 
ATOM   715  N  N   B ARG A 1 89  ? 0.242   13.128  -6.079  0.50 10.86 ? 89  ARG A N   1 
ATOM   716  C  CA  A ARG A 1 89  ? 1.697   12.989  -5.982  0.50 12.38 ? 89  ARG A CA  1 
ATOM   717  C  CA  B ARG A 1 89  ? 1.690   13.031  -6.060  0.50 11.65 ? 89  ARG A CA  1 
ATOM   718  C  C   A ARG A 1 89  ? 2.133   11.916  -5.130  0.50 9.90  ? 89  ARG A C   1 
ATOM   719  C  C   B ARG A 1 89  ? 2.167   11.945  -5.123  0.50 10.00 ? 89  ARG A C   1 
ATOM   720  O  O   A ARG A 1 89  ? 1.583   11.755  -4.013  0.50 10.60 ? 89  ARG A O   1 
ATOM   721  O  O   B ARG A 1 89  ? 1.716   11.843  -3.970  0.50 10.68 ? 89  ARG A O   1 
ATOM   722  C  CB  A ARG A 1 89  ? 2.287   14.246  -5.294  0.50 14.72 ? 89  ARG A CB  1 
ATOM   723  C  CB  B ARG A 1 89  ? 2.277   14.389  -5.646  0.50 12.32 ? 89  ARG A CB  1 
ATOM   724  C  CG  A ARG A 1 89  ? 2.314   15.503  -6.046  0.50 15.75 ? 89  ARG A CG  1 
ATOM   725  C  CG  B ARG A 1 89  ? 3.768   14.532  -5.829  0.50 14.48 ? 89  ARG A CG  1 
ATOM   726  C  CD  A ARG A 1 89  ? 3.669   16.164  -6.088  0.50 21.26 ? 89  ARG A CD  1 
ATOM   727  C  CD  B ARG A 1 89  ? 4.220   15.958  -5.565  0.50 17.59 ? 89  ARG A CD  1 
ATOM   728  N  NE  A ARG A 1 89  ? 3.538   17.341  -6.922  0.50 20.71 ? 89  ARG A NE  1 
ATOM   729  N  NE  B ARG A 1 89  ? 3.567   16.905  -6.464  0.50 18.71 ? 89  ARG A NE  1 
ATOM   730  C  CZ  A ARG A 1 89  ? 3.687   18.584  -6.489  0.50 22.15 ? 89  ARG A CZ  1 
ATOM   731  C  CZ  B ARG A 1 89  ? 3.671   18.224  -6.358  0.50 20.18 ? 89  ARG A CZ  1 
ATOM   732  N  NH1 A ARG A 1 89  ? 4.010   18.815  -5.225  0.50 21.79 ? 89  ARG A NH1 1 
ATOM   733  N  NH1 B ARG A 1 89  ? 4.403   18.744  -5.386  0.50 18.93 ? 89  ARG A NH1 1 
ATOM   734  N  NH2 A ARG A 1 89  ? 3.521   19.591  -7.332  0.50 21.41 ? 89  ARG A NH2 1 
ATOM   735  N  NH2 B ARG A 1 89  ? 3.040   19.018  -7.215  0.50 16.94 ? 89  ARG A NH2 1 
ATOM   736  N  N   . LEU A 1 90  ? 3.115   11.117  -5.610  1.00 11.04 ? 90  LEU A N   1 
ATOM   737  C  CA  . LEU A 1 90  ? 3.634   10.018  -4.792  1.00 11.56 ? 90  LEU A CA  1 
ATOM   738  C  C   . LEU A 1 90  ? 4.400   10.566  -3.589  1.00 10.32 ? 90  LEU A C   1 
ATOM   739  O  O   . LEU A 1 90  ? 5.292   11.463  -3.747  1.00 12.58 ? 90  LEU A O   1 
ATOM   740  C  CB  . LEU A 1 90  ? 4.604   9.162   -5.610  1.00 11.88 ? 90  LEU A CB  1 
ATOM   741  C  CG  . LEU A 1 90  ? 5.271   7.998   -4.868  1.00 12.35 ? 90  LEU A CG  1 
ATOM   742  C  CD1 . LEU A 1 90  ? 4.300   6.937   -4.397  1.00 12.94 ? 90  LEU A CD1 1 
ATOM   743  C  CD2 . LEU A 1 90  ? 6.318   7.378   -5.765  1.00 13.61 ? 90  LEU A CD2 1 
ATOM   744  N  N   . ILE A 1 91  ? 4.087   10.106  -2.402  1.00 10.71 ? 91  ILE A N   1 
ATOM   745  C  CA  . ILE A 1 91  ? 4.837   10.476  -1.181  1.00 10.70 ? 91  ILE A CA  1 
ATOM   746  C  C   . ILE A 1 91  ? 5.577   9.314   -0.542  1.00 11.50 ? 91  ILE A C   1 
ATOM   747  O  O   . ILE A 1 91  ? 6.725   9.459   -0.083  1.00 10.74 ? 91  ILE A O   1 
ATOM   748  C  CB  . ILE A 1 91  ? 3.974   11.217  -0.151  1.00 10.27 ? 91  ILE A CB  1 
ATOM   749  C  CG1 . ILE A 1 91  ? 4.712   11.507  1.158   1.00 14.88 ? 91  ILE A CG1 1 
ATOM   750  C  CG2 . ILE A 1 91  ? 2.677   10.417  0.169   1.00 12.66 ? 91  ILE A CG2 1 
ATOM   751  C  CD1 . ILE A 1 91  ? 4.023   12.527  2.030   1.00 18.02 ? 91  ILE A CD1 1 
ATOM   752  N  N   . GLN A 1 92  ? 4.991   8.080   -0.558  1.00 10.74 ? 92  GLN A N   1 
ATOM   753  C  CA  . GLN A 1 92  ? 5.762   6.967   0.076   1.00 10.86 ? 92  GLN A CA  1 
ATOM   754  C  C   . GLN A 1 92  ? 5.134   5.675   -0.445  1.00 10.61 ? 92  GLN A C   1 
ATOM   755  O  O   . GLN A 1 92  ? 4.031   5.680   -0.991  1.00 10.48 ? 92  GLN A O   1 
ATOM   756  C  CB  . GLN A 1 92  ? 5.689   7.000   1.610   1.00 12.16 ? 92  GLN A CB  1 
ATOM   757  C  CG  . GLN A 1 92  ? 4.298   6.939   2.232   1.00 13.89 ? 92  GLN A CG  1 
ATOM   758  C  CD  . GLN A 1 92  ? 4.100   5.645   2.970   1.00 14.14 ? 92  GLN A CD  1 
ATOM   759  O  OE1 . GLN A 1 92  ? 3.927   4.585   2.346   1.00 15.03 ? 92  GLN A OE1 1 
ATOM   760  N  NE2 . GLN A 1 92  ? 4.205   5.672   4.250   1.00 22.36 ? 92  GLN A NE2 1 
ATOM   761  N  N   . PHE A 1 93  ? 5.870   4.557   -0.253  1.00 10.36 ? 93  PHE A N   1 
ATOM   762  C  CA  . PHE A 1 93  ? 5.271   3.202   -0.339  1.00 9.61  ? 93  PHE A CA  1 
ATOM   763  C  C   . PHE A 1 93  ? 5.662   2.415   0.854   1.00 8.81  ? 93  PHE A C   1 
ATOM   764  O  O   . PHE A 1 93  ? 6.656   2.647   1.539   1.00 9.47  ? 93  PHE A O   1 
ATOM   765  C  CB  . PHE A 1 93  ? 5.575   2.512   -1.697  1.00 10.08 ? 93  PHE A CB  1 
ATOM   766  C  CG  . PHE A 1 93  ? 6.985   2.115   -1.909  1.00 9.80  ? 93  PHE A CG  1 
ATOM   767  C  CD1 . PHE A 1 93  ? 7.499   0.969   -1.269  1.00 11.39 ? 93  PHE A CD1 1 
ATOM   768  C  CD2 . PHE A 1 93  ? 7.805   2.813   -2.797  1.00 10.87 ? 93  PHE A CD2 1 
ATOM   769  C  CE1 . PHE A 1 93  ? 8.831   0.605   -1.472  1.00 10.71 ? 93  PHE A CE1 1 
ATOM   770  C  CE2 . PHE A 1 93  ? 9.106   2.376   -3.035  1.00 10.73 ? 93  PHE A CE2 1 
ATOM   771  C  CZ  . PHE A 1 93  ? 9.630   1.272   -2.391  1.00 11.22 ? 93  PHE A CZ  1 
ATOM   772  N  N   . HIS A 1 94  ? 4.884   1.381   1.099   1.00 8.86  ? 94  HIS A N   1 
ATOM   773  C  CA  . HIS A 1 94  ? 5.134   0.417   2.166   1.00 8.59  ? 94  HIS A CA  1 
ATOM   774  C  C   . HIS A 1 94  ? 4.409   -0.863  1.728   1.00 8.15  ? 94  HIS A C   1 
ATOM   775  O  O   . HIS A 1 94  ? 3.698   -0.898  0.746   1.00 8.01  ? 94  HIS A O   1 
ATOM   776  C  CB  . HIS A 1 94  ? 4.612   0.916   3.537   1.00 8.58  ? 94  HIS A CB  1 
ATOM   777  C  CG  . HIS A 1 94  ? 3.132   1.178   3.464   1.00 7.89  ? 94  HIS A CG  1 
ATOM   778  N  ND1 . HIS A 1 94  ? 2.583   2.389   3.035   1.00 9.05  ? 94  HIS A ND1 1 
ATOM   779  C  CD2 . HIS A 1 94  ? 2.077   0.342   3.703   1.00 8.06  ? 94  HIS A CD2 1 
ATOM   780  C  CE1 . HIS A 1 94  ? 1.246   2.248   3.014   1.00 9.10  ? 94  HIS A CE1 1 
ATOM   781  N  NE2 . HIS A 1 94  ? 0.938   1.022   3.432   1.00 8.17  ? 94  HIS A NE2 1 
ATOM   782  N  N   . PHE A 1 95  ? 4.642   -1.901  2.553   1.00 8.59  ? 95  PHE A N   1 
ATOM   783  C  CA  . PHE A 1 95  ? 4.027   -3.206  2.323   1.00 8.23  ? 95  PHE A CA  1 
ATOM   784  C  C   . PHE A 1 95  ? 3.334   -3.673  3.575   1.00 8.39  ? 95  PHE A C   1 
ATOM   785  O  O   . PHE A 1 95  ? 3.653   -3.245  4.721   1.00 9.07  ? 95  PHE A O   1 
ATOM   786  C  CB  . PHE A 1 95  ? 5.080   -4.272  1.984   1.00 9.14  ? 95  PHE A CB  1 
ATOM   787  C  CG  . PHE A 1 95  ? 5.877   -3.994  0.701   1.00 8.09  ? 95  PHE A CG  1 
ATOM   788  C  CD1 . PHE A 1 95  ? 6.935   -3.086  0.733   1.00 9.81  ? 95  PHE A CD1 1 
ATOM   789  C  CD2 . PHE A 1 95  ? 5.645   -4.646  -0.499  1.00 9.55  ? 95  PHE A CD2 1 
ATOM   790  C  CE1 . PHE A 1 95  ? 7.722   -2.842  -0.415  1.00 10.98 ? 95  PHE A CE1 1 
ATOM   791  C  CE2 . PHE A 1 95  ? 6.415   -4.440  -1.609  1.00 9.25  ? 95  PHE A CE2 1 
ATOM   792  C  CZ  . PHE A 1 95  ? 7.500   -3.519  -1.587  1.00 10.74 ? 95  PHE A CZ  1 
ATOM   793  N  N   . HIS A 1 96  ? 2.444   -4.666  3.380   1.00 8.32  ? 96  HIS A N   1 
ATOM   794  C  CA  . HIS A 1 96  ? 1.864   -5.451  4.447   1.00 8.59  ? 96  HIS A CA  1 
ATOM   795  C  C   . HIS A 1 96  ? 2.155   -6.905  4.061   1.00 8.31  ? 96  HIS A C   1 
ATOM   796  O  O   . HIS A 1 96  ? 2.096   -7.253  2.882   1.00 9.04  ? 96  HIS A O   1 
ATOM   797  C  CB  . HIS A 1 96  ? 0.362   -5.242  4.572   1.00 8.84  ? 96  HIS A CB  1 
ATOM   798  C  CG  . HIS A 1 96  ? -0.017  -3.826  4.746   1.00 8.20  ? 96  HIS A CG  1 
ATOM   799  N  ND1 . HIS A 1 96  ? -0.274  -3.265  5.978   1.00 8.98  ? 96  HIS A ND1 1 
ATOM   800  C  CD2 . HIS A 1 96  ? -0.101  -2.816  3.835   1.00 8.81  ? 96  HIS A CD2 1 
ATOM   801  C  CE1 . HIS A 1 96  ? -0.597  -1.952  5.815   1.00 9.70  ? 96  HIS A CE1 1 
ATOM   802  N  NE2 . HIS A 1 96  ? -0.487  -1.652  4.508   1.00 7.30  ? 96  HIS A NE2 1 
ATOM   803  N  N   . TRP A 1 97  ? 2.505   -7.761  5.015   1.00 8.67  ? 97  TRP A N   1 
ATOM   804  C  CA  . TRP A 1 97  ? 2.833   -9.147  4.651   1.00 8.81  ? 97  TRP A CA  1 
ATOM   805  C  C   . TRP A 1 97  ? 2.553   -10.060 5.853   1.00 8.18  ? 97  TRP A C   1 
ATOM   806  O  O   . TRP A 1 97  ? 2.234   -9.644  6.990   1.00 8.96  ? 97  TRP A O   1 
ATOM   807  C  CB  . TRP A 1 97  ? 4.309   -9.284  4.255   1.00 9.35  ? 97  TRP A CB  1 
ATOM   808  C  CG  . TRP A 1 97  ? 5.284   -8.903  5.360   1.00 8.90  ? 97  TRP A CG  1 
ATOM   809  C  CD1 . TRP A 1 97  ? 5.854   -9.734  6.284   1.00 10.31 ? 97  TRP A CD1 1 
ATOM   810  C  CD2 . TRP A 1 97  ? 5.817   -7.581  5.619   1.00 8.69  ? 97  TRP A CD2 1 
ATOM   811  N  NE1 . TRP A 1 97  ? 6.718   -9.018  7.063   1.00 10.28 ? 97  TRP A NE1 1 
ATOM   812  C  CE2 . TRP A 1 97  ? 6.706   -7.709  6.735   1.00 9.04  ? 97  TRP A CE2 1 
ATOM   813  C  CE3 . TRP A 1 97  ? 5.630   -6.308  5.029   1.00 9.19  ? 97  TRP A CE3 1 
ATOM   814  C  CZ2 . TRP A 1 97  ? 7.418   -6.629  7.250   1.00 11.02 ? 97  TRP A CZ2 1 
ATOM   815  C  CZ3 . TRP A 1 97  ? 6.308   -5.215  5.566   1.00 10.77 ? 97  TRP A CZ3 1 
ATOM   816  C  CH2 . TRP A 1 97  ? 7.185   -5.349  6.678   1.00 9.92  ? 97  TRP A CH2 1 
ATOM   817  N  N   . GLY A 1 98  ? 2.635   -11.385 5.558   1.00 9.04  ? 98  GLY A N   1 
ATOM   818  C  CA  . GLY A 1 98  ? 2.189   -12.406 6.536   1.00 9.92  ? 98  GLY A CA  1 
ATOM   819  C  C   . GLY A 1 98  ? 3.377   -13.128 7.149   1.00 9.94  ? 98  GLY A C   1 
ATOM   820  O  O   . GLY A 1 98  ? 4.559   -12.976 6.744   1.00 10.30 ? 98  GLY A O   1 
ATOM   821  N  N   . SER A 1 99  ? 3.006   -14.027 8.092   1.00 11.19 ? 99  SER A N   1 
ATOM   822  C  CA  . SER A 1 99  ? 4.023   -14.941 8.690   1.00 12.99 ? 99  SER A CA  1 
ATOM   823  C  C   . SER A 1 99  ? 4.214   -16.179 7.814   1.00 11.85 ? 99  SER A C   1 
ATOM   824  O  O   . SER A 1 99  ? 5.213   -16.926 8.022   1.00 15.75 ? 99  SER A O   1 
ATOM   825  C  CB  . SER A 1 99  ? 3.496   -15.310 10.054  1.00 14.43 ? 99  SER A CB  1 
ATOM   826  O  OG  . SER A 1 99  ? 2.182   -15.855 10.003  1.00 13.61 ? 99  SER A OG  1 
ATOM   827  N  N   . LEU A 1 100 ? 3.319   -16.414 6.861   1.00 13.01 ? 100 LEU A N   1 
ATOM   828  C  CA  . LEU A 1 100 ? 3.334   -17.540 5.953   1.00 14.42 ? 100 LEU A CA  1 
ATOM   829  C  C   . LEU A 1 100 ? 2.866   -17.067 4.586   1.00 12.62 ? 100 LEU A C   1 
ATOM   830  O  O   . LEU A 1 100 ? 2.158   -16.043 4.501   1.00 12.72 ? 100 LEU A O   1 
ATOM   831  C  CB  . LEU A 1 100 ? 2.270   -18.567 6.353   1.00 19.34 ? 100 LEU A CB  1 
ATOM   832  C  CG  . LEU A 1 100 ? 2.460   -19.006 7.748   1.00 22.81 ? 100 LEU A CG  1 
ATOM   833  C  CD1 . LEU A 1 100 ? 1.137   -19.220 8.472   1.00 34.95 ? 100 LEU A CD1 1 
ATOM   834  C  CD2 . LEU A 1 100 ? 3.404   -20.191 7.684   1.00 29.91 ? 100 LEU A CD2 1 
ATOM   835  N  N   . ASP A 1 101 ? 3.116   -17.781 3.513   1.00 12.41 ? 101 ASP A N   1 
ATOM   836  C  CA  . ASP A 1 101 ? 2.827   -17.274 2.129   1.00 12.53 ? 101 ASP A CA  1 
ATOM   837  C  C   . ASP A 1 101 ? 1.343   -17.198 1.895   1.00 12.54 ? 101 ASP A C   1 
ATOM   838  O  O   . ASP A 1 101 ? 0.946   -16.468 1.016   1.00 14.23 ? 101 ASP A O   1 
ATOM   839  C  CB  . ASP A 1 101 ? 3.459   -18.147 1.054   1.00 15.92 ? 101 ASP A CB  1 
ATOM   840  C  CG  . ASP A 1 101 ? 5.008   -18.204 1.126   1.00 17.70 ? 101 ASP A CG  1 
ATOM   841  O  OD1 . ASP A 1 101 ? 5.683   -17.370 1.761   1.00 15.37 ? 101 ASP A OD1 1 
ATOM   842  O  OD2 . ASP A 1 101 ? 5.591   -19.087 0.473   1.00 21.48 ? 101 ASP A OD2 1 
ATOM   843  N  N   . GLY A 1 102 ? 0.518   -17.956 2.659   1.00 12.82 ? 102 GLY A N   1 
ATOM   844  C  CA  . GLY A 1 102 ? -0.921  -17.908 2.501   1.00 13.68 ? 102 GLY A CA  1 
ATOM   845  C  C   . GLY A 1 102 ? -1.688  -16.764 3.088   1.00 12.21 ? 102 GLY A C   1 
ATOM   846  O  O   . GLY A 1 102 ? -2.931  -16.732 3.049   1.00 13.75 ? 102 GLY A O   1 
ATOM   847  N  N   . GLN A 1 103 ? -1.001  -15.754 3.647   1.00 11.47 ? 103 GLN A N   1 
ATOM   848  C  CA  . GLN A 1 103 ? -1.720  -14.568 4.182   1.00 10.71 ? 103 GLN A CA  1 
ATOM   849  C  C   . GLN A 1 103 ? -0.732  -13.470 4.112   1.00 9.22  ? 103 GLN A C   1 
ATOM   850  O  O   . GLN A 1 103 ? 0.470   -13.662 3.955   1.00 10.44 ? 103 GLN A O   1 
ATOM   851  C  CB  . GLN A 1 103 ? -2.211  -14.876 5.606   1.00 11.34 ? 103 GLN A CB  1 
ATOM   852  C  CG  . GLN A 1 103 ? -1.094  -15.078 6.624   1.00 12.22 ? 103 GLN A CG  1 
ATOM   853  C  CD  . GLN A 1 103 ? -1.590  -15.733 7.862   1.00 17.87 ? 103 GLN A CD  1 
ATOM   854  O  OE1 . GLN A 1 103 ? -2.283  -16.745 7.757   1.00 26.04 ? 103 GLN A OE1 1 
ATOM   855  N  NE2 . GLN A 1 103 ? -1.269  -15.199 9.029   1.00 14.84 ? 103 GLN A NE2 1 
ATOM   856  N  N   . GLY A 1 104 ? -1.247  -12.241 4.275   1.00 9.03  ? 104 GLY A N   1 
ATOM   857  C  CA  . GLY A 1 104 ? -0.402  -11.034 4.289   1.00 9.34  ? 104 GLY A CA  1 
ATOM   858  C  C   . GLY A 1 104 ? -1.066  -9.873  3.623   1.00 8.30  ? 104 GLY A C   1 
ATOM   859  O  O   . GLY A 1 104 ? -0.785  -8.727  3.990   1.00 9.70  ? 104 GLY A O   1 
ATOM   860  N  N   . SER A 1 105 ? -1.841  -10.116 2.536   1.00 7.80  ? 105 SER A N   1 
ATOM   861  C  CA  . SER A 1 105 ? -2.519  -8.994  1.878   1.00 8.12  ? 105 SER A CA  1 
ATOM   862  C  C   . SER A 1 105 ? -3.638  -8.451  2.752   1.00 8.29  ? 105 SER A C   1 
ATOM   863  O  O   . SER A 1 105 ? -4.186  -9.120  3.635   1.00 9.15  ? 105 SER A O   1 
ATOM   864  C  CB  . SER A 1 105 ? -3.013  -9.372  0.501   1.00 8.66  ? 105 SER A CB  1 
ATOM   865  O  OG  . SER A 1 105 ? -4.066  -10.335 0.493   1.00 8.85  ? 105 SER A OG  1 
ATOM   866  N  N   . GLU A 1 106 ? -3.987  -7.189  2.485   1.00 8.00  ? 106 GLU A N   1 
ATOM   867  C  CA  . GLU A 1 106 ? -5.108  -6.481  3.182   1.00 8.15  ? 106 GLU A CA  1 
ATOM   868  C  C   . GLU A 1 106 ? -6.404  -6.683  2.369   1.00 7.63  ? 106 GLU A C   1 
ATOM   869  O  O   . GLU A 1 106 ? -7.376  -7.298  2.841   1.00 7.87  ? 106 GLU A O   1 
ATOM   870  C  CB  . GLU A 1 106 ? -4.731  -5.036  3.393   1.00 8.46  ? 106 GLU A CB  1 
ATOM   871  C  CG  . GLU A 1 106 ? -3.496  -4.895  4.274   1.00 9.66  ? 106 GLU A CG  1 
ATOM   872  C  CD  . GLU A 1 106 ? -3.555  -3.626  5.030   1.00 9.07  ? 106 GLU A CD  1 
ATOM   873  O  OE1 . GLU A 1 106 ? -3.570  -2.548  4.404   1.00 9.18  ? 106 GLU A OE1 1 
ATOM   874  O  OE2 . GLU A 1 106 ? -3.532  -3.655  6.277   1.00 9.74  ? 106 GLU A OE2 1 
ATOM   875  N  N   . HIS A 1 107 ? -6.373  -6.275  1.089   1.00 7.45  ? 107 HIS A N   1 
ATOM   876  C  CA  . HIS A 1 107 ? -7.480  -6.638  0.204   1.00 6.88  ? 107 HIS A CA  1 
ATOM   877  C  C   . HIS A 1 107 ? -7.357  -8.113  -0.088  1.00 7.75  ? 107 HIS A C   1 
ATOM   878  O  O   . HIS A 1 107 ? -6.271  -8.712  -0.054  1.00 7.99  ? 107 HIS A O   1 
ATOM   879  C  CB  . HIS A 1 107 ? -7.397  -5.847  -1.096  1.00 7.30  ? 107 HIS A CB  1 
ATOM   880  C  CG  . HIS A 1 107 ? -7.634  -4.369  -0.827  1.00 6.97  ? 107 HIS A CG  1 
ATOM   881  N  ND1 . HIS A 1 107 ? -6.642  -3.480  -0.531  1.00 8.01  ? 107 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A 1 107 ? -8.822  -3.661  -0.759  1.00 7.87  ? 107 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A 1 107 ? -7.211  -2.242  -0.290  1.00 7.48  ? 107 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A 1 107 ? -8.525  -2.358  -0.433  1.00 7.63  ? 107 HIS A NE2 1 
ATOM   885  N  N   . THR A 1 108 ? -8.538  -8.674  -0.384  1.00 8.36  ? 108 THR A N   1 
ATOM   886  C  CA  . THR A 1 108 ? -8.621  -10.069 -0.821  1.00 8.29  ? 108 THR A CA  1 
ATOM   887  C  C   . THR A 1 108 ? -9.430  -10.086 -2.134  1.00 7.62  ? 108 THR A C   1 
ATOM   888  O  O   . THR A 1 108 ? -10.167 -9.132  -2.436  1.00 8.49  ? 108 THR A O   1 
ATOM   889  C  CB  . THR A 1 108 ? -9.229  -11.001 0.249   1.00 9.30  ? 108 THR A CB  1 
ATOM   890  O  OG1 . THR A 1 108 ? -10.503 -10.515 0.633   1.00 10.03 ? 108 THR A OG1 1 
ATOM   891  C  CG2 . THR A 1 108 ? -8.328  -11.066 1.474   1.00 10.51 ? 108 THR A CG2 1 
ATOM   892  N  N   . VAL A 1 109 ? -9.301  -11.160 -2.883  1.00 7.77  ? 109 VAL A N   1 
ATOM   893  C  CA  . VAL A 1 109 ? -9.978  -11.228 -4.233  1.00 9.15  ? 109 VAL A CA  1 
ATOM   894  C  C   . VAL A 1 109 ? -10.789 -12.543 -4.200  1.00 9.12  ? 109 VAL A C   1 
ATOM   895  O  O   . VAL A 1 109 ? -10.158 -13.627 -4.142  1.00 9.76  ? 109 VAL A O   1 
ATOM   896  C  CB  . VAL A 1 109 ? -8.920  -11.246 -5.377  1.00 9.06  ? 109 VAL A CB  1 
ATOM   897  C  CG1 . VAL A 1 109 ? -9.640  -11.409 -6.695  1.00 11.21 ? 109 VAL A CG1 1 
ATOM   898  C  CG2 . VAL A 1 109 ? -8.094  -9.976  -5.381  1.00 9.73  ? 109 VAL A CG2 1 
ATOM   899  N  N   . ASP A 1 110 ? -12.108 -12.419 -4.118  1.00 10.54 ? 110 ASP A N   1 
ATOM   900  C  CA  . ASP A 1 110 ? -12.931 -13.632 -3.952  1.00 11.68 ? 110 ASP A CA  1 
ATOM   901  C  C   . ASP A 1 110 ? -12.398 -14.440 -2.747  1.00 10.51 ? 110 ASP A C   1 
ATOM   902  O  O   . ASP A 1 110 ? -12.291 -15.686 -2.789  1.00 11.66 ? 110 ASP A O   1 
ATOM   903  C  CB  . ASP A 1 110 ? -12.990 -14.469 -5.210  1.00 13.33 ? 110 ASP A CB  1 
ATOM   904  C  CG  . ASP A 1 110 ? -13.662 -13.674 -6.356  1.00 12.94 ? 110 ASP A CG  1 
ATOM   905  O  OD1 . ASP A 1 110 ? -14.514 -12.812 -6.106  1.00 14.44 ? 110 ASP A OD1 1 
ATOM   906  O  OD2 . ASP A 1 110 ? -13.384 -14.017 -7.497  1.00 16.52 ? 110 ASP A OD2 1 
ATOM   907  N  N   . LYS A 1 111 ? -12.072 -13.718 -1.666  1.00 9.76  ? 111 LYS A N   1 
ATOM   908  C  CA  . LYS A 1 111 ? -11.613 -14.269 -0.382  1.00 11.16 ? 111 LYS A CA  1 
ATOM   909  C  C   . LYS A 1 111 ? -10.134 -14.761 -0.454  1.00 9.56  ? 111 LYS A C   1 
ATOM   910  O  O   . LYS A 1 111 ? -9.577  -15.158 0.590   1.00 11.15 ? 111 LYS A O   1 
ATOM   911  C  CB  . LYS A 1 111 ? -12.536 -15.329 0.189   1.00 12.60 ? 111 LYS A CB  1 
ATOM   912  C  CG  . LYS A 1 111 ? -13.979 -14.857 0.378   1.00 15.89 ? 111 LYS A CG  1 
ATOM   913  C  CD  . LYS A 1 111 ? -13.989 -13.753 1.394   1.00 20.90 ? 111 LYS A CD  1 
ATOM   914  C  CE  . LYS A 1 111 ? -15.433 -13.264 1.682   1.00 26.02 ? 111 LYS A CE  1 
ATOM   915  N  NZ  . LYS A 1 111 ? -15.808 -13.590 3.054   1.00 28.43 ? 111 LYS A NZ  1 
ATOM   916  N  N   . LYS A 1 112 ? -9.483  -14.749 -1.615  1.00 8.98  ? 112 LYS A N   1 
ATOM   917  C  CA  . LYS A 1 112 ? -8.090  -15.156 -1.710  1.00 10.57 ? 112 LYS A CA  1 
ATOM   918  C  C   . LYS A 1 112 ? -7.202  -14.090 -1.055  1.00 9.12  ? 112 LYS A C   1 
ATOM   919  O  O   . LYS A 1 112 ? -7.317  -12.883 -1.342  1.00 9.73  ? 112 LYS A O   1 
ATOM   920  C  CB  . LYS A 1 112 ? -7.647  -15.286 -3.200  1.00 11.69 ? 112 LYS A CB  1 
ATOM   921  C  CG  . LYS A 1 112 ? -6.127  -15.604 -3.378  1.00 12.22 ? 112 LYS A CG  1 
ATOM   922  C  CD  . LYS A 1 112 ? -5.731  -15.714 -4.845  1.00 15.57 ? 112 LYS A CD  1 
ATOM   923  C  CE  . LYS A 1 112 ? -4.221  -15.861 -4.942  1.00 17.02 ? 112 LYS A CE  1 
ATOM   924  N  NZ  . LYS A 1 112 ? -3.882  -17.199 -4.534  1.00 18.65 ? 112 LYS A NZ  1 
ATOM   925  N  N   A LYS A 1 113 ? -6.321  -14.559 -0.182  0.50 9.69  ? 113 LYS A N   1 
ATOM   926  N  N   B LYS A 1 113 ? -6.358  -14.511 -0.100  0.50 9.56  ? 113 LYS A N   1 
ATOM   927  C  CA  A LYS A 1 113 ? -5.268  -13.758 0.383   0.50 8.95  ? 113 LYS A CA  1 
ATOM   928  C  CA  B LYS A 1 113 ? -5.296  -13.669 0.493   0.50 9.94  ? 113 LYS A CA  1 
ATOM   929  C  C   A LYS A 1 113 ? -3.988  -13.971 -0.395  0.50 9.22  ? 113 LYS A C   1 
ATOM   930  C  C   B LYS A 1 113 ? -3.957  -13.945 -0.163  0.50 10.02 ? 113 LYS A C   1 
ATOM   931  O  O   A LYS A 1 113 ? -3.645  -15.094 -0.780  0.50 8.03  ? 113 LYS A O   1 
ATOM   932  O  O   B LYS A 1 113 ? -3.538  -15.112 -0.221  0.50 10.55 ? 113 LYS A O   1 
ATOM   933  C  CB  A LYS A 1 113 ? -5.069  -14.222 1.838   0.50 9.72  ? 113 LYS A CB  1 
ATOM   934  C  CB  B LYS A 1 113 ? -5.146  -14.027 1.988   0.50 10.11 ? 113 LYS A CB  1 
ATOM   935  C  CG  A LYS A 1 113 ? -6.268  -13.986 2.750   0.50 10.08 ? 113 LYS A CG  1 
ATOM   936  C  CG  B LYS A 1 113 ? -6.274  -13.518 2.874   0.50 9.84  ? 113 LYS A CG  1 
ATOM   937  C  CD  A LYS A 1 113 ? -6.010  -14.696 4.067   0.50 11.17 ? 113 LYS A CD  1 
ATOM   938  C  CD  B LYS A 1 113 ? -6.221  -14.266 4.189   0.50 10.99 ? 113 LYS A CD  1 
ATOM   939  C  CE  A LYS A 1 113 ? -6.804  -14.096 5.236   0.50 11.24 ? 113 LYS A CE  1 
ATOM   940  C  CE  B LYS A 1 113 ? -7.302  -13.696 5.098   0.50 12.12 ? 113 LYS A CE  1 
ATOM   941  N  NZ  A LYS A 1 113 ? -8.224  -14.506 5.127   0.50 14.84 ? 113 LYS A NZ  1 
ATOM   942  N  NZ  B LYS A 1 113 ? -7.417  -14.472 6.344   0.50 14.96 ? 113 LYS A NZ  1 
ATOM   943  N  N   . TYR A 1 114 ? -3.271  -12.880 -0.617  1.00 8.88  ? 114 TYR A N   1 
ATOM   944  C  CA  . TYR A 1 114 ? -1.956  -12.960 -1.222  1.00 8.52  ? 114 TYR A CA  1 
ATOM   945  C  C   . TYR A 1 114 ? -0.870  -12.882 -0.131  1.00 8.72  ? 114 TYR A C   1 
ATOM   946  O  O   . TYR A 1 114 ? -1.179  -12.589 1.039   1.00 9.14  ? 114 TYR A O   1 
ATOM   947  C  CB  . TYR A 1 114 ? -1.751  -11.838 -2.238  1.00 8.78  ? 114 TYR A CB  1 
ATOM   948  C  CG  . TYR A 1 114 ? -2.502  -12.058 -3.540  1.00 9.61  ? 114 TYR A CG  1 
ATOM   949  C  CD1 . TYR A 1 114 ? -3.823  -11.636 -3.695  1.00 11.39 ? 114 TYR A CD1 1 
ATOM   950  C  CD2 . TYR A 1 114 ? -1.894  -12.689 -4.613  1.00 11.11 ? 114 TYR A CD2 1 
ATOM   951  C  CE1 . TYR A 1 114 ? -4.502  -11.838 -4.882  1.00 13.17 ? 114 TYR A CE1 1 
ATOM   952  C  CE2 . TYR A 1 114 ? -2.565  -12.887 -5.806  1.00 13.46 ? 114 TYR A CE2 1 
ATOM   953  C  CZ  . TYR A 1 114 ? -3.876  -12.468 -5.933  1.00 12.55 ? 114 TYR A CZ  1 
ATOM   954  O  OH  . TYR A 1 114 ? -4.544  -12.669 -7.119  1.00 17.54 ? 114 TYR A OH  1 
ATOM   955  N  N   . ALA A 1 115 ? 0.363   -13.215 -0.479  1.00 8.83  ? 115 ALA A N   1 
ATOM   956  C  CA  . ALA A 1 115 ? 1.435   -13.207 0.496   1.00 8.87  ? 115 ALA A CA  1 
ATOM   957  C  C   . ALA A 1 115 ? 1.722   -11.831 1.047   1.00 8.56  ? 115 ALA A C   1 
ATOM   958  O  O   . ALA A 1 115 ? 2.305   -11.690 2.127   1.00 9.25  ? 115 ALA A O   1 
ATOM   959  C  CB  . ALA A 1 115 ? 2.681   -13.805 -0.154  1.00 10.90 ? 115 ALA A CB  1 
ATOM   960  N  N   . ALA A 1 116 ? 1.476   -10.796 0.232   1.00 8.77  ? 116 ALA A N   1 
ATOM   961  C  CA  . ALA A 1 116 ? 1.804   -9.407  0.717   1.00 8.39  ? 116 ALA A CA  1 
ATOM   962  C  C   . ALA A 1 116 ? 1.032   -8.470  -0.210  1.00 8.72  ? 116 ALA A C   1 
ATOM   963  O  O   . ALA A 1 116 ? 0.418   -8.854  -1.224  1.00 8.43  ? 116 ALA A O   1 
ATOM   964  C  CB  . ALA A 1 116 ? 3.327   -9.174  0.678   1.00 9.29  ? 116 ALA A CB  1 
ATOM   965  N  N   . GLU A 1 117 ? 1.066   -7.207  0.183   1.00 8.25  ? 117 GLU A N   1 
ATOM   966  C  CA  . GLU A 1 117 ? 0.427   -6.160  -0.628  1.00 7.45  ? 117 GLU A CA  1 
ATOM   967  C  C   . GLU A 1 117 ? 1.293   -4.889  -0.504  1.00 7.44  ? 117 GLU A C   1 
ATOM   968  O  O   . GLU A 1 117 ? 1.627   -4.482  0.634   1.00 8.80  ? 117 GLU A O   1 
ATOM   969  C  CB  . GLU A 1 117 ? -0.982  -5.936  -0.160  1.00 7.72  ? 117 GLU A CB  1 
ATOM   970  C  CG  . GLU A 1 117 ? -1.807  -4.987  -1.023  1.00 8.79  ? 117 GLU A CG  1 
ATOM   971  C  CD  . GLU A 1 117 ? -3.302  -4.957  -0.598  1.00 8.73  ? 117 GLU A CD  1 
ATOM   972  O  OE1 . GLU A 1 117 ? -3.799  -5.951  -0.038  1.00 8.39  ? 117 GLU A OE1 1 
ATOM   973  O  OE2 . GLU A 1 117 ? -3.933  -3.870  -0.818  1.00 9.47  ? 117 GLU A OE2 1 
ATOM   974  N  N   . LEU A 1 118 ? 1.584   -4.291  -1.651  1.00 7.71  ? 118 LEU A N   1 
ATOM   975  C  CA  . LEU A 1 118 ? 2.343   -3.043  -1.776  1.00 7.76  ? 118 LEU A CA  1 
ATOM   976  C  C   . LEU A 1 118 ? 1.327   -1.920  -1.936  1.00 7.99  ? 118 LEU A C   1 
ATOM   977  O  O   . LEU A 1 118 ? 0.384   -1.990  -2.743  1.00 7.35  ? 118 LEU A O   1 
ATOM   978  C  CB  . LEU A 1 118 ? 3.189   -3.148  -3.059  1.00 8.32  ? 118 LEU A CB  1 
ATOM   979  C  CG  . LEU A 1 118 ? 3.770   -1.855  -3.606  1.00 8.98  ? 118 LEU A CG  1 
ATOM   980  C  CD1 . LEU A 1 118 ? 4.709   -1.128  -2.630  1.00 9.45  ? 118 LEU A CD1 1 
ATOM   981  C  CD2 . LEU A 1 118 ? 4.525   -2.107  -4.894  1.00 10.39 ? 118 LEU A CD2 1 
ATOM   982  N  N   . HIS A 1 119 ? 1.557   -0.839  -1.162  1.00 7.14  ? 119 HIS A N   1 
ATOM   983  C  CA  . HIS A 1 119 ? 0.728   0.390   -1.211  1.00 7.37  ? 119 HIS A CA  1 
ATOM   984  C  C   . HIS A 1 119 ? 1.590   1.572   -1.575  1.00 8.05  ? 119 HIS A C   1 
ATOM   985  O  O   . HIS A 1 119 ? 2.552   1.907   -0.827  1.00 9.00  ? 119 HIS A O   1 
ATOM   986  C  CB  . HIS A 1 119 ? 0.113   0.618   0.186   1.00 7.90  ? 119 HIS A CB  1 
ATOM   987  C  CG  . HIS A 1 119 ? -0.978  -0.376  0.431   1.00 6.47  ? 119 HIS A CG  1 
ATOM   988  N  ND1 . HIS A 1 119 ? -1.464  -0.631  1.689   1.00 7.56  ? 119 HIS A ND1 1 
ATOM   989  C  CD2 . HIS A 1 119 ? -1.689  -1.194  -0.403  1.00 7.71  ? 119 HIS A CD2 1 
ATOM   990  C  CE1 . HIS A 1 119 ? -2.409  -1.568  1.667   1.00 8.69  ? 119 HIS A CE1 1 
ATOM   991  N  NE2 . HIS A 1 119 ? -2.567  -1.920  0.378   1.00 8.33  ? 119 HIS A NE2 1 
ATOM   992  N  N   . LEU A 1 120 ? 1.280   2.140   -2.743  1.00 7.30  ? 120 LEU A N   1 
ATOM   993  C  CA  . LEU A 1 120 ? 1.924   3.409   -3.143  1.00 8.63  ? 120 LEU A CA  1 
ATOM   994  C  C   . LEU A 1 120 ? 0.922   4.544   -2.882  1.00 7.70  ? 120 LEU A C   1 
ATOM   995  O  O   . LEU A 1 120 ? -0.157  4.582   -3.418  1.00 8.69  ? 120 LEU A O   1 
ATOM   996  C  CB  . LEU A 1 120 ? 2.286   3.326   -4.612  1.00 8.12  ? 120 LEU A CB  1 
ATOM   997  C  CG  . LEU A 1 120 ? 3.376   2.267   -4.976  1.00 10.12 ? 120 LEU A CG  1 
ATOM   998  C  CD1 . LEU A 1 120 ? 2.852   1.329   -6.075  1.00 13.65 ? 120 LEU A CD1 1 
ATOM   999  C  CD2 . LEU A 1 120 ? 4.651   3.003   -5.381  1.00 11.85 ? 120 LEU A CD2 1 
ATOM   1000 N  N   . VAL A 1 121 ? 1.331   5.384   -1.942  1.00 8.66  ? 121 VAL A N   1 
ATOM   1001 C  CA  . VAL A 1 121 ? 0.440   6.431   -1.337  1.00 8.76  ? 121 VAL A CA  1 
ATOM   1002 C  C   . VAL A 1 121 ? 0.702   7.785   -2.039  1.00 9.39  ? 121 VAL A C   1 
ATOM   1003 O  O   . VAL A 1 121 ? 1.838   8.229   -2.140  1.00 10.02 ? 121 VAL A O   1 
ATOM   1004 C  CB  . VAL A 1 121 ? 0.735   6.581   0.186   1.00 9.13  ? 121 VAL A CB  1 
ATOM   1005 C  CG1 . VAL A 1 121 ? -0.226  7.644   0.772   1.00 10.43 ? 121 VAL A CG1 1 
ATOM   1006 C  CG2 . VAL A 1 121 ? 0.628   5.220   0.924   1.00 9.92  ? 121 VAL A CG2 1 
ATOM   1007 N  N   . HIS A 1 122 ? -0.356  8.399   -2.580  1.00 8.54  ? 122 HIS A N   1 
ATOM   1008 C  CA  . HIS A 1 122 ? -0.279  9.650   -3.344  1.00 8.87  ? 122 HIS A CA  1 
ATOM   1009 C  C   . HIS A 1 122 ? -1.293  10.620  -2.725  1.00 9.62  ? 122 HIS A C   1 
ATOM   1010 O  O   . HIS A 1 122 ? -2.397  10.233  -2.377  1.00 9.60  ? 122 HIS A O   1 
ATOM   1011 C  CB  . HIS A 1 122 ? -0.693  9.457   -4.802  1.00 8.96  ? 122 HIS A CB  1 
ATOM   1012 C  CG  . HIS A 1 122 ? -0.015  8.312   -5.480  1.00 8.56  ? 122 HIS A CG  1 
ATOM   1013 N  ND1 . HIS A 1 122 ? -0.338  6.986   -5.217  1.00 8.82  ? 122 HIS A ND1 1 
ATOM   1014 C  CD2 . HIS A 1 122 ? 1.024   8.273   -6.420  1.00 9.45  ? 122 HIS A CD2 1 
ATOM   1015 C  CE1 . HIS A 1 122 ? 0.403   6.178   -5.976  1.00 10.35 ? 122 HIS A CE1 1 
ATOM   1016 N  NE2 . HIS A 1 122 ? 1.261   6.932   -6.706  1.00 9.96  ? 122 HIS A NE2 1 
ATOM   1017 N  N   . TRP A 1 123 ? -0.946  11.914  -2.647  1.00 9.24  ? 123 TRP A N   1 
ATOM   1018 C  CA  . TRP A 1 123 ? -1.906  12.941  -2.176  1.00 9.85  ? 123 TRP A CA  1 
ATOM   1019 C  C   . TRP A 1 123 ? -2.329  13.888  -3.283  1.00 9.04  ? 123 TRP A C   1 
ATOM   1020 O  O   . TRP A 1 123 ? -1.580  14.241  -4.214  1.00 10.53 ? 123 TRP A O   1 
ATOM   1021 C  CB  . TRP A 1 123 ? -1.285  13.725  -1.002  1.00 11.31 ? 123 TRP A CB  1 
ATOM   1022 C  CG  . TRP A 1 123 ? 0.050   14.355  -1.279  1.00 12.39 ? 123 TRP A CG  1 
ATOM   1023 C  CD1 . TRP A 1 123 ? 1.309   13.778  -1.143  1.00 14.20 ? 123 TRP A CD1 1 
ATOM   1024 C  CD2 . TRP A 1 123 ? 0.303   15.731  -1.704  1.00 13.24 ? 123 TRP A CD2 1 
ATOM   1025 N  NE1 . TRP A 1 123 ? 2.293   14.680  -1.462  1.00 14.35 ? 123 TRP A NE1 1 
ATOM   1026 C  CE2 . TRP A 1 123 ? 1.758   15.868  -1.808  1.00 13.39 ? 123 TRP A CE2 1 
ATOM   1027 C  CE3 . TRP A 1 123 ? -0.500  16.820  -2.011  1.00 12.09 ? 123 TRP A CE3 1 
ATOM   1028 C  CZ2 . TRP A 1 123 ? 2.357   17.051  -2.197  1.00 16.03 ? 123 TRP A CZ2 1 
ATOM   1029 C  CZ3 . TRP A 1 123 ? 0.113   18.006  -2.399  1.00 14.73 ? 123 TRP A CZ3 1 
ATOM   1030 C  CH2 . TRP A 1 123 ? 1.509   18.119  -2.493  1.00 15.44 ? 123 TRP A CH2 1 
ATOM   1031 N  N   . ASN A 1 124 ? -3.590  14.291  -3.120  1.00 10.87 ? 124 ASN A N   1 
ATOM   1032 C  CA  . ASN A 1 124 ? -4.197  15.217  -4.115  1.00 10.89 ? 124 ASN A CA  1 
ATOM   1033 C  C   . ASN A 1 124 ? -3.587  16.638  -4.047  1.00 10.02 ? 124 ASN A C   1 
ATOM   1034 O  O   . ASN A 1 124 ? -3.617  17.310  -3.033  1.00 10.90 ? 124 ASN A O   1 
ATOM   1035 C  CB  . ASN A 1 124 ? -5.690  15.257  -3.810  1.00 10.95 ? 124 ASN A CB  1 
ATOM   1036 C  CG  . ASN A 1 124 ? -6.504  15.889  -4.911  1.00 11.95 ? 124 ASN A CG  1 
ATOM   1037 O  OD1 . ASN A 1 124 ? -6.029  16.766  -5.635  1.00 12.73 ? 124 ASN A OD1 1 
ATOM   1038 N  ND2 . ASN A 1 124 ? -7.757  15.430  -5.043  1.00 12.98 ? 124 ASN A ND2 1 
ATOM   1039 N  N   . THR A 1 125 ? -3.016  17.003  -5.198  1.00 11.15 ? 125 THR A N   1 
ATOM   1040 C  CA  . THR A 1 125 ? -2.243  18.291  -5.225  1.00 13.01 ? 125 THR A CA  1 
ATOM   1041 C  C   . THR A 1 125 ? -3.121  19.485  -5.012  1.00 12.96 ? 125 THR A C   1 
ATOM   1042 O  O   . THR A 1 125 ? -2.598  20.519  -4.602  1.00 15.87 ? 125 THR A O   1 
ATOM   1043 C  CB  . THR A 1 125 ? -1.441  18.468  -6.530  1.00 14.61 ? 125 THR A CB  1 
ATOM   1044 O  OG1 . THR A 1 125 ? -2.335  18.454  -7.640  1.00 18.85 ? 125 THR A OG1 1 
ATOM   1045 C  CG2 . THR A 1 125 ? -0.417  17.376  -6.710  1.00 17.07 ? 125 THR A CG2 1 
ATOM   1046 N  N   . LYS A 1 126 ? -4.447  19.387  -5.091  1.00 12.84 ? 127 LYS A N   1 
ATOM   1047 C  CA  . LYS A 1 126 ? -5.272  20.535  -4.826  1.00 14.86 ? 127 LYS A CA  1 
ATOM   1048 C  C   . LYS A 1 126 ? -5.301  20.858  -3.322  1.00 13.54 ? 127 LYS A C   1 
ATOM   1049 O  O   . LYS A 1 126 ? -5.789  21.969  -2.930  1.00 16.68 ? 127 LYS A O   1 
ATOM   1050 C  CB  . LYS A 1 126 ? -6.648  20.254  -5.395  1.00 18.35 ? 127 LYS A CB  1 
ATOM   1051 C  CG  . LYS A 1 126 ? -7.545  19.453  -4.537  1.00 18.95 ? 127 LYS A CG  1 
ATOM   1052 C  CD  . LYS A 1 126 ? -8.731  19.295  -5.480  1.00 25.88 ? 127 LYS A CD  1 
ATOM   1053 C  CE  . LYS A 1 126 ? -9.880  18.509  -5.035  1.00 28.88 ? 127 LYS A CE  1 
ATOM   1054 N  NZ  . LYS A 1 126 ? -11.113 19.123  -5.678  1.00 38.03 ? 127 LYS A NZ  1 
ATOM   1055 N  N   . TYR A 1 127 ? -4.770  19.996  -2.458  1.00 12.86 ? 128 TYR A N   1 
ATOM   1056 C  CA  . TYR A 1 127 ? -4.740  20.303  -1.012  1.00 11.99 ? 128 TYR A CA  1 
ATOM   1057 C  C   . TYR A 1 127 ? -3.352  20.694  -0.512  1.00 11.30 ? 128 TYR A C   1 
ATOM   1058 O  O   . TYR A 1 127 ? -3.206  20.917  0.685   1.00 14.25 ? 128 TYR A O   1 
ATOM   1059 C  CB  . TYR A 1 127 ? -5.299  19.108  -0.209  1.00 12.40 ? 128 TYR A CB  1 
ATOM   1060 C  CG  . TYR A 1 127 ? -6.713  18.809  -0.611  1.00 11.99 ? 128 TYR A CG  1 
ATOM   1061 C  CD1 . TYR A 1 127 ? -7.697  19.802  -0.548  1.00 12.44 ? 128 TYR A CD1 1 
ATOM   1062 C  CD2 . TYR A 1 127 ? -7.067  17.514  -1.125  1.00 12.28 ? 128 TYR A CD2 1 
ATOM   1063 C  CE1 . TYR A 1 127 ? -9.008  19.492  -0.951  1.00 13.64 ? 128 TYR A CE1 1 
ATOM   1064 C  CE2 . TYR A 1 127 ? -8.367  17.226  -1.495  1.00 13.29 ? 128 TYR A CE2 1 
ATOM   1065 C  CZ  . TYR A 1 127 ? -9.333  18.240  -1.389  1.00 12.74 ? 128 TYR A CZ  1 
ATOM   1066 O  OH  . TYR A 1 127 ? -10.599 18.007  -1.782  1.00 14.28 ? 128 TYR A OH  1 
ATOM   1067 N  N   . GLY A 1 128 ? -2.379  20.768  -1.455  1.00 12.58 ? 129 GLY A N   1 
ATOM   1068 C  CA  . GLY A 1 128 ? -1.140  21.459  -1.121  1.00 14.50 ? 129 GLY A CA  1 
ATOM   1069 C  C   . GLY A 1 128 ? -0.117  20.618  -0.346  1.00 13.60 ? 129 GLY A C   1 
ATOM   1070 O  O   . GLY A 1 128 ? 1.080   20.774  -0.625  1.00 14.77 ? 129 GLY A O   1 
ATOM   1071 N  N   . ASP A 1 129 ? -0.527  19.751  0.604   1.00 14.28 ? 130 ASP A N   1 
ATOM   1072 C  CA  . ASP A 1 129 ? 0.438   18.847  1.239   1.00 14.99 ? 130 ASP A CA  1 
ATOM   1073 C  C   . ASP A 1 129 ? -0.338  17.656  1.760   1.00 14.31 ? 130 ASP A C   1 
ATOM   1074 O  O   . ASP A 1 129 ? -1.565  17.711  1.840   1.00 14.58 ? 130 ASP A O   1 
ATOM   1075 C  CB  . ASP A 1 129 ? 1.373   19.502  2.257   1.00 18.65 ? 130 ASP A CB  1 
ATOM   1076 C  CG  . ASP A 1 129 ? 0.679   19.937  3.538   1.00 18.47 ? 130 ASP A CG  1 
ATOM   1077 O  OD1 . ASP A 1 129 ? -0.389  19.397  3.921   1.00 28.66 ? 130 ASP A OD1 1 
ATOM   1078 O  OD2 . ASP A 1 129 ? 1.253   20.836  4.192   1.00 34.56 ? 130 ASP A OD2 1 
ATOM   1079 N  N   . PHE A 1 130 ? 0.387   16.601  2.104   1.00 13.89 ? 131 PHE A N   1 
ATOM   1080 C  CA  . PHE A 1 130 ? -0.277  15.395  2.513   1.00 16.58 ? 131 PHE A CA  1 
ATOM   1081 C  C   . PHE A 1 130 ? -1.043  15.547  3.844   1.00 16.41 ? 131 PHE A C   1 
ATOM   1082 O  O   . PHE A 1 130 ? -2.085  14.933  4.010   1.00 13.93 ? 131 PHE A O   1 
ATOM   1083 C  CB  . PHE A 1 130 ? 0.654   14.186  2.577   1.00 18.62 ? 131 PHE A CB  1 
ATOM   1084 C  CG  . PHE A 1 130 ? 1.559   14.142  3.748   1.00 23.80 ? 131 PHE A CG  1 
ATOM   1085 C  CD1 . PHE A 1 130 ? 2.855   14.680  3.677   1.00 29.05 ? 131 PHE A CD1 1 
ATOM   1086 C  CD2 . PHE A 1 130 ? 1.137   13.561  4.945   1.00 24.16 ? 131 PHE A CD2 1 
ATOM   1087 C  CE1 . PHE A 1 130 ? 3.715   14.609  4.789   1.00 33.97 ? 131 PHE A CE1 1 
ATOM   1088 C  CE2 . PHE A 1 130 ? 2.001   13.464  6.060   1.00 34.09 ? 131 PHE A CE2 1 
ATOM   1089 C  CZ  . PHE A 1 130 ? 3.288   14.023  5.974   1.00 43.49 ? 131 PHE A CZ  1 
ATOM   1090 N  N   . GLY A 1 131 ? -0.569  16.399  4.805   1.00 16.17 ? 132 GLY A N   1 
ATOM   1091 C  CA  . GLY A 1 131 ? -1.267  16.525  6.118   1.00 15.85 ? 132 GLY A CA  1 
ATOM   1092 C  C   . GLY A 1 131 ? -2.650  17.149  5.946   1.00 16.20 ? 132 GLY A C   1 
ATOM   1093 O  O   . GLY A 1 131 ? -3.608  16.821  6.630   1.00 17.99 ? 132 GLY A O   1 
ATOM   1094 N  N   . LYS A 1 132 ? -2.738  18.080  4.986   1.00 16.00 ? 133 LYS A N   1 
ATOM   1095 C  CA  . LYS A 1 132 ? -4.074  18.633  4.655   1.00 15.42 ? 133 LYS A CA  1 
ATOM   1096 C  C   . LYS A 1 132 ? -4.899  17.645  3.850   1.00 13.64 ? 133 LYS A C   1 
ATOM   1097 O  O   . LYS A 1 132 ? -6.108  17.568  4.044   1.00 13.21 ? 133 LYS A O   1 
ATOM   1098 C  CB  . LYS A 1 132 ? -3.968  19.983  3.935   1.00 17.32 ? 133 LYS A CB  1 
ATOM   1099 C  CG  . LYS A 1 132 ? -3.508  21.162  4.828   1.00 21.56 ? 133 LYS A CG  1 
ATOM   1100 C  CD  . LYS A 1 132 ? -4.545  21.593  5.901   1.00 30.42 ? 133 LYS A CD  1 
ATOM   1101 C  CE  . LYS A 1 132 ? -5.390  22.761  5.427   1.00 37.60 ? 133 LYS A CE  1 
ATOM   1102 N  NZ  . LYS A 1 132 ? -6.080  22.406  4.136   1.00 50.79 ? 133 LYS A NZ  1 
ATOM   1103 N  N   . ALA A 1 133 ? -4.266  16.924  2.912   1.00 12.09 ? 134 ALA A N   1 
ATOM   1104 C  CA  . ALA A 1 133 ? -5.045  16.024  2.076   1.00 11.99 ? 134 ALA A CA  1 
ATOM   1105 C  C   . ALA A 1 133 ? -5.716  14.957  2.894   1.00 11.61 ? 134 ALA A C   1 
ATOM   1106 O  O   . ALA A 1 133 ? -6.832  14.591  2.556   1.00 11.59 ? 134 ALA A O   1 
ATOM   1107 C  CB  . ALA A 1 133 ? -4.096  15.382  1.076   1.00 12.36 ? 134 ALA A CB  1 
ATOM   1108 N  N   . VAL A 1 134 ? -5.121  14.423  3.953   1.00 11.69 ? 135 VAL A N   1 
ATOM   1109 C  CA  . VAL A 1 134 ? -5.784  13.335  4.697   1.00 13.31 ? 135 VAL A CA  1 
ATOM   1110 C  C   . VAL A 1 134 ? -7.023  13.748  5.414   1.00 12.57 ? 135 VAL A C   1 
ATOM   1111 O  O   . VAL A 1 134 ? -7.781  12.895  5.818   1.00 13.99 ? 135 VAL A O   1 
ATOM   1112 C  CB  . VAL A 1 134 ? -4.919  12.596  5.746   1.00 12.84 ? 135 VAL A CB  1 
ATOM   1113 C  CG1 . VAL A 1 134 ? -3.720  11.977  5.096   1.00 15.06 ? 135 VAL A CG1 1 
ATOM   1114 C  CG2 . VAL A 1 134 ? -4.466  13.479  6.883   1.00 15.42 ? 135 VAL A CG2 1 
ATOM   1115 N  N   . GLN A 1 135 ? -7.225  15.070  5.508   1.00 12.82 ? 136 GLN A N   1 
ATOM   1116 C  CA  . GLN A 1 135 ? -8.485  15.599  6.105   1.00 14.33 ? 136 GLN A CA  1 
ATOM   1117 C  C   . GLN A 1 135 ? -9.632  15.713  5.135   1.00 13.84 ? 136 GLN A C   1 
ATOM   1118 O  O   . GLN A 1 135 ? -10.698 16.316  5.401   1.00 16.95 ? 136 GLN A O   1 
ATOM   1119 C  CB  . GLN A 1 135 ? -8.190  16.970  6.788   1.00 15.36 ? 136 GLN A CB  1 
ATOM   1120 C  CG  . GLN A 1 135 ? -7.081  16.888  7.847   1.00 19.80 ? 136 GLN A CG  1 
ATOM   1121 C  CD  . GLN A 1 135 ? -6.788  18.246  8.496   1.00 24.53 ? 136 GLN A CD  1 
ATOM   1122 O  OE1 . GLN A 1 135 ? -7.706  18.910  9.015   1.00 35.42 ? 136 GLN A OE1 1 
ATOM   1123 N  NE2 . GLN A 1 135 ? -5.532  18.699  8.399   1.00 29.33 ? 136 GLN A NE2 1 
ATOM   1124 N  N   . GLN A 1 136 ? -9.369  15.244  3.898   1.00 11.94 ? 137 GLN A N   1 
ATOM   1125 C  CA  . GLN A 1 136 ? -10.358 15.456  2.820   1.00 12.83 ? 137 GLN A CA  1 
ATOM   1126 C  C   . GLN A 1 136 ? -10.880 14.122  2.326   1.00 12.14 ? 137 GLN A C   1 
ATOM   1127 O  O   . GLN A 1 136 ? -10.101 13.164  2.214   1.00 12.45 ? 137 GLN A O   1 
ATOM   1128 C  CB  . GLN A 1 136 ? -9.798  16.224  1.623   1.00 14.32 ? 137 GLN A CB  1 
ATOM   1129 C  CG  . GLN A 1 136 ? -8.928  17.429  1.968   1.00 17.71 ? 137 GLN A CG  1 
ATOM   1130 C  CD  . GLN A 1 136 ? -9.676  18.414  2.795   1.00 20.64 ? 137 GLN A CD  1 
ATOM   1131 O  OE1 . GLN A 1 136 ? -10.901 18.607  2.634   1.00 20.18 ? 137 GLN A OE1 1 
ATOM   1132 N  NE2 . GLN A 1 136 ? -8.926  19.064  3.759   1.00 26.45 ? 137 GLN A NE2 1 
ATOM   1133 N  N   . PRO A 1 137 ? -12.139 14.054  1.808   1.00 10.53 ? 138 PRO A N   1 
ATOM   1134 C  CA  . PRO A 1 137 ? -12.664 12.753  1.374   1.00 12.34 ? 138 PRO A CA  1 
ATOM   1135 C  C   . PRO A 1 137 ? -11.984 12.242  0.102   1.00 10.72 ? 138 PRO A C   1 
ATOM   1136 O  O   . PRO A 1 137 ? -12.067 11.047  -0.128  1.00 14.23 ? 138 PRO A O   1 
ATOM   1137 C  CB  . PRO A 1 137 ? -14.170 12.995  1.197   1.00 16.06 ? 138 PRO A CB  1 
ATOM   1138 C  CG  . PRO A 1 137 ? -14.256 14.447  0.980   1.00 18.84 ? 138 PRO A CG  1 
ATOM   1139 C  CD  . PRO A 1 137 ? -13.197 15.098  1.872   1.00 16.06 ? 138 PRO A CD  1 
ATOM   1140 N  N   . ASP A 1 138 ? -11.366 13.104  -0.711  1.00 10.35 ? 139 ASP A N   1 
ATOM   1141 C  CA  . ASP A 1 138 ? -10.672 12.714  -1.956  1.00 11.11 ? 139 ASP A CA  1 
ATOM   1142 C  C   . ASP A 1 138 ? -9.206  13.138  -1.768  1.00 10.04 ? 139 ASP A C   1 
ATOM   1143 O  O   . ASP A 1 138 ? -8.602  13.550  -2.678  1.00 11.04 ? 139 ASP A O   1 
ATOM   1144 C  CB  . ASP A 1 138 ? -11.349 13.378  -3.173  1.00 12.16 ? 139 ASP A CB  1 
ATOM   1145 C  CG  . ASP A 1 138 ? -11.342 14.873  -3.106  1.00 12.66 ? 139 ASP A CG  1 
ATOM   1146 O  OD1 . ASP A 1 138 ? -11.145 15.485  -2.006  1.00 13.33 ? 139 ASP A OD1 1 
ATOM   1147 O  OD2 . ASP A 1 138 ? -11.714 15.464  -4.152  1.00 16.71 ? 139 ASP A OD2 1 
ATOM   1148 N  N   . GLY A 1 139 ? -8.645  13.074  -0.548  1.00 9.57  ? 140 GLY A N   1 
ATOM   1149 C  CA  . GLY A 1 139 ? -7.303  13.544  -0.303  1.00 10.12 ? 140 GLY A CA  1 
ATOM   1150 C  C   . GLY A 1 139 ? -6.194  12.637  -0.861  1.00 9.29  ? 140 GLY A C   1 
ATOM   1151 O  O   . GLY A 1 139 ? -5.136  13.127  -1.205  1.00 10.07 ? 140 GLY A O   1 
ATOM   1152 N  N   . LEU A 1 140 ? -6.418  11.314  -0.807  1.00 8.77  ? 141 LEU A N   1 
ATOM   1153 C  CA  . LEU A 1 140 ? -5.377  10.330  -1.161  1.00 8.49  ? 141 LEU A CA  1 
ATOM   1154 C  C   . LEU A 1 140 ? -5.860  9.406   -2.257  1.00 9.09  ? 141 LEU A C   1 
ATOM   1155 O  O   . LEU A 1 140 ? -7.016  9.118   -2.359  1.00 8.75  ? 141 LEU A O   1 
ATOM   1156 C  CB  . LEU A 1 140 ? -5.015  9.480   0.055   1.00 9.54  ? 141 LEU A CB  1 
ATOM   1157 C  CG  . LEU A 1 140 ? -4.377  10.190  1.262   1.00 10.87 ? 141 LEU A CG  1 
ATOM   1158 C  CD1 . LEU A 1 140 ? -3.862  9.130   2.233   1.00 12.50 ? 141 LEU A CD1 1 
ATOM   1159 C  CD2 . LEU A 1 140 ? -3.257  11.170  1.034   1.00 12.35 ? 141 LEU A CD2 1 
ATOM   1160 N  N   . ALA A 1 141 ? -4.900  8.924   -3.028  1.00 8.72  ? 142 ALA A N   1 
ATOM   1161 C  CA  . ALA A 1 141 ? -5.100  7.773   -3.916  1.00 9.15  ? 142 ALA A CA  1 
ATOM   1162 C  C   . ALA A 1 141 ? -4.000  6.797   -3.581  1.00 7.77  ? 142 ALA A C   1 
ATOM   1163 O  O   . ALA A 1 141 ? -2.789  7.120   -3.565  1.00 9.03  ? 142 ALA A O   1 
ATOM   1164 C  CB  . ALA A 1 141 ? -5.037  8.200   -5.377  1.00 10.14 ? 142 ALA A CB  1 
ATOM   1165 N  N   . VAL A 1 142 ? -4.424  5.568   -3.179  1.00 8.08  ? 143 VAL A N   1 
ATOM   1166 C  CA  . VAL A 1 142 ? -3.451  4.515   -2.854  1.00 8.63  ? 143 VAL A CA  1 
ATOM   1167 C  C   . VAL A 1 142 ? -3.584  3.442   -3.962  1.00 6.96  ? 143 VAL A C   1 
ATOM   1168 O  O   . VAL A 1 142 ? -4.668  2.912   -4.206  1.00 7.83  ? 143 VAL A O   1 
ATOM   1169 C  CB  . VAL A 1 142 ? -3.626  3.936   -1.433  1.00 8.17  ? 143 VAL A CB  1 
ATOM   1170 C  CG1 . VAL A 1 142 ? -2.480  2.916   -1.153  1.00 8.71  ? 143 VAL A CG1 1 
ATOM   1171 C  CG2 . VAL A 1 142 ? -3.510  5.063   -0.404  1.00 9.69  ? 143 VAL A CG2 1 
ATOM   1172 N  N   . LEU A 1 143 ? -2.441  3.209   -4.626  1.00 7.43  ? 144 LEU A N   1 
ATOM   1173 C  CA  . LEU A 1 143 ? -2.310  2.139   -5.564  1.00 7.99  ? 144 LEU A CA  1 
ATOM   1174 C  C   . LEU A 1 143 ? -1.871  0.866   -4.842  1.00 6.84  ? 144 LEU A C   1 
ATOM   1175 O  O   . LEU A 1 143 ? -0.777  0.827   -4.290  1.00 8.19  ? 144 LEU A O   1 
ATOM   1176 C  CB  . LEU A 1 143 ? -1.317  2.575   -6.682  1.00 9.42  ? 144 LEU A CB  1 
ATOM   1177 C  CG  . LEU A 1 143 ? -1.094  1.574   -7.818  1.00 9.06  ? 144 LEU A CG  1 
ATOM   1178 C  CD1 . LEU A 1 143 ? -2.362  1.277   -8.574  1.00 11.79 ? 144 LEU A CD1 1 
ATOM   1179 C  CD2 . LEU A 1 143 ? -0.055  2.225   -8.780  1.00 11.38 ? 144 LEU A CD2 1 
ATOM   1180 N  N   . GLY A 1 144 ? -2.728  -0.164  -4.909  1.00 7.20  ? 145 GLY A N   1 
ATOM   1181 C  CA  . GLY A 1 144 ? -2.394  -1.449  -4.240  1.00 7.08  ? 145 GLY A CA  1 
ATOM   1182 C  C   . GLY A 1 144 ? -2.034  -2.500  -5.256  1.00 7.31  ? 145 GLY A C   1 
ATOM   1183 O  O   . GLY A 1 144 ? -2.690  -2.642  -6.268  1.00 8.17  ? 145 GLY A O   1 
ATOM   1184 N  N   . ILE A 1 145 ? -0.952  -3.226  -4.912  1.00 7.10  ? 146 ILE A N   1 
ATOM   1185 C  CA  . ILE A 1 145 ? -0.452  -4.296  -5.839  1.00 7.10  ? 146 ILE A CA  1 
ATOM   1186 C  C   . ILE A 1 145 ? -0.213  -5.544  -4.970  1.00 7.84  ? 146 ILE A C   1 
ATOM   1187 O  O   . ILE A 1 145 ? 0.512   -5.497  -3.979  1.00 9.01  ? 146 ILE A O   1 
ATOM   1188 C  CB  . ILE A 1 145 ? 0.858   -3.778  -6.505  1.00 7.82  ? 146 ILE A CB  1 
ATOM   1189 C  CG1 . ILE A 1 145 ? 0.590   -2.441  -7.276  1.00 10.58 ? 146 ILE A CG1 1 
ATOM   1190 C  CG2 . ILE A 1 145 ? 1.445   -4.899  -7.394  1.00 11.05 ? 146 ILE A CG2 1 
ATOM   1191 C  CD1 . ILE A 1 145 ? 1.777   -1.857  -7.962  1.00 12.01 ? 146 ILE A CD1 1 
ATOM   1192 N  N   . PHE A 1 146 ? -0.829  -6.658  -5.419  1.00 7.71  ? 147 PHE A N   1 
ATOM   1193 C  CA  . PHE A 1 146 ? -0.647  -7.916  -4.673  1.00 7.81  ? 147 PHE A CA  1 
ATOM   1194 C  C   . PHE A 1 146 ? 0.728   -8.497  -5.005  1.00 8.07  ? 147 PHE A C   1 
ATOM   1195 O  O   . PHE A 1 146 ? 1.228   -8.400  -6.104  1.00 9.29  ? 147 PHE A O   1 
ATOM   1196 C  CB  . PHE A 1 146 ? -1.732  -8.872  -5.094  1.00 8.91  ? 147 PHE A CB  1 
ATOM   1197 C  CG  . PHE A 1 146 ? -3.096  -8.425  -4.713  1.00 7.69  ? 147 PHE A CG  1 
ATOM   1198 C  CD1 . PHE A 1 146 ? -3.376  -8.261  -3.347  1.00 8.33  ? 147 PHE A CD1 1 
ATOM   1199 C  CD2 . PHE A 1 146 ? -4.098  -8.179  -5.640  1.00 8.54  ? 147 PHE A CD2 1 
ATOM   1200 C  CE1 . PHE A 1 146 ? -4.674  -7.856  -2.940  1.00 7.94  ? 147 PHE A CE1 1 
ATOM   1201 C  CE2 . PHE A 1 146 ? -5.387  -7.798  -5.224  1.00 8.55  ? 147 PHE A CE2 1 
ATOM   1202 C  CZ  . PHE A 1 146 ? -5.690  -7.639  -3.871  1.00 7.73  ? 147 PHE A CZ  1 
ATOM   1203 N  N   . LEU A 1 147 ? 1.275   -9.201  -4.032  1.00 9.11  ? 148 LEU A N   1 
ATOM   1204 C  CA  . LEU A 1 147 ? 2.510   -9.998  -4.207  1.00 8.37  ? 148 LEU A CA  1 
ATOM   1205 C  C   . LEU A 1 147 ? 2.173   -11.478 -3.996  1.00 8.80  ? 148 LEU A C   1 
ATOM   1206 O  O   . LEU A 1 147 ? 1.568   -11.845 -2.968  1.00 9.42  ? 148 LEU A O   1 
ATOM   1207 C  CB  . LEU A 1 147 ? 3.581   -9.640  -3.165  1.00 9.31  ? 148 LEU A CB  1 
ATOM   1208 C  CG  . LEU A 1 147 ? 4.405   -8.362  -3.420  1.00 9.62  ? 148 LEU A CG  1 
ATOM   1209 C  CD1 . LEU A 1 147 ? 3.519   -7.074  -3.529  1.00 10.41 ? 148 LEU A CD1 1 
ATOM   1210 C  CD2 . LEU A 1 147 ? 5.524   -8.157  -2.377  1.00 10.70 ? 148 LEU A CD2 1 
ATOM   1211 N  N   . LYS A 1 148 ? 2.568   -12.299 -4.959  1.00 9.48  ? 149 LYS A N   1 
ATOM   1212 C  CA  . LYS A 1 148 ? 2.542   -13.771 -4.780  1.00 10.31 ? 149 LYS A CA  1 
ATOM   1213 C  C   . LYS A 1 148 ? 3.987   -14.291 -4.777  1.00 10.65 ? 149 LYS A C   1 
ATOM   1214 O  O   . LYS A 1 148 ? 4.868   -13.691 -5.359  1.00 11.51 ? 149 LYS A O   1 
ATOM   1215 C  CB  . LYS A 1 148 ? 1.711   -14.413 -5.934  1.00 11.33 ? 149 LYS A CB  1 
ATOM   1216 C  CG  . LYS A 1 148 ? 2.315   -14.319 -7.321  1.00 13.46 ? 149 LYS A CG  1 
ATOM   1217 C  CD  . LYS A 1 148 ? 1.405   -15.035 -8.345  1.00 17.94 ? 149 LYS A CD  1 
ATOM   1218 C  CE  . LYS A 1 148 ? 2.085   -15.246 -9.668  1.00 22.46 ? 149 LYS A CE  1 
ATOM   1219 N  NZ  . LYS A 1 148 ? 1.228   -16.098 -10.551 1.00 44.06 ? 149 LYS A NZ  1 
ATOM   1220 N  N   . VAL A 1 149 ? 4.199   -15.452 -4.193  1.00 11.19 ? 150 VAL A N   1 
ATOM   1221 C  CA  . VAL A 1 149 ? 5.546   -16.016 -4.188  1.00 12.22 ? 150 VAL A CA  1 
ATOM   1222 C  C   . VAL A 1 149 ? 5.796   -16.909 -5.392  1.00 12.74 ? 150 VAL A C   1 
ATOM   1223 O  O   . VAL A 1 149 ? 5.030   -17.863 -5.646  1.00 13.37 ? 150 VAL A O   1 
ATOM   1224 C  CB  . VAL A 1 149 ? 5.733   -16.788 -2.835  1.00 13.93 ? 150 VAL A CB  1 
ATOM   1225 C  CG1 . VAL A 1 149 ? 7.039   -17.593 -2.870  1.00 14.37 ? 150 VAL A CG1 1 
ATOM   1226 C  CG2 . VAL A 1 149 ? 5.688   -15.790 -1.670  1.00 15.29 ? 150 VAL A CG2 1 
ATOM   1227 N  N   . GLY A 1 150 ? 6.858   -16.643 -6.136  1.00 11.94 ? 151 GLY A N   1 
ATOM   1228 C  CA  . GLY A 1 150 ? 7.229   -17.469 -7.280  1.00 14.56 ? 151 GLY A CA  1 
ATOM   1229 C  C   . GLY A 1 150 ? 8.567   -17.001 -7.702  1.00 13.28 ? 151 GLY A C   1 
ATOM   1230 O  O   . GLY A 1 150 ? 9.518   -17.057 -6.926  1.00 14.58 ? 151 GLY A O   1 
ATOM   1231 N  N   A SER A 1 151 ? 8.640   -16.511 -8.937  0.50 14.26 ? 152 SER A N   1 
ATOM   1232 N  N   B SER A 1 151 ? 8.630   -16.502 -8.932  0.50 14.48 ? 152 SER A N   1 
ATOM   1233 C  CA  A SER A 1 151 ? 9.894   -15.935 -9.426  0.50 15.44 ? 152 SER A CA  1 
ATOM   1234 C  CA  B SER A 1 151 ? 9.866   -15.882 -9.391  0.50 15.58 ? 152 SER A CA  1 
ATOM   1235 C  C   A SER A 1 151 ? 10.237  -14.581 -8.746  0.50 14.60 ? 152 SER A C   1 
ATOM   1236 C  C   B SER A 1 151 ? 10.244  -14.629 -8.564  0.50 15.28 ? 152 SER A C   1 
ATOM   1237 O  O   A SER A 1 151 ? 9.338   -13.807 -8.382  0.50 12.20 ? 152 SER A O   1 
ATOM   1238 O  O   B SER A 1 151 ? 9.395   -13.969 -7.942  0.50 13.40 ? 152 SER A O   1 
ATOM   1239 C  CB  A SER A 1 151 ? 9.866   -15.774 -10.929 0.50 19.62 ? 152 SER A CB  1 
ATOM   1240 C  CB  B SER A 1 151 ? 9.812   -15.525 -10.865 0.50 19.03 ? 152 SER A CB  1 
ATOM   1241 O  OG  A SER A 1 151 ? 8.854   -14.846 -11.273 0.50 19.20 ? 152 SER A OG  1 
ATOM   1242 O  OG  B SER A 1 151 ? 9.374   -16.622 -11.640 0.50 20.11 ? 152 SER A OG  1 
ATOM   1243 N  N   . ALA A 1 152 ? 11.536  -14.331 -8.532  1.00 14.49 ? 153 ALA A N   1 
ATOM   1244 C  CA  . ALA A 1 152 ? 11.981  -13.090 -7.952  1.00 12.84 ? 153 ALA A CA  1 
ATOM   1245 C  C   . ALA A 1 152 ? 11.528  -11.872 -8.715  1.00 13.46 ? 153 ALA A C   1 
ATOM   1246 O  O   . ALA A 1 152 ? 11.404  -11.893 -9.917  1.00 13.83 ? 153 ALA A O   1 
ATOM   1247 C  CB  . ALA A 1 152 ? 13.513  -13.066 -7.725  1.00 13.99 ? 153 ALA A CB  1 
ATOM   1248 N  N   . LYS A 1 153 ? 11.359  -10.764 -7.973  1.00 12.64 ? 154 LYS A N   1 
ATOM   1249 C  CA  . LYS A 1 153 ? 11.077  -9.443  -8.606  1.00 14.65 ? 154 LYS A CA  1 
ATOM   1250 C  C   . LYS A 1 153 ? 12.399  -8.646  -8.519  1.00 11.74 ? 154 LYS A C   1 
ATOM   1251 O  O   . LYS A 1 153 ? 12.829  -8.219  -7.468  1.00 12.46 ? 154 LYS A O   1 
ATOM   1252 C  CB  . LYS A 1 153 ? 9.972   -8.694  -7.802  1.00 14.23 ? 154 LYS A CB  1 
ATOM   1253 C  CG  . LYS A 1 153 ? 9.513   -7.442  -8.511  1.00 13.74 ? 154 LYS A CG  1 
ATOM   1254 C  CD  . LYS A 1 153 ? 8.688   -7.752  -9.742  1.00 14.15 ? 154 LYS A CD  1 
ATOM   1255 C  CE  . LYS A 1 153 ? 7.865   -6.560  -10.160 1.00 16.07 ? 154 LYS A CE  1 
ATOM   1256 N  NZ  . LYS A 1 153 ? 7.315   -6.967  -11.475 1.00 17.19 ? 154 LYS A NZ  1 
ATOM   1257 N  N   . PRO A 1 154 ? 13.110  -8.551  -9.647  1.00 13.26 ? 155 PRO A N   1 
ATOM   1258 C  CA  . PRO A 1 154 ? 14.478  -7.950  -9.592  1.00 14.11 ? 155 PRO A CA  1 
ATOM   1259 C  C   . PRO A 1 154 ? 14.466  -6.493  -9.048  1.00 12.76 ? 155 PRO A C   1 
ATOM   1260 O  O   . PRO A 1 154 ? 15.315  -6.138  -8.201  1.00 15.63 ? 155 PRO A O   1 
ATOM   1261 C  CB  . PRO A 1 154 ? 14.961  -8.039  -11.073 1.00 15.62 ? 155 PRO A CB  1 
ATOM   1262 C  CG  . PRO A 1 154 ? 14.085  -9.080  -11.700 1.00 22.03 ? 155 PRO A CG  1 
ATOM   1263 C  CD  . PRO A 1 154 ? 12.769  -9.032  -11.009 1.00 14.91 ? 155 PRO A CD  1 
ATOM   1264 N  N   . GLY A 1 155 ? 13.405  -5.744  -9.416  1.00 12.76 ? 156 GLY A N   1 
ATOM   1265 C  CA  . GLY A 1 155 ? 13.192  -4.355  -8.972  1.00 15.26 ? 156 GLY A CA  1 
ATOM   1266 C  C   . GLY A 1 155 ? 12.947  -4.191  -7.474  1.00 15.90 ? 156 GLY A C   1 
ATOM   1267 O  O   . GLY A 1 155 ? 13.064  -3.070  -6.961  1.00 19.08 ? 156 GLY A O   1 
ATOM   1268 N  N   . LEU A 1 156 ? 12.612  -5.267  -6.773  1.00 13.28 ? 157 LEU A N   1 
ATOM   1269 C  CA  . LEU A 1 156 ? 12.489  -5.261  -5.325  1.00 12.79 ? 157 LEU A CA  1 
ATOM   1270 C  C   . LEU A 1 156 ? 13.818  -5.434  -4.590  1.00 10.57 ? 157 LEU A C   1 
ATOM   1271 O  O   . LEU A 1 156 ? 13.900  -5.203  -3.390  1.00 11.69 ? 157 LEU A O   1 
ATOM   1272 C  CB  . LEU A 1 156 ? 11.477  -6.363  -4.908  1.00 13.39 ? 157 LEU A CB  1 
ATOM   1273 C  CG  . LEU A 1 156 ? 11.118  -6.504  -3.398  1.00 12.90 ? 157 LEU A CG  1 
ATOM   1274 C  CD1 . LEU A 1 156 ? 10.519  -5.161  -2.882  1.00 15.15 ? 157 LEU A CD1 1 
ATOM   1275 C  CD2 . LEU A 1 156 ? 10.106  -7.618  -3.238  1.00 12.81 ? 157 LEU A CD2 1 
ATOM   1276 N  N   . GLN A 1 157 ? 14.840  -6.009  -5.255  1.00 14.04 ? 158 GLN A N   1 
ATOM   1277 C  CA  . GLN A 1 157 ? 15.995  -6.477  -4.486  1.00 14.14 ? 158 GLN A CA  1 
ATOM   1278 C  C   . GLN A 1 157 ? 16.753  -5.381  -3.759  1.00 13.75 ? 158 GLN A C   1 
ATOM   1279 O  O   . GLN A 1 157 ? 17.198  -5.589  -2.665  1.00 14.71 ? 158 GLN A O   1 
ATOM   1280 C  CB  . GLN A 1 157 ? 16.899  -7.359  -5.362  1.00 14.24 ? 158 GLN A CB  1 
ATOM   1281 C  CG  . GLN A 1 157 ? 18.023  -8.092  -4.561  1.00 16.96 ? 158 GLN A CG  1 
ATOM   1282 C  CD  . GLN A 1 157 ? 17.425  -9.102  -3.596  1.00 13.57 ? 158 GLN A CD  1 
ATOM   1283 O  OE1 . GLN A 1 157 ? 16.335  -9.667  -3.871  1.00 15.13 ? 158 GLN A OE1 1 
ATOM   1284 N  NE2 . GLN A 1 157 ? 18.043  -9.313  -2.458  1.00 17.26 ? 158 GLN A NE2 1 
ATOM   1285 N  N   . LYS A 1 158 ? 16.774  -4.160  -4.290  1.00 14.46 ? 159 LYS A N   1 
ATOM   1286 C  CA  . LYS A 1 158 ? 17.408  -3.026  -3.598  1.00 15.27 ? 159 LYS A CA  1 
ATOM   1287 C  C   . LYS A 1 158 ? 16.785  -2.744  -2.232  1.00 13.53 ? 159 LYS A C   1 
ATOM   1288 O  O   . LYS A 1 158 ? 17.429  -2.355  -1.298  1.00 15.82 ? 159 LYS A O   1 
ATOM   1289 C  CB  . LYS A 1 158 ? 17.514  -1.802  -4.506  1.00 19.34 ? 159 LYS A CB  1 
ATOM   1290 C  CG  . LYS A 1 158 ? 18.529  -2.083  -5.618  1.00 26.80 ? 159 LYS A CG  1 
ATOM   1291 C  CD  . LYS A 1 158 ? 18.931  -0.803  -6.381  1.00 35.13 ? 159 LYS A CD  1 
ATOM   1292 C  CE  . LYS A 1 158 ? 19.837  -1.117  -7.590  1.00 40.25 ? 159 LYS A CE  1 
ATOM   1293 N  NZ  . LYS A 1 158 ? 19.871  -0.072  -8.705  1.00 44.41 ? 159 LYS A NZ  1 
ATOM   1294 N  N   . VAL A 1 159 ? 15.411  -2.864  -2.176  1.00 11.03 ? 160 VAL A N   1 
ATOM   1295 C  CA  . VAL A 1 159 ? 14.692  -2.745  -0.916  1.00 12.32 ? 160 VAL A CA  1 
ATOM   1296 C  C   . VAL A 1 159 ? 15.090  -3.857  0.036   1.00 11.54 ? 160 VAL A C   1 
ATOM   1297 O  O   . VAL A 1 159 ? 15.462  -3.614  1.178   1.00 13.00 ? 160 VAL A O   1 
ATOM   1298 C  CB  . VAL A 1 159 ? 13.144  -2.725  -1.166  1.00 12.18 ? 160 VAL A CB  1 
ATOM   1299 C  CG1 . VAL A 1 159 ? 12.413  -2.801  0.196   1.00 14.71 ? 160 VAL A CG1 1 
ATOM   1300 C  CG2 . VAL A 1 159 ? 12.740  -1.471  -1.925  1.00 15.90 ? 160 VAL A CG2 1 
ATOM   1301 N  N   . VAL A 1 160 ? 15.012  -5.115  -0.460  1.00 13.09 ? 161 VAL A N   1 
ATOM   1302 C  CA  . VAL A 1 160 ? 15.312  -6.288  0.347   1.00 14.94 ? 161 VAL A CA  1 
ATOM   1303 C  C   . VAL A 1 160 ? 16.690  -6.182  0.978   1.00 12.69 ? 161 VAL A C   1 
ATOM   1304 O  O   . VAL A 1 160 ? 16.874  -6.449  2.155   1.00 15.25 ? 161 VAL A O   1 
ATOM   1305 C  CB  . VAL A 1 160 ? 15.201  -7.635  -0.556  1.00 16.69 ? 161 VAL A CB  1 
ATOM   1306 C  CG1 . VAL A 1 160 ? 15.790  -8.844  0.191   1.00 18.42 ? 161 VAL A CG1 1 
ATOM   1307 C  CG2 . VAL A 1 160 ? 13.759  -7.825  -1.022  1.00 19.49 ? 161 VAL A CG2 1 
ATOM   1308 N  N   . ASP A 1 161 ? 17.650  -5.736  0.193   1.00 16.17 ? 162 ASP A N   1 
ATOM   1309 C  CA  . ASP A 1 161 ? 19.059  -5.766  0.682   1.00 15.70 ? 162 ASP A CA  1 
ATOM   1310 C  C   . ASP A 1 161 ? 19.357  -4.675  1.715   1.00 16.53 ? 162 ASP A C   1 
ATOM   1311 O  O   . ASP A 1 161 ? 20.396  -4.816  2.382   1.00 19.88 ? 162 ASP A O   1 
ATOM   1312 C  CB  . ASP A 1 161 ? 19.937  -5.570  -0.504  1.00 18.88 ? 162 ASP A CB  1 
ATOM   1313 C  CG  . ASP A 1 161 ? 20.154  -6.892  -1.270  1.00 21.38 ? 162 ASP A CG  1 
ATOM   1314 O  OD1 . ASP A 1 161 ? 20.109  -7.957  -0.641  1.00 26.93 ? 162 ASP A OD1 1 
ATOM   1315 O  OD2 . ASP A 1 161 ? 20.352  -6.865  -2.466  1.00 25.53 ? 162 ASP A OD2 1 
ATOM   1316 N  N   . VAL A 1 162 ? 18.501  -3.628  1.883   1.00 13.58 ? 163 VAL A N   1 
ATOM   1317 C  CA  . VAL A 1 162 ? 18.746  -2.586  2.883   1.00 17.29 ? 163 VAL A CA  1 
ATOM   1318 C  C   . VAL A 1 162 ? 18.048  -2.886  4.178   1.00 15.86 ? 163 VAL A C   1 
ATOM   1319 O  O   . VAL A 1 162 ? 18.288  -2.241  5.214   1.00 16.65 ? 163 VAL A O   1 
ATOM   1320 C  CB  . VAL A 1 162 ? 18.331  -1.189  2.267   1.00 20.59 ? 163 VAL A CB  1 
ATOM   1321 C  CG1 . VAL A 1 162 ? 16.870  -0.947  2.325   1.00 17.58 ? 163 VAL A CG1 1 
ATOM   1322 C  CG2 . VAL A 1 162 ? 19.036  -0.012  2.847   1.00 25.56 ? 163 VAL A CG2 1 
ATOM   1323 N  N   . LEU A 1 163 ? 17.192  -3.945  4.179   1.00 14.82 ? 164 LEU A N   1 
ATOM   1324 C  CA  . LEU A 1 163 ? 16.381  -4.181  5.371   1.00 14.23 ? 164 LEU A CA  1 
ATOM   1325 C  C   . LEU A 1 163 ? 17.228  -4.532  6.594   1.00 13.95 ? 164 LEU A C   1 
ATOM   1326 O  O   . LEU A 1 163 ? 16.802  -4.219  7.726   1.00 14.08 ? 164 LEU A O   1 
ATOM   1327 C  CB  . LEU A 1 163 ? 15.296  -5.205  5.168   1.00 14.09 ? 164 LEU A CB  1 
ATOM   1328 C  CG  . LEU A 1 163 ? 14.289  -4.839  4.069   1.00 12.89 ? 164 LEU A CG  1 
ATOM   1329 C  CD1 . LEU A 1 163 ? 13.279  -5.975  3.938   1.00 14.89 ? 164 LEU A CD1 1 
ATOM   1330 C  CD2 . LEU A 1 163 ? 13.526  -3.537  4.296   1.00 13.24 ? 164 LEU A CD2 1 
ATOM   1331 N  N   . ASP A 1 164 ? 18.384  -5.216  6.408   1.00 16.69 ? 165 ASP A N   1 
ATOM   1332 C  CA  . ASP A 1 164 ? 19.258  -5.564  7.586   1.00 20.01 ? 165 ASP A CA  1 
ATOM   1333 C  C   . ASP A 1 164 ? 19.763  -4.296  8.326   1.00 19.99 ? 165 ASP A C   1 
ATOM   1334 O  O   . ASP A 1 164 ? 20.025  -4.309  9.535   1.00 26.97 ? 165 ASP A O   1 
ATOM   1335 C  CB  . ASP A 1 164 ? 20.445  -6.403  7.131   1.00 23.22 ? 165 ASP A CB  1 
ATOM   1336 C  CG  . ASP A 1 164 ? 21.497  -5.553  6.416   1.00 31.81 ? 165 ASP A CG  1 
ATOM   1337 O  OD1 . ASP A 1 164 ? 21.214  -4.972  5.341   1.00 38.83 ? 165 ASP A OD1 1 
ATOM   1338 O  OD2 . ASP A 1 164 ? 22.649  -5.466  6.946   1.00 50.88 ? 165 ASP A OD2 1 
ATOM   1339 N  N   . SER A 1 165 ? 19.763  -3.184  7.636   1.00 16.04 ? 166 SER A N   1 
ATOM   1340 C  CA  . SER A 1 165 ? 20.181  -1.929  8.276   1.00 17.03 ? 166 SER A CA  1 
ATOM   1341 C  C   . SER A 1 165 ? 19.042  -1.194  9.042   1.00 16.44 ? 166 SER A C   1 
ATOM   1342 O  O   . SER A 1 165 ? 19.310  -0.184  9.764   1.00 16.97 ? 166 SER A O   1 
ATOM   1343 C  CB  . SER A 1 165 ? 20.784  -0.986  7.257   1.00 21.50 ? 166 SER A CB  1 
ATOM   1344 O  OG  . SER A 1 165 ? 19.785  -0.347  6.442   1.00 20.94 ? 166 SER A OG  1 
ATOM   1345 N  N   . ILE A 1 166 ? 17.805  -1.644  8.852   1.00 14.36 ? 167 ILE A N   1 
ATOM   1346 C  CA  . ILE A 1 166 ? 16.687  -1.039  9.571   1.00 15.97 ? 167 ILE A CA  1 
ATOM   1347 C  C   . ILE A 1 166 ? 15.872  -2.079  10.299  1.00 14.07 ? 167 ILE A C   1 
ATOM   1348 O  O   . ILE A 1 166 ? 14.622  -2.079  10.288  1.00 13.30 ? 167 ILE A O   1 
ATOM   1349 C  CB  . ILE A 1 166 ? 15.800  -0.200  8.634   1.00 14.14 ? 167 ILE A CB  1 
ATOM   1350 C  CG1 . ILE A 1 166 ? 15.239  -1.041  7.480   1.00 12.85 ? 167 ILE A CG1 1 
ATOM   1351 C  CG2 . ILE A 1 166 ? 16.531  1.065   8.140   1.00 16.13 ? 167 ILE A CG2 1 
ATOM   1352 C  CD1 . ILE A 1 166 ? 13.983  -0.356  6.936   1.00 14.25 ? 167 ILE A CD1 1 
ATOM   1353 N  N   . LYS A 1 167 ? 16.599  -2.957  10.981  1.00 14.30 ? 168 LYS A N   1 
ATOM   1354 C  CA  . LYS A 1 167 ? 15.934  -4.102  11.544  1.00 14.31 ? 168 LYS A CA  1 
ATOM   1355 C  C   . LYS A 1 167 ? 14.811  -3.782  12.591  1.00 15.21 ? 168 LYS A C   1 
ATOM   1356 O  O   . LYS A 1 167 ? 13.797  -4.468  12.658  1.00 14.27 ? 168 LYS A O   1 
ATOM   1357 C  CB  . LYS A 1 167 ? 16.967  -5.080  12.139  1.00 16.39 ? 168 LYS A CB  1 
ATOM   1358 C  CG  . LYS A 1 167 ? 16.314  -6.403  12.581  1.00 19.70 ? 168 LYS A CG  1 
ATOM   1359 C  CD  . LYS A 1 167 ? 17.401  -7.269  13.257  1.00 28.27 ? 168 LYS A CD  1 
ATOM   1360 C  CE  . LYS A 1 167 ? 16.741  -8.509  13.813  1.00 34.22 ? 168 LYS A CE  1 
ATOM   1361 N  NZ  . LYS A 1 167 ? 17.673  -9.280  14.690  1.00 45.78 ? 168 LYS A NZ  1 
ATOM   1362 N  N   . THR A 1 168 ? 15.044  -2.730  13.455  1.00 14.35 ? 169 THR A N   1 
ATOM   1363 C  CA  . THR A 1 168 ? 14.176  -2.470  14.587  1.00 15.59 ? 169 THR A CA  1 
ATOM   1364 C  C   . THR A 1 168 ? 13.477  -1.087  14.452  1.00 12.98 ? 169 THR A C   1 
ATOM   1365 O  O   . THR A 1 168 ? 13.943  -0.220  13.693  1.00 15.07 ? 169 THR A O   1 
ATOM   1366 C  CB  . THR A 1 168 ? 15.033  -2.564  15.907  1.00 18.03 ? 169 THR A CB  1 
ATOM   1367 O  OG1 . THR A 1 168 ? 16.223  -1.788  15.773  1.00 19.20 ? 169 THR A OG1 1 
ATOM   1368 C  CG2 . THR A 1 168 ? 15.392  -4.010  16.234  1.00 17.87 ? 169 THR A CG2 1 
ATOM   1369 N  N   . LYS A 1 169 ? 12.388  -0.939  15.194  1.00 15.81 ? 170 LYS A N   1 
ATOM   1370 C  CA  . LYS A 1 169 ? 11.606  0.287   15.229  1.00 13.01 ? 170 LYS A CA  1 
ATOM   1371 C  C   . LYS A 1 169 ? 12.505  1.471   15.486  1.00 17.67 ? 170 LYS A C   1 
ATOM   1372 O  O   . LYS A 1 169 ? 13.321  1.506   16.468  1.00 19.37 ? 170 LYS A O   1 
ATOM   1373 C  CB  . LYS A 1 169 ? 10.552  0.170   16.314  1.00 16.28 ? 170 LYS A CB  1 
ATOM   1374 C  CG  . LYS A 1 169 ? 9.720   1.441   16.474  1.00 16.34 ? 170 LYS A CG  1 
ATOM   1375 C  CD  . LYS A 1 169 ? 8.663   1.251   17.551  1.00 20.49 ? 170 LYS A CD  1 
ATOM   1376 C  CE  . LYS A 1 169 ? 7.824   2.528   17.629  1.00 29.85 ? 170 LYS A CE  1 
ATOM   1377 N  NZ  . LYS A 1 169 ? 7.158   2.850   18.935  1.00 43.52 ? 170 LYS A NZ  1 
ATOM   1378 N  N   . GLY A 1 170 ? 12.382  2.473   14.615  1.00 13.38 ? 171 GLY A N   1 
ATOM   1379 C  CA  . GLY A 1 170 ? 13.071  3.746   14.804  1.00 17.00 ? 171 GLY A CA  1 
ATOM   1380 C  C   . GLY A 1 170 ? 14.257  3.871   13.895  1.00 16.56 ? 171 GLY A C   1 
ATOM   1381 O  O   . GLY A 1 170 ? 14.799  5.018   13.764  1.00 23.10 ? 171 GLY A O   1 
ATOM   1382 N  N   . LYS A 1 171 ? 14.764  2.738   13.344  1.00 15.59 ? 172 LYS A N   1 
ATOM   1383 C  CA  . LYS A 1 171 ? 15.890  2.831   12.471  1.00 12.96 ? 172 LYS A CA  1 
ATOM   1384 C  C   . LYS A 1 171 ? 15.554  3.321   11.075  1.00 13.68 ? 172 LYS A C   1 
ATOM   1385 O  O   . LYS A 1 171 ? 14.492  2.934   10.514  1.00 13.95 ? 172 LYS A O   1 
ATOM   1386 C  CB  . LYS A 1 171 ? 16.695  1.541   12.352  1.00 13.57 ? 172 LYS A CB  1 
ATOM   1387 C  CG  . LYS A 1 171 ? 17.158  1.056   13.714  1.00 19.40 ? 172 LYS A CG  1 
ATOM   1388 C  CD  . LYS A 1 171 ? 18.194  -0.069  13.578  1.00 21.97 ? 172 LYS A CD  1 
ATOM   1389 C  CE  . LYS A 1 171 ? 19.267  -0.122  14.661  1.00 35.00 ? 172 LYS A CE  1 
ATOM   1390 N  NZ  . LYS A 1 171 ? 20.380  -0.866  14.013  1.00 39.94 ? 172 LYS A NZ  1 
ATOM   1391 N  N   . SER A 1 172 ? 16.399  4.155   10.498  1.00 15.84 ? 173 SER A N   1 
ATOM   1392 C  CA  . SER A 1 172 ? 16.229  4.675   9.184   1.00 13.89 ? 173 SER A CA  1 
ATOM   1393 C  C   . SER A 1 172 ? 17.510  4.703   8.424   1.00 15.18 ? 173 SER A C   1 
ATOM   1394 O  O   . SER A 1 172 ? 18.632  4.679   9.010   1.00 17.88 ? 173 SER A O   1 
ATOM   1395 C  CB  . SER A 1 172 ? 15.501  6.044   9.152   1.00 15.42 ? 173 SER A CB  1 
ATOM   1396 O  OG  . SER A 1 172 ? 16.319  7.073   9.744   1.00 18.83 ? 173 SER A OG  1 
ATOM   1397 N  N   . ALA A 1 173 ? 17.457  4.829   7.104   1.00 14.18 ? 174 ALA A N   1 
ATOM   1398 C  CA  . ALA A 1 173 ? 18.642  4.986   6.311   1.00 16.47 ? 174 ALA A CA  1 
ATOM   1399 C  C   . ALA A 1 173 ? 18.353  5.839   5.147   1.00 15.53 ? 174 ALA A C   1 
ATOM   1400 O  O   . ALA A 1 173 ? 17.200  5.848   4.677   1.00 14.38 ? 174 ALA A O   1 
ATOM   1401 C  CB  . ALA A 1 173 ? 19.073  3.595   5.824   1.00 16.96 ? 174 ALA A CB  1 
ATOM   1402 N  N   A ASP A 1 174 ? 19.466  6.271   4.523   0.50 19.59 ? 175 ASP A N   1 
ATOM   1403 N  N   B ASP A 1 174 ? 19.296  6.681   4.704   0.50 13.05 ? 175 ASP A N   1 
ATOM   1404 C  CA  A ASP A 1 174 ? 19.435  6.910   3.215   0.50 16.89 ? 175 ASP A CA  1 
ATOM   1405 C  CA  B ASP A 1 174 ? 19.133  7.250   3.337   0.50 13.23 ? 175 ASP A CA  1 
ATOM   1406 C  C   A ASP A 1 174 ? 18.960  5.948   2.152   0.50 15.68 ? 175 ASP A C   1 
ATOM   1407 C  C   B ASP A 1 174 ? 18.883  6.137   2.302   0.50 15.22 ? 175 ASP A C   1 
ATOM   1408 O  O   A ASP A 1 174 ? 19.399  4.775   2.116   0.50 18.95 ? 175 ASP A O   1 
ATOM   1409 O  O   B ASP A 1 174 ? 19.361  5.031   2.499   0.50 13.52 ? 175 ASP A O   1 
ATOM   1410 C  CB  A ASP A 1 174 ? 20.820  7.465   2.816   0.50 23.28 ? 175 ASP A CB  1 
ATOM   1411 C  CB  B ASP A 1 174 ? 20.300  8.211   2.937   0.50 14.14 ? 175 ASP A CB  1 
ATOM   1412 C  CG  A ASP A 1 174 ? 21.294  8.631   3.700   0.50 35.39 ? 175 ASP A CG  1 
ATOM   1413 C  CG  B ASP A 1 174 ? 21.590  7.480   2.584   0.50 19.17 ? 175 ASP A CG  1 
ATOM   1414 O  OD1 A ASP A 1 174 ? 20.450  9.392   4.201   0.50 25.81 ? 175 ASP A OD1 1 
ATOM   1415 O  OD1 B ASP A 1 174 ? 22.441  7.280   3.495   0.50 24.85 ? 175 ASP A OD1 1 
ATOM   1416 O  OD2 A ASP A 1 174 ? 22.547  8.800   3.863   0.50 38.25 ? 175 ASP A OD2 1 
ATOM   1417 O  OD2 B ASP A 1 174 ? 21.761  7.080   1.403   0.50 22.08 ? 175 ASP A OD2 1 
ATOM   1418 N  N   . PHE A 1 175 ? 18.066  6.414   1.259   1.00 14.88 ? 176 PHE A N   1 
ATOM   1419 C  CA  . PHE A 1 175 ? 17.621  5.408   0.267   1.00 14.45 ? 176 PHE A CA  1 
ATOM   1420 C  C   . PHE A 1 175 ? 17.251  6.160   -0.991  1.00 15.01 ? 176 PHE A C   1 
ATOM   1421 O  O   . PHE A 1 175 ? 16.089  6.503   -1.211  1.00 15.98 ? 176 PHE A O   1 
ATOM   1422 C  CB  . PHE A 1 175 ? 16.392  4.612   0.779   1.00 14.75 ? 176 PHE A CB  1 
ATOM   1423 C  CG  . PHE A 1 175 ? 16.148  3.346   0.000   1.00 15.95 ? 176 PHE A CG  1 
ATOM   1424 C  CD1 . PHE A 1 175 ? 17.050  2.297   0.015   1.00 15.77 ? 176 PHE A CD1 1 
ATOM   1425 C  CD2 . PHE A 1 175 ? 14.990  3.175   -0.716  1.00 15.62 ? 176 PHE A CD2 1 
ATOM   1426 C  CE1 . PHE A 1 175 ? 16.812  1.132   -0.706  1.00 16.54 ? 176 PHE A CE1 1 
ATOM   1427 C  CE2 . PHE A 1 175 ? 14.730  2.022   -1.496  1.00 15.02 ? 176 PHE A CE2 1 
ATOM   1428 C  CZ  . PHE A 1 175 ? 15.632  0.980   -1.448  1.00 16.75 ? 176 PHE A CZ  1 
ATOM   1429 N  N   . THR A 1 176 ? 18.253  6.515   -1.785  1.00 14.46 ? 177 THR A N   1 
ATOM   1430 C  CA  . THR A 1 176 ? 18.105  7.355   -2.938  1.00 14.00 ? 177 THR A CA  1 
ATOM   1431 C  C   . THR A 1 176 ? 18.147  6.562   -4.264  1.00 12.34 ? 177 THR A C   1 
ATOM   1432 O  O   . THR A 1 176 ? 18.608  5.411   -4.294  1.00 12.87 ? 177 THR A O   1 
ATOM   1433 C  CB  . THR A 1 176 ? 19.208  8.445   -3.001  1.00 14.19 ? 177 THR A CB  1 
ATOM   1434 O  OG1 . THR A 1 176 ? 20.482  7.801   -2.996  1.00 16.68 ? 177 THR A OG1 1 
ATOM   1435 C  CG2 . THR A 1 176 ? 19.051  9.514   -1.861  1.00 21.26 ? 177 THR A CG2 1 
ATOM   1436 N  N   . ASN A 1 177 ? 17.556  7.114   -5.310  1.00 11.93 ? 178 ASN A N   1 
ATOM   1437 C  CA  . ASN A 1 177 ? 17.599  6.571   -6.662  1.00 12.08 ? 178 ASN A CA  1 
ATOM   1438 C  C   . ASN A 1 177 ? 16.861  5.244   -6.760  1.00 13.11 ? 178 ASN A C   1 
ATOM   1439 O  O   . ASN A 1 177 ? 17.160  4.473   -7.662  1.00 17.81 ? 178 ASN A O   1 
ATOM   1440 C  CB  . ASN A 1 177 ? 19.047  6.447   -7.220  1.00 12.50 ? 178 ASN A CB  1 
ATOM   1441 C  CG  . ASN A 1 177 ? 19.684  7.808   -7.289  1.00 15.66 ? 178 ASN A CG  1 
ATOM   1442 O  OD1 . ASN A 1 177 ? 19.273  8.639   -8.128  1.00 17.85 ? 178 ASN A OD1 1 
ATOM   1443 N  ND2 . ASN A 1 177 ? 20.587  8.108   -6.363  1.00 14.78 ? 178 ASN A ND2 1 
ATOM   1444 N  N   . PHE A 1 178 ? 15.881  4.988   -5.867  1.00 12.16 ? 179 PHE A N   1 
ATOM   1445 C  CA  . PHE A 1 178 ? 15.056  3.742   -6.036  1.00 12.49 ? 179 PHE A CA  1 
ATOM   1446 C  C   . PHE A 1 178 ? 13.942  4.087   -7.016  1.00 11.96 ? 179 PHE A C   1 
ATOM   1447 O  O   . PHE A 1 178 ? 13.217  5.039   -6.863  1.00 12.62 ? 179 PHE A O   1 
ATOM   1448 C  CB  . PHE A 1 178 ? 14.480  3.287   -4.716  1.00 13.81 ? 179 PHE A CB  1 
ATOM   1449 C  CG  . PHE A 1 178 ? 13.683  2.047   -4.904  1.00 12.46 ? 179 PHE A CG  1 
ATOM   1450 C  CD1 . PHE A 1 178 ? 14.307  0.819   -5.092  1.00 15.32 ? 179 PHE A CD1 1 
ATOM   1451 C  CD2 . PHE A 1 178 ? 12.258  2.115   -5.052  1.00 11.78 ? 179 PHE A CD2 1 
ATOM   1452 C  CE1 . PHE A 1 178 ? 13.580  -0.323  -5.351  1.00 13.84 ? 179 PHE A CE1 1 
ATOM   1453 C  CE2 . PHE A 1 178 ? 11.565  0.918   -5.363  1.00 12.51 ? 179 PHE A CE2 1 
ATOM   1454 C  CZ  . PHE A 1 178 ? 12.204  -0.253  -5.476  1.00 12.46 ? 179 PHE A CZ  1 
ATOM   1455 N  N   . ASP A 1 179 ? 13.863  3.283   -8.052  1.00 12.49 ? 180 ASP A N   1 
ATOM   1456 C  CA  . ASP A 1 179 ? 12.846  3.451   -9.098  1.00 13.01 ? 180 ASP A CA  1 
ATOM   1457 C  C   . ASP A 1 179 ? 11.605  2.570   -8.917  1.00 13.47 ? 180 ASP A C   1 
ATOM   1458 O  O   . ASP A 1 179 ? 11.630  1.341   -9.119  1.00 13.48 ? 180 ASP A O   1 
ATOM   1459 C  CB  . ASP A 1 179 ? 13.480  3.132   -10.452 1.00 14.46 ? 180 ASP A CB  1 
ATOM   1460 C  CG  . ASP A 1 179 ? 12.573  3.458   -11.626 1.00 17.63 ? 180 ASP A CG  1 
ATOM   1461 O  OD1 . ASP A 1 179 ? 11.353  3.655   -11.495 1.00 15.23 ? 180 ASP A OD1 1 
ATOM   1462 O  OD2 . ASP A 1 179 ? 13.114  3.527   -12.752 1.00 22.14 ? 180 ASP A OD2 1 
ATOM   1463 N  N   . PRO A 1 180 ? 10.474  3.177   -8.481  1.00 12.12 ? 181 PRO A N   1 
ATOM   1464 C  CA  . PRO A 1 180 ? 9.282   2.343   -8.202  1.00 11.82 ? 181 PRO A CA  1 
ATOM   1465 C  C   . PRO A 1 180 ? 8.580   1.742   -9.408  1.00 10.28 ? 181 PRO A C   1 
ATOM   1466 O  O   . PRO A 1 180 ? 7.714   0.804   -9.248  1.00 11.50 ? 181 PRO A O   1 
ATOM   1467 C  CB  . PRO A 1 180 ? 8.395   3.298   -7.423  1.00 14.08 ? 181 PRO A CB  1 
ATOM   1468 C  CG  . PRO A 1 180 ? 8.711   4.662   -8.014  1.00 13.81 ? 181 PRO A CG  1 
ATOM   1469 C  CD  . PRO A 1 180 ? 10.253  4.576   -8.167  1.00 12.56 ? 181 PRO A CD  1 
ATOM   1470 N  N   . ARG A 1 181 ? 8.992   2.125   -10.619 1.00 11.59 ? 182 ARG A N   1 
ATOM   1471 C  CA  . ARG A 1 181 ? 8.513   1.429   -11.829 1.00 13.20 ? 182 ARG A CA  1 
ATOM   1472 C  C   . ARG A 1 181 ? 8.856   -0.047  -11.755 1.00 11.56 ? 182 ARG A C   1 
ATOM   1473 O  O   . ARG A 1 181 ? 8.193   -0.875  -12.405 1.00 14.10 ? 182 ARG A O   1 
ATOM   1474 C  CB  . ARG A 1 181 ? 9.054   2.028   -13.146 1.00 13.34 ? 182 ARG A CB  1 
ATOM   1475 C  CG  . ARG A 1 181 ? 8.537   3.445   -13.351 1.00 13.84 ? 182 ARG A CG  1 
ATOM   1476 C  CD  . ARG A 1 181 ? 9.085   4.187   -14.548 1.00 17.56 ? 182 ARG A CD  1 
ATOM   1477 N  NE  . ARG A 1 181 ? 10.542  4.392   -14.386 1.00 17.64 ? 182 ARG A NE  1 
ATOM   1478 C  CZ  . ARG A 1 181 ? 11.230  5.073   -15.295 1.00 24.18 ? 182 ARG A CZ  1 
ATOM   1479 N  NH1 . ARG A 1 181 ? 10.630  5.514   -16.398 1.00 25.40 ? 182 ARG A NH1 1 
ATOM   1480 N  NH2 . ARG A 1 181 ? 12.507  5.251   -15.157 1.00 26.49 ? 182 ARG A NH2 1 
ATOM   1481 N  N   . GLY A 1 182 ? 9.924   -0.394  -11.045 1.00 12.51 ? 183 GLY A N   1 
ATOM   1482 C  CA  . GLY A 1 182 ? 10.390  -1.816  -10.950 1.00 13.66 ? 183 GLY A CA  1 
ATOM   1483 C  C   . GLY A 1 182 ? 9.484   -2.674  -10.085 1.00 15.18 ? 183 GLY A C   1 
ATOM   1484 O  O   . GLY A 1 182 ? 9.769   -3.896  -9.978  1.00 15.65 ? 183 GLY A O   1 
ATOM   1485 N  N   . LEU A 1 183 ? 8.452   -2.092  -9.419  1.00 11.78 ? 184 LEU A N   1 
ATOM   1486 C  CA  . LEU A 1 183 ? 7.552   -2.826  -8.605  1.00 11.05 ? 184 LEU A CA  1 
ATOM   1487 C  C   . LEU A 1 183 ? 6.204   -3.027  -9.270  1.00 10.94 ? 184 LEU A C   1 
ATOM   1488 O  O   . LEU A 1 183 ? 5.315   -3.668  -8.662  1.00 12.16 ? 184 LEU A O   1 
ATOM   1489 C  CB  . LEU A 1 183 ? 7.345   -2.075  -7.293  1.00 12.14 ? 184 LEU A CB  1 
ATOM   1490 C  CG  . LEU A 1 183 ? 8.613   -1.910  -6.437  1.00 12.95 ? 184 LEU A CG  1 
ATOM   1491 C  CD1 . LEU A 1 183 ? 8.357   -1.064  -5.220  1.00 15.82 ? 184 LEU A CD1 1 
ATOM   1492 C  CD2 . LEU A 1 183 ? 9.258   -3.274  -6.094  1.00 15.13 ? 184 LEU A CD2 1 
ATOM   1493 N  N   . LEU A 1 184 ? 6.008   -2.605  -10.524 1.00 11.64 ? 185 LEU A N   1 
ATOM   1494 C  CA  . LEU A 1 184 ? 4.701   -2.694  -11.177 1.00 11.27 ? 185 LEU A CA  1 
ATOM   1495 C  C   . LEU A 1 184 ? 4.551   -3.978  -11.961 1.00 14.00 ? 185 LEU A C   1 
ATOM   1496 O  O   . LEU A 1 184 ? 5.549   -4.480  -12.513 1.00 18.39 ? 185 LEU A O   1 
ATOM   1497 C  CB  . LEU A 1 184 ? 4.449   -1.487  -12.151 1.00 12.29 ? 185 LEU A CB  1 
ATOM   1498 C  CG  . LEU A 1 184 ? 4.626   -0.088  -11.486 1.00 12.61 ? 185 LEU A CG  1 
ATOM   1499 C  CD1 . LEU A 1 184 ? 4.456   1.018   -12.500 1.00 14.36 ? 185 LEU A CD1 1 
ATOM   1500 C  CD2 . LEU A 1 184 ? 3.565   0.102   -10.366 1.00 13.54 ? 185 LEU A CD2 1 
ATOM   1501 N  N   . PRO A 1 185 ? 3.340   -4.508  -12.096 1.00 10.67 ? 186 PRO A N   1 
ATOM   1502 C  CA  . PRO A 1 185 ? 3.108   -5.668  -13.000 1.00 11.25 ? 186 PRO A CA  1 
ATOM   1503 C  C   . PRO A 1 185 ? 2.974   -5.144  -14.419 1.00 12.50 ? 186 PRO A C   1 
ATOM   1504 O  O   . PRO A 1 185 ? 3.009   -3.931  -14.623 1.00 12.88 ? 186 PRO A O   1 
ATOM   1505 C  CB  . PRO A 1 185 ? 1.758   -6.247  -12.451 1.00 12.20 ? 186 PRO A CB  1 
ATOM   1506 C  CG  . PRO A 1 185 ? 1.000   -4.972  -11.937 1.00 11.20 ? 186 PRO A CG  1 
ATOM   1507 C  CD  . PRO A 1 185 ? 2.139   -4.081  -11.307 1.00 11.63 ? 186 PRO A CD  1 
ATOM   1508 N  N   A GLU A 1 186 ? 2.800   -6.115  -15.300 0.50 12.54 ? 187 GLU A N   1 
ATOM   1509 N  N   B GLU A 1 186 ? 2.711   -5.993  -15.444 0.50 14.00 ? 187 GLU A N   1 
ATOM   1510 C  CA  A GLU A 1 186 ? 2.655   -5.810  -16.685 0.50 13.47 ? 187 GLU A CA  1 
ATOM   1511 C  CA  B GLU A 1 186 ? 2.526   -5.462  -16.872 0.50 13.53 ? 187 GLU A CA  1 
ATOM   1512 C  C   A GLU A 1 186 ? 1.427   -4.907  -16.949 0.50 10.86 ? 187 GLU A C   1 
ATOM   1513 C  C   B GLU A 1 186 ? 1.225   -4.782  -17.081 0.50 13.01 ? 187 GLU A C   1 
ATOM   1514 O  O   A GLU A 1 186 ? 1.610   -3.765  -17.451 0.50 11.63 ? 187 GLU A O   1 
ATOM   1515 O  O   B GLU A 1 186 ? 1.057   -3.801  -17.791 0.50 14.66 ? 187 GLU A O   1 
ATOM   1516 C  CB  A GLU A 1 186 ? 2.633   -7.121  -17.421 0.50 12.94 ? 187 GLU A CB  1 
ATOM   1517 C  CB  B GLU A 1 186 ? 2.481   -6.594  -17.892 0.50 13.12 ? 187 GLU A CB  1 
ATOM   1518 C  CG  A GLU A 1 186 ? 2.567   -6.996  -18.893 0.50 18.45 ? 187 GLU A CG  1 
ATOM   1519 C  CG  B GLU A 1 186 ? 3.683   -7.456  -17.865 0.50 14.13 ? 187 GLU A CG  1 
ATOM   1520 C  CD  A GLU A 1 186 ? 2.395   -8.369  -19.534 0.50 19.60 ? 187 GLU A CD  1 
ATOM   1521 C  CD  B GLU A 1 186 ? 3.582   -8.673  -18.808 0.50 15.49 ? 187 GLU A CD  1 
ATOM   1522 O  OE1 A GLU A 1 186 ? 3.086   -9.358  -19.074 0.50 18.77 ? 187 GLU A OE1 1 
ATOM   1523 O  OE1 B GLU A 1 186 ? 2.477   -9.015  -19.386 0.50 15.80 ? 187 GLU A OE1 1 
ATOM   1524 O  OE2 A GLU A 1 186 ? 1.562   -8.431  -20.459 0.50 23.89 ? 187 GLU A OE2 1 
ATOM   1525 O  OE2 B GLU A 1 186 ? 4.645   -9.258  -19.024 0.50 19.62 ? 187 GLU A OE2 1 
ATOM   1526 N  N   . SER A 1 187 ? 0.225   -5.358  -16.496 1.00 12.04 ? 188 SER A N   1 
ATOM   1527 C  CA  . SER A 1 187 ? -1.041  -4.738  -16.744 1.00 12.22 ? 188 SER A CA  1 
ATOM   1528 C  C   . SER A 1 187 ? -1.451  -3.719  -15.677 1.00 11.84 ? 188 SER A C   1 
ATOM   1529 O  O   . SER A 1 187 ? -1.219  -3.955  -14.477 1.00 15.24 ? 188 SER A O   1 
ATOM   1530 C  CB  . SER A 1 187 ? -2.138  -5.829  -16.764 1.00 14.74 ? 188 SER A CB  1 
ATOM   1531 O  OG  . SER A 1 187 ? -3.462  -5.262  -16.917 1.00 14.09 ? 188 SER A OG  1 
ATOM   1532 N  N   . LEU A 1 188 ? -2.116  -2.651  -16.106 1.00 12.19 ? 189 LEU A N   1 
ATOM   1533 C  CA  . LEU A 1 188 ? -2.681  -1.648  -15.210 1.00 12.03 ? 189 LEU A CA  1 
ATOM   1534 C  C   . LEU A 1 188 ? -4.201  -1.752  -15.081 1.00 11.55 ? 189 LEU A C   1 
ATOM   1535 O  O   . LEU A 1 188 ? -4.854  -0.815  -14.600 1.00 13.78 ? 189 LEU A O   1 
ATOM   1536 C  CB  . LEU A 1 188 ? -2.222  -0.211  -15.528 1.00 13.43 ? 189 LEU A CB  1 
ATOM   1537 C  CG  . LEU A 1 188 ? -0.756  0.160   -15.435 1.00 15.65 ? 189 LEU A CG  1 
ATOM   1538 C  CD1 . LEU A 1 188 ? -0.606  1.632   -15.877 1.00 16.54 ? 189 LEU A CD1 1 
ATOM   1539 C  CD2 . LEU A 1 188 ? -0.237  -0.011  -14.016 1.00 16.19 ? 189 LEU A CD2 1 
ATOM   1540 N  N   . ASP A 1 189 ? -4.772  -2.914  -15.419 1.00 11.71 ? 190 ASP A N   1 
ATOM   1541 C  CA  . ASP A 1 189 ? -6.160  -3.122  -15.154 1.00 11.79 ? 190 ASP A CA  1 
ATOM   1542 C  C   . ASP A 1 189 ? -6.437  -3.145  -13.618 1.00 9.35  ? 190 ASP A C   1 
ATOM   1543 O  O   . ASP A 1 189 ? -5.612  -3.675  -12.870 1.00 10.09 ? 190 ASP A O   1 
ATOM   1544 C  CB  . ASP A 1 189 ? -6.558  -4.508  -15.684 1.00 15.15 ? 190 ASP A CB  1 
ATOM   1545 C  CG  . ASP A 1 189 ? -6.735  -4.538  -17.262 1.00 17.82 ? 190 ASP A CG  1 
ATOM   1546 O  OD1 . ASP A 1 189 ? -6.736  -3.469  -17.871 1.00 25.90 ? 190 ASP A OD1 1 
ATOM   1547 O  OD2 . ASP A 1 189 ? -6.889  -5.639  -17.717 1.00 25.93 ? 190 ASP A OD2 1 
ATOM   1548 N  N   . TYR A 1 190 ? -7.553  -2.535  -13.201 1.00 9.69  ? 191 TYR A N   1 
ATOM   1549 C  CA  . TYR A 1 190 ? -7.742  -2.308  -11.771 1.00 8.81  ? 191 TYR A CA  1 
ATOM   1550 C  C   . TYR A 1 190 ? -9.158  -2.375  -11.368 1.00 8.79  ? 191 TYR A C   1 
ATOM   1551 O  O   . TYR A 1 190 ? -10.136 -2.251  -12.155 1.00 9.38  ? 191 TYR A O   1 
ATOM   1552 C  CB  . TYR A 1 190 ? -7.152  -0.905  -11.407 1.00 9.85  ? 191 TYR A CB  1 
ATOM   1553 C  CG  . TYR A 1 190 ? -7.855  0.259   -12.077 1.00 9.50  ? 191 TYR A CG  1 
ATOM   1554 C  CD1 . TYR A 1 190 ? -9.001  0.816   -11.533 1.00 11.21 ? 191 TYR A CD1 1 
ATOM   1555 C  CD2 . TYR A 1 190 ? -7.372  0.785   -13.267 1.00 9.90  ? 191 TYR A CD2 1 
ATOM   1556 C  CE1 . TYR A 1 190 ? -9.654  1.864   -12.154 1.00 10.77 ? 191 TYR A CE1 1 
ATOM   1557 C  CE2 . TYR A 1 190 ? -8.012  1.838   -13.902 1.00 10.54 ? 191 TYR A CE2 1 
ATOM   1558 C  CZ  . TYR A 1 190 ? -9.157  2.376   -13.343 1.00 11.21 ? 191 TYR A CZ  1 
ATOM   1559 O  OH  . TYR A 1 190 ? -9.810  3.421   -13.963 1.00 12.47 ? 191 TYR A OH  1 
ATOM   1560 N  N   . TRP A 1 191 ? -9.324  -2.524  -10.026 1.00 8.64  ? 192 TRP A N   1 
ATOM   1561 C  CA  . TRP A 1 191 ? -10.573 -2.263  -9.329  1.00 8.00  ? 192 TRP A CA  1 
ATOM   1562 C  C   . TRP A 1 191 ? -10.461 -0.987  -8.550  1.00 7.87  ? 192 TRP A C   1 
ATOM   1563 O  O   . TRP A 1 191 ? -9.363  -0.639  -8.088  1.00 9.30  ? 192 TRP A O   1 
ATOM   1564 C  CB  . TRP A 1 191 ? -10.910 -3.409  -8.351  1.00 9.31  ? 192 TRP A CB  1 
ATOM   1565 C  CG  . TRP A 1 191 ? -11.138 -4.726  -9.005  1.00 9.59  ? 192 TRP A CG  1 
ATOM   1566 C  CD1 . TRP A 1 191 ? -12.297 -5.156  -9.703  1.00 10.81 ? 192 TRP A CD1 1 
ATOM   1567 C  CD2 . TRP A 1 191 ? -10.235 -5.863  -8.952  1.00 9.62  ? 192 TRP A CD2 1 
ATOM   1568 N  NE1 . TRP A 1 191 ? -12.080 -6.477  -10.072 1.00 10.46 ? 192 TRP A NE1 1 
ATOM   1569 C  CE2 . TRP A 1 191 ? -10.848 -6.917  -9.693  1.00 10.09 ? 192 TRP A CE2 1 
ATOM   1570 C  CE3 . TRP A 1 191 ? -8.938  -6.070  -8.402  1.00 9.77  ? 192 TRP A CE3 1 
ATOM   1571 C  CZ2 . TRP A 1 191 ? -10.261 -8.184  -9.773  1.00 10.88 ? 192 TRP A CZ2 1 
ATOM   1572 C  CZ3 . TRP A 1 191 ? -8.378  -7.321  -8.491  1.00 9.94  ? 192 TRP A CZ3 1 
ATOM   1573 C  CH2 . TRP A 1 191 ? -9.036  -8.352  -9.151  1.00 11.56 ? 192 TRP A CH2 1 
ATOM   1574 N  N   . THR A 1 192 ? -11.563 -0.292  -8.337  1.00 7.60  ? 193 THR A N   1 
ATOM   1575 C  CA  . THR A 1 192 ? -11.501 0.945   -7.543  1.00 8.39  ? 193 THR A CA  1 
ATOM   1576 C  C   . THR A 1 192 ? -12.713 1.131   -6.653  1.00 7.77  ? 193 THR A C   1 
ATOM   1577 O  O   . THR A 1 192 ? -13.849 0.701   -7.060  1.00 8.37  ? 193 THR A O   1 
ATOM   1578 C  CB  . THR A 1 192 ? -11.296 2.156   -8.446  1.00 8.41  ? 193 THR A CB  1 
ATOM   1579 O  OG1 . THR A 1 192 ? -11.145 3.375   -7.678  1.00 8.63  ? 193 THR A OG1 1 
ATOM   1580 C  CG2 . THR A 1 192 ? -12.388 2.382   -9.459  1.00 10.28 ? 193 THR A CG2 1 
ATOM   1581 N  N   . TYR A 1 193 ? -12.553 1.702   -5.462  1.00 8.33  ? 194 TYR A N   1 
ATOM   1582 C  CA  . TYR A 1 193 ? -13.677 1.953   -4.585  1.00 7.77  ? 194 TYR A CA  1 
ATOM   1583 C  C   . TYR A 1 193 ? -13.221 2.992   -3.585  1.00 7.00  ? 194 TYR A C   1 
ATOM   1584 O  O   . TYR A 1 193 ? -12.009 3.238   -3.382  1.00 8.07  ? 194 TYR A O   1 
ATOM   1585 C  CB  . TYR A 1 193 ? -14.125 0.661   -3.828  1.00 9.16  ? 194 TYR A CB  1 
ATOM   1586 C  CG  . TYR A 1 193 ? -13.177 0.199   -2.770  1.00 8.16  ? 194 TYR A CG  1 
ATOM   1587 C  CD1 . TYR A 1 193 ? -12.023 -0.522  -3.065  1.00 7.82  ? 194 TYR A CD1 1 
ATOM   1588 C  CD2 . TYR A 1 193 ? -13.440 0.545   -1.448  1.00 8.91  ? 194 TYR A CD2 1 
ATOM   1589 C  CE1 . TYR A 1 193 ? -11.106 -0.850  -2.077  1.00 7.54  ? 194 TYR A CE1 1 
ATOM   1590 C  CE2 . TYR A 1 193 ? -12.567 0.216   -0.414  1.00 9.94  ? 194 TYR A CE2 1 
ATOM   1591 C  CZ  . TYR A 1 193 ? -11.372 -0.469  -0.753  1.00 7.44  ? 194 TYR A CZ  1 
ATOM   1592 O  OH  . TYR A 1 193 ? -10.497 -0.760  0.279   1.00 8.65  ? 194 TYR A OH  1 
ATOM   1593 N  N   . PRO A 1 194 ? -14.179 3.681   -2.913  1.00 8.60  ? 195 PRO A N   1 
ATOM   1594 C  CA  . PRO A 1 194 ? -13.835 4.677   -1.915  1.00 8.50  ? 195 PRO A CA  1 
ATOM   1595 C  C   . PRO A 1 194 ? -13.613 4.039   -0.539  1.00 7.97  ? 195 PRO A C   1 
ATOM   1596 O  O   . PRO A 1 194 ? -14.475 3.262   -0.094  1.00 9.40  ? 195 PRO A O   1 
ATOM   1597 C  CB  . PRO A 1 194 ? -15.090 5.610   -1.881  1.00 11.21 ? 195 PRO A CB  1 
ATOM   1598 C  CG  . PRO A 1 194 ? -16.190 4.676   -2.277  1.00 11.25 ? 195 PRO A CG  1 
ATOM   1599 C  CD  . PRO A 1 194 ? -15.599 3.682   -3.232  1.00 10.29 ? 195 PRO A CD  1 
ATOM   1600 N  N   . GLY A 1 195 ? -12.509 4.403   0.106   1.00 7.84  ? 196 GLY A N   1 
ATOM   1601 C  CA  . GLY A 1 195 ? -12.204 3.791   1.406   1.00 8.92  ? 196 GLY A CA  1 
ATOM   1602 C  C   . GLY A 1 195 ? -11.387 4.650   2.289   1.00 8.80  ? 196 GLY A C   1 
ATOM   1603 O  O   . GLY A 1 195 ? -11.536 5.885   2.339   1.00 8.76  ? 196 GLY A O   1 
ATOM   1604 N  N   . SER A 1 196 ? -10.491 3.993   3.028   1.00 8.20  ? 197 SER A N   1 
ATOM   1605 C  CA  . SER A 1 196 ? -9.816  4.650   4.160   1.00 8.04  ? 197 SER A CA  1 
ATOM   1606 C  C   . SER A 1 196 ? -8.379  4.237   4.255   1.00 8.59  ? 197 SER A C   1 
ATOM   1607 O  O   . SER A 1 196 ? -7.923  3.265   3.591   1.00 8.38  ? 197 SER A O   1 
ATOM   1608 C  CB  . SER A 1 196 ? -10.491 4.214   5.504   1.00 9.81  ? 197 SER A CB  1 
ATOM   1609 O  OG  . SER A 1 196 ? -10.153 2.871   5.877   1.00 9.50  ? 197 SER A OG  1 
ATOM   1610 N  N   . LEU A 1 197 ? -7.578  4.886   5.093   1.00 7.66  ? 198 LEU A N   1 
ATOM   1611 C  CA  . LEU A 1 197 ? -6.312  4.328   5.557   1.00 8.74  ? 198 LEU A CA  1 
ATOM   1612 C  C   . LEU A 1 197 ? -6.612  3.000   6.191   1.00 8.40  ? 198 LEU A C   1 
ATOM   1613 O  O   . LEU A 1 197 ? -7.662  2.847   6.927   1.00 8.95  ? 198 LEU A O   1 
ATOM   1614 C  CB  . LEU A 1 197 ? -5.644  5.254   6.572   1.00 10.78 ? 198 LEU A CB  1 
ATOM   1615 C  CG  . LEU A 1 197 ? -5.346  6.672   6.112   1.00 12.00 ? 198 LEU A CG  1 
ATOM   1616 C  CD1 . LEU A 1 197 ? -4.749  7.495   7.283   1.00 14.85 ? 198 LEU A CD1 1 
ATOM   1617 C  CD2 . LEU A 1 197 ? -4.411  6.708   4.920   1.00 11.55 ? 198 LEU A CD2 1 
ATOM   1618 N  N   . THR A 1 198 ? -5.714  2.025   6.098   1.00 9.09  ? 199 THR A N   1 
ATOM   1619 C  CA  . THR A 1 198 ? -5.896  0.743   6.759   1.00 8.39  ? 199 THR A CA  1 
ATOM   1620 C  C   . THR A 1 198 ? -5.174  0.686   8.102   1.00 9.26  ? 199 THR A C   1 
ATOM   1621 O  O   . THR A 1 198 ? -5.261  -0.383  8.729   1.00 10.18 ? 199 THR A O   1 
ATOM   1622 C  CB  . THR A 1 198 ? -5.458  -0.394  5.834   1.00 8.85  ? 199 THR A CB  1 
ATOM   1623 O  OG1 . THR A 1 198 ? -4.018  -0.336  5.789   1.00 8.66  ? 199 THR A OG1 1 
ATOM   1624 C  CG2 . THR A 1 198 ? -6.114  -0.384  4.504   1.00 9.67  ? 199 THR A CG2 1 
ATOM   1625 N  N   . THR A 1 199 ? -4.469  1.759   8.508   1.00 11.13 ? 200 THR A N   1 
ATOM   1626 C  CA  . THR A 1 199 ? -3.900  1.861   9.826   1.00 11.59 ? 200 THR A CA  1 
ATOM   1627 C  C   . THR A 1 199 ? -4.514  3.078   10.527  1.00 13.30 ? 200 THR A C   1 
ATOM   1628 O  O   . THR A 1 199 ? -4.887  4.027   9.872   1.00 11.94 ? 200 THR A O   1 
ATOM   1629 C  CB  . THR A 1 199 ? -2.376  2.077   9.736   1.00 13.65 ? 200 THR A CB  1 
ATOM   1630 O  OG1 . THR A 1 199 ? -2.124  3.161   8.780   1.00 17.94 ? 200 THR A OG1 1 
ATOM   1631 C  CG2 . THR A 1 199 ? -1.669  0.841   9.178   1.00 13.19 ? 200 THR A CG2 1 
ATOM   1632 N  N   . PRO A 1 200 ? -4.568  3.041   11.896  1.00 12.83 ? 201 PRO A N   1 
ATOM   1633 C  CA  . PRO A 1 200 ? -4.845  4.295   12.629  1.00 13.23 ? 201 PRO A CA  1 
ATOM   1634 C  C   . PRO A 1 200 ? -4.051  5.456   12.009  1.00 13.37 ? 201 PRO A C   1 
ATOM   1635 O  O   . PRO A 1 200 ? -2.840  5.326   11.723  1.00 14.69 ? 201 PRO A O   1 
ATOM   1636 C  CB  . PRO A 1 200 ? -4.363  3.913   13.995  1.00 14.48 ? 201 PRO A CB  1 
ATOM   1637 C  CG  . PRO A 1 200 ? -4.695  2.427   14.124  1.00 15.33 ? 201 PRO A CG  1 
ATOM   1638 C  CD  . PRO A 1 200 ? -4.243  1.905   12.818  1.00 13.26 ? 201 PRO A CD  1 
ATOM   1639 N  N   . PRO A 1 201 ? -4.687  6.628   11.796  1.00 13.55 ? 202 PRO A N   1 
ATOM   1640 C  CA  . PRO A 1 201 ? -6.030  7.017   12.284  1.00 13.37 ? 202 PRO A CA  1 
ATOM   1641 C  C   . PRO A 1 201 ? -7.256  6.650   11.414  1.00 12.22 ? 202 PRO A C   1 
ATOM   1642 O  O   . PRO A 1 201 ? -8.383  7.020   11.722  1.00 12.86 ? 202 PRO A O   1 
ATOM   1643 C  CB  . PRO A 1 201 ? -5.902  8.511   12.402  1.00 16.12 ? 202 PRO A CB  1 
ATOM   1644 C  CG  . PRO A 1 201 ? -4.990  8.883   11.233  1.00 17.85 ? 202 PRO A CG  1 
ATOM   1645 C  CD  . PRO A 1 201 ? -3.929  7.771   11.257  1.00 15.79 ? 202 PRO A CD  1 
ATOM   1646 N  N   . LEU A 1 202 ? -7.042  5.755   10.398  1.00 11.64 ? 203 LEU A N   1 
ATOM   1647 C  CA  . LEU A 1 202 ? -8.168  5.126   9.695   1.00 11.33 ? 203 LEU A CA  1 
ATOM   1648 C  C   . LEU A 1 202 ? -9.068  6.161   8.935   1.00 9.86  ? 203 LEU A C   1 
ATOM   1649 O  O   . LEU A 1 202 ? -10.230 5.890   8.663   1.00 11.65 ? 203 LEU A O   1 
ATOM   1650 C  CB  . LEU A 1 202 ? -9.000  4.213   10.627  1.00 10.92 ? 203 LEU A CB  1 
ATOM   1651 C  CG  . LEU A 1 202 ? -8.215  3.031   11.261  1.00 11.47 ? 203 LEU A CG  1 
ATOM   1652 C  CD1 . LEU A 1 202 ? -9.109  2.423   12.333  1.00 13.74 ? 203 LEU A CD1 1 
ATOM   1653 C  CD2 . LEU A 1 202 ? -7.746  1.998   10.235  1.00 11.38 ? 203 LEU A CD2 1 
ATOM   1654 N  N   . LEU A 1 203 ? -8.407  7.296   8.561   1.00 11.34 ? 204 LEU A N   1 
ATOM   1655 C  CA  . LEU A 1 203 ? -9.189  8.378   7.980   1.00 12.28 ? 204 LEU A CA  1 
ATOM   1656 C  C   . LEU A 1 203 ? -9.837  7.950   6.663   1.00 10.95 ? 204 LEU A C   1 
ATOM   1657 O  O   . LEU A 1 203 ? -9.186  7.223   5.851   1.00 10.58 ? 204 LEU A O   1 
ATOM   1658 C  CB  . LEU A 1 203 ? -8.262  9.597   7.770   1.00 15.12 ? 204 LEU A CB  1 
ATOM   1659 C  CG  . LEU A 1 203 ? -7.746  10.180  9.139   1.00 15.63 ? 204 LEU A CG  1 
ATOM   1660 C  CD1 . LEU A 1 203 ? -6.609  11.132  8.794   1.00 19.95 ? 204 LEU A CD1 1 
ATOM   1661 C  CD2 . LEU A 1 203 ? -8.888  10.851  9.986   1.00 19.75 ? 204 LEU A CD2 1 
ATOM   1662 N  N   . GLU A 1 204 ? -11.076 8.372   6.427   1.00 12.29 ? 205 GLU A N   1 
ATOM   1663 C  CA  . GLU A 1 204 ? -11.810 8.017   5.223   1.00 11.02 ? 205 GLU A CA  1 
ATOM   1664 C  C   . GLU A 1 204 ? -11.512 9.028   4.102   1.00 12.45 ? 205 GLU A C   1 
ATOM   1665 O  O   . GLU A 1 204 ? -12.417 9.761   3.661   1.00 14.07 ? 205 GLU A O   1 
ATOM   1666 C  CB  . GLU A 1 204 ? -13.281 7.889   5.582   1.00 14.04 ? 205 GLU A CB  1 
ATOM   1667 C  CG  . GLU A 1 204 ? -13.435 6.675   6.522   1.00 13.69 ? 205 GLU A CG  1 
ATOM   1668 C  CD  . GLU A 1 204 ? -14.867 6.366   6.915   1.00 13.03 ? 205 GLU A CD  1 
ATOM   1669 O  OE1 . GLU A 1 204 ? -15.729 7.287   6.904   1.00 16.86 ? 205 GLU A OE1 1 
ATOM   1670 O  OE2 . GLU A 1 204 ? -15.229 5.189   7.197   1.00 12.50 ? 205 GLU A OE2 1 
ATOM   1671 N  N   . CYS A 1 205 ? -10.281 8.947   3.603   1.00 10.14 ? 206 CYS A N   1 
ATOM   1672 C  CA  . CYS A 1 205 ? -9.761  9.934   2.684   1.00 9.97  ? 206 CYS A CA  1 
ATOM   1673 C  C   . CYS A 1 205 ? -9.196  9.327   1.441   1.00 9.11  ? 206 CYS A C   1 
ATOM   1674 O  O   . CYS A 1 205 ? -8.486  10.021  0.694   1.00 10.07 ? 206 CYS A O   1 
ATOM   1675 C  CB  . CYS A 1 205 ? -8.643  10.743  3.358   1.00 10.41 ? 206 CYS A CB  1 
ATOM   1676 S  SG  . CYS A 1 205 ? -7.251  9.796   3.966   1.00 12.12 ? 206 CYS A SG  1 
ATOM   1677 N  N   . VAL A 1 206 ? -9.413  8.014   1.179   1.00 9.09  ? 207 VAL A N   1 
ATOM   1678 C  CA  . VAL A 1 206 ? -8.648  7.301   0.111   1.00 8.18  ? 207 VAL A CA  1 
ATOM   1679 C  C   . VAL A 1 206 ? -9.583  6.902   -1.017  1.00 8.19  ? 207 VAL A C   1 
ATOM   1680 O  O   . VAL A 1 206 ? -10.571 6.221   -0.822  1.00 9.70  ? 207 VAL A O   1 
ATOM   1681 C  CB  . VAL A 1 206 ? -7.991  6.026   0.675   1.00 8.92  ? 207 VAL A CB  1 
ATOM   1682 C  CG1 . VAL A 1 206 ? -7.161  5.332   -0.446  1.00 9.02  ? 207 VAL A CG1 1 
ATOM   1683 C  CG2 . VAL A 1 206 ? -7.041  6.408   1.816   1.00 10.49 ? 207 VAL A CG2 1 
ATOM   1684 N  N   . THR A 1 207 ? -9.150  7.180   -2.264  1.00 8.10  ? 208 THR A N   1 
ATOM   1685 C  CA  . THR A 1 207 ? -9.629  6.431   -3.413  1.00 8.74  ? 208 THR A CA  1 
ATOM   1686 C  C   . THR A 1 207 ? -8.646  5.282   -3.681  1.00 7.77  ? 208 THR A C   1 
ATOM   1687 O  O   . THR A 1 207 ? -7.474  5.509   -3.943  1.00 8.15  ? 208 THR A O   1 
ATOM   1688 C  CB  . THR A 1 207 ? -9.644  7.320   -4.698  1.00 8.73  ? 208 THR A CB  1 
ATOM   1689 O  OG1 . THR A 1 207 ? -10.527 8.424   -4.447  1.00 9.45  ? 208 THR A OG1 1 
ATOM   1690 C  CG2 . THR A 1 207 ? -10.192 6.489   -5.893  1.00 10.29 ? 208 THR A CG2 1 
ATOM   1691 N  N   . TRP A 1 208 ? -9.172  4.058   -3.459  1.00 7.67  ? 209 TRP A N   1 
ATOM   1692 C  CA  . TRP A 1 208 ? -8.352  2.857   -3.640  1.00 7.38  ? 209 TRP A CA  1 
ATOM   1693 C  C   . TRP A 1 208 ? -8.335  2.440   -5.072  1.00 7.20  ? 209 TRP A C   1 
ATOM   1694 O  O   . TRP A 1 208 ? -9.409  2.392   -5.723  1.00 7.71  ? 209 TRP A O   1 
ATOM   1695 C  CB  . TRP A 1 208 ? -8.856  1.704   -2.771  1.00 7.50  ? 209 TRP A CB  1 
ATOM   1696 C  CG  . TRP A 1 208 ? -8.375  1.805   -1.393  1.00 6.43  ? 209 TRP A CG  1 
ATOM   1697 C  CD1 . TRP A 1 208 ? -8.975  2.386   -0.285  1.00 8.26  ? 209 TRP A CD1 1 
ATOM   1698 C  CD2 . TRP A 1 208 ? -7.070  1.400   -0.972  1.00 7.42  ? 209 TRP A CD2 1 
ATOM   1699 N  NE1 . TRP A 1 208 ? -8.131  2.375   0.772   1.00 8.81  ? 209 TRP A NE1 1 
ATOM   1700 C  CE2 . TRP A 1 208 ? -6.945  1.777   0.442   1.00 8.21  ? 209 TRP A CE2 1 
ATOM   1701 C  CE3 . TRP A 1 208 ? -6.001  0.773   -1.597  1.00 7.34  ? 209 TRP A CE3 1 
ATOM   1702 C  CZ2 . TRP A 1 208 ? -5.782  1.537   1.149   1.00 8.12  ? 209 TRP A CZ2 1 
ATOM   1703 C  CZ3 . TRP A 1 208 ? -4.874  0.519   -0.901  1.00 8.66  ? 209 TRP A CZ3 1 
ATOM   1704 C  CH2 . TRP A 1 208 ? -4.764  0.852   0.462   1.00 8.49  ? 209 TRP A CH2 1 
ATOM   1705 N  N   . ILE A 1 209 ? -7.146  2.107   -5.601  1.00 7.35  ? 210 ILE A N   1 
ATOM   1706 C  CA  . ILE A 1 209 ? -6.996  1.546   -6.956  1.00 7.54  ? 210 ILE A CA  1 
ATOM   1707 C  C   . ILE A 1 209 ? -6.160  0.298   -6.770  1.00 7.02  ? 210 ILE A C   1 
ATOM   1708 O  O   . ILE A 1 209 ? -5.011  0.390   -6.379  1.00 7.84  ? 210 ILE A O   1 
ATOM   1709 C  CB  . ILE A 1 209 ? -6.327  2.561   -7.890  1.00 8.36  ? 210 ILE A CB  1 
ATOM   1710 C  CG1 . ILE A 1 209 ? -7.155  3.828   -7.961  1.00 10.10 ? 210 ILE A CG1 1 
ATOM   1711 C  CG2 . ILE A 1 209 ? -6.018  1.977   -9.304  1.00 9.96  ? 210 ILE A CG2 1 
ATOM   1712 C  CD1 . ILE A 1 209 ? -6.433  4.989   -8.614  1.00 12.55 ? 210 ILE A CD1 1 
ATOM   1713 N  N   . VAL A 1 210 ? -6.777  -0.866  -6.955  1.00 6.79  ? 211 VAL A N   1 
ATOM   1714 C  CA  . VAL A 1 210 ? -6.118  -2.164  -6.687  1.00 7.06  ? 211 VAL A CA  1 
ATOM   1715 C  C   . VAL A 1 210 ? -5.892  -2.850  -8.040  1.00 6.48  ? 211 VAL A C   1 
ATOM   1716 O  O   . VAL A 1 210 ? -6.863  -3.121  -8.736  1.00 8.44  ? 211 VAL A O   1 
ATOM   1717 C  CB  . VAL A 1 210 ? -6.988  -3.045  -5.704  1.00 7.84  ? 211 VAL A CB  1 
ATOM   1718 C  CG1 . VAL A 1 210 ? -6.238  -4.390  -5.468  1.00 8.27  ? 211 VAL A CG1 1 
ATOM   1719 C  CG2 . VAL A 1 210 ? -7.144  -2.242  -4.363  1.00 8.97  ? 211 VAL A CG2 1 
ATOM   1720 N  N   . LEU A 1 211 ? -4.645  -3.133  -8.369  1.00 7.61  ? 212 LEU A N   1 
ATOM   1721 C  CA  . LEU A 1 211 ? -4.381  -3.769  -9.651  1.00 8.85  ? 212 LEU A CA  1 
ATOM   1722 C  C   . LEU A 1 211 ? -4.782  -5.246  -9.613  1.00 9.64  ? 212 LEU A C   1 
ATOM   1723 O  O   . LEU A 1 211 ? -4.554  -5.946  -8.641  1.00 9.15  ? 212 LEU A O   1 
ATOM   1724 C  CB  . LEU A 1 211 ? -2.868  -3.626  -10.001 1.00 8.42  ? 212 LEU A CB  1 
ATOM   1725 C  CG  . LEU A 1 211 ? -2.366  -2.188  -10.144 1.00 9.41  ? 212 LEU A CG  1 
ATOM   1726 C  CD1 . LEU A 1 211 ? -0.916  -2.254  -10.715 1.00 10.63 ? 212 LEU A CD1 1 
ATOM   1727 C  CD2 . LEU A 1 211 ? -3.278  -1.360  -11.048 1.00 10.65 ? 212 LEU A CD2 1 
ATOM   1728 N  N   . LYS A 1 212 ? -5.368  -5.682  -10.733 1.00 9.24  ? 213 LYS A N   1 
ATOM   1729 C  CA  . LYS A 1 212 ? -5.761  -7.090  -10.818 1.00 10.26 ? 213 LYS A CA  1 
ATOM   1730 C  C   . LYS A 1 212 ? -4.527  -8.033  -10.893 1.00 9.30  ? 213 LYS A C   1 
ATOM   1731 O  O   . LYS A 1 212 ? -4.578  -9.096  -10.333 1.00 11.46 ? 213 LYS A O   1 
ATOM   1732 C  CB  . LYS A 1 212 ? -6.612  -7.289  -12.039 1.00 13.60 ? 213 LYS A CB  1 
ATOM   1733 C  CG  . LYS A 1 212 ? -7.009  -8.741  -12.400 1.00 18.35 ? 213 LYS A CG  1 
ATOM   1734 C  CD  . LYS A 1 212 ? -7.464  -8.772  -13.880 1.00 28.54 ? 213 LYS A CD  1 
ATOM   1735 C  CE  . LYS A 1 212 ? -6.663  -7.894  -14.802 1.00 36.26 ? 213 LYS A CE  1 
ATOM   1736 N  NZ  . LYS A 1 212 ? -5.193  -8.110  -14.696 1.00 24.69 ? 213 LYS A NZ  1 
ATOM   1737 N  N   . GLU A 1 213 ? -3.448  -7.655  -11.570 1.00 8.84  ? 214 GLU A N   1 
ATOM   1738 C  CA  . GLU A 1 213 ? -2.302  -8.542  -11.799 1.00 9.42  ? 214 GLU A CA  1 
ATOM   1739 C  C   . GLU A 1 213 ? -1.358  -8.450  -10.636 1.00 9.28  ? 214 GLU A C   1 
ATOM   1740 O  O   . GLU A 1 213 ? -0.855  -7.356  -10.385 1.00 9.55  ? 214 GLU A O   1 
ATOM   1741 C  CB  . GLU A 1 213 ? -1.628  -8.173  -13.098 1.00 11.23 ? 214 GLU A CB  1 
ATOM   1742 C  CG  . GLU A 1 213 ? -0.517  -9.159  -13.440 1.00 15.30 ? 214 GLU A CG  1 
ATOM   1743 C  CD  . GLU A 1 213 ? 0.324   -8.738  -14.638 1.00 15.99 ? 214 GLU A CD  1 
ATOM   1744 O  OE1 . GLU A 1 213 ? -0.229  -8.092  -15.551 1.00 15.19 ? 214 GLU A OE1 1 
ATOM   1745 O  OE2 . GLU A 1 213 ? 1.533   -9.065  -14.681 1.00 30.24 ? 214 GLU A OE2 1 
ATOM   1746 N  N   . PRO A 1 214 ? -1.108  -9.543  -9.909  1.00 9.27  ? 215 PRO A N   1 
ATOM   1747 C  CA  . PRO A 1 214 ? -0.083  -9.494  -8.866  1.00 10.16 ? 215 PRO A CA  1 
ATOM   1748 C  C   . PRO A 1 214 ? 1.335   -9.428  -9.452  1.00 10.41 ? 215 PRO A C   1 
ATOM   1749 O  O   . PRO A 1 214 ? 1.537   -9.836  -10.639 1.00 12.50 ? 215 PRO A O   1 
ATOM   1750 C  CB  . PRO A 1 214 ? -0.223  -10.819 -8.156  1.00 10.24 ? 215 PRO A CB  1 
ATOM   1751 C  CG  . PRO A 1 214 ? -0.787  -11.733 -9.220  1.00 17.08 ? 215 PRO A CG  1 
ATOM   1752 C  CD  . PRO A 1 214 ? -1.654  -10.905 -10.091 1.00 11.56 ? 215 PRO A CD  1 
ATOM   1753 N  N   . ILE A 1 215 ? 2.284   -8.981  -8.633  1.00 9.24  ? 216 ILE A N   1 
ATOM   1754 C  CA  . ILE A 1 215 ? 3.689   -9.187  -9.010  1.00 10.60 ? 216 ILE A CA  1 
ATOM   1755 C  C   . ILE A 1 215 ? 4.113   -10.473 -8.317  1.00 10.41 ? 216 ILE A C   1 
ATOM   1756 O  O   . ILE A 1 215 ? 3.590   -10.866 -7.264  1.00 11.42 ? 216 ILE A O   1 
ATOM   1757 C  CB  . ILE A 1 215 ? 4.560   -8.001  -8.622  1.00 11.29 ? 216 ILE A CB  1 
ATOM   1758 C  CG1 . ILE A 1 215 ? 4.521   -7.710  -7.093  1.00 11.13 ? 216 ILE A CG1 1 
ATOM   1759 C  CG2 . ILE A 1 215 ? 4.198   -6.776  -9.534  1.00 12.92 ? 216 ILE A CG2 1 
ATOM   1760 C  CD1 . ILE A 1 215 ? 5.690   -6.723  -6.746  1.00 12.04 ? 216 ILE A CD1 1 
ATOM   1761 N  N   . SER A 1 216 ? 5.121   -11.146 -8.889  1.00 11.34 ? 217 SER A N   1 
ATOM   1762 C  CA  . SER A 1 216 ? 5.776   -12.314 -8.250  1.00 11.75 ? 217 SER A CA  1 
ATOM   1763 C  C   . SER A 1 216 ? 7.015   -11.855 -7.551  1.00 9.88  ? 217 SER A C   1 
ATOM   1764 O  O   . SER A 1 216 ? 7.823   -11.125 -8.169  1.00 13.63 ? 217 SER A O   1 
ATOM   1765 C  CB  . SER A 1 216 ? 6.194   -13.381 -9.294  1.00 17.46 ? 217 SER A CB  1 
ATOM   1766 O  OG  . SER A 1 216 ? 5.022   -13.961 -9.778  1.00 20.62 ? 217 SER A OG  1 
ATOM   1767 N  N   . VAL A 1 217 ? 7.223   -12.304 -6.340  1.00 10.76 ? 218 VAL A N   1 
ATOM   1768 C  CA  . VAL A 1 217 ? 8.449   -12.104 -5.648  1.00 11.05 ? 218 VAL A CA  1 
ATOM   1769 C  C   . VAL A 1 217 ? 8.951   -13.488 -5.244  1.00 10.87 ? 218 VAL A C   1 
ATOM   1770 O  O   . VAL A 1 217 ? 8.165   -14.426 -5.090  1.00 11.78 ? 218 VAL A O   1 
ATOM   1771 C  CB  . VAL A 1 217 ? 8.265   -11.188 -4.414  1.00 11.87 ? 218 VAL A CB  1 
ATOM   1772 C  CG1 . VAL A 1 217 ? 7.725   -9.806  -4.856  1.00 12.76 ? 218 VAL A CG1 1 
ATOM   1773 C  CG2 . VAL A 1 217 ? 7.355   -11.837 -3.381  1.00 13.88 ? 218 VAL A CG2 1 
ATOM   1774 N  N   . SER A 1 218 ? 10.239  -13.639 -4.919  1.00 10.99 ? 219 SER A N   1 
ATOM   1775 C  CA  . SER A 1 218 ? 10.708  -14.971 -4.519  1.00 12.58 ? 219 SER A CA  1 
ATOM   1776 C  C   . SER A 1 218 ? 10.487  -15.216 -3.043  1.00 11.78 ? 219 SER A C   1 
ATOM   1777 O  O   . SER A 1 218 ? 10.305  -14.320 -2.186  1.00 11.86 ? 219 SER A O   1 
ATOM   1778 C  CB  . SER A 1 218 ? 12.207  -15.142 -4.872  1.00 13.41 ? 219 SER A CB  1 
ATOM   1779 O  OG  . SER A 1 218 ? 12.932  -14.290 -3.977  1.00 14.37 ? 219 SER A OG  1 
ATOM   1780 N  N   A SER A 1 219 ? 10.517  -16.508 -2.703  0.50 12.46 ? 220 SER A N   1 
ATOM   1781 N  N   B SER A 1 219 ? 10.529  -16.491 -2.646  0.50 12.08 ? 220 SER A N   1 
ATOM   1782 C  CA  A SER A 1 219 ? 10.414  -16.917 -1.330  0.50 12.18 ? 220 SER A CA  1 
ATOM   1783 C  CA  B SER A 1 219 ? 10.400  -16.860 -1.246  0.50 11.94 ? 220 SER A CA  1 
ATOM   1784 C  C   A SER A 1 219 ? 11.473  -16.203 -0.479  0.50 13.54 ? 220 SER A C   1 
ATOM   1785 C  C   B SER A 1 219 ? 11.526  -16.230 -0.396  0.50 13.70 ? 220 SER A C   1 
ATOM   1786 O  O   A SER A 1 219 ? 11.146  -15.698 0.585   0.50 14.08 ? 220 SER A O   1 
ATOM   1787 O  O   B SER A 1 219 ? 11.321  -15.825 0.750   0.50 14.77 ? 220 SER A O   1 
ATOM   1788 C  CB  A SER A 1 219 ? 10.443  -18.462 -1.211  0.50 17.15 ? 220 SER A CB  1 
ATOM   1789 C  CB  B SER A 1 219 ? 10.353  -18.393 -1.149  0.50 15.27 ? 220 SER A CB  1 
ATOM   1790 O  OG  A SER A 1 219 ? 11.678  -19.036 -1.606  0.50 15.86 ? 220 SER A OG  1 
ATOM   1791 O  OG  B SER A 1 219 ? 10.197  -18.822 0.178   0.50 17.13 ? 220 SER A OG  1 
ATOM   1792 N  N   . GLU A 1 220 ? 12.717  -16.103 -0.989  1.00 13.45 ? 221 GLU A N   1 
ATOM   1793 C  CA  . GLU A 1 220 ? 13.833  -15.473 -0.241  1.00 15.41 ? 221 GLU A CA  1 
ATOM   1794 C  C   . GLU A 1 220 ? 13.562  -13.965 -0.013  1.00 14.53 ? 221 GLU A C   1 
ATOM   1795 O  O   . GLU A 1 220 ? 13.907  -13.452 1.045   1.00 15.17 ? 221 GLU A O   1 
ATOM   1796 C  CB  . GLU A 1 220 ? 15.175  -15.640 -0.944  1.00 17.21 ? 221 GLU A CB  1 
ATOM   1797 C  CG  . GLU A 1 220 ? 15.636  -17.149 -0.950  1.00 21.13 ? 221 GLU A CG  1 
ATOM   1798 C  CD  . GLU A 1 220 ? 15.157  -17.906 -2.173  1.00 22.47 ? 221 GLU A CD  1 
ATOM   1799 O  OE1 . GLU A 1 220 ? 14.298  -17.372 -2.905  1.00 20.78 ? 221 GLU A OE1 1 
ATOM   1800 O  OE2 . GLU A 1 220 ? 15.639  -19.035 -2.402  1.00 38.95 ? 221 GLU A OE2 1 
ATOM   1801 N  N   . GLN A 1 221 ? 12.964  -13.316 -1.002  1.00 12.28 ? 222 GLN A N   1 
ATOM   1802 C  CA  . GLN A 1 221 ? 12.655  -11.895 -0.826  1.00 12.49 ? 222 GLN A CA  1 
ATOM   1803 C  C   . GLN A 1 221 ? 11.652  -11.685 0.325   1.00 13.73 ? 222 GLN A C   1 
ATOM   1804 O  O   . GLN A 1 221 ? 11.859  -10.873 1.218   1.00 12.71 ? 222 GLN A O   1 
ATOM   1805 C  CB  . GLN A 1 221 ? 12.103  -11.407 -2.107  1.00 11.98 ? 222 GLN A CB  1 
ATOM   1806 C  CG  . GLN A 1 221 ? 13.237  -11.201 -3.152  1.00 12.46 ? 222 GLN A CG  1 
ATOM   1807 C  CD  . GLN A 1 221 ? 12.818  -10.628 -4.474  1.00 11.01 ? 222 GLN A CD  1 
ATOM   1808 O  OE1 . GLN A 1 221 ? 11.741  -10.997 -4.986  1.00 12.20 ? 222 GLN A OE1 1 
ATOM   1809 N  NE2 . GLN A 1 221 ? 13.600  -9.722  -5.065  1.00 11.75 ? 222 GLN A NE2 1 
ATOM   1810 N  N   . VAL A 1 222 ? 10.586  -12.472 0.374   1.00 12.70 ? 223 VAL A N   1 
ATOM   1811 C  CA  . VAL A 1 222 ? 9.588   -12.260 1.431   1.00 13.06 ? 223 VAL A CA  1 
ATOM   1812 C  C   . VAL A 1 222 ? 10.132  -12.720 2.808   1.00 13.76 ? 223 VAL A C   1 
ATOM   1813 O  O   . VAL A 1 222 ? 9.822   -12.134 3.832   1.00 14.17 ? 223 VAL A O   1 
ATOM   1814 C  CB  . VAL A 1 222 ? 8.214   -12.818 1.008   1.00 16.09 ? 223 VAL A CB  1 
ATOM   1815 C  CG1 . VAL A 1 222 ? 8.233   -14.322 0.926   1.00 18.81 ? 223 VAL A CG1 1 
ATOM   1816 C  CG2 . VAL A 1 222 ? 7.100   -12.237 1.906   1.00 21.05 ? 223 VAL A CG2 1 
ATOM   1817 N  N   . LEU A 1 223 ? 11.020  -13.750 2.809   1.00 14.91 ? 224 LEU A N   1 
ATOM   1818 C  CA  . LEU A 1 223 ? 11.654  -14.169 4.064   1.00 16.42 ? 224 LEU A CA  1 
ATOM   1819 C  C   . LEU A 1 223 ? 12.472  -13.051 4.656   1.00 15.44 ? 224 LEU A C   1 
ATOM   1820 O  O   . LEU A 1 223 ? 12.479  -12.912 5.882   1.00 16.88 ? 224 LEU A O   1 
ATOM   1821 C  CB  . LEU A 1 223 ? 12.512  -15.431 3.859   1.00 20.03 ? 224 LEU A CB  1 
ATOM   1822 C  CG  . LEU A 1 223 ? 11.657  -16.731 3.720   1.00 20.77 ? 224 LEU A CG  1 
ATOM   1823 C  CD1 . LEU A 1 223 ? 12.522  -17.891 3.146   1.00 29.15 ? 224 LEU A CD1 1 
ATOM   1824 C  CD2 . LEU A 1 223 ? 11.020  -17.186 5.044   1.00 26.46 ? 224 LEU A CD2 1 
ATOM   1825 N  N   . LYS A 1 224 ? 13.025  -12.185 3.821   1.00 14.88 ? 225 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 224 ? 13.743  -11.069 4.368   1.00 14.34 ? 225 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 224 ? 12.822  -10.001 4.979   1.00 13.70 ? 225 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 224 ? 13.144  -9.399  6.010   1.00 13.39 ? 225 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 224 ? 14.757  -10.545 3.322   1.00 15.91 ? 225 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 224 ? 15.914  -11.605 3.155   1.00 19.27 ? 225 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 224 ? 16.979  -11.275 2.163   1.00 22.83 ? 225 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 224 ? 18.093  -12.368 2.073   1.00 28.29 ? 225 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 224 ? 19.211  -12.077 1.138   1.00 27.44 ? 225 LYS A NZ  1 
ATOM   1834 N  N   . PHE A 1 225 ? 11.637  -9.788  4.431   1.00 11.37 ? 226 PHE A N   1 
ATOM   1835 C  CA  . PHE A 1 225 ? 10.672  -8.926  5.101   1.00 10.99 ? 226 PHE A CA  1 
ATOM   1836 C  C   . PHE A 1 225 ? 10.373  -9.455  6.512   1.00 12.34 ? 226 PHE A C   1 
ATOM   1837 O  O   . PHE A 1 225 ? 10.251  -8.671  7.456   1.00 12.67 ? 226 PHE A O   1 
ATOM   1838 C  CB  . PHE A 1 225 ? 9.283   -8.926  4.391   1.00 11.83 ? 226 PHE A CB  1 
ATOM   1839 C  CG  . PHE A 1 225 ? 9.212   -8.157  3.085   1.00 11.35 ? 226 PHE A CG  1 
ATOM   1840 C  CD1 . PHE A 1 225 ? 10.340  -7.753  2.384   1.00 16.57 ? 226 PHE A CD1 1 
ATOM   1841 C  CD2 . PHE A 1 225 ? 7.967   -7.857  2.552   1.00 17.88 ? 226 PHE A CD2 1 
ATOM   1842 C  CE1 . PHE A 1 225 ? 10.213  -7.063  1.183   1.00 14.63 ? 226 PHE A CE1 1 
ATOM   1843 C  CE2 . PHE A 1 225 ? 7.838   -7.169  1.360   1.00 18.83 ? 226 PHE A CE2 1 
ATOM   1844 C  CZ  . PHE A 1 225 ? 8.962   -6.772  0.671   1.00 16.65 ? 226 PHE A CZ  1 
ATOM   1845 N  N   . ARG A 1 226 ? 10.245  -10.780 6.662   1.00 11.91 ? 227 ARG A N   1 
ATOM   1846 C  CA  . ARG A 1 226 ? 9.873   -11.428 7.924   1.00 13.69 ? 227 ARG A CA  1 
ATOM   1847 C  C   . ARG A 1 226 ? 11.029  -11.481 8.946   1.00 11.17 ? 227 ARG A C   1 
ATOM   1848 O  O   . ARG A 1 226 ? 10.761  -11.869 10.110  1.00 14.22 ? 227 ARG A O   1 
ATOM   1849 C  CB  . ARG A 1 226 ? 9.413   -12.875 7.642   1.00 13.56 ? 227 ARG A CB  1 
ATOM   1850 C  CG  . ARG A 1 226 ? 8.166   -12.971 6.740   1.00 12.43 ? 227 ARG A CG  1 
ATOM   1851 C  CD  . ARG A 1 226 ? 7.729   -14.397 6.671   1.00 14.02 ? 227 ARG A CD  1 
ATOM   1852 N  NE  . ARG A 1 226 ? 6.650   -14.550 5.685   1.00 12.69 ? 227 ARG A NE  1 
ATOM   1853 C  CZ  . ARG A 1 226 ? 6.605   -15.428 4.692   1.00 12.51 ? 227 ARG A CZ  1 
ATOM   1854 N  NH1 . ARG A 1 226 ? 7.581   -16.376 4.517   1.00 18.34 ? 227 ARG A NH1 1 
ATOM   1855 N  NH2 . ARG A 1 226 ? 5.642   -15.338 3.801   1.00 14.08 ? 227 ARG A NH2 1 
ATOM   1856 N  N   . LYS A 1 227 ? 12.193  -10.949 8.577   1.00 12.73 ? 228 LYS A N   1 
ATOM   1857 C  CA  . LYS A 1 227 ? 13.264  -10.800 9.576   1.00 13.81 ? 228 LYS A CA  1 
ATOM   1858 C  C   . LYS A 1 227 ? 13.263  -9.454  10.255  1.00 14.95 ? 228 LYS A C   1 
ATOM   1859 O  O   . LYS A 1 227 ? 13.995  -9.264  11.216  1.00 14.54 ? 228 LYS A O   1 
ATOM   1860 C  CB  . LYS A 1 227 ? 14.659  -11.023 8.909   1.00 15.89 ? 228 LYS A CB  1 
ATOM   1861 C  CG  . LYS A 1 227 ? 14.890  -12.487 8.439   1.00 19.52 ? 228 LYS A CG  1 
ATOM   1862 C  CD  . LYS A 1 227 ? 16.273  -12.602 7.812   1.00 24.06 ? 228 LYS A CD  1 
ATOM   1863 C  CE  . LYS A 1 227 ? 17.435  -12.837 8.787   1.00 36.43 ? 228 LYS A CE  1 
ATOM   1864 N  NZ  . LYS A 1 227 ? 18.791  -12.926 8.118   1.00 68.85 ? 228 LYS A NZ  1 
ATOM   1865 N  N   . LEU A 1 228 ? 12.495  -8.490  9.735   1.00 12.86 ? 229 LEU A N   1 
ATOM   1866 C  CA  . LEU A 1 228 ? 12.244  -7.225  10.462  1.00 12.23 ? 229 LEU A CA  1 
ATOM   1867 C  C   . LEU A 1 228 ? 11.632  -7.466  11.843  1.00 13.15 ? 229 LEU A C   1 
ATOM   1868 O  O   . LEU A 1 228 ? 11.078  -8.497  12.094  1.00 12.44 ? 229 LEU A O   1 
ATOM   1869 C  CB  . LEU A 1 228 ? 11.372  -6.278  9.591   1.00 12.00 ? 229 LEU A CB  1 
ATOM   1870 C  CG  . LEU A 1 228 ? 12.087  -5.799  8.336   1.00 10.96 ? 229 LEU A CG  1 
ATOM   1871 C  CD1 . LEU A 1 228 ? 11.028  -5.219  7.384   1.00 12.16 ? 229 LEU A CD1 1 
ATOM   1872 C  CD2 . LEU A 1 228 ? 13.194  -4.756  8.633   1.00 14.36 ? 229 LEU A CD2 1 
ATOM   1873 N  N   . ASN A 1 229 ? 11.746  -6.441  12.721  1.00 12.09 ? 230 ASN A N   1 
ATOM   1874 C  CA  . ASN A 1 229 ? 11.211  -6.497  14.086  1.00 14.14 ? 230 ASN A CA  1 
ATOM   1875 C  C   . ASN A 1 229 ? 10.206  -5.339  14.252  1.00 12.95 ? 230 ASN A C   1 
ATOM   1876 O  O   . ASN A 1 229 ? 10.479  -4.226  13.835  1.00 14.80 ? 230 ASN A O   1 
ATOM   1877 C  CB  . ASN A 1 229 ? 12.366  -6.247  15.087  1.00 15.44 ? 230 ASN A CB  1 
ATOM   1878 C  CG  . ASN A 1 229 ? 13.299  -7.454  15.331  1.00 15.67 ? 230 ASN A CG  1 
ATOM   1879 O  OD1 . ASN A 1 229 ? 14.164  -7.328  16.202  1.00 19.46 ? 230 ASN A OD1 1 
ATOM   1880 N  ND2 . ASN A 1 229 ? 13.226  -8.543  14.571  1.00 16.44 ? 230 ASN A ND2 1 
ATOM   1881 N  N   . PHE A 1 230 ? 9.129   -5.622  14.994  1.00 13.45 ? 231 PHE A N   1 
ATOM   1882 C  CA  . PHE A 1 230 ? 8.191   -4.639  15.498  1.00 13.14 ? 231 PHE A CA  1 
ATOM   1883 C  C   . PHE A 1 230 ? 8.844   -3.826  16.626  1.00 15.78 ? 231 PHE A C   1 
ATOM   1884 O  O   . PHE A 1 230 ? 8.597   -2.603  16.736  1.00 15.60 ? 231 PHE A O   1 
ATOM   1885 C  CB  . PHE A 1 230 ? 6.948   -5.282  16.122  1.00 15.97 ? 231 PHE A CB  1 
ATOM   1886 C  CG  . PHE A 1 230 ? 5.944   -5.831  15.129  1.00 13.04 ? 231 PHE A CG  1 
ATOM   1887 C  CD1 . PHE A 1 230 ? 5.427   -4.995  14.088  1.00 13.99 ? 231 PHE A CD1 1 
ATOM   1888 C  CD2 . PHE A 1 230 ? 5.449   -7.122  15.263  1.00 16.06 ? 231 PHE A CD2 1 
ATOM   1889 C  CE1 . PHE A 1 230 ? 4.442   -5.435  13.223  1.00 15.45 ? 231 PHE A CE1 1 
ATOM   1890 C  CE2 . PHE A 1 230 ? 4.451   -7.583  14.404  1.00 15.20 ? 231 PHE A CE2 1 
ATOM   1891 C  CZ  . PHE A 1 230 ? 3.968   -6.714  13.396  1.00 13.75 ? 231 PHE A CZ  1 
ATOM   1892 N  N   . ASN A 1 231 ? 9.645   -4.514  17.473  1.00 15.75 ? 232 ASN A N   1 
ATOM   1893 C  CA  . ASN A 1 231 ? 10.205  -3.918  18.686  1.00 15.22 ? 232 ASN A CA  1 
ATOM   1894 C  C   . ASN A 1 231 ? 11.337  -2.940  18.328  1.00 16.78 ? 232 ASN A C   1 
ATOM   1895 O  O   . ASN A 1 231 ? 11.958  -3.044  17.261  1.00 14.44 ? 232 ASN A O   1 
ATOM   1896 C  CB  . ASN A 1 231 ? 10.768  -5.020  19.606  1.00 16.22 ? 232 ASN A CB  1 
ATOM   1897 C  CG  . ASN A 1 231 ? 11.671  -5.928  18.851  1.00 17.81 ? 232 ASN A CG  1 
ATOM   1898 O  OD1 . ASN A 1 231 ? 11.194  -6.735  18.047  1.00 17.06 ? 232 ASN A OD1 1 
ATOM   1899 N  ND2 . ASN A 1 231 ? 12.966  -5.804  19.057  1.00 20.10 ? 232 ASN A ND2 1 
ATOM   1900 N  N   . GLY A 1 232 ? 11.693  -2.039  19.252  1.00 16.50 ? 233 GLY A N   1 
ATOM   1901 C  CA  . GLY A 1 232 ? 12.920  -1.327  19.128  1.00 20.69 ? 233 GLY A CA  1 
ATOM   1902 C  C   . GLY A 1 232 ? 14.154  -2.142  19.583  1.00 19.92 ? 233 GLY A C   1 
ATOM   1903 O  O   . GLY A 1 232 ? 13.973  -3.169  20.288  1.00 21.51 ? 233 GLY A O   1 
ATOM   1904 N  N   . GLU A 1 233 ? 15.332  -1.663  19.148  1.00 22.99 ? 234 GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 233 ? 16.721  -2.170  19.479  1.00 23.58 ? 234 GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 233 ? 16.748  -2.269  21.022  1.00 39.81 ? 234 GLU A C   1 
ATOM   1907 O  O   . GLU A 1 233 ? 16.438  -1.314  21.728  1.00 31.22 ? 234 GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 233 ? 17.902  -1.289  18.896  1.00 24.97 ? 234 GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 233 ? 19.341  -1.829  19.081  1.00 31.15 ? 234 GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 233 ? 20.426  -0.959  18.436  1.00 38.22 ? 234 GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 233 ? 21.600  -1.388  18.514  1.00 45.05 ? 234 GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 233 ? 20.167  0.142   17.872  1.00 35.14 ? 234 GLU A OE2 1 
ATOM   1913 N  N   A GLY A 1 234 ? 17.099  -3.426  21.587  0.50 31.20 ? 235 GLY A N   1 
ATOM   1914 N  N   B GLY A 1 234 ? 17.045  -3.481  21.487  0.50 29.68 ? 235 GLY A N   1 
ATOM   1915 C  CA  A GLY A 1 234 ? 17.086  -3.575  23.063  0.50 39.89 ? 235 GLY A CA  1 
ATOM   1916 C  CA  B GLY A 1 234 ? 17.150  -3.765  22.910  0.50 30.53 ? 235 GLY A CA  1 
ATOM   1917 C  C   A GLY A 1 234 ? 15.700  -3.707  23.728  0.50 48.60 ? 235 GLY A C   1 
ATOM   1918 C  C   B GLY A 1 234 ? 15.941  -4.389  23.615  0.50 28.01 ? 235 GLY A C   1 
ATOM   1919 O  O   A GLY A 1 234 ? 15.517  -3.249  24.857  0.50 39.69 ? 235 GLY A O   1 
ATOM   1920 O  O   B GLY A 1 234 ? 16.125  -4.912  24.678  0.50 21.01 ? 235 GLY A O   1 
ATOM   1921 N  N   . GLU A 1 235 ? 14.718  -4.319  23.042  1.00 31.07 ? 236 GLU A N   1 
ATOM   1922 C  CA  . GLU A 1 235 ? 13.432  -4.770  23.696  1.00 29.50 ? 236 GLU A CA  1 
ATOM   1923 C  C   . GLU A 1 235 ? 13.251  -6.223  23.268  1.00 23.28 ? 236 GLU A C   1 
ATOM   1924 O  O   . GLU A 1 235 ? 13.922  -6.588  22.367  1.00 21.65 ? 236 GLU A O   1 
ATOM   1925 C  CB  . GLU A 1 235 ? 12.232  -3.999  23.116  1.00 32.72 ? 236 GLU A CB  1 
ATOM   1926 C  CG  . GLU A 1 235 ? 12.018  -2.585  23.667  1.00 34.56 ? 236 GLU A CG  1 
ATOM   1927 C  CD  . GLU A 1 235 ? 11.299  -1.647  22.685  1.00 53.29 ? 236 GLU A CD  1 
ATOM   1928 O  OE1 . GLU A 1 235 ? 10.362  -2.073  21.902  1.00 45.52 ? 236 GLU A OE1 1 
ATOM   1929 O  OE2 . GLU A 1 235 ? 11.738  -0.468  22.720  1.00 40.24 ? 236 GLU A OE2 1 
ATOM   1930 N  N   . PRO A 1 236 ? 12.399  -7.074  23.927  1.00 21.68 ? 237 PRO A N   1 
ATOM   1931 C  CA  . PRO A 1 236 ? 12.395  -8.441  23.345  1.00 22.07 ? 237 PRO A CA  1 
ATOM   1932 C  C   . PRO A 1 236 ? 12.007  -8.525  21.845  1.00 17.85 ? 237 PRO A C   1 
ATOM   1933 O  O   . PRO A 1 236 ? 11.089  -7.810  21.403  1.00 17.04 ? 237 PRO A O   1 
ATOM   1934 C  CB  . PRO A 1 236 ? 11.297  -9.161  24.173  1.00 19.79 ? 237 PRO A CB  1 
ATOM   1935 C  CG  . PRO A 1 236 ? 11.244  -8.413  25.483  1.00 26.82 ? 237 PRO A CG  1 
ATOM   1936 C  CD  . PRO A 1 236 ? 11.531  -6.961  25.112  1.00 26.86 ? 237 PRO A CD  1 
ATOM   1937 N  N   . GLU A 1 237 ? 12.664  -9.384  21.092  1.00 18.41 ? 238 GLU A N   1 
ATOM   1938 C  CA  . GLU A 1 237 ? 12.470  -9.488  19.622  1.00 17.39 ? 238 GLU A CA  1 
ATOM   1939 C  C   . GLU A 1 237 ? 11.104  -10.085 19.272  1.00 14.86 ? 238 GLU A C   1 
ATOM   1940 O  O   . GLU A 1 237 ? 10.751  -11.184 19.680  1.00 17.69 ? 238 GLU A O   1 
ATOM   1941 C  CB  . GLU A 1 237 ? 13.505  -10.426 18.990  1.00 20.51 ? 238 GLU A CB  1 
ATOM   1942 C  CG  . GLU A 1 237 ? 13.268  -10.474 17.508  1.00 21.40 ? 238 GLU A CG  1 
ATOM   1943 C  CD  . GLU A 1 237 ? 14.372  -11.149 16.714  1.00 23.34 ? 238 GLU A CD  1 
ATOM   1944 O  OE1 . GLU A 1 237 ? 14.943  -12.105 17.298  1.00 35.52 ? 238 GLU A OE1 1 
ATOM   1945 O  OE2 . GLU A 1 237 ? 14.688  -10.738 15.542  1.00 20.82 ? 238 GLU A OE2 1 
ATOM   1946 N  N   . GLU A 1 238 ? 10.326  -9.308  18.514  1.00 15.29 ? 239 GLU A N   1 
ATOM   1947 C  CA  . GLU A 1 238 ? 9.010   -9.773  18.026  1.00 17.14 ? 239 GLU A CA  1 
ATOM   1948 C  C   . GLU A 1 238 ? 9.038   -9.552  16.513  1.00 13.99 ? 239 GLU A C   1 
ATOM   1949 O  O   . GLU A 1 238 ? 9.228   -8.417  16.040  1.00 15.34 ? 239 GLU A O   1 
ATOM   1950 C  CB  . GLU A 1 238 ? 7.854   -8.934  18.631  1.00 17.83 ? 239 GLU A CB  1 
ATOM   1951 C  CG  . GLU A 1 238 ? 7.562   -9.324  20.109  1.00 22.91 ? 239 GLU A CG  1 
ATOM   1952 C  CD  . GLU A 1 238 ? 6.306   -8.671  20.616  1.00 19.47 ? 239 GLU A CD  1 
ATOM   1953 O  OE1 . GLU A 1 238 ? 5.166   -9.077  20.147  1.00 23.90 ? 239 GLU A OE1 1 
ATOM   1954 O  OE2 . GLU A 1 238 ? 6.404   -7.761  21.507  1.00 24.24 ? 239 GLU A OE2 1 
ATOM   1955 N  N   . LEU A 1 239 ? 8.999   -10.644 15.742  1.00 14.71 ? 240 LEU A N   1 
ATOM   1956 C  CA  . LEU A 1 239 ? 9.190   -10.495 14.278  1.00 14.92 ? 240 LEU A CA  1 
ATOM   1957 C  C   . LEU A 1 239 ? 8.030   -9.650  13.658  1.00 12.46 ? 240 LEU A C   1 
ATOM   1958 O  O   . LEU A 1 239 ? 6.891   -9.823  14.054  1.00 13.56 ? 240 LEU A O   1 
ATOM   1959 C  CB  . LEU A 1 239 ? 9.266   -11.883 13.575  1.00 16.60 ? 240 LEU A CB  1 
ATOM   1960 C  CG  . LEU A 1 239 ? 10.530  -12.728 13.863  1.00 17.59 ? 240 LEU A CG  1 
ATOM   1961 C  CD1 . LEU A 1 239 ? 10.466  -14.036 13.075  1.00 28.77 ? 240 LEU A CD1 1 
ATOM   1962 C  CD2 . LEU A 1 239 ? 11.764  -11.939 13.526  1.00 17.40 ? 240 LEU A CD2 1 
ATOM   1963 N  N   . MET A 1 240 ? 8.394   -8.762  12.748  1.00 11.66 ? 241 MET A N   1 
ATOM   1964 C  CA  . MET A 1 240 ? 7.382   -7.955  12.047  1.00 13.36 ? 241 MET A CA  1 
ATOM   1965 C  C   . MET A 1 240 ? 6.747   -8.836  10.951  1.00 11.49 ? 241 MET A C   1 
ATOM   1966 O  O   . MET A 1 240 ? 7.319   -8.958  9.847   1.00 11.16 ? 241 MET A O   1 
ATOM   1967 C  CB  . MET A 1 240 ? 8.064   -6.764  11.403  1.00 14.66 ? 241 MET A CB  1 
ATOM   1968 C  CG  . MET A 1 240 ? 7.106   -5.774  10.713  1.00 13.44 ? 241 MET A CG  1 
ATOM   1969 S  SD  . MET A 1 240 ? 7.909   -4.342  10.015  1.00 14.70 ? 241 MET A SD  1 
ATOM   1970 C  CE  . MET A 1 240 ? 8.096   -3.360  11.480  1.00 14.08 ? 241 MET A CE  1 
ATOM   1971 N  N   . VAL A 1 241 ? 5.634   -9.437  11.313  1.00 10.42 ? 242 VAL A N   1 
ATOM   1972 C  CA  . VAL A 1 241 ? 4.891   -10.302 10.363  1.00 11.05 ? 242 VAL A CA  1 
ATOM   1973 C  C   . VAL A 1 241 ? 3.428   -10.082 10.690  1.00 10.10 ? 242 VAL A C   1 
ATOM   1974 O  O   . VAL A 1 241 ? 3.066   -9.699  11.834  1.00 11.60 ? 242 VAL A O   1 
ATOM   1975 C  CB  . VAL A 1 241 ? 5.236   -11.805 10.504  1.00 10.97 ? 242 VAL A CB  1 
ATOM   1976 C  CG1 . VAL A 1 241 ? 6.657   -12.064 10.057  1.00 13.01 ? 242 VAL A CG1 1 
ATOM   1977 C  CG2 . VAL A 1 241 ? 4.989   -12.279 11.936  1.00 12.73 ? 242 VAL A CG2 1 
ATOM   1978 N  N   . ASP A 1 242 ? 2.538   -10.380 9.724   1.00 10.08 ? 243 ASP A N   1 
ATOM   1979 C  CA  . ASP A 1 242 ? 1.063   -10.249 9.945   1.00 10.07 ? 243 ASP A CA  1 
ATOM   1980 C  C   . ASP A 1 242 ? 0.702   -8.822  10.347  1.00 9.52  ? 243 ASP A C   1 
ATOM   1981 O  O   . ASP A 1 242 ? -0.160  -8.587  11.208  1.00 11.70 ? 243 ASP A O   1 
ATOM   1982 C  CB  . ASP A 1 242 ? 0.486   -11.349 10.877  1.00 10.82 ? 243 ASP A CB  1 
ATOM   1983 C  CG  . ASP A 1 242 ? 0.645   -12.700 10.297  1.00 10.72 ? 243 ASP A CG  1 
ATOM   1984 O  OD1 . ASP A 1 242 ? 0.448   -12.858 9.071   1.00 10.27 ? 243 ASP A OD1 1 
ATOM   1985 O  OD2 . ASP A 1 242 ? 1.023   -13.635 11.073  1.00 14.01 ? 243 ASP A OD2 1 
ATOM   1986 N  N   . ASN A 1 243 ? 1.244   -7.892  9.601   1.00 9.15  ? 244 ASN A N   1 
ATOM   1987 C  CA  . ASN A 1 243 ? 0.910   -6.460  9.784   1.00 9.46  ? 244 ASN A CA  1 
ATOM   1988 C  C   . ASN A 1 243 ? -0.146  -5.988  8.782   1.00 8.09  ? 244 ASN A C   1 
ATOM   1989 O  O   . ASN A 1 243 ? 0.051   -4.961  8.127   1.00 10.02 ? 244 ASN A O   1 
ATOM   1990 C  CB  . ASN A 1 243 ? 2.180   -5.557  9.728   1.00 10.25 ? 244 ASN A CB  1 
ATOM   1991 C  CG  . ASN A 1 243 ? 2.989   -5.761  8.445   1.00 9.39  ? 244 ASN A CG  1 
ATOM   1992 O  OD1 . ASN A 1 243 ? 2.646   -6.594  7.577   1.00 10.36 ? 244 ASN A OD1 1 
ATOM   1993 N  ND2 . ASN A 1 243 ? 3.989   -4.987  8.276   1.00 13.19 ? 244 ASN A ND2 1 
ATOM   1994 N  N   . TRP A 1 244 ? -1.212  -6.752  8.715   1.00 8.85  ? 245 TRP A N   1 
ATOM   1995 C  CA  . TRP A 1 244 ? -2.350  -6.484  7.818   1.00 8.81  ? 245 TRP A CA  1 
ATOM   1996 C  C   . TRP A 1 244 ? -3.588  -6.370  8.630   1.00 8.23  ? 245 TRP A C   1 
ATOM   1997 O  O   . TRP A 1 244 ? -3.829  -7.120  9.570   1.00 10.36 ? 245 TRP A O   1 
ATOM   1998 C  CB  . TRP A 1 244 ? -2.476  -7.573  6.732   1.00 8.55  ? 245 TRP A CB  1 
ATOM   1999 C  CG  . TRP A 1 244 ? -2.408  -8.983  7.191   1.00 8.39  ? 245 TRP A CG  1 
ATOM   2000 C  CD1 . TRP A 1 244 ? -1.286  -9.736  7.508   1.00 9.19  ? 245 TRP A CD1 1 
ATOM   2001 C  CD2 . TRP A 1 244 ? -3.544  -9.867  7.427   1.00 8.46  ? 245 TRP A CD2 1 
ATOM   2002 N  NE1 . TRP A 1 244 ? -1.680  -10.993 7.909   1.00 9.12  ? 245 TRP A NE1 1 
ATOM   2003 C  CE2 . TRP A 1 244 ? -3.048  -11.123 7.868   1.00 8.63  ? 245 TRP A CE2 1 
ATOM   2004 C  CE3 . TRP A 1 244 ? -4.919  -9.726  7.235   1.00 9.74  ? 245 TRP A CE3 1 
ATOM   2005 C  CZ2 . TRP A 1 244 ? -3.898  -12.192 8.165   1.00 10.20 ? 245 TRP A CZ2 1 
ATOM   2006 C  CZ3 . TRP A 1 244 ? -5.756  -10.781 7.529   1.00 12.06 ? 245 TRP A CZ3 1 
ATOM   2007 C  CH2 . TRP A 1 244 ? -5.235  -12.003 7.978   1.00 11.01 ? 245 TRP A CH2 1 
ATOM   2008 N  N   . ARG A 1 245 ? -4.462  -5.483  8.200   1.00 8.72  ? 246 ARG A N   1 
ATOM   2009 C  CA  . ARG A 1 245 ? -5.843  -5.384  8.696   1.00 8.84  ? 246 ARG A CA  1 
ATOM   2010 C  C   . ARG A 1 245 ? -6.717  -6.334  7.876   1.00 8.17  ? 246 ARG A C   1 
ATOM   2011 O  O   . ARG A 1 245 ? -6.611  -6.316  6.671   1.00 9.71  ? 246 ARG A O   1 
ATOM   2012 C  CB  . ARG A 1 245 ? -6.332  -3.936  8.585   1.00 8.90  ? 246 ARG A CB  1 
ATOM   2013 C  CG  . ARG A 1 245 ? -7.672  -3.722  9.307   1.00 8.42  ? 246 ARG A CG  1 
ATOM   2014 C  CD  . ARG A 1 245 ? -8.275  -2.391  8.953   1.00 9.60  ? 246 ARG A CD  1 
ATOM   2015 N  NE  . ARG A 1 245 ? -9.340  -2.022  9.919   1.00 9.88  ? 246 ARG A NE  1 
ATOM   2016 C  CZ  . ARG A 1 245 ? -10.161 -0.997  9.809   1.00 10.19 ? 246 ARG A CZ  1 
ATOM   2017 N  NH1 . ARG A 1 245 ? -10.153 -0.189  8.749   1.00 10.46 ? 246 ARG A NH1 1 
ATOM   2018 N  NH2 . ARG A 1 245 ? -11.075 -0.765  10.817  1.00 12.08 ? 246 ARG A NH2 1 
ATOM   2019 N  N   . PRO A 1 246 ? -7.591  -7.092  8.494   1.00 10.41 ? 247 PRO A N   1 
ATOM   2020 C  CA  . PRO A 1 246 ? -8.509  -7.923  7.723   1.00 9.92  ? 247 PRO A CA  1 
ATOM   2021 C  C   . PRO A 1 246 ? -9.555  -7.103  6.958   1.00 8.68  ? 247 PRO A C   1 
ATOM   2022 O  O   . PRO A 1 246 ? -9.818  -5.912  7.235   1.00 9.65  ? 247 PRO A O   1 
ATOM   2023 C  CB  . PRO A 1 246 ? -9.175  -8.842  8.787   1.00 13.19 ? 247 PRO A CB  1 
ATOM   2024 C  CG  . PRO A 1 246 ? -8.308  -8.743  9.989   1.00 18.99 ? 247 PRO A CG  1 
ATOM   2025 C  CD  . PRO A 1 246 ? -7.701  -7.338  9.952   1.00 12.88 ? 247 PRO A CD  1 
ATOM   2026 N  N   . ALA A 1 247 ? -10.201 -7.757  5.985   1.00 9.62  ? 248 ALA A N   1 
ATOM   2027 C  CA  . ALA A 1 247 ? -11.305 -7.144  5.268   1.00 9.76  ? 248 ALA A CA  1 
ATOM   2028 C  C   . ALA A 1 247 ? -12.408 -6.604  6.153   1.00 10.56 ? 248 ALA A C   1 
ATOM   2029 O  O   . ALA A 1 247 ? -12.798 -7.277  7.132   1.00 12.06 ? 248 ALA A O   1 
ATOM   2030 C  CB  . ALA A 1 247 ? -11.843 -8.186  4.244   1.00 13.18 ? 248 ALA A CB  1 
ATOM   2031 N  N   . GLN A 1 248 ? -12.918 -5.412  5.798   1.00 9.77  ? 249 GLN A N   1 
ATOM   2032 C  CA  . GLN A 1 248 ? -13.922 -4.717  6.591   1.00 10.03 ? 249 GLN A CA  1 
ATOM   2033 C  C   . GLN A 1 248 ? -15.211 -4.702  5.768   1.00 10.86 ? 249 GLN A C   1 
ATOM   2034 O  O   . GLN A 1 248 ? -15.267 -4.958  4.558   1.00 12.35 ? 249 GLN A O   1 
ATOM   2035 C  CB  . GLN A 1 248 ? -13.504 -3.297  6.807   1.00 10.94 ? 249 GLN A CB  1 
ATOM   2036 C  CG  . GLN A 1 248 ? -12.186 -3.231  7.601   1.00 12.10 ? 249 GLN A CG  1 
ATOM   2037 C  CD  . GLN A 1 248 ? -12.291 -3.896  8.966   1.00 11.43 ? 249 GLN A CD  1 
ATOM   2038 O  OE1 . GLN A 1 248 ? -13.221 -3.558  9.707   1.00 15.69 ? 249 GLN A OE1 1 
ATOM   2039 N  NE2 . GLN A 1 248 ? -11.461 -4.858  9.279   1.00 13.38 ? 249 GLN A NE2 1 
ATOM   2040 N  N   . PRO A 1 249 ? -16.361 -4.422  6.415   1.00 13.59 ? 250 PRO A N   1 
ATOM   2041 C  CA  . PRO A 1 249 ? -17.652 -4.468  5.724   1.00 14.13 ? 250 PRO A CA  1 
ATOM   2042 C  C   . PRO A 1 249 ? -17.730 -3.458  4.568   1.00 11.48 ? 250 PRO A C   1 
ATOM   2043 O  O   . PRO A 1 249 ? -17.404 -2.286  4.736   1.00 12.83 ? 250 PRO A O   1 
ATOM   2044 C  CB  . PRO A 1 249 ? -18.669 -4.140  6.856   1.00 18.69 ? 250 PRO A CB  1 
ATOM   2045 C  CG  . PRO A 1 249 ? -17.961 -4.481  8.113   1.00 20.10 ? 250 PRO A CG  1 
ATOM   2046 C  CD  . PRO A 1 249 ? -16.517 -4.154  7.851   1.00 13.94 ? 250 PRO A CD  1 
ATOM   2047 N  N   . LEU A 1 250 ? -18.228 -3.937  3.451   1.00 12.34 ? 251 LEU A N   1 
ATOM   2048 C  CA  . LEU A 1 250 ? -18.331 -3.060  2.294   1.00 12.66 ? 251 LEU A CA  1 
ATOM   2049 C  C   . LEU A 1 250 ? -19.422 -2.013  2.432   1.00 12.81 ? 251 LEU A C   1 
ATOM   2050 O  O   . LEU A 1 250 ? -19.350 -0.859  1.919   1.00 13.40 ? 251 LEU A O   1 
ATOM   2051 C  CB  . LEU A 1 250 ? -18.638 -3.919  1.063   1.00 13.84 ? 251 LEU A CB  1 
ATOM   2052 C  CG  . LEU A 1 250 ? -18.579 -3.223  -0.311  1.00 15.15 ? 251 LEU A CG  1 
ATOM   2053 C  CD1 . LEU A 1 250 ? -17.187 -2.618  -0.628  1.00 12.98 ? 251 LEU A CD1 1 
ATOM   2054 C  CD2 . LEU A 1 250 ? -19.002 -4.185  -1.436  1.00 17.39 ? 251 LEU A CD2 1 
ATOM   2055 N  N   . LYS A 1 251 ? -20.478 -2.366  3.180   1.00 14.99 ? 252 LYS A N   1 
ATOM   2056 C  CA  . LYS A 1 251 ? -21.557 -1.365  3.516   1.00 15.52 ? 252 LYS A CA  1 
ATOM   2057 C  C   . LYS A 1 251 ? -22.169 -0.879  2.205   1.00 16.26 ? 252 LYS A C   1 
ATOM   2058 O  O   . LYS A 1 251 ? -22.435 -1.745  1.343   1.00 24.45 ? 252 LYS A O   1 
ATOM   2059 C  CB  . LYS A 1 251 ? -21.129 -0.302  4.494   1.00 19.25 ? 252 LYS A CB  1 
ATOM   2060 C  CG  . LYS A 1 251 ? -20.774 -0.971  5.821   1.00 22.41 ? 252 LYS A CG  1 
ATOM   2061 C  CD  . LYS A 1 251 ? -20.612 -0.024  6.943   1.00 29.00 ? 252 LYS A CD  1 
ATOM   2062 C  CE  . LYS A 1 251 ? -20.407 -0.827  8.197   1.00 28.42 ? 252 LYS A CE  1 
ATOM   2063 N  NZ  . LYS A 1 251 ? -19.992 0.121   9.303   1.00 33.21 ? 252 LYS A NZ  1 
ATOM   2064 N  N   A ASN A 1 252 ? -22.291 0.447   2.090   0.50 16.38 ? 253 ASN A N   1 
ATOM   2065 N  N   B ASN A 1 252 ? -22.503 0.356   1.930   0.50 18.62 ? 253 ASN A N   1 
ATOM   2066 C  CA  A ASN A 1 252 ? -23.045 1.028   0.988   0.50 21.47 ? 253 ASN A CA  1 
ATOM   2067 C  CA  B ASN A 1 252 ? -23.284 0.384   0.654   0.50 21.80 ? 253 ASN A CA  1 
ATOM   2068 C  C   A ASN A 1 252 ? -22.345 0.970   -0.446  0.50 23.20 ? 253 ASN A C   1 
ATOM   2069 C  C   B ASN A 1 252 ? -22.453 0.368   -0.713  0.50 17.88 ? 253 ASN A C   1 
ATOM   2070 O  O   A ASN A 1 252 ? -22.992 1.388   -1.463  0.50 19.65 ? 253 ASN A O   1 
ATOM   2071 O  O   B ASN A 1 252 ? -22.953 0.373   -1.838  0.50 17.64 ? 253 ASN A O   1 
ATOM   2072 C  CB  A ASN A 1 252 ? -23.624 2.423   1.433   0.50 22.93 ? 253 ASN A CB  1 
ATOM   2073 C  CB  B ASN A 1 252 ? -24.458 1.375   0.790   0.50 21.78 ? 253 ASN A CB  1 
ATOM   2074 C  CG  A ASN A 1 252 ? -24.694 2.970   0.492   0.50 22.82 ? 253 ASN A CG  1 
ATOM   2075 C  CG  B ASN A 1 252 ? -25.428 0.950   1.883   0.50 23.39 ? 253 ASN A CG  1 
ATOM   2076 O  OD1 A ASN A 1 252 ? -25.478 2.216   -0.073  0.50 28.95 ? 253 ASN A OD1 1 
ATOM   2077 O  OD1 B ASN A 1 252 ? -25.978 -0.168  1.830   0.50 25.41 ? 253 ASN A OD1 1 
ATOM   2078 N  ND2 A ASN A 1 252 ? -24.696 4.290   0.297   0.50 20.05 ? 253 ASN A ND2 1 
ATOM   2079 N  ND2 B ASN A 1 252 ? -25.622 1.811   2.903   0.50 35.69 ? 253 ASN A ND2 1 
ATOM   2080 N  N   . ARG A 1 253 ? -21.141 0.341   -0.562  1.00 13.53 ? 254 ARG A N   1 
ATOM   2081 C  CA  . ARG A 1 253 ? -20.223 0.826   -1.605  1.00 11.84 ? 254 ARG A CA  1 
ATOM   2082 C  C   . ARG A 1 253 ? -20.236 -0.099  -2.773  1.00 11.89 ? 254 ARG A C   1 
ATOM   2083 O  O   . ARG A 1 253 ? -20.508 -1.306  -2.645  1.00 17.58 ? 254 ARG A O   1 
ATOM   2084 C  CB  . ARG A 1 253 ? -18.783 0.930   -1.066  1.00 10.50 ? 254 ARG A CB  1 
ATOM   2085 C  CG  . ARG A 1 253 ? -18.697 1.983   0.023   1.00 10.28 ? 254 ARG A CG  1 
ATOM   2086 C  CD  . ARG A 1 253 ? -17.328 2.017   0.651   1.00 10.39 ? 254 ARG A CD  1 
ATOM   2087 N  NE  . ARG A 1 253 ? -17.117 0.841   1.535   1.00 10.46 ? 254 ARG A NE  1 
ATOM   2088 C  CZ  . ARG A 1 253 ? -15.971 0.561   2.196   1.00 9.77  ? 254 ARG A CZ  1 
ATOM   2089 N  NH1 . ARG A 1 253 ? -14.875 1.249   1.954   1.00 9.92  ? 254 ARG A NH1 1 
ATOM   2090 N  NH2 . ARG A 1 253 ? -15.980 -0.450  3.060   1.00 9.29  ? 254 ARG A NH2 1 
ATOM   2091 N  N   A GLN A 1 254 ? -19.856 0.454   -3.932  0.50 11.89 ? 255 GLN A N   1 
ATOM   2092 N  N   B GLN A 1 254 ? -19.925 0.421   -3.959  0.50 12.10 ? 255 GLN A N   1 
ATOM   2093 C  CA  A GLN A 1 254 ? -19.700 -0.276  -5.207  0.50 14.34 ? 255 GLN A CA  1 
ATOM   2094 C  CA  B GLN A 1 254 ? -19.696 -0.415  -5.150  0.50 13.55 ? 255 GLN A CA  1 
ATOM   2095 C  C   A GLN A 1 254 ? -18.251 -0.309  -5.657  0.50 11.65 ? 255 GLN A C   1 
ATOM   2096 C  C   B GLN A 1 254 ? -18.206 -0.368  -5.420  0.50 12.52 ? 255 GLN A C   1 
ATOM   2097 O  O   A GLN A 1 254 ? -17.639 0.751   -5.802  0.50 13.41 ? 255 GLN A O   1 
ATOM   2098 O  O   B GLN A 1 254 ? -17.521 0.632   -5.120  0.50 11.34 ? 255 GLN A O   1 
ATOM   2099 C  CB  A GLN A 1 254 ? -20.458 0.420   -6.317  0.50 15.94 ? 255 GLN A CB  1 
ATOM   2100 C  CB  B GLN A 1 254 ? -20.510 0.086   -6.349  0.50 15.50 ? 255 GLN A CB  1 
ATOM   2101 C  CG  A GLN A 1 254 ? -20.417 -0.455  -7.553  0.50 21.54 ? 255 GLN A CG  1 
ATOM   2102 C  CG  B GLN A 1 254 ? -22.005 0.079   -6.055  0.50 17.01 ? 255 GLN A CG  1 
ATOM   2103 C  CD  A GLN A 1 254 ? -21.405 -0.105  -8.617  0.50 23.89 ? 255 GLN A CD  1 
ATOM   2104 C  CD  B GLN A 1 254 ? -22.884 0.599   -7.185  0.50 26.12 ? 255 GLN A CD  1 
ATOM   2105 O  OE1 A GLN A 1 254 ? -22.230 -0.967  -8.977  0.50 30.37 ? 255 GLN A OE1 1 
ATOM   2106 O  OE1 B GLN A 1 254 ? -22.385 1.061   -8.225  0.50 20.95 ? 255 GLN A OE1 1 
ATOM   2107 N  NE2 A GLN A 1 254 ? -21.329 1.134   -9.173  0.50 20.80 ? 255 GLN A NE2 1 
ATOM   2108 N  NE2 B GLN A 1 254 ? -24.220 0.572   -6.981  0.50 21.57 ? 255 GLN A NE2 1 
ATOM   2109 N  N   . ILE A 1 255 ? -17.721 -1.503  -5.872  1.00 11.83 ? 256 ILE A N   1 
ATOM   2110 C  CA  . ILE A 1 255 ? -16.377 -1.662  -6.462  1.00 10.94 ? 256 ILE A CA  1 
ATOM   2111 C  C   . ILE A 1 255 ? -16.559 -1.709  -7.989  1.00 10.35 ? 256 ILE A C   1 
ATOM   2112 O  O   . ILE A 1 255 ? -17.453 -2.416  -8.501  1.00 11.80 ? 256 ILE A O   1 
ATOM   2113 C  CB  . ILE A 1 255 ? -15.711 -2.910  -5.971  1.00 10.55 ? 256 ILE A CB  1 
ATOM   2114 C  CG1 . ILE A 1 255 ? -15.709 -2.921  -4.369  1.00 10.62 ? 256 ILE A CG1 1 
ATOM   2115 C  CG2 . ILE A 1 255 ? -14.266 -2.970  -6.594  1.00 12.59 ? 256 ILE A CG2 1 
ATOM   2116 C  CD1 . ILE A 1 255 ? -14.968 -4.110  -3.841  1.00 14.78 ? 256 ILE A CD1 1 
ATOM   2117 N  N   . LYS A 1 256 ? -15.785 -0.871  -8.663  1.00 9.41  ? 257 LYS A N   1 
ATOM   2118 C  CA  . LYS A 1 256 ? -15.821 -0.750  -10.132 1.00 11.43 ? 257 LYS A CA  1 
ATOM   2119 C  C   . LYS A 1 256 ? -14.595 -1.343  -10.753 1.00 10.01 ? 257 LYS A C   1 
ATOM   2120 O  O   . LYS A 1 256 ? -13.525 -1.283  -10.126 1.00 12.12 ? 257 LYS A O   1 
ATOM   2121 C  CB  . LYS A 1 256 ? -15.927 0.741   -10.529 1.00 12.59 ? 257 LYS A CB  1 
ATOM   2122 C  CG  . LYS A 1 256 ? -17.293 1.315   -10.089 1.00 17.73 ? 257 LYS A CG  1 
ATOM   2123 C  CD  . LYS A 1 256 ? -17.476 2.760   -10.283 1.00 23.91 ? 257 LYS A CD  1 
ATOM   2124 C  CE  . LYS A 1 256 ? -18.733 3.187   -9.507  1.00 35.15 ? 257 LYS A CE  1 
ATOM   2125 N  NZ  . LYS A 1 256 ? -19.212 4.575   -9.798  1.00 37.22 ? 257 LYS A NZ  1 
ATOM   2126 N  N   . ALA A 1 257 ? -14.682 -1.979  -11.905 1.00 10.71 ? 258 ALA A N   1 
ATOM   2127 C  CA  . ALA A 1 257 ? -13.584 -2.592  -12.628 1.00 10.81 ? 258 ALA A CA  1 
ATOM   2128 C  C   . ALA A 1 257 ? -13.312 -1.797  -13.849 1.00 11.37 ? 258 ALA A C   1 
ATOM   2129 O  O   . ALA A 1 257 ? -14.255 -1.372  -14.582 1.00 11.77 ? 258 ALA A O   1 
ATOM   2130 C  CB  . ALA A 1 257 ? -13.909 -4.063  -13.000 1.00 12.04 ? 258 ALA A CB  1 
ATOM   2131 N  N   . SER A 1 258 ? -12.044 -1.671  -14.185 1.00 11.22 ? 259 SER A N   1 
ATOM   2132 C  CA  . SER A 1 258 ? -11.638 -0.962  -15.398 1.00 12.42 ? 259 SER A CA  1 
ATOM   2133 C  C   . SER A 1 258 ? -11.658 -1.850  -16.631 1.00 12.55 ? 259 SER A C   1 
ATOM   2134 O  O   . SER A 1 258 ? -11.380 -1.346  -17.756 1.00 16.71 ? 259 SER A O   1 
ATOM   2135 C  CB  . SER A 1 258 ? -10.243 -0.419  -15.257 1.00 12.65 ? 259 SER A CB  1 
ATOM   2136 O  OG  . SER A 1 258 ? -9.237  -1.436  -15.279 1.00 12.33 ? 259 SER A OG  1 
ATOM   2137 N  N   . PHE A 1 259 ? -12.004 -3.123  -16.452 1.00 14.26 ? 260 PHE A N   1 
ATOM   2138 C  CA  . PHE A 1 259 ? -11.782 -4.152  -17.463 1.00 15.50 ? 260 PHE A CA  1 
ATOM   2139 C  C   . PHE A 1 259 ? -12.982 -5.113  -17.386 1.00 16.72 ? 260 PHE A C   1 
ATOM   2140 O  O   . PHE A 1 259 ? -13.669 -5.233  -16.326 1.00 17.99 ? 260 PHE A O   1 
ATOM   2141 C  CB  . PHE A 1 259 ? -10.477 -4.903  -17.199 1.00 14.58 ? 260 PHE A CB  1 
ATOM   2142 C  CG  . PHE A 1 259 ? -10.485 -5.650  -15.866 1.00 13.36 ? 260 PHE A CG  1 
ATOM   2143 C  CD1 . PHE A 1 259 ? -10.201 -4.963  -14.666 1.00 13.23 ? 260 PHE A CD1 1 
ATOM   2144 C  CD2 . PHE A 1 259 ? -10.915 -6.977  -15.815 1.00 16.81 ? 260 PHE A CD2 1 
ATOM   2145 C  CE1 . PHE A 1 259 ? -10.270 -5.634  -13.440 1.00 15.40 ? 260 PHE A CE1 1 
ATOM   2146 C  CE2 . PHE A 1 259 ? -11.025 -7.644  -14.589 1.00 19.73 ? 260 PHE A CE2 1 
ATOM   2147 C  CZ  . PHE A 1 259 ? -10.674 -6.967  -13.401 1.00 20.02 ? 260 PHE A CZ  1 
ATOM   2148 N  N   . LYS A 1 260 ? -13.164 -5.821  -18.506 1.00 27.95 ? 261 LYS A N   1 
ATOM   2149 C  CA  . LYS A 1 260 ? -14.249 -6.792  -18.833 1.00 33.09 ? 261 LYS A CA  1 
ATOM   2150 C  C   . LYS A 1 260 ? -15.589 -6.086  -19.091 1.00 50.36 ? 261 LYS A C   1 
ATOM   2151 O  O   . LYS A 1 260 ? -15.981 -5.856  -20.240 1.00 64.44 ? 261 LYS A O   1 
ATOM   2152 C  CB  . LYS A 1 260 ? -14.398 -7.907  -17.795 1.00 36.77 ? 261 LYS A CB  1 
ATOM   2153 C  CG  . LYS A 1 260 ? -13.687 -9.143  -18.259 1.00 50.35 ? 261 LYS A CG  1 
ATOM   2154 C  CD  . LYS A 1 260 ? -12.206 -8.877  -18.174 1.00 33.54 ? 261 LYS A CD  1 
ATOM   2155 C  CE  . LYS A 1 260 ? -11.444 -10.155 -17.879 1.00 39.17 ? 261 LYS A CE  1 
ATOM   2156 N  NZ  . LYS A 1 260 ? -11.546 -10.591 -16.454 1.00 34.11 ? 261 LYS A NZ  1 
ATOM   2157 N  N   . HIS B 1 3   ? -12.893 1.781   65.430  1.00 30.03 ? 3   HIS B N   1 
ATOM   2158 C  CA  . HIS B 1 3   ? -13.775 0.747   64.725  1.00 35.74 ? 3   HIS B CA  1 
ATOM   2159 C  C   . HIS B 1 3   ? -14.326 1.255   63.391  1.00 39.74 ? 3   HIS B C   1 
ATOM   2160 O  O   . HIS B 1 3   ? -15.561 1.439   63.212  1.00 45.52 ? 3   HIS B O   1 
ATOM   2161 C  CB  . HIS B 1 3   ? -14.901 0.254   65.638  1.00 33.25 ? 3   HIS B CB  1 
ATOM   2162 C  CG  . HIS B 1 3   ? -15.844 -0.710  64.963  1.00 63.72 ? 3   HIS B CG  1 
ATOM   2163 N  ND1 . HIS B 1 3   ? -15.804 -2.052  65.178  1.00 58.60 ? 3   HIS B ND1 1 
ATOM   2164 C  CD2 . HIS B 1 3   ? -16.888 -0.496  64.020  1.00 44.81 ? 3   HIS B CD2 1 
ATOM   2165 C  CE1 . HIS B 1 3   ? -16.756 -2.661  64.420  1.00 80.23 ? 3   HIS B CE1 1 
ATOM   2166 N  NE2 . HIS B 1 3   ? -17.409 -1.710  63.710  1.00 68.38 ? 3   HIS B NE2 1 
ATOM   2167 N  N   . HIS B 1 4   ? -13.432 1.522   62.430  1.00 32.26 ? 4   HIS B N   1 
ATOM   2168 C  CA  . HIS B 1 4   ? -13.949 2.036   61.173  1.00 31.15 ? 4   HIS B CA  1 
ATOM   2169 C  C   . HIS B 1 4   ? -14.199 0.925   60.218  1.00 20.66 ? 4   HIS B C   1 
ATOM   2170 O  O   . HIS B 1 4   ? -13.885 -0.275  60.423  1.00 20.16 ? 4   HIS B O   1 
ATOM   2171 C  CB  . HIS B 1 4   ? -13.165 3.205   60.562  1.00 37.83 ? 4   HIS B CB  1 
ATOM   2172 C  CG  . HIS B 1 4   ? -11.645 3.065   60.639  1.00 53.70 ? 4   HIS B CG  1 
ATOM   2173 N  ND1 . HIS B 1 4   ? -11.001 1.886   60.426  1.00 48.47 ? 4   HIS B ND1 1 
ATOM   2174 C  CD2 . HIS B 1 4   ? -10.640 4.022   60.908  1.00 67.32 ? 4   HIS B CD2 1 
ATOM   2175 C  CE1 . HIS B 1 4   ? -9.657  2.076   60.562  1.00 83.39 ? 4   HIS B CE1 1 
ATOM   2176 N  NE2 . HIS B 1 4   ? -9.442  3.382   60.855  1.00 76.20 ? 4   HIS B NE2 1 
ATOM   2177 N  N   . TRP B 1 5   ? -14.692 1.347   59.079  1.00 17.67 ? 5   TRP B N   1 
ATOM   2178 C  CA  . TRP B 1 5   ? -15.248 0.400   58.128  1.00 13.72 ? 5   TRP B CA  1 
ATOM   2179 C  C   . TRP B 1 5   ? -14.181 -0.377  57.414  1.00 14.21 ? 5   TRP B C   1 
ATOM   2180 O  O   . TRP B 1 5   ? -13.053 0.089   57.220  1.00 15.26 ? 5   TRP B O   1 
ATOM   2181 C  CB  . TRP B 1 5   ? -16.199 1.116   57.144  1.00 15.38 ? 5   TRP B CB  1 
ATOM   2182 C  CG  . TRP B 1 5   ? -15.511 1.964   56.106  1.00 14.84 ? 5   TRP B CG  1 
ATOM   2183 C  CD1 . TRP B 1 5   ? -15.166 3.303   56.189  1.00 16.09 ? 5   TRP B CD1 1 
ATOM   2184 C  CD2 . TRP B 1 5   ? -15.010 1.494   54.824  1.00 12.94 ? 5   TRP B CD2 1 
ATOM   2185 N  NE1 . TRP B 1 5   ? -14.501 3.713   55.087  1.00 14.31 ? 5   TRP B NE1 1 
ATOM   2186 C  CE2 . TRP B 1 5   ? -14.430 2.654   54.170  1.00 13.65 ? 5   TRP B CE2 1 
ATOM   2187 C  CE3 . TRP B 1 5   ? -15.067 0.272   54.139  1.00 11.48 ? 5   TRP B CE3 1 
ATOM   2188 C  CZ2 . TRP B 1 5   ? -13.861 2.573   52.904  1.00 14.11 ? 5   TRP B CZ2 1 
ATOM   2189 C  CZ3 . TRP B 1 5   ? -14.475 0.241   52.841  1.00 11.83 ? 5   TRP B CZ3 1 
ATOM   2190 C  CH2 . TRP B 1 5   ? -13.914 1.360   52.271  1.00 13.38 ? 5   TRP B CH2 1 
ATOM   2191 N  N   . GLY B 1 6   ? -14.573 -1.586  56.987  1.00 13.25 ? 6   GLY B N   1 
ATOM   2192 C  CA  . GLY B 1 6   ? -13.603 -2.393  56.142  1.00 12.84 ? 6   GLY B CA  1 
ATOM   2193 C  C   . GLY B 1 6   ? -14.387 -3.544  55.546  1.00 13.14 ? 6   GLY B C   1 
ATOM   2194 O  O   . GLY B 1 6   ? -15.591 -3.402  55.211  1.00 12.87 ? 6   GLY B O   1 
ATOM   2195 N  N   . TYR B 1 7   ? -13.692 -4.686  55.416  1.00 12.39 ? 7   TYR B N   1 
ATOM   2196 C  CA  . TYR B 1 7   ? -14.336 -5.844  54.784  1.00 13.44 ? 7   TYR B CA  1 
ATOM   2197 C  C   . TYR B 1 7   ? -14.512 -7.082  55.682  1.00 23.46 ? 7   TYR B C   1 
ATOM   2198 O  O   . TYR B 1 7   ? -15.207 -8.091  55.230  1.00 27.71 ? 7   TYR B O   1 
ATOM   2199 C  CB  . TYR B 1 7   ? -13.614 -6.158  53.487  1.00 13.85 ? 7   TYR B CB  1 
ATOM   2200 C  CG  . TYR B 1 7   ? -13.890 -5.040  52.474  1.00 10.15 ? 7   TYR B CG  1 
ATOM   2201 C  CD1 . TYR B 1 7   ? -15.062 -5.063  51.696  1.00 10.80 ? 7   TYR B CD1 1 
ATOM   2202 C  CD2 . TYR B 1 7   ? -12.953 -4.025  52.285  1.00 11.38 ? 7   TYR B CD2 1 
ATOM   2203 C  CE1 . TYR B 1 7   ? -15.228 -4.061  50.721  1.00 9.85  ? 7   TYR B CE1 1 
ATOM   2204 C  CE2 . TYR B 1 7   ? -13.158 -3.024  51.298  1.00 10.40 ? 7   TYR B CE2 1 
ATOM   2205 C  CZ  . TYR B 1 7   ? -14.313 -3.050  50.532  1.00 10.02 ? 7   TYR B CZ  1 
ATOM   2206 O  OH  . TYR B 1 7   ? -14.494 -2.115  49.560  1.00 11.21 ? 7   TYR B OH  1 
ATOM   2207 N  N   . GLY B 1 8   ? -14.045 -6.950  56.954  1.00 19.64 ? 8   GLY B N   1 
ATOM   2208 C  CA  . GLY B 1 8   ? -14.054 -8.084  57.957  1.00 20.62 ? 8   GLY B CA  1 
ATOM   2209 C  C   . GLY B 1 8   ? -15.443 -8.431  58.503  1.00 23.48 ? 8   GLY B C   1 
ATOM   2210 O  O   . GLY B 1 8   ? -16.476 -7.764  58.290  1.00 23.74 ? 8   GLY B O   1 
ATOM   2211 N  N   . LYS B 1 9   ? -15.435 -9.393  59.455  1.00 32.47 ? 9   LYS B N   1 
ATOM   2212 C  CA  . LYS B 1 9   ? -16.718 -9.832  60.096  1.00 36.34 ? 9   LYS B CA  1 
ATOM   2213 C  C   . LYS B 1 9   ? -17.338 -8.696  60.871  1.00 26.00 ? 9   LYS B C   1 
ATOM   2214 O  O   . LYS B 1 9   ? -18.609 -8.463  60.891  1.00 25.65 ? 9   LYS B O   1 
ATOM   2215 C  CB  . LYS B 1 9   ? -16.507 -10.997 61.061  1.00 40.48 ? 9   LYS B CB  1 
ATOM   2216 C  CG  . LYS B 1 9   ? -17.769 -11.336 61.856  1.00 26.48 ? 9   LYS B CG  1 
ATOM   2217 N  N   . HIS B 1 10  ? -16.432 -7.930  61.462  1.00 21.16 ? 10  HIS B N   1 
ATOM   2218 C  CA  . HIS B 1 10  ? -16.939 -6.955  62.380  1.00 20.42 ? 10  HIS B CA  1 
ATOM   2219 C  C   . HIS B 1 10  ? -17.223 -5.593  61.829  1.00 18.02 ? 10  HIS B C   1 
ATOM   2220 O  O   . HIS B 1 10  ? -17.970 -4.841  62.447  1.00 22.18 ? 10  HIS B O   1 
ATOM   2221 C  CB  . HIS B 1 10  ? -16.019 -6.925  63.577  1.00 19.10 ? 10  HIS B CB  1 
ATOM   2222 C  CG  . HIS B 1 10  ? -15.860 -8.332  64.220  1.00 20.45 ? 10  HIS B CG  1 
ATOM   2223 N  ND1 . HIS B 1 10  ? -16.872 -8.900  64.903  1.00 21.35 ? 10  HIS B ND1 1 
ATOM   2224 C  CD2 . HIS B 1 10  ? -14.761 -9.244  64.270  1.00 21.09 ? 10  HIS B CD2 1 
ATOM   2225 C  CE1 . HIS B 1 10  ? -16.527 -10.137 65.317  1.00 19.13 ? 10  HIS B CE1 1 
ATOM   2226 N  NE2 . HIS B 1 10  ? -15.190 -10.352 64.946  1.00 21.17 ? 10  HIS B NE2 1 
ATOM   2227 N  N   . ASN B 1 11  ? -16.735 -5.335  60.607  1.00 16.24 ? 11  ASN B N   1 
ATOM   2228 C  CA  . ASN B 1 11  ? -16.772 -3.960  60.064  1.00 16.82 ? 11  ASN B CA  1 
ATOM   2229 C  C   . ASN B 1 11  ? -17.106 -3.942  58.571  1.00 14.39 ? 11  ASN B C   1 
ATOM   2230 O  O   . ASN B 1 11  ? -16.962 -2.869  57.966  1.00 14.83 ? 11  ASN B O   1 
ATOM   2231 C  CB  . ASN B 1 11  ? -15.443 -3.245  60.320  1.00 16.33 ? 11  ASN B CB  1 
ATOM   2232 C  CG  . ASN B 1 11  ? -14.289 -3.822  59.562  1.00 16.22 ? 11  ASN B CG  1 
ATOM   2233 O  OD1 . ASN B 1 11  ? -14.375 -4.870  58.923  1.00 18.08 ? 11  ASN B OD1 1 
ATOM   2234 N  ND2 . ASN B 1 11  ? -13.165 -3.200  59.695  1.00 18.73 ? 11  ASN B ND2 1 
ATOM   2235 N  N   . GLY B 1 12  ? -17.556 -5.070  58.038  1.00 13.93 ? 12  GLY B N   1 
ATOM   2236 C  CA  . GLY B 1 12  ? -17.782 -5.218  56.577  1.00 12.91 ? 12  GLY B CA  1 
ATOM   2237 C  C   . GLY B 1 12  ? -19.098 -4.714  56.175  1.00 12.47 ? 12  GLY B C   1 
ATOM   2238 O  O   . GLY B 1 12  ? -19.842 -4.012  56.887  1.00 12.65 ? 12  GLY B O   1 
ATOM   2239 N  N   . PRO B 1 13  ? -19.431 -5.002  54.883  1.00 12.26 ? 13  PRO B N   1 
ATOM   2240 C  CA  . PRO B 1 13  ? -20.607 -4.432  54.241  1.00 12.02 ? 13  PRO B CA  1 
ATOM   2241 C  C   . PRO B 1 13  ? -21.897 -4.448  55.018  1.00 11.89 ? 13  PRO B C   1 
ATOM   2242 O  O   . PRO B 1 13  ? -22.673 -3.474  54.941  1.00 13.47 ? 13  PRO B O   1 
ATOM   2243 C  CB  . PRO B 1 13  ? -20.691 -5.242  52.900  1.00 12.34 ? 13  PRO B CB  1 
ATOM   2244 C  CG  . PRO B 1 13  ? -19.248 -5.509  52.604  1.00 14.49 ? 13  PRO B CG  1 
ATOM   2245 C  CD  . PRO B 1 13  ? -18.580 -5.747  53.947  1.00 12.83 ? 13  PRO B CD  1 
ATOM   2246 N  N   A GLU B 1 14  ? -22.113 -5.540  55.748  0.50 12.24 ? 14  GLU B N   1 
ATOM   2247 N  N   B GLU B 1 14  ? -22.230 -5.500  55.791  0.50 13.68 ? 14  GLU B N   1 
ATOM   2248 C  CA  A GLU B 1 14  ? -23.310 -5.643  56.530  0.50 13.79 ? 14  GLU B CA  1 
ATOM   2249 C  CA  B GLU B 1 14  ? -23.541 -5.469  56.538  0.50 16.01 ? 14  GLU B CA  1 
ATOM   2250 C  C   A GLU B 1 14  ? -23.460 -4.629  57.696  0.50 12.73 ? 14  GLU B C   1 
ATOM   2251 C  C   B GLU B 1 14  ? -23.529 -4.474  57.742  0.50 13.89 ? 14  GLU B C   1 
ATOM   2252 O  O   A GLU B 1 14  ? -24.587 -4.513  58.231  0.50 13.86 ? 14  GLU B O   1 
ATOM   2253 O  O   B GLU B 1 14  ? -24.579 -4.196  58.362  0.50 18.92 ? 14  GLU B O   1 
ATOM   2254 C  CB  A GLU B 1 14  ? -23.486 -7.096  56.953  0.50 14.25 ? 14  GLU B CB  1 
ATOM   2255 C  CB  B GLU B 1 14  ? -23.971 -6.858  57.021  0.50 19.06 ? 14  GLU B CB  1 
ATOM   2256 C  CG  A GLU B 1 14  ? -22.555 -7.592  58.002  0.50 15.20 ? 14  GLU B CG  1 
ATOM   2257 C  CG  B GLU B 1 14  ? -23.810 -7.957  55.953  0.50 19.54 ? 14  GLU B CG  1 
ATOM   2258 C  CD  A GLU B 1 14  ? -21.223 -8.072  57.462  0.50 15.09 ? 14  GLU B CD  1 
ATOM   2259 C  CD  B GLU B 1 14  ? -24.688 -7.744  54.733  0.50 22.11 ? 14  GLU B CD  1 
ATOM   2260 O  OE1 A GLU B 1 14  ? -20.838 -7.645  56.358  0.50 13.62 ? 14  GLU B OE1 1 
ATOM   2261 O  OE1 B GLU B 1 14  ? -25.914 -7.592  54.903  0.50 27.73 ? 14  GLU B OE1 1 
ATOM   2262 O  OE2 A GLU B 1 14  ? -20.565 -8.884  58.139  0.50 18.88 ? 14  GLU B OE2 1 
ATOM   2263 O  OE2 B GLU B 1 14  ? -24.144 -7.730  53.611  0.50 22.36 ? 14  GLU B OE2 1 
ATOM   2264 N  N   . HIS B 1 15  ? -22.365 -3.950  58.062  1.00 11.70 ? 15  HIS B N   1 
ATOM   2265 C  CA  . HIS B 1 15  ? -22.252 -2.990  59.184  1.00 11.52 ? 15  HIS B CA  1 
ATOM   2266 C  C   . HIS B 1 15  ? -22.306 -1.574  58.698  1.00 11.60 ? 15  HIS B C   1 
ATOM   2267 O  O   . HIS B 1 15  ? -22.552 -0.642  59.478  1.00 12.88 ? 15  HIS B O   1 
ATOM   2268 C  CB  . HIS B 1 15  ? -20.949 -3.187  59.944  1.00 13.70 ? 15  HIS B CB  1 
ATOM   2269 C  CG  . HIS B 1 15  ? -20.942 -4.487  60.683  1.00 15.77 ? 15  HIS B CG  1 
ATOM   2270 N  ND1 . HIS B 1 15  ? -21.492 -4.620  61.972  1.00 19.97 ? 15  HIS B ND1 1 
ATOM   2271 C  CD2 . HIS B 1 15  ? -20.433 -5.733  60.313  1.00 16.50 ? 15  HIS B CD2 1 
ATOM   2272 C  CE1 . HIS B 1 15  ? -21.353 -5.908  62.332  1.00 21.60 ? 15  HIS B CE1 1 
ATOM   2273 N  NE2 . HIS B 1 15  ? -20.698 -6.586  61.365  1.00 20.74 ? 15  HIS B NE2 1 
ATOM   2274 N  N   . TRP B 1 16  ? -22.036 -1.316  57.384  1.00 10.48 ? 16  TRP B N   1 
ATOM   2275 C  CA  . TRP B 1 16  ? -21.788 0.012   56.898  1.00 10.98 ? 16  TRP B CA  1 
ATOM   2276 C  C   . TRP B 1 16  ? -22.948 0.955   57.122  1.00 10.11 ? 16  TRP B C   1 
ATOM   2277 O  O   . TRP B 1 16  ? -22.747 2.198   57.291  1.00 11.88 ? 16  TRP B O   1 
ATOM   2278 C  CB  . TRP B 1 16  ? -21.429 -0.014  55.431  1.00 10.30 ? 16  TRP B CB  1 
ATOM   2279 C  CG  . TRP B 1 16  ? -20.147 -0.719  55.166  1.00 10.04 ? 16  TRP B CG  1 
ATOM   2280 C  CD1 . TRP B 1 16  ? -19.138 -1.154  56.020  1.00 10.53 ? 16  TRP B CD1 1 
ATOM   2281 C  CD2 . TRP B 1 16  ? -19.638 -1.024  53.814  1.00 10.07 ? 16  TRP B CD2 1 
ATOM   2282 N  NE1 . TRP B 1 16  ? -18.116 -1.674  55.356  1.00 10.96 ? 16  TRP B NE1 1 
ATOM   2283 C  CE2 . TRP B 1 16  ? -18.361 -1.627  53.989  1.00 9.92  ? 16  TRP B CE2 1 
ATOM   2284 C  CE3 . TRP B 1 16  ? -20.154 -0.832  52.516  1.00 10.30 ? 16  TRP B CE3 1 
ATOM   2285 C  CZ2 . TRP B 1 16  ? -17.572 -2.064  52.896  1.00 10.14 ? 16  TRP B CZ2 1 
ATOM   2286 C  CZ3 . TRP B 1 16  ? -19.383 -1.294  51.438  1.00 9.87  ? 16  TRP B CZ3 1 
ATOM   2287 C  CH2 . TRP B 1 16  ? -18.093 -1.856  51.619  1.00 10.06 ? 16  TRP B CH2 1 
ATOM   2288 N  N   . HIS B 1 17  ? -24.191 0.462   57.108  1.00 10.99 ? 17  HIS B N   1 
ATOM   2289 C  CA  . HIS B 1 17  ? -25.363 1.319   57.219  1.00 11.22 ? 17  HIS B CA  1 
ATOM   2290 C  C   . HIS B 1 17  ? -25.421 2.110   58.585  1.00 11.97 ? 17  HIS B C   1 
ATOM   2291 O  O   . HIS B 1 17  ? -26.062 3.153   58.615  1.00 13.50 ? 17  HIS B O   1 
ATOM   2292 C  CB  . HIS B 1 17  ? -26.638 0.556   57.048  1.00 12.83 ? 17  HIS B CB  1 
ATOM   2293 C  CG  . HIS B 1 17  ? -26.950 -0.348  58.235  1.00 13.90 ? 17  HIS B CG  1 
ATOM   2294 N  ND1 . HIS B 1 17  ? -27.837 0.038   59.221  1.00 17.46 ? 17  HIS B ND1 1 
ATOM   2295 C  CD2 . HIS B 1 17  ? -26.424 -1.551  58.615  1.00 12.60 ? 17  HIS B CD2 1 
ATOM   2296 C  CE1 . HIS B 1 17  ? -27.856 -0.889  60.177  1.00 19.23 ? 17  HIS B CE1 1 
ATOM   2297 N  NE2 . HIS B 1 17  ? -27.035 -1.877  59.857  1.00 15.16 ? 17  HIS B NE2 1 
ATOM   2298 N  N   . LYS B 1 18  ? -24.679 1.633   59.609  1.00 12.12 ? 18  LYS B N   1 
ATOM   2299 C  CA  . LYS B 1 18  ? -24.739 2.329   60.946  1.00 14.61 ? 18  LYS B CA  1 
ATOM   2300 C  C   . LYS B 1 18  ? -24.046 3.678   60.827  1.00 15.22 ? 18  LYS B C   1 
ATOM   2301 O  O   . LYS B 1 18  ? -24.553 4.690   61.294  1.00 20.60 ? 18  LYS B O   1 
ATOM   2302 C  CB  . LYS B 1 18  ? -24.084 1.414   62.010  1.00 14.46 ? 18  LYS B CB  1 
ATOM   2303 C  CG  . LYS B 1 18  ? -24.950 0.216   62.324  1.00 15.37 ? 18  LYS B CG  1 
ATOM   2304 C  CD  . LYS B 1 18  ? -24.349 -0.762  63.250  1.00 15.81 ? 18  LYS B CD  1 
ATOM   2305 C  CE  . LYS B 1 18  ? -23.394 -1.706  62.579  1.00 15.62 ? 18  LYS B CE  1 
ATOM   2306 N  NZ  . LYS B 1 18  ? -22.615 -2.513  63.532  1.00 16.80 ? 18  LYS B NZ  1 
ATOM   2307 N  N   . ASP B 1 19  ? -22.891 3.724   60.158  1.00 14.76 ? 19  ASP B N   1 
ATOM   2308 C  CA  . ASP B 1 19  ? -22.204 5.024   59.978  1.00 16.03 ? 19  ASP B CA  1 
ATOM   2309 C  C   . ASP B 1 19  ? -22.640 5.775   58.717  1.00 15.99 ? 19  ASP B C   1 
ATOM   2310 O  O   . ASP B 1 19  ? -22.570 6.968   58.629  1.00 16.45 ? 19  ASP B O   1 
ATOM   2311 C  CB  . ASP B 1 19  ? -20.672 4.794   59.943  1.00 16.98 ? 19  ASP B CB  1 
ATOM   2312 C  CG  . ASP B 1 19  ? -20.011 4.774   61.321  1.00 24.64 ? 19  ASP B CG  1 
ATOM   2313 O  OD1 . ASP B 1 19  ? -20.399 5.523   62.273  1.00 25.56 ? 19  ASP B OD1 1 
ATOM   2314 O  OD2 . ASP B 1 19  ? -19.066 3.997   61.433  1.00 42.72 ? 19  ASP B OD2 1 
ATOM   2315 N  N   . PHE B 1 20  ? -23.210 5.063   57.763  1.00 13.61 ? 20  PHE B N   1 
ATOM   2316 C  CA  . PHE B 1 20  ? -23.595 5.590   56.402  1.00 14.10 ? 20  PHE B CA  1 
ATOM   2317 C  C   . PHE B 1 20  ? -24.960 5.056   56.025  1.00 13.79 ? 20  PHE B C   1 
ATOM   2318 O  O   . PHE B 1 20  ? -25.099 4.060   55.306  1.00 13.05 ? 20  PHE B O   1 
ATOM   2319 C  CB  . PHE B 1 20  ? -22.552 5.175   55.363  1.00 12.31 ? 20  PHE B CB  1 
ATOM   2320 C  CG  . PHE B 1 20  ? -21.171 5.569   55.770  1.00 12.95 ? 20  PHE B CG  1 
ATOM   2321 C  CD1 . PHE B 1 20  ? -20.723 6.873   55.556  1.00 16.79 ? 20  PHE B CD1 1 
ATOM   2322 C  CD2 . PHE B 1 20  ? -20.295 4.640   56.433  1.00 15.60 ? 20  PHE B CD2 1 
ATOM   2323 C  CE1 . PHE B 1 20  ? -19.385 7.212   55.961  1.00 15.65 ? 20  PHE B CE1 1 
ATOM   2324 C  CE2 . PHE B 1 20  ? -19.011 4.995   56.873  1.00 18.70 ? 20  PHE B CE2 1 
ATOM   2325 C  CZ  . PHE B 1 20  ? -18.572 6.285   56.604  1.00 15.68 ? 20  PHE B CZ  1 
ATOM   2326 N  N   . PRO B 1 21  ? -26.064 5.648   56.558  1.00 13.59 ? 21  PRO B N   1 
ATOM   2327 C  CA  . PRO B 1 21  ? -27.408 5.154   56.400  1.00 12.78 ? 21  PRO B CA  1 
ATOM   2328 C  C   . PRO B 1 21  ? -27.861 5.066   54.936  1.00 11.65 ? 21  PRO B C   1 
ATOM   2329 O  O   . PRO B 1 21  ? -28.770 4.306   54.626  1.00 13.36 ? 21  PRO B O   1 
ATOM   2330 C  CB  . PRO B 1 21  ? -28.314 6.132   57.214  1.00 18.33 ? 21  PRO B CB  1 
ATOM   2331 C  CG  . PRO B 1 21  ? -27.356 6.810   58.111  1.00 24.07 ? 21  PRO B CG  1 
ATOM   2332 C  CD  . PRO B 1 21  ? -25.942 6.658   57.629  1.00 16.86 ? 21  PRO B CD  1 
ATOM   2333 N  N   . ILE B 1 22  ? -27.172 5.805   54.022  1.00 11.84 ? 22  ILE B N   1 
ATOM   2334 C  CA  . ILE B 1 22  ? -27.493 5.724   52.607  1.00 13.24 ? 22  ILE B CA  1 
ATOM   2335 C  C   . ILE B 1 22  ? -27.195 4.317   52.058  1.00 11.81 ? 22  ILE B C   1 
ATOM   2336 O  O   . ILE B 1 22  ? -27.658 3.988   50.982  1.00 13.05 ? 22  ILE B O   1 
ATOM   2337 C  CB  . ILE B 1 22  ? -26.757 6.834   51.848  1.00 12.60 ? 22  ILE B CB  1 
ATOM   2338 C  CG1 . ILE B 1 22  ? -27.408 7.147   50.506  1.00 13.65 ? 22  ILE B CG1 1 
ATOM   2339 C  CG2 . ILE B 1 22  ? -25.248 6.508   51.694  1.00 12.93 ? 22  ILE B CG2 1 
ATOM   2340 C  CD1 . ILE B 1 22  ? -26.707 8.267   49.770  1.00 16.27 ? 22  ILE B CD1 1 
ATOM   2341 N  N   . ALA B 1 23  ? -26.499 3.482   52.843  1.00 11.30 ? 23  ALA B N   1 
ATOM   2342 C  CA  . ALA B 1 23  ? -26.265 2.078   52.454  1.00 10.85 ? 23  ALA B CA  1 
ATOM   2343 C  C   . ALA B 1 23  ? -27.526 1.374   52.069  1.00 11.62 ? 23  ALA B C   1 
ATOM   2344 O  O   . ALA B 1 23  ? -27.502 0.342   51.363  1.00 12.69 ? 23  ALA B O   1 
ATOM   2345 C  CB  . ALA B 1 23  ? -25.534 1.344   53.595  1.00 11.66 ? 23  ALA B CB  1 
ATOM   2346 N  N   . LYS B 1 24  ? -28.658 1.789   52.679  1.00 12.41 ? 24  LYS B N   1 
ATOM   2347 C  CA  . LYS B 1 24  ? -29.963 1.166   52.408  1.00 12.10 ? 24  LYS B CA  1 
ATOM   2348 C  C   . LYS B 1 24  ? -30.812 2.050   51.514  1.00 14.53 ? 24  LYS B C   1 
ATOM   2349 O  O   . LYS B 1 24  ? -32.076 1.942   51.497  1.00 16.24 ? 24  LYS B O   1 
ATOM   2350 C  CB  . LYS B 1 24  ? -30.776 0.889   53.715  1.00 15.05 ? 24  LYS B CB  1 
ATOM   2351 C  CG  . LYS B 1 24  ? -30.038 -0.030  54.673  1.00 15.75 ? 24  LYS B CG  1 
ATOM   2352 C  CD  . LYS B 1 24  ? -30.955 -0.368  55.849  1.00 20.72 ? 24  LYS B CD  1 
ATOM   2353 C  CE  . LYS B 1 24  ? -30.246 -1.191  56.902  1.00 20.75 ? 24  LYS B CE  1 
ATOM   2354 N  NZ  . LYS B 1 24  ? -30.174 -2.540  56.328  1.00 26.77 ? 24  LYS B NZ  1 
ATOM   2355 N  N   . GLY B 1 25  ? -30.155 2.886   50.689  1.00 13.08 ? 25  GLY B N   1 
ATOM   2356 C  CA  . GLY B 1 25  ? -30.747 3.927   49.856  1.00 13.92 ? 25  GLY B CA  1 
ATOM   2357 C  C   . GLY B 1 25  ? -31.449 3.311   48.633  1.00 12.69 ? 25  GLY B C   1 
ATOM   2358 O  O   . GLY B 1 25  ? -31.523 2.087   48.387  1.00 13.76 ? 25  GLY B O   1 
ATOM   2359 N  N   . GLU B 1 26  ? -31.935 4.220   47.788  1.00 13.55 ? 26  GLU B N   1 
ATOM   2360 C  CA  . GLU B 1 26  ? -32.692 3.858   46.586  1.00 14.11 ? 26  GLU B CA  1 
ATOM   2361 C  C   . GLU B 1 26  ? -31.874 3.567   45.339  1.00 12.83 ? 26  GLU B C   1 
ATOM   2362 O  O   . GLU B 1 26  ? -32.442 3.060   44.347  1.00 13.42 ? 26  GLU B O   1 
ATOM   2363 C  CB  . GLU B 1 26  ? -33.697 5.022   46.264  1.00 15.16 ? 26  GLU B CB  1 
ATOM   2364 C  CG  . GLU B 1 26  ? -34.724 5.246   47.396  1.00 17.27 ? 26  GLU B CG  1 
ATOM   2365 C  CD  . GLU B 1 26  ? -35.531 3.935   47.754  1.00 25.31 ? 26  GLU B CD  1 
ATOM   2366 O  OE1 . GLU B 1 26  ? -36.072 3.221   46.825  1.00 32.60 ? 26  GLU B OE1 1 
ATOM   2367 O  OE2 . GLU B 1 26  ? -35.621 3.560   48.963  1.00 37.44 ? 26  GLU B OE2 1 
ATOM   2368 N  N   . ARG B 1 27  ? -30.580 3.882   45.334  1.00 11.33 ? 27  ARG B N   1 
ATOM   2369 C  CA  . ARG B 1 27  ? -29.765 3.639   44.116  1.00 9.88  ? 27  ARG B CA  1 
ATOM   2370 C  C   . ARG B 1 27  ? -28.360 3.190   44.512  1.00 9.82  ? 27  ARG B C   1 
ATOM   2371 O  O   . ARG B 1 27  ? -27.366 3.798   44.114  1.00 10.78 ? 27  ARG B O   1 
ATOM   2372 C  CB  . ARG B 1 27  ? -29.779 4.852   43.109  1.00 12.91 ? 27  ARG B CB  1 
ATOM   2373 C  CG  . ARG B 1 27  ? -29.397 6.159   43.784  1.00 15.39 ? 27  ARG B CG  1 
ATOM   2374 C  CD  . ARG B 1 27  ? -29.215 7.339   42.771  1.00 16.60 ? 27  ARG B CD  1 
ATOM   2375 N  NE  . ARG B 1 27  ? -27.994 7.246   41.967  1.00 15.87 ? 27  ARG B NE  1 
ATOM   2376 C  CZ  . ARG B 1 27  ? -27.569 8.194   41.134  1.00 14.81 ? 27  ARG B CZ  1 
ATOM   2377 N  NH1 . ARG B 1 27  ? -28.264 9.315   40.989  1.00 16.27 ? 27  ARG B NH1 1 
ATOM   2378 N  NH2 . ARG B 1 27  ? -26.450 8.024   40.441  1.00 13.87 ? 27  ARG B NH2 1 
ATOM   2379 N  N   . GLN B 1 28  ? -28.314 2.097   45.306  1.00 9.68  ? 28  GLN B N   1 
ATOM   2380 C  CA  . GLN B 1 28  ? -27.007 1.571   45.785  1.00 9.79  ? 28  GLN B CA  1 
ATOM   2381 C  C   . GLN B 1 28  ? -26.408 0.579   44.769  1.00 8.11  ? 28  GLN B C   1 
ATOM   2382 O  O   . GLN B 1 28  ? -27.101 -0.074  43.978  1.00 8.69  ? 28  GLN B O   1 
ATOM   2383 C  CB  . GLN B 1 28  ? -27.233 0.877   47.157  1.00 9.74  ? 28  GLN B CB  1 
ATOM   2384 C  CG  . GLN B 1 28  ? -27.524 1.956   48.233  1.00 10.65 ? 28  GLN B CG  1 
ATOM   2385 C  CD  . GLN B 1 28  ? -26.268 2.762   48.546  1.00 9.24  ? 28  GLN B CD  1 
ATOM   2386 O  OE1 . GLN B 1 28  ? -25.306 2.181   49.036  1.00 9.72  ? 28  GLN B OE1 1 
ATOM   2387 N  NE2 . GLN B 1 28  ? -26.200 4.057   48.158  1.00 9.67  ? 28  GLN B NE2 1 
ATOM   2388 N  N   . SER B 1 29  ? -25.084 0.525   44.823  1.00 7.86  ? 29  SER B N   1 
ATOM   2389 C  CA  . SER B 1 29  ? -24.302 -0.369  43.942  1.00 7.75  ? 29  SER B CA  1 
ATOM   2390 C  C   . SER B 1 29  ? -23.400 -1.243  44.809  1.00 7.83  ? 29  SER B C   1 
ATOM   2391 O  O   . SER B 1 29  ? -23.080 -0.903  45.947  1.00 8.75  ? 29  SER B O   1 
ATOM   2392 C  CB  . SER B 1 29  ? -23.409 0.477   43.060  1.00 8.40  ? 29  SER B CB  1 
ATOM   2393 O  OG  . SER B 1 29  ? -24.203 1.222   42.105  1.00 8.95  ? 29  SER B OG  1 
ATOM   2394 N  N   . PRO B 1 30  ? -22.950 -2.369  44.284  1.00 7.31  ? 30  PRO B N   1 
ATOM   2395 C  CA  . PRO B 1 30  ? -23.263 -2.912  42.950  1.00 7.90  ? 30  PRO B CA  1 
ATOM   2396 C  C   . PRO B 1 30  ? -24.642 -3.572  42.914  1.00 7.76  ? 30  PRO B C   1 
ATOM   2397 O  O   . PRO B 1 30  ? -25.321 -3.622  43.929  1.00 8.16  ? 30  PRO B O   1 
ATOM   2398 C  CB  . PRO B 1 30  ? -22.165 -3.947  42.747  1.00 7.63  ? 30  PRO B CB  1 
ATOM   2399 C  CG  . PRO B 1 30  ? -22.047 -4.540  44.132  1.00 7.78  ? 30  PRO B CG  1 
ATOM   2400 C  CD  . PRO B 1 30  ? -22.102 -3.307  45.074  1.00 8.58  ? 30  PRO B CD  1 
ATOM   2401 N  N   . VAL B 1 31  ? -24.945 -4.136  41.762  1.00 7.88  ? 31  VAL B N   1 
ATOM   2402 C  CA  . VAL B 1 31  ? -26.154 -4.914  41.510  1.00 8.90  ? 31  VAL B CA  1 
ATOM   2403 C  C   . VAL B 1 31  ? -25.846 -6.116  40.712  1.00 8.29  ? 31  VAL B C   1 
ATOM   2404 O  O   . VAL B 1 31  ? -24.838 -6.165  40.029  1.00 9.55  ? 31  VAL B O   1 
ATOM   2405 C  CB  . VAL B 1 31  ? -27.304 -4.074  40.805  1.00 9.15  ? 31  VAL B CB  1 
ATOM   2406 C  CG1 . VAL B 1 31  ? -27.661 -2.858  41.656  1.00 11.65 ? 31  VAL B CG1 1 
ATOM   2407 C  CG2 . VAL B 1 31  ? -26.852 -3.672  39.396  1.00 10.09 ? 31  VAL B CG2 1 
ATOM   2408 N  N   . ASP B 1 32  ? -26.760 -7.100  40.768  1.00 8.71  ? 32  ASP B N   1 
ATOM   2409 C  CA  . ASP B 1 32  ? -26.757 -8.169  39.787  1.00 10.11 ? 32  ASP B CA  1 
ATOM   2410 C  C   . ASP B 1 32  ? -27.338 -7.678  38.495  1.00 8.32  ? 32  ASP B C   1 
ATOM   2411 O  O   . ASP B 1 32  ? -28.392 -7.024  38.464  1.00 10.64 ? 32  ASP B O   1 
ATOM   2412 C  CB  . ASP B 1 32  ? -27.571 -9.342  40.331  1.00 10.10 ? 32  ASP B CB  1 
ATOM   2413 C  CG  . ASP B 1 32  ? -27.531 -10.529 39.353  1.00 11.50 ? 32  ASP B CG  1 
ATOM   2414 O  OD1 . ASP B 1 32  ? -26.437 -10.969 38.900  1.00 10.25 ? 32  ASP B OD1 1 
ATOM   2415 O  OD2 . ASP B 1 32  ? -28.623 -10.999 38.909  1.00 13.32 ? 32  ASP B OD2 1 
ATOM   2416 N  N   . ILE B 1 33  ? -26.655 -7.980  37.394  1.00 8.62  ? 33  ILE B N   1 
ATOM   2417 C  CA  . ILE B 1 33  ? -27.123 -7.572  36.065  1.00 9.63  ? 33  ILE B CA  1 
ATOM   2418 C  C   . ILE B 1 33  ? -27.842 -8.803  35.532  1.00 10.81 ? 33  ILE B C   1 
ATOM   2419 O  O   . ILE B 1 33  ? -27.224 -9.774  35.121  1.00 11.35 ? 33  ILE B O   1 
ATOM   2420 C  CB  . ILE B 1 33  ? -25.972 -7.134  35.157  1.00 10.59 ? 33  ILE B CB  1 
ATOM   2421 C  CG1 . ILE B 1 33  ? -25.248 -5.907  35.794  1.00 9.80  ? 33  ILE B CG1 1 
ATOM   2422 C  CG2 . ILE B 1 33  ? -26.442 -6.866  33.738  1.00 11.15 ? 33  ILE B CG2 1 
ATOM   2423 C  CD1 . ILE B 1 33  ? -23.891 -5.586  35.102  1.00 12.94 ? 33  ILE B CD1 1 
ATOM   2424 N  N   . ASP B 1 34  ? -29.172 -8.724  35.517  1.00 12.43 ? 34  ASP B N   1 
ATOM   2425 C  CA  . ASP B 1 34  ? -30.020 -9.801  34.931  1.00 14.32 ? 34  ASP B CA  1 
ATOM   2426 C  C   . ASP B 1 34  ? -30.028 -9.497  33.427  1.00 12.79 ? 34  ASP B C   1 
ATOM   2427 O  O   . ASP B 1 34  ? -30.660 -8.514  32.965  1.00 13.97 ? 34  ASP B O   1 
ATOM   2428 C  CB  . ASP B 1 34  ? -31.429 -9.780  35.580  1.00 14.16 ? 34  ASP B CB  1 
ATOM   2429 C  CG  . ASP B 1 34  ? -32.377 -10.832 34.968  1.00 18.94 ? 34  ASP B CG  1 
ATOM   2430 O  OD1 . ASP B 1 34  ? -32.220 -11.173 33.822  1.00 18.87 ? 34  ASP B OD1 1 
ATOM   2431 O  OD2 . ASP B 1 34  ? -33.344 -11.277 35.649  1.00 25.63 ? 34  ASP B OD2 1 
ATOM   2432 N  N   . THR B 1 35  ? -29.290 -10.276 32.667  1.00 13.25 ? 35  THR B N   1 
ATOM   2433 C  CA  . THR B 1 35  ? -29.082 -9.913  31.271  1.00 14.92 ? 35  THR B CA  1 
ATOM   2434 C  C   . THR B 1 35  ? -30.330 -10.089 30.441  1.00 17.29 ? 35  THR B C   1 
ATOM   2435 O  O   . THR B 1 35  ? -30.419 -9.483  29.345  1.00 17.05 ? 35  THR B O   1 
ATOM   2436 C  CB  . THR B 1 35  ? -28.004 -10.781 30.637  1.00 13.23 ? 35  THR B CB  1 
ATOM   2437 O  OG1 . THR B 1 35  ? -28.420 -12.167 30.583  1.00 16.08 ? 35  THR B OG1 1 
ATOM   2438 C  CG2 . THR B 1 35  ? -26.668 -10.652 31.365  1.00 17.00 ? 35  THR B CG2 1 
ATOM   2439 N  N   . HIS B 1 36  ? -31.323 -10.822 30.963  1.00 18.69 ? 36  HIS B N   1 
ATOM   2440 C  CA  . HIS B 1 36  ? -32.675 -11.017 30.306  1.00 16.92 ? 36  HIS B CA  1 
ATOM   2441 C  C   . HIS B 1 36  ? -33.710 -9.988  30.655  1.00 21.74 ? 36  HIS B C   1 
ATOM   2442 O  O   . HIS B 1 36  ? -34.798 -9.905  30.043  1.00 28.21 ? 36  HIS B O   1 
ATOM   2443 C  CB  . HIS B 1 36  ? -33.223 -12.333 30.764  1.00 18.31 ? 36  HIS B CB  1 
ATOM   2444 C  CG  . HIS B 1 36  ? -32.296 -13.413 30.485  1.00 22.62 ? 36  HIS B CG  1 
ATOM   2445 N  ND1 . HIS B 1 36  ? -31.574 -14.078 31.490  1.00 29.56 ? 36  HIS B ND1 1 
ATOM   2446 C  CD2 . HIS B 1 36  ? -31.824 -13.884 29.289  1.00 17.98 ? 36  HIS B CD2 1 
ATOM   2447 C  CE1 . HIS B 1 36  ? -30.762 -14.985 30.893  1.00 19.47 ? 36  HIS B CE1 1 
ATOM   2448 N  NE2 . HIS B 1 36  ? -30.910 -14.875 29.578  1.00 20.91 ? 36  HIS B NE2 1 
ATOM   2449 N  N   . THR B 1 37  ? -33.452 -9.169  31.633  1.00 19.14 ? 37  THR B N   1 
ATOM   2450 C  CA  . THR B 1 37  ? -34.366 -8.083  31.823  1.00 17.84 ? 37  THR B CA  1 
ATOM   2451 C  C   . THR B 1 37  ? -33.727 -6.714  31.453  1.00 19.41 ? 37  THR B C   1 
ATOM   2452 O  O   . THR B 1 37  ? -34.456 -5.700  31.456  1.00 22.02 ? 37  THR B O   1 
ATOM   2453 C  CB  . THR B 1 37  ? -35.056 -8.124  33.199  1.00 28.66 ? 37  THR B CB  1 
ATOM   2454 O  OG1 . THR B 1 37  ? -34.105 -7.951  34.200  1.00 33.57 ? 37  THR B OG1 1 
ATOM   2455 C  CG2 . THR B 1 37  ? -35.732 -9.490  33.460  1.00 25.60 ? 37  THR B CG2 1 
ATOM   2456 N  N   . ALA B 1 38  ? -32.418 -6.687  31.139  1.00 15.75 ? 38  ALA B N   1 
ATOM   2457 C  CA  . ALA B 1 38  ? -31.798 -5.466  30.709  1.00 16.73 ? 38  ALA B CA  1 
ATOM   2458 C  C   . ALA B 1 38  ? -32.393 -5.070  29.389  1.00 17.28 ? 38  ALA B C   1 
ATOM   2459 O  O   . ALA B 1 38  ? -32.608 -5.905  28.515  1.00 20.08 ? 38  ALA B O   1 
ATOM   2460 C  CB  . ALA B 1 38  ? -30.278 -5.638  30.606  1.00 16.68 ? 38  ALA B CB  1 
ATOM   2461 N  N   . LYS B 1 39  ? -32.689 -3.797  29.254  1.00 15.88 ? 39  LYS B N   1 
ATOM   2462 C  CA  . LYS B 1 39  ? -33.289 -3.314  27.989  1.00 17.13 ? 39  LYS B CA  1 
ATOM   2463 C  C   . LYS B 1 39  ? -32.264 -2.813  26.952  1.00 18.29 ? 39  LYS B C   1 
ATOM   2464 O  O   . LYS B 1 39  ? -31.587 -1.823  27.218  1.00 16.39 ? 39  LYS B O   1 
ATOM   2465 C  CB  . LYS B 1 39  ? -34.267 -2.180  28.344  1.00 21.42 ? 39  LYS B CB  1 
ATOM   2466 C  CG  . LYS B 1 39  ? -34.903 -1.380  27.221  1.00 28.14 ? 39  LYS B CG  1 
ATOM   2467 C  CD  . LYS B 1 39  ? -35.923 -2.209  26.445  1.00 23.94 ? 39  LYS B CD  1 
ATOM   2468 C  CE  . LYS B 1 39  ? -36.664 -1.348  25.419  1.00 26.30 ? 39  LYS B CE  1 
ATOM   2469 N  NZ  . LYS B 1 39  ? -37.760 -2.078  24.771  1.00 28.02 ? 39  LYS B NZ  1 
ATOM   2470 N  N   . TYR B 1 40  ? -32.297 -3.351  25.727  1.00 18.18 ? 40  TYR B N   1 
ATOM   2471 C  CA  . TYR B 1 40  ? -31.453 -2.875  24.634  1.00 17.51 ? 40  TYR B CA  1 
ATOM   2472 C  C   . TYR B 1 40  ? -31.923 -1.497  24.308  1.00 15.44 ? 40  TYR B C   1 
ATOM   2473 O  O   . TYR B 1 40  ? -33.128 -1.343  23.955  1.00 19.43 ? 40  TYR B O   1 
ATOM   2474 C  CB  . TYR B 1 40  ? -31.426 -3.826  23.394  1.00 22.73 ? 40  TYR B CB  1 
ATOM   2475 C  CG  . TYR B 1 40  ? -30.845 -3.160  22.192  1.00 21.98 ? 40  TYR B CG  1 
ATOM   2476 C  CD1 . TYR B 1 40  ? -29.512 -2.703  22.198  1.00 21.48 ? 40  TYR B CD1 1 
ATOM   2477 C  CD2 . TYR B 1 40  ? -31.641 -2.947  21.056  1.00 31.07 ? 40  TYR B CD2 1 
ATOM   2478 C  CE1 . TYR B 1 40  ? -28.955 -2.066  21.100  1.00 26.68 ? 40  TYR B CE1 1 
ATOM   2479 C  CE2 . TYR B 1 40  ? -31.102 -2.305  19.934  1.00 33.60 ? 40  TYR B CE2 1 
ATOM   2480 C  CZ  . TYR B 1 40  ? -29.764 -1.861  19.943  1.00 28.90 ? 40  TYR B CZ  1 
ATOM   2481 O  OH  . TYR B 1 40  ? -29.199 -1.223  18.828  1.00 34.35 ? 40  TYR B OH  1 
ATOM   2482 N  N   . ASP B 1 41  ? -31.047 -0.512  24.318  1.00 18.61 ? 41  ASP B N   1 
ATOM   2483 C  CA  . ASP B 1 41  ? -31.471 0.843   23.993  1.00 18.83 ? 41  ASP B CA  1 
ATOM   2484 C  C   . ASP B 1 41  ? -30.709 1.339   22.749  1.00 24.22 ? 41  ASP B C   1 
ATOM   2485 O  O   . ASP B 1 41  ? -29.534 1.693   22.841  1.00 20.69 ? 41  ASP B O   1 
ATOM   2486 C  CB  . ASP B 1 41  ? -31.329 1.768   25.193  1.00 27.74 ? 41  ASP B CB  1 
ATOM   2487 C  CG  . ASP B 1 41  ? -31.804 3.169   24.895  1.00 33.55 ? 41  ASP B CG  1 
ATOM   2488 O  OD1 . ASP B 1 41  ? -32.160 3.422   23.725  1.00 30.55 ? 41  ASP B OD1 1 
ATOM   2489 O  OD2 . ASP B 1 41  ? -31.861 4.016   25.828  1.00 33.91 ? 41  ASP B OD2 1 
ATOM   2490 N  N   . PRO B 1 42  ? -31.363 1.298   21.562  1.00 23.67 ? 42  PRO B N   1 
ATOM   2491 C  CA  . PRO B 1 42  ? -30.696 1.527   20.262  1.00 26.68 ? 42  PRO B CA  1 
ATOM   2492 C  C   . PRO B 1 42  ? -30.282 3.014   20.143  1.00 29.20 ? 42  PRO B C   1 
ATOM   2493 O  O   . PRO B 1 42  ? -29.420 3.386   19.288  1.00 31.89 ? 42  PRO B O   1 
ATOM   2494 C  CB  . PRO B 1 42  ? -31.829 1.175   19.257  1.00 28.50 ? 42  PRO B CB  1 
ATOM   2495 C  CG  . PRO B 1 42  ? -33.078 1.529   20.018  1.00 27.81 ? 42  PRO B CG  1 
ATOM   2496 C  CD  . PRO B 1 42  ? -32.782 0.857   21.337  1.00 27.36 ? 42  PRO B CD  1 
ATOM   2497 N  N   . SER B 1 43  ? -30.856 3.840   21.045  1.00 23.92 ? 43  SER B N   1 
ATOM   2498 C  CA  . SER B 1 43  ? -30.610 5.271   21.090  1.00 29.98 ? 43  SER B CA  1 
ATOM   2499 C  C   . SER B 1 43  ? -29.292 5.620   21.887  1.00 32.12 ? 43  SER B C   1 
ATOM   2500 O  O   . SER B 1 43  ? -28.773 6.780   21.764  1.00 42.13 ? 43  SER B O   1 
ATOM   2501 C  CB  . SER B 1 43  ? -31.826 5.912   21.724  1.00 38.69 ? 43  SER B CB  1 
ATOM   2502 O  OG  . SER B 1 43  ? -31.613 6.181   23.092  1.00 30.85 ? 43  SER B OG  1 
ATOM   2503 N  N   . LEU B 1 44  ? -28.767 4.657   22.687  1.00 26.38 ? 44  LEU B N   1 
ATOM   2504 C  CA  . LEU B 1 44  ? -27.490 4.827   23.403  1.00 29.92 ? 44  LEU B CA  1 
ATOM   2505 C  C   . LEU B 1 44  ? -26.327 4.953   22.405  1.00 36.47 ? 44  LEU B C   1 
ATOM   2506 O  O   . LEU B 1 44  ? -26.301 4.327   21.351  1.00 32.17 ? 44  LEU B O   1 
ATOM   2507 C  CB  . LEU B 1 44  ? -27.222 3.687   24.394  1.00 27.17 ? 44  LEU B CB  1 
ATOM   2508 C  CG  . LEU B 1 44  ? -27.901 3.667   25.756  1.00 22.68 ? 44  LEU B CG  1 
ATOM   2509 C  CD1 . LEU B 1 44  ? -27.701 2.261   26.274  1.00 23.59 ? 44  LEU B CD1 1 
ATOM   2510 C  CD2 . LEU B 1 44  ? -27.364 4.670   26.753  1.00 25.84 ? 44  LEU B CD2 1 
ATOM   2511 N  N   . LYS B 1 45  ? -25.369 5.799   22.739  1.00 33.01 ? 45  LYS B N   1 
ATOM   2512 C  CA  . LYS B 1 45  ? -24.259 6.011   21.850  1.00 32.01 ? 45  LYS B CA  1 
ATOM   2513 C  C   . LYS B 1 45  ? -23.140 5.070   22.173  1.00 25.40 ? 45  LYS B C   1 
ATOM   2514 O  O   . LYS B 1 45  ? -23.143 4.390   23.284  1.00 31.67 ? 45  LYS B O   1 
ATOM   2515 C  CB  . LYS B 1 45  ? -23.772 7.388   21.972  1.00 23.09 ? 45  LYS B CB  1 
ATOM   2516 C  CG  . LYS B 1 45  ? -24.804 8.494   21.931  1.00 51.07 ? 45  LYS B CG  1 
ATOM   2517 C  CD  . LYS B 1 45  ? -24.121 9.868   21.888  1.00 40.36 ? 45  LYS B CD  1 
ATOM   2518 N  N   . PRO B 1 46  ? -22.190 4.955   21.176  1.00 23.76 ? 46  PRO B N   1 
ATOM   2519 C  CA  . PRO B 1 46  ? -20.996 4.172   21.515  1.00 21.84 ? 46  PRO B CA  1 
ATOM   2520 C  C   . PRO B 1 46  ? -20.379 4.945   22.633  1.00 20.05 ? 46  PRO B C   1 
ATOM   2521 O  O   . PRO B 1 46  ? -20.399 6.142   22.653  1.00 19.16 ? 46  PRO B O   1 
ATOM   2522 C  CB  . PRO B 1 46  ? -20.150 4.198   20.217  1.00 23.21 ? 46  PRO B CB  1 
ATOM   2523 C  CG  . PRO B 1 46  ? -21.175 4.397   19.152  1.00 26.86 ? 46  PRO B CG  1 
ATOM   2524 C  CD  . PRO B 1 46  ? -22.202 5.326   19.742  1.00 28.12 ? 46  PRO B CD  1 
ATOM   2525 N  N   . LEU B 1 47  ? -19.723 4.218   23.464  1.00 20.41 ? 47  LEU B N   1 
ATOM   2526 C  CA  . LEU B 1 47  ? -18.991 4.851   24.479  1.00 20.91 ? 47  LEU B CA  1 
ATOM   2527 C  C   . LEU B 1 47  ? -17.778 5.494   23.750  1.00 21.42 ? 47  LEU B C   1 
ATOM   2528 O  O   . LEU B 1 47  ? -17.228 4.923   22.813  1.00 24.87 ? 47  LEU B O   1 
ATOM   2529 C  CB  . LEU B 1 47  ? -18.548 3.759   25.414  1.00 28.35 ? 47  LEU B CB  1 
ATOM   2530 C  CG  . LEU B 1 47  ? -18.173 4.105   26.799  1.00 23.91 ? 47  LEU B CG  1 
ATOM   2531 C  CD1 . LEU B 1 47  ? -19.318 4.866   27.559  1.00 24.69 ? 47  LEU B CD1 1 
ATOM   2532 C  CD2 . LEU B 1 47  ? -17.680 2.818   27.494  1.00 24.07 ? 47  LEU B CD2 1 
ATOM   2533 N  N   . SER B 1 48  ? -17.333 6.659   24.218  1.00 14.84 ? 48  SER B N   1 
ATOM   2534 C  CA  . SER B 1 48  ? -16.091 7.222   23.788  1.00 15.21 ? 48  SER B CA  1 
ATOM   2535 C  C   . SER B 1 48  ? -15.090 7.214   24.967  1.00 15.39 ? 48  SER B C   1 
ATOM   2536 O  O   . SER B 1 48  ? -15.267 7.931   25.996  1.00 15.36 ? 48  SER B O   1 
ATOM   2537 C  CB  . SER B 1 48  ? -16.358 8.675   23.390  1.00 17.72 ? 48  SER B CB  1 
ATOM   2538 O  OG  . SER B 1 48  ? -15.164 9.380   23.069  1.00 19.59 ? 48  SER B OG  1 
ATOM   2539 N  N   . VAL B 1 49  ? -14.021 6.445   24.856  1.00 14.57 ? 49  VAL B N   1 
ATOM   2540 C  CA  . VAL B 1 49  ? -12.998 6.337   25.884  1.00 16.34 ? 49  VAL B CA  1 
ATOM   2541 C  C   . VAL B 1 49  ? -11.741 6.899   25.276  1.00 16.39 ? 49  VAL B C   1 
ATOM   2542 O  O   . VAL B 1 49  ? -11.227 6.265   24.346  1.00 22.28 ? 49  VAL B O   1 
ATOM   2543 C  CB  . VAL B 1 49  ? -12.759 4.872   26.298  1.00 20.31 ? 49  VAL B CB  1 
ATOM   2544 C  CG1 . VAL B 1 49  ? -11.836 4.820   27.500  1.00 26.05 ? 49  VAL B CG1 1 
ATOM   2545 C  CG2 . VAL B 1 49  ? -14.102 4.177   26.577  1.00 20.86 ? 49  VAL B CG2 1 
ATOM   2546 N  N   . SER B 1 50  ? -11.243 8.056   25.737  1.00 17.31 ? 50  SER B N   1 
ATOM   2547 C  CA  . SER B 1 50  ? -10.094 8.711   25.093  1.00 17.10 ? 50  SER B CA  1 
ATOM   2548 C  C   . SER B 1 50  ? -8.989  8.809   26.072  1.00 15.62 ? 50  SER B C   1 
ATOM   2549 O  O   . SER B 1 50  ? -8.915  9.840   26.755  1.00 17.08 ? 50  SER B O   1 
ATOM   2550 C  CB  . SER B 1 50  ? -10.396 10.101  24.456  1.00 19.90 ? 50  SER B CB  1 
ATOM   2551 O  OG  . SER B 1 50  ? -11.465 9.893   23.543  1.00 22.71 ? 50  SER B OG  1 
ATOM   2552 N  N   . TYR B 1 51  ? -8.144  7.804   26.169  1.00 16.65 ? 51  TYR B N   1 
ATOM   2553 C  CA  . TYR B 1 51  ? -7.035  7.748   27.137  1.00 15.42 ? 51  TYR B CA  1 
ATOM   2554 C  C   . TYR B 1 51  ? -5.643  7.997   26.597  1.00 16.62 ? 51  TYR B C   1 
ATOM   2555 O  O   . TYR B 1 51  ? -4.669  7.852   27.319  1.00 17.34 ? 51  TYR B O   1 
ATOM   2556 C  CB  . TYR B 1 51  ? -7.043  6.367   27.802  1.00 15.76 ? 51  TYR B CB  1 
ATOM   2557 C  CG  . TYR B 1 51  ? -8.228  6.080   28.769  1.00 14.00 ? 51  TYR B CG  1 
ATOM   2558 C  CD1 . TYR B 1 51  ? -9.088  7.087   29.231  1.00 13.53 ? 51  TYR B CD1 1 
ATOM   2559 C  CD2 . TYR B 1 51  ? -8.445  4.779   29.222  1.00 13.53 ? 51  TYR B CD2 1 
ATOM   2560 C  CE1 . TYR B 1 51  ? -10.135 6.781   30.122  1.00 11.78 ? 51  TYR B CE1 1 
ATOM   2561 C  CE2 . TYR B 1 51  ? -9.474  4.485   30.096  1.00 13.40 ? 51  TYR B CE2 1 
ATOM   2562 C  CZ  . TYR B 1 51  ? -10.309 5.467   30.543  1.00 10.90 ? 51  TYR B CZ  1 
ATOM   2563 O  OH  . TYR B 1 51  ? -11.320 5.118   31.416  1.00 11.59 ? 51  TYR B OH  1 
ATOM   2564 N  N   . ASP B 1 52  ? -5.555  8.408   25.303  1.00 18.91 ? 52  ASP B N   1 
ATOM   2565 C  CA  . ASP B 1 52  ? -4.217  8.730   24.698  1.00 20.51 ? 52  ASP B CA  1 
ATOM   2566 C  C   . ASP B 1 52  ? -3.310  9.701   25.484  1.00 22.19 ? 52  ASP B C   1 
ATOM   2567 O  O   . ASP B 1 52  ? -2.058  9.483   25.581  1.00 26.65 ? 52  ASP B O   1 
ATOM   2568 C  CB  . ASP B 1 52  ? -4.349  9.165   23.213  1.00 21.28 ? 52  ASP B CB  1 
ATOM   2569 C  CG  . ASP B 1 52  ? -5.449  10.178  22.981  1.00 33.41 ? 52  ASP B CG  1 
ATOM   2570 O  OD1 . ASP B 1 52  ? -6.664  9.884   23.312  1.00 45.33 ? 52  ASP B OD1 1 
ATOM   2571 O  OD2 . ASP B 1 52  ? -5.110  11.276  22.436  1.00 58.31 ? 52  ASP B OD2 1 
ATOM   2572 N  N   . GLN B 1 53  ? -3.893  10.682  26.167  1.00 21.17 ? 53  GLN B N   1 
ATOM   2573 C  CA  . GLN B 1 53  ? -2.981  11.614  26.864  1.00 23.38 ? 53  GLN B CA  1 
ATOM   2574 C  C   . GLN B 1 53  ? -2.990  11.345  28.375  1.00 20.94 ? 53  GLN B C   1 
ATOM   2575 O  O   . GLN B 1 53  ? -2.567  12.186  29.164  1.00 19.30 ? 53  GLN B O   1 
ATOM   2576 C  CB  . GLN B 1 53  ? -3.365  13.082  26.526  1.00 27.97 ? 53  GLN B CB  1 
ATOM   2577 C  CG  . GLN B 1 53  ? -3.258  13.430  25.033  1.00 35.93 ? 53  GLN B CG  1 
ATOM   2578 C  CD  . GLN B 1 53  ? -1.804  13.356  24.614  1.00 51.64 ? 53  GLN B CD  1 
ATOM   2579 O  OE1 . GLN B 1 53  ? -0.908  13.815  25.359  1.00 60.82 ? 53  GLN B OE1 1 
ATOM   2580 N  NE2 . GLN B 1 53  ? -1.538  12.729  23.457  1.00 78.40 ? 53  GLN B NE2 1 
ATOM   2581 N  N   . ALA B 1 54  ? -3.511  10.201  28.819  1.00 18.90 ? 54  ALA B N   1 
ATOM   2582 C  CA  . ALA B 1 54  ? -3.564  9.943   30.275  1.00 14.11 ? 54  ALA B CA  1 
ATOM   2583 C  C   . ALA B 1 54  ? -2.190  9.985   30.924  1.00 17.34 ? 54  ALA B C   1 
ATOM   2584 O  O   . ALA B 1 54  ? -1.234  9.476   30.333  1.00 22.64 ? 54  ALA B O   1 
ATOM   2585 C  CB  . ALA B 1 54  ? -4.219  8.581   30.595  1.00 17.50 ? 54  ALA B CB  1 
ATOM   2586 N  N   . THR B 1 55  ? -2.050  10.671  32.071  1.00 14.85 ? 55  THR B N   1 
ATOM   2587 C  CA  . THR B 1 55  ? -0.763  10.842  32.772  1.00 16.49 ? 55  THR B CA  1 
ATOM   2588 C  C   . THR B 1 55  ? -0.942  10.261  34.168  1.00 13.87 ? 55  THR B C   1 
ATOM   2589 O  O   . THR B 1 55  ? -1.500  10.884  35.023  1.00 13.28 ? 55  THR B O   1 
ATOM   2590 C  CB  . THR B 1 55  ? -0.336  12.349  32.954  1.00 22.95 ? 55  THR B CB  1 
ATOM   2591 O  OG1 . THR B 1 55  ? -0.380  13.018  31.700  1.00 33.97 ? 55  THR B OG1 1 
ATOM   2592 C  CG2 . THR B 1 55  ? 1.095   12.310  33.404  1.00 22.44 ? 55  THR B CG2 1 
ATOM   2593 N  N   . SER B 1 56  ? -0.468  9.050   34.391  1.00 12.90 ? 56  SER B N   1 
ATOM   2594 C  CA  . SER B 1 56  ? -0.524  8.488   35.729  1.00 11.90 ? 56  SER B CA  1 
ATOM   2595 C  C   . SER B 1 56  ? 0.520   9.171   36.635  1.00 14.26 ? 56  SER B C   1 
ATOM   2596 O  O   . SER B 1 56  ? 1.536   9.646   36.069  1.00 15.89 ? 56  SER B O   1 
ATOM   2597 C  CB  . SER B 1 56  ? -0.327  6.947   35.730  1.00 14.51 ? 56  SER B CB  1 
ATOM   2598 O  OG  . SER B 1 56  ? 0.956   6.613   35.244  1.00 13.15 ? 56  SER B OG  1 
ATOM   2599 N  N   . LEU B 1 57  ? 0.298   9.178   37.948  1.00 12.04 ? 57  LEU B N   1 
ATOM   2600 C  CA  . LEU B 1 57  ? 1.185   9.820   38.931  1.00 17.18 ? 57  LEU B CA  1 
ATOM   2601 C  C   . LEU B 1 57  ? 1.748   8.834   39.892  1.00 14.27 ? 57  LEU B C   1 
ATOM   2602 O  O   . LEU B 1 57  ? 2.971   8.835   40.178  1.00 15.03 ? 57  LEU B O   1 
ATOM   2603 C  CB  . LEU B 1 57  ? 0.473   10.968  39.675  1.00 19.69 ? 57  LEU B CB  1 
ATOM   2604 C  CG  . LEU B 1 57  ? 0.041   12.112  38.712  1.00 21.32 ? 57  LEU B CG  1 
ATOM   2605 C  CD1 . LEU B 1 57  ? -0.640  13.167  39.550  1.00 23.17 ? 57  LEU B CD1 1 
ATOM   2606 C  CD2 . LEU B 1 57  ? 1.244   12.673  37.944  1.00 32.66 ? 57  LEU B CD2 1 
ATOM   2607 N  N   . ARG B 1 58  ? 0.911   8.048   40.511  1.00 13.63 ? 58  ARG B N   1 
ATOM   2608 C  CA  . ARG B 1 58  ? 1.301   7.331   41.708  1.00 12.69 ? 58  ARG B CA  1 
ATOM   2609 C  C   . ARG B 1 58  ? 0.353   6.217   41.926  1.00 12.20 ? 58  ARG B C   1 
ATOM   2610 O  O   . ARG B 1 58  ? -0.756  6.216   41.408  1.00 12.89 ? 58  ARG B O   1 
ATOM   2611 C  CB  . ARG B 1 58  ? 1.130   8.333   42.878  1.00 16.05 ? 58  ARG B CB  1 
ATOM   2612 C  CG  . ARG B 1 58  ? 1.701   7.966   44.163  1.00 19.60 ? 58  ARG B CG  1 
ATOM   2613 C  CD  . ARG B 1 58  ? 1.533   9.188   45.060  1.00 28.22 ? 58  ARG B CD  1 
ATOM   2614 N  NE  . ARG B 1 58  ? 0.146   9.148   45.538  1.00 20.57 ? 58  ARG B NE  1 
ATOM   2615 C  CZ  . ARG B 1 58  ? -0.284  9.342   46.786  1.00 19.39 ? 58  ARG B CZ  1 
ATOM   2616 N  NH1 . ARG B 1 58  ? 0.562   9.660   47.767  1.00 20.60 ? 58  ARG B NH1 1 
ATOM   2617 N  NH2 . ARG B 1 58  ? -1.591  9.245   47.023  1.00 19.09 ? 58  ARG B NH2 1 
ATOM   2618 N  N   . ILE B 1 59  ? 0.793   5.248   42.692  1.00 11.52 ? 59  ILE B N   1 
ATOM   2619 C  CA  . ILE B 1 59  ? -0.013  4.123   43.148  1.00 11.58 ? 59  ILE B CA  1 
ATOM   2620 C  C   . ILE B 1 59  ? -0.024  4.109   44.671  1.00 9.89  ? 59  ILE B C   1 
ATOM   2621 O  O   . ILE B 1 59  ? 1.060   4.321   45.321  1.00 11.40 ? 59  ILE B O   1 
ATOM   2622 C  CB  . ILE B 1 59  ? 0.474   2.791   42.484  1.00 11.87 ? 59  ILE B CB  1 
ATOM   2623 C  CG1 . ILE B 1 59  ? -0.561  1.639   42.715  1.00 12.53 ? 59  ILE B CG1 1 
ATOM   2624 C  CG2 . ILE B 1 59  ? 1.930   2.396   42.931  1.00 12.05 ? 59  ILE B CG2 1 
ATOM   2625 C  CD1 . ILE B 1 59  ? -0.208  0.379   41.935  1.00 12.21 ? 59  ILE B CD1 1 
ATOM   2626 N  N   . LEU B 1 60  ? -1.181  3.869   45.274  1.00 11.92 ? 60  LEU B N   1 
ATOM   2627 C  CA  . LEU B 1 60  ? -1.368  3.968   46.721  1.00 10.20 ? 60  LEU B CA  1 
ATOM   2628 C  C   . LEU B 1 60  ? -2.077  2.761   47.273  1.00 11.27 ? 60  LEU B C   1 
ATOM   2629 O  O   . LEU B 1 60  ? -3.156  2.416   46.740  1.00 11.00 ? 60  LEU B O   1 
ATOM   2630 C  CB  . LEU B 1 60  ? -2.206  5.281   47.015  1.00 12.25 ? 60  LEU B CB  1 
ATOM   2631 C  CG  . LEU B 1 60  ? -2.595  5.459   48.508  1.00 11.92 ? 60  LEU B CG  1 
ATOM   2632 C  CD1 . LEU B 1 60  ? -1.376  5.701   49.448  1.00 13.98 ? 60  LEU B CD1 1 
ATOM   2633 C  CD2 . LEU B 1 60  ? -3.678  6.589   48.532  1.00 14.62 ? 60  LEU B CD2 1 
ATOM   2634 N  N   . ASN B 1 61  ? -1.592  2.167   48.355  1.00 10.68 ? 61  ASN B N   1 
ATOM   2635 C  CA  . ASN B 1 61  ? -2.372  1.202   49.145  1.00 10.98 ? 61  ASN B CA  1 
ATOM   2636 C  C   . ASN B 1 61  ? -3.114  1.995   50.183  1.00 12.64 ? 61  ASN B C   1 
ATOM   2637 O  O   . ASN B 1 61  ? -2.513  2.594   51.088  1.00 13.63 ? 61  ASN B O   1 
ATOM   2638 C  CB  . ASN B 1 61  ? -1.439  0.131   49.741  1.00 13.41 ? 61  ASN B CB  1 
ATOM   2639 C  CG  . ASN B 1 61  ? -2.154  -0.799  50.682  1.00 11.11 ? 61  ASN B CG  1 
ATOM   2640 O  OD1 . ASN B 1 61  ? -3.248  -0.518  51.191  1.00 12.53 ? 61  ASN B OD1 1 
ATOM   2641 N  ND2 . ASN B 1 61  ? -1.615  -2.009  50.827  1.00 10.75 ? 61  ASN B ND2 1 
ATOM   2642 N  N   . ASN B 1 62  ? -4.429  2.096   50.034  1.00 12.58 ? 62  ASN B N   1 
ATOM   2643 C  CA  . ASN B 1 62  ? -5.222  2.984   50.880  1.00 14.58 ? 62  ASN B CA  1 
ATOM   2644 C  C   . ASN B 1 62  ? -5.835  2.223   52.044  1.00 15.08 ? 62  ASN B C   1 
ATOM   2645 O  O   . ASN B 1 62  ? -6.622  2.804   52.806  1.00 18.97 ? 62  ASN B O   1 
ATOM   2646 C  CB  . ASN B 1 62  ? -6.294  3.773   50.062  1.00 16.32 ? 62  ASN B CB  1 
ATOM   2647 C  CG  . ASN B 1 62  ? -7.233  2.838   49.302  1.00 13.77 ? 62  ASN B CG  1 
ATOM   2648 O  OD1 . ASN B 1 62  ? -7.695  1.874   49.858  1.00 14.34 ? 62  ASN B OD1 1 
ATOM   2649 N  ND2 . ASN B 1 62  ? -7.374  3.031   47.975  1.00 18.90 ? 62  ASN B ND2 1 
ATOM   2650 N  N   . GLY B 1 63  ? -5.490  0.942   52.241  1.00 12.85 ? 63  GLY B N   1 
ATOM   2651 C  CA  . GLY B 1 63  ? -5.975  0.126   53.330  1.00 12.11 ? 63  GLY B CA  1 
ATOM   2652 C  C   . GLY B 1 63  ? -7.270  -0.615  52.971  1.00 12.52 ? 63  GLY B C   1 
ATOM   2653 O  O   . GLY B 1 63  ? -7.738  -1.443  53.718  1.00 13.23 ? 63  GLY B O   1 
ATOM   2654 N  N   . HIS B 1 64  ? -7.867  -0.296  51.801  1.00 11.50 ? 64  HIS B N   1 
ATOM   2655 C  CA  . HIS B 1 64  ? -9.114  -1.011  51.299  1.00 12.60 ? 64  HIS B CA  1 
ATOM   2656 C  C   . HIS B 1 64  ? -8.844  -1.654  49.973  1.00 10.84 ? 64  HIS B C   1 
ATOM   2657 O  O   . HIS B 1 64  ? -9.288  -2.807  49.716  1.00 14.06 ? 64  HIS B O   1 
ATOM   2658 C  CB  . HIS B 1 64  ? -10.277 -0.052  51.163  1.00 13.28 ? 64  HIS B CB  1 
ATOM   2659 C  CG  . HIS B 1 64  ? -10.538 0.727   52.468  1.00 15.32 ? 64  HIS B CG  1 
ATOM   2660 N  ND1 . HIS B 1 64  ? -11.071 0.113   53.597  1.00 17.39 ? 64  HIS B ND1 1 
ATOM   2661 C  CD2 . HIS B 1 64  ? -10.365 2.048   52.793  1.00 16.03 ? 64  HIS B CD2 1 
ATOM   2662 C  CE1 . HIS B 1 64  ? -11.221 1.030   54.582  1.00 18.22 ? 64  HIS B CE1 1 
ATOM   2663 N  NE2 . HIS B 1 64  ? -10.797 2.204   54.102  1.00 19.76 ? 64  HIS B NE2 1 
ATOM   2664 N  N   . ALA B 1 65  ? -8.143  -0.967  49.099  1.00 11.23 ? 65  ALA B N   1 
ATOM   2665 C  CA  . ALA B 1 65  ? -7.683  -1.487  47.775  1.00 12.01 ? 65  ALA B CA  1 
ATOM   2666 C  C   . ALA B 1 65  ? -6.353  -0.740  47.486  1.00 9.90  ? 65  ALA B C   1 
ATOM   2667 O  O   . ALA B 1 65  ? -5.822  -0.030  48.376  1.00 12.08 ? 65  ALA B O   1 
ATOM   2668 C  CB  . ALA B 1 65  ? -8.782  -1.225  46.702  1.00 12.46 ? 65  ALA B CB  1 
ATOM   2669 N  N   . PHE B 1 66  ? -5.887  -0.819  46.259  1.00 11.14 ? 66  PHE B N   1 
ATOM   2670 C  CA  . PHE B 1 66  ? -4.884  0.082   45.753  1.00 10.80 ? 66  PHE B CA  1 
ATOM   2671 C  C   . PHE B 1 66  ? -5.464  0.964   44.668  1.00 10.65 ? 66  PHE B C   1 
ATOM   2672 O  O   . PHE B 1 66  ? -6.292  0.486   43.902  1.00 12.55 ? 66  PHE B O   1 
ATOM   2673 C  CB  . PHE B 1 66  ? -3.541  -0.681  45.380  1.00 12.97 ? 66  PHE B CB  1 
ATOM   2674 C  CG  . PHE B 1 66  ? -3.705  -1.542  44.180  1.00 10.72 ? 66  PHE B CG  1 
ATOM   2675 C  CD1 . PHE B 1 66  ? -3.578  -1.003  42.910  1.00 12.09 ? 66  PHE B CD1 1 
ATOM   2676 C  CD2 . PHE B 1 66  ? -4.004  -2.902  44.330  1.00 11.52 ? 66  PHE B CD2 1 
ATOM   2677 C  CE1 . PHE B 1 66  ? -3.729  -1.761  41.792  1.00 12.20 ? 66  PHE B CE1 1 
ATOM   2678 C  CE2 . PHE B 1 66  ? -4.146  -3.698  43.189  1.00 11.69 ? 66  PHE B CE2 1 
ATOM   2679 C  CZ  . PHE B 1 66  ? -3.957  -3.141  41.911  1.00 11.04 ? 66  PHE B CZ  1 
ATOM   2680 N  N   A ASN B 1 67  ? -4.915  2.157   44.509  0.50 9.70  ? 67  ASN B N   1 
ATOM   2681 N  N   B ASN B 1 67  ? -5.150  2.247   44.686  0.50 11.25 ? 67  ASN B N   1 
ATOM   2682 C  CA  A ASN B 1 67  ? -5.381  3.193   43.564  0.50 11.58 ? 67  ASN B CA  1 
ATOM   2683 C  CA  B ASN B 1 67  ? -5.535  3.118   43.573  0.50 12.71 ? 67  ASN B CA  1 
ATOM   2684 C  C   A ASN B 1 67  ? -4.275  3.717   42.669  0.50 10.35 ? 67  ASN B C   1 
ATOM   2685 C  C   B ASN B 1 67  ? -4.328  3.556   42.720  0.50 10.00 ? 67  ASN B C   1 
ATOM   2686 O  O   A ASN B 1 67  ? -3.246  4.249   43.158  0.50 11.74 ? 67  ASN B O   1 
ATOM   2687 O  O   B ASN B 1 67  ? -3.248  3.774   43.346  0.50 11.63 ? 67  ASN B O   1 
ATOM   2688 C  CB  A ASN B 1 67  ? -5.934  4.462   44.268  0.50 12.70 ? 67  ASN B CB  1 
ATOM   2689 C  CB  B ASN B 1 67  ? -6.523  4.306   43.909  0.50 14.86 ? 67  ASN B CB  1 
ATOM   2690 C  CG  A ASN B 1 67  ? -7.029  4.175   45.235  0.50 17.59 ? 67  ASN B CG  1 
ATOM   2691 C  CG  B ASN B 1 67  ? -6.509  4.846   45.370  0.50 17.37 ? 67  ASN B CG  1 
ATOM   2692 O  OD1 A ASN B 1 67  ? -7.038  4.792   46.353  0.50 22.76 ? 67  ASN B OD1 1 
ATOM   2693 O  OD1 B ASN B 1 67  ? -5.597  4.768   46.167  0.50 16.35 ? 67  ASN B OD1 1 
ATOM   2694 N  ND2 A ASN B 1 67  ? -7.937  3.272   44.896  0.50 12.90 ? 67  ASN B ND2 1 
ATOM   2695 N  ND2 B ASN B 1 67  ? -7.645  5.413   45.719  0.50 19.39 ? 67  ASN B ND2 1 
ATOM   2696 N  N   . VAL B 1 68  ? -4.482  3.640   41.382  1.00 9.97  ? 68  VAL B N   1 
ATOM   2697 C  CA  . VAL B 1 68  ? -3.524  4.284   40.485  1.00 11.35 ? 68  VAL B CA  1 
ATOM   2698 C  C   . VAL B 1 68  ? -4.124  5.651   40.165  1.00 11.00 ? 68  VAL B C   1 
ATOM   2699 O  O   . VAL B 1 68  ? -5.272  5.713   39.665  1.00 11.55 ? 68  VAL B O   1 
ATOM   2700 C  CB  . VAL B 1 68  ? -3.291  3.472   39.216  1.00 12.58 ? 68  VAL B CB  1 
ATOM   2701 C  CG1 . VAL B 1 68  ? -2.453  4.327   38.241  1.00 14.25 ? 68  VAL B CG1 1 
ATOM   2702 C  CG2 . VAL B 1 68  ? -2.589  2.168   39.526  1.00 12.36 ? 68  VAL B CG2 1 
ATOM   2703 N  N   . GLU B 1 69  ? -3.450  6.737   40.492  1.00 13.28 ? 69  GLU B N   1 
ATOM   2704 C  CA  . GLU B 1 69  ? -3.961  8.128   40.415  1.00 11.38 ? 69  GLU B CA  1 
ATOM   2705 C  C   . GLU B 1 69  ? -3.439  8.746   39.154  1.00 12.77 ? 69  GLU B C   1 
ATOM   2706 O  O   . GLU B 1 69  ? -2.232  8.508   38.764  1.00 14.60 ? 69  GLU B O   1 
ATOM   2707 C  CB  . GLU B 1 69  ? -3.469  8.902   41.599  1.00 13.86 ? 69  GLU B CB  1 
ATOM   2708 C  CG  . GLU B 1 69  ? -3.987  8.324   42.879  1.00 19.42 ? 69  GLU B CG  1 
ATOM   2709 C  CD  . GLU B 1 69  ? -3.137  8.772   44.003  1.00 18.51 ? 69  GLU B CD  1 
ATOM   2710 O  OE1 . GLU B 1 69  ? -2.056  9.418   43.770  1.00 20.86 ? 69  GLU B OE1 1 
ATOM   2711 O  OE2 . GLU B 1 69  ? -3.518  8.391   45.122  1.00 19.93 ? 69  GLU B OE2 1 
ATOM   2712 N  N   . PHE B 1 70  ? -4.255  9.634   38.591  1.00 11.50 ? 70  PHE B N   1 
ATOM   2713 C  CA  . PHE B 1 70  ? -3.898  10.327  37.353  1.00 11.82 ? 70  PHE B CA  1 
ATOM   2714 C  C   . PHE B 1 70  ? -3.883  11.854  37.657  1.00 13.34 ? 70  PHE B C   1 
ATOM   2715 O  O   . PHE B 1 70  ? -4.623  12.356  38.506  1.00 13.37 ? 70  PHE B O   1 
ATOM   2716 C  CB  . PHE B 1 70  ? -4.893  10.011  36.220  1.00 11.67 ? 70  PHE B CB  1 
ATOM   2717 C  CG  . PHE B 1 70  ? -4.725  8.607   35.703  1.00 10.99 ? 70  PHE B CG  1 
ATOM   2718 C  CD1 . PHE B 1 70  ? -5.190  7.505   36.432  1.00 10.87 ? 70  PHE B CD1 1 
ATOM   2719 C  CD2 . PHE B 1 70  ? -3.949  8.379   34.589  1.00 11.43 ? 70  PHE B CD2 1 
ATOM   2720 C  CE1 . PHE B 1 70  ? -4.904  6.181   36.009  1.00 12.07 ? 70  PHE B CE1 1 
ATOM   2721 C  CE2 . PHE B 1 70  ? -3.672  7.057   34.167  1.00 11.32 ? 70  PHE B CE2 1 
ATOM   2722 C  CZ  . PHE B 1 70  ? -4.163  5.958   34.880  1.00 11.31 ? 70  PHE B CZ  1 
ATOM   2723 N  N   . ASP B 1 71  ? -3.047  12.563  36.870  1.00 14.78 ? 71  ASP B N   1 
ATOM   2724 C  CA  . ASP B 1 71  ? -3.145  14.030  36.845  1.00 14.36 ? 71  ASP B CA  1 
ATOM   2725 C  C   . ASP B 1 71  ? -4.406  14.430  36.080  1.00 14.31 ? 71  ASP B C   1 
ATOM   2726 O  O   . ASP B 1 71  ? -4.478  14.246  34.860  1.00 19.73 ? 71  ASP B O   1 
ATOM   2727 C  CB  . ASP B 1 71  ? -1.920  14.553  36.124  1.00 20.87 ? 71  ASP B CB  1 
ATOM   2728 C  CG  . ASP B 1 71  ? -1.837  16.076  36.157  1.00 24.96 ? 71  ASP B CG  1 
ATOM   2729 O  OD1 . ASP B 1 71  ? -2.873  16.714  36.491  1.00 22.43 ? 71  ASP B OD1 1 
ATOM   2730 O  OD2 . ASP B 1 71  ? -0.737  16.556  35.811  1.00 36.07 ? 71  ASP B OD2 1 
ATOM   2731 N  N   . ASP B 1 72  ? -5.422  14.926  36.777  1.00 13.43 ? 72  ASP B N   1 
ATOM   2732 C  CA  . ASP B 1 72  ? -6.738  15.341  36.209  1.00 13.95 ? 72  ASP B CA  1 
ATOM   2733 C  C   . ASP B 1 72  ? -6.827  16.887  36.133  1.00 15.69 ? 72  ASP B C   1 
ATOM   2734 O  O   . ASP B 1 72  ? -7.907  17.419  36.228  1.00 18.37 ? 72  ASP B O   1 
ATOM   2735 C  CB  . ASP B 1 72  ? -7.874  14.726  37.016  1.00 15.36 ? 72  ASP B CB  1 
ATOM   2736 C  CG  . ASP B 1 72  ? -7.973  15.264  38.401  1.00 15.45 ? 72  ASP B CG  1 
ATOM   2737 O  OD1 . ASP B 1 72  ? -7.001  15.926  38.896  1.00 17.26 ? 72  ASP B OD1 1 
ATOM   2738 O  OD2 . ASP B 1 72  ? -8.976  15.049  39.095  1.00 15.92 ? 72  ASP B OD2 1 
ATOM   2739 N  N   . SER B 1 73  ? -5.665  17.530  36.054  1.00 17.20 ? 73  SER B N   1 
ATOM   2740 C  CA  . SER B 1 73  ? -5.628  19.042  36.060  1.00 19.03 ? 73  SER B CA  1 
ATOM   2741 C  C   . SER B 1 73  ? -5.809  19.577  34.641  1.00 20.19 ? 73  SER B C   1 
ATOM   2742 O  O   . SER B 1 73  ? -6.060  20.788  34.480  1.00 18.20 ? 73  SER B O   1 
ATOM   2743 C  CB  . SER B 1 73  ? -4.310  19.533  36.664  1.00 23.63 ? 73  SER B CB  1 
ATOM   2744 O  OG  . SER B 1 73  ? -3.234  19.312  35.784  1.00 21.84 ? 73  SER B OG  1 
ATOM   2745 N  N   . GLN B 1 74  ? -5.759  18.726  33.620  1.00 21.21 ? 74  GLN B N   1 
ATOM   2746 C  CA  . GLN B 1 74  ? -6.036  19.165  32.247  1.00 20.36 ? 74  GLN B CA  1 
ATOM   2747 C  C   . GLN B 1 74  ? -7.009  18.208  31.658  1.00 19.69 ? 74  GLN B C   1 
ATOM   2748 O  O   . GLN B 1 74  ? -7.259  17.111  32.172  1.00 18.43 ? 74  GLN B O   1 
ATOM   2749 C  CB  . GLN B 1 74  ? -4.746  19.256  31.390  1.00 23.17 ? 74  GLN B CB  1 
ATOM   2750 C  CG  . GLN B 1 74  ? -3.652  20.194  32.007  1.00 23.46 ? 74  GLN B CG  1 
ATOM   2751 C  CD  . GLN B 1 74  ? -2.291  20.117  31.285  1.00 25.52 ? 74  GLN B CD  1 
ATOM   2752 O  OE1 . GLN B 1 74  ? -2.211  20.010  30.074  1.00 38.40 ? 74  GLN B OE1 1 
ATOM   2753 N  NE2 . GLN B 1 74  ? -1.214  20.168  32.061  1.00 37.32 ? 74  GLN B NE2 1 
ATOM   2754 N  N   . ASP B 1 75  ? -7.517  18.625  30.523  1.00 22.77 ? 75  ASP B N   1 
ATOM   2755 C  CA  . ASP B 1 75  ? -8.483  17.888  29.763  1.00 19.94 ? 75  ASP B CA  1 
ATOM   2756 C  C   . ASP B 1 75  ? -7.714  16.700  29.017  1.00 22.86 ? 75  ASP B C   1 
ATOM   2757 O  O   . ASP B 1 75  ? -7.387  16.850  27.822  1.00 28.81 ? 75  ASP B O   1 
ATOM   2758 C  CB  . ASP B 1 75  ? -9.105  18.932  28.766  1.00 26.65 ? 75  ASP B CB  1 
ATOM   2759 C  CG  . ASP B 1 75  ? -10.052 18.322  27.773  1.00 29.53 ? 75  ASP B CG  1 
ATOM   2760 O  OD1 . ASP B 1 75  ? -10.416 17.124  27.969  1.00 31.78 ? 75  ASP B OD1 1 
ATOM   2761 O  OD2 . ASP B 1 75  ? -10.469 19.049  26.804  1.00 37.10 ? 75  ASP B OD2 1 
ATOM   2762 N  N   . LYS B 1 76  ? -7.437  15.576  29.677  1.00 22.01 ? 76  LYS B N   1 
ATOM   2763 C  CA  . LYS B 1 76  ? -6.591  14.572  29.078  1.00 26.01 ? 76  LYS B CA  1 
ATOM   2764 C  C   . LYS B 1 76  ? -7.408  13.329  28.796  1.00 41.42 ? 76  LYS B C   1 
ATOM   2765 O  O   . LYS B 1 76  ? -8.020  13.231  27.738  1.00 50.78 ? 76  LYS B O   1 
ATOM   2766 C  CB  . LYS B 1 76  ? -5.362  14.369  29.924  1.00 25.70 ? 76  LYS B CB  1 
ATOM   2767 C  CG  . LYS B 1 76  ? -4.501  15.623  29.807  1.00 30.24 ? 76  LYS B CG  1 
ATOM   2768 C  CD  . LYS B 1 76  ? -3.080  15.306  30.182  1.00 29.13 ? 76  LYS B CD  1 
ATOM   2769 N  N   . ALA B 1 77  ? -7.506  12.463  29.771  1.00 25.86 ? 77  ALA B N   1 
ATOM   2770 C  CA  . ALA B 1 77  ? -8.126  11.154  29.642  1.00 19.07 ? 77  ALA B CA  1 
ATOM   2771 C  C   . ALA B 1 77  ? -9.609  11.298  29.963  1.00 17.07 ? 77  ALA B C   1 
ATOM   2772 O  O   . ALA B 1 77  ? -9.970  11.517  31.121  1.00 22.12 ? 77  ALA B O   1 
ATOM   2773 C  CB  . ALA B 1 77  ? -7.477  10.256  30.698  1.00 20.82 ? 77  ALA B CB  1 
ATOM   2774 N  N   . VAL B 1 78  ? -10.467 11.176  28.990  1.00 14.48 ? 78  VAL B N   1 
ATOM   2775 C  CA  . VAL B 1 78  ? -11.881 11.497  29.190  1.00 15.37 ? 78  VAL B CA  1 
ATOM   2776 C  C   . VAL B 1 78  ? -12.829 10.422  28.665  1.00 13.46 ? 78  VAL B C   1 
ATOM   2777 O  O   . VAL B 1 78  ? -12.590 9.753   27.661  1.00 15.03 ? 78  VAL B O   1 
ATOM   2778 C  CB  . VAL B 1 78  ? -12.267 12.842  28.611  1.00 22.67 ? 78  VAL B CB  1 
ATOM   2779 C  CG1 . VAL B 1 78  ? -11.428 13.966  29.136  1.00 22.27 ? 78  VAL B CG1 1 
ATOM   2780 C  CG2 . VAL B 1 78  ? -11.996 12.795  27.189  1.00 23.21 ? 78  VAL B CG2 1 
ATOM   2781 N  N   . LEU B 1 79  ? -13.925 10.247  29.407  1.00 11.44 ? 79  LEU B N   1 
ATOM   2782 C  CA  . LEU B 1 79  ? -15.003 9.370   29.070  1.00 12.09 ? 79  LEU B CA  1 
ATOM   2783 C  C   . LEU B 1 79  ? -16.138 10.235  28.663  1.00 12.27 ? 79  LEU B C   1 
ATOM   2784 O  O   . LEU B 1 79  ? -16.586 11.156  29.410  1.00 14.94 ? 79  LEU B O   1 
ATOM   2785 C  CB  . LEU B 1 79  ? -15.308 8.430   30.283  1.00 14.24 ? 79  LEU B CB  1 
ATOM   2786 C  CG  . LEU B 1 79  ? -16.329 7.393   30.081  1.00 14.28 ? 79  LEU B CG  1 
ATOM   2787 C  CD1 . LEU B 1 79  ? -15.931 6.340   29.054  1.00 18.15 ? 79  LEU B CD1 1 
ATOM   2788 C  CD2 . LEU B 1 79  ? -16.625 6.758   31.422  1.00 15.20 ? 79  LEU B CD2 1 
ATOM   2789 N  N   . LYS B 1 80  ? -16.772 9.901   27.543  1.00 13.35 ? 80  LYS B N   1 
ATOM   2790 C  CA  . LYS B 1 80  ? -18.018 10.591  27.148  1.00 14.47 ? 80  LYS B CA  1 
ATOM   2791 C  C   . LYS B 1 80  ? -18.898 9.698   26.256  1.00 13.87 ? 80  LYS B C   1 
ATOM   2792 O  O   . LYS B 1 80  ? -18.543 8.527   26.056  1.00 15.04 ? 80  LYS B O   1 
ATOM   2793 C  CB  . LYS B 1 80  ? -17.717 11.906  26.453  1.00 17.10 ? 80  LYS B CB  1 
ATOM   2794 C  CG  . LYS B 1 80  ? -17.098 11.763  25.099  1.00 18.67 ? 80  LYS B CG  1 
ATOM   2795 C  CD  . LYS B 1 80  ? -16.827 13.169  24.496  1.00 21.65 ? 80  LYS B CD  1 
ATOM   2796 N  N   . GLY B 1 81  ? -20.029 10.229  25.783  1.00 15.83 ? 81  GLY B N   1 
ATOM   2797 C  CA  . GLY B 1 81  ? -20.973 9.460   24.973  1.00 16.38 ? 81  GLY B CA  1 
ATOM   2798 C  C   . GLY B 1 81  ? -21.618 8.366   25.803  1.00 17.66 ? 81  GLY B C   1 
ATOM   2799 O  O   . GLY B 1 81  ? -21.733 8.498   27.036  1.00 17.00 ? 81  GLY B O   1 
ATOM   2800 N  N   . GLY B 1 82  ? -22.058 7.264   25.167  1.00 21.87 ? 82  GLY B N   1 
ATOM   2801 C  CA  . GLY B 1 82  ? -22.964 6.333   25.878  1.00 20.68 ? 82  GLY B CA  1 
ATOM   2802 C  C   . GLY B 1 82  ? -24.180 6.967   26.487  1.00 22.14 ? 82  GLY B C   1 
ATOM   2803 O  O   . GLY B 1 82  ? -24.911 7.795   25.846  1.00 22.84 ? 82  GLY B O   1 
ATOM   2804 N  N   . PRO B 1 83  ? -24.399 6.663   27.782  1.00 19.41 ? 83  PRO B N   1 
ATOM   2805 C  CA  . PRO B 1 83  ? -25.481 7.261   28.488  1.00 19.75 ? 83  PRO B CA  1 
ATOM   2806 C  C   . PRO B 1 83  ? -25.167 8.680   28.951  1.00 16.30 ? 83  PRO B C   1 
ATOM   2807 O  O   . PRO B 1 83  ? -26.007 9.311   29.530  1.00 21.71 ? 83  PRO B O   1 
ATOM   2808 C  CB  . PRO B 1 83  ? -25.676 6.310   29.669  1.00 20.14 ? 83  PRO B CB  1 
ATOM   2809 C  CG  . PRO B 1 83  ? -24.275 5.933   30.003  1.00 17.61 ? 83  PRO B CG  1 
ATOM   2810 C  CD  . PRO B 1 83  ? -23.531 5.807   28.661  1.00 18.52 ? 83  PRO B CD  1 
ATOM   2811 N  N   . LEU B 1 84  ? -23.912 9.114   28.766  1.00 14.58 ? 84  LEU B N   1 
ATOM   2812 C  CA  . LEU B 1 84  ? -23.511 10.337  29.473  1.00 15.19 ? 84  LEU B CA  1 
ATOM   2813 C  C   . LEU B 1 84  ? -23.854 11.629  28.733  1.00 15.69 ? 84  LEU B C   1 
ATOM   2814 O  O   . LEU B 1 84  ? -23.744 11.641  27.507  1.00 16.52 ? 84  LEU B O   1 
ATOM   2815 C  CB  . LEU B 1 84  ? -21.992 10.270  29.696  1.00 12.48 ? 84  LEU B CB  1 
ATOM   2816 C  CG  . LEU B 1 84  ? -21.514 8.993   30.476  1.00 12.22 ? 84  LEU B CG  1 
ATOM   2817 C  CD1 . LEU B 1 84  ? -19.971 8.932   30.449  1.00 13.39 ? 84  LEU B CD1 1 
ATOM   2818 C  CD2 . LEU B 1 84  ? -22.049 8.991   31.894  1.00 11.73 ? 84  LEU B CD2 1 
ATOM   2819 N  N   . ASP B 1 85  ? -24.203 12.666  29.499  1.00 16.83 ? 85  ASP B N   1 
ATOM   2820 C  CA  . ASP B 1 85  ? -24.255 14.015  28.905  1.00 18.57 ? 85  ASP B CA  1 
ATOM   2821 C  C   . ASP B 1 85  ? -22.989 14.669  29.349  1.00 21.14 ? 85  ASP B C   1 
ATOM   2822 O  O   . ASP B 1 85  ? -22.611 14.582  30.511  1.00 23.07 ? 85  ASP B O   1 
ATOM   2823 C  CB  . ASP B 1 85  ? -25.469 14.770  29.491  1.00 18.96 ? 85  ASP B CB  1 
ATOM   2824 C  CG  . ASP B 1 85  ? -26.813 14.297  28.923  0.50 14.93 ? 85  ASP B CG  1 
ATOM   2825 O  OD1 . ASP B 1 85  ? -26.945 14.175  27.700  0.50 20.80 ? 85  ASP B OD1 1 
ATOM   2826 O  OD2 . ASP B 1 85  ? -27.747 14.120  29.705  0.50 18.19 ? 85  ASP B OD2 1 
ATOM   2827 N  N   . GLY B 1 86  ? -22.353 15.422  28.480  1.00 24.27 ? 86  GLY B N   1 
ATOM   2828 C  CA  . GLY B 1 86  ? -21.078 16.096  28.862  1.00 22.85 ? 86  GLY B CA  1 
ATOM   2829 C  C   . GLY B 1 86  ? -19.786 15.208  28.880  1.00 18.60 ? 86  GLY B C   1 
ATOM   2830 O  O   . GLY B 1 86  ? -19.732 14.185  28.165  1.00 27.63 ? 86  GLY B O   1 
ATOM   2831 N  N   A THR B 1 87  ? -18.746 15.617  29.628  0.50 15.25 ? 87  THR B N   1 
ATOM   2832 N  N   B THR B 1 87  ? -18.819 15.548  29.735  0.50 15.15 ? 87  THR B N   1 
ATOM   2833 C  CA  A THR B 1 87  ? -17.382 15.043  29.575  0.50 15.55 ? 87  THR B CA  1 
ATOM   2834 C  CA  B THR B 1 87  ? -17.516 14.910  29.690  0.50 14.18 ? 87  THR B CA  1 
ATOM   2835 C  C   A THR B 1 87  ? -17.068 14.638  31.030  0.50 12.53 ? 87  THR B C   1 
ATOM   2836 C  C   B THR B 1 87  ? -16.902 14.683  31.070  0.50 12.70 ? 87  THR B C   1 
ATOM   2837 O  O   A THR B 1 87  ? -17.474 15.356  31.959  0.50 9.86  ? 87  THR B O   1 
ATOM   2838 O  O   B THR B 1 87  ? -16.857 15.538  31.961  0.50 10.91 ? 87  THR B O   1 
ATOM   2839 C  CB  A THR B 1 87  ? -16.325 16.125  29.059  0.50 15.75 ? 87  THR B CB  1 
ATOM   2840 C  CB  B THR B 1 87  ? -16.545 15.749  28.828  0.50 13.92 ? 87  THR B CB  1 
ATOM   2841 O  OG1 A THR B 1 87  ? -16.553 16.484  27.688  0.50 20.72 ? 87  THR B OG1 1 
ATOM   2842 O  OG1 B THR B 1 87  ? -16.442 17.053  29.424  0.50 12.56 ? 87  THR B OG1 1 
ATOM   2843 C  CG2 A THR B 1 87  ? -14.901 15.696  29.180  0.50 14.68 ? 87  THR B CG2 1 
ATOM   2844 C  CG2 B THR B 1 87  ? -17.138 15.855  27.392  0.50 15.73 ? 87  THR B CG2 1 
ATOM   2845 N  N   . TYR B 1 88  ? -16.414 13.480  31.220  1.00 11.95 ? 88  TYR B N   1 
ATOM   2846 C  CA  . TYR B 1 88  ? -15.989 13.010  32.536  1.00 10.32 ? 88  TYR B CA  1 
ATOM   2847 C  C   . TYR B 1 88  ? -14.528 12.719  32.463  1.00 10.01 ? 88  TYR B C   1 
ATOM   2848 O  O   . TYR B 1 88  ? -14.036 12.063  31.545  1.00 14.46 ? 88  TYR B O   1 
ATOM   2849 C  CB  . TYR B 1 88  ? -16.774 11.771  32.938  1.00 10.44 ? 88  TYR B CB  1 
ATOM   2850 C  CG  . TYR B 1 88  ? -18.218 11.984  33.252  1.00 9.89  ? 88  TYR B CG  1 
ATOM   2851 C  CD1 . TYR B 1 88  ? -19.163 12.306  32.257  1.00 12.17 ? 88  TYR B CD1 1 
ATOM   2852 C  CD2 . TYR B 1 88  ? -18.664 11.841  34.575  1.00 8.74  ? 88  TYR B CD2 1 
ATOM   2853 C  CE1 . TYR B 1 88  ? -20.496 12.482  32.564  1.00 10.71 ? 88  TYR B CE1 1 
ATOM   2854 C  CE2 . TYR B 1 88  ? -20.015 11.959  34.862  1.00 9.60  ? 88  TYR B CE2 1 
ATOM   2855 C  CZ  . TYR B 1 88  ? -20.951 12.275  33.871  1.00 10.02 ? 88  TYR B CZ  1 
ATOM   2856 O  OH  . TYR B 1 88  ? -22.248 12.356  34.189  1.00 11.13 ? 88  TYR B OH  1 
ATOM   2857 N  N   . ARG B 1 89  ? -13.764 13.186  33.431  1.00 9.55  ? 89  ARG B N   1 
ATOM   2858 C  CA  . ARG B 1 89  ? -12.339 13.114  33.407  1.00 10.90 ? 89  ARG B CA  1 
ATOM   2859 C  C   . ARG B 1 89  ? -11.787 12.014  34.347  1.00 9.42  ? 89  ARG B C   1 
ATOM   2860 O  O   . ARG B 1 89  ? -12.229 11.893  35.517  1.00 9.35  ? 89  ARG B O   1 
ATOM   2861 C  CB  . ARG B 1 89  ? -11.758 14.441  33.869  1.00 12.59 ? 89  ARG B CB  1 
ATOM   2862 C  CG  . ARG B 1 89  ? -10.274 14.540  33.630  1.00 15.27 ? 89  ARG B CG  1 
ATOM   2863 C  CD  . ARG B 1 89  ? -9.778  15.974  33.973  1.00 16.27 ? 89  ARG B CD  1 
ATOM   2864 N  NE  . ARG B 1 89  ? -10.335 16.959  33.003  1.00 16.72 ? 89  ARG B NE  1 
ATOM   2865 C  CZ  . ARG B 1 89  ? -10.265 18.316  33.205  1.00 16.25 ? 89  ARG B CZ  1 
ATOM   2866 N  NH1 . ARG B 1 89  ? -9.613  18.791  34.263  1.00 18.72 ? 89  ARG B NH1 1 
ATOM   2867 N  NH2 . ARG B 1 89  ? -10.844 19.153  32.364  1.00 17.89 ? 89  ARG B NH2 1 
ATOM   2868 N  N   . LEU B 1 90  ? -10.858 11.185  33.822  1.00 9.83  ? 90  LEU B N   1 
ATOM   2869 C  CA  . LEU B 1 90  ? -10.308 10.071  34.619  1.00 9.06  ? 90  LEU B CA  1 
ATOM   2870 C  C   . LEU B 1 90  ? -9.505  10.646  35.777  1.00 9.41  ? 90  LEU B C   1 
ATOM   2871 O  O   . LEU B 1 90  ? -8.592  11.508  35.609  1.00 11.92 ? 90  LEU B O   1 
ATOM   2872 C  CB  . LEU B 1 90  ? -9.387  9.222   33.731  1.00 10.07 ? 90  LEU B CB  1 
ATOM   2873 C  CG  . LEU B 1 90  ? -8.662  8.065   34.431  1.00 11.04 ? 90  LEU B CG  1 
ATOM   2874 C  CD1 . LEU B 1 90  ? -9.654  7.028   34.957  1.00 13.16 ? 90  LEU B CD1 1 
ATOM   2875 C  CD2 . LEU B 1 90  ? -7.734  7.428   33.432  1.00 14.71 ? 90  LEU B CD2 1 
ATOM   2876 N  N   . ILE B 1 91  ? -9.754  10.166  36.991  1.00 8.84  ? 91  ILE B N   1 
ATOM   2877 C  CA  . ILE B 1 91  ? -8.981  10.513  38.195  1.00 9.62  ? 91  ILE B CA  1 
ATOM   2878 C  C   . ILE B 1 91  ? -8.214  9.351   38.760  1.00 8.97  ? 91  ILE B C   1 
ATOM   2879 O  O   . ILE B 1 91  ? -7.074  9.532   39.195  1.00 9.44  ? 91  ILE B O   1 
ATOM   2880 C  CB  . ILE B 1 91  ? -9.828  11.264  39.252  1.00 9.72  ? 91  ILE B CB  1 
ATOM   2881 C  CG1 . ILE B 1 91  ? -9.043  11.575  40.508  1.00 13.52 ? 91  ILE B CG1 1 
ATOM   2882 C  CG2 . ILE B 1 91  ? -11.106 10.478  39.591  1.00 11.53 ? 91  ILE B CG2 1 
ATOM   2883 C  CD1 . ILE B 1 91  ? -9.722  12.582  41.411  1.00 16.53 ? 91  ILE B CD1 1 
ATOM   2884 N  N   . GLN B 1 92  ? -8.800  8.125   38.767  1.00 9.51  ? 92  GLN B N   1 
ATOM   2885 C  CA  . GLN B 1 92  ? -8.043  7.014   39.325  1.00 8.37  ? 92  GLN B CA  1 
ATOM   2886 C  C   . GLN B 1 92  ? -8.639  5.735   38.837  1.00 8.52  ? 92  GLN B C   1 
ATOM   2887 O  O   . GLN B 1 92  ? -9.778  5.746   38.379  1.00 8.61  ? 92  GLN B O   1 
ATOM   2888 C  CB  . GLN B 1 92  ? -8.072  7.045   40.868  1.00 10.47 ? 92  GLN B CB  1 
ATOM   2889 C  CG  . GLN B 1 92  ? -9.457  7.043   41.535  1.00 12.05 ? 92  GLN B CG  1 
ATOM   2890 C  CD  . GLN B 1 92  ? -9.648  5.733   42.282  1.00 12.31 ? 92  GLN B CD  1 
ATOM   2891 O  OE1 . GLN B 1 92  ? -9.772  4.694   41.630  1.00 14.09 ? 92  GLN B OE1 1 
ATOM   2892 N  NE2 . GLN B 1 92  ? -9.551  5.751   43.557  1.00 19.32 ? 92  GLN B NE2 1 
ATOM   2893 N  N   . PHE B 1 93  ? -7.922  4.608   38.938  1.00 9.14  ? 93  PHE B N   1 
ATOM   2894 C  CA  . PHE B 1 93  ? -8.562  3.291   38.859  1.00 8.49  ? 93  PHE B CA  1 
ATOM   2895 C  C   . PHE B 1 93  ? -8.150  2.486   40.049  1.00 7.36  ? 93  PHE B C   1 
ATOM   2896 O  O   . PHE B 1 93  ? -7.101  2.674   40.683  1.00 8.90  ? 93  PHE B O   1 
ATOM   2897 C  CB  . PHE B 1 93  ? -8.333  2.575   37.505  1.00 9.11  ? 93  PHE B CB  1 
ATOM   2898 C  CG  . PHE B 1 93  ? -6.896  2.166   37.258  1.00 9.05  ? 93  PHE B CG  1 
ATOM   2899 C  CD1 . PHE B 1 93  ? -6.395  0.984   37.809  1.00 10.69 ? 93  PHE B CD1 1 
ATOM   2900 C  CD2 . PHE B 1 93  ? -6.130  2.823   36.266  1.00 10.44 ? 93  PHE B CD2 1 
ATOM   2901 C  CE1 . PHE B 1 93  ? -5.085  0.565   37.559  1.00 10.47 ? 93  PHE B CE1 1 
ATOM   2902 C  CE2 . PHE B 1 93  ? -4.853  2.395   35.995  1.00 10.67 ? 93  PHE B CE2 1 
ATOM   2903 C  CZ  . PHE B 1 93  ? -4.338  1.266   36.651  1.00 10.72 ? 93  PHE B CZ  1 
ATOM   2904 N  N   . HIS B 1 94  ? -8.954  1.449   40.359  1.00 8.29  ? 94  HIS B N   1 
ATOM   2905 C  CA  . HIS B 1 94  ? -8.667  0.485   41.421  1.00 7.44  ? 94  HIS B CA  1 
ATOM   2906 C  C   . HIS B 1 94  ? -9.359  -0.802  41.072  1.00 6.87  ? 94  HIS B C   1 
ATOM   2907 O  O   . HIS B 1 94  ? -10.149 -0.861  40.127  1.00 7.56  ? 94  HIS B O   1 
ATOM   2908 C  CB  . HIS B 1 94  ? -9.106  0.997   42.783  1.00 8.06  ? 94  HIS B CB  1 
ATOM   2909 C  CG  . HIS B 1 94  ? -10.591 1.275   42.809  1.00 7.87  ? 94  HIS B CG  1 
ATOM   2910 N  ND1 . HIS B 1 94  ? -11.165 2.468   42.414  1.00 8.06  ? 94  HIS B ND1 1 
ATOM   2911 C  CD2 . HIS B 1 94  ? -11.621 0.432   43.089  1.00 6.77  ? 94  HIS B CD2 1 
ATOM   2912 C  CE1 . HIS B 1 94  ? -12.520 2.336   42.479  1.00 7.85  ? 94  HIS B CE1 1 
ATOM   2913 N  NE2 . HIS B 1 94  ? -12.819 1.084   42.876  1.00 6.93  ? 94  HIS B NE2 1 
ATOM   2914 N  N   . PHE B 1 95  ? -9.135  -1.838  41.890  1.00 7.29  ? 95  PHE B N   1 
ATOM   2915 C  CA  . PHE B 1 95  ? -9.752  -3.136  41.654  1.00 7.36  ? 95  PHE B CA  1 
ATOM   2916 C  C   . PHE B 1 95  ? -10.424 -3.601  42.954  1.00 7.25  ? 95  PHE B C   1 
ATOM   2917 O  O   . PHE B 1 95  ? -10.085 -3.168  44.064  1.00 9.00  ? 95  PHE B O   1 
ATOM   2918 C  CB  . PHE B 1 95  ? -8.734  -4.215  41.291  1.00 8.88  ? 95  PHE B CB  1 
ATOM   2919 C  CG  . PHE B 1 95  ? -7.965  -3.933  40.011  1.00 7.43  ? 95  PHE B CG  1 
ATOM   2920 C  CD1 . PHE B 1 95  ? -6.892  -3.031  39.986  1.00 8.06  ? 95  PHE B CD1 1 
ATOM   2921 C  CD2 . PHE B 1 95  ? -8.282  -4.581  38.823  1.00 8.54  ? 95  PHE B CD2 1 
ATOM   2922 C  CE1 . PHE B 1 95  ? -6.119  -2.827  38.855  1.00 9.65  ? 95  PHE B CE1 1 
ATOM   2923 C  CE2 . PHE B 1 95  ? -7.503  -4.420  37.675  1.00 9.38  ? 95  PHE B CE2 1 
ATOM   2924 C  CZ  . PHE B 1 95  ? -6.436  -3.488  37.711  1.00 9.31  ? 95  PHE B CZ  1 
ATOM   2925 N  N   . HIS B 1 96  ? -11.318 -4.565  42.788  1.00 8.12  ? 96  HIS B N   1 
ATOM   2926 C  CA  . HIS B 1 96  ? -11.852 -5.353  43.909  1.00 6.73  ? 96  HIS B CA  1 
ATOM   2927 C  C   . HIS B 1 96  ? -11.604 -6.824  43.533  1.00 7.68  ? 96  HIS B C   1 
ATOM   2928 O  O   . HIS B 1 96  ? -11.737 -7.188  42.329  1.00 7.94  ? 96  HIS B O   1 
ATOM   2929 C  CB  . HIS B 1 96  ? -13.397 -5.163  44.039  1.00 7.77  ? 96  HIS B CB  1 
ATOM   2930 C  CG  . HIS B 1 96  ? -13.787 -3.732  44.238  1.00 7.15  ? 96  HIS B CG  1 
ATOM   2931 N  ND1 . HIS B 1 96  ? -13.980 -3.178  45.463  1.00 7.27  ? 96  HIS B ND1 1 
ATOM   2932 C  CD2 . HIS B 1 96  ? -13.915 -2.709  43.324  1.00 8.16  ? 96  HIS B CD2 1 
ATOM   2933 C  CE1 . HIS B 1 96  ? -14.300 -1.848  45.272  1.00 8.39  ? 96  HIS B CE1 1 
ATOM   2934 N  NE2 . HIS B 1 96  ? -14.194 -1.560  43.983  1.00 6.84  ? 96  HIS B NE2 1 
ATOM   2935 N  N   . TRP B 1 97  ? -11.246 -7.685  44.483  1.00 6.98  ? 97  TRP B N   1 
ATOM   2936 C  CA  . TRP B 1 97  ? -10.902 -9.074  44.159  1.00 7.15  ? 97  TRP B CA  1 
ATOM   2937 C  C   . TRP B 1 97  ? -11.153 -9.985  45.339  1.00 6.58  ? 97  TRP B C   1 
ATOM   2938 O  O   . TRP B 1 97  ? -11.491 -9.542  46.469  1.00 7.75  ? 97  TRP B O   1 
ATOM   2939 C  CB  . TRP B 1 97  ? -9.433  -9.189  43.705  1.00 8.12  ? 97  TRP B CB  1 
ATOM   2940 C  CG  . TRP B 1 97  ? -8.429  -8.800  44.725  1.00 7.72  ? 97  TRP B CG  1 
ATOM   2941 C  CD1 . TRP B 1 97  ? -7.867  -9.634  45.681  1.00 8.12  ? 97  TRP B CD1 1 
ATOM   2942 C  CD2 . TRP B 1 97  ? -7.908  -7.480  44.959  1.00 8.51  ? 97  TRP B CD2 1 
ATOM   2943 N  NE1 . TRP B 1 97  ? -6.925  -8.929  46.405  1.00 9.20  ? 97  TRP B NE1 1 
ATOM   2944 C  CE2 . TRP B 1 97  ? -6.953  -7.585  46.029  1.00 8.25  ? 97  TRP B CE2 1 
ATOM   2945 C  CE3 . TRP B 1 97  ? -8.147  -6.199  44.389  1.00 8.29  ? 97  TRP B CE3 1 
ATOM   2946 C  CZ2 . TRP B 1 97  ? -6.249  -6.498  46.479  1.00 9.50  ? 97  TRP B CZ2 1 
ATOM   2947 C  CZ3 . TRP B 1 97  ? -7.442  -5.090  44.873  1.00 8.18  ? 97  TRP B CZ3 1 
ATOM   2948 C  CH2 . TRP B 1 97  ? -6.486  -5.244  45.886  1.00 9.87  ? 97  TRP B CH2 1 
ATOM   2949 N  N   . GLY B 1 98  ? -11.072 -11.288 45.036  1.00 7.31  ? 98  GLY B N   1 
ATOM   2950 C  CA  . GLY B 1 98  ? -11.470 -12.279 45.986  1.00 8.15  ? 98  GLY B CA  1 
ATOM   2951 C  C   . GLY B 1 98  ? -10.260 -12.972 46.632  1.00 8.66  ? 98  GLY B C   1 
ATOM   2952 O  O   . GLY B 1 98  ? -9.126  -12.841 46.241  1.00 10.04 ? 98  GLY B O   1 
ATOM   2953 N  N   . SER B 1 99  ? -10.628 -13.860 47.599  1.00 10.19 ? 99  SER B N   1 
ATOM   2954 C  CA  . SER B 1 99  ? -9.668  -14.814 48.231  1.00 10.51 ? 99  SER B CA  1 
ATOM   2955 C  C   . SER B 1 99  ? -9.535  -16.068 47.366  1.00 11.78 ? 99  SER B C   1 
ATOM   2956 O  O   . SER B 1 99  ? -8.558  -16.823 47.588  1.00 14.25 ? 99  SER B O   1 
ATOM   2957 C  CB  . SER B 1 99  ? -10.168 -15.137 49.654  1.00 11.10 ? 99  SER B CB  1 
ATOM   2958 O  OG  . SER B 1 99  ? -11.454 -15.665 49.597  1.00 12.56 ? 99  SER B OG  1 
ATOM   2959 N  N   . LEU B 1 100 ? -10.458 -16.299 46.437  1.00 11.16 ? 100 LEU B N   1 
ATOM   2960 C  CA  . LEU B 1 100 ? -10.551 -17.442 45.576  1.00 13.10 ? 100 LEU B CA  1 
ATOM   2961 C  C   . LEU B 1 100 ? -10.943 -16.975 44.205  1.00 10.59 ? 100 LEU B C   1 
ATOM   2962 O  O   . LEU B 1 100 ? -11.621 -15.945 44.093  1.00 11.09 ? 100 LEU B O   1 
ATOM   2963 C  CB  . LEU B 1 100 ? -11.722 -18.373 45.996  1.00 16.58 ? 100 LEU B CB  1 
ATOM   2964 C  CG  . LEU B 1 100 ? -11.587 -18.814 47.440  1.00 17.31 ? 100 LEU B CG  1 
ATOM   2965 C  CD1 . LEU B 1 100 ? -12.914 -19.193 48.048  1.00 24.53 ? 100 LEU B CD1 1 
ATOM   2966 C  CD2 . LEU B 1 100 ? -10.552 -19.937 47.569  1.00 24.01 ? 100 LEU B CD2 1 
ATOM   2967 N  N   . ASP B 1 101 ? -10.655 -17.684 43.110  1.00 10.54 ? 101 ASP B N   1 
ATOM   2968 C  CA  . ASP B 1 101 ? -10.959 -17.222 41.744  1.00 11.52 ? 101 ASP B CA  1 
ATOM   2969 C  C   . ASP B 1 101 ? -12.448 -17.154 41.525  1.00 12.33 ? 101 ASP B C   1 
ATOM   2970 O  O   . ASP B 1 101 ? -12.878 -16.452 40.657  1.00 12.91 ? 101 ASP B O   1 
ATOM   2971 C  CB  . ASP B 1 101 ? -10.335 -18.122 40.663  1.00 11.13 ? 101 ASP B CB  1 
ATOM   2972 C  CG  . ASP B 1 101 ? -8.807  -18.220 40.749  1.00 14.06 ? 101 ASP B CG  1 
ATOM   2973 O  OD1 . ASP B 1 101 ? -8.133  -17.293 41.235  1.00 13.82 ? 101 ASP B OD1 1 
ATOM   2974 O  OD2 . ASP B 1 101 ? -8.278  -19.215 40.240  1.00 18.32 ? 101 ASP B OD2 1 
ATOM   2975 N  N   . GLY B 1 102 ? -13.234 -17.883 42.352  1.00 11.64 ? 102 GLY B N   1 
ATOM   2976 C  CA  . GLY B 1 102 ? -14.683 -17.883 42.174  1.00 12.35 ? 102 GLY B CA  1 
ATOM   2977 C  C   . GLY B 1 102 ? -15.461 -16.729 42.775  1.00 11.51 ? 102 GLY B C   1 
ATOM   2978 O  O   . GLY B 1 102 ? -16.673 -16.702 42.706  1.00 12.72 ? 102 GLY B O   1 
ATOM   2979 N  N   . GLN B 1 103 ? -14.770 -15.692 43.284  1.00 10.35 ? 103 GLN B N   1 
ATOM   2980 C  CA  . GLN B 1 103 ? -15.486 -14.511 43.808  1.00 8.28  ? 103 GLN B CA  1 
ATOM   2981 C  C   . GLN B 1 103 ? -14.484 -13.368 43.704  1.00 7.44  ? 103 GLN B C   1 
ATOM   2982 O  O   . GLN B 1 103 ? -13.290 -13.562 43.533  1.00 9.22  ? 103 GLN B O   1 
ATOM   2983 C  CB  . GLN B 1 103 ? -15.945 -14.767 45.222  1.00 9.58  ? 103 GLN B CB  1 
ATOM   2984 C  CG  . GLN B 1 103 ? -14.792 -14.988 46.209  1.00 10.34 ? 103 GLN B CG  1 
ATOM   2985 C  CD  . GLN B 1 103 ? -15.275 -15.622 47.481  1.00 13.05 ? 103 GLN B CD  1 
ATOM   2986 O  OE1 . GLN B 1 103 ? -16.006 -16.635 47.458  1.00 18.99 ? 103 GLN B OE1 1 
ATOM   2987 N  NE2 . GLN B 1 103 ? -14.872 -15.081 48.619  1.00 12.90 ? 103 GLN B NE2 1 
ATOM   2988 N  N   . GLY B 1 104 ? -15.050 -12.150 43.868  1.00 7.94  ? 104 GLY B N   1 
ATOM   2989 C  CA  . GLY B 1 104 ? -14.198 -10.972 43.826  1.00 7.69  ? 104 GLY B CA  1 
ATOM   2990 C  C   . GLY B 1 104 ? -14.880 -9.812  43.161  1.00 7.77  ? 104 GLY B C   1 
ATOM   2991 O  O   . GLY B 1 104 ? -14.587 -8.649  43.536  1.00 8.52  ? 104 GLY B O   1 
ATOM   2992 N  N   . SER B 1 105 ? -15.684 -10.056 42.116  1.00 7.46  ? 105 SER B N   1 
ATOM   2993 C  CA  . SER B 1 105 ? -16.356 -8.920  41.474  1.00 7.70  ? 105 SER B CA  1 
ATOM   2994 C  C   . SER B 1 105 ? -17.460 -8.387  42.391  1.00 7.22  ? 105 SER B C   1 
ATOM   2995 O  O   . SER B 1 105 ? -17.990 -9.070  43.299  1.00 8.71  ? 105 SER B O   1 
ATOM   2996 C  CB  . SER B 1 105 ? -16.875 -9.263  40.123  1.00 8.54  ? 105 SER B CB  1 
ATOM   2997 O  OG  . SER B 1 105 ? -17.934 -10.252 40.150  1.00 7.82  ? 105 SER B OG  1 
ATOM   2998 N  N   . GLU B 1 106 ? -17.780 -7.128  42.138  1.00 7.01  ? 106 GLU B N   1 
ATOM   2999 C  CA  . GLU B 1 106 ? -18.891 -6.404  42.854  1.00 7.70  ? 106 GLU B CA  1 
ATOM   3000 C  C   . GLU B 1 106 ? -20.199 -6.617  42.038  1.00 7.47  ? 106 GLU B C   1 
ATOM   3001 O  O   . GLU B 1 106 ? -21.164 -7.189  42.568  1.00 7.49  ? 106 GLU B O   1 
ATOM   3002 C  CB  . GLU B 1 106 ? -18.526 -4.925  43.030  1.00 7.84  ? 106 GLU B CB  1 
ATOM   3003 C  CG  . GLU B 1 106 ? -17.248 -4.772  43.900  1.00 8.86  ? 106 GLU B CG  1 
ATOM   3004 C  CD  . GLU B 1 106 ? -17.280 -3.532  44.652  1.00 8.84  ? 106 GLU B CD  1 
ATOM   3005 O  OE1 . GLU B 1 106 ? -17.295 -2.472  44.008  1.00 8.54  ? 106 GLU B OE1 1 
ATOM   3006 O  OE2 . GLU B 1 106 ? -17.240 -3.558  45.885  1.00 9.44  ? 106 GLU B OE2 1 
ATOM   3007 N  N   . HIS B 1 107 ? -20.212 -6.187  40.798  1.00 7.20  ? 107 HIS B N   1 
ATOM   3008 C  CA  . HIS B 1 107 ? -21.341 -6.549  39.934  1.00 6.80  ? 107 HIS B CA  1 
ATOM   3009 C  C   . HIS B 1 107 ? -21.287 -8.048  39.652  1.00 7.65  ? 107 HIS B C   1 
ATOM   3010 O  O   . HIS B 1 107 ? -20.181 -8.617  39.636  1.00 7.47  ? 107 HIS B O   1 
ATOM   3011 C  CB  . HIS B 1 107 ? -21.325 -5.771  38.613  1.00 7.75  ? 107 HIS B CB  1 
ATOM   3012 C  CG  . HIS B 1 107 ? -21.555 -4.301  38.889  1.00 7.82  ? 107 HIS B CG  1 
ATOM   3013 N  ND1 . HIS B 1 107 ? -20.512 -3.422  39.171  1.00 7.67  ? 107 HIS B ND1 1 
ATOM   3014 C  CD2 . HIS B 1 107 ? -22.716 -3.576  38.995  1.00 8.24  ? 107 HIS B CD2 1 
ATOM   3015 C  CE1 . HIS B 1 107 ? -21.086 -2.180  39.448  1.00 7.34  ? 107 HIS B CE1 1 
ATOM   3016 N  NE2 . HIS B 1 107 ? -22.397 -2.286  39.335  1.00 7.17  ? 107 HIS B NE2 1 
ATOM   3017 N  N   . THR B 1 108 ? -22.458 -8.611  39.385  1.00 8.24  ? 108 THR B N   1 
ATOM   3018 C  CA  . THR B 1 108 ? -22.513 -9.996  38.979  1.00 8.77  ? 108 THR B CA  1 
ATOM   3019 C  C   . THR B 1 108 ? -23.338 -9.986  37.690  1.00 7.60  ? 108 THR B C   1 
ATOM   3020 O  O   . THR B 1 108 ? -24.109 -9.019  37.401  1.00 8.82  ? 108 THR B O   1 
ATOM   3021 C  CB  . THR B 1 108 ? -23.129 -10.898 40.048  1.00 8.81  ? 108 THR B CB  1 
ATOM   3022 O  OG1 . THR B 1 108 ? -24.388 -10.413 40.505  1.00 9.65  ? 108 THR B OG1 1 
ATOM   3023 C  CG2 . THR B 1 108 ? -22.153 -10.959 41.236  1.00 10.72 ? 108 THR B CG2 1 
ATOM   3024 N  N   . VAL B 1 109 ? -23.219 -11.039 36.899  1.00 8.87  ? 109 VAL B N   1 
ATOM   3025 C  CA  . VAL B 1 109 ? -23.988 -11.134 35.614  1.00 9.34  ? 109 VAL B CA  1 
ATOM   3026 C  C   . VAL B 1 109 ? -24.815 -12.460 35.638  1.00 9.17  ? 109 VAL B C   1 
ATOM   3027 O  O   . VAL B 1 109 ? -24.203 -13.555 35.682  1.00 9.92  ? 109 VAL B O   1 
ATOM   3028 C  CB  . VAL B 1 109 ? -22.988 -11.189 34.429  1.00 9.96  ? 109 VAL B CB  1 
ATOM   3029 C  CG1 . VAL B 1 109 ? -23.710 -11.329 33.085  1.00 12.26 ? 109 VAL B CG1 1 
ATOM   3030 C  CG2 . VAL B 1 109 ? -22.120 -9.938  34.407  1.00 11.68 ? 109 VAL B CG2 1 
ATOM   3031 N  N   . ASP B 1 110 ? -26.127 -12.314 35.734  1.00 9.97  ? 110 ASP B N   1 
ATOM   3032 C  CA  . ASP B 1 110 ? -26.990 -13.511 35.980  1.00 11.47 ? 110 ASP B CA  1 
ATOM   3033 C  C   . ASP B 1 110 ? -26.414 -14.335 37.163  1.00 10.55 ? 110 ASP B C   1 
ATOM   3034 O  O   . ASP B 1 110 ? -26.323 -15.579 37.117  1.00 11.63 ? 110 ASP B O   1 
ATOM   3035 C  CB  . ASP B 1 110 ? -27.131 -14.311 34.725  1.00 14.18 ? 110 ASP B CB  1 
ATOM   3036 C  CG  . ASP B 1 110 ? -27.786 -13.490 33.602  1.00 12.87 ? 110 ASP B CG  1 
ATOM   3037 O  OD1 . ASP B 1 110 ? -28.658 -12.681 33.938  1.00 15.04 ? 110 ASP B OD1 1 
ATOM   3038 O  OD2 . ASP B 1 110 ? -27.449 -13.794 32.462  1.00 17.06 ? 110 ASP B OD2 1 
ATOM   3039 N  N   . LYS B 1 111 ? -25.991 -13.634 38.243  1.00 10.27 ? 111 LYS B N   1 
ATOM   3040 C  CA  . LYS B 1 111 ? -25.464 -14.171 39.509  1.00 10.59 ? 111 LYS B CA  1 
ATOM   3041 C  C   . LYS B 1 111 ? -24.014 -14.692 39.398  1.00 10.49 ? 111 LYS B C   1 
ATOM   3042 O  O   . LYS B 1 111 ? -23.415 -15.092 40.403  1.00 11.73 ? 111 LYS B O   1 
ATOM   3043 C  CB  . LYS B 1 111 ? -26.376 -15.229 40.118  1.00 13.08 ? 111 LYS B CB  1 
ATOM   3044 C  CG  . LYS B 1 111 ? -27.784 -14.664 40.397  1.00 14.93 ? 111 LYS B CG  1 
ATOM   3045 C  CD  . LYS B 1 111 ? -27.760 -13.472 41.387  1.00 18.46 ? 111 LYS B CD  1 
ATOM   3046 C  CE  . LYS B 1 111 ? -29.131 -12.943 41.812  1.00 22.18 ? 111 LYS B CE  1 
ATOM   3047 N  NZ  . LYS B 1 111 ? -29.623 -13.658 42.969  1.00 22.25 ? 111 LYS B NZ  1 
ATOM   3048 N  N   . LYS B 1 112 ? -23.438 -14.654 38.198  1.00 9.44  ? 112 LYS B N   1 
ATOM   3049 C  CA  . LYS B 1 112 ? -22.034 -15.041 38.041  1.00 9.74  ? 112 LYS B CA  1 
ATOM   3050 C  C   . LYS B 1 112 ? -21.121 -14.001 38.699  1.00 9.22  ? 112 LYS B C   1 
ATOM   3051 O  O   . LYS B 1 112 ? -21.251 -12.797 38.439  1.00 9.53  ? 112 LYS B O   1 
ATOM   3052 C  CB  . LYS B 1 112 ? -21.618 -15.155 36.557  1.00 11.05 ? 112 LYS B CB  1 
ATOM   3053 C  CG  . LYS B 1 112 ? -20.151 -15.518 36.317  1.00 11.86 ? 112 LYS B CG  1 
ATOM   3054 C  CD  . LYS B 1 112 ? -19.792 -15.552 34.846  1.00 15.44 ? 112 LYS B CD  1 
ATOM   3055 C  CE  . LYS B 1 112 ? -18.304 -15.723 34.701  1.00 16.79 ? 112 LYS B CE  1 
ATOM   3056 N  NZ  . LYS B 1 112 ? -17.847 -17.023 35.112  1.00 16.57 ? 112 LYS B NZ  1 
ATOM   3057 N  N   A LYS B 1 113 ? -20.225 -14.481 39.541  0.50 8.87  ? 113 LYS B N   1 
ATOM   3058 N  N   B LYS B 1 113 ? -20.201 -14.493 39.524  0.50 9.15  ? 113 LYS B N   1 
ATOM   3059 C  CA  A LYS B 1 113 ? -19.169 -13.670 40.091  0.50 8.64  ? 113 LYS B CA  1 
ATOM   3060 C  CA  B LYS B 1 113 ? -19.137 -13.697 40.131  0.50 9.09  ? 113 LYS B CA  1 
ATOM   3061 C  C   A LYS B 1 113 ? -17.894 -13.891 39.266  0.50 8.99  ? 113 LYS B C   1 
ATOM   3062 C  C   B LYS B 1 113 ? -17.780 -13.907 39.439  0.50 9.74  ? 113 LYS B C   1 
ATOM   3063 O  O   A LYS B 1 113 ? -17.601 -15.036 38.893  0.50 8.51  ? 113 LYS B O   1 
ATOM   3064 O  O   B LYS B 1 113 ? -17.303 -15.054 39.337  0.50 9.56  ? 113 LYS B O   1 
ATOM   3065 C  CB  A LYS B 1 113 ? -18.898 -14.123 41.555  0.50 9.06  ? 113 LYS B CB  1 
ATOM   3066 C  CB  B LYS B 1 113 ? -18.951 -14.113 41.617  0.50 9.36  ? 113 LYS B CB  1 
ATOM   3067 C  CG  A LYS B 1 113 ? -20.097 -13.953 42.471  0.50 9.36  ? 113 LYS B CG  1 
ATOM   3068 C  CG  B LYS B 1 113 ? -20.077 -13.637 42.513  0.50 10.47 ? 113 LYS B CG  1 
ATOM   3069 C  CD  A LYS B 1 113 ? -19.810 -14.626 43.816  0.50 9.70  ? 113 LYS B CD  1 
ATOM   3070 C  CD  B LYS B 1 113 ? -19.887 -14.143 43.934  0.50 9.96  ? 113 LYS B CD  1 
ATOM   3071 C  CE  A LYS B 1 113 ? -20.536 -13.955 44.974  0.50 10.00 ? 113 LYS B CE  1 
ATOM   3072 C  CE  B LYS B 1 113 ? -21.054 -13.643 44.809  0.50 10.94 ? 113 LYS B CE  1 
ATOM   3073 N  NZ  A LYS B 1 113 ? -21.962 -14.404 45.065  0.50 11.56 ? 113 LYS B NZ  1 
ATOM   3074 N  NZ  B LYS B 1 113 ? -21.054 -14.410 46.095  0.50 14.64 ? 113 LYS B NZ  1 
ATOM   3075 N  N   . TYR B 1 114 ? -17.155 -12.821 38.991  1.00 8.80  ? 114 TYR B N   1 
ATOM   3076 C  CA  . TYR B 1 114 ? -15.864 -12.900 38.337  1.00 8.17  ? 114 TYR B CA  1 
ATOM   3077 C  C   . TYR B 1 114 ? -14.764 -12.849 39.422  1.00 7.68  ? 114 TYR B C   1 
ATOM   3078 O  O   . TYR B 1 114 ? -15.053 -12.544 40.617  1.00 8.08  ? 114 TYR B O   1 
ATOM   3079 C  CB  . TYR B 1 114 ? -15.686 -11.769 37.333  1.00 7.71  ? 114 TYR B CB  1 
ATOM   3080 C  CG  . TYR B 1 114 ? -16.452 -11.987 36.048  1.00 8.49  ? 114 TYR B CG  1 
ATOM   3081 C  CD1 . TYR B 1 114 ? -17.775 -11.569 35.916  1.00 10.17 ? 114 TYR B CD1 1 
ATOM   3082 C  CD2 . TYR B 1 114 ? -15.858 -12.615 34.970  1.00 10.24 ? 114 TYR B CD2 1 
ATOM   3083 C  CE1 . TYR B 1 114 ? -18.481 -11.784 34.748  1.00 11.33 ? 114 TYR B CE1 1 
ATOM   3084 C  CE2 . TYR B 1 114 ? -16.551 -12.820 33.793  1.00 12.74 ? 114 TYR B CE2 1 
ATOM   3085 C  CZ  . TYR B 1 114 ? -17.860 -12.401 33.690  1.00 12.21 ? 114 TYR B CZ  1 
ATOM   3086 O  OH  . TYR B 1 114 ? -18.565 -12.601 32.526  1.00 16.63 ? 114 TYR B OH  1 
ATOM   3087 N  N   . ALA B 1 115 ? -13.519 -13.133 39.073  1.00 7.08  ? 115 ALA B N   1 
ATOM   3088 C  CA  . ALA B 1 115 ? -12.414 -13.167 40.024  1.00 7.96  ? 115 ALA B CA  1 
ATOM   3089 C  C   . ALA B 1 115 ? -12.097 -11.752 40.568  1.00 8.26  ? 115 ALA B C   1 
ATOM   3090 O  O   . ALA B 1 115 ? -11.507 -11.596 41.624  1.00 8.13  ? 115 ALA B O   1 
ATOM   3091 C  CB  . ALA B 1 115 ? -11.216 -13.826 39.336  1.00 9.26  ? 115 ALA B CB  1 
ATOM   3092 N  N   . ALA B 1 116 ? -12.364 -10.743 39.725  1.00 8.08  ? 116 ALA B N   1 
ATOM   3093 C  CA  . ALA B 1 116 ? -12.051 -9.332  40.159  1.00 8.16  ? 116 ALA B CA  1 
ATOM   3094 C  C   . ALA B 1 116 ? -12.832 -8.404  39.265  1.00 7.86  ? 116 ALA B C   1 
ATOM   3095 O  O   . ALA B 1 116 ? -13.444 -8.818  38.274  1.00 7.47  ? 116 ALA B O   1 
ATOM   3096 C  CB  . ALA B 1 116 ? -10.511 -9.114  40.108  1.00 7.82  ? 116 ALA B CB  1 
ATOM   3097 N  N   . GLU B 1 117 ? -12.761 -7.132  39.626  1.00 7.80  ? 117 GLU B N   1 
ATOM   3098 C  CA  . GLU B 1 117 ? -13.455 -6.090  38.862  1.00 7.85  ? 117 GLU B CA  1 
ATOM   3099 C  C   . GLU B 1 117 ? -12.588 -4.799  38.944  1.00 8.01  ? 117 GLU B C   1 
ATOM   3100 O  O   . GLU B 1 117 ? -12.204 -4.410  40.056  1.00 8.42  ? 117 GLU B O   1 
ATOM   3101 C  CB  . GLU B 1 117 ? -14.865 -5.884  39.408  1.00 7.92  ? 117 GLU B CB  1 
ATOM   3102 C  CG  . GLU B 1 117 ? -15.721 -4.931  38.506  1.00 8.31  ? 117 GLU B CG  1 
ATOM   3103 C  CD  . GLU B 1 117 ? -17.193 -4.884  38.989  1.00 8.26  ? 117 GLU B CD  1 
ATOM   3104 O  OE1 . GLU B 1 117 ? -17.671 -5.879  39.567  1.00 8.56  ? 117 GLU B OE1 1 
ATOM   3105 O  OE2 . GLU B 1 117 ? -17.803 -3.798  38.797  1.00 8.53  ? 117 GLU B OE2 1 
ATOM   3106 N  N   . LEU B 1 118 ? -12.279 -4.238  37.759  1.00 7.44  ? 118 LEU B N   1 
ATOM   3107 C  CA  . LEU B 1 118 ? -11.531 -3.003  37.623  1.00 6.68  ? 118 LEU B CA  1 
ATOM   3108 C  C   . LEU B 1 118 ? -12.536 -1.871  37.519  1.00 6.47  ? 118 LEU B C   1 
ATOM   3109 O  O   . LEU B 1 118 ? -13.507 -1.939  36.715  1.00 7.34  ? 118 LEU B O   1 
ATOM   3110 C  CB  . LEU B 1 118 ? -10.728 -3.108  36.302  1.00 8.35  ? 118 LEU B CB  1 
ATOM   3111 C  CG  . LEU B 1 118 ? -10.160 -1.785  35.704  1.00 7.98  ? 118 LEU B CG  1 
ATOM   3112 C  CD1 . LEU B 1 118 ? -9.186  -1.117  36.660  1.00 9.42  ? 118 LEU B CD1 1 
ATOM   3113 C  CD2 . LEU B 1 118 ? -9.423  -2.141  34.431  1.00 9.31  ? 118 LEU B CD2 1 
ATOM   3114 N  N   . HIS B 1 119 ? -12.305 -0.775  38.263  1.00 6.46  ? 119 HIS B N   1 
ATOM   3115 C  CA  . HIS B 1 119 ? -13.133 0.441   38.219  1.00 7.14  ? 119 HIS B CA  1 
ATOM   3116 C  C   . HIS B 1 119 ? -12.289 1.623   37.856  1.00 6.62  ? 119 HIS B C   1 
ATOM   3117 O  O   . HIS B 1 119 ? -11.306 1.964   38.555  1.00 7.50  ? 119 HIS B O   1 
ATOM   3118 C  CB  . HIS B 1 119 ? -13.728 0.680   39.629  1.00 6.21  ? 119 HIS B CB  1 
ATOM   3119 C  CG  . HIS B 1 119 ? -14.808 -0.311  39.948  1.00 6.76  ? 119 HIS B CG  1 
ATOM   3120 N  ND1 . HIS B 1 119 ? -15.262 -0.563  41.237  1.00 7.20  ? 119 HIS B ND1 1 
ATOM   3121 C  CD2 . HIS B 1 119 ? -15.497 -1.137  39.134  1.00 8.10  ? 119 HIS B CD2 1 
ATOM   3122 C  CE1 . HIS B 1 119 ? -16.209 -1.472  41.212  1.00 8.04  ? 119 HIS B CE1 1 
ATOM   3123 N  NE2 . HIS B 1 119 ? -16.377 -1.843  39.914  1.00 8.63  ? 119 HIS B NE2 1 
ATOM   3124 N  N   . LEU B 1 120 ? -12.623 2.208   36.680  1.00 7.70  ? 120 LEU B N   1 
ATOM   3125 C  CA  . LEU B 1 120 ? -11.972 3.497   36.239  1.00 8.26  ? 120 LEU B CA  1 
ATOM   3126 C  C   . LEU B 1 120 ? -12.937 4.603   36.564  1.00 6.97  ? 120 LEU B C   1 
ATOM   3127 O  O   . LEU B 1 120 ? -14.052 4.629   36.075  1.00 7.44  ? 120 LEU B O   1 
ATOM   3128 C  CB  . LEU B 1 120 ? -11.636 3.414   34.749  1.00 8.67  ? 120 LEU B CB  1 
ATOM   3129 C  CG  . LEU B 1 120 ? -10.590 2.345   34.404  1.00 9.20  ? 120 LEU B CG  1 
ATOM   3130 C  CD1 . LEU B 1 120 ? -11.197 1.407   33.383  1.00 13.01 ? 120 LEU B CD1 1 
ATOM   3131 C  CD2 . LEU B 1 120 ? -9.314  2.976   33.910  1.00 12.44 ? 120 LEU B CD2 1 
ATOM   3132 N  N   . VAL B 1 121 ? -12.520 5.454   37.504  1.00 7.09  ? 121 VAL B N   1 
ATOM   3133 C  CA  . VAL B 1 121 ? -13.424 6.491   38.087  1.00 8.04  ? 121 VAL B CA  1 
ATOM   3134 C  C   . VAL B 1 121 ? -13.164 7.825   37.399  1.00 7.36  ? 121 VAL B C   1 
ATOM   3135 O  O   . VAL B 1 121 ? -12.012 8.270   37.292  1.00 8.26  ? 121 VAL B O   1 
ATOM   3136 C  CB  . VAL B 1 121 ? -13.111 6.637   39.582  1.00 8.42  ? 121 VAL B CB  1 
ATOM   3137 C  CG1 . VAL B 1 121 ? -14.032 7.687   40.260  1.00 8.97  ? 121 VAL B CG1 1 
ATOM   3138 C  CG2 . VAL B 1 121 ? -13.116 5.254   40.322  1.00 8.65  ? 121 VAL B CG2 1 
ATOM   3139 N  N   . HIS B 1 122 ? -14.254 8.430   36.939  1.00 7.20  ? 122 HIS B N   1 
ATOM   3140 C  CA  . HIS B 1 122 ? -14.192 9.711   36.195  1.00 7.79  ? 122 HIS B CA  1 
ATOM   3141 C  C   . HIS B 1 122 ? -15.180 10.682  36.812  1.00 8.25  ? 122 HIS B C   1 
ATOM   3142 O  O   . HIS B 1 122 ? -16.274 10.300  37.234  1.00 8.40  ? 122 HIS B O   1 
ATOM   3143 C  CB  . HIS B 1 122 ? -14.603 9.527   34.737  1.00 8.56  ? 122 HIS B CB  1 
ATOM   3144 C  CG  . HIS B 1 122 ? -13.953 8.380   34.014  1.00 8.83  ? 122 HIS B CG  1 
ATOM   3145 N  ND1 . HIS B 1 122 ? -14.280 7.065   34.276  1.00 8.69  ? 122 HIS B ND1 1 
ATOM   3146 C  CD2 . HIS B 1 122 ? -12.976 8.341   33.023  1.00 9.42  ? 122 HIS B CD2 1 
ATOM   3147 C  CE1 . HIS B 1 122 ? -13.561 6.243   33.474  1.00 9.52  ? 122 HIS B CE1 1 
ATOM   3148 N  NE2 . HIS B 1 122 ? -12.745 7.019   32.715  1.00 9.39  ? 122 HIS B NE2 1 
ATOM   3149 N  N   . TRP B 1 123 ? -14.851 11.963  36.848  1.00 7.73  ? 123 TRP B N   1 
ATOM   3150 C  CA  . TRP B 1 123 ? -15.772 12.988  37.385  1.00 8.08  ? 123 TRP B CA  1 
ATOM   3151 C  C   . TRP B 1 123 ? -16.205 13.958  36.335  1.00 7.41  ? 123 TRP B C   1 
ATOM   3152 O  O   . TRP B 1 123 ? -15.455 14.315  35.384  1.00 8.74  ? 123 TRP B O   1 
ATOM   3153 C  CB  . TRP B 1 123 ? -15.111 13.774  38.581  1.00 10.00 ? 123 TRP B CB  1 
ATOM   3154 C  CG  . TRP B 1 123 ? -13.782 14.399  38.292  1.00 10.59 ? 123 TRP B CG  1 
ATOM   3155 C  CD1 . TRP B 1 123 ? -12.520 13.813  38.416  1.00 10.96 ? 123 TRP B CD1 1 
ATOM   3156 C  CD2 . TRP B 1 123 ? -13.530 15.769  37.858  1.00 10.45 ? 123 TRP B CD2 1 
ATOM   3157 N  NE1 . TRP B 1 123 ? -11.538 14.706  38.081  1.00 11.15 ? 123 TRP B NE1 1 
ATOM   3158 C  CE2 . TRP B 1 123 ? -12.079 15.895  37.730  1.00 11.78 ? 123 TRP B CE2 1 
ATOM   3159 C  CE3 . TRP B 1 123 ? -14.331 16.858  37.552  1.00 10.69 ? 123 TRP B CE3 1 
ATOM   3160 C  CZ2 . TRP B 1 123 ? -11.483 17.077  37.327  1.00 11.59 ? 123 TRP B CZ2 1 
ATOM   3161 C  CZ3 . TRP B 1 123 ? -13.714 18.042  37.147  1.00 11.88 ? 123 TRP B CZ3 1 
ATOM   3162 C  CH2 . TRP B 1 123 ? -12.328 18.140  37.033  1.00 11.55 ? 123 TRP B CH2 1 
ATOM   3163 N  N   . ASN B 1 124 ? -17.440 14.368  36.484  1.00 8.79  ? 124 ASN B N   1 
ATOM   3164 C  CA  . ASN B 1 124 ? -18.088 15.276  35.512  1.00 9.46  ? 124 ASN B CA  1 
ATOM   3165 C  C   . ASN B 1 124 ? -17.491 16.684  35.551  1.00 9.02  ? 124 ASN B C   1 
ATOM   3166 O  O   . ASN B 1 124 ? -17.552 17.337  36.574  1.00 9.12  ? 124 ASN B O   1 
ATOM   3167 C  CB  . ASN B 1 124 ? -19.584 15.308  35.864  1.00 10.41 ? 124 ASN B CB  1 
ATOM   3168 C  CG  . ASN B 1 124 ? -20.417 15.927  34.793  1.00 10.48 ? 124 ASN B CG  1 
ATOM   3169 O  OD1 . ASN B 1 124 ? -19.952 16.842  34.066  1.00 11.85 ? 124 ASN B OD1 1 
ATOM   3170 N  ND2 . ASN B 1 124 ? -21.676 15.465  34.692  1.00 11.87 ? 124 ASN B ND2 1 
ATOM   3171 N  N   . THR B 1 125 ? -16.902 17.103  34.428  1.00 10.02 ? 125 THR B N   1 
ATOM   3172 C  CA  . THR B 1 125 ? -16.160 18.386  34.408  1.00 10.67 ? 125 THR B CA  1 
ATOM   3173 C  C   . THR B 1 125 ? -17.075 19.547  34.602  1.00 12.19 ? 125 THR B C   1 
ATOM   3174 O  O   . THR B 1 125 ? -16.550 20.590  35.037  1.00 13.84 ? 125 THR B O   1 
ATOM   3175 C  CB  . THR B 1 125 ? -15.361 18.496  33.078  1.00 14.77 ? 125 THR B CB  1 
ATOM   3176 O  OG1 . THR B 1 125 ? -16.288 18.508  32.011  1.00 17.77 ? 125 THR B OG1 1 
ATOM   3177 C  CG2 . THR B 1 125 ? -14.357 17.365  32.945  1.00 16.32 ? 125 THR B CG2 1 
ATOM   3178 N  N   . LYS B 1 126 ? -18.402 19.428  34.537  1.00 11.22 ? 127 LYS B N   1 
ATOM   3179 C  CA  . LYS B 1 126 ? -19.248 20.575  34.853  1.00 13.19 ? 127 LYS B CA  1 
ATOM   3180 C  C   . LYS B 1 126 ? -19.236 20.926  36.325  1.00 11.19 ? 127 LYS B C   1 
ATOM   3181 O  O   . LYS B 1 126 ? -19.731 22.004  36.687  1.00 14.46 ? 127 LYS B O   1 
ATOM   3182 C  CB  . LYS B 1 126 ? -20.683 20.326  34.320  1.00 16.37 ? 127 LYS B CB  1 
ATOM   3183 C  CG  . LYS B 1 126 ? -21.546 19.434  35.196  1.00 14.98 ? 127 LYS B CG  1 
ATOM   3184 C  CD  . LYS B 1 126 ? -22.894 19.005  34.510  1.00 19.24 ? 127 LYS B CD  1 
ATOM   3185 C  CE  . LYS B 1 126 ? -23.966 20.070  34.771  1.00 23.99 ? 127 LYS B CE  1 
ATOM   3186 N  NZ  . LYS B 1 126 ? -25.286 19.663  34.121  1.00 27.32 ? 127 LYS B NZ  1 
ATOM   3187 N  N   . TYR B 1 127 ? -18.660 20.052  37.172  1.00 10.80 ? 128 TYR B N   1 
ATOM   3188 C  CA  . TYR B 1 127 ? -18.647 20.372  38.597  1.00 10.08 ? 128 TYR B CA  1 
ATOM   3189 C  C   . TYR B 1 127 ? -17.245 20.758  39.095  1.00 10.19 ? 128 TYR B C   1 
ATOM   3190 O  O   . TYR B 1 127 ? -17.089 20.981  40.311  1.00 11.46 ? 128 TYR B O   1 
ATOM   3191 C  CB  . TYR B 1 127 ? -19.184 19.190  39.436  1.00 11.54 ? 128 TYR B CB  1 
ATOM   3192 C  CG  . TYR B 1 127 ? -20.602 18.867  39.094  1.00 9.91  ? 128 TYR B CG  1 
ATOM   3193 C  CD1 . TYR B 1 127 ? -21.584 19.856  39.144  1.00 11.51 ? 128 TYR B CD1 1 
ATOM   3194 C  CD2 . TYR B 1 127 ? -20.957 17.602  38.640  1.00 10.34 ? 128 TYR B CD2 1 
ATOM   3195 C  CE1 . TYR B 1 127 ? -22.895 19.563  38.820  1.00 12.69 ? 128 TYR B CE1 1 
ATOM   3196 C  CE2 . TYR B 1 127 ? -22.247 17.296  38.287  1.00 11.30 ? 128 TYR B CE2 1 
ATOM   3197 C  CZ  . TYR B 1 127 ? -23.233 18.346  38.368  1.00 11.76 ? 128 TYR B CZ  1 
ATOM   3198 O  OH  . TYR B 1 127 ? -24.533 18.084  38.003  1.00 13.59 ? 128 TYR B OH  1 
ATOM   3199 N  N   . GLY B 1 128 ? -16.290 20.859  38.156  1.00 10.45 ? 129 GLY B N   1 
ATOM   3200 C  CA  . GLY B 1 128 ? -15.026 21.559  38.539  1.00 10.96 ? 129 GLY B CA  1 
ATOM   3201 C  C   . GLY B 1 128 ? -13.976 20.680  39.225  1.00 10.59 ? 129 GLY B C   1 
ATOM   3202 O  O   . GLY B 1 128 ? -12.766 20.845  38.949  1.00 12.76 ? 129 GLY B O   1 
ATOM   3203 N  N   . ASP B 1 129 ? -14.383 19.818  40.174  1.00 11.30 ? 130 ASP B N   1 
ATOM   3204 C  CA  . ASP B 1 129 ? -13.412 18.893  40.763  1.00 12.46 ? 130 ASP B CA  1 
ATOM   3205 C  C   . ASP B 1 129 ? -14.198 17.720  41.312  1.00 13.04 ? 130 ASP B C   1 
ATOM   3206 O  O   . ASP B 1 129 ? -15.431 17.750  41.334  1.00 12.88 ? 130 ASP B O   1 
ATOM   3207 C  CB  . ASP B 1 129 ? -12.451 19.529  41.729  1.00 17.11 ? 130 ASP B CB  1 
ATOM   3208 C  CG  . ASP B 1 129 ? -13.092 20.005  42.990  1.00 16.10 ? 130 ASP B CG  1 
ATOM   3209 O  OD1 . ASP B 1 129 ? -14.279 19.732  43.232  1.00 20.28 ? 130 ASP B OD1 1 
ATOM   3210 O  OD2 . ASP B 1 129 ? -12.365 20.663  43.751  1.00 20.95 ? 130 ASP B OD2 1 
ATOM   3211 N  N   . PHE B 1 130 ? -13.481 16.662  41.688  1.00 11.40 ? 131 PHE B N   1 
ATOM   3212 C  CA  . PHE B 1 130 ? -14.162 15.461  42.094  1.00 13.20 ? 131 PHE B CA  1 
ATOM   3213 C  C   . PHE B 1 130 ? -14.877 15.634  43.419  1.00 11.34 ? 131 PHE B C   1 
ATOM   3214 O  O   . PHE B 1 130 ? -15.942 15.031  43.631  1.00 11.34 ? 131 PHE B O   1 
ATOM   3215 C  CB  . PHE B 1 130 ? -13.269 14.240  42.171  1.00 14.62 ? 131 PHE B CB  1 
ATOM   3216 C  CG  . PHE B 1 130 ? -12.334 14.225  43.332  1.00 18.12 ? 131 PHE B CG  1 
ATOM   3217 C  CD1 . PHE B 1 130 ? -11.040 14.827  43.285  1.00 20.30 ? 131 PHE B CD1 1 
ATOM   3218 C  CD2 . PHE B 1 130 ? -12.726 13.620  44.545  1.00 19.87 ? 131 PHE B CD2 1 
ATOM   3219 C  CE1 . PHE B 1 130 ? -10.150 14.771  44.380  1.00 23.34 ? 131 PHE B CE1 1 
ATOM   3220 C  CE2 . PHE B 1 130 ? -11.818 13.597  45.668  1.00 26.31 ? 131 PHE B CE2 1 
ATOM   3221 C  CZ  . PHE B 1 130 ? -10.541 14.177  45.564  1.00 31.18 ? 131 PHE B CZ  1 
ATOM   3222 N  N   . GLY B 1 131 ? -14.366 16.469  44.349  1.00 12.55 ? 132 GLY B N   1 
ATOM   3223 C  CA  . GLY B 1 131 ? -15.006 16.590  45.672  1.00 13.26 ? 132 GLY B CA  1 
ATOM   3224 C  C   . GLY B 1 131 ? -16.405 17.209  45.538  1.00 13.55 ? 132 GLY B C   1 
ATOM   3225 O  O   . GLY B 1 131 ? -17.328 16.908  46.280  1.00 15.28 ? 132 GLY B O   1 
ATOM   3226 N  N   . LYS B 1 132 ? -16.536 18.143  44.592  1.00 12.78 ? 133 LYS B N   1 
ATOM   3227 C  CA  . LYS B 1 132 ? -17.870 18.687  44.303  1.00 12.34 ? 133 LYS B CA  1 
ATOM   3228 C  C   . LYS B 1 132 ? -18.724 17.754  43.492  1.00 11.35 ? 133 LYS B C   1 
ATOM   3229 O  O   . LYS B 1 132 ? -19.953 17.649  43.719  1.00 12.21 ? 133 LYS B O   1 
ATOM   3230 C  CB  . LYS B 1 132 ? -17.764 20.078  43.622  1.00 13.70 ? 133 LYS B CB  1 
ATOM   3231 C  CG  . LYS B 1 132 ? -17.091 21.189  44.458  1.00 18.47 ? 133 LYS B CG  1 
ATOM   3232 C  CD  . LYS B 1 132 ? -17.496 21.364  45.924  1.00 30.31 ? 133 LYS B CD  1 
ATOM   3233 C  CE  . LYS B 1 132 ? -18.130 22.770  46.028  1.00 22.38 ? 133 LYS B CE  1 
ATOM   3234 N  NZ  . LYS B 1 132 ? -19.301 22.695  45.058  1.00 34.65 ? 133 LYS B NZ  1 
ATOM   3235 N  N   . ALA B 1 133 ? -18.108 17.016  42.563  1.00 10.93 ? 134 ALA B N   1 
ATOM   3236 C  CA  . ALA B 1 133 ? -18.864 16.083  41.751  1.00 10.36 ? 134 ALA B CA  1 
ATOM   3237 C  C   . ALA B 1 133 ? -19.535 14.991  42.557  1.00 9.41  ? 134 ALA B C   1 
ATOM   3238 O  O   . ALA B 1 133 ? -20.692 14.638  42.220  1.00 10.44 ? 134 ALA B O   1 
ATOM   3239 C  CB  . ALA B 1 133 ? -17.936 15.474  40.735  1.00 10.67 ? 134 ALA B CB  1 
ATOM   3240 N  N   . VAL B 1 134 ? -18.927 14.519  43.645  1.00 10.62 ? 135 VAL B N   1 
ATOM   3241 C  CA  . VAL B 1 134 ? -19.577 13.400  44.367  1.00 10.72 ? 135 VAL B CA  1 
ATOM   3242 C  C   . VAL B 1 134 ? -20.794 13.821  45.109  1.00 10.89 ? 135 VAL B C   1 
ATOM   3243 O  O   . VAL B 1 134 ? -21.508 12.975  45.599  1.00 11.95 ? 135 VAL B O   1 
ATOM   3244 C  CB  . VAL B 1 134 ? -18.624 12.715  45.371  1.00 10.57 ? 135 VAL B CB  1 
ATOM   3245 C  CG1 . VAL B 1 134 ? -17.452 12.056  44.625  1.00 14.02 ? 135 VAL B CG1 1 
ATOM   3246 C  CG2 . VAL B 1 134 ? -18.089 13.614  46.465  1.00 13.39 ? 135 VAL B CG2 1 
ATOM   3247 N  N   . GLN B 1 135 ? -21.027 15.149  45.180  1.00 11.11 ? 136 GLN B N   1 
ATOM   3248 C  CA  . GLN B 1 135 ? -22.238 15.685  45.830  1.00 12.88 ? 136 GLN B CA  1 
ATOM   3249 C  C   . GLN B 1 135 ? -23.455 15.754  44.893  1.00 13.11 ? 136 GLN B C   1 
ATOM   3250 O  O   . GLN B 1 135 ? -24.507 16.353  45.223  1.00 15.12 ? 136 GLN B O   1 
ATOM   3251 C  CB  . GLN B 1 135 ? -21.918 17.064  46.491  1.00 13.75 ? 136 GLN B CB  1 
ATOM   3252 C  CG  . GLN B 1 135 ? -20.866 16.922  47.581  1.00 17.07 ? 136 GLN B CG  1 
ATOM   3253 C  CD  . GLN B 1 135 ? -20.532 18.300  48.172  1.00 23.44 ? 136 GLN B CD  1 
ATOM   3254 O  OE1 . GLN B 1 135 ? -21.435 18.996  48.713  1.00 35.83 ? 136 GLN B OE1 1 
ATOM   3255 N  NE2 . GLN B 1 135 ? -19.263 18.726  48.037  1.00 28.20 ? 136 GLN B NE2 1 
ATOM   3256 N  N   . GLN B 1 136 ? -23.264 15.287  43.637  1.00 11.74 ? 137 GLN B N   1 
ATOM   3257 C  CA  . GLN B 1 136 ? -24.241 15.494  42.590  1.00 11.24 ? 137 GLN B CA  1 
ATOM   3258 C  C   . GLN B 1 136 ? -24.707 14.160  42.083  1.00 13.19 ? 137 GLN B C   1 
ATOM   3259 O  O   . GLN B 1 136 ? -23.917 13.210  41.964  1.00 11.66 ? 137 GLN B O   1 
ATOM   3260 C  CB  . GLN B 1 136 ? -23.672 16.275  41.382  1.00 11.73 ? 137 GLN B CB  1 
ATOM   3261 C  CG  . GLN B 1 136 ? -22.895 17.485  41.769  1.00 15.37 ? 137 GLN B CG  1 
ATOM   3262 C  CD  . GLN B 1 136 ? -23.683 18.468  42.569  1.00 18.59 ? 137 GLN B CD  1 
ATOM   3263 O  OE1 . GLN B 1 136 ? -24.924 18.626  42.420  1.00 17.10 ? 137 GLN B OE1 1 
ATOM   3264 N  NE2 . GLN B 1 136 ? -22.949 19.202  43.456  1.00 29.70 ? 137 GLN B NE2 1 
ATOM   3265 N  N   . PRO B 1 137 ? -25.962 14.052  41.597  1.00 10.94 ? 138 PRO B N   1 
ATOM   3266 C  CA  . PRO B 1 137 ? -26.453 12.743  41.175  1.00 11.60 ? 138 PRO B CA  1 
ATOM   3267 C  C   . PRO B 1 137 ? -25.840 12.244  39.909  1.00 11.21 ? 138 PRO B C   1 
ATOM   3268 O  O   . PRO B 1 137 ? -25.876 11.046  39.635  1.00 13.94 ? 138 PRO B O   1 
ATOM   3269 C  CB  . PRO B 1 137 ? -27.981 12.957  40.968  1.00 15.93 ? 138 PRO B CB  1 
ATOM   3270 C  CG  . PRO B 1 137 ? -28.254 14.364  41.378  1.00 20.68 ? 138 PRO B CG  1 
ATOM   3271 C  CD  . PRO B 1 137 ? -27.010 15.087  41.744  1.00 14.08 ? 138 PRO B CD  1 
ATOM   3272 N  N   . ASP B 1 138 ? -25.262 13.136  39.118  1.00 10.77 ? 139 ASP B N   1 
ATOM   3273 C  CA  . ASP B 1 138 ? -24.578 12.751  37.867  1.00 11.72 ? 139 ASP B CA  1 
ATOM   3274 C  C   . ASP B 1 138 ? -23.069 13.178  37.985  1.00 10.42 ? 139 ASP B C   1 
ATOM   3275 O  O   . ASP B 1 138 ? -22.491 13.578  37.006  1.00 10.61 ? 139 ASP B O   1 
ATOM   3276 C  CB  . ASP B 1 138 ? -25.264 13.420  36.649  1.00 12.35 ? 139 ASP B CB  1 
ATOM   3277 C  CG  . ASP B 1 138 ? -25.279 14.909  36.724  1.00 13.92 ? 139 ASP B CG  1 
ATOM   3278 O  OD1 . ASP B 1 138 ? -25.048 15.535  37.783  1.00 13.43 ? 139 ASP B OD1 1 
ATOM   3279 O  OD2 . ASP B 1 138 ? -25.693 15.478  35.670  1.00 17.26 ? 139 ASP B OD2 1 
ATOM   3280 N  N   . GLY B 1 139 ? -22.525 13.110  39.196  1.00 10.21 ? 140 GLY B N   1 
ATOM   3281 C  CA  . GLY B 1 139 ? -21.149 13.587  39.415  1.00 9.95  ? 140 GLY B CA  1 
ATOM   3282 C  C   . GLY B 1 139 ? -20.061 12.697  38.845  1.00 7.92  ? 140 GLY B C   1 
ATOM   3283 O  O   . GLY B 1 139 ? -19.017 13.186  38.454  1.00 8.89  ? 140 GLY B O   1 
ATOM   3284 N  N   . LEU B 1 140 ? -20.264 11.362  38.866  1.00 8.09  ? 141 LEU B N   1 
ATOM   3285 C  CA  . LEU B 1 140 ? -19.212 10.415  38.478  1.00 7.91  ? 141 LEU B CA  1 
ATOM   3286 C  C   . LEU B 1 140 ? -19.727 9.455   37.436  1.00 7.55  ? 141 LEU B C   1 
ATOM   3287 O  O   . LEU B 1 140 ? -20.927 9.188   37.342  1.00 8.31  ? 141 LEU B O   1 
ATOM   3288 C  CB  . LEU B 1 140 ? -18.779 9.560   39.673  1.00 8.97  ? 141 LEU B CB  1 
ATOM   3289 C  CG  . LEU B 1 140 ? -18.136 10.288  40.870  1.00 9.76  ? 141 LEU B CG  1 
ATOM   3290 C  CD1 . LEU B 1 140 ? -17.665 9.204   41.852  1.00 10.25 ? 141 LEU B CD1 1 
ATOM   3291 C  CD2 . LEU B 1 140 ? -17.038 11.263  40.562  1.00 11.13 ? 141 LEU B CD2 1 
ATOM   3292 N  N   . ALA B 1 141 ? -18.766 8.963   36.631  1.00 7.58  ? 142 ALA B N   1 
ATOM   3293 C  CA  . ALA B 1 141 ? -19.030 7.836   35.733  1.00 8.39  ? 142 ALA B CA  1 
ATOM   3294 C  C   . ALA B 1 141 ? -17.941 6.845   36.018  1.00 7.16  ? 142 ALA B C   1 
ATOM   3295 O  O   . ALA B 1 141 ? -16.737 7.187   36.009  1.00 8.06  ? 142 ALA B O   1 
ATOM   3296 C  CB  . ALA B 1 141 ? -18.900 8.278   34.277  1.00 8.99  ? 142 ALA B CB  1 
ATOM   3297 N  N   . VAL B 1 142 ? -18.348 5.604   36.426  1.00 7.93  ? 143 VAL B N   1 
ATOM   3298 C  CA  . VAL B 1 142 ? -17.363 4.581   36.726  1.00 8.14  ? 143 VAL B CA  1 
ATOM   3299 C  C   . VAL B 1 142 ? -17.497 3.489   35.669  1.00 7.94  ? 143 VAL B C   1 
ATOM   3300 O  O   . VAL B 1 142 ? -18.595 3.007   35.440  1.00 7.81  ? 143 VAL B O   1 
ATOM   3301 C  CB  . VAL B 1 142 ? -17.485 4.008   38.159  1.00 7.33  ? 143 VAL B CB  1 
ATOM   3302 C  CG1 . VAL B 1 142 ? -16.313 2.995   38.352  1.00 7.94  ? 143 VAL B CG1 1 
ATOM   3303 C  CG2 . VAL B 1 142 ? -17.317 5.140   39.160  1.00 8.68  ? 143 VAL B CG2 1 
ATOM   3304 N  N   . LEU B 1 143 ? -16.401 3.268   34.955  1.00 7.17  ? 144 LEU B N   1 
ATOM   3305 C  CA  . LEU B 1 143 ? -16.300 2.212   33.947  1.00 7.80  ? 144 LEU B CA  1 
ATOM   3306 C  C   . LEU B 1 143 ? -15.834 0.924   34.666  1.00 7.08  ? 144 LEU B C   1 
ATOM   3307 O  O   . LEU B 1 143 ? -14.741 0.900   35.209  1.00 8.25  ? 144 LEU B O   1 
ATOM   3308 C  CB  . LEU B 1 143 ? -15.341 2.636   32.851  1.00 9.44  ? 144 LEU B CB  1 
ATOM   3309 C  CG  . LEU B 1 143 ? -15.093 1.647   31.682  1.00 10.39 ? 144 LEU B CG  1 
ATOM   3310 C  CD1 . LEU B 1 143 ? -16.422 1.416   30.944  1.00 12.04 ? 144 LEU B CD1 1 
ATOM   3311 C  CD2 . LEU B 1 143 ? -14.074 2.319   30.704  1.00 10.95 ? 144 LEU B CD2 1 
ATOM   3312 N  N   . GLY B 1 144 ? -16.680 -0.099  34.633  1.00 7.40  ? 145 GLY B N   1 
ATOM   3313 C  CA  . GLY B 1 144 ? -16.353 -1.376  35.300  1.00 7.31  ? 145 GLY B CA  1 
ATOM   3314 C  C   . GLY B 1 144 ? -16.022 -2.464  34.282  1.00 7.08  ? 145 GLY B C   1 
ATOM   3315 O  O   . GLY B 1 144 ? -16.698 -2.582  33.294  1.00 8.44  ? 145 GLY B O   1 
ATOM   3316 N  N   . ILE B 1 145 ? -14.958 -3.195  34.605  1.00 7.02  ? 146 ILE B N   1 
ATOM   3317 C  CA  . ILE B 1 145 ? -14.463 -4.236  33.677  1.00 8.01  ? 146 ILE B CA  1 
ATOM   3318 C  C   . ILE B 1 145 ? -14.220 -5.467  34.523  1.00 7.28  ? 146 ILE B C   1 
ATOM   3319 O  O   . ILE B 1 145 ? -13.490 -5.439  35.501  1.00 8.19  ? 146 ILE B O   1 
ATOM   3320 C  CB  . ILE B 1 145 ? -13.184 -3.783  32.926  1.00 8.11  ? 146 ILE B CB  1 
ATOM   3321 C  CG1 . ILE B 1 145 ? -13.473 -2.454  32.153  1.00 10.61 ? 146 ILE B CG1 1 
ATOM   3322 C  CG2 . ILE B 1 145 ? -12.611 -4.916  32.051  1.00 10.25 ? 146 ILE B CG2 1 
ATOM   3323 C  CD1 . ILE B 1 145 ? -12.227 -1.885  31.498  1.00 11.85 ? 146 ILE B CD1 1 
ATOM   3324 N  N   . PHE B 1 146 ? -14.824 -6.598  34.115  1.00 7.29  ? 147 PHE B N   1 
ATOM   3325 C  CA  . PHE B 1 146 ? -14.626 -7.854  34.830  1.00 7.64  ? 147 PHE B CA  1 
ATOM   3326 C  C   . PHE B 1 146 ? -13.278 -8.466  34.477  1.00 7.70  ? 147 PHE B C   1 
ATOM   3327 O  O   . PHE B 1 146 ? -12.815 -8.341  33.333  1.00 8.95  ? 147 PHE B O   1 
ATOM   3328 C  CB  . PHE B 1 146 ? -15.722 -8.822  34.490  1.00 7.84  ? 147 PHE B CB  1 
ATOM   3329 C  CG  . PHE B 1 146 ? -17.086 -8.381  34.949  1.00 7.05  ? 147 PHE B CG  1 
ATOM   3330 C  CD1 . PHE B 1 146 ? -17.360 -8.207  36.297  1.00 7.71  ? 147 PHE B CD1 1 
ATOM   3331 C  CD2 . PHE B 1 146 ? -18.096 -8.139  34.032  1.00 7.71  ? 147 PHE B CD2 1 
ATOM   3332 C  CE1 . PHE B 1 146 ? -18.612 -7.799  36.720  1.00 7.83  ? 147 PHE B CE1 1 
ATOM   3333 C  CE2 . PHE B 1 146 ? -19.351 -7.732  34.447  1.00 8.48  ? 147 PHE B CE2 1 
ATOM   3334 C  CZ  . PHE B 1 146 ? -19.610 -7.562  35.794  1.00 7.81  ? 147 PHE B CZ  1 
ATOM   3335 N  N   . LEU B 1 147 ? -12.687 -9.135  35.447  1.00 7.88  ? 148 LEU B N   1 
ATOM   3336 C  CA  . LEU B 1 147 ? -11.484 -9.964  35.241  1.00 8.02  ? 148 LEU B CA  1 
ATOM   3337 C  C   . LEU B 1 147 ? -11.796 -11.431 35.511  1.00 8.09  ? 148 LEU B C   1 
ATOM   3338 O  O   . LEU B 1 147 ? -12.384 -11.794 36.574  1.00 8.77  ? 148 LEU B O   1 
ATOM   3339 C  CB  . LEU B 1 147 ? -10.345 -9.608  36.235  1.00 8.70  ? 148 LEU B CB  1 
ATOM   3340 C  CG  . LEU B 1 147 ? -9.539  -8.288  35.900  1.00 9.01  ? 148 LEU B CG  1 
ATOM   3341 C  CD1 . LEU B 1 147 ? -10.373 -7.006  35.795  1.00 10.19 ? 148 LEU B CD1 1 
ATOM   3342 C  CD2 . LEU B 1 147 ? -8.416  -8.074  36.937  1.00 9.67  ? 148 LEU B CD2 1 
ATOM   3343 N  N   . LYS B 1 148 ? -11.391 -12.280 34.542  1.00 8.45  ? 149 LYS B N   1 
ATOM   3344 C  CA  . LYS B 1 148 ? -11.453 -13.757 34.722  1.00 9.65  ? 149 LYS B CA  1 
ATOM   3345 C  C   . LYS B 1 148 ? -10.003 -14.260 34.708  1.00 10.33 ? 149 LYS B C   1 
ATOM   3346 O  O   . LYS B 1 148 ? -9.095  -13.622 34.174  1.00 10.95 ? 149 LYS B O   1 
ATOM   3347 C  CB  . LYS B 1 148 ? -12.294 -14.430 33.652  1.00 10.89 ? 149 LYS B CB  1 
ATOM   3348 C  CG  . LYS B 1 148 ? -11.703 -14.307 32.251  1.00 12.61 ? 149 LYS B CG  1 
ATOM   3349 C  CD  . LYS B 1 148 ? -12.597 -15.042 31.266  1.00 17.27 ? 149 LYS B CD  1 
ATOM   3350 C  CE  . LYS B 1 148 ? -11.901 -15.325 29.980  1.00 23.67 ? 149 LYS B CE  1 
ATOM   3351 N  NZ  . LYS B 1 148 ? -12.903 -16.078 29.165  1.00 37.27 ? 149 LYS B NZ  1 
ATOM   3352 N  N   . VAL B 1 149 ? -9.753  -15.410 35.333  1.00 10.51 ? 150 VAL B N   1 
ATOM   3353 C  CA  . VAL B 1 149 ? -8.403  -15.964 35.340  1.00 10.54 ? 150 VAL B CA  1 
ATOM   3354 C  C   . VAL B 1 149 ? -8.205  -16.901 34.127  1.00 11.75 ? 150 VAL B C   1 
ATOM   3355 O  O   . VAL B 1 149 ? -8.950  -17.859 33.895  1.00 12.20 ? 150 VAL B O   1 
ATOM   3356 C  CB  . VAL B 1 149 ? -8.213  -16.768 36.661  1.00 10.88 ? 150 VAL B CB  1 
ATOM   3357 C  CG1 . VAL B 1 149 ? -6.912  -17.564 36.656  1.00 12.49 ? 150 VAL B CG1 1 
ATOM   3358 C  CG2 . VAL B 1 149 ? -8.213  -15.759 37.818  1.00 14.48 ? 150 VAL B CG2 1 
ATOM   3359 N  N   . GLY B 1 150 ? -7.168  -16.623 33.374  1.00 10.65 ? 151 GLY B N   1 
ATOM   3360 C  CA  . GLY B 1 150 ? -6.841  -17.471 32.227  1.00 11.70 ? 151 GLY B CA  1 
ATOM   3361 C  C   . GLY B 1 150 ? -5.491  -16.989 31.729  1.00 11.57 ? 151 GLY B C   1 
ATOM   3362 O  O   . GLY B 1 150 ? -4.507  -17.066 32.454  1.00 12.39 ? 151 GLY B O   1 
ATOM   3363 N  N   A SER B 1 151 ? -5.417  -16.510 30.475  0.50 12.78 ? 152 SER B N   1 
ATOM   3364 N  N   B SER B 1 151 ? -5.447  -16.479 30.489  0.50 12.86 ? 152 SER B N   1 
ATOM   3365 C  CA  A SER B 1 151 ? -4.163  -15.931 29.906  0.50 12.74 ? 152 SER B CA  1 
ATOM   3366 C  CA  B SER B 1 151 ? -4.224  -15.843 29.939  0.50 11.73 ? 152 SER B CA  1 
ATOM   3367 C  C   A SER B 1 151 ? -3.819  -14.612 30.628  0.50 12.34 ? 152 SER B C   1 
ATOM   3368 C  C   B SER B 1 151 ? -3.803  -14.622 30.773  0.50 12.20 ? 152 SER B C   1 
ATOM   3369 O  O   A SER B 1 151 ? -4.755  -13.878 31.044  0.50 10.84 ? 152 SER B O   1 
ATOM   3370 O  O   B SER B 1 151 ? -4.642  -13.956 31.400  0.50 10.84 ? 152 SER B O   1 
ATOM   3371 C  CB  A SER B 1 151 ? -4.327  -15.669 28.406  0.50 16.97 ? 152 SER B CB  1 
ATOM   3372 C  CB  B SER B 1 151 ? -4.422  -15.449 28.473  0.50 14.51 ? 152 SER B CB  1 
ATOM   3373 O  OG  A SER B 1 151 ? -5.337  -14.693 28.194  0.50 17.81 ? 152 SER B OG  1 
ATOM   3374 O  OG  B SER B 1 151 ? -4.836  -16.582 27.765  0.50 17.64 ? 152 SER B OG  1 
ATOM   3375 N  N   . ALA B 1 152 ? -2.506  -14.320 30.771  1.00 11.90 ? 153 ALA B N   1 
ATOM   3376 C  CA  . ALA B 1 152 ? -2.034  -13.092 31.391  1.00 11.04 ? 153 ALA B CA  1 
ATOM   3377 C  C   . ALA B 1 152 ? -2.504  -11.864 30.571  1.00 10.35 ? 153 ALA B C   1 
ATOM   3378 O  O   . ALA B 1 152 ? -2.657  -11.941 29.343  1.00 13.00 ? 153 ALA B O   1 
ATOM   3379 C  CB  . ALA B 1 152 ? -0.537  -13.063 31.488  1.00 13.49 ? 153 ALA B CB  1 
ATOM   3380 N  N   . LYS B 1 153 ? -2.729  -10.726 31.257  1.00 10.71 ? 154 LYS B N   1 
ATOM   3381 C  CA  . LYS B 1 153 ? -2.956  -9.467  30.589  1.00 11.16 ? 154 LYS B CA  1 
ATOM   3382 C  C   . LYS B 1 153 ? -1.604  -8.698  30.616  1.00 12.22 ? 154 LYS B C   1 
ATOM   3383 O  O   . LYS B 1 153 ? -1.176  -8.244  31.674  1.00 10.51 ? 154 LYS B O   1 
ATOM   3384 C  CB  . LYS B 1 153 ? -4.050  -8.665  31.320  1.00 11.55 ? 154 LYS B CB  1 
ATOM   3385 C  CG  . LYS B 1 153 ? -4.608  -7.463  30.516  1.00 12.17 ? 154 LYS B CG  1 
ATOM   3386 C  CD  . LYS B 1 153 ? -5.390  -7.886  29.227  1.00 13.08 ? 154 LYS B CD  1 
ATOM   3387 C  CE  . LYS B 1 153 ? -6.122  -6.704  28.578  1.00 14.84 ? 154 LYS B CE  1 
ATOM   3388 N  NZ  . LYS B 1 153 ? -6.494  -7.043  27.187  1.00 19.55 ? 154 LYS B NZ  1 
ATOM   3389 N  N   . PRO B 1 154 ? -0.910  -8.623  29.445  1.00 12.04 ? 155 PRO B N   1 
ATOM   3390 C  CA  . PRO B 1 154 ? 0.463   -7.992  29.494  1.00 13.91 ? 155 PRO B CA  1 
ATOM   3391 C  C   . PRO B 1 154 ? 0.409   -6.575  30.047  1.00 11.46 ? 155 PRO B C   1 
ATOM   3392 O  O   . PRO B 1 154 ? 1.321   -6.198  30.752  1.00 15.08 ? 155 PRO B O   1 
ATOM   3393 C  CB  . PRO B 1 154 ? 0.930   -8.068  28.020  1.00 14.11 ? 155 PRO B CB  1 
ATOM   3394 C  CG  . PRO B 1 154 ? 0.095   -9.247  27.460  1.00 16.51 ? 155 PRO B CG  1 
ATOM   3395 C  CD  . PRO B 1 154 ? -1.257  -9.153  28.111  1.00 13.76 ? 155 PRO B CD  1 
ATOM   3396 N  N   . GLY B 1 155 ? -0.656  -5.805  29.700  1.00 10.93 ? 156 GLY B N   1 
ATOM   3397 C  CA  . GLY B 1 155 ? -0.792  -4.404  30.094  1.00 13.65 ? 156 GLY B CA  1 
ATOM   3398 C  C   . GLY B 1 155 ? -1.048  -4.224  31.579  1.00 12.19 ? 156 GLY B C   1 
ATOM   3399 O  O   . GLY B 1 155 ? -0.965  -3.122  32.088  1.00 16.77 ? 156 GLY B O   1 
ATOM   3400 N  N   . LEU B 1 156 ? -1.361  -5.301  32.319  1.00 11.05 ? 157 LEU B N   1 
ATOM   3401 C  CA  . LEU B 1 156 ? -1.464  -5.271  33.771  1.00 9.49  ? 157 LEU B CA  1 
ATOM   3402 C  C   . LEU B 1 156 ? -0.148  -5.443  34.481  1.00 10.29 ? 157 LEU B C   1 
ATOM   3403 O  O   . LEU B 1 156 ? -0.041  -5.215  35.703  1.00 9.46  ? 157 LEU B O   1 
ATOM   3404 C  CB  . LEU B 1 156 ? -2.523  -6.299  34.162  1.00 11.65 ? 157 LEU B CB  1 
ATOM   3405 C  CG  . LEU B 1 156 ? -2.861  -6.424  35.685  1.00 10.41 ? 157 LEU B CG  1 
ATOM   3406 C  CD1 . LEU B 1 156 ? -3.419  -5.114  36.312  1.00 12.68 ? 157 LEU B CD1 1 
ATOM   3407 C  CD2 . LEU B 1 156 ? -3.829  -7.583  35.967  1.00 11.30 ? 157 LEU B CD2 1 
ATOM   3408 N  N   . GLN B 1 157 ? 0.880   -6.013  33.821  1.00 10.24 ? 158 GLN B N   1 
ATOM   3409 C  CA  . GLN B 1 157 ? 2.060   -6.499  34.541  1.00 12.05 ? 158 GLN B CA  1 
ATOM   3410 C  C   . GLN B 1 157 ? 2.790   -5.400  35.272  1.00 11.93 ? 158 GLN B C   1 
ATOM   3411 O  O   . GLN B 1 157 ? 3.235   -5.622  36.368  1.00 11.85 ? 158 GLN B O   1 
ATOM   3412 C  CB  . GLN B 1 157 ? 3.021   -7.264  33.590  1.00 13.68 ? 158 GLN B CB  1 
ATOM   3413 C  CG  . GLN B 1 157 ? 4.097   -8.042  34.411  1.00 15.20 ? 158 GLN B CG  1 
ATOM   3414 C  CD  . GLN B 1 157 ? 3.482   -9.079  35.380  1.00 12.89 ? 158 GLN B CD  1 
ATOM   3415 O  OE1 . GLN B 1 157 ? 2.366   -9.638  35.114  1.00 14.00 ? 158 GLN B OE1 1 
ATOM   3416 N  NE2 . GLN B 1 157 ? 4.131   -9.314  36.469  1.00 14.25 ? 158 GLN B NE2 1 
ATOM   3417 N  N   . LYS B 1 158 ? 2.840   -4.182  34.703  1.00 13.05 ? 159 LYS B N   1 
ATOM   3418 C  CA  . LYS B 1 158 ? 3.519   -3.049  35.402  1.00 12.44 ? 159 LYS B CA  1 
ATOM   3419 C  C   . LYS B 1 158 ? 2.888   -2.760  36.754  1.00 12.22 ? 159 LYS B C   1 
ATOM   3420 O  O   . LYS B 1 158 ? 3.542   -2.410  37.707  1.00 13.00 ? 159 LYS B O   1 
ATOM   3421 C  CB  . LYS B 1 158 ? 3.603   -1.829  34.480  1.00 16.64 ? 159 LYS B CB  1 
ATOM   3422 C  CG  . LYS B 1 158 ? 4.728   -2.030  33.465  1.00 25.40 ? 159 LYS B CG  1 
ATOM   3423 C  CD  . LYS B 1 158 ? 5.022   -0.784  32.632  1.00 32.49 ? 159 LYS B CD  1 
ATOM   3424 C  CE  . LYS B 1 158 ? 5.956   -1.071  31.415  1.00 35.58 ? 159 LYS B CE  1 
ATOM   3425 N  NZ  . LYS B 1 158 ? 6.173   0.127   30.473  1.00 38.28 ? 159 LYS B NZ  1 
ATOM   3426 N  N   . VAL B 1 159 ? 1.558   -2.941  36.837  1.00 12.13 ? 160 VAL B N   1 
ATOM   3427 C  CA  . VAL B 1 159 ? 0.874   -2.722  38.066  1.00 9.63  ? 160 VAL B CA  1 
ATOM   3428 C  C   . VAL B 1 159 ? 1.223   -3.838  39.069  1.00 11.61 ? 160 VAL B C   1 
ATOM   3429 O  O   . VAL B 1 159 ? 1.573   -3.591  40.220  1.00 12.45 ? 160 VAL B O   1 
ATOM   3430 C  CB  . VAL B 1 159 ? -0.674  -2.750  37.857  1.00 11.03 ? 160 VAL B CB  1 
ATOM   3431 C  CG1 . VAL B 1 159 ? -1.395  -2.775  39.214  1.00 12.20 ? 160 VAL B CG1 1 
ATOM   3432 C  CG2 . VAL B 1 159 ? -1.126  -1.556  37.024  1.00 15.42 ? 160 VAL B CG2 1 
ATOM   3433 N  N   . VAL B 1 160 ? 1.148   -5.086  38.605  1.00 11.13 ? 161 VAL B N   1 
ATOM   3434 C  CA  . VAL B 1 160 ? 1.439   -6.211  39.449  1.00 13.71 ? 161 VAL B CA  1 
ATOM   3435 C  C   . VAL B 1 160 ? 2.861   -6.121  40.017  1.00 12.34 ? 161 VAL B C   1 
ATOM   3436 O  O   . VAL B 1 160 ? 3.060   -6.387  41.212  1.00 13.00 ? 161 VAL B O   1 
ATOM   3437 C  CB  . VAL B 1 160 ? 1.319   -7.585  38.585  1.00 14.55 ? 161 VAL B CB  1 
ATOM   3438 C  CG1 . VAL B 1 160 ? 1.996   -8.738  39.287  1.00 16.97 ? 161 VAL B CG1 1 
ATOM   3439 C  CG2 . VAL B 1 160 ? -0.167  -7.813  38.276  1.00 17.03 ? 161 VAL B CG2 1 
ATOM   3440 N  N   . ASP B 1 161 ? 3.828   -5.701  39.183  1.00 12.74 ? 162 ASP B N   1 
ATOM   3441 C  CA  . ASP B 1 161 ? 5.226   -5.745  39.679  1.00 15.20 ? 162 ASP B CA  1 
ATOM   3442 C  C   . ASP B 1 161 ? 5.497   -4.677  40.705  1.00 15.97 ? 162 ASP B C   1 
ATOM   3443 O  O   . ASP B 1 161 ? 6.480   -4.819  41.457  1.00 20.07 ? 162 ASP B O   1 
ATOM   3444 C  CB  . ASP B 1 161 ? 6.177   -5.676  38.562  1.00 18.57 ? 162 ASP B CB  1 
ATOM   3445 C  CG  . ASP B 1 161 ? 6.244   -6.992  37.847  1.00 17.72 ? 162 ASP B CG  1 
ATOM   3446 O  OD1 . ASP B 1 161 ? 6.081   -8.043  38.477  1.00 22.41 ? 162 ASP B OD1 1 
ATOM   3447 O  OD2 . ASP B 1 161 ? 6.451   -6.966  36.642  1.00 19.38 ? 162 ASP B OD2 1 
ATOM   3448 N  N   . VAL B 1 162 ? 4.698   -3.586  40.769  1.00 13.86 ? 163 VAL B N   1 
ATOM   3449 C  CA  . VAL B 1 162 ? 4.965   -2.546  41.771  1.00 13.97 ? 163 VAL B CA  1 
ATOM   3450 C  C   . VAL B 1 162 ? 4.340   -2.866  43.126  1.00 13.45 ? 163 VAL B C   1 
ATOM   3451 O  O   . VAL B 1 162 ? 4.586   -2.190  44.094  1.00 14.13 ? 163 VAL B O   1 
ATOM   3452 C  CB  . VAL B 1 162 ? 4.546   -1.126  41.253  1.00 15.34 ? 163 VAL B CB  1 
ATOM   3453 C  CG1 . VAL B 1 162 ? 3.049   -0.923  41.270  1.00 15.99 ? 163 VAL B CG1 1 
ATOM   3454 C  CG2 . VAL B 1 162 ? 5.270   0.007   41.898  1.00 15.24 ? 163 VAL B CG2 1 
ATOM   3455 N  N   . LEU B 1 163 ? 3.408   -3.858  43.176  1.00 12.07 ? 164 LEU B N   1 
ATOM   3456 C  CA  . LEU B 1 163 ? 2.672   -4.105  44.389  1.00 11.18 ? 164 LEU B CA  1 
ATOM   3457 C  C   . LEU B 1 163 ? 3.534   -4.467  45.589  1.00 13.83 ? 164 LEU B C   1 
ATOM   3458 O  O   . LEU B 1 163 ? 3.186   -4.159  46.717  1.00 14.21 ? 164 LEU B O   1 
ATOM   3459 C  CB  . LEU B 1 163 ? 1.579   -5.160  44.198  1.00 13.22 ? 164 LEU B CB  1 
ATOM   3460 C  CG  . LEU B 1 163 ? 0.506   -4.792  43.131  1.00 11.43 ? 164 LEU B CG  1 
ATOM   3461 C  CD1 . LEU B 1 163 ? -0.556  -5.900  43.025  1.00 14.67 ? 164 LEU B CD1 1 
ATOM   3462 C  CD2 . LEU B 1 163 ? -0.145  -3.435  43.429  1.00 12.59 ? 164 LEU B CD2 1 
ATOM   3463 N  N   . ASP B 1 164 ? 4.653   -5.129  45.374  1.00 14.53 ? 165 ASP B N   1 
ATOM   3464 C  CA  . ASP B 1 164 ? 5.516   -5.469  46.522  1.00 16.44 ? 165 ASP B CA  1 
ATOM   3465 C  C   . ASP B 1 164 ? 6.076   -4.175  47.221  1.00 15.99 ? 165 ASP B C   1 
ATOM   3466 O  O   . ASP B 1 164 ? 6.457   -4.255  48.389  1.00 22.24 ? 165 ASP B O   1 
ATOM   3467 C  CB  . ASP B 1 164 ? 6.711   -6.319  46.098  1.00 22.62 ? 165 ASP B CB  1 
ATOM   3468 C  CG  . ASP B 1 164 ? 7.786   -5.469  45.430  1.00 30.31 ? 165 ASP B CG  1 
ATOM   3469 O  OD1 . ASP B 1 164 ? 7.568   -4.914  44.309  1.00 30.81 ? 165 ASP B OD1 1 
ATOM   3470 O  OD2 . ASP B 1 164 ? 8.884   -5.321  46.058  1.00 57.15 ? 165 ASP B OD2 1 
ATOM   3471 N  N   . SER B 1 165 ? 6.062   -3.025  46.537  1.00 13.98 ? 166 SER B N   1 
ATOM   3472 C  CA  . SER B 1 165 ? 6.538   -1.775  47.136  1.00 15.32 ? 166 SER B CA  1 
ATOM   3473 C  C   . SER B 1 165 ? 5.425   -1.026  47.913  1.00 14.41 ? 166 SER B C   1 
ATOM   3474 O  O   . SER B 1 165 ? 5.707   -0.005  48.549  1.00 16.27 ? 166 SER B O   1 
ATOM   3475 C  CB  . SER B 1 165 ? 7.214   -0.897  46.075  1.00 19.54 ? 166 SER B CB  1 
ATOM   3476 O  OG  . SER B 1 165 ? 6.174   -0.324  45.296  1.00 19.31 ? 166 SER B OG  1 
ATOM   3477 N  N   . ILE B 1 166 ? 4.168   -1.502  47.827  1.00 12.58 ? 167 ILE B N   1 
ATOM   3478 C  CA  . ILE B 1 166 ? 3.065   -0.869  48.503  1.00 12.05 ? 167 ILE B CA  1 
ATOM   3479 C  C   . ILE B 1 166 ? 2.277   -1.902  49.308  1.00 12.51 ? 167 ILE B C   1 
ATOM   3480 O  O   . ILE B 1 166 ? 1.042   -1.921  49.309  1.00 12.41 ? 167 ILE B O   1 
ATOM   3481 C  CB  . ILE B 1 166 ? 2.196   -0.024  47.535  1.00 12.43 ? 167 ILE B CB  1 
ATOM   3482 C  CG1 . ILE B 1 166 ? 1.598   -0.907  46.415  1.00 11.20 ? 167 ILE B CG1 1 
ATOM   3483 C  CG2 . ILE B 1 166 ? 2.947   1.246   47.013  1.00 13.95 ? 167 ILE B CG2 1 
ATOM   3484 C  CD1 . ILE B 1 166 ? 0.321   -0.282  45.959  1.00 12.58 ? 167 ILE B CD1 1 
ATOM   3485 N  N   . LYS B 1 167 ? 2.990   -2.810  50.008  1.00 12.54 ? 168 LYS B N   1 
ATOM   3486 C  CA  . LYS B 1 167 ? 2.344   -3.969  50.621  1.00 12.18 ? 168 LYS B CA  1 
ATOM   3487 C  C   . LYS B 1 167 ? 1.267   -3.568  51.616  1.00 12.69 ? 168 LYS B C   1 
ATOM   3488 O  O   . LYS B 1 167 ? 0.238   -4.216  51.765  1.00 13.07 ? 168 LYS B O   1 
ATOM   3489 C  CB  . LYS B 1 167 ? 3.381   -4.873  51.264  1.00 13.35 ? 168 LYS B CB  1 
ATOM   3490 C  CG  . LYS B 1 167 ? 2.748   -6.172  51.860  1.00 16.02 ? 168 LYS B CG  1 
ATOM   3491 C  CD  . LYS B 1 167 ? 3.843   -7.094  52.484  1.00 21.87 ? 168 LYS B CD  1 
ATOM   3492 C  CE  . LYS B 1 167 ? 3.209   -8.009  53.517  1.00 28.85 ? 168 LYS B CE  1 
ATOM   3493 N  NZ  . LYS B 1 167 ? 4.037   -9.146  53.955  1.00 44.26 ? 168 LYS B NZ  1 
ATOM   3494 N  N   . THR B 1 168 ? 1.555   -2.489  52.364  1.00 13.19 ? 169 THR B N   1 
ATOM   3495 C  CA  . THR B 1 168 ? 0.731   -2.198  53.536  1.00 12.99 ? 169 THR B CA  1 
ATOM   3496 C  C   . THR B 1 168 ? 0.050   -0.767  53.444  1.00 12.43 ? 169 THR B C   1 
ATOM   3497 O  O   . THR B 1 168 ? 0.480   0.065   52.644  1.00 12.55 ? 169 THR B O   1 
ATOM   3498 C  CB  . THR B 1 168 ? 1.607   -2.236  54.848  1.00 13.85 ? 169 THR B CB  1 
ATOM   3499 O  OG1 . THR B 1 168 ? 2.765   -1.465  54.647  1.00 15.79 ? 169 THR B OG1 1 
ATOM   3500 C  CG2 . THR B 1 168 ? 1.913   -3.708  55.180  1.00 15.08 ? 169 THR B CG2 1 
ATOM   3501 N  N   . LYS B 1 169 ? -1.010  -0.607  54.194  1.00 12.75 ? 170 LYS B N   1 
ATOM   3502 C  CA  . LYS B 1 169 ? -1.824  0.579   54.190  1.00 14.16 ? 170 LYS B CA  1 
ATOM   3503 C  C   . LYS B 1 169 ? -0.975  1.852   54.353  1.00 14.10 ? 170 LYS B C   1 
ATOM   3504 O  O   . LYS B 1 169 ? -0.104  1.899   55.276  1.00 18.08 ? 170 LYS B O   1 
ATOM   3505 C  CB  . LYS B 1 169 ? -2.787  0.470   55.342  1.00 13.85 ? 170 LYS B CB  1 
ATOM   3506 C  CG  . LYS B 1 169 ? -3.718  1.710   55.500  1.00 16.51 ? 170 LYS B CG  1 
ATOM   3507 C  CD  . LYS B 1 169 ? -4.785  1.494   56.582  1.00 17.14 ? 170 LYS B CD  1 
ATOM   3508 C  CE  . LYS B 1 169 ? -4.248  0.917   57.880  1.00 25.32 ? 170 LYS B CE  1 
ATOM   3509 N  NZ  . LYS B 1 169 ? -5.243  1.046   58.999  1.00 39.70 ? 170 LYS B NZ  1 
ATOM   3510 N  N   . GLY B 1 170 ? -1.172  2.812   53.468  1.00 14.01 ? 171 GLY B N   1 
ATOM   3511 C  CA  . GLY B 1 170 ? -0.566  4.126   53.530  1.00 14.34 ? 171 GLY B CA  1 
ATOM   3512 C  C   . GLY B 1 170 ? 0.755   4.171   52.740  1.00 16.93 ? 171 GLY B C   1 
ATOM   3513 O  O   . GLY B 1 170 ? 1.345   5.297   52.553  1.00 18.09 ? 171 GLY B O   1 
ATOM   3514 N  N   . LYS B 1 171 ? 1.220   3.015   52.196  1.00 12.84 ? 172 LYS B N   1 
ATOM   3515 C  CA  . LYS B 1 171 ? 2.369   3.106   51.282  1.00 13.66 ? 172 LYS B CA  1 
ATOM   3516 C  C   . LYS B 1 171 ? 1.986   3.557   49.882  1.00 13.63 ? 172 LYS B C   1 
ATOM   3517 O  O   . LYS B 1 171 ? 0.947   3.141   49.335  1.00 13.51 ? 172 LYS B O   1 
ATOM   3518 C  CB  . LYS B 1 171 ? 3.071   1.750   51.208  1.00 15.79 ? 172 LYS B CB  1 
ATOM   3519 C  CG  . LYS B 1 171 ? 3.631   1.371   52.561  1.00 17.64 ? 172 LYS B CG  1 
ATOM   3520 C  CD  . LYS B 1 171 ? 4.843   0.400   52.499  1.00 23.02 ? 172 LYS B CD  1 
ATOM   3521 C  CE  . LYS B 1 171 ? 5.846   0.522   53.677  1.00 34.85 ? 172 LYS B CE  1 
ATOM   3522 N  NZ  . LYS B 1 171 ? 6.628   -0.737  53.792  1.00 45.41 ? 172 LYS B NZ  1 
ATOM   3523 N  N   . SER B 1 172 ? 2.780   4.406   49.291  1.00 13.47 ? 173 SER B N   1 
ATOM   3524 C  CA  . SER B 1 172 ? 2.651   4.779   47.912  1.00 14.79 ? 173 SER B CA  1 
ATOM   3525 C  C   . SER B 1 172 ? 3.973   4.702   47.150  1.00 14.06 ? 173 SER B C   1 
ATOM   3526 O  O   . SER B 1 172 ? 5.100   4.658   47.753  1.00 17.25 ? 173 SER B O   1 
ATOM   3527 C  CB  . SER B 1 172 ? 2.098   6.218   47.771  1.00 14.10 ? 173 SER B CB  1 
ATOM   3528 O  OG  . SER B 1 172 ? 2.979   7.108   48.445  1.00 19.32 ? 173 SER B OG  1 
ATOM   3529 N  N   . ALA B 1 173 ? 3.894   4.766   45.839  1.00 14.75 ? 174 ALA B N   1 
ATOM   3530 C  CA  . ALA B 1 173 ? 5.106   4.704   44.955  1.00 14.95 ? 174 ALA B CA  1 
ATOM   3531 C  C   . ALA B 1 173 ? 4.824   5.522   43.710  1.00 14.88 ? 174 ALA B C   1 
ATOM   3532 O  O   . ALA B 1 173 ? 3.661   5.592   43.229  1.00 13.31 ? 174 ALA B O   1 
ATOM   3533 C  CB  . ALA B 1 173 ? 5.423   3.258   44.596  1.00 17.31 ? 174 ALA B CB  1 
ATOM   3534 N  N   . ASP B 1 174 ? 5.835   6.163   43.149  1.00 15.93 ? 175 ASP B N   1 
ATOM   3535 C  CA  . ASP B 1 174 ? 5.714   6.832   41.876  1.00 16.82 ? 175 ASP B CA  1 
ATOM   3536 C  C   . ASP B 1 174 ? 5.253   5.815   40.847  1.00 18.77 ? 175 ASP B C   1 
ATOM   3537 O  O   . ASP B 1 174 ? 5.692   4.658   40.873  1.00 19.74 ? 175 ASP B O   1 
ATOM   3538 C  CB  . ASP B 1 174 ? 7.096   7.412   41.454  1.00 21.99 ? 175 ASP B CB  1 
ATOM   3539 C  CG  . ASP B 1 174 ? 7.532   8.473   42.438  1.00 26.24 ? 175 ASP B CG  1 
ATOM   3540 O  OD1 . ASP B 1 174 ? 6.650   9.279   42.933  1.00 32.98 ? 175 ASP B OD1 1 
ATOM   3541 O  OD2 . ASP B 1 174 ? 8.744   8.491   42.812  1.00 29.14 ? 175 ASP B OD2 1 
ATOM   3542 N  N   . PHE B 1 175 ? 4.364   6.238   39.952  1.00 14.12 ? 176 PHE B N   1 
ATOM   3543 C  CA  . PHE B 1 175 ? 3.825   5.289   38.973  1.00 14.17 ? 176 PHE B CA  1 
ATOM   3544 C  C   . PHE B 1 175 ? 3.451   6.100   37.763  1.00 13.33 ? 176 PHE B C   1 
ATOM   3545 O  O   . PHE B 1 175 ? 2.289   6.402   37.525  1.00 16.90 ? 176 PHE B O   1 
ATOM   3546 C  CB  . PHE B 1 175 ? 2.619   4.501   39.525  1.00 13.62 ? 176 PHE B CB  1 
ATOM   3547 C  CG  . PHE B 1 175 ? 2.363   3.239   38.792  1.00 13.10 ? 176 PHE B CG  1 
ATOM   3548 C  CD1 . PHE B 1 175 ? 3.268   2.202   38.786  1.00 15.93 ? 176 PHE B CD1 1 
ATOM   3549 C  CD2 . PHE B 1 175 ? 1.181   3.095   38.126  1.00 14.95 ? 176 PHE B CD2 1 
ATOM   3550 C  CE1 . PHE B 1 175 ? 2.992   1.023   38.090  1.00 17.58 ? 176 PHE B CE1 1 
ATOM   3551 C  CE2 . PHE B 1 175 ? 0.830   1.940   37.440  1.00 14.39 ? 176 PHE B CE2 1 
ATOM   3552 C  CZ  . PHE B 1 175 ? 1.757   0.910   37.416  1.00 15.16 ? 176 PHE B CZ  1 
ATOM   3553 N  N   . THR B 1 176 ? 4.423   6.547   37.015  1.00 13.89 ? 177 THR B N   1 
ATOM   3554 C  CA  . THR B 1 176 ? 4.230   7.374   35.845  1.00 14.32 ? 177 THR B CA  1 
ATOM   3555 C  C   . THR B 1 176 ? 4.191   6.585   34.557  1.00 10.19 ? 177 THR B C   1 
ATOM   3556 O  O   . THR B 1 176 ? 4.674   5.442   34.460  1.00 13.39 ? 177 THR B O   1 
ATOM   3557 C  CB  . THR B 1 176 ? 5.335   8.419   35.746  1.00 16.22 ? 177 THR B CB  1 
ATOM   3558 O  OG1 . THR B 1 176 ? 6.618   7.742   35.652  1.00 20.83 ? 177 THR B OG1 1 
ATOM   3559 C  CG2 . THR B 1 176 ? 5.279   9.341   36.962  1.00 21.16 ? 177 THR B CG2 1 
ATOM   3560 N  N   . ASN B 1 177 ? 3.598   7.163   33.520  1.00 13.46 ? 178 ASN B N   1 
ATOM   3561 C  CA  . ASN B 1 177 ? 3.642   6.588   32.168  1.00 15.19 ? 178 ASN B CA  1 
ATOM   3562 C  C   . ASN B 1 177 ? 2.929   5.246   32.070  1.00 16.14 ? 178 ASN B C   1 
ATOM   3563 O  O   . ASN B 1 177 ? 3.185   4.478   31.153  1.00 19.80 ? 178 ASN B O   1 
ATOM   3564 C  CB  . ASN B 1 177 ? 5.060   6.506   31.644  1.00 16.10 ? 178 ASN B CB  1 
ATOM   3565 C  CG  . ASN B 1 177 ? 5.675   7.905   31.621  1.00 15.45 ? 178 ASN B CG  1 
ATOM   3566 O  OD1 . ASN B 1 177 ? 5.310   8.757   30.797  1.00 20.29 ? 178 ASN B OD1 1 
ATOM   3567 N  ND2 . ASN B 1 177 ? 6.582   8.154   32.564  1.00 15.90 ? 178 ASN B ND2 1 
ATOM   3568 N  N   . PHE B 1 178 ? 1.977   5.016   32.961  1.00 12.95 ? 179 PHE B N   1 
ATOM   3569 C  CA  . PHE B 1 178 ? 1.163   3.830   32.804  1.00 11.84 ? 179 PHE B CA  1 
ATOM   3570 C  C   . PHE B 1 178 ? -0.031  4.057   31.918  1.00 11.90 ? 179 PHE B C   1 
ATOM   3571 O  O   . PHE B 1 178 ? -0.752  5.040   32.133  1.00 13.42 ? 179 PHE B O   1 
ATOM   3572 C  CB  . PHE B 1 178 ? 0.645   3.377   34.167  1.00 12.12 ? 179 PHE B CB  1 
ATOM   3573 C  CG  . PHE B 1 178 ? -0.190  2.133   34.008  1.00 11.13 ? 179 PHE B CG  1 
ATOM   3574 C  CD1 . PHE B 1 178 ? 0.465   0.864   33.760  1.00 13.04 ? 179 PHE B CD1 1 
ATOM   3575 C  CD2 . PHE B 1 178 ? -1.585  2.148   33.985  1.00 11.86 ? 179 PHE B CD2 1 
ATOM   3576 C  CE1 . PHE B 1 178 ? -0.290  -0.285  33.541  1.00 13.38 ? 179 PHE B CE1 1 
ATOM   3577 C  CE2 . PHE B 1 178 ? -2.289  0.955   33.709  1.00 10.99 ? 179 PHE B CE2 1 
ATOM   3578 C  CZ  . PHE B 1 178 ? -1.664  -0.242  33.481  1.00 11.04 ? 179 PHE B CZ  1 
ATOM   3579 N  N   . ASP B 1 179 ? -0.226  3.230   30.896  1.00 12.72 ? 180 ASP B N   1 
ATOM   3580 C  CA  . ASP B 1 179 ? -1.249  3.459   29.907  1.00 12.04 ? 180 ASP B CA  1 
ATOM   3581 C  C   . ASP B 1 179 ? -2.470  2.567   30.172  1.00 11.74 ? 180 ASP B C   1 
ATOM   3582 O  O   . ASP B 1 179 ? -2.407  1.331   30.010  1.00 12.03 ? 180 ASP B O   1 
ATOM   3583 C  CB  . ASP B 1 179 ? -0.685  3.193   28.515  1.00 13.11 ? 180 ASP B CB  1 
ATOM   3584 C  CG  . ASP B 1 179 ? -1.623  3.572   27.380  1.00 16.73 ? 180 ASP B CG  1 
ATOM   3585 O  OD1 . ASP B 1 179 ? -2.847  3.714   27.563  1.00 14.84 ? 180 ASP B OD1 1 
ATOM   3586 O  OD2 . ASP B 1 179 ? -1.066  3.770   26.255  1.00 22.38 ? 180 ASP B OD2 1 
ATOM   3587 N  N   . PRO B 1 180 ? -3.568  3.168   30.678  1.00 11.53 ? 181 PRO B N   1 
ATOM   3588 C  CA  . PRO B 1 180 ? -4.736  2.294   31.059  1.00 12.49 ? 181 PRO B CA  1 
ATOM   3589 C  C   . PRO B 1 180 ? -5.418  1.692   29.837  1.00 11.21 ? 181 PRO B C   1 
ATOM   3590 O  O   . PRO B 1 180 ? -6.268  0.766   29.994  1.00 10.96 ? 181 PRO B O   1 
ATOM   3591 C  CB  . PRO B 1 180 ? -5.640  3.258   31.770  1.00 13.27 ? 181 PRO B CB  1 
ATOM   3592 C  CG  . PRO B 1 180 ? -5.319  4.611   31.193  1.00 13.48 ? 181 PRO B CG  1 
ATOM   3593 C  CD  . PRO B 1 180 ? -3.816  4.585   30.892  1.00 13.49 ? 181 PRO B CD  1 
ATOM   3594 N  N   . ARG B 1 181 ? -5.091  2.093   28.591  1.00 11.98 ? 182 ARG B N   1 
ATOM   3595 C  CA  . ARG B 1 181 ? -5.656  1.393   27.390  1.00 11.28 ? 182 ARG B CA  1 
ATOM   3596 C  C   . ARG B 1 181 ? -5.256  -0.052  27.377  1.00 12.46 ? 182 ARG B C   1 
ATOM   3597 O  O   . ARG B 1 181 ? -5.954  -0.835  26.755  1.00 12.32 ? 182 ARG B O   1 
ATOM   3598 C  CB  . ARG B 1 181 ? -5.190  2.082   26.085  1.00 11.81 ? 182 ARG B CB  1 
ATOM   3599 C  CG  . ARG B 1 181 ? -5.793  3.480   25.951  1.00 13.13 ? 182 ARG B CG  1 
ATOM   3600 C  CD  . ARG B 1 181 ? -5.295  4.227   24.723  1.00 15.13 ? 182 ARG B CD  1 
ATOM   3601 N  NE  . ARG B 1 181 ? -3.869  4.498   24.881  1.00 14.77 ? 182 ARG B NE  1 
ATOM   3602 C  CZ  . ARG B 1 181 ? -3.183  5.231   24.000  1.00 19.79 ? 182 ARG B CZ  1 
ATOM   3603 N  NH1 . ARG B 1 181 ? -3.776  5.758   22.910  1.00 23.64 ? 182 ARG B NH1 1 
ATOM   3604 N  NH2 . ARG B 1 181 ? -1.895  5.433   24.226  1.00 20.30 ? 182 ARG B NH2 1 
ATOM   3605 N  N   . GLY B 1 182 ? -4.148  -0.431  28.048  1.00 11.14 ? 183 GLY B N   1 
ATOM   3606 C  CA  . GLY B 1 182 ? -3.731  -1.841  28.034  1.00 12.41 ? 183 GLY B CA  1 
ATOM   3607 C  C   . GLY B 1 182 ? -4.574  -2.736  28.969  1.00 13.12 ? 183 GLY B C   1 
ATOM   3608 O  O   . GLY B 1 182 ? -4.298  -3.933  29.069  1.00 13.47 ? 183 GLY B O   1 
ATOM   3609 N  N   . LEU B 1 183 ? -5.598  -2.148  29.619  1.00 10.97 ? 184 LEU B N   1 
ATOM   3610 C  CA  . LEU B 1 183 ? -6.502  -2.853  30.544  1.00 11.29 ? 184 LEU B CA  1 
ATOM   3611 C  C   . LEU B 1 183 ? -7.879  -3.058  29.926  1.00 11.53 ? 184 LEU B C   1 
ATOM   3612 O  O   . LEU B 1 183 ? -8.772  -3.630  30.600  1.00 12.28 ? 184 LEU B O   1 
ATOM   3613 C  CB  . LEU B 1 183 ? -6.661  -2.158  31.881  1.00 12.13 ? 184 LEU B CB  1 
ATOM   3614 C  CG  . LEU B 1 183 ? -5.353  -2.013  32.661  1.00 11.76 ? 184 LEU B CG  1 
ATOM   3615 C  CD1 . LEU B 1 183 ? -5.593  -1.162  33.865  1.00 14.11 ? 184 LEU B CD1 1 
ATOM   3616 C  CD2 . LEU B 1 183 ? -4.718  -3.338  33.059  1.00 17.95 ? 184 LEU B CD2 1 
ATOM   3617 N  N   . LEU B 1 184 ? -8.109  -2.608  28.691  1.00 11.30 ? 185 LEU B N   1 
ATOM   3618 C  CA  . LEU B 1 184 ? -9.437  -2.639  28.122  1.00 10.96 ? 185 LEU B CA  1 
ATOM   3619 C  C   . LEU B 1 184 ? -9.694  -3.826  27.163  1.00 11.37 ? 185 LEU B C   1 
ATOM   3620 O  O   . LEU B 1 184 ? -8.797  -4.160  26.320  1.00 14.19 ? 185 LEU B O   1 
ATOM   3621 C  CB  . LEU B 1 184 ? -9.746  -1.365  27.255  1.00 10.96 ? 185 LEU B CB  1 
ATOM   3622 C  CG  . LEU B 1 184 ? -9.501  -0.043  27.998  1.00 11.83 ? 185 LEU B CG  1 
ATOM   3623 C  CD1 . LEU B 1 184 ? -9.708  1.121   27.037  1.00 13.35 ? 185 LEU B CD1 1 
ATOM   3624 C  CD2 . LEU B 1 184 ? -10.376 0.132   29.252  1.00 13.26 ? 185 LEU B CD2 1 
ATOM   3625 N  N   . PRO B 1 185 ? -10.859 -4.444  27.254  1.00 10.92 ? 186 PRO B N   1 
ATOM   3626 C  CA  . PRO B 1 185 ? -11.184 -5.550  26.333  1.00 10.42 ? 186 PRO B CA  1 
ATOM   3627 C  C   . PRO B 1 185 ? -11.465 -5.022  24.910  1.00 11.91 ? 186 PRO B C   1 
ATOM   3628 O  O   . PRO B 1 185 ? -11.547 -3.809  24.714  1.00 12.84 ? 186 PRO B O   1 
ATOM   3629 C  CB  . PRO B 1 185 ? -12.447 -6.157  26.970  1.00 11.29 ? 186 PRO B CB  1 
ATOM   3630 C  CG  . PRO B 1 185 ? -13.158 -4.955  27.558  1.00 11.18 ? 186 PRO B CG  1 
ATOM   3631 C  CD  . PRO B 1 185 ? -12.018 -4.057  28.093  1.00 11.46 ? 186 PRO B CD  1 
ATOM   3632 N  N   . GLU B 1 186 ? -11.654 -5.931  23.942  1.00 12.28 ? 187 GLU B N   1 
ATOM   3633 C  CA  . GLU B 1 186 ? -11.866 -5.485  22.563  1.00 13.15 ? 187 GLU B CA  1 
ATOM   3634 C  C   . GLU B 1 186 ? -13.097 -4.736  22.428  1.00 14.13 ? 187 GLU B C   1 
ATOM   3635 O  O   . GLU B 1 186 ? -13.101 -3.668  21.869  1.00 18.20 ? 187 GLU B O   1 
ATOM   3636 C  CB  . GLU B 1 186 ? -12.029 -6.725  21.655  1.00 16.23 ? 187 GLU B CB  1 
ATOM   3637 C  CG  . GLU B 1 186 ? -10.746 -7.425  21.440  1.00 20.61 ? 187 GLU B CG  1 
ATOM   3638 C  CD  . GLU B 1 186 ? -10.948 -8.723  20.574  1.00 19.09 ? 187 GLU B CD  1 
ATOM   3639 O  OE1 . GLU B 1 186 ? -12.043 -8.933  20.103  1.00 20.24 ? 187 GLU B OE1 1 
ATOM   3640 O  OE2 . GLU B 1 186 ? -9.976  -9.419  20.435  1.00 24.50 ? 187 GLU B OE2 1 
ATOM   3641 N  N   . SER B 1 187 ? -14.189 -5.265  22.972  1.00 13.18 ? 188 SER B N   1 
ATOM   3642 C  CA  . SER B 1 187 ? -15.466 -4.661  22.798  1.00 14.43 ? 188 SER B CA  1 
ATOM   3643 C  C   . SER B 1 187 ? -15.811 -3.652  23.882  1.00 13.88 ? 188 SER B C   1 
ATOM   3644 O  O   . SER B 1 187 ? -15.579 -3.923  25.080  1.00 14.74 ? 188 SER B O   1 
ATOM   3645 C  CB  . SER B 1 187 ? -16.612 -5.707  22.834  1.00 13.84 ? 188 SER B CB  1 
ATOM   3646 O  OG  . SER B 1 187 ? -17.891 -5.180  22.639  1.00 15.26 ? 188 SER B OG  1 
ATOM   3647 N  N   . LEU B 1 188 ? -16.491 -2.600  23.483  1.00 12.31 ? 189 LEU B N   1 
ATOM   3648 C  CA  . LEU B 1 188 ? -17.040 -1.598  24.404  1.00 14.11 ? 189 LEU B CA  1 
ATOM   3649 C  C   . LEU B 1 188 ? -18.541 -1.773  24.602  1.00 11.80 ? 189 LEU B C   1 
ATOM   3650 O  O   . LEU B 1 188 ? -19.214 -0.880  25.117  1.00 15.74 ? 189 LEU B O   1 
ATOM   3651 C  CB  . LEU B 1 188 ? -16.649 -0.178  24.012  1.00 17.29 ? 189 LEU B CB  1 
ATOM   3652 C  CG  . LEU B 1 188 ? -15.197 0.251   24.072  1.00 17.82 ? 189 LEU B CG  1 
ATOM   3653 C  CD1 . LEU B 1 188 ? -15.075 1.732   23.672  1.00 19.47 ? 189 LEU B CD1 1 
ATOM   3654 C  CD2 . LEU B 1 188 ? -14.651 0.002   25.476  1.00 14.97 ? 189 LEU B CD2 1 
ATOM   3655 N  N   . ASP B 1 189 ? -19.174 -2.906  24.226  1.00 12.73 ? 190 ASP B N   1 
ATOM   3656 C  CA  . ASP B 1 189 ? -20.577 -3.213  24.613  1.00 13.76 ? 190 ASP B CA  1 
ATOM   3657 C  C   . ASP B 1 189 ? -20.741 -3.117  26.138  1.00 10.80 ? 190 ASP B C   1 
ATOM   3658 O  O   . ASP B 1 189 ? -19.812 -3.633  26.844  1.00 11.34 ? 190 ASP B O   1 
ATOM   3659 C  CB  . ASP B 1 189 ? -20.961 -4.647  24.200  1.00 18.68 ? 190 ASP B CB  1 
ATOM   3660 C  CG  . ASP B 1 189 ? -21.142 -4.835  22.683  1.00 23.52 ? 190 ASP B CG  1 
ATOM   3661 O  OD1 . ASP B 1 189 ? -21.254 -3.833  21.982  1.00 25.37 ? 190 ASP B OD1 1 
ATOM   3662 O  OD2 . ASP B 1 189 ? -21.237 -5.997  22.279  1.00 29.00 ? 190 ASP B OD2 1 
ATOM   3663 N  N   . TYR B 1 190 ? -21.830 -2.527  26.601  1.00 10.05 ? 191 TYR B N   1 
ATOM   3664 C  CA  . TYR B 1 190 ? -21.932 -2.295  28.033  1.00 10.37 ? 191 TYR B CA  1 
ATOM   3665 C  C   . TYR B 1 190 ? -23.353 -2.374  28.480  1.00 10.28 ? 191 TYR B C   1 
ATOM   3666 O  O   . TYR B 1 190 ? -24.345 -2.218  27.707  1.00 10.65 ? 191 TYR B O   1 
ATOM   3667 C  CB  . TYR B 1 190 ? -21.328 -0.881  28.369  1.00 11.37 ? 191 TYR B CB  1 
ATOM   3668 C  CG  . TYR B 1 190 ? -22.049 0.301   27.754  1.00 10.58 ? 191 TYR B CG  1 
ATOM   3669 C  CD1 . TYR B 1 190 ? -23.179 0.855   28.322  1.00 11.88 ? 191 TYR B CD1 1 
ATOM   3670 C  CD2 . TYR B 1 190 ? -21.585 0.850   26.528  1.00 11.19 ? 191 TYR B CD2 1 
ATOM   3671 C  CE1 . TYR B 1 190 ? -23.866 1.906   27.657  1.00 12.49 ? 191 TYR B CE1 1 
ATOM   3672 C  CE2 . TYR B 1 190 ? -22.214 1.929   25.908  1.00 13.31 ? 191 TYR B CE2 1 
ATOM   3673 C  CZ  . TYR B 1 190 ? -23.335 2.440   26.486  1.00 13.80 ? 191 TYR B CZ  1 
ATOM   3674 O  OH  . TYR B 1 190 ? -24.014 3.457   25.845  1.00 15.60 ? 191 TYR B OH  1 
ATOM   3675 N  N   . TRP B 1 191 ? -23.486 -2.471  29.796  1.00 9.34  ? 192 TRP B N   1 
ATOM   3676 C  CA  . TRP B 1 191 ? -24.701 -2.220  30.529  1.00 9.34  ? 192 TRP B CA  1 
ATOM   3677 C  C   . TRP B 1 191 ? -24.567 -0.934  31.370  1.00 8.34  ? 192 TRP B C   1 
ATOM   3678 O  O   . TRP B 1 191 ? -23.434 -0.582  31.744  1.00 10.40 ? 192 TRP B O   1 
ATOM   3679 C  CB  . TRP B 1 191 ? -25.030 -3.358  31.498  1.00 10.70 ? 192 TRP B CB  1 
ATOM   3680 C  CG  . TRP B 1 191 ? -25.267 -4.657  30.877  1.00 9.53  ? 192 TRP B CG  1 
ATOM   3681 C  CD1 . TRP B 1 191 ? -26.431 -5.076  30.209  1.00 10.41 ? 192 TRP B CD1 1 
ATOM   3682 C  CD2 . TRP B 1 191 ? -24.346 -5.779  30.863  1.00 10.09 ? 192 TRP B CD2 1 
ATOM   3683 N  NE1 . TRP B 1 191 ? -26.240 -6.414  29.828  1.00 12.00 ? 192 TRP B NE1 1 
ATOM   3684 C  CE2 . TRP B 1 191 ? -25.023 -6.862  30.217  1.00 11.45 ? 192 TRP B CE2 1 
ATOM   3685 C  CE3 . TRP B 1 191 ? -23.097 -5.990  31.406  1.00 10.42 ? 192 TRP B CE3 1 
ATOM   3686 C  CZ2 . TRP B 1 191 ? -24.403 -8.116  30.078  1.00 11.46 ? 192 TRP B CZ2 1 
ATOM   3687 C  CZ3 . TRP B 1 191 ? -22.486 -7.231  31.308  1.00 10.98 ? 192 TRP B CZ3 1 
ATOM   3688 C  CH2 . TRP B 1 191 ? -23.152 -8.271  30.673  1.00 11.75 ? 192 TRP B CH2 1 
ATOM   3689 N  N   . THR B 1 192 ? -25.628 -0.225  31.595  1.00 8.20  ? 193 THR B N   1 
ATOM   3690 C  CA  . THR B 1 192 ? -25.536 1.055   32.344  1.00 8.81  ? 193 THR B CA  1 
ATOM   3691 C  C   . THR B 1 192 ? -26.743 1.233   33.232  1.00 8.50  ? 193 THR B C   1 
ATOM   3692 O  O   . THR B 1 192 ? -27.892 0.790   32.872  1.00 9.95  ? 193 THR B O   1 
ATOM   3693 C  CB  . THR B 1 192 ? -25.289 2.226   31.391  1.00 8.57  ? 193 THR B CB  1 
ATOM   3694 O  OG1 . THR B 1 192 ? -25.158 3.437   32.221  1.00 9.80  ? 193 THR B OG1 1 
ATOM   3695 C  CG2 . THR B 1 192 ? -26.509 2.475   30.485  1.00 10.99 ? 193 THR B CG2 1 
ATOM   3696 N  N   . TYR B 1 193 ? -26.549 1.838   34.437  1.00 8.98  ? 194 TYR B N   1 
ATOM   3697 C  CA  . TYR B 1 193 ? -27.633 2.093   35.331  1.00 9.26  ? 194 TYR B CA  1 
ATOM   3698 C  C   . TYR B 1 193 ? -27.143 3.124   36.335  1.00 8.29  ? 194 TYR B C   1 
ATOM   3699 O  O   . TYR B 1 193 ? -25.942 3.320   36.502  1.00 8.84  ? 194 TYR B O   1 
ATOM   3700 C  CB  . TYR B 1 193 ? -28.109 0.791   36.106  1.00 9.43  ? 194 TYR B CB  1 
ATOM   3701 C  CG  . TYR B 1 193 ? -27.129 0.292   37.130  1.00 8.81  ? 194 TYR B CG  1 
ATOM   3702 C  CD1 . TYR B 1 193 ? -26.009 -0.457  36.788  1.00 8.97  ? 194 TYR B CD1 1 
ATOM   3703 C  CD2 . TYR B 1 193 ? -27.334 0.648   38.466  1.00 8.71  ? 194 TYR B CD2 1 
ATOM   3704 C  CE1 . TYR B 1 193 ? -25.041 -0.743  37.759  1.00 8.80  ? 194 TYR B CE1 1 
ATOM   3705 C  CE2 . TYR B 1 193 ? -26.408 0.328   39.443  1.00 9.31  ? 194 TYR B CE2 1 
ATOM   3706 C  CZ  . TYR B 1 193 ? -25.273 -0.391  39.093  1.00 8.28  ? 194 TYR B CZ  1 
ATOM   3707 O  OH  . TYR B 1 193 ? -24.337 -0.684  40.083  1.00 8.09  ? 194 TYR B OH  1 
ATOM   3708 N  N   . PRO B 1 194 ? -28.063 3.821   36.999  1.00 9.02  ? 195 PRO B N   1 
ATOM   3709 C  CA  . PRO B 1 194 ? -27.704 4.824   37.984  1.00 9.08  ? 195 PRO B CA  1 
ATOM   3710 C  C   . PRO B 1 194 ? -27.467 4.181   39.377  1.00 8.10  ? 195 PRO B C   1 
ATOM   3711 O  O   . PRO B 1 194 ? -28.312 3.387   39.858  1.00 10.09 ? 195 PRO B O   1 
ATOM   3712 C  CB  . PRO B 1 194 ? -28.914 5.761   38.037  1.00 11.05 ? 195 PRO B CB  1 
ATOM   3713 C  CG  . PRO B 1 194 ? -30.085 4.804   37.660  1.00 11.17 ? 195 PRO B CG  1 
ATOM   3714 C  CD  . PRO B 1 194 ? -29.520 3.856   36.669  1.00 10.87 ? 195 PRO B CD  1 
ATOM   3715 N  N   . GLY B 1 195 ? -26.337 4.509   39.983  1.00 8.10  ? 196 GLY B N   1 
ATOM   3716 C  CA  . GLY B 1 195 ? -25.980 3.872   41.263  1.00 8.06  ? 196 GLY B CA  1 
ATOM   3717 C  C   . GLY B 1 195 ? -25.134 4.727   42.139  1.00 8.06  ? 196 GLY B C   1 
ATOM   3718 O  O   . GLY B 1 195 ? -25.289 5.972   42.188  1.00 8.60  ? 196 GLY B O   1 
ATOM   3719 N  N   . SER B 1 196 ? -24.268 4.061   42.887  1.00 7.76  ? 197 SER B N   1 
ATOM   3720 C  CA  . SER B 1 196 ? -23.566 4.725   44.005  1.00 7.37  ? 197 SER B CA  1 
ATOM   3721 C  C   . SER B 1 196 ? -22.101 4.318   44.021  1.00 7.54  ? 197 SER B C   1 
ATOM   3722 O  O   . SER B 1 196 ? -21.673 3.364   43.346  1.00 7.91  ? 197 SER B O   1 
ATOM   3723 C  CB  . SER B 1 196 ? -24.123 4.328   45.373  1.00 8.69  ? 197 SER B CB  1 
ATOM   3724 O  OG  . SER B 1 196 ? -23.848 2.966   45.683  1.00 8.35  ? 197 SER B OG  1 
ATOM   3725 N  N   . LEU B 1 197 ? -21.296 4.971   44.847  1.00 7.41  ? 198 LEU B N   1 
ATOM   3726 C  CA  . LEU B 1 197 ? -20.012 4.386   45.269  1.00 8.01  ? 198 LEU B CA  1 
ATOM   3727 C  C   . LEU B 1 197 ? -20.250 3.080   45.935  1.00 7.81  ? 198 LEU B C   1 
ATOM   3728 O  O   . LEU B 1 197 ? -21.281 2.918   46.672  1.00 7.98  ? 198 LEU B O   1 
ATOM   3729 C  CB  . LEU B 1 197 ? -19.328 5.344   46.248  1.00 10.15 ? 198 LEU B CB  1 
ATOM   3730 C  CG  . LEU B 1 197 ? -19.059 6.763   45.781  1.00 9.40  ? 198 LEU B CG  1 
ATOM   3731 C  CD1 . LEU B 1 197 ? -18.378 7.592   46.894  1.00 11.75 ? 198 LEU B CD1 1 
ATOM   3732 C  CD2 . LEU B 1 197 ? -18.128 6.809   44.586  1.00 11.11 ? 198 LEU B CD2 1 
ATOM   3733 N  N   . THR B 1 198 ? -19.339 2.122   45.841  1.00 7.79  ? 199 THR B N   1 
ATOM   3734 C  CA  . THR B 1 198 ? -19.528 0.846   46.457  1.00 8.44  ? 199 THR B CA  1 
ATOM   3735 C  C   . THR B 1 198 ? -18.793 0.742   47.768  1.00 8.56  ? 199 THR B C   1 
ATOM   3736 O  O   . THR B 1 198 ? -18.834 -0.308  48.390  1.00 8.85  ? 199 THR B O   1 
ATOM   3737 C  CB  . THR B 1 198 ? -19.115 -0.306  45.539  1.00 8.09  ? 199 THR B CB  1 
ATOM   3738 O  OG1 . THR B 1 198 ? -17.699 -0.270  45.390  1.00 7.29  ? 199 THR B OG1 1 
ATOM   3739 C  CG2 . THR B 1 198 ? -19.851 -0.308  44.202  1.00 8.66  ? 199 THR B CG2 1 
ATOM   3740 N  N   . THR B 1 199 ? -18.105 1.814   48.197  1.00 9.14  ? 200 THR B N   1 
ATOM   3741 C  CA  . THR B 1 199 ? -17.484 1.909   49.481  1.00 9.90  ? 200 THR B CA  1 
ATOM   3742 C  C   . THR B 1 199 ? -18.085 3.149   50.201  1.00 9.50  ? 200 THR B C   1 
ATOM   3743 O  O   . THR B 1 199 ? -18.436 4.125   49.571  1.00 10.44 ? 200 THR B O   1 
ATOM   3744 C  CB  . THR B 1 199 ? -15.960 2.173   49.366  1.00 12.34 ? 200 THR B CB  1 
ATOM   3745 O  OG1 . THR B 1 199 ? -15.729 3.204   48.327  1.00 15.94 ? 200 THR B OG1 1 
ATOM   3746 C  CG2 . THR B 1 199 ? -15.287 0.882   48.827  1.00 12.41 ? 200 THR B CG2 1 
ATOM   3747 N  N   . PRO B 1 200 ? -18.079 3.123   51.560  1.00 10.20 ? 201 PRO B N   1 
ATOM   3748 C  CA  . PRO B 1 200 ? -18.388 4.361   52.315  1.00 11.64 ? 201 PRO B CA  1 
ATOM   3749 C  C   . PRO B 1 200 ? -17.591 5.522   51.672  1.00 11.31 ? 201 PRO B C   1 
ATOM   3750 O  O   . PRO B 1 200 ? -16.405 5.349   51.386  1.00 12.88 ? 201 PRO B O   1 
ATOM   3751 C  CB  . PRO B 1 200 ? -17.898 3.984   53.740  1.00 11.12 ? 201 PRO B CB  1 
ATOM   3752 C  CG  . PRO B 1 200 ? -18.214 2.532   53.832  1.00 12.24 ? 201 PRO B CG  1 
ATOM   3753 C  CD  . PRO B 1 200 ? -17.750 1.991   52.475  1.00 10.63 ? 201 PRO B CD  1 
ATOM   3754 N  N   . PRO B 1 201 ? -18.198 6.682   51.517  1.00 11.03 ? 202 PRO B N   1 
ATOM   3755 C  CA  . PRO B 1 201 ? -19.532 7.063   52.046  1.00 11.68 ? 202 PRO B CA  1 
ATOM   3756 C  C   . PRO B 1 201 ? -20.758 6.673   51.205  1.00 11.68 ? 202 PRO B C   1 
ATOM   3757 O  O   . PRO B 1 201 ? -21.882 7.067   51.528  1.00 11.69 ? 202 PRO B O   1 
ATOM   3758 C  CB  . PRO B 1 201 ? -19.401 8.571   52.143  1.00 13.48 ? 202 PRO B CB  1 
ATOM   3759 C  CG  . PRO B 1 201 ? -18.422 8.960   51.022  1.00 15.35 ? 202 PRO B CG  1 
ATOM   3760 C  CD  . PRO B 1 201 ? -17.427 7.841   51.006  1.00 13.91 ? 202 PRO B CD  1 
ATOM   3761 N  N   . LEU B 1 202 ? -20.579 5.834   50.162  1.00 9.04  ? 203 LEU B N   1 
ATOM   3762 C  CA  . LEU B 1 202 ? -21.717 5.196   49.469  1.00 8.50  ? 203 LEU B CA  1 
ATOM   3763 C  C   . LEU B 1 202 ? -22.647 6.237   48.761  1.00 9.78  ? 203 LEU B C   1 
ATOM   3764 O  O   . LEU B 1 202 ? -23.839 5.974   48.527  1.00 10.06 ? 203 LEU B O   1 
ATOM   3765 C  CB  . LEU B 1 202 ? -22.545 4.301   50.417  1.00 9.08  ? 203 LEU B CB  1 
ATOM   3766 C  CG  . LEU B 1 202 ? -21.725 3.130   51.001  1.00 9.42  ? 203 LEU B CG  1 
ATOM   3767 C  CD1 . LEU B 1 202 ? -22.545 2.499   52.135  1.00 12.07 ? 203 LEU B CD1 1 
ATOM   3768 C  CD2 . LEU B 1 202 ? -21.357 2.076   49.955  1.00 9.98  ? 203 LEU B CD2 1 
ATOM   3769 N  N   . LEU B 1 203 ? -22.042 7.357   48.340  1.00 9.74  ? 204 LEU B N   1 
ATOM   3770 C  CA  . LEU B 1 203 ? -22.808 8.447   47.796  1.00 9.94  ? 204 LEU B CA  1 
ATOM   3771 C  C   . LEU B 1 203 ? -23.447 8.013   46.491  1.00 9.84  ? 204 LEU B C   1 
ATOM   3772 O  O   . LEU B 1 203 ? -22.821 7.319   45.656  1.00 9.37  ? 204 LEU B O   1 
ATOM   3773 C  CB  . LEU B 1 203 ? -21.898 9.648   47.554  1.00 12.86 ? 204 LEU B CB  1 
ATOM   3774 C  CG  . LEU B 1 203 ? -21.249 10.193  48.853  1.00 13.05 ? 204 LEU B CG  1 
ATOM   3775 C  CD1 . LEU B 1 203 ? -20.140 11.209  48.519  1.00 16.70 ? 204 LEU B CD1 1 
ATOM   3776 C  CD2 . LEU B 1 203 ? -22.365 10.859  49.741  1.00 18.35 ? 204 LEU B CD2 1 
ATOM   3777 N  N   . GLU B 1 204 ? -24.681 8.489   46.256  1.00 9.85  ? 205 GLU B N   1 
ATOM   3778 C  CA  . GLU B 1 204 ? -25.481 8.145   45.113  1.00 9.03  ? 205 GLU B CA  1 
ATOM   3779 C  C   . GLU B 1 204 ? -25.186 9.124   43.988  1.00 10.07 ? 205 GLU B C   1 
ATOM   3780 O  O   . GLU B 1 204 ? -26.082 9.898   43.567  1.00 11.61 ? 205 GLU B O   1 
ATOM   3781 C  CB  . GLU B 1 204 ? -26.929 8.047   45.527  1.00 11.09 ? 205 GLU B CB  1 
ATOM   3782 C  CG  . GLU B 1 204 ? -27.096 6.814   46.447  1.00 12.19 ? 205 GLU B CG  1 
ATOM   3783 C  CD  . GLU B 1 204 ? -28.498 6.507   46.896  1.00 13.76 ? 205 GLU B CD  1 
ATOM   3784 O  OE1 . GLU B 1 204 ? -29.334 7.462   46.960  1.00 15.64 ? 205 GLU B OE1 1 
ATOM   3785 O  OE2 . GLU B 1 204 ? -28.815 5.316   47.217  1.00 12.68 ? 205 GLU B OE2 1 
ATOM   3786 N  N   . CYS B 1 205 ? -24.022 8.999   43.410  1.00 9.63  ? 206 CYS B N   1 
ATOM   3787 C  CA  . CYS B 1 205 ? -23.508 9.974   42.463  1.00 8.64  ? 206 CYS B CA  1 
ATOM   3788 C  C   . CYS B 1 205 ? -22.969 9.413   41.194  1.00 8.25  ? 206 CYS B C   1 
ATOM   3789 O  O   . CYS B 1 205 ? -22.285 10.092  40.437  1.00 9.72  ? 206 CYS B O   1 
ATOM   3790 C  CB  . CYS B 1 205 ? -22.419 10.817  43.158  1.00 10.12 ? 206 CYS B CB  1 
ATOM   3791 S  SG  . CYS B 1 205 ? -20.966 9.894   43.709  1.00 10.74 ? 206 CYS B SG  1 
ATOM   3792 N  N   . VAL B 1 206 ? -23.181 8.108   40.972  1.00 8.88  ? 207 VAL B N   1 
ATOM   3793 C  CA  . VAL B 1 206 ? -22.430 7.362   39.939  1.00 7.84  ? 207 VAL B CA  1 
ATOM   3794 C  C   . VAL B 1 206 ? -23.368 6.938   38.802  1.00 8.36  ? 207 VAL B C   1 
ATOM   3795 O  O   . VAL B 1 206 ? -24.406 6.304   39.034  1.00 10.12 ? 207 VAL B O   1 
ATOM   3796 C  CB  . VAL B 1 206 ? -21.757 6.088   40.489  1.00 7.71  ? 207 VAL B CB  1 
ATOM   3797 C  CG1 . VAL B 1 206 ? -21.008 5.360   39.315  1.00 9.29  ? 207 VAL B CG1 1 
ATOM   3798 C  CG2 . VAL B 1 206 ? -20.777 6.505   41.598  1.00 9.43  ? 207 VAL B CG2 1 
ATOM   3799 N  N   . THR B 1 207 ? -22.999 7.231   37.545  1.00 8.25  ? 208 THR B N   1 
ATOM   3800 C  CA  . THR B 1 207 ? -23.546 6.478   36.397  1.00 8.32  ? 208 THR B CA  1 
ATOM   3801 C  C   . THR B 1 207 ? -22.547 5.338   36.114  1.00 8.38  ? 208 THR B C   1 
ATOM   3802 O  O   . THR B 1 207 ? -21.376 5.566   35.834  1.00 8.47  ? 208 THR B O   1 
ATOM   3803 C  CB  . THR B 1 207 ? -23.591 7.368   35.116  1.00 8.70  ? 208 THR B CB  1 
ATOM   3804 O  OG1 . THR B 1 207 ? -24.435 8.476   35.359  1.00 9.66  ? 208 THR B OG1 1 
ATOM   3805 C  CG2 . THR B 1 207 ? -24.179 6.520   33.964  1.00 10.49 ? 208 THR B CG2 1 
ATOM   3806 N  N   . TRP B 1 208 ? -23.074 4.122   36.337  1.00 8.00  ? 209 TRP B N   1 
ATOM   3807 C  CA  . TRP B 1 208 ? -22.276 2.919   36.142  1.00 7.47  ? 209 TRP B CA  1 
ATOM   3808 C  C   . TRP B 1 208 ? -22.304 2.473   34.664  1.00 7.09  ? 209 TRP B C   1 
ATOM   3809 O  O   . TRP B 1 208 ? -23.372 2.429   34.047  1.00 8.11  ? 209 TRP B O   1 
ATOM   3810 C  CB  . TRP B 1 208 ? -22.790 1.740   37.041  1.00 8.10  ? 209 TRP B CB  1 
ATOM   3811 C  CG  . TRP B 1 208 ? -22.217 1.854   38.404  1.00 7.82  ? 209 TRP B CG  1 
ATOM   3812 C  CD1 . TRP B 1 208 ? -22.793 2.459   39.529  1.00 7.48  ? 209 TRP B CD1 1 
ATOM   3813 C  CD2 . TRP B 1 208 ? -20.900 1.464   38.799  1.00 7.21  ? 209 TRP B CD2 1 
ATOM   3814 N  NE1 . TRP B 1 208 ? -21.911 2.477   40.556  1.00 8.88  ? 209 TRP B NE1 1 
ATOM   3815 C  CE2 . TRP B 1 208 ? -20.748 1.856   40.192  1.00 7.40  ? 209 TRP B CE2 1 
ATOM   3816 C  CE3 . TRP B 1 208 ? -19.833 0.864   38.143  1.00 7.01  ? 209 TRP B CE3 1 
ATOM   3817 C  CZ2 . TRP B 1 208 ? -19.549 1.632   40.871  1.00 8.45  ? 209 TRP B CZ2 1 
ATOM   3818 C  CZ3 . TRP B 1 208 ? -18.683 0.599   38.839  1.00 8.84  ? 209 TRP B CZ3 1 
ATOM   3819 C  CH2 . TRP B 1 208 ? -18.543 0.958   40.193  1.00 8.31  ? 209 TRP B CH2 1 
ATOM   3820 N  N   . ILE B 1 209 ? -21.144 2.170   34.141  1.00 7.39  ? 210 ILE B N   1 
ATOM   3821 C  CA  . ILE B 1 209 ? -21.051 1.617   32.757  1.00 7.79  ? 210 ILE B CA  1 
ATOM   3822 C  C   . ILE B 1 209 ? -20.201 0.369   32.935  1.00 7.37  ? 210 ILE B C   1 
ATOM   3823 O  O   . ILE B 1 209 ? -19.030 0.454   33.255  1.00 8.56  ? 210 ILE B O   1 
ATOM   3824 C  CB  . ILE B 1 209 ? -20.344 2.655   31.845  1.00 8.74  ? 210 ILE B CB  1 
ATOM   3825 C  CG1 . ILE B 1 209 ? -21.226 3.920   31.794  1.00 10.53 ? 210 ILE B CG1 1 
ATOM   3826 C  CG2 . ILE B 1 209 ? -20.152 2.058   30.400  1.00 10.53 ? 210 ILE B CG2 1 
ATOM   3827 C  CD1 . ILE B 1 209 ? -20.563 5.102   31.124  1.00 12.86 ? 210 ILE B CD1 1 
ATOM   3828 N  N   . VAL B 1 210 ? -20.816 -0.801  32.789  1.00 7.55  ? 211 VAL B N   1 
ATOM   3829 C  CA  . VAL B 1 210 ? -20.146 -2.092  33.034  1.00 8.51  ? 211 VAL B CA  1 
ATOM   3830 C  C   . VAL B 1 210 ? -19.927 -2.808  31.697  1.00 7.07  ? 211 VAL B C   1 
ATOM   3831 O  O   . VAL B 1 210 ? -20.956 -3.080  31.033  1.00 8.85  ? 211 VAL B O   1 
ATOM   3832 C  CB  . VAL B 1 210 ? -20.962 -2.965  34.040  1.00 8.20  ? 211 VAL B CB  1 
ATOM   3833 C  CG1 . VAL B 1 210 ? -20.287 -4.336  34.240  1.00 8.60  ? 211 VAL B CG1 1 
ATOM   3834 C  CG2 . VAL B 1 210 ? -21.092 -2.183  35.370  1.00 8.96  ? 211 VAL B CG2 1 
ATOM   3835 N  N   . LEU B 1 211 ? -18.720 -3.063  31.300  1.00 8.61  ? 212 LEU B N   1 
ATOM   3836 C  CA  . LEU B 1 211 ? -18.481 -3.741  30.037  1.00 8.47  ? 212 LEU B CA  1 
ATOM   3837 C  C   . LEU B 1 211 ? -18.882 -5.204  30.106  1.00 8.70  ? 212 LEU B C   1 
ATOM   3838 O  O   . LEU B 1 211 ? -18.645 -5.911  31.069  1.00 9.70  ? 212 LEU B O   1 
ATOM   3839 C  CB  . LEU B 1 211 ? -17.010 -3.602  29.612  1.00 9.41  ? 212 LEU B CB  1 
ATOM   3840 C  CG  . LEU B 1 211 ? -16.525 -2.152  29.397  1.00 9.86  ? 212 LEU B CG  1 
ATOM   3841 C  CD1 . LEU B 1 211 ? -15.090 -2.166  28.782  1.00 13.31 ? 212 LEU B CD1 1 
ATOM   3842 C  CD2 . LEU B 1 211 ? -17.469 -1.310  28.599  1.00 11.90 ? 212 LEU B CD2 1 
ATOM   3843 N  N   A LYS B 1 212 ? -19.486 -5.609  28.984  0.50 9.46  ? 213 LYS B N   1 
ATOM   3844 N  N   B LYS B 1 212 ? -19.438 -5.722  29.019  0.50 8.94  ? 213 LYS B N   1 
ATOM   3845 C  CA  A LYS B 1 212 ? -19.857 -6.999  28.757  0.50 9.84  ? 213 LYS B CA  1 
ATOM   3846 C  CA  B LYS B 1 212 ? -19.785 -7.149  29.010  0.50 8.97  ? 213 LYS B CA  1 
ATOM   3847 C  C   A LYS B 1 212 ? -18.726 -7.975  28.733  0.50 9.28  ? 213 LYS B C   1 
ATOM   3848 C  C   B LYS B 1 212 ? -18.563 -8.057  28.853  0.50 9.19  ? 213 LYS B C   1 
ATOM   3849 O  O   A LYS B 1 212 ? -18.933 -9.081  29.252  0.50 10.41 ? 213 LYS B O   1 
ATOM   3850 O  O   B LYS B 1 212 ? -18.459 -9.155  29.425  0.50 10.37 ? 213 LYS B O   1 
ATOM   3851 C  CB  A LYS B 1 212 ? -20.636 -7.147  27.433  0.50 12.08 ? 213 LYS B CB  1 
ATOM   3852 C  CB  B LYS B 1 212 ? -20.863 -7.392  27.925  0.50 9.93  ? 213 LYS B CB  1 
ATOM   3853 C  CG  A LYS B 1 212 ? -20.934 -8.579  26.934  0.50 16.99 ? 213 LYS B CG  1 
ATOM   3854 C  CG  B LYS B 1 212 ? -21.178 -8.857  27.588  0.50 11.53 ? 213 LYS B CG  1 
ATOM   3855 C  CD  A LYS B 1 212 ? -21.461 -8.517  25.481  0.50 22.03 ? 213 LYS B CD  1 
ATOM   3856 C  CD  B LYS B 1 212 ? -22.299 -8.971  26.560  0.50 13.88 ? 213 LYS B CD  1 
ATOM   3857 C  CE  A LYS B 1 212 ? -20.427 -8.230  24.380  0.50 19.98 ? 213 LYS B CE  1 
ATOM   3858 C  CE  B LYS B 1 212 ? -22.631 -10.398 26.150  0.50 20.59 ? 213 LYS B CE  1 
ATOM   3859 N  NZ  A LYS B 1 212 ? -19.037 -7.799  24.777  0.50 11.85 ? 213 LYS B NZ  1 
ATOM   3860 N  NZ  B LYS B 1 212 ? -23.196 -10.439 24.769  0.50 28.80 ? 213 LYS B NZ  1 
ATOM   3861 N  N   . GLU B 1 213 ? -17.626 -7.673  28.010  1.00 9.03  ? 214 GLU B N   1 
ATOM   3862 C  CA  . GLU B 1 213 ? -16.515 -8.546  27.772  1.00 10.00 ? 214 GLU B CA  1 
ATOM   3863 C  C   . GLU B 1 213 ? -15.493 -8.418  28.904  1.00 9.17  ? 214 GLU B C   1 
ATOM   3864 O  O   . GLU B 1 213 ? -14.969 -7.301  29.131  1.00 9.64  ? 214 GLU B O   1 
ATOM   3865 C  CB  . GLU B 1 213 ? -15.845 -8.128  26.454  1.00 11.14 ? 214 GLU B CB  1 
ATOM   3866 C  CG  . GLU B 1 213 ? -14.717 -9.070  26.057  1.00 13.72 ? 214 GLU B CG  1 
ATOM   3867 C  CD  . GLU B 1 213 ? -13.989 -8.601  24.794  1.00 13.08 ? 214 GLU B CD  1 
ATOM   3868 O  OE1 . GLU B 1 213 ? -14.649 -7.993  23.921  1.00 16.28 ? 214 GLU B OE1 1 
ATOM   3869 O  OE2 . GLU B 1 213 ? -12.780 -8.842  24.722  1.00 25.12 ? 214 GLU B OE2 1 
ATOM   3870 N  N   . PRO B 1 214 ? -15.188 -9.529  29.618  1.00 8.57  ? 215 PRO B N   1 
ATOM   3871 C  CA  . PRO B 1 214 ? -14.140 -9.486  30.624  1.00 8.77  ? 215 PRO B CA  1 
ATOM   3872 C  C   . PRO B 1 214 ? -12.766 -9.432  30.013  1.00 9.78  ? 215 PRO B C   1 
ATOM   3873 O  O   . PRO B 1 214 ? -12.598 -9.797  28.820  1.00 11.55 ? 215 PRO B O   1 
ATOM   3874 C  CB  . PRO B 1 214 ? -14.273 -10.798 31.367  1.00 11.31 ? 215 PRO B CB  1 
ATOM   3875 C  CG  . PRO B 1 214 ? -14.793 -11.717 30.307  1.00 14.77 ? 215 PRO B CG  1 
ATOM   3876 C  CD  . PRO B 1 214 ? -15.722 -10.889 29.456  1.00 10.88 ? 215 PRO B CD  1 
ATOM   3877 N  N   . ILE B 1 215 ? -11.778 -8.981  30.757  1.00 8.96  ? 216 ILE B N   1 
ATOM   3878 C  CA  . ILE B 1 215 ? -10.369 -9.246  30.373  1.00 9.26  ? 216 ILE B CA  1 
ATOM   3879 C  C   . ILE B 1 215 ? -9.897  -10.488 31.105  1.00 10.48 ? 216 ILE B C   1 
ATOM   3880 O  O   . ILE B 1 215 ? -10.432 -10.842 32.191  1.00 10.24 ? 216 ILE B O   1 
ATOM   3881 C  CB  . ILE B 1 215 ? -9.428  -8.045  30.663  1.00 10.39 ? 216 ILE B CB  1 
ATOM   3882 C  CG1 . ILE B 1 215 ? -9.457  -7.689  32.144  1.00 10.56 ? 216 ILE B CG1 1 
ATOM   3883 C  CG2 . ILE B 1 215 ? -9.826  -6.840  29.764  1.00 11.32 ? 216 ILE B CG2 1 
ATOM   3884 C  CD1 . ILE B 1 215 ? -8.297  -6.706  32.509  1.00 11.63 ? 216 ILE B CD1 1 
ATOM   3885 N  N   . SER B 1 216 ? -8.922  -11.158 30.547  0.50 4.93  ? 217 SER B N   1 
ATOM   3886 C  CA  . SER B 1 216 ? -8.283  -12.294 31.203  0.50 4.75  ? 217 SER B CA  1 
ATOM   3887 C  C   . SER B 1 216 ? -7.023  -11.843 31.850  0.50 4.54  ? 217 SER B C   1 
ATOM   3888 O  O   . SER B 1 216 ? -6.248  -11.111 31.220  0.50 4.80  ? 217 SER B O   1 
ATOM   3889 C  CB  . SER B 1 216 ? -7.956  -13.363 30.171  0.50 6.69  ? 217 SER B CB  1 
ATOM   3890 O  OG  . SER B 1 216 ? -9.086  -13.971 29.723  0.50 11.16 ? 217 SER B OG  1 
ATOM   3891 N  N   . VAL B 1 217 ? -6.765  -12.288 33.093  1.00 9.29  ? 218 VAL B N   1 
ATOM   3892 C  CA  . VAL B 1 217 ? -5.528  -12.069 33.795  1.00 9.69  ? 218 VAL B CA  1 
ATOM   3893 C  C   . VAL B 1 217 ? -5.020  -13.455 34.207  1.00 9.54  ? 218 VAL B C   1 
ATOM   3894 O  O   . VAL B 1 217 ? -5.847  -14.398 34.319  1.00 9.64  ? 218 VAL B O   1 
ATOM   3895 C  CB  . VAL B 1 217 ? -5.678  -11.123 35.003  1.00 10.02 ? 218 VAL B CB  1 
ATOM   3896 C  CG1 . VAL B 1 217 ? -6.262  -9.754  34.567  1.00 11.46 ? 218 VAL B CG1 1 
ATOM   3897 C  CG2 . VAL B 1 217 ? -6.574  -11.740 36.080  1.00 11.46 ? 218 VAL B CG2 1 
ATOM   3898 N  N   . SER B 1 218 ? -3.737  -13.615 34.475  1.00 9.73  ? 219 SER B N   1 
ATOM   3899 C  CA  . SER B 1 218 ? -3.289  -14.945 34.875  1.00 10.99 ? 219 SER B CA  1 
ATOM   3900 C  C   . SER B 1 218 ? -3.486  -15.187 36.350  1.00 10.10 ? 219 SER B C   1 
ATOM   3901 O  O   . SER B 1 218 ? -3.584  -14.272 37.193  1.00 10.04 ? 219 SER B O   1 
ATOM   3902 C  CB  . SER B 1 218 ? -1.810  -15.129 34.484  1.00 10.74 ? 219 SER B CB  1 
ATOM   3903 O  OG  . SER B 1 218 ? -1.016  -14.220 35.233  1.00 12.59 ? 219 SER B OG  1 
ATOM   3904 N  N   A SER B 1 219 ? -3.475  -16.473 36.679  0.50 11.01 ? 220 SER B N   1 
ATOM   3905 N  N   B SER B 1 219 ? -3.397  -16.444 36.771  0.50 10.50 ? 220 SER B N   1 
ATOM   3906 C  CA  A SER B 1 219 ? -3.476  -16.907 38.030  0.50 11.17 ? 220 SER B CA  1 
ATOM   3907 C  CA  B SER B 1 219 ? -3.521  -16.786 38.167  0.50 11.34 ? 220 SER B CA  1 
ATOM   3908 C  C   A SER B 1 219 ? -2.430  -16.163 38.818  0.50 10.41 ? 220 SER B C   1 
ATOM   3909 C  C   B SER B 1 219 ? -2.335  -16.180 38.926  0.50 11.03 ? 220 SER B C   1 
ATOM   3910 O  O   A SER B 1 219 ? -2.767  -15.639 39.907  0.50 11.70 ? 220 SER B O   1 
ATOM   3911 O  O   B SER B 1 219 ? -2.426  -15.760 40.080  0.50 10.79 ? 220 SER B O   1 
ATOM   3912 C  CB  A SER B 1 219 ? -3.350  -18.457 38.107  0.50 12.56 ? 220 SER B CB  1 
ATOM   3913 C  CB  B SER B 1 219 ? -3.650  -18.326 38.272  0.50 13.71 ? 220 SER B CB  1 
ATOM   3914 O  OG  A SER B 1 219 ? -2.148  -18.973 37.548  0.50 11.98 ? 220 SER B OG  1 
ATOM   3915 O  OG  B SER B 1 219 ? -3.576  -18.760 39.596  0.50 16.08 ? 220 SER B OG  1 
ATOM   3916 N  N   . GLU B 1 220 ? -1.193  -16.079 38.281  1.00 10.74 ? 221 GLU B N   1 
ATOM   3917 C  CA  . GLU B 1 220 ? -0.053  -15.438 38.950  1.00 13.14 ? 221 GLU B CA  1 
ATOM   3918 C  C   . GLU B 1 220 ? -0.318  -13.943 39.203  1.00 11.00 ? 221 GLU B C   1 
ATOM   3919 O  O   . GLU B 1 220 ? 0.111   -13.382 40.246  1.00 12.65 ? 221 GLU B O   1 
ATOM   3920 C  CB  . GLU B 1 220 ? 1.260   -15.590 38.208  1.00 14.86 ? 221 GLU B CB  1 
ATOM   3921 C  CG  . GLU B 1 220 ? 1.730   -17.057 38.126  1.00 18.47 ? 221 GLU B CG  1 
ATOM   3922 C  CD  . GLU B 1 220 ? 1.085   -17.861 37.031  1.00 20.14 ? 221 GLU B CD  1 
ATOM   3923 O  OE1 . GLU B 1 220 ? 0.267   -17.423 36.187  1.00 18.88 ? 221 GLU B OE1 1 
ATOM   3924 O  OE2 . GLU B 1 220 ? 1.548   -19.039 36.889  1.00 33.04 ? 221 GLU B OE2 1 
ATOM   3925 N  N   . GLN B 1 221 ? -0.935  -13.259 38.229  1.00 10.23 ? 222 GLN B N   1 
ATOM   3926 C  CA  . GLN B 1 221 ? -1.217  -11.840 38.398  1.00 10.16 ? 222 GLN B CA  1 
ATOM   3927 C  C   . GLN B 1 221 ? -2.173  -11.628 39.615  1.00 9.69  ? 222 GLN B C   1 
ATOM   3928 O  O   . GLN B 1 221 ? -1.967  -10.759 40.470  1.00 11.20 ? 222 GLN B O   1 
ATOM   3929 C  CB  . GLN B 1 221 ? -1.788  -11.272 37.115  1.00 10.38 ? 222 GLN B CB  1 
ATOM   3930 C  CG  . GLN B 1 221 ? -0.698  -11.144 36.042  1.00 10.93 ? 222 GLN B CG  1 
ATOM   3931 C  CD  . GLN B 1 221 ? -1.169  -10.595 34.721  1.00 10.19 ? 222 GLN B CD  1 
ATOM   3932 O  OE1 . GLN B 1 221 ? -2.249  -10.963 34.234  1.00 10.14 ? 222 GLN B OE1 1 
ATOM   3933 N  NE2 . GLN B 1 221 ? -0.360  -9.686  34.138  1.00 9.79  ? 222 GLN B NE2 1 
ATOM   3934 N  N   . VAL B 1 222 ? -3.262  -12.385 39.656  1.00 10.84 ? 223 VAL B N   1 
ATOM   3935 C  CA  . VAL B 1 222 ? -4.257  -12.198 40.754  1.00 11.15 ? 223 VAL B CA  1 
ATOM   3936 C  C   . VAL B 1 222 ? -3.662  -12.674 42.105  1.00 11.66 ? 223 VAL B C   1 
ATOM   3937 O  O   . VAL B 1 222 ? -3.957  -12.083 43.172  1.00 11.45 ? 223 VAL B O   1 
ATOM   3938 C  CB  . VAL B 1 222 ? -5.661  -12.747 40.422  1.00 14.51 ? 223 VAL B CB  1 
ATOM   3939 C  CG1 . VAL B 1 222 ? -5.630  -14.261 40.369  1.00 16.10 ? 223 VAL B CG1 1 
ATOM   3940 C  CG2 . VAL B 1 222 ? -6.722  -12.223 41.413  1.00 15.45 ? 223 VAL B CG2 1 
ATOM   3941 N  N   . LEU B 1 223 ? -2.808  -13.697 42.070  1.00 12.36 ? 224 LEU B N   1 
ATOM   3942 C  CA  . LEU B 1 223 ? -2.158  -14.125 43.332  1.00 13.48 ? 224 LEU B CA  1 
ATOM   3943 C  C   . LEU B 1 223 ? -1.343  -12.966 43.903  1.00 13.91 ? 224 LEU B C   1 
ATOM   3944 O  O   . LEU B 1 223 ? -1.280  -12.836 45.143  1.00 13.53 ? 224 LEU B O   1 
ATOM   3945 C  CB  . LEU B 1 223 ? -1.258  -15.348 43.082  1.00 17.57 ? 224 LEU B CB  1 
ATOM   3946 C  CG  . LEU B 1 223 ? -2.097  -16.651 42.991  1.00 19.10 ? 224 LEU B CG  1 
ATOM   3947 C  CD1 . LEU B 1 223 ? -1.283  -17.824 42.385  1.00 22.86 ? 224 LEU B CD1 1 
ATOM   3948 C  CD2 . LEU B 1 223 ? -2.635  -17.131 44.358  1.00 22.05 ? 224 LEU B CD2 1 
ATOM   3949 N  N   . LYS B 1 224 ? -0.736  -12.100 43.068  1.00 12.06 ? 225 LYS B N   1 
ATOM   3950 C  CA  . LYS B 1 224 ? 0.022   -10.950 43.604  1.00 13.81 ? 225 LYS B CA  1 
ATOM   3951 C  C   . LYS B 1 224 ? -0.877  -9.902  44.217  1.00 11.86 ? 225 LYS B C   1 
ATOM   3952 O  O   . LYS B 1 224 ? -0.558  -9.318  45.239  1.00 12.74 ? 225 LYS B O   1 
ATOM   3953 C  CB  . LYS B 1 224 ? 0.943   -10.443 42.488  1.00 16.23 ? 225 LYS B CB  1 
ATOM   3954 C  CG  . LYS B 1 224 ? 2.133   -11.479 42.377  1.00 19.64 ? 225 LYS B CG  1 
ATOM   3955 C  CD  . LYS B 1 224 ? 3.136   -11.239 41.283  1.00 24.95 ? 225 LYS B CD  1 
ATOM   3956 C  CE  . LYS B 1 224 ? 4.253   -12.315 41.217  1.00 26.40 ? 225 LYS B CE  1 
ATOM   3957 N  NZ  . LYS B 1 224 ? 5.110   -12.014 40.020  1.00 29.11 ? 225 LYS B NZ  1 
ATOM   3958 N  N   . PHE B 1 225 ? -2.090  -9.692  43.677  1.00 10.82 ? 226 PHE B N   1 
ATOM   3959 C  CA  . PHE B 1 225 ? -3.078  -8.802  44.345  1.00 10.94 ? 226 PHE B CA  1 
ATOM   3960 C  C   . PHE B 1 225 ? -3.379  -9.348  45.766  1.00 10.39 ? 226 PHE B C   1 
ATOM   3961 O  O   . PHE B 1 225 ? -3.480  -8.563  46.714  1.00 11.03 ? 226 PHE B O   1 
ATOM   3962 C  CB  . PHE B 1 225 ? -4.470  -8.814  43.663  1.00 10.03 ? 226 PHE B CB  1 
ATOM   3963 C  CG  . PHE B 1 225 ? -4.566  -8.054  42.347  1.00 10.81 ? 226 PHE B CG  1 
ATOM   3964 C  CD1 . PHE B 1 225 ? -3.450  -7.670  41.582  1.00 13.94 ? 226 PHE B CD1 1 
ATOM   3965 C  CD2 . PHE B 1 225 ? -5.824  -7.741  41.837  1.00 15.14 ? 226 PHE B CD2 1 
ATOM   3966 C  CE1 . PHE B 1 225 ? -3.617  -7.001  40.385  1.00 14.20 ? 226 PHE B CE1 1 
ATOM   3967 C  CE2 . PHE B 1 225 ? -5.986  -7.064  40.632  1.00 15.56 ? 226 PHE B CE2 1 
ATOM   3968 C  CZ  . PHE B 1 225 ? -4.879  -6.701  39.895  1.00 15.75 ? 226 PHE B CZ  1 
ATOM   3969 N  N   . ARG B 1 226 ? -3.471  -10.684 45.922  1.00 10.52 ? 227 ARG B N   1 
ATOM   3970 C  CA  . ARG B 1 226 ? -3.822  -11.293 47.202  1.00 10.45 ? 227 ARG B CA  1 
ATOM   3971 C  C   . ARG B 1 226 ? -2.683  -11.297 48.273  1.00 12.14 ? 227 ARG B C   1 
ATOM   3972 O  O   . ARG B 1 226 ? -2.893  -11.680 49.404  1.00 13.28 ? 227 ARG B O   1 
ATOM   3973 C  CB  . ARG B 1 226 ? -4.292  -12.738 46.940  1.00 11.84 ? 227 ARG B CB  1 
ATOM   3974 C  CG  . ARG B 1 226 ? -5.553  -12.852 46.077  1.00 11.16 ? 227 ARG B CG  1 
ATOM   3975 C  CD  . ARG B 1 226 ? -5.994  -14.305 45.996  1.00 13.80 ? 227 ARG B CD  1 
ATOM   3976 N  NE  . ARG B 1 226 ? -7.105  -14.436 45.055  1.00 12.76 ? 227 ARG B NE  1 
ATOM   3977 C  CZ  . ARG B 1 226 ? -7.154  -15.309 44.048  1.00 11.99 ? 227 ARG B CZ  1 
ATOM   3978 N  NH1 . ARG B 1 226 ? -6.163  -16.229 43.878  1.00 15.48 ? 227 ARG B NH1 1 
ATOM   3979 N  NH2 . ARG B 1 226 ? -8.153  -15.255 43.215  1.00 13.04 ? 227 ARG B NH2 1 
ATOM   3980 N  N   . LYS B 1 227 ? -1.496  -10.859 47.904  1.00 12.05 ? 228 LYS B N   1 
ATOM   3981 C  CA  . LYS B 1 227 ? -0.354  -10.674 48.841  1.00 13.42 ? 228 LYS B CA  1 
ATOM   3982 C  C   . LYS B 1 227 ? -0.369  -9.305  49.486  1.00 11.88 ? 228 LYS B C   1 
ATOM   3983 O  O   . LYS B 1 227 ? 0.413   -9.073  50.415  1.00 13.43 ? 228 LYS B O   1 
ATOM   3984 C  CB  . LYS B 1 227 ? 0.998   -10.888 48.088  1.00 14.81 ? 228 LYS B CB  1 
ATOM   3985 C  CG  . LYS B 1 227 ? 1.186   -12.340 47.643  1.00 18.33 ? 228 LYS B CG  1 
ATOM   3986 C  CD  . LYS B 1 227 ? 2.572   -12.531 47.032  1.00 28.74 ? 228 LYS B CD  1 
ATOM   3987 C  CE  . LYS B 1 227 ? 3.624   -12.870 48.123  1.00 39.16 ? 228 LYS B CE  1 
ATOM   3988 N  NZ  . LYS B 1 227 ? 5.059   -12.710 47.728  1.00 47.86 ? 228 LYS B NZ  1 
ATOM   3989 N  N   . LEU B 1 228 ? -1.170  -8.366  48.985  1.00 11.30 ? 229 LEU B N   1 
ATOM   3990 C  CA  . LEU B 1 228 ? -1.257  -7.056  49.613  1.00 10.84 ? 229 LEU B CA  1 
ATOM   3991 C  C   . LEU B 1 228 ? -1.905  -7.266  51.026  1.00 10.27 ? 229 LEU B C   1 
ATOM   3992 O  O   . LEU B 1 228 ? -2.532  -8.301  51.338  1.00 11.89 ? 229 LEU B O   1 
ATOM   3993 C  CB  . LEU B 1 228 ? -2.120  -6.108  48.781  1.00 10.63 ? 229 LEU B CB  1 
ATOM   3994 C  CG  . LEU B 1 228 ? -1.504  -5.677  47.478  1.00 11.88 ? 229 LEU B CG  1 
ATOM   3995 C  CD1 . LEU B 1 228 ? -2.590  -5.050  46.615  1.00 12.24 ? 229 LEU B CD1 1 
ATOM   3996 C  CD2 . LEU B 1 228 ? -0.427  -4.591  47.738  1.00 14.95 ? 229 LEU B CD2 1 
ATOM   3997 N  N   . ASN B 1 229 ? -1.821  -6.192  51.813  1.00 11.73 ? 230 ASN B N   1 
ATOM   3998 C  CA  . ASN B 1 229 ? -2.289  -6.216  53.185  1.00 11.09 ? 230 ASN B CA  1 
ATOM   3999 C  C   . ASN B 1 229 ? -3.252  -5.013  53.405  1.00 11.91 ? 230 ASN B C   1 
ATOM   4000 O  O   . ASN B 1 229 ? -2.991  -3.905  52.914  1.00 12.86 ? 230 ASN B O   1 
ATOM   4001 C  CB  . ASN B 1 229 ? -1.134  -6.035  54.228  1.00 12.18 ? 230 ASN B CB  1 
ATOM   4002 C  CG  . ASN B 1 229 ? -0.259  -7.241  54.469  1.00 15.94 ? 230 ASN B CG  1 
ATOM   4003 O  OD1 . ASN B 1 229 ? 0.639   -7.104  55.321  1.00 19.50 ? 230 ASN B OD1 1 
ATOM   4004 N  ND2 . ASN B 1 229 ? -0.399  -8.334  53.761  1.00 14.51 ? 230 ASN B ND2 1 
ATOM   4005 N  N   . PHE B 1 230 ? -4.314  -5.309  54.180  1.00 11.45 ? 231 PHE B N   1 
ATOM   4006 C  CA  . PHE B 1 230 ? -5.200  -4.247  54.667  1.00 12.27 ? 231 PHE B CA  1 
ATOM   4007 C  C   . PHE B 1 230 ? -4.560  -3.431  55.777  1.00 14.44 ? 231 PHE B C   1 
ATOM   4008 O  O   . PHE B 1 230 ? -4.844  -2.181  55.864  1.00 14.15 ? 231 PHE B O   1 
ATOM   4009 C  CB  . PHE B 1 230 ? -6.482  -4.839  55.292  1.00 13.77 ? 231 PHE B CB  1 
ATOM   4010 C  CG  . PHE B 1 230 ? -7.523  -5.410  54.304  1.00 12.66 ? 231 PHE B CG  1 
ATOM   4011 C  CD1 . PHE B 1 230 ? -8.077  -4.642  53.256  1.00 13.12 ? 231 PHE B CD1 1 
ATOM   4012 C  CD2 . PHE B 1 230 ? -8.028  -6.653  54.523  1.00 14.30 ? 231 PHE B CD2 1 
ATOM   4013 C  CE1 . PHE B 1 230 ? -9.077  -5.152  52.446  1.00 11.97 ? 231 PHE B CE1 1 
ATOM   4014 C  CE2 . PHE B 1 230 ? -9.055  -7.226  53.687  1.00 12.69 ? 231 PHE B CE2 1 
ATOM   4015 C  CZ  . PHE B 1 230 ? -9.586  -6.430  52.655  1.00 11.73 ? 231 PHE B CZ  1 
ATOM   4016 N  N   . ASN B 1 231 ? -3.734  -4.119  56.579  1.00 13.23 ? 232 ASN B N   1 
ATOM   4017 C  CA  . ASN B 1 231 ? -3.107  -3.479  57.785  1.00 14.76 ? 232 ASN B CA  1 
ATOM   4018 C  C   . ASN B 1 231 ? -1.956  -2.610  57.368  1.00 14.89 ? 232 ASN B C   1 
ATOM   4019 O  O   . ASN B 1 231 ? -1.390  -2.714  56.232  1.00 14.89 ? 232 ASN B O   1 
ATOM   4020 C  CB  . ASN B 1 231 ? -2.570  -4.569  58.683  1.00 18.07 ? 232 ASN B CB  1 
ATOM   4021 C  CG  . ASN B 1 231 ? -1.634  -5.472  57.925  1.00 15.36 ? 232 ASN B CG  1 
ATOM   4022 O  OD1 . ASN B 1 231 ? -2.123  -6.349  57.186  1.00 15.14 ? 232 ASN B OD1 1 
ATOM   4023 N  ND2 . ASN B 1 231 ? -0.303  -5.298  58.093  1.00 17.80 ? 232 ASN B ND2 1 
ATOM   4024 N  N   . GLY B 1 232 ? -1.630  -1.664  58.281  1.00 18.14 ? 233 GLY B N   1 
ATOM   4025 C  CA  . GLY B 1 232 ? -0.393  -0.875  58.158  1.00 18.54 ? 233 GLY B CA  1 
ATOM   4026 C  C   . GLY B 1 232 ? 0.830   -1.691  58.589  1.00 17.12 ? 233 GLY B C   1 
ATOM   4027 O  O   . GLY B 1 232 ? 0.703   -2.738  59.207  1.00 17.04 ? 233 GLY B O   1 
ATOM   4028 N  N   . GLU B 1 233 ? 2.021   -1.194  58.210  1.00 16.94 ? 234 GLU B N   1 
ATOM   4029 C  CA  . GLU B 1 233 ? 3.310   -1.796  58.597  1.00 16.64 ? 234 GLU B CA  1 
ATOM   4030 C  C   . GLU B 1 233 ? 3.383   -1.852  60.102  1.00 16.18 ? 234 GLU B C   1 
ATOM   4031 O  O   . GLU B 1 233 ? 3.015   -0.920  60.782  1.00 19.23 ? 234 GLU B O   1 
ATOM   4032 C  CB  . GLU B 1 233 ? 4.460   -0.974  57.998  1.00 17.62 ? 234 GLU B CB  1 
ATOM   4033 C  CG  . GLU B 1 233 ? 5.846   -1.533  58.206  1.00 19.03 ? 234 GLU B CG  1 
ATOM   4034 C  CD  . GLU B 1 233 ? 6.902   -0.611  57.659  1.00 24.65 ? 234 GLU B CD  1 
ATOM   4035 O  OE1 . GLU B 1 233 ? 6.583   0.515   57.188  1.00 27.61 ? 234 GLU B OE1 1 
ATOM   4036 O  OE2 . GLU B 1 233 ? 8.078   -0.980  57.849  1.00 29.39 ? 234 GLU B OE2 1 
ATOM   4037 N  N   . GLY B 1 234 ? 3.843   -2.998  60.607  1.00 19.37 ? 235 GLY B N   1 
ATOM   4038 C  CA  . GLY B 1 234 ? 3.908   -3.216  62.100  1.00 21.42 ? 235 GLY B CA  1 
ATOM   4039 C  C   . GLY B 1 234 ? 2.659   -3.621  62.807  1.00 25.41 ? 235 GLY B C   1 
ATOM   4040 O  O   . GLY B 1 234 ? 2.632   -3.724  64.058  1.00 24.71 ? 235 GLY B O   1 
ATOM   4041 N  N   . GLU B 1 235 ? 1.614   -3.872  62.041  1.00 23.66 ? 236 GLU B N   1 
ATOM   4042 C  CA  . GLU B 1 235 ? 0.347   -4.399  62.572  1.00 22.01 ? 236 GLU B CA  1 
ATOM   4043 C  C   . GLU B 1 235 ? 0.173   -5.844  62.114  1.00 25.42 ? 236 GLU B C   1 
ATOM   4044 O  O   . GLU B 1 235 ? 0.817   -6.275  61.116  1.00 23.28 ? 236 GLU B O   1 
ATOM   4045 C  CB  . GLU B 1 235 ? -0.826  -3.568  62.044  1.00 22.13 ? 236 GLU B CB  1 
ATOM   4046 C  CG  . GLU B 1 235 ? -0.750  -2.160  62.481  1.00 24.68 ? 236 GLU B CG  1 
ATOM   4047 C  CD  . GLU B 1 235 ? -1.737  -1.275  61.814  1.00 30.39 ? 236 GLU B CD  1 
ATOM   4048 O  OE1 . GLU B 1 235 ? -2.468  -1.731  60.882  1.00 29.55 ? 236 GLU B OE1 1 
ATOM   4049 O  OE2 . GLU B 1 235 ? -1.740  -0.114  62.234  1.00 34.94 ? 236 GLU B OE2 1 
ATOM   4050 N  N   . PRO B 1 236 ? -0.700  -6.580  62.798  1.00 20.08 ? 237 PRO B N   1 
ATOM   4051 C  CA  . PRO B 1 236 ? -0.985  -8.006  62.521  1.00 21.86 ? 237 PRO B CA  1 
ATOM   4052 C  C   . PRO B 1 236 ? -1.392  -8.128  61.026  1.00 17.83 ? 237 PRO B C   1 
ATOM   4053 O  O   . PRO B 1 236 ? -2.242  -7.336  60.556  1.00 20.31 ? 237 PRO B O   1 
ATOM   4054 C  CB  . PRO B 1 236 ? -2.179  -8.301  63.487  1.00 26.31 ? 237 PRO B CB  1 
ATOM   4055 C  CG  . PRO B 1 236 ? -1.976  -7.335  64.594  1.00 32.51 ? 237 PRO B CG  1 
ATOM   4056 C  CD  . PRO B 1 236 ? -1.367  -6.098  64.024  1.00 26.07 ? 237 PRO B CD  1 
ATOM   4057 N  N   . GLU B 1 237 ? -0.788  -9.086  60.321  1.00 20.08 ? 238 GLU B N   1 
ATOM   4058 C  CA  . GLU B 1 237 ? -1.102  -9.264  58.928  1.00 18.56 ? 238 GLU B CA  1 
ATOM   4059 C  C   . GLU B 1 237 ? -2.546  -9.696  58.662  1.00 16.11 ? 238 GLU B C   1 
ATOM   4060 O  O   . GLU B 1 237 ? -2.987  -10.687 59.125  1.00 16.47 ? 238 GLU B O   1 
ATOM   4061 C  CB  . GLU B 1 237 ? -0.177  -10.326 58.278  1.00 20.09 ? 238 GLU B CB  1 
ATOM   4062 C  CG  . GLU B 1 237 ? -0.272  -10.168 56.789  1.00 25.58 ? 238 GLU B CG  1 
ATOM   4063 C  CD  . GLU B 1 237 ? 0.613   -11.052 55.939  1.00 27.57 ? 238 GLU B CD  1 
ATOM   4064 O  OE1 . GLU B 1 237 ? 0.785   -12.241 56.329  1.00 34.99 ? 238 GLU B OE1 1 
ATOM   4065 O  OE2 . GLU B 1 237 ? 1.072   -10.565 54.853  1.00 24.03 ? 238 GLU B OE2 1 
ATOM   4066 N  N   . GLU B 1 238 ? -3.251  -8.930  57.808  1.00 15.33 ? 239 GLU B N   1 
ATOM   4067 C  CA  . GLU B 1 238 ? -4.540  -9.272  57.292  1.00 16.09 ? 239 GLU B CA  1 
ATOM   4068 C  C   . GLU B 1 238 ? -4.521  -9.140  55.765  1.00 14.30 ? 239 GLU B C   1 
ATOM   4069 O  O   . GLU B 1 238 ? -4.387  -8.028  55.243  1.00 16.69 ? 239 GLU B O   1 
ATOM   4070 C  CB  . GLU B 1 238 ? -5.557  -8.278  57.838  1.00 20.23 ? 239 GLU B CB  1 
ATOM   4071 C  CG  . GLU B 1 238 ? -5.970  -8.587  59.296  1.00 35.19 ? 239 GLU B CG  1 
ATOM   4072 C  CD  . GLU B 1 238 ? -6.937  -7.578  59.928  1.00 57.51 ? 239 GLU B CD  1 
ATOM   4073 O  OE1 . GLU B 1 238 ? -6.984  -6.372  59.498  1.00 51.85 ? 239 GLU B OE1 1 
ATOM   4074 O  OE2 . GLU B 1 238 ? -7.637  -8.022  60.893  1.00 70.96 ? 239 GLU B OE2 1 
ATOM   4075 N  N   . LEU B 1 239 ? -4.549  -10.283 55.044  1.00 13.62 ? 240 LEU B N   1 
ATOM   4076 C  CA  . LEU B 1 239 ? -4.425  -10.227 53.603  1.00 13.47 ? 240 LEU B CA  1 
ATOM   4077 C  C   . LEU B 1 239 ? -5.586  -9.362  53.029  1.00 10.16 ? 240 LEU B C   1 
ATOM   4078 O  O   . LEU B 1 239 ? -6.758  -9.530  53.385  1.00 11.98 ? 240 LEU B O   1 
ATOM   4079 C  CB  . LEU B 1 239 ? -4.510  -11.647 53.061  1.00 13.30 ? 240 LEU B CB  1 
ATOM   4080 C  CG  . LEU B 1 239 ? -3.303  -12.540 53.466  1.00 14.26 ? 240 LEU B CG  1 
ATOM   4081 C  CD1 . LEU B 1 239 ? -3.422  -13.923 52.811  1.00 19.41 ? 240 LEU B CD1 1 
ATOM   4082 C  CD2 . LEU B 1 239 ? -1.988  -11.890 53.103  1.00 15.86 ? 240 LEU B CD2 1 
ATOM   4083 N  N   . MET B 1 240 ? -5.225  -8.545  52.059  1.00 10.59 ? 241 MET B N   1 
ATOM   4084 C  CA  . MET B 1 240 ? -6.187  -7.734  51.292  1.00 12.03 ? 241 MET B CA  1 
ATOM   4085 C  C   . MET B 1 240 ? -6.838  -8.652  50.243  1.00 9.17  ? 241 MET B C   1 
ATOM   4086 O  O   . MET B 1 240 ? -6.333  -8.837  49.157  1.00 10.64 ? 241 MET B O   1 
ATOM   4087 C  CB  . MET B 1 240 ? -5.457  -6.533  50.654  1.00 13.59 ? 241 MET B CB  1 
ATOM   4088 C  CG  . MET B 1 240 ? -6.478  -5.509  49.959  1.00 11.55 ? 241 MET B CG  1 
ATOM   4089 S  SD  . MET B 1 240 ? -5.626  -4.146  49.169  1.00 12.10 ? 241 MET B SD  1 
ATOM   4090 C  CE  . MET B 1 240 ? -5.501  -3.112  50.645  1.00 13.30 ? 241 MET B CE  1 
ATOM   4091 N  N   . VAL B 1 241 ? -7.950  -9.245  50.675  1.00 9.76  ? 242 VAL B N   1 
ATOM   4092 C  CA  . VAL B 1 241 ? -8.721  -10.141 49.823  1.00 9.67  ? 242 VAL B CA  1 
ATOM   4093 C  C   . VAL B 1 241 ? -10.183 -9.940  50.192  1.00 9.75  ? 242 VAL B C   1 
ATOM   4094 O  O   . VAL B 1 241 ? -10.521 -9.533  51.335  1.00 10.40 ? 242 VAL B O   1 
ATOM   4095 C  CB  . VAL B 1 241 ? -8.375  -11.675 49.989  1.00 9.05  ? 242 VAL B CB  1 
ATOM   4096 C  CG1 . VAL B 1 241 ? -6.951  -11.971 49.589  1.00 10.34 ? 242 VAL B CG1 1 
ATOM   4097 C  CG2 . VAL B 1 241 ? -8.583  -12.117 51.429  1.00 11.05 ? 242 VAL B CG2 1 
ATOM   4098 N  N   . ASP B 1 242 ? -11.072 -10.259 49.249  1.00 8.08  ? 243 ASP B N   1 
ATOM   4099 C  CA  . ASP B 1 242 ? -12.514 -10.105 49.423  1.00 8.43  ? 243 ASP B CA  1 
ATOM   4100 C  C   . ASP B 1 242 ? -12.890 -8.680  49.847  1.00 8.53  ? 243 ASP B C   1 
ATOM   4101 O  O   . ASP B 1 242 ? -13.750 -8.436  50.718  1.00 10.64 ? 243 ASP B O   1 
ATOM   4102 C  CB  . ASP B 1 242 ? -13.086 -11.167 50.426  1.00 9.27  ? 243 ASP B CB  1 
ATOM   4103 C  CG  . ASP B 1 242 ? -12.980 -12.542 49.853  1.00 9.75  ? 243 ASP B CG  1 
ATOM   4104 O  OD1 . ASP B 1 242 ? -13.236 -12.754 48.640  1.00 9.26  ? 243 ASP B OD1 1 
ATOM   4105 O  OD2 . ASP B 1 242 ? -12.571 -13.485 50.613  1.00 11.72 ? 243 ASP B OD2 1 
ATOM   4106 N  N   . ASN B 1 243 ? -12.374 -7.723  49.096  1.00 7.77  ? 244 ASN B N   1 
ATOM   4107 C  CA  . ASN B 1 243 ? -12.670 -6.286  49.301  1.00 8.73  ? 244 ASN B CA  1 
ATOM   4108 C  C   . ASN B 1 243 ? -13.751 -5.865  48.314  1.00 7.91  ? 244 ASN B C   1 
ATOM   4109 O  O   . ASN B 1 243 ? -13.620 -4.823  47.643  1.00 8.91  ? 244 ASN B O   1 
ATOM   4110 C  CB  . ASN B 1 243 ? -11.370 -5.425  49.153  1.00 8.50  ? 244 ASN B CB  1 
ATOM   4111 C  CG  . ASN B 1 243 ? -10.636 -5.619  47.804  1.00 9.02  ? 244 ASN B CG  1 
ATOM   4112 O  OD1 . ASN B 1 243 ? -11.032 -6.446  47.000  1.00 9.29  ? 244 ASN B OD1 1 
ATOM   4113 N  ND2 . ASN B 1 243 ? -9.674  -4.795  47.571  1.00 12.29 ? 244 ASN B ND2 1 
ATOM   4114 N  N   . TRP B 1 244 ? -14.856 -6.645  48.268  1.00 7.64  ? 245 TRP B N   1 
ATOM   4115 C  CA  . TRP B 1 244 ? -15.975 -6.379  47.401  1.00 7.06  ? 245 TRP B CA  1 
ATOM   4116 C  C   . TRP B 1 244 ? -17.240 -6.273  48.202  1.00 8.54  ? 245 TRP B C   1 
ATOM   4117 O  O   . TRP B 1 244 ? -17.421 -6.985  49.199  1.00 9.47  ? 245 TRP B O   1 
ATOM   4118 C  CB  . TRP B 1 244 ? -16.144 -7.470  46.319  1.00 8.22  ? 245 TRP B CB  1 
ATOM   4119 C  CG  . TRP B 1 244 ? -16.101 -8.893  46.798  1.00 7.73  ? 245 TRP B CG  1 
ATOM   4120 C  CD1 . TRP B 1 244 ? -14.960 -9.650  47.087  1.00 8.60  ? 245 TRP B CD1 1 
ATOM   4121 C  CD2 . TRP B 1 244 ? -17.238 -9.746  47.043  1.00 7.86  ? 245 TRP B CD2 1 
ATOM   4122 N  NE1 . TRP B 1 244 ? -15.307 -10.893 47.501  1.00 8.82  ? 245 TRP B NE1 1 
ATOM   4123 C  CE2 . TRP B 1 244 ? -16.709 -11.002 47.522  1.00 8.02  ? 245 TRP B CE2 1 
ATOM   4124 C  CE3 . TRP B 1 244 ? -18.649 -9.585  46.892  1.00 8.97  ? 245 TRP B CE3 1 
ATOM   4125 C  CZ2 . TRP B 1 244 ? -17.554 -12.079 47.821  1.00 9.63  ? 245 TRP B CZ2 1 
ATOM   4126 C  CZ3 . TRP B 1 244 ? -19.477 -10.662 47.228  1.00 11.67 ? 245 TRP B CZ3 1 
ATOM   4127 C  CH2 . TRP B 1 244 ? -18.910 -11.908 47.624  1.00 10.00 ? 245 TRP B CH2 1 
ATOM   4128 N  N   . ARG B 1 245 ? -18.116 -5.376  47.810  1.00 7.82  ? 246 ARG B N   1 
ATOM   4129 C  CA  . ARG B 1 245 ? -19.509 -5.283  48.392  1.00 8.01  ? 246 ARG B CA  1 
ATOM   4130 C  C   . ARG B 1 245 ? -20.423 -6.213  47.586  1.00 7.93  ? 246 ARG B C   1 
ATOM   4131 O  O   . ARG B 1 245 ? -20.334 -6.230  46.365  1.00 8.33  ? 246 ARG B O   1 
ATOM   4132 C  CB  . ARG B 1 245 ? -19.992 -3.842  48.267  1.00 9.22  ? 246 ARG B CB  1 
ATOM   4133 C  CG  . ARG B 1 245 ? -21.287 -3.640  49.031  1.00 7.83  ? 246 ARG B CG  1 
ATOM   4134 C  CD  . ARG B 1 245 ? -21.837 -2.258  48.721  1.00 9.13  ? 246 ARG B CD  1 
ATOM   4135 N  NE  . ARG B 1 245 ? -22.919 -1.943  49.705  1.00 9.06  ? 246 ARG B NE  1 
ATOM   4136 C  CZ  . ARG B 1 245 ? -23.750 -0.926  49.612  1.00 10.06 ? 246 ARG B CZ  1 
ATOM   4137 N  NH1 . ARG B 1 245 ? -23.795 -0.124  48.542  1.00 10.26 ? 246 ARG B NH1 1 
ATOM   4138 N  NH2 . ARG B 1 245 ? -24.624 -0.666  50.659  1.00 10.84 ? 246 ARG B NH2 1 
ATOM   4139 N  N   . PRO B 1 246 ? -21.273 -6.998  48.226  1.00 9.12  ? 247 PRO B N   1 
ATOM   4140 C  CA  . PRO B 1 246 ? -22.172 -7.863  47.451  1.00 8.87  ? 247 PRO B CA  1 
ATOM   4141 C  C   . PRO B 1 246 ? -23.226 -7.024  46.747  1.00 8.83  ? 247 PRO B C   1 
ATOM   4142 O  O   . PRO B 1 246 ? -23.484 -5.815  47.039  1.00 9.04  ? 247 PRO B O   1 
ATOM   4143 C  CB  . PRO B 1 246 ? -22.834 -8.752  48.525  1.00 12.35 ? 247 PRO B CB  1 
ATOM   4144 C  CG  . PRO B 1 246 ? -22.023 -8.559  49.794  1.00 17.52 ? 247 PRO B CG  1 
ATOM   4145 C  CD  . PRO B 1 246 ? -21.399 -7.196  49.678  1.00 11.35 ? 247 PRO B CD  1 
ATOM   4146 N  N   . ALA B 1 247 ? -23.940 -7.682  45.833  1.00 8.91  ? 248 ALA B N   1 
ATOM   4147 C  CA  . ALA B 1 247 ? -25.066 -7.060  45.133  1.00 9.84  ? 248 ALA B CA  1 
ATOM   4148 C  C   . ALA B 1 247 ? -26.114 -6.522  46.040  1.00 9.36  ? 248 ALA B C   1 
ATOM   4149 O  O   . ALA B 1 247 ? -26.469 -7.178  47.010  1.00 11.31 ? 248 ALA B O   1 
ATOM   4150 C  CB  . ALA B 1 247 ? -25.646 -8.082  44.155  1.00 12.33 ? 248 ALA B CB  1 
ATOM   4151 N  N   . GLN B 1 248 ? -26.654 -5.342  45.702  1.00 9.75  ? 249 GLN B N   1 
ATOM   4152 C  CA  . GLN B 1 248 ? -27.652 -4.615  46.449  1.00 9.63  ? 249 GLN B CA  1 
ATOM   4153 C  C   . GLN B 1 248 ? -28.964 -4.625  45.748  1.00 9.36  ? 249 GLN B C   1 
ATOM   4154 O  O   . GLN B 1 248 ? -29.041 -4.836  44.531  1.00 10.86 ? 249 GLN B O   1 
ATOM   4155 C  CB  . GLN B 1 248 ? -27.195 -3.217  46.698  1.00 9.61  ? 249 GLN B CB  1 
ATOM   4156 C  CG  . GLN B 1 248 ? -25.869 -3.139  47.494  1.00 10.49 ? 249 GLN B CG  1 
ATOM   4157 C  CD  . GLN B 1 248 ? -25.986 -3.839  48.832  1.00 11.61 ? 249 GLN B CD  1 
ATOM   4158 O  OE1 . GLN B 1 248 ? -26.892 -3.501  49.614  1.00 14.35 ? 249 GLN B OE1 1 
ATOM   4159 N  NE2 . GLN B 1 248 ? -25.078 -4.723  49.143  1.00 12.28 ? 249 GLN B NE2 1 
ATOM   4160 N  N   . PRO B 1 249 ? -30.077 -4.386  46.453  1.00 11.94 ? 250 PRO B N   1 
ATOM   4161 C  CA  . PRO B 1 249 ? -31.369 -4.421  45.739  1.00 12.84 ? 250 PRO B CA  1 
ATOM   4162 C  C   . PRO B 1 249 ? -31.505 -3.414  44.603  1.00 11.03 ? 250 PRO B C   1 
ATOM   4163 O  O   . PRO B 1 249 ? -31.150 -2.234  44.724  1.00 12.50 ? 250 PRO B O   1 
ATOM   4164 C  CB  . PRO B 1 249 ? -32.382 -4.103  46.858  1.00 17.35 ? 250 PRO B CB  1 
ATOM   4165 C  CG  . PRO B 1 249 ? -31.690 -4.461  48.163  1.00 18.23 ? 250 PRO B CG  1 
ATOM   4166 C  CD  . PRO B 1 249 ? -30.225 -4.115  47.901  1.00 13.80 ? 250 PRO B CD  1 
ATOM   4167 N  N   . LEU B 1 250 ? -31.996 -3.890  43.464  1.00 12.28 ? 251 LEU B N   1 
ATOM   4168 C  CA  . LEU B 1 250 ? -32.161 -2.995  42.302  1.00 12.51 ? 251 LEU B CA  1 
ATOM   4169 C  C   . LEU B 1 250 ? -33.190 -1.891  42.509  1.00 13.62 ? 251 LEU B C   1 
ATOM   4170 O  O   . LEU B 1 250 ? -33.087 -0.780  41.976  1.00 13.06 ? 251 LEU B O   1 
ATOM   4171 C  CB  . LEU B 1 250 ? -32.574 -3.810  41.113  1.00 14.45 ? 251 LEU B CB  1 
ATOM   4172 C  CG  . LEU B 1 250 ? -32.542 -3.146  39.769  1.00 14.08 ? 251 LEU B CG  1 
ATOM   4173 C  CD1 . LEU B 1 250 ? -31.180 -2.555  39.324  1.00 15.15 ? 251 LEU B CD1 1 
ATOM   4174 C  CD2 . LEU B 1 250 ? -33.038 -4.099  38.683  1.00 17.68 ? 251 LEU B CD2 1 
ATOM   4175 N  N   . LYS B 1 251 ? -34.225 -2.192  43.330  1.00 14.47 ? 252 LYS B N   1 
ATOM   4176 C  CA  . LYS B 1 251 ? -35.289 -1.197  43.660  1.00 13.88 ? 252 LYS B CA  1 
ATOM   4177 C  C   . LYS B 1 251 ? -35.885 -0.652  42.339  1.00 15.75 ? 252 LYS B C   1 
ATOM   4178 O  O   . LYS B 1 251 ? -36.134 -1.415  41.394  1.00 19.64 ? 252 LYS B O   1 
ATOM   4179 C  CB  . LYS B 1 251 ? -34.805 -0.127  44.654  1.00 17.07 ? 252 LYS B CB  1 
ATOM   4180 C  CG  . LYS B 1 251 ? -34.471 -0.826  45.962  1.00 18.99 ? 252 LYS B CG  1 
ATOM   4181 C  CD  . LYS B 1 251 ? -34.147 0.118   47.047  1.00 22.87 ? 252 LYS B CD  1 
ATOM   4182 C  CE  . LYS B 1 251 ? -34.053 -0.633  48.357  1.00 26.35 ? 252 LYS B CE  1 
ATOM   4183 N  NZ  . LYS B 1 251 ? -33.706 0.376   49.412  1.00 30.22 ? 252 LYS B NZ  1 
ATOM   4184 N  N   . ASN B 1 252 ? -36.143 0.621   42.266  1.00 14.42 ? 253 ASN B N   1 
ATOM   4185 C  CA  . ASN B 1 252 ? -36.891 0.986   41.098  1.00 23.27 ? 253 ASN B CA  1 
ATOM   4186 C  C   . ASN B 1 252 ? -36.256 0.934   39.619  1.00 32.72 ? 253 ASN B C   1 
ATOM   4187 O  O   . ASN B 1 252 ? -36.882 1.166   38.569  1.00 33.68 ? 253 ASN B O   1 
ATOM   4188 C  CB  . ASN B 1 252 ? -37.725 2.259   41.461  1.00 30.15 ? 253 ASN B CB  1 
ATOM   4189 C  CG  . ASN B 1 252 ? -38.638 2.759   40.357  1.00 31.81 ? 253 ASN B CG  1 
ATOM   4190 O  OD1 . ASN B 1 252 ? -39.328 2.018   39.709  1.00 48.16 ? 253 ASN B OD1 1 
ATOM   4191 N  ND2 . ASN B 1 252 ? -38.669 4.080   40.233  1.00 25.50 ? 253 ASN B ND2 1 
ATOM   4192 N  N   . ARG B 1 253 ? -35.009 0.515   39.521  1.00 17.26 ? 254 ARG B N   1 
ATOM   4193 C  CA  . ARG B 1 253 ? -34.114 0.912   38.386  1.00 13.17 ? 254 ARG B CA  1 
ATOM   4194 C  C   . ARG B 1 253 ? -34.228 -0.013  37.231  1.00 13.40 ? 254 ARG B C   1 
ATOM   4195 O  O   . ARG B 1 253 ? -34.493 -1.190  37.421  1.00 17.53 ? 254 ARG B O   1 
ATOM   4196 C  CB  . ARG B 1 253 ? -32.669 0.966   38.914  1.00 12.23 ? 254 ARG B CB  1 
ATOM   4197 C  CG  . ARG B 1 253 ? -32.516 2.098   39.969  1.00 11.65 ? 254 ARG B CG  1 
ATOM   4198 C  CD  . ARG B 1 253 ? -31.127 2.098   40.595  1.00 11.36 ? 254 ARG B CD  1 
ATOM   4199 N  NE  . ARG B 1 253 ? -30.950 0.940   41.540  1.00 11.72 ? 254 ARG B NE  1 
ATOM   4200 C  CZ  . ARG B 1 253 ? -29.787 0.665   42.150  1.00 9.82  ? 254 ARG B CZ  1 
ATOM   4201 N  NH1 . ARG B 1 253 ? -28.684 1.349   41.877  1.00 9.40  ? 254 ARG B NH1 1 
ATOM   4202 N  NH2 . ARG B 1 253 ? -29.772 -0.320  43.049  1.00 10.03 ? 254 ARG B NH2 1 
ATOM   4203 N  N   . GLN B 1 254 ? -33.829 0.475   36.069  1.00 13.30 ? 255 GLN B N   1 
ATOM   4204 C  CA  . GLN B 1 254 ? -33.709 -0.290  34.878  1.00 15.87 ? 255 GLN B CA  1 
ATOM   4205 C  C   . GLN B 1 254 ? -32.269 -0.269  34.458  1.00 17.93 ? 255 GLN B C   1 
ATOM   4206 O  O   . GLN B 1 254 ? -31.545 0.770   34.536  1.00 19.57 ? 255 GLN B O   1 
ATOM   4207 C  CB  . GLN B 1 254 ? -34.514 0.432   33.780  1.00 21.97 ? 255 GLN B CB  1 
ATOM   4208 C  CG  . GLN B 1 254 ? -34.376 -0.151  32.390  1.00 41.93 ? 255 GLN B CG  1 
ATOM   4209 C  CD  . GLN B 1 254 ? -35.417 -1.193  32.149  1.00 50.33 ? 255 GLN B CD  1 
ATOM   4210 O  OE1 . GLN B 1 254 ? -36.541 -0.860  31.805  1.00 85.73 ? 255 GLN B OE1 1 
ATOM   4211 N  NE2 . GLN B 1 254 ? -35.056 -2.469  32.322  1.00 72.09 ? 255 GLN B NE2 1 
ATOM   4212 N  N   . ILE B 1 255 ? -31.754 -1.438  34.154  1.00 12.53 ? 256 ILE B N   1 
ATOM   4213 C  CA  . ILE B 1 255 ? -30.427 -1.548  33.551  1.00 11.74 ? 256 ILE B CA  1 
ATOM   4214 C  C   . ILE B 1 255 ? -30.625 -1.526  32.017  1.00 11.85 ? 256 ILE B C   1 
ATOM   4215 O  O   . ILE B 1 255 ? -31.502 -2.226  31.489  1.00 13.93 ? 256 ILE B O   1 
ATOM   4216 C  CB  . ILE B 1 255 ? -29.701 -2.806  34.029  1.00 11.36 ? 256 ILE B CB  1 
ATOM   4217 C  CG1 . ILE B 1 255 ? -29.678 -2.823  35.584  1.00 11.94 ? 256 ILE B CG1 1 
ATOM   4218 C  CG2 . ILE B 1 255 ? -28.348 -2.903  33.346  1.00 15.03 ? 256 ILE B CG2 1 
ATOM   4219 C  CD1 . ILE B 1 255 ? -28.931 -4.044  36.085  1.00 15.25 ? 256 ILE B CD1 1 
ATOM   4220 N  N   . LYS B 1 256 ? -29.877 -0.685  31.306  1.00 12.03 ? 257 LYS B N   1 
ATOM   4221 C  CA  . LYS B 1 256 ? -29.920 -0.604  29.861  1.00 12.38 ? 257 LYS B CA  1 
ATOM   4222 C  C   . LYS B 1 256 ? -28.733 -1.269  29.230  1.00 11.77 ? 257 LYS B C   1 
ATOM   4223 O  O   . LYS B 1 256 ? -27.638 -1.243  29.850  1.00 13.28 ? 257 LYS B O   1 
ATOM   4224 C  CB  . LYS B 1 256 ? -29.972 0.865   29.419  1.00 15.44 ? 257 LYS B CB  1 
ATOM   4225 C  CG  . LYS B 1 256 ? -31.247 1.534   29.949  1.00 19.51 ? 257 LYS B CG  1 
ATOM   4226 C  CD  . LYS B 1 256 ? -31.454 2.966   29.538  1.00 27.59 ? 257 LYS B CD  1 
ATOM   4227 C  CE  . LYS B 1 256 ? -32.617 3.627   30.308  1.00 42.23 ? 257 LYS B CE  1 
ATOM   4228 N  NZ  . LYS B 1 256 ? -32.343 5.078   30.544  1.00 45.88 ? 257 LYS B NZ  1 
ATOM   4229 N  N   . ALA B 1 257 ? -28.877 -1.859  28.040  1.00 13.19 ? 258 ALA B N   1 
ATOM   4230 C  CA  . ALA B 1 257 ? -27.789 -2.504  27.323  1.00 13.49 ? 258 ALA B CA  1 
ATOM   4231 C  C   . ALA B 1 257 ? -27.501 -1.724  26.047  1.00 12.95 ? 258 ALA B C   1 
ATOM   4232 O  O   . ALA B 1 257 ? -28.438 -1.243  25.359  1.00 15.32 ? 258 ALA B O   1 
ATOM   4233 C  CB  . ALA B 1 257 ? -28.129 -3.974  26.933  1.00 14.46 ? 258 ALA B CB  1 
ATOM   4234 N  N   . SER B 1 258 ? -26.254 -1.601  25.673  1.00 12.96 ? 259 SER B N   1 
ATOM   4235 C  CA  . SER B 1 258 ? -25.894 -0.860  24.478  1.00 15.05 ? 259 SER B CA  1 
ATOM   4236 C  C   . SER B 1 258 ? -25.956 -1.813  23.252  1.00 15.64 ? 259 SER B C   1 
ATOM   4237 O  O   . SER B 1 258 ? -25.654 -1.364  22.107  1.00 19.70 ? 259 SER B O   1 
ATOM   4238 C  CB  . SER B 1 258 ? -24.485 -0.336  24.610  1.00 16.30 ? 259 SER B CB  1 
ATOM   4239 O  OG  . SER B 1 258 ? -23.509 -1.366  24.532  1.00 13.19 ? 259 SER B OG  1 
ATOM   4240 N  N   . PHE B 1 259 ? -26.324 -3.076  23.444  1.00 15.65 ? 260 PHE B N   1 
ATOM   4241 C  CA  . PHE B 1 259 ? -26.101 -4.094  22.400  1.00 18.88 ? 260 PHE B CA  1 
ATOM   4242 C  C   . PHE B 1 259 ? -27.273 -5.071  22.507  1.00 21.74 ? 260 PHE B C   1 
ATOM   4243 O  O   . PHE B 1 259 ? -27.973 -5.225  23.582  1.00 22.59 ? 260 PHE B O   1 
ATOM   4244 C  CB  . PHE B 1 259 ? -24.752 -4.836  22.626  1.00 19.46 ? 260 PHE B CB  1 
ATOM   4245 C  CG  . PHE B 1 259 ? -24.769 -5.589  23.953  1.00 20.32 ? 260 PHE B CG  1 
ATOM   4246 C  CD1 . PHE B 1 259 ? -24.462 -4.912  25.129  1.00 17.65 ? 260 PHE B CD1 1 
ATOM   4247 C  CD2 . PHE B 1 259 ? -25.209 -6.942  24.010  1.00 21.15 ? 260 PHE B CD2 1 
ATOM   4248 C  CE1 . PHE B 1 259 ? -24.577 -5.570  26.362  1.00 18.24 ? 260 PHE B CE1 1 
ATOM   4249 C  CE2 . PHE B 1 259 ? -25.349 -7.624  25.246  1.00 21.82 ? 260 PHE B CE2 1 
ATOM   4250 C  CZ  . PHE B 1 259 ? -25.005 -6.929  26.436  1.00 19.52 ? 260 PHE B CZ  1 
ATOM   4251 N  N   . LYS B 1 260 ? -27.416 -5.728  21.335  1.00 32.54 ? 261 LYS B N   1 
ATOM   4252 C  CA  . LYS B 1 260 ? -28.444 -6.681  20.935  1.00 37.07 ? 261 LYS B CA  1 
ATOM   4253 C  C   . LYS B 1 260 ? -29.868 -6.129  20.846  1.00 47.90 ? 261 LYS B C   1 
ATOM   4254 O  O   . LYS B 1 260 ? -30.352 -5.785  19.761  1.00 58.63 ? 261 LYS B O   1 
ATOM   4255 C  CB  . LYS B 1 260 ? -28.410 -7.917  21.807  1.00 37.27 ? 261 LYS B CB  1 
ATOM   4256 C  CG  . LYS B 1 260 ? -27.520 -9.027  21.286  1.00 56.63 ? 261 LYS B CG  1 
ATOM   4257 C  CD  . LYS B 1 260 ? -26.026 -8.746  21.458  1.00 42.84 ? 261 LYS B CD  1 
ATOM   4258 C  CE  . LYS B 1 260 ? -25.262 -10.056 21.675  1.00 44.82 ? 261 LYS B CE  1 
ATOM   4259 N  NZ  . LYS B 1 260 ? -25.440 -10.729 23.030  1.00 40.69 ? 261 LYS B NZ  1 
ATOM   4260 N  N   . HIS C 1 3   ? 8.166   22.411  43.539  1.00 29.44 ? 3   HIS C N   1 
ATOM   4261 C  CA  . HIS C 1 3   ? 9.100   21.397  44.215  1.00 33.84 ? 3   HIS C CA  1 
ATOM   4262 C  C   . HIS C 1 3   ? 9.641   21.866  45.578  1.00 35.83 ? 3   HIS C C   1 
ATOM   4263 O  O   . HIS C 1 3   ? 10.901  22.050  45.803  1.00 44.01 ? 3   HIS C O   1 
ATOM   4264 C  CB  . HIS C 1 3   ? 10.259  21.023  43.299  1.00 33.68 ? 3   HIS C CB  1 
ATOM   4265 C  CG  . HIS C 1 3   ? 11.044  19.837  43.784  1.00 42.65 ? 3   HIS C CG  1 
ATOM   4266 N  ND1 . HIS C 1 3   ? 10.688  18.552  43.473  1.00 38.26 ? 3   HIS C ND1 1 
ATOM   4267 C  CD2 . HIS C 1 3   ? 12.203  19.759  44.603  1.00 37.96 ? 3   HIS C CD2 1 
ATOM   4268 C  CE1 . HIS C 1 3   ? 11.589  17.698  44.054  1.00 49.89 ? 3   HIS C CE1 1 
ATOM   4269 N  NE2 . HIS C 1 3   ? 12.504  18.441  44.751  1.00 41.44 ? 3   HIS C NE2 1 
ATOM   4270 N  N   . HIS C 1 4   ? 8.687   22.098  46.496  1.00 34.55 ? 4   HIS C N   1 
ATOM   4271 C  CA  . HIS C 1 4   ? 9.063   22.622  47.794  1.00 29.85 ? 4   HIS C CA  1 
ATOM   4272 C  C   . HIS C 1 4   ? 9.419   21.558  48.726  1.00 21.57 ? 4   HIS C C   1 
ATOM   4273 O  O   . HIS C 1 4   ? 9.226   20.366  48.489  1.00 21.03 ? 4   HIS C O   1 
ATOM   4274 C  CB  . HIS C 1 4   ? 8.178   23.745  48.331  1.00 37.58 ? 4   HIS C CB  1 
ATOM   4275 C  CG  . HIS C 1 4   ? 8.878   25.118  48.274  1.00 66.51 ? 4   HIS C CG  1 
ATOM   4276 N  ND1 . HIS C 1 4   ? 9.778   25.525  49.212  1.00 62.13 ? 4   HIS C ND1 1 
ATOM   4277 C  CD2 . HIS C 1 4   ? 8.842   26.144  47.299  1.00 60.77 ? 4   HIS C CD2 1 
ATOM   4278 C  CE1 . HIS C 1 4   ? 10.260  26.753  48.889  1.00 61.50 ? 4   HIS C CE1 1 
ATOM   4279 N  NE2 . HIS C 1 4   ? 9.694   27.129  47.713  1.00 68.51 ? 4   HIS C NE2 1 
ATOM   4280 N  N   . TRP C 1 5   ? 9.989   21.961  49.815  1.00 18.90 ? 5   TRP C N   1 
ATOM   4281 C  CA  . TRP C 1 5   ? 10.543  20.999  50.742  1.00 14.72 ? 5   TRP C CA  1 
ATOM   4282 C  C   . TRP C 1 5   ? 9.479   20.220  51.472  1.00 13.18 ? 5   TRP C C   1 
ATOM   4283 O  O   . TRP C 1 5   ? 8.333   20.664  51.664  1.00 15.12 ? 5   TRP C O   1 
ATOM   4284 C  CB  . TRP C 1 5   ? 11.480  21.720  51.711  1.00 14.68 ? 5   TRP C CB  1 
ATOM   4285 C  CG  . TRP C 1 5   ? 10.814  22.557  52.778  1.00 14.66 ? 5   TRP C CG  1 
ATOM   4286 C  CD1 . TRP C 1 5   ? 10.474  23.938  52.699  1.00 17.00 ? 5   TRP C CD1 1 
ATOM   4287 C  CD2 . TRP C 1 5   ? 10.330  22.095  54.082  1.00 14.14 ? 5   TRP C CD2 1 
ATOM   4288 N  NE1 . TRP C 1 5   ? 9.867   24.337  53.837  1.00 16.01 ? 5   TRP C NE1 1 
ATOM   4289 C  CE2 . TRP C 1 5   ? 9.720   23.241  54.707  1.00 13.94 ? 5   TRP C CE2 1 
ATOM   4290 C  CE3 . TRP C 1 5   ? 10.356  20.869  54.763  1.00 12.01 ? 5   TRP C CE3 1 
ATOM   4291 C  CZ2 . TRP C 1 5   ? 9.191   23.186  56.007  1.00 13.07 ? 5   TRP C CZ2 1 
ATOM   4292 C  CZ3 . TRP C 1 5   ? 9.778   20.818  56.059  1.00 12.83 ? 5   TRP C CZ3 1 
ATOM   4293 C  CH2 . TRP C 1 5   ? 9.203   21.968  56.636  1.00 13.95 ? 5   TRP C CH2 1 
ATOM   4294 N  N   . GLY C 1 6   ? 9.867   19.006  51.877  1.00 12.64 ? 6   GLY C N   1 
ATOM   4295 C  CA  . GLY C 1 6   ? 8.937   18.239  52.724  1.00 13.36 ? 6   GLY C CA  1 
ATOM   4296 C  C   . GLY C 1 6   ? 9.715   17.095  53.329  1.00 13.96 ? 6   GLY C C   1 
ATOM   4297 O  O   . GLY C 1 6   ? 10.897  17.249  53.660  1.00 13.52 ? 6   GLY C O   1 
ATOM   4298 N  N   . TYR C 1 7   ? 9.032   15.946  53.470  1.00 13.71 ? 7   TYR C N   1 
ATOM   4299 C  CA  . TYR C 1 7   ? 9.665   14.772  54.085  1.00 13.53 ? 7   TYR C CA  1 
ATOM   4300 C  C   . TYR C 1 7   ? 9.803   13.566  53.153  1.00 22.44 ? 7   TYR C C   1 
ATOM   4301 O  O   . TYR C 1 7   ? 10.429  12.574  53.520  1.00 26.73 ? 7   TYR C O   1 
ATOM   4302 C  CB  . TYR C 1 7   ? 8.902   14.456  55.387  1.00 15.03 ? 7   TYR C CB  1 
ATOM   4303 C  CG  . TYR C 1 7   ? 9.179   15.564  56.444  1.00 12.12 ? 7   TYR C CG  1 
ATOM   4304 C  CD1 . TYR C 1 7   ? 10.359  15.529  57.192  1.00 12.34 ? 7   TYR C CD1 1 
ATOM   4305 C  CD2 . TYR C 1 7   ? 8.257   16.581  56.620  1.00 11.95 ? 7   TYR C CD2 1 
ATOM   4306 C  CE1 . TYR C 1 7   ? 10.568  16.536  58.173  1.00 9.25  ? 7   TYR C CE1 1 
ATOM   4307 C  CE2 . TYR C 1 7   ? 8.450   17.553  57.623  1.00 11.49 ? 7   TYR C CE2 1 
ATOM   4308 C  CZ  . TYR C 1 7   ? 9.645   17.533  58.368  1.00 9.86  ? 7   TYR C CZ  1 
ATOM   4309 O  OH  . TYR C 1 7   ? 9.763   18.466  59.332  1.00 11.67 ? 7   TYR C OH  1 
ATOM   4310 N  N   . GLY C 1 8   ? 9.253   13.673  51.942  1.00 18.81 ? 8   GLY C N   1 
ATOM   4311 C  CA  . GLY C 1 8   ? 9.292   12.580  50.939  1.00 21.15 ? 8   GLY C CA  1 
ATOM   4312 C  C   . GLY C 1 8   ? 10.707  12.200  50.427  1.00 22.39 ? 8   GLY C C   1 
ATOM   4313 O  O   . GLY C 1 8   ? 11.772  12.866  50.620  1.00 28.14 ? 8   GLY C O   1 
ATOM   4314 N  N   . LYS C 1 9   ? 10.681  11.253  49.473  1.00 32.32 ? 9   LYS C N   1 
ATOM   4315 C  CA  . LYS C 1 9   ? 11.959  10.752  48.834  1.00 37.95 ? 9   LYS C CA  1 
ATOM   4316 C  C   . LYS C 1 9   ? 12.632  11.847  48.030  1.00 27.75 ? 9   LYS C C   1 
ATOM   4317 O  O   . LYS C 1 9   ? 13.910  12.033  47.985  1.00 25.50 ? 9   LYS C O   1 
ATOM   4318 C  CB  . LYS C 1 9   ? 11.731  9.553   47.903  1.00 60.21 ? 9   LYS C CB  1 
ATOM   4319 C  CG  . LYS C 1 9   ? 13.035  9.048   47.261  1.00 37.80 ? 9   LYS C CG  1 
ATOM   4320 N  N   . HIS C 1 10  ? 11.742  12.622  47.443  1.00 20.11 ? 10  HIS C N   1 
ATOM   4321 C  CA  . HIS C 1 10  ? 12.266  13.611  46.528  1.00 18.83 ? 10  HIS C CA  1 
ATOM   4322 C  C   . HIS C 1 10  ? 12.540  14.983  47.102  1.00 16.72 ? 10  HIS C C   1 
ATOM   4323 O  O   . HIS C 1 10  ? 13.241  15.778  46.469  1.00 19.98 ? 10  HIS C O   1 
ATOM   4324 C  CB  . HIS C 1 10  ? 11.339  13.642  45.323  1.00 21.47 ? 10  HIS C CB  1 
ATOM   4325 C  CG  . HIS C 1 10  ? 11.199  12.259  44.659  1.00 20.71 ? 10  HIS C CG  1 
ATOM   4326 N  ND1 . HIS C 1 10  ? 12.245  11.702  44.002  1.00 21.53 ? 10  HIS C ND1 1 
ATOM   4327 C  CD2 . HIS C 1 10  ? 10.136  11.328  44.617  1.00 21.98 ? 10  HIS C CD2 1 
ATOM   4328 C  CE1 . HIS C 1 10  ? 11.898  10.481  43.565  1.00 20.13 ? 10  HIS C CE1 1 
ATOM   4329 N  NE2 . HIS C 1 10  ? 10.585  10.249  43.944  1.00 25.29 ? 10  HIS C NE2 1 
ATOM   4330 N  N   . ASN C 1 11  ? 11.974  15.275  48.305  1.00 16.05 ? 11  ASN C N   1 
ATOM   4331 C  CA  . ASN C 1 11  ? 12.032  16.662  48.819  1.00 14.71 ? 11  ASN C CA  1 
ATOM   4332 C  C   . ASN C 1 11  ? 12.395  16.678  50.322  1.00 13.66 ? 11  ASN C C   1 
ATOM   4333 O  O   . ASN C 1 11  ? 12.252  17.716  50.941  1.00 14.76 ? 11  ASN C O   1 
ATOM   4334 C  CB  . ASN C 1 11  ? 10.701  17.353  48.567  1.00 15.16 ? 11  ASN C CB  1 
ATOM   4335 C  CG  . ASN C 1 11  ? 9.549   16.789  49.338  1.00 15.45 ? 11  ASN C CG  1 
ATOM   4336 O  OD1 . ASN C 1 11  ? 9.605   15.722  49.938  1.00 18.17 ? 11  ASN C OD1 1 
ATOM   4337 N  ND2 . ASN C 1 11  ? 8.449   17.439  49.203  1.00 17.67 ? 11  ASN C ND2 1 
ATOM   4338 N  N   . GLY C 1 12  ? 12.896  15.560  50.842  1.00 14.04 ? 12  GLY C N   1 
ATOM   4339 C  CA  . GLY C 1 12  ? 13.122  15.376  52.285  1.00 12.99 ? 12  GLY C CA  1 
ATOM   4340 C  C   . GLY C 1 12  ? 14.455  15.899  52.689  1.00 11.75 ? 12  GLY C C   1 
ATOM   4341 O  O   . GLY C 1 12  ? 15.164  16.625  52.000  1.00 12.40 ? 12  GLY C O   1 
ATOM   4342 N  N   . PRO C 1 13  ? 14.800  15.609  53.984  1.00 11.95 ? 13  PRO C N   1 
ATOM   4343 C  CA  . PRO C 1 13  ? 15.939  16.222  54.628  1.00 12.65 ? 13  PRO C CA  1 
ATOM   4344 C  C   . PRO C 1 13  ? 17.223  16.181  53.884  1.00 11.67 ? 13  PRO C C   1 
ATOM   4345 O  O   . PRO C 1 13  ? 17.989  17.154  53.962  1.00 12.64 ? 13  PRO C O   1 
ATOM   4346 C  CB  . PRO C 1 13  ? 16.025  15.394  55.961  1.00 12.87 ? 13  PRO C CB  1 
ATOM   4347 C  CG  . PRO C 1 13  ? 14.602  15.109  56.281  1.00 13.99 ? 13  PRO C CG  1 
ATOM   4348 C  CD  . PRO C 1 13  ? 13.957  14.852  54.949  1.00 12.90 ? 13  PRO C CD  1 
ATOM   4349 N  N   A GLU C 1 14  ? 17.454  15.067  53.174  0.50 12.21 ? 14  GLU C N   1 
ATOM   4350 N  N   B GLU C 1 14  ? 17.569  15.111  53.127  0.50 13.80 ? 14  GLU C N   1 
ATOM   4351 C  CA  A GLU C 1 14  ? 18.646  14.934  52.409  0.50 14.26 ? 14  GLU C CA  1 
ATOM   4352 C  CA  B GLU C 1 14  ? 18.864  15.141  52.390  0.50 15.83 ? 14  GLU C CA  1 
ATOM   4353 C  C   A GLU C 1 14  ? 18.790  15.969  51.199  0.50 13.24 ? 14  GLU C C   1 
ATOM   4354 C  C   B GLU C 1 14  ? 18.869  16.140  51.177  0.50 14.43 ? 14  GLU C C   1 
ATOM   4355 O  O   A GLU C 1 14  ? 19.897  16.077  50.665  0.50 13.00 ? 14  GLU C O   1 
ATOM   4356 O  O   B GLU C 1 14  ? 19.920  16.396  50.573  0.50 17.99 ? 14  GLU C O   1 
ATOM   4357 C  CB  A GLU C 1 14  ? 18.835  13.462  52.015  0.50 17.70 ? 14  GLU C CB  1 
ATOM   4358 C  CB  B GLU C 1 14  ? 19.316  13.754  51.909  0.50 18.25 ? 14  GLU C CB  1 
ATOM   4359 C  CG  A GLU C 1 14  ? 17.919  12.871  50.982  0.50 14.04 ? 14  GLU C CG  1 
ATOM   4360 C  CG  B GLU C 1 14  ? 19.138  12.632  52.959  0.50 18.48 ? 14  GLU C CG  1 
ATOM   4361 C  CD  A GLU C 1 14  ? 16.553  12.495  51.536  0.50 16.70 ? 14  GLU C CD  1 
ATOM   4362 C  CD  B GLU C 1 14  ? 19.917  12.884  54.240  0.50 22.06 ? 14  GLU C CD  1 
ATOM   4363 O  OE1 A GLU C 1 14  ? 16.160  13.036  52.591  0.50 15.00 ? 14  GLU C OE1 1 
ATOM   4364 O  OE1 B GLU C 1 14  ? 19.311  12.806  55.329  0.50 21.50 ? 14  GLU C OE1 1 
ATOM   4365 O  OE2 A GLU C 1 14  ? 15.865  11.661  50.910  0.50 21.75 ? 14  GLU C OE2 1 
ATOM   4366 O  OE2 B GLU C 1 14  ? 21.136  13.152  54.166  0.50 26.88 ? 14  GLU C OE2 1 
ATOM   4367 N  N   . HIS C 1 15  ? 17.698  16.663  50.819  1.00 12.70 ? 15  HIS C N   1 
ATOM   4368 C  CA  . HIS C 1 15  ? 17.586  17.630  49.729  1.00 11.74 ? 15  HIS C CA  1 
ATOM   4369 C  C   . HIS C 1 15  ? 17.614  19.026  50.198  1.00 11.49 ? 15  HIS C C   1 
ATOM   4370 O  O   . HIS C 1 15  ? 17.830  19.973  49.419  1.00 13.44 ? 15  HIS C O   1 
ATOM   4371 C  CB  . HIS C 1 15  ? 16.284  17.423  48.961  1.00 12.54 ? 15  HIS C CB  1 
ATOM   4372 C  CG  . HIS C 1 15  ? 16.278  16.157  48.195  1.00 14.31 ? 15  HIS C CG  1 
ATOM   4373 N  ND1 . HIS C 1 15  ? 16.762  16.073  46.892  1.00 19.19 ? 15  HIS C ND1 1 
ATOM   4374 C  CD2 . HIS C 1 15  ? 15.769  14.911  48.528  1.00 16.15 ? 15  HIS C CD2 1 
ATOM   4375 C  CE1 . HIS C 1 15  ? 16.627  14.810  46.463  1.00 24.11 ? 15  HIS C CE1 1 
ATOM   4376 N  NE2 . HIS C 1 15  ? 16.024  14.082  47.436  1.00 20.63 ? 15  HIS C NE2 1 
ATOM   4377 N  N   . TRP C 1 16  ? 17.356  19.286  51.523  1.00 10.75 ? 16  TRP C N   1 
ATOM   4378 C  CA  . TRP C 1 16  ? 17.124  20.633  51.995  1.00 10.90 ? 16  TRP C CA  1 
ATOM   4379 C  C   . TRP C 1 16  ? 18.263  21.601  51.772  1.00 10.57 ? 16  TRP C C   1 
ATOM   4380 O  O   . TRP C 1 16  ? 18.048  22.803  51.592  1.00 11.75 ? 16  TRP C O   1 
ATOM   4381 C  CB  . TRP C 1 16  ? 16.740  20.611  53.488  1.00 9.60  ? 16  TRP C CB  1 
ATOM   4382 C  CG  . TRP C 1 16  ? 15.444  19.912  53.762  1.00 10.52 ? 16  TRP C CG  1 
ATOM   4383 C  CD1 . TRP C 1 16  ? 14.452  19.456  52.892  1.00 10.42 ? 16  TRP C CD1 1 
ATOM   4384 C  CD2 . TRP C 1 16  ? 14.973  19.568  55.095  1.00 11.50 ? 16  TRP C CD2 1 
ATOM   4385 N  NE1 . TRP C 1 16  ? 13.437  18.901  53.558  1.00 11.14 ? 16  TRP C NE1 1 
ATOM   4386 C  CE2 . TRP C 1 16  ? 13.708  18.956  54.917  1.00 9.66  ? 16  TRP C CE2 1 
ATOM   4387 C  CE3 . TRP C 1 16  ? 15.483  19.774  56.382  1.00 9.87  ? 16  TRP C CE3 1 
ATOM   4388 C  CZ2 . TRP C 1 16  ? 12.927  18.531  56.006  1.00 10.06 ? 16  TRP C CZ2 1 
ATOM   4389 C  CZ3 . TRP C 1 16  ? 14.728  19.305  57.481  1.00 9.81  ? 16  TRP C CZ3 1 
ATOM   4390 C  CH2 . TRP C 1 16  ? 13.468  18.776  57.283  1.00 10.39 ? 16  TRP C CH2 1 
ATOM   4391 N  N   . HIS C 1 17  ? 19.494  21.109  51.782  1.00 11.56 ? 17  HIS C N   1 
ATOM   4392 C  CA  . HIS C 1 17  ? 20.663  21.947  51.670  1.00 11.79 ? 17  HIS C CA  1 
ATOM   4393 C  C   . HIS C 1 17  ? 20.746  22.695  50.297  1.00 12.37 ? 17  HIS C C   1 
ATOM   4394 O  O   . HIS C 1 17  ? 21.376  23.750  50.260  1.00 13.83 ? 17  HIS C O   1 
ATOM   4395 C  CB  . HIS C 1 17  ? 21.965  21.159  51.886  1.00 13.43 ? 17  HIS C CB  1 
ATOM   4396 C  CG  . HIS C 1 17  ? 22.298  20.300  50.663  1.00 14.09 ? 17  HIS C CG  1 
ATOM   4397 N  ND1 . HIS C 1 17  ? 23.183  20.711  49.667  1.00 16.74 ? 17  HIS C ND1 1 
ATOM   4398 C  CD2 . HIS C 1 17  ? 21.783  19.078  50.259  1.00 13.79 ? 17  HIS C CD2 1 
ATOM   4399 C  CE1 . HIS C 1 17  ? 23.208  19.757  48.707  1.00 16.98 ? 17  HIS C CE1 1 
ATOM   4400 N  NE2 . HIS C 1 17  ? 22.370  18.778  49.010  1.00 14.82 ? 17  HIS C NE2 1 
ATOM   4401 N  N   . LYS C 1 18  ? 19.974  22.221  49.283  1.00 11.45 ? 18  LYS C N   1 
ATOM   4402 C  CA  . LYS C 1 18  ? 20.090  22.949  48.002  1.00 14.12 ? 18  LYS C CA  1 
ATOM   4403 C  C   . LYS C 1 18  ? 19.368  24.311  48.067  1.00 16.63 ? 18  LYS C C   1 
ATOM   4404 O  O   . LYS C 1 18  ? 19.897  25.335  47.606  1.00 20.26 ? 18  LYS C O   1 
ATOM   4405 C  CB  . LYS C 1 18  ? 19.477  22.033  46.932  1.00 13.89 ? 18  LYS C CB  1 
ATOM   4406 C  CG  . LYS C 1 18  ? 20.402  20.846  46.621  1.00 16.05 ? 18  LYS C CG  1 
ATOM   4407 C  CD  . LYS C 1 18  ? 19.702  19.919  45.670  1.00 16.31 ? 18  LYS C CD  1 
ATOM   4408 C  CE  . LYS C 1 18  ? 18.694  18.948  46.305  1.00 14.38 ? 18  LYS C CE  1 
ATOM   4409 N  NZ  . LYS C 1 18  ? 17.896  18.108  45.366  1.00 15.44 ? 18  LYS C NZ  1 
ATOM   4410 N  N   . ASP C 1 19  ? 18.197  24.334  48.710  1.00 15.10 ? 19  ASP C N   1 
ATOM   4411 C  CA  . ASP C 1 19  ? 17.555  25.603  48.950  1.00 16.58 ? 19  ASP C CA  1 
ATOM   4412 C  C   . ASP C 1 19  ? 17.997  26.366  50.187  1.00 16.84 ? 19  ASP C C   1 
ATOM   4413 O  O   . ASP C 1 19  ? 17.833  27.585  50.252  1.00 16.09 ? 19  ASP C O   1 
ATOM   4414 C  CB  . ASP C 1 19  ? 16.039  25.399  48.946  1.00 17.97 ? 19  ASP C CB  1 
ATOM   4415 C  CG  . ASP C 1 19  ? 15.383  25.571  47.556  1.00 25.49 ? 19  ASP C CG  1 
ATOM   4416 O  OD1 . ASP C 1 19  ? 15.906  26.284  46.652  1.00 31.60 ? 19  ASP C OD1 1 
ATOM   4417 O  OD2 . ASP C 1 19  ? 14.344  24.979  47.383  1.00 39.48 ? 19  ASP C OD2 1 
ATOM   4418 N  N   . PHE C 1 20  ? 18.564  25.629  51.173  1.00 13.86 ? 20  PHE C N   1 
ATOM   4419 C  CA  . PHE C 1 20  ? 18.912  26.218  52.522  1.00 13.09 ? 20  PHE C CA  1 
ATOM   4420 C  C   . PHE C 1 20  ? 20.264  25.684  52.867  1.00 13.12 ? 20  PHE C C   1 
ATOM   4421 O  O   . PHE C 1 20  ? 20.426  24.671  53.572  1.00 12.43 ? 20  PHE C O   1 
ATOM   4422 C  CB  . PHE C 1 20  ? 17.846  25.778  53.573  1.00 11.98 ? 20  PHE C CB  1 
ATOM   4423 C  CG  . PHE C 1 20  ? 16.456  26.174  53.135  1.00 13.52 ? 20  PHE C CG  1 
ATOM   4424 C  CD1 . PHE C 1 20  ? 16.050  27.468  53.313  1.00 18.44 ? 20  PHE C CD1 1 
ATOM   4425 C  CD2 . PHE C 1 20  ? 15.565  25.242  52.478  1.00 14.51 ? 20  PHE C CD2 1 
ATOM   4426 C  CE1 . PHE C 1 20  ? 14.753  27.856  52.890  1.00 18.10 ? 20  PHE C CE1 1 
ATOM   4427 C  CE2 . PHE C 1 20  ? 14.285  25.628  52.047  1.00 17.17 ? 20  PHE C CE2 1 
ATOM   4428 C  CZ  . PHE C 1 20  ? 13.899  26.943  52.316  1.00 17.12 ? 20  PHE C CZ  1 
ATOM   4429 N  N   . PRO C 1 21  ? 21.348  26.286  52.292  1.00 12.55 ? 21  PRO C N   1 
ATOM   4430 C  CA  . PRO C 1 21  ? 22.690  25.756  52.464  1.00 12.35 ? 21  PRO C CA  1 
ATOM   4431 C  C   . PRO C 1 21  ? 23.173  25.680  53.946  1.00 12.22 ? 21  PRO C C   1 
ATOM   4432 O  O   . PRO C 1 21  ? 24.097  24.922  54.230  1.00 13.73 ? 21  PRO C O   1 
ATOM   4433 C  CB  . PRO C 1 21  ? 23.608  26.681  51.638  1.00 15.98 ? 21  PRO C CB  1 
ATOM   4434 C  CG  . PRO C 1 21  ? 22.693  27.774  51.243  1.00 20.59 ? 21  PRO C CG  1 
ATOM   4435 C  CD  . PRO C 1 21  ? 21.281  27.299  51.242  1.00 16.63 ? 21  PRO C CD  1 
ATOM   4436 N  N   A ILE C 1 22  ? 22.573  26.438  54.886  0.50 12.79 ? 22  ILE C N   1 
ATOM   4437 N  N   B ILE C 1 22  ? 22.465  26.407  54.836  0.50 11.12 ? 22  ILE C N   1 
ATOM   4438 C  CA  A ILE C 1 22  ? 22.944  26.308  56.301  0.50 12.90 ? 22  ILE C CA  1 
ATOM   4439 C  CA  B ILE C 1 22  ? 22.720  26.386  56.259  0.50 11.37 ? 22  ILE C CA  1 
ATOM   4440 C  C   A ILE C 1 22  ? 22.553  24.905  56.805  0.50 11.94 ? 22  ILE C C   1 
ATOM   4441 C  C   B ILE C 1 22  ? 22.466  24.967  56.806  0.50 10.86 ? 22  ILE C C   1 
ATOM   4442 O  O   A ILE C 1 22  ? 22.972  24.573  57.920  0.50 12.81 ? 22  ILE C O   1 
ATOM   4443 O  O   B ILE C 1 22  ? 22.974  24.660  57.896  0.50 12.21 ? 22  ILE C O   1 
ATOM   4444 C  CB  A ILE C 1 22  ? 22.238  27.345  57.187  0.50 14.51 ? 22  ILE C CB  1 
ATOM   4445 C  CB  B ILE C 1 22  ? 21.941  27.513  56.998  0.50 11.91 ? 22  ILE C CB  1 
ATOM   4446 C  CG1 A ILE C 1 22  ? 22.988  27.560  58.519  0.50 16.64 ? 22  ILE C CG1 1 
ATOM   4447 C  CG1 B ILE C 1 22  ? 22.599  27.824  58.347  0.50 9.94  ? 22  ILE C CG1 1 
ATOM   4448 C  CG2 A ILE C 1 22  ? 20.796  26.899  57.432  0.50 15.58 ? 22  ILE C CG2 1 
ATOM   4449 C  CG2 B ILE C 1 22  ? 20.452  27.202  57.139  0.50 9.14  ? 22  ILE C CG2 1 
ATOM   4450 C  CD1 A ILE C 1 22  ? 24.159  28.524  58.493  0.50 16.23 ? 22  ILE C CD1 1 
ATOM   4451 C  CD1 B ILE C 1 22  ? 21.983  28.951  59.145  0.50 11.11 ? 22  ILE C CD1 1 
ATOM   4452 N  N   . ALA C 1 23  ? 21.811  24.075  56.028  1.00 11.20 ? 23  ALA C N   1 
ATOM   4453 C  CA  . ALA C 1 23  ? 21.581  22.685  56.451  1.00 11.19 ? 23  ALA C CA  1 
ATOM   4454 C  C   . ALA C 1 23  ? 22.854  21.983  56.812  1.00 11.54 ? 23  ALA C C   1 
ATOM   4455 O  O   . ALA C 1 23  ? 22.844  20.977  57.558  1.00 11.99 ? 23  ALA C O   1 
ATOM   4456 C  CB  . ALA C 1 23  ? 20.805  21.892  55.318  1.00 12.33 ? 23  ALA C CB  1 
ATOM   4457 N  N   . LYS C 1 24  ? 24.002  22.397  56.205  1.00 12.33 ? 24  LYS C N   1 
ATOM   4458 C  CA  . LYS C 1 24  ? 25.319  21.794  56.499  1.00 11.94 ? 24  LYS C CA  1 
ATOM   4459 C  C   . LYS C 1 24  ? 26.135  22.713  57.378  1.00 14.79 ? 24  LYS C C   1 
ATOM   4460 O  O   . LYS C 1 24  ? 27.374  22.546  57.414  1.00 15.85 ? 24  LYS C O   1 
ATOM   4461 C  CB  . LYS C 1 24  ? 26.104  21.495  55.161  1.00 14.56 ? 24  LYS C CB  1 
ATOM   4462 C  CG  . LYS C 1 24  ? 25.359  20.578  54.270  1.00 17.23 ? 24  LYS C CG  1 
ATOM   4463 C  CD  . LYS C 1 24  ? 26.199  20.312  53.021  1.00 19.39 ? 24  LYS C CD  1 
ATOM   4464 C  CE  . LYS C 1 24  ? 25.493  19.333  52.065  1.00 20.35 ? 24  LYS C CE  1 
ATOM   4465 N  NZ  . LYS C 1 24  ? 25.817  17.987  52.556  1.00 30.44 ? 24  LYS C NZ  1 
ATOM   4466 N  N   . GLY C 1 25  ? 25.483  23.539  58.220  1.00 14.33 ? 25  GLY C N   1 
ATOM   4467 C  CA  . GLY C 1 25  ? 26.085  24.517  59.039  1.00 14.80 ? 25  GLY C CA  1 
ATOM   4468 C  C   . GLY C 1 25  ? 26.766  23.918  60.284  1.00 12.34 ? 25  GLY C C   1 
ATOM   4469 O  O   . GLY C 1 25  ? 26.830  22.707  60.538  1.00 13.87 ? 25  GLY C O   1 
ATOM   4470 N  N   . GLU C 1 26  ? 27.262  24.800  61.125  1.00 13.19 ? 26  GLU C N   1 
ATOM   4471 C  CA  . GLU C 1 26  ? 28.009  24.406  62.304  1.00 13.33 ? 26  GLU C CA  1 
ATOM   4472 C  C   . GLU C 1 26  ? 27.204  24.182  63.559  1.00 13.27 ? 26  GLU C C   1 
ATOM   4473 O  O   . GLU C 1 26  ? 27.754  23.640  64.534  1.00 14.23 ? 26  GLU C O   1 
ATOM   4474 C  CB  . GLU C 1 26  ? 29.022  25.566  62.647  1.00 15.39 ? 26  GLU C CB  1 
ATOM   4475 C  CG  . GLU C 1 26  ? 30.057  25.813  61.550  1.00 17.53 ? 26  GLU C CG  1 
ATOM   4476 C  CD  . GLU C 1 26  ? 30.851  24.537  61.132  1.00 25.23 ? 26  GLU C CD  1 
ATOM   4477 O  OE1 . GLU C 1 26  ? 31.410  23.836  62.022  1.00 30.13 ? 26  GLU C OE1 1 
ATOM   4478 O  OE2 . GLU C 1 26  ? 30.890  24.193  59.916  1.00 38.18 ? 26  GLU C OE2 1 
ATOM   4479 N  N   . ARG C 1 27  ? 25.907  24.494  63.568  1.00 11.72 ? 27  ARG C N   1 
ATOM   4480 C  CA  . ARG C 1 27  ? 25.136  24.251  64.813  1.00 9.75  ? 27  ARG C CA  1 
ATOM   4481 C  C   . ARG C 1 27  ? 23.720  23.768  64.388  1.00 10.20 ? 27  ARG C C   1 
ATOM   4482 O  O   . ARG C 1 27  ? 22.668  24.355  64.812  1.00 10.20 ? 27  ARG C O   1 
ATOM   4483 C  CB  . ARG C 1 27  ? 25.104  25.466  65.755  1.00 14.11 ? 27  ARG C CB  1 
ATOM   4484 C  CG  . ARG C 1 27  ? 24.640  26.766  65.166  1.00 14.80 ? 27  ARG C CG  1 
ATOM   4485 C  CD  . ARG C 1 27  ? 24.500  27.954  66.133  1.00 18.34 ? 27  ARG C CD  1 
ATOM   4486 N  NE  . ARG C 1 27  ? 23.236  27.880  66.940  1.00 16.02 ? 27  ARG C NE  1 
ATOM   4487 C  CZ  . ARG C 1 27  ? 22.842  28.778  67.824  1.00 13.08 ? 27  ARG C CZ  1 
ATOM   4488 N  NH1 . ARG C 1 27  ? 23.544  29.908  68.072  1.00 17.42 ? 27  ARG C NH1 1 
ATOM   4489 N  NH2 . ARG C 1 27  ? 21.757  28.593  68.457  1.00 15.23 ? 27  ARG C NH2 1 
ATOM   4490 N  N   . GLN C 1 28  ? 23.660  22.673  63.591  1.00 10.15 ? 28  GLN C N   1 
ATOM   4491 C  CA  . GLN C 1 28  ? 22.333  22.165  63.108  1.00 10.37 ? 28  GLN C CA  1 
ATOM   4492 C  C   . GLN C 1 28  ? 21.732  21.209  64.148  1.00 8.73  ? 28  GLN C C   1 
ATOM   4493 O  O   . GLN C 1 28  ? 22.410  20.515  64.921  1.00 9.31  ? 28  GLN C O   1 
ATOM   4494 C  CB  . GLN C 1 28  ? 22.549  21.478  61.751  1.00 10.30 ? 28  GLN C CB  1 
ATOM   4495 C  CG  . GLN C 1 28  ? 22.834  22.531  60.667  1.00 10.56 ? 28  GLN C CG  1 
ATOM   4496 C  CD  . GLN C 1 28  ? 21.574  23.343  60.359  1.00 9.24  ? 28  GLN C CD  1 
ATOM   4497 O  OE1 . GLN C 1 28  ? 20.597  22.806  59.855  1.00 9.41  ? 28  GLN C OE1 1 
ATOM   4498 N  NE2 . GLN C 1 28  ? 21.544  24.625  60.708  1.00 9.42  ? 28  GLN C NE2 1 
ATOM   4499 N  N   . SER C 1 29  ? 20.419  21.118  64.069  1.00 7.74  ? 29  SER C N   1 
ATOM   4500 C  CA  . SER C 1 29  ? 19.639  20.232  64.950  1.00 7.94  ? 29  SER C CA  1 
ATOM   4501 C  C   . SER C 1 29  ? 18.742  19.350  64.059  1.00 8.15  ? 29  SER C C   1 
ATOM   4502 O  O   . SER C 1 29  ? 18.415  19.708  62.908  1.00 8.59  ? 29  SER C O   1 
ATOM   4503 C  CB  . SER C 1 29  ? 18.711  21.071  65.833  1.00 8.28  ? 29  SER C CB  1 
ATOM   4504 O  OG  . SER C 1 29  ? 19.521  21.816  66.787  1.00 8.66  ? 29  SER C OG  1 
ATOM   4505 N  N   . PRO C 1 30  ? 18.268  18.243  64.600  1.00 7.61  ? 30  PRO C N   1 
ATOM   4506 C  CA  . PRO C 1 30  ? 18.570  17.698  65.960  1.00 7.30  ? 30  PRO C CA  1 
ATOM   4507 C  C   . PRO C 1 30  ? 19.937  17.019  65.996  1.00 7.15  ? 30  PRO C C   1 
ATOM   4508 O  O   . PRO C 1 30  ? 20.647  16.981  64.985  1.00 7.69  ? 30  PRO C O   1 
ATOM   4509 C  CB  . PRO C 1 30  ? 17.470  16.670  66.131  1.00 7.72  ? 30  PRO C CB  1 
ATOM   4510 C  CG  . PRO C 1 30  ? 17.329  16.096  64.739  1.00 8.11  ? 30  PRO C CG  1 
ATOM   4511 C  CD  . PRO C 1 30  ? 17.451  17.287  63.776  1.00 8.31  ? 30  PRO C CD  1 
ATOM   4512 N  N   . VAL C 1 31  ? 20.280  16.445  67.150  1.00 7.67  ? 31  VAL C N   1 
ATOM   4513 C  CA  . VAL C 1 31  ? 21.506  15.689  67.385  1.00 8.07  ? 31  VAL C CA  1 
ATOM   4514 C  C   . VAL C 1 31  ? 21.165  14.496  68.186  1.00 8.27  ? 31  VAL C C   1 
ATOM   4515 O  O   . VAL C 1 31  ? 20.138  14.386  68.867  1.00 9.16  ? 31  VAL C O   1 
ATOM   4516 C  CB  . VAL C 1 31  ? 22.636  16.521  68.096  1.00 9.35  ? 31  VAL C CB  1 
ATOM   4517 C  CG1 . VAL C 1 31  ? 22.953  17.730  67.237  1.00 10.79 ? 31  VAL C CG1 1 
ATOM   4518 C  CG2 . VAL C 1 31  ? 22.205  16.934  69.511  1.00 10.08 ? 31  VAL C CG2 1 
ATOM   4519 N  N   . ASP C 1 32  ? 22.089  13.509  68.112  1.00 8.94  ? 32  ASP C N   1 
ATOM   4520 C  CA  . ASP C 1 32  ? 22.117  12.421  69.079  1.00 9.05  ? 32  ASP C CA  1 
ATOM   4521 C  C   . ASP C 1 32  ? 22.649  12.921  70.403  1.00 8.86  ? 32  ASP C C   1 
ATOM   4522 O  O   . ASP C 1 32  ? 23.709  13.548  70.450  1.00 12.03 ? 32  ASP C O   1 
ATOM   4523 C  CB  . ASP C 1 32  ? 22.910  11.239  68.578  1.00 10.48 ? 32  ASP C CB  1 
ATOM   4524 C  CG  . ASP C 1 32  ? 22.856  10.106  69.549  1.00 10.75 ? 32  ASP C CG  1 
ATOM   4525 O  OD1 . ASP C 1 32  ? 21.780  9.633   69.960  1.00 10.42 ? 32  ASP C OD1 1 
ATOM   4526 O  OD2 . ASP C 1 32  ? 23.963  9.639   69.969  1.00 12.73 ? 32  ASP C OD2 1 
ATOM   4527 N  N   . ILE C 1 33  ? 21.968  12.639  71.479  1.00 8.92  ? 33  ILE C N   1 
ATOM   4528 C  CA  . ILE C 1 33  ? 22.458  13.046  72.807  1.00 9.92  ? 33  ILE C CA  1 
ATOM   4529 C  C   . ILE C 1 33  ? 23.159  11.801  73.374  1.00 10.08 ? 33  ILE C C   1 
ATOM   4530 O  O   . ILE C 1 33  ? 22.547  10.828  73.749  1.00 11.08 ? 33  ILE C O   1 
ATOM   4531 C  CB  . ILE C 1 33  ? 21.305  13.486  73.697  1.00 9.74  ? 33  ILE C CB  1 
ATOM   4532 C  CG1 . ILE C 1 33  ? 20.515  14.671  73.067  1.00 10.22 ? 33  ILE C CG1 1 
ATOM   4533 C  CG2 . ILE C 1 33  ? 21.739  13.748  75.139  1.00 11.27 ? 33  ILE C CG2 1 
ATOM   4534 C  CD1 . ILE C 1 33  ? 19.204  15.007  73.768  1.00 12.50 ? 33  ILE C CD1 1 
ATOM   4535 N  N   . ASP C 1 34  ? 24.486  11.899  73.430  1.00 11.94 ? 34  ASP C N   1 
ATOM   4536 C  CA  . ASP C 1 34  ? 25.309  10.805  74.021  1.00 13.40 ? 34  ASP C CA  1 
ATOM   4537 C  C   . ASP C 1 34  ? 25.323  11.101  75.505  1.00 13.50 ? 34  ASP C C   1 
ATOM   4538 O  O   . ASP C 1 34  ? 25.976  12.091  75.941  1.00 15.29 ? 34  ASP C O   1 
ATOM   4539 C  CB  . ASP C 1 34  ? 26.738  10.792  73.345  1.00 13.72 ? 34  ASP C CB  1 
ATOM   4540 C  CG  . ASP C 1 34  ? 27.721  9.766   73.975  1.00 17.83 ? 34  ASP C CG  1 
ATOM   4541 O  OD1 . ASP C 1 34  ? 27.516  9.436   75.119  1.00 17.88 ? 34  ASP C OD1 1 
ATOM   4542 O  OD2 . ASP C 1 34  ? 28.633  9.237   73.300  1.00 24.08 ? 34  ASP C OD2 1 
ATOM   4543 N  N   . THR C 1 35  ? 24.565  10.355  76.259  1.00 12.39 ? 35  THR C N   1 
ATOM   4544 C  CA  . THR C 1 35  ? 24.396  10.695  77.646  1.00 13.75 ? 35  THR C CA  1 
ATOM   4545 C  C   . THR C 1 35  ? 25.662  10.568  78.458  1.00 17.04 ? 35  THR C C   1 
ATOM   4546 O  O   . THR C 1 35  ? 25.734  11.118  79.590  1.00 18.09 ? 35  THR C O   1 
ATOM   4547 C  CB  . THR C 1 35  ? 23.341  9.819   78.247  1.00 14.48 ? 35  THR C CB  1 
ATOM   4548 O  OG1 . THR C 1 35  ? 23.738  8.449   78.301  1.00 16.63 ? 35  THR C OG1 1 
ATOM   4549 C  CG2 . THR C 1 35  ? 21.978  9.952   77.489  1.00 17.35 ? 35  THR C CG2 1 
ATOM   4550 N  N   . HIS C 1 36  ? 26.663  9.842   77.928  1.00 17.34 ? 36  HIS C N   1 
ATOM   4551 C  CA  . HIS C 1 36  ? 27.961  9.614   78.638  1.00 17.36 ? 36  HIS C CA  1 
ATOM   4552 C  C   . HIS C 1 36  ? 29.025  10.602  78.242  1.00 21.88 ? 36  HIS C C   1 
ATOM   4553 O  O   . HIS C 1 36  ? 30.166  10.647  78.791  1.00 26.36 ? 36  HIS C O   1 
ATOM   4554 C  CB  . HIS C 1 36  ? 28.451  8.187   78.312  1.00 21.64 ? 36  HIS C CB  1 
ATOM   4555 C  CG  . HIS C 1 36  ? 27.450  7.108   78.651  1.00 20.41 ? 36  HIS C CG  1 
ATOM   4556 N  ND1 . HIS C 1 36  ? 27.141  6.779   79.920  1.00 23.99 ? 36  HIS C ND1 1 
ATOM   4557 C  CD2 . HIS C 1 36  ? 26.682  6.280   77.833  1.00 24.43 ? 36  HIS C CD2 1 
ATOM   4558 C  CE1 . HIS C 1 36  ? 26.226  5.792   79.917  1.00 24.68 ? 36  HIS C CE1 1 
ATOM   4559 N  NE2 . HIS C 1 36  ? 25.945  5.488   78.639  1.00 25.44 ? 36  HIS C NE2 1 
ATOM   4560 N  N   . THR C 1 37  ? 28.750  11.457  77.300  1.00 17.15 ? 37  THR C N   1 
ATOM   4561 C  CA  . THR C 1 37  ? 29.683  12.552  77.074  1.00 16.88 ? 37  THR C CA  1 
ATOM   4562 C  C   . THR C 1 37  ? 29.050  13.943  77.421  1.00 19.41 ? 37  THR C C   1 
ATOM   4563 O  O   . THR C 1 37  ? 29.767  14.949  77.436  1.00 21.00 ? 37  THR C O   1 
ATOM   4564 C  CB  . THR C 1 37  ? 30.371  12.537  75.700  1.00 28.33 ? 37  THR C CB  1 
ATOM   4565 O  OG1 . THR C 1 37  ? 29.395  12.602  74.710  1.00 27.15 ? 37  THR C OG1 1 
ATOM   4566 C  CG2 . THR C 1 37  ? 31.054  11.211  75.443  1.00 23.19 ? 37  THR C CG2 1 
ATOM   4567 N  N   . ALA C 1 38  ? 27.740  13.958  77.725  1.00 14.89 ? 38  ALA C N   1 
ATOM   4568 C  CA  . ALA C 1 38  ? 27.081  15.166  78.183  1.00 15.76 ? 38  ALA C CA  1 
ATOM   4569 C  C   . ALA C 1 38  ? 27.655  15.526  79.502  1.00 18.06 ? 38  ALA C C   1 
ATOM   4570 O  O   . ALA C 1 38  ? 27.899  14.690  80.311  1.00 19.20 ? 38  ALA C O   1 
ATOM   4571 C  CB  . ALA C 1 38  ? 25.541  14.991  78.321  1.00 16.15 ? 38  ALA C CB  1 
ATOM   4572 N  N   . LYS C 1 39  ? 27.974  16.811  79.642  1.00 14.69 ? 39  LYS C N   1 
ATOM   4573 C  CA  . LYS C 1 39  ? 28.615  17.257  80.875  1.00 17.00 ? 39  LYS C CA  1 
ATOM   4574 C  C   . LYS C 1 39  ? 27.574  17.784  81.914  1.00 16.57 ? 39  LYS C C   1 
ATOM   4575 O  O   . LYS C 1 39  ? 26.932  18.777  81.651  1.00 15.65 ? 39  LYS C O   1 
ATOM   4576 C  CB  . LYS C 1 39  ? 29.597  18.371  80.524  1.00 21.39 ? 39  LYS C CB  1 
ATOM   4577 C  CG  . LYS C 1 39  ? 30.140  19.160  81.695  1.00 25.68 ? 39  LYS C CG  1 
ATOM   4578 C  CD  . LYS C 1 39  ? 31.296  18.413  82.391  1.00 22.95 ? 39  LYS C CD  1 
ATOM   4579 C  CE  . LYS C 1 39  ? 31.789  19.177  83.593  1.00 26.51 ? 39  LYS C CE  1 
ATOM   4580 N  NZ  . LYS C 1 39  ? 32.940  18.456  84.129  1.00 26.07 ? 39  LYS C NZ  1 
ATOM   4581 N  N   . TYR C 1 40  ? 27.582  17.215  83.140  1.00 16.35 ? 40  TYR C N   1 
ATOM   4582 C  CA  . TYR C 1 40  ? 26.766  17.720  84.258  1.00 17.95 ? 40  TYR C CA  1 
ATOM   4583 C  C   . TYR C 1 40  ? 27.242  19.150  84.574  1.00 17.32 ? 40  TYR C C   1 
ATOM   4584 O  O   . TYR C 1 40  ? 28.426  19.383  84.903  1.00 19.11 ? 40  TYR C O   1 
ATOM   4585 C  CB  . TYR C 1 40  ? 26.746  16.751  85.485  1.00 22.15 ? 40  TYR C CB  1 
ATOM   4586 C  CG  . TYR C 1 40  ? 26.192  17.418  86.697  1.00 22.81 ? 40  TYR C CG  1 
ATOM   4587 C  CD1 . TYR C 1 40  ? 24.883  17.889  86.697  1.00 22.27 ? 40  TYR C CD1 1 
ATOM   4588 C  CD2 . TYR C 1 40  ? 26.974  17.561  87.895  1.00 32.09 ? 40  TYR C CD2 1 
ATOM   4589 C  CE1 . TYR C 1 40  ? 24.315  18.482  87.819  1.00 25.59 ? 40  TYR C CE1 1 
ATOM   4590 C  CE2 . TYR C 1 40  ? 26.414  18.183  89.015  1.00 36.59 ? 40  TYR C CE2 1 
ATOM   4591 C  CZ  . TYR C 1 40  ? 25.090  18.655  88.978  1.00 30.62 ? 40  TYR C CZ  1 
ATOM   4592 O  OH  . TYR C 1 40  ? 24.545  19.291  90.075  1.00 33.41 ? 40  TYR C OH  1 
ATOM   4593 N  N   . ASP C 1 41  ? 26.342  20.108  84.556  1.00 16.26 ? 41  ASP C N   1 
ATOM   4594 C  CA  . ASP C 1 41  ? 26.716  21.468  84.905  1.00 18.32 ? 41  ASP C CA  1 
ATOM   4595 C  C   . ASP C 1 41  ? 25.978  21.894  86.168  1.00 24.36 ? 41  ASP C C   1 
ATOM   4596 O  O   . ASP C 1 41  ? 24.822  22.281  86.073  1.00 22.26 ? 41  ASP C O   1 
ATOM   4597 C  CB  . ASP C 1 41  ? 26.471  22.429  83.735  1.00 26.36 ? 41  ASP C CB  1 
ATOM   4598 C  CG  . ASP C 1 41  ? 27.121  23.777  83.970  1.00 32.71 ? 41  ASP C CG  1 
ATOM   4599 O  OD1 . ASP C 1 41  ? 27.463  24.020  85.158  1.00 30.79 ? 41  ASP C OD1 1 
ATOM   4600 O  OD2 . ASP C 1 41  ? 27.318  24.568  83.005  1.00 32.62 ? 41  ASP C OD2 1 
ATOM   4601 N  N   . PRO C 1 42  ? 26.654  21.836  87.344  1.00 25.95 ? 42  PRO C N   1 
ATOM   4602 C  CA  . PRO C 1 42  ? 26.021  22.190  88.643  1.00 27.08 ? 42  PRO C CA  1 
ATOM   4603 C  C   . PRO C 1 42  ? 25.616  23.690  88.708  1.00 26.15 ? 42  PRO C C   1 
ATOM   4604 O  O   . PRO C 1 42  ? 24.750  24.086  89.569  1.00 30.77 ? 42  PRO C O   1 
ATOM   4605 C  CB  . PRO C 1 42  ? 27.123  21.855  89.650  1.00 31.23 ? 42  PRO C CB  1 
ATOM   4606 C  CG  . PRO C 1 42  ? 28.403  22.033  88.865  1.00 31.97 ? 42  PRO C CG  1 
ATOM   4607 C  CD  . PRO C 1 42  ? 28.056  21.372  87.552  1.00 24.96 ? 42  PRO C CD  1 
ATOM   4608 N  N   . SER C 1 43  ? 26.234  24.520  87.834  1.00 22.06 ? 43  SER C N   1 
ATOM   4609 C  CA  . SER C 1 43  ? 25.883  25.949  87.758  1.00 27.46 ? 43  SER C CA  1 
ATOM   4610 C  C   . SER C 1 43  ? 24.567  26.232  86.932  1.00 27.86 ? 43  SER C C   1 
ATOM   4611 O  O   . SER C 1 43  ? 24.002  27.355  87.026  1.00 38.46 ? 43  SER C O   1 
ATOM   4612 C  CB  . SER C 1 43  ? 27.052  26.705  87.154  1.00 37.43 ? 43  SER C CB  1 
ATOM   4613 O  OG  . SER C 1 43  ? 26.894  26.821  85.764  1.00 31.88 ? 43  SER C OG  1 
ATOM   4614 N  N   . LEU C 1 44  ? 24.059  25.233  86.166  1.00 23.56 ? 44  LEU C N   1 
ATOM   4615 C  CA  . LEU C 1 44  ? 22.767  25.404  85.464  1.00 29.53 ? 44  LEU C CA  1 
ATOM   4616 C  C   . LEU C 1 44  ? 21.624  25.526  86.481  1.00 35.11 ? 44  LEU C C   1 
ATOM   4617 O  O   . LEU C 1 44  ? 21.588  24.854  87.512  1.00 31.08 ? 44  LEU C O   1 
ATOM   4618 C  CB  . LEU C 1 44  ? 22.476  24.260  84.494  1.00 24.76 ? 44  LEU C CB  1 
ATOM   4619 C  CG  . LEU C 1 44  ? 23.181  24.217  83.128  1.00 21.62 ? 44  LEU C CG  1 
ATOM   4620 C  CD1 . LEU C 1 44  ? 23.025  22.781  82.617  1.00 21.55 ? 44  LEU C CD1 1 
ATOM   4621 C  CD2 . LEU C 1 44  ? 22.752  25.253  82.106  1.00 22.45 ? 44  LEU C CD2 1 
ATOM   4622 N  N   . LYS C 1 45  ? 20.696  26.420  86.193  1.00 31.60 ? 45  LYS C N   1 
ATOM   4623 C  CA  . LYS C 1 45  ? 19.575  26.633  87.102  1.00 33.85 ? 45  LYS C CA  1 
ATOM   4624 C  C   . LYS C 1 45  ? 18.439  25.682  86.785  1.00 30.10 ? 45  LYS C C   1 
ATOM   4625 O  O   . LYS C 1 45  ? 18.451  25.045  85.648  1.00 28.92 ? 45  LYS C O   1 
ATOM   4626 C  CB  . LYS C 1 45  ? 19.140  28.023  86.906  1.00 25.44 ? 45  LYS C CB  1 
ATOM   4627 C  CG  . LYS C 1 45  ? 20.322  28.973  86.689  1.00 60.05 ? 45  LYS C CG  1 
ATOM   4628 C  CD  . LYS C 1 45  ? 20.745  29.711  87.946  1.00 54.89 ? 45  LYS C CD  1 
ATOM   4629 C  CE  . LYS C 1 45  ? 20.401  31.196  87.847  1.00 60.85 ? 45  LYS C CE  1 
ATOM   4630 N  NZ  . LYS C 1 45  ? 18.969  31.431  87.497  1.00 54.66 ? 45  LYS C NZ  1 
ATOM   4631 N  N   . PRO C 1 46  ? 17.463  25.542  87.753  1.00 22.82 ? 46  PRO C N   1 
ATOM   4632 C  CA  . PRO C 1 46  ? 16.284  24.774  87.415  1.00 21.91 ? 46  PRO C CA  1 
ATOM   4633 C  C   . PRO C 1 46  ? 15.659  25.525  86.272  1.00 18.76 ? 46  PRO C C   1 
ATOM   4634 O  O   . PRO C 1 46  ? 15.739  26.741  86.243  1.00 19.72 ? 46  PRO C O   1 
ATOM   4635 C  CB  . PRO C 1 46  ? 15.417  24.835  88.723  1.00 23.69 ? 46  PRO C CB  1 
ATOM   4636 C  CG  . PRO C 1 46  ? 16.427  24.888  89.802  1.00 25.82 ? 46  PRO C CG  1 
ATOM   4637 C  CD  . PRO C 1 46  ? 17.566  25.714  89.224  1.00 24.04 ? 46  PRO C CD  1 
ATOM   4638 N  N   . LEU C 1 47  ? 14.988  24.777  85.428  1.00 23.12 ? 47  LEU C N   1 
ATOM   4639 C  CA  . LEU C 1 47  ? 14.261  25.427  84.420  1.00 20.33 ? 47  LEU C CA  1 
ATOM   4640 C  C   . LEU C 1 47  ? 13.047  26.063  85.138  1.00 21.29 ? 47  LEU C C   1 
ATOM   4641 O  O   . LEU C 1 47  ? 12.442  25.433  86.035  1.00 23.41 ? 47  LEU C O   1 
ATOM   4642 C  CB  . LEU C 1 47  ? 13.827  24.321  83.475  1.00 27.39 ? 47  LEU C CB  1 
ATOM   4643 C  CG  . LEU C 1 47  ? 13.362  24.690  82.128  1.00 26.32 ? 47  LEU C CG  1 
ATOM   4644 C  CD1 . LEU C 1 47  ? 14.474  25.560  81.462  1.00 26.03 ? 47  LEU C CD1 1 
ATOM   4645 C  CD2 . LEU C 1 47  ? 13.011  23.389  81.369  1.00 22.08 ? 47  LEU C CD2 1 
ATOM   4646 N  N   . SER C 1 48  ? 12.615  27.239  84.690  1.00 15.24 ? 48  SER C N   1 
ATOM   4647 C  CA  . SER C 1 48  ? 11.331  27.803  85.134  1.00 15.25 ? 48  SER C CA  1 
ATOM   4648 C  C   . SER C 1 48  ? 10.365  27.796  83.940  1.00 15.06 ? 48  SER C C   1 
ATOM   4649 O  O   . SER C 1 48  ? 10.574  28.481  82.904  1.00 16.03 ? 48  SER C O   1 
ATOM   4650 C  CB  . SER C 1 48  ? 11.618  29.251  85.572  1.00 17.61 ? 48  SER C CB  1 
ATOM   4651 O  OG  . SER C 1 48  ? 10.434  29.999  85.855  1.00 18.97 ? 48  SER C OG  1 
ATOM   4652 N  N   . VAL C 1 49  ? 9.306   27.052  84.067  1.00 17.05 ? 49  VAL C N   1 
ATOM   4653 C  CA  . VAL C 1 49  ? 8.269   26.946  83.051  1.00 15.35 ? 49  VAL C CA  1 
ATOM   4654 C  C   . VAL C 1 49  ? 6.988   27.502  83.646  1.00 17.89 ? 49  VAL C C   1 
ATOM   4655 O  O   . VAL C 1 49  ? 6.437   26.901  84.573  1.00 23.79 ? 49  VAL C O   1 
ATOM   4656 C  CB  . VAL C 1 49  ? 8.021   25.470  82.614  1.00 17.60 ? 49  VAL C CB  1 
ATOM   4657 C  CG1 . VAL C 1 49  ? 7.107   25.418  81.399  1.00 23.09 ? 49  VAL C CG1 1 
ATOM   4658 C  CG2 . VAL C 1 49  ? 9.341   24.772  82.323  1.00 19.53 ? 49  VAL C CG2 1 
ATOM   4659 N  N   . SER C 1 50  ? 6.504   28.641  83.167  1.00 17.47 ? 50  SER C N   1 
ATOM   4660 C  CA  . SER C 1 50  ? 5.409   29.322  83.826  1.00 17.99 ? 50  SER C CA  1 
ATOM   4661 C  C   . SER C 1 50  ? 4.312   29.445  82.823  1.00 15.00 ? 50  SER C C   1 
ATOM   4662 O  O   . SER C 1 50  ? 4.226   30.441  82.088  1.00 16.79 ? 50  SER C O   1 
ATOM   4663 C  CB  . SER C 1 50  ? 5.757   30.689  84.450  1.00 20.54 ? 50  SER C CB  1 
ATOM   4664 O  OG  . SER C 1 50  ? 6.839   30.498  85.325  1.00 23.78 ? 50  SER C OG  1 
ATOM   4665 N  N   . TYR C 1 51  ? 3.485   28.434  82.735  1.00 14.84 ? 51  TYR C N   1 
ATOM   4666 C  CA  . TYR C 1 51  ? 2.362   28.324  81.791  1.00 14.03 ? 51  TYR C CA  1 
ATOM   4667 C  C   . TYR C 1 51  ? 0.956   28.583  82.320  1.00 16.08 ? 51  TYR C C   1 
ATOM   4668 O  O   . TYR C 1 51  ? -0.024  28.428  81.580  1.00 17.18 ? 51  TYR C O   1 
ATOM   4669 C  CB  . TYR C 1 51  ? 2.369   26.973  81.059  1.00 14.69 ? 51  TYR C CB  1 
ATOM   4670 C  CG  . TYR C 1 51  ? 3.552   26.695  80.126  1.00 13.97 ? 51  TYR C CG  1 
ATOM   4671 C  CD1 . TYR C 1 51  ? 4.406   27.688  79.637  1.00 13.81 ? 51  TYR C CD1 1 
ATOM   4672 C  CD2 . TYR C 1 51  ? 3.777   25.398  79.702  1.00 13.73 ? 51  TYR C CD2 1 
ATOM   4673 C  CE1 . TYR C 1 51  ? 5.464   27.361  78.740  1.00 12.07 ? 51  TYR C CE1 1 
ATOM   4674 C  CE2 . TYR C 1 51  ? 4.841   25.057  78.831  1.00 12.36 ? 51  TYR C CE2 1 
ATOM   4675 C  CZ  . TYR C 1 51  ? 5.616   26.060  78.328  1.00 10.70 ? 51  TYR C CZ  1 
ATOM   4676 O  OH  . TYR C 1 51  ? 6.626   25.715  77.474  1.00 12.55 ? 51  TYR C OH  1 
ATOM   4677 N  N   . ASP C 1 52  ? 0.856   28.998  83.592  1.00 19.60 ? 52  ASP C N   1 
ATOM   4678 C  CA  . ASP C 1 52  ? -0.462  29.312  84.190  1.00 21.21 ? 52  ASP C CA  1 
ATOM   4679 C  C   . ASP C 1 52  ? -1.381  30.272  83.408  1.00 21.54 ? 52  ASP C C   1 
ATOM   4680 O  O   . ASP C 1 52  ? -2.625  30.060  83.327  1.00 28.45 ? 52  ASP C O   1 
ATOM   4681 C  CB  . ASP C 1 52  ? -0.281  29.772  85.658  1.00 22.43 ? 52  ASP C CB  1 
ATOM   4682 C  CG  . ASP C 1 52  ? 0.844   30.789  85.840  1.00 32.85 ? 52  ASP C CG  1 
ATOM   4683 O  OD1 . ASP C 1 52  ? 2.039   30.455  85.501  1.00 46.99 ? 52  ASP C OD1 1 
ATOM   4684 O  OD2 . ASP C 1 52  ? 0.554   31.909  86.395  1.00 53.10 ? 52  ASP C OD2 1 
ATOM   4685 N  N   . GLN C 1 53  ? -0.800  31.271  82.779  1.00 19.75 ? 53  GLN C N   1 
ATOM   4686 C  CA  . GLN C 1 53  ? -1.717  32.191  82.028  1.00 24.47 ? 53  GLN C CA  1 
ATOM   4687 C  C   . GLN C 1 53  ? -1.763  31.928  80.493  1.00 20.37 ? 53  GLN C C   1 
ATOM   4688 O  O   . GLN C 1 53  ? -2.212  32.759  79.696  1.00 20.86 ? 53  GLN C O   1 
ATOM   4689 C  CB  . GLN C 1 53  ? -1.280  33.646  82.293  1.00 23.39 ? 53  GLN C CB  1 
ATOM   4690 C  CG  . GLN C 1 53  ? -1.519  34.093  83.722  1.00 35.82 ? 53  GLN C CG  1 
ATOM   4691 C  CD  . GLN C 1 53  ? -2.999  34.054  83.999  1.00 42.31 ? 53  GLN C CD  1 
ATOM   4692 O  OE1 . GLN C 1 53  ? -3.836  34.589  83.221  1.00 42.36 ? 53  GLN C OE1 1 
ATOM   4693 N  NE2 . GLN C 1 53  ? -3.355  33.371  85.059  1.00 49.00 ? 53  GLN C NE2 1 
ATOM   4694 N  N   . ALA C 1 54  ? -1.271  30.785  80.054  1.00 17.33 ? 54  ALA C N   1 
ATOM   4695 C  CA  . ALA C 1 54  ? -1.164  30.550  78.616  1.00 15.50 ? 54  ALA C CA  1 
ATOM   4696 C  C   . ALA C 1 54  ? -2.511  30.606  77.980  1.00 17.74 ? 54  ALA C C   1 
ATOM   4697 O  O   . ALA C 1 54  ? -3.496  30.093  78.573  1.00 22.18 ? 54  ALA C O   1 
ATOM   4698 C  CB  . ALA C 1 54  ? -0.557  29.151  78.316  1.00 18.87 ? 54  ALA C CB  1 
ATOM   4699 N  N   A THR C 1 55  ? -2.612  31.299  76.827  0.50 15.11 ? 55  THR C N   1 
ATOM   4700 N  N   B THR C 1 55  ? -2.622  31.224  76.809  0.50 14.82 ? 55  THR C N   1 
ATOM   4701 C  CA  A THR C 1 55  ? -3.892  31.404  76.058  0.50 18.14 ? 55  THR C CA  1 
ATOM   4702 C  CA  B THR C 1 55  ? -3.927  31.386  76.168  0.50 17.31 ? 55  THR C CA  1 
ATOM   4703 C  C   A THR C 1 55  ? -3.783  30.860  74.624  0.50 13.40 ? 55  THR C C   1 
ATOM   4704 C  C   B THR C 1 55  ? -3.715  30.846  74.764  0.50 13.83 ? 55  THR C C   1 
ATOM   4705 O  O   A THR C 1 55  ? -3.296  31.474  73.680  0.50 11.82 ? 55  THR C O   1 
ATOM   4706 O  O   B THR C 1 55  ? -3.025  31.487  73.982  0.50 12.04 ? 55  THR C O   1 
ATOM   4707 C  CB  A THR C 1 55  ? -4.620  32.785  76.190  0.50 23.46 ? 55  THR C CB  1 
ATOM   4708 C  CB  B THR C 1 55  ? -4.293  32.888  76.110  0.50 19.15 ? 55  THR C CB  1 
ATOM   4709 O  OG1 A THR C 1 55  ? -5.512  32.998  75.079  0.50 26.96 ? 55  THR C OG1 1 
ATOM   4710 O  OG1 B THR C 1 55  ? -3.297  33.532  75.346  0.50 23.24 ? 55  THR C OG1 1 
ATOM   4711 C  CG2 A THR C 1 55  ? -3.664  33.852  76.249  0.50 17.36 ? 55  THR C CG2 1 
ATOM   4712 C  CG2 B THR C 1 55  ? -4.304  33.505  77.472  0.50 17.53 ? 55  THR C CG2 1 
ATOM   4713 N  N   . SER C 1 56  ? -4.253  29.655  74.459  1.00 13.65 ? 56  SER C N   1 
ATOM   4714 C  CA  . SER C 1 56  ? -4.162  29.066  73.102  1.00 11.50 ? 56  SER C CA  1 
ATOM   4715 C  C   . SER C 1 56  ? -5.236  29.725  72.242  1.00 12.96 ? 56  SER C C   1 
ATOM   4716 O  O   . SER C 1 56  ? -6.270  30.182  72.771  1.00 14.91 ? 56  SER C O   1 
ATOM   4717 C  CB  . SER C 1 56  ? -4.332  27.536  73.115  1.00 13.63 ? 56  SER C CB  1 
ATOM   4718 O  OG  . SER C 1 56  ? -5.620  27.207  73.634  1.00 12.87 ? 56  SER C OG  1 
ATOM   4719 N  N   . LEU C 1 57  ? -4.956  29.795  70.947  1.00 13.39 ? 57  LEU C N   1 
ATOM   4720 C  CA  . LEU C 1 57  ? -5.865  30.386  69.980  1.00 16.20 ? 57  LEU C CA  1 
ATOM   4721 C  C   . LEU C 1 57  ? -6.417  29.438  69.009  1.00 12.60 ? 57  LEU C C   1 
ATOM   4722 O  O   . LEU C 1 57  ? -7.630  29.389  68.737  1.00 14.07 ? 57  LEU C O   1 
ATOM   4723 C  CB  . LEU C 1 57  ? -5.220  31.537  69.217  1.00 18.22 ? 57  LEU C CB  1 
ATOM   4724 C  CG  . LEU C 1 57  ? -4.755  32.729  70.087  1.00 20.51 ? 57  LEU C CG  1 
ATOM   4725 C  CD1 . LEU C 1 57  ? -3.850  33.665  69.260  1.00 26.80 ? 57  LEU C CD1 1 
ATOM   4726 C  CD2 . LEU C 1 57  ? -6.012  33.459  70.566  1.00 31.34 ? 57  LEU C CD2 1 
ATOM   4727 N  N   . ARG C 1 58  ? -5.569  28.645  68.390  1.00 14.09 ? 58  ARG C N   1 
ATOM   4728 C  CA  . ARG C 1 58  ? -5.978  27.953  67.186  1.00 13.28 ? 58  ARG C CA  1 
ATOM   4729 C  C   . ARG C 1 58  ? -5.063  26.830  66.971  1.00 11.00 ? 58  ARG C C   1 
ATOM   4730 O  O   . ARG C 1 58  ? -3.932  26.835  67.467  1.00 11.50 ? 58  ARG C O   1 
ATOM   4731 C  CB  . ARG C 1 58  ? -5.763  28.949  66.025  1.00 15.69 ? 58  ARG C CB  1 
ATOM   4732 C  CG  . ARG C 1 58  ? -6.429  28.604  64.763  1.00 20.57 ? 58  ARG C CG  1 
ATOM   4733 C  CD  . ARG C 1 58  ? -6.203  29.811  63.859  1.00 21.39 ? 58  ARG C CD  1 
ATOM   4734 N  NE  . ARG C 1 58  ? -4.810  29.751  63.363  1.00 18.73 ? 58  ARG C NE  1 
ATOM   4735 C  CZ  . ARG C 1 58  ? -4.397  29.916  62.109  1.00 17.57 ? 58  ARG C CZ  1 
ATOM   4736 N  NH1 . ARG C 1 58  ? -5.251  30.219  61.135  1.00 21.36 ? 58  ARG C NH1 1 
ATOM   4737 N  NH2 . ARG C 1 58  ? -3.096  29.828  61.849  1.00 18.67 ? 58  ARG C NH2 1 
ATOM   4738 N  N   . ILE C 1 59  ? -5.516  25.848  66.200  1.00 11.31 ? 59  ILE C N   1 
ATOM   4739 C  CA  . ILE C 1 59  ? -4.684  24.735  65.762  1.00 10.12 ? 59  ILE C CA  1 
ATOM   4740 C  C   . ILE C 1 59  ? -4.645  24.703  64.222  1.00 10.64 ? 59  ILE C C   1 
ATOM   4741 O  O   . ILE C 1 59  ? -5.699  24.878  63.566  1.00 11.75 ? 59  ILE C O   1 
ATOM   4742 C  CB  . ILE C 1 59  ? -5.117  23.391  66.411  1.00 10.73 ? 59  ILE C CB  1 
ATOM   4743 C  CG1 . ILE C 1 59  ? -4.106  22.227  66.146  1.00 11.32 ? 59  ILE C CG1 1 
ATOM   4744 C  CG2 . ILE C 1 59  ? -6.553  23.023  65.945  1.00 11.95 ? 59  ILE C CG2 1 
ATOM   4745 C  CD1 . ILE C 1 59  ? -4.453  21.001  66.976  1.00 13.23 ? 59  ILE C CD1 1 
ATOM   4746 N  N   . LEU C 1 60  ? -3.503  24.486  63.625  1.00 13.37 ? 60  LEU C N   1 
ATOM   4747 C  CA  . LEU C 1 60  ? -3.347  24.560  62.179  1.00 10.00 ? 60  LEU C CA  1 
ATOM   4748 C  C   . LEU C 1 60  ? -2.618  23.383  61.635  1.00 11.93 ? 60  LEU C C   1 
ATOM   4749 O  O   . LEU C 1 60  ? -1.540  23.051  62.186  1.00 11.71 ? 60  LEU C O   1 
ATOM   4750 C  CB  . LEU C 1 60  ? -2.520  25.874  61.886  1.00 12.89 ? 60  LEU C CB  1 
ATOM   4751 C  CG  . LEU C 1 60  ? -2.077  26.002  60.413  1.00 12.40 ? 60  LEU C CG  1 
ATOM   4752 C  CD1 . LEU C 1 60  ? -3.253  26.263  59.423  1.00 15.01 ? 60  LEU C CD1 1 
ATOM   4753 C  CD2 . LEU C 1 60  ? -0.990  27.132  60.367  1.00 15.87 ? 60  LEU C CD2 1 
ATOM   4754 N  N   . ASN C 1 61  ? -3.118  22.781  60.548  1.00 10.94 ? 61  ASN C N   1 
ATOM   4755 C  CA  . ASN C 1 61  ? -2.347  21.830  59.747  1.00 11.36 ? 61  ASN C CA  1 
ATOM   4756 C  C   . ASN C 1 61  ? -1.575  22.606  58.697  1.00 13.62 ? 61  ASN C C   1 
ATOM   4757 O  O   . ASN C 1 61  ? -2.212  23.201  57.811  1.00 13.55 ? 61  ASN C O   1 
ATOM   4758 C  CB  . ASN C 1 61  ? -3.261  20.755  59.094  1.00 12.79 ? 61  ASN C CB  1 
ATOM   4759 C  CG  . ASN C 1 61  ? -2.522  19.803  58.198  1.00 10.62 ? 61  ASN C CG  1 
ATOM   4760 O  OD1 . ASN C 1 61  ? -1.410  20.080  57.707  1.00 12.20 ? 61  ASN C OD1 1 
ATOM   4761 N  ND2 . ASN C 1 61  ? -3.056  18.562  58.089  1.00 11.84 ? 61  ASN C ND2 1 
ATOM   4762 N  N   . ASN C 1 62  ? -0.239  22.726  58.803  1.00 12.89 ? 62  ASN C N   1 
ATOM   4763 C  CA  . ASN C 1 62  ? 0.539   23.612  57.965  1.00 14.41 ? 62  ASN C CA  1 
ATOM   4764 C  C   . ASN C 1 62  ? 1.164   22.818  56.834  1.00 15.10 ? 62  ASN C C   1 
ATOM   4765 O  O   . ASN C 1 62  ? 1.946   23.370  56.008  1.00 18.85 ? 62  ASN C O   1 
ATOM   4766 C  CB  . ASN C 1 62  ? 1.583   24.389  58.784  1.00 16.88 ? 62  ASN C CB  1 
ATOM   4767 C  CG  . ASN C 1 62  ? 2.567   23.462  59.524  1.00 14.08 ? 62  ASN C CG  1 
ATOM   4768 O  OD1 . ASN C 1 62  ? 2.994   22.475  59.002  1.00 15.16 ? 62  ASN C OD1 1 
ATOM   4769 N  ND2 . ASN C 1 62  ? 2.748   23.675  60.805  1.00 21.96 ? 62  ASN C ND2 1 
ATOM   4770 N  N   . GLY C 1 63  ? 0.819   21.542  56.663  1.00 12.77 ? 63  GLY C N   1 
ATOM   4771 C  CA  . GLY C 1 63  ? 1.353   20.729  55.574  1.00 12.96 ? 63  GLY C CA  1 
ATOM   4772 C  C   . GLY C 1 63  ? 2.623   19.963  55.924  1.00 12.65 ? 63  GLY C C   1 
ATOM   4773 O  O   . GLY C 1 63  ? 3.049   19.132  55.141  1.00 14.45 ? 63  GLY C O   1 
ATOM   4774 N  N   . HIS C 1 64  ? 3.194   20.293  57.096  1.00 12.05 ? 64  HIS C N   1 
ATOM   4775 C  CA  . HIS C 1 64  ? 4.446   19.579  57.597  1.00 11.56 ? 64  HIS C CA  1 
ATOM   4776 C  C   . HIS C 1 64  ? 4.184   18.961  58.942  1.00 11.51 ? 64  HIS C C   1 
ATOM   4777 O  O   . HIS C 1 64  ? 4.637   17.807  59.207  1.00 14.21 ? 64  HIS C O   1 
ATOM   4778 C  CB  . HIS C 1 64  ? 5.596   20.569  57.719  1.00 12.86 ? 64  HIS C CB  1 
ATOM   4779 C  CG  . HIS C 1 64  ? 5.874   21.347  56.419  1.00 14.33 ? 64  HIS C CG  1 
ATOM   4780 N  ND1 . HIS C 1 64  ? 6.383   20.731  55.292  1.00 17.24 ? 64  HIS C ND1 1 
ATOM   4781 C  CD2 . HIS C 1 64  ? 5.709   22.672  56.102  1.00 16.31 ? 64  HIS C CD2 1 
ATOM   4782 C  CE1 . HIS C 1 64  ? 6.569   21.640  54.325  1.00 18.34 ? 64  HIS C CE1 1 
ATOM   4783 N  NE2 . HIS C 1 64  ? 6.151   22.830  54.808  1.00 17.03 ? 64  HIS C NE2 1 
ATOM   4784 N  N   . ALA C 1 65  ? 3.448   19.646  59.784  1.00 12.07 ? 65  ALA C N   1 
ATOM   4785 C  CA  . ALA C 1 65  ? 2.995   19.104  61.081  1.00 11.48 ? 65  ALA C CA  1 
ATOM   4786 C  C   . ALA C 1 65  ? 1.656   19.837  61.396  1.00 11.70 ? 65  ALA C C   1 
ATOM   4787 O  O   . ALA C 1 65  ? 1.157   20.572  60.503  1.00 12.59 ? 65  ALA C O   1 
ATOM   4788 C  CB  . ALA C 1 65  ? 4.076   19.380  62.145  1.00 12.81 ? 65  ALA C CB  1 
ATOM   4789 N  N   . PHE C 1 66  ? 1.210   19.795  62.617  1.00 10.87 ? 66  PHE C N   1 
ATOM   4790 C  CA  . PHE C 1 66  ? 0.197   20.709  63.112  1.00 11.09 ? 66  PHE C CA  1 
ATOM   4791 C  C   . PHE C 1 66  ? 0.766   21.564  64.216  1.00 10.81 ? 66  PHE C C   1 
ATOM   4792 O  O   . PHE C 1 66  ? 1.609   21.061  64.972  1.00 12.33 ? 66  PHE C O   1 
ATOM   4793 C  CB  . PHE C 1 66  ? -1.108  19.952  63.553  1.00 12.41 ? 66  PHE C CB  1 
ATOM   4794 C  CG  . PHE C 1 66  ? -0.954  19.100  64.731  1.00 10.18 ? 66  PHE C CG  1 
ATOM   4795 C  CD1 . PHE C 1 66  ? -1.117  19.594  65.985  1.00 11.17 ? 66  PHE C CD1 1 
ATOM   4796 C  CD2 . PHE C 1 66  ? -0.712  17.740  64.558  1.00 11.76 ? 66  PHE C CD2 1 
ATOM   4797 C  CE1 . PHE C 1 66  ? -0.947  18.799  67.096  1.00 12.29 ? 66  PHE C CE1 1 
ATOM   4798 C  CE2 . PHE C 1 66  ? -0.576  16.920  65.678  1.00 11.64 ? 66  PHE C CE2 1 
ATOM   4799 C  CZ  . PHE C 1 66  ? -0.692  17.420  66.990  1.00 11.21 ? 66  PHE C CZ  1 
ATOM   4800 N  N   . ASN C 1 67  ? 0.330   22.801  64.301  1.00 10.87 ? 67  ASN C N   1 
ATOM   4801 C  CA  . ASN C 1 67  ? 0.790   23.754  65.322  1.00 12.17 ? 67  ASN C CA  1 
ATOM   4802 C  C   . ASN C 1 67  ? -0.377  24.202  66.223  1.00 9.89  ? 67  ASN C C   1 
ATOM   4803 O  O   . ASN C 1 67  ? -1.473  24.572  65.650  1.00 12.88 ? 67  ASN C O   1 
ATOM   4804 C  CB  . ASN C 1 67  ? 1.339   25.080  64.776  1.00 17.37 ? 67  ASN C CB  1 
ATOM   4805 C  CG  . ASN C 1 67  ? 2.365   24.886  63.681  1.00 25.82 ? 67  ASN C CG  1 
ATOM   4806 O  OD1 . ASN C 1 67  ? 2.335   25.572  62.660  1.00 33.88 ? 67  ASN C OD1 1 
ATOM   4807 N  ND2 . ASN C 1 67  ? 3.285   23.955  63.889  1.00 23.03 ? 67  ASN C ND2 1 
ATOM   4808 N  N   . VAL C 1 68  ? -0.182  24.222  67.537  1.00 10.19 ? 68  VAL C N   1 
ATOM   4809 C  CA  . VAL C 1 68  ? -1.129  24.866  68.382  1.00 11.01 ? 68  VAL C CA  1 
ATOM   4810 C  C   . VAL C 1 68  ? -0.523  26.260  68.665  1.00 11.52 ? 68  VAL C C   1 
ATOM   4811 O  O   . VAL C 1 68  ? 0.570   26.330  69.233  1.00 11.52 ? 68  VAL C O   1 
ATOM   4812 C  CB  . VAL C 1 68  ? -1.398  24.070  69.670  1.00 12.18 ? 68  VAL C CB  1 
ATOM   4813 C  CG1 . VAL C 1 68  ? -2.229  24.958  70.643  1.00 14.10 ? 68  VAL C CG1 1 
ATOM   4814 C  CG2 . VAL C 1 68  ? -2.146  22.750  69.369  1.00 14.06 ? 68  VAL C CG2 1 
ATOM   4815 N  N   . GLU C 1 69  ? -1.200  27.320  68.283  1.00 12.39 ? 69  GLU C N   1 
ATOM   4816 C  CA  . GLU C 1 69  ? -0.731  28.719  68.477  1.00 12.25 ? 69  GLU C CA  1 
ATOM   4817 C  C   . GLU C 1 69  ? -1.267  29.331  69.745  1.00 12.56 ? 69  GLU C C   1 
ATOM   4818 O  O   . GLU C 1 69  ? -2.400  29.029  70.215  1.00 13.59 ? 69  GLU C O   1 
ATOM   4819 C  CB  . GLU C 1 69  ? -1.235  29.540  67.316  1.00 14.13 ? 69  GLU C CB  1 
ATOM   4820 C  CG  . GLU C 1 69  ? -0.642  28.972  66.047  1.00 18.34 ? 69  GLU C CG  1 
ATOM   4821 C  CD  . GLU C 1 69  ? -1.466  29.338  64.829  1.00 22.87 ? 69  GLU C CD  1 
ATOM   4822 O  OE1 . GLU C 1 69  ? -2.528  29.945  65.024  1.00 23.11 ? 69  GLU C OE1 1 
ATOM   4823 O  OE2 . GLU C 1 69  ? -1.056  29.022  63.691  1.00 24.95 ? 69  GLU C OE2 1 
ATOM   4824 N  N   . PHE C 1 70  ? -0.451  30.209  70.322  1.00 11.25 ? 70  PHE C N   1 
ATOM   4825 C  CA  . PHE C 1 70  ? -0.778  30.950  71.555  1.00 11.56 ? 70  PHE C CA  1 
ATOM   4826 C  C   . PHE C 1 70  ? -0.803  32.452  71.269  1.00 12.38 ? 70  PHE C C   1 
ATOM   4827 O  O   . PHE C 1 70  ? -0.050  32.952  70.425  1.00 13.49 ? 70  PHE C O   1 
ATOM   4828 C  CB  . PHE C 1 70  ? 0.250   30.586  72.627  1.00 11.91 ? 70  PHE C CB  1 
ATOM   4829 C  CG  . PHE C 1 70  ? 0.021   29.184  73.163  1.00 10.55 ? 70  PHE C CG  1 
ATOM   4830 C  CD1 . PHE C 1 70  ? 0.498   28.079  72.474  1.00 11.21 ? 70  PHE C CD1 1 
ATOM   4831 C  CD2 . PHE C 1 70  ? -0.686  28.973  74.304  1.00 11.04 ? 70  PHE C CD2 1 
ATOM   4832 C  CE1 . PHE C 1 70  ? 0.173   26.773  72.922  1.00 12.60 ? 70  PHE C CE1 1 
ATOM   4833 C  CE2 . PHE C 1 70  ? -1.006  27.711  74.753  1.00 12.54 ? 70  PHE C CE2 1 
ATOM   4834 C  CZ  . PHE C 1 70  ? -0.554  26.570  74.048  1.00 11.79 ? 70  PHE C CZ  1 
ATOM   4835 N  N   . ASP C 1 71  ? -1.598  33.161  72.072  1.00 14.14 ? 71  ASP C N   1 
ATOM   4836 C  CA  . ASP C 1 71  ? -1.543  34.636  72.042  1.00 14.81 ? 71  ASP C CA  1 
ATOM   4837 C  C   . ASP C 1 71  ? -0.286  34.993  72.794  1.00 16.00 ? 71  ASP C C   1 
ATOM   4838 O  O   . ASP C 1 71  ? -0.205  34.816  74.051  1.00 21.29 ? 71  ASP C O   1 
ATOM   4839 C  CB  . ASP C 1 71  ? -2.803  35.191  72.749  1.00 20.82 ? 71  ASP C CB  1 
ATOM   4840 C  CG  . ASP C 1 71  ? -2.826  36.688  72.847  1.00 27.43 ? 71  ASP C CG  1 
ATOM   4841 O  OD1 . ASP C 1 71  ? -1.796  37.302  72.507  1.00 22.22 ? 71  ASP C OD1 1 
ATOM   4842 O  OD2 . ASP C 1 71  ? -3.879  37.201  73.309  1.00 35.54 ? 71  ASP C OD2 1 
ATOM   4843 N  N   . ASP C 1 72  ? 0.698   35.518  72.081  1.00 14.36 ? 72  ASP C N   1 
ATOM   4844 C  CA  . ASP C 1 72  ? 1.998   35.916  72.635  1.00 14.31 ? 72  ASP C CA  1 
ATOM   4845 C  C   . ASP C 1 72  ? 2.122   37.464  72.763  1.00 16.13 ? 72  ASP C C   1 
ATOM   4846 O  O   . ASP C 1 72  ? 3.243   37.972  72.688  1.00 18.68 ? 72  ASP C O   1 
ATOM   4847 C  CB  . ASP C 1 72  ? 3.188   35.304  71.886  1.00 15.94 ? 72  ASP C CB  1 
ATOM   4848 C  CG  . ASP C 1 72  ? 3.312   35.853  70.469  1.00 15.24 ? 72  ASP C CG  1 
ATOM   4849 O  OD1 . ASP C 1 72  ? 2.321   36.539  70.009  1.00 18.14 ? 72  ASP C OD1 1 
ATOM   4850 O  OD2 . ASP C 1 72  ? 4.346   35.695  69.792  1.00 15.85 ? 72  ASP C OD2 1 
ATOM   4851 N  N   . SER C 1 73  ? 0.971   38.146  72.818  1.00 16.00 ? 73  SER C N   1 
ATOM   4852 C  CA  . SER C 1 73  ? 0.972   39.683  72.803  1.00 19.17 ? 73  SER C CA  1 
ATOM   4853 C  C   . SER C 1 73  ? 1.139   40.228  74.209  1.00 19.36 ? 73  SER C C   1 
ATOM   4854 O  O   . SER C 1 73  ? 1.359   41.442  74.354  1.00 17.84 ? 73  SER C O   1 
ATOM   4855 C  CB  . SER C 1 73  ? -0.334  40.177  72.224  1.00 23.00 ? 73  SER C CB  1 
ATOM   4856 O  OG  . SER C 1 73  ? -1.456  39.908  73.062  1.00 20.80 ? 73  SER C OG  1 
ATOM   4857 N  N   . GLN C 1 74  ? 1.042   39.384  75.256  1.00 20.95 ? 74  GLN C N   1 
ATOM   4858 C  CA  . GLN C 1 74  ? 1.347   39.783  76.638  1.00 21.53 ? 74  GLN C CA  1 
ATOM   4859 C  C   . GLN C 1 74  ? 2.309   38.834  77.237  1.00 19.12 ? 74  GLN C C   1 
ATOM   4860 O  O   . GLN C 1 74  ? 2.511   37.733  76.731  1.00 17.16 ? 74  GLN C O   1 
ATOM   4861 C  CB  . GLN C 1 74  ? 0.080   39.843  77.524  1.00 23.91 ? 74  GLN C CB  1 
ATOM   4862 C  CG  . GLN C 1 74  ? -0.938  40.862  77.050  1.00 25.97 ? 74  GLN C CG  1 
ATOM   4863 C  CD  . GLN C 1 74  ? -2.153  40.922  77.945  1.00 33.86 ? 74  GLN C CD  1 
ATOM   4864 O  OE1 . GLN C 1 74  ? -2.047  41.224  79.149  1.00 51.17 ? 74  GLN C OE1 1 
ATOM   4865 N  NE2 . GLN C 1 74  ? -3.309  40.626  77.371  1.00 37.80 ? 74  GLN C NE2 1 
ATOM   4866 N  N   . ASP C 1 75  ? 2.802   39.233  78.415  1.00 20.47 ? 75  ASP C N   1 
ATOM   4867 C  CA  . ASP C 1 75  ? 3.823   38.536  79.118  1.00 20.96 ? 75  ASP C CA  1 
ATOM   4868 C  C   . ASP C 1 75  ? 3.044   37.331  79.864  1.00 22.20 ? 75  ASP C C   1 
ATOM   4869 O  O   . ASP C 1 75  ? 2.669   37.513  81.084  1.00 25.51 ? 75  ASP C O   1 
ATOM   4870 C  CB  . ASP C 1 75  ? 4.457   39.583  80.082  1.00 31.52 ? 75  ASP C CB  1 
ATOM   4871 C  CG  . ASP C 1 75  ? 5.446   38.966  81.108  1.00 35.10 ? 75  ASP C CG  1 
ATOM   4872 O  OD1 . ASP C 1 75  ? 5.908   37.820  80.887  1.00 33.39 ? 75  ASP C OD1 1 
ATOM   4873 O  OD2 . ASP C 1 75  ? 5.756   39.639  82.143  1.00 39.99 ? 75  ASP C OD2 1 
ATOM   4874 N  N   . LYS C 1 76  ? 2.783   36.202  79.173  1.00 21.37 ? 76  LYS C N   1 
ATOM   4875 C  CA  . LYS C 1 76  ? 1.842   35.212  79.729  1.00 24.72 ? 76  LYS C CA  1 
ATOM   4876 C  C   . LYS C 1 76  ? 2.629   33.956  80.076  1.00 34.61 ? 76  LYS C C   1 
ATOM   4877 O  O   . LYS C 1 76  ? 3.151   33.818  81.184  1.00 43.18 ? 76  LYS C O   1 
ATOM   4878 C  CB  . LYS C 1 76  ? 0.606   34.931  78.891  1.00 27.68 ? 76  LYS C CB  1 
ATOM   4879 C  CG  . LYS C 1 76  ? -0.458  36.068  79.014  1.00 37.74 ? 76  LYS C CG  1 
ATOM   4880 C  CD  . LYS C 1 76  ? -1.551  35.882  77.956  1.00 33.93 ? 76  LYS C CD  1 
ATOM   4881 C  CE  . LYS C 1 76  ? -2.728  36.890  78.041  1.00 38.52 ? 76  LYS C CE  1 
ATOM   4882 N  NZ  . LYS C 1 76  ? -3.777  36.676  77.012  1.00 33.77 ? 76  LYS C NZ  1 
ATOM   4883 N  N   . ALA C 1 77  ? 2.735   33.121  79.096  1.00 23.82 ? 77  ALA C N   1 
ATOM   4884 C  CA  . ALA C 1 77  ? 3.399   31.822  79.207  1.00 20.07 ? 77  ALA C CA  1 
ATOM   4885 C  C   . ALA C 1 77  ? 4.953   31.944  78.959  1.00 15.11 ? 77  ALA C C   1 
ATOM   4886 O  O   . ALA C 1 77  ? 5.322   32.124  77.796  1.00 21.91 ? 77  ALA C O   1 
ATOM   4887 C  CB  . ALA C 1 77  ? 2.794   30.917  78.160  1.00 20.34 ? 77  ALA C CB  1 
ATOM   4888 N  N   . VAL C 1 78  ? 5.830   31.799  79.939  1.00 13.83 ? 78  VAL C N   1 
ATOM   4889 C  CA  . VAL C 1 78  ? 7.218   32.100  79.696  1.00 15.84 ? 78  VAL C CA  1 
ATOM   4890 C  C   . VAL C 1 78  ? 8.151   30.983  80.211  1.00 13.66 ? 78  VAL C C   1 
ATOM   4891 O  O   . VAL C 1 78  ? 7.902   30.289  81.213  1.00 16.03 ? 78  VAL C O   1 
ATOM   4892 C  CB  . VAL C 1 78  ? 7.636   33.469  80.236  1.00 24.12 ? 78  VAL C CB  1 
ATOM   4893 C  CG1 . VAL C 1 78  ? 6.744   34.579  79.785  1.00 21.75 ? 78  VAL C CG1 1 
ATOM   4894 C  CG2 . VAL C 1 78  ? 7.573   33.452  81.686  1.00 22.85 ? 78  VAL C CG2 1 
ATOM   4895 N  N   . LEU C 1 79  ? 9.249   30.838  79.480  1.00 12.23 ? 79  LEU C N   1 
ATOM   4896 C  CA  . LEU C 1 79  ? 10.347  29.949  79.843  1.00 12.33 ? 79  LEU C CA  1 
ATOM   4897 C  C   . LEU C 1 79  ? 11.492  30.799  80.217  1.00 13.11 ? 79  LEU C C   1 
ATOM   4898 O  O   . LEU C 1 79  ? 11.878  31.746  79.459  1.00 14.33 ? 79  LEU C O   1 
ATOM   4899 C  CB  . LEU C 1 79  ? 10.624  29.001  78.653  1.00 13.46 ? 79  LEU C CB  1 
ATOM   4900 C  CG  . LEU C 1 79  ? 11.686  28.011  78.825  1.00 13.95 ? 79  LEU C CG  1 
ATOM   4901 C  CD1 . LEU C 1 79  ? 11.217  26.982  79.862  1.00 16.63 ? 79  LEU C CD1 1 
ATOM   4902 C  CD2 . LEU C 1 79  ? 11.978  27.315  77.532  1.00 13.63 ? 79  LEU C CD2 1 
ATOM   4903 N  N   . LYS C 1 80  ? 12.116  30.495  81.364  1.00 13.70 ? 80  LYS C N   1 
ATOM   4904 C  CA  . LYS C 1 80  ? 13.347  31.201  81.778  1.00 13.56 ? 80  LYS C CA  1 
ATOM   4905 C  C   . LYS C 1 80  ? 14.196  30.292  82.648  1.00 13.75 ? 80  LYS C C   1 
ATOM   4906 O  O   . LYS C 1 80  ? 13.816  29.111  82.852  1.00 14.87 ? 80  LYS C O   1 
ATOM   4907 C  CB  . LYS C 1 80  ? 13.052  32.570  82.420  1.00 17.23 ? 80  LYS C CB  1 
ATOM   4908 C  CG  . LYS C 1 80  ? 12.364  32.366  83.748  1.00 19.62 ? 80  LYS C CG  1 
ATOM   4909 C  CD  . LYS C 1 80  ? 12.059  33.765  84.341  1.00 22.92 ? 80  LYS C CD  1 
ATOM   4910 N  N   . GLY C 1 81  ? 15.276  30.853  83.161  1.00 15.33 ? 81  GLY C N   1 
ATOM   4911 C  CA  . GLY C 1 81  ? 16.247  30.035  83.879  1.00 15.76 ? 81  GLY C CA  1 
ATOM   4912 C  C   . GLY C 1 81  ? 16.919  28.953  83.065  1.00 19.38 ? 81  GLY C C   1 
ATOM   4913 O  O   . GLY C 1 81  ? 17.074  29.092  81.861  1.00 18.56 ? 81  GLY C O   1 
ATOM   4914 N  N   . GLY C 1 82  ? 17.361  27.860  83.710  1.00 22.06 ? 82  GLY C N   1 
ATOM   4915 C  CA  . GLY C 1 82  ? 18.294  26.975  83.028  1.00 20.27 ? 82  GLY C CA  1 
ATOM   4916 C  C   . GLY C 1 82  ? 19.516  27.611  82.388  1.00 20.70 ? 82  GLY C C   1 
ATOM   4917 O  O   . GLY C 1 82  ? 20.283  28.439  82.950  1.00 22.68 ? 82  GLY C O   1 
ATOM   4918 N  N   . PRO C 1 83  ? 19.713  27.267  81.106  1.00 18.88 ? 83  PRO C N   1 
ATOM   4919 C  CA  . PRO C 1 83  ? 20.778  27.835  80.366  1.00 18.94 ? 83  PRO C CA  1 
ATOM   4920 C  C   . PRO C 1 83  ? 20.447  29.262  79.896  1.00 17.29 ? 83  PRO C C   1 
ATOM   4921 O  O   . PRO C 1 83  ? 21.335  29.935  79.431  1.00 21.01 ? 83  PRO C O   1 
ATOM   4922 C  CB  . PRO C 1 83  ? 20.917  26.832  79.173  1.00 20.15 ? 83  PRO C CB  1 
ATOM   4923 C  CG  . PRO C 1 83  ? 19.485  26.547  78.903  1.00 17.56 ? 83  PRO C CG  1 
ATOM   4924 C  CD  . PRO C 1 83  ? 18.810  26.408  80.278  1.00 18.78 ? 83  PRO C CD  1 
ATOM   4925 N  N   . LEU C 1 84  ? 19.200  29.720  80.113  1.00 14.53 ? 84  LEU C N   1 
ATOM   4926 C  CA  . LEU C 1 84  ? 18.773  30.912  79.426  1.00 15.56 ? 84  LEU C CA  1 
ATOM   4927 C  C   . LEU C 1 84  ? 19.106  32.197  80.185  1.00 16.47 ? 84  LEU C C   1 
ATOM   4928 O  O   . LEU C 1 84  ? 18.966  32.224  81.406  1.00 19.47 ? 84  LEU C O   1 
ATOM   4929 C  CB  . LEU C 1 84  ? 17.285  30.880  79.202  1.00 12.89 ? 84  LEU C CB  1 
ATOM   4930 C  CG  . LEU C 1 84  ? 16.786  29.621  78.446  1.00 12.69 ? 84  LEU C CG  1 
ATOM   4931 C  CD1 . LEU C 1 84  ? 15.259  29.538  78.382  1.00 13.76 ? 84  LEU C CD1 1 
ATOM   4932 C  CD2 . LEU C 1 84  ? 17.321  29.603  76.990  1.00 11.60 ? 84  LEU C CD2 1 
ATOM   4933 N  N   . ASP C 1 85  ? 19.442  33.233  79.413  1.00 17.34 ? 85  ASP C N   1 
ATOM   4934 C  CA  . ASP C 1 85  ? 19.529  34.591  79.987  1.00 19.43 ? 85  ASP C CA  1 
ATOM   4935 C  C   . ASP C 1 85  ? 18.258  35.269  79.511  1.00 18.51 ? 85  ASP C C   1 
ATOM   4936 O  O   . ASP C 1 85  ? 17.857  35.166  78.334  1.00 22.67 ? 85  ASP C O   1 
ATOM   4937 C  CB  . ASP C 1 85  ? 20.727  35.324  79.363  1.00 20.77 ? 85  ASP C CB  1 
ATOM   4938 C  CG  . ASP C 1 85  ? 22.064  34.928  79.967  1.00 28.89 ? 85  ASP C CG  1 
ATOM   4939 O  OD1 . ASP C 1 85  ? 22.176  34.742  81.211  1.00 36.63 ? 85  ASP C OD1 1 
ATOM   4940 O  OD2 . ASP C 1 85  ? 23.040  34.840  79.178  1.00 30.44 ? 85  ASP C OD2 1 
ATOM   4941 N  N   . GLY C 1 86  ? 17.622  36.046  80.368  1.00 22.23 ? 86  GLY C N   1 
ATOM   4942 C  CA  . GLY C 1 86  ? 16.393  36.701  79.977  1.00 20.68 ? 86  GLY C CA  1 
ATOM   4943 C  C   . GLY C 1 86  ? 15.126  35.783  79.948  1.00 18.77 ? 86  GLY C C   1 
ATOM   4944 O  O   . GLY C 1 86  ? 15.064  34.743  80.622  1.00 23.74 ? 86  GLY C O   1 
ATOM   4945 N  N   A THR C 1 87  ? 14.065  36.248  79.247  0.50 16.06 ? 87  THR C N   1 
ATOM   4946 N  N   B THR C 1 87  ? 14.126  36.168  79.187  0.50 15.71 ? 87  THR C N   1 
ATOM   4947 C  CA  A THR C 1 87  ? 12.675  35.682  79.259  0.50 14.94 ? 87  THR C CA  1 
ATOM   4948 C  CA  B THR C 1 87  ? 12.884  35.473  79.269  0.50 13.88 ? 87  THR C CA  1 
ATOM   4949 C  C   A THR C 1 87  ? 12.163  35.318  77.844  0.50 13.32 ? 87  THR C C   1 
ATOM   4950 C  C   B THR C 1 87  ? 12.444  35.210  77.828  0.50 9.91  ? 87  THR C C   1 
ATOM   4951 O  O   A THR C 1 87  ? 12.107  36.131  76.959  0.50 11.90 ? 87  THR C O   1 
ATOM   4952 O  O   B THR C 1 87  ? 12.745  36.007  76.912  0.50 8.94  ? 87  THR C O   1 
ATOM   4953 C  CB  A THR C 1 87  ? 11.631  36.695  79.809  0.50 15.64 ? 87  THR C CB  1 
ATOM   4954 C  CB  B THR C 1 87  ? 11.904  36.332  80.073  0.50 14.51 ? 87  THR C CB  1 
ATOM   4955 O  OG1 A THR C 1 87  ? 11.971  37.105  81.142  0.50 22.25 ? 87  THR C OG1 1 
ATOM   4956 O  OG1 B THR C 1 87  ? 11.756  37.599  79.437  0.50 13.35 ? 87  THR C OG1 1 
ATOM   4957 C  CG2 A THR C 1 87  ? 10.235  36.053  79.845  0.50 19.55 ? 87  THR C CG2 1 
ATOM   4958 C  CG2 B THR C 1 87  ? 12.447  36.544  81.530  0.50 15.00 ? 87  THR C CG2 1 
ATOM   4959 N  N   . TYR C 1 88  ? 11.721  34.096  77.661  1.00 11.99 ? 88  TYR C N   1 
ATOM   4960 C  CA  . TYR C 1 88  ? 11.322  33.617  76.327  1.00 10.49 ? 88  TYR C CA  1 
ATOM   4961 C  C   . TYR C 1 88  ? 9.846   33.315  76.412  1.00 9.95  ? 88  TYR C C   1 
ATOM   4962 O  O   . TYR C 1 88  ? 9.353   32.671  77.346  1.00 14.27 ? 88  TYR C O   1 
ATOM   4963 C  CB  . TYR C 1 88  ? 12.117  32.377  75.984  1.00 11.10 ? 88  TYR C CB  1 
ATOM   4964 C  CG  . TYR C 1 88  ? 13.534  32.595  75.642  1.00 10.46 ? 88  TYR C CG  1 
ATOM   4965 C  CD1 . TYR C 1 88  ? 14.465  32.941  76.604  1.00 10.87 ? 88  TYR C CD1 1 
ATOM   4966 C  CD2 . TYR C 1 88  ? 13.985  32.436  74.316  1.00 9.64  ? 88  TYR C CD2 1 
ATOM   4967 C  CE1 . TYR C 1 88  ? 15.794  33.093  76.306  1.00 10.74 ? 88  TYR C CE1 1 
ATOM   4968 C  CE2 . TYR C 1 88  ? 15.331  32.546  74.025  1.00 9.26  ? 88  TYR C CE2 1 
ATOM   4969 C  CZ  . TYR C 1 88  ? 16.265  32.889  75.002  1.00 9.09  ? 88  TYR C CZ  1 
ATOM   4970 O  OH  . TYR C 1 88  ? 17.573  32.953  74.702  1.00 10.83 ? 88  TYR C OH  1 
ATOM   4971 N  N   . ARG C 1 89  ? 9.078   33.794  75.454  1.00 9.44  ? 89  ARG C N   1 
ATOM   4972 C  CA  . ARG C 1 89  ? 7.650   33.707  75.451  1.00 9.50  ? 89  ARG C CA  1 
ATOM   4973 C  C   . ARG C 1 89  ? 7.091   32.589  74.552  1.00 8.94  ? 89  ARG C C   1 
ATOM   4974 O  O   . ARG C 1 89  ? 7.526   32.495  73.366  1.00 9.45  ? 89  ARG C O   1 
ATOM   4975 C  CB  . ARG C 1 89  ? 7.009   35.014  75.020  1.00 13.23 ? 89  ARG C CB  1 
ATOM   4976 C  CG  . ARG C 1 89  ? 5.549   35.130  75.313  1.00 14.44 ? 89  ARG C CG  1 
ATOM   4977 C  CD  . ARG C 1 89  ? 5.126   36.584  74.919  1.00 15.75 ? 89  ARG C CD  1 
ATOM   4978 N  NE  . ARG C 1 89  ? 5.724   37.579  75.851  1.00 16.84 ? 89  ARG C NE  1 
ATOM   4979 C  CZ  . ARG C 1 89  ? 5.617   38.921  75.674  1.00 16.83 ? 89  ARG C CZ  1 
ATOM   4980 N  NH1 . ARG C 1 89  ? 4.885   39.392  74.686  1.00 17.29 ? 89  ARG C NH1 1 
ATOM   4981 N  NH2 . ARG C 1 89  ? 6.193   39.759  76.520  1.00 17.19 ? 89  ARG C NH2 1 
ATOM   4982 N  N   . LEU C 1 90  ? 6.188   31.765  75.044  1.00 9.11  ? 90  LEU C N   1 
ATOM   4983 C  CA  . LEU C 1 90  ? 5.629   30.663  74.257  1.00 9.34  ? 90  LEU C CA  1 
ATOM   4984 C  C   . LEU C 1 90  ? 4.799   31.219  73.116  1.00 9.24  ? 90  LEU C C   1 
ATOM   4985 O  O   . LEU C 1 90  ? 3.917   32.092  73.301  1.00 11.60 ? 90  LEU C O   1 
ATOM   4986 C  CB  . LEU C 1 90  ? 4.722   29.842  75.177  1.00 9.84  ? 90  LEU C CB  1 
ATOM   4987 C  CG  . LEU C 1 90  ? 3.971   28.685  74.550  1.00 10.50 ? 90  LEU C CG  1 
ATOM   4988 C  CD1 . LEU C 1 90  ? 4.903   27.587  74.000  1.00 12.79 ? 90  LEU C CD1 1 
ATOM   4989 C  CD2 . LEU C 1 90  ? 2.949   28.023  75.469  1.00 13.69 ? 90  LEU C CD2 1 
ATOM   4990 N  N   . ILE C 1 91  ? 5.094   30.779  71.907  1.00 9.10  ? 91  ILE C N   1 
ATOM   4991 C  CA  . ILE C 1 91  ? 4.294   31.102  70.706  1.00 10.01 ? 91  ILE C CA  1 
ATOM   4992 C  C   . ILE C 1 91  ? 3.524   29.972  70.132  1.00 9.06  ? 91  ILE C C   1 
ATOM   4993 O  O   . ILE C 1 91  ? 2.392   30.145  69.722  1.00 9.12  ? 91  ILE C O   1 
ATOM   4994 C  CB  . ILE C 1 91  ? 5.137   31.833  69.628  1.00 9.99  ? 91  ILE C CB  1 
ATOM   4995 C  CG1 . ILE C 1 91  ? 4.334   32.132  68.379  1.00 12.26 ? 91  ILE C CG1 1 
ATOM   4996 C  CG2 . ILE C 1 91  ? 6.426   31.047  69.287  1.00 11.09 ? 91  ILE C CG2 1 
ATOM   4997 C  CD1 . ILE C 1 91  ? 5.080   33.162  67.558  1.00 17.03 ? 91  ILE C CD1 1 
ATOM   4998 N  N   . GLN C 1 92  ? 4.085   28.741  70.107  1.00 9.46  ? 92  GLN C N   1 
ATOM   4999 C  CA  . GLN C 1 92  ? 3.316   27.613  69.563  1.00 9.47  ? 92  GLN C CA  1 
ATOM   5000 C  C   . GLN C 1 92  ? 3.949   26.331  70.045  1.00 9.42  ? 92  GLN C C   1 
ATOM   5001 O  O   . GLN C 1 92  ? 5.094   26.337  70.505  1.00 8.80  ? 92  GLN C O   1 
ATOM   5002 C  CB  . GLN C 1 92  ? 3.336   27.621  68.012  1.00 11.33 ? 92  GLN C CB  1 
ATOM   5003 C  CG  . GLN C 1 92  ? 4.769   27.618  67.377  1.00 12.12 ? 92  GLN C CG  1 
ATOM   5004 C  CD  . GLN C 1 92  ? 4.990   26.308  66.641  1.00 13.30 ? 92  GLN C CD  1 
ATOM   5005 O  OE1 . GLN C 1 92  ? 5.132   25.296  67.280  1.00 13.37 ? 92  GLN C OE1 1 
ATOM   5006 N  NE2 . GLN C 1 92  ? 4.919   26.298  65.369  1.00 19.16 ? 92  GLN C NE2 1 
ATOM   5007 N  N   . PHE C 1 93  ? 3.244   25.215  69.927  1.00 8.84  ? 93  PHE C N   1 
ATOM   5008 C  CA  . PHE C 1 93  ? 3.872   23.888  70.007  1.00 8.09  ? 93  PHE C CA  1 
ATOM   5009 C  C   . PHE C 1 93  ? 3.457   23.080  68.814  1.00 8.01  ? 93  PHE C C   1 
ATOM   5010 O  O   . PHE C 1 93  ? 2.399   23.298  68.203  1.00 9.10  ? 93  PHE C O   1 
ATOM   5011 C  CB  . PHE C 1 93  ? 3.669   23.178  71.338  1.00 7.81  ? 93  PHE C CB  1 
ATOM   5012 C  CG  . PHE C 1 93  ? 2.232   22.753  71.627  1.00 8.62  ? 93  PHE C CG  1 
ATOM   5013 C  CD1 . PHE C 1 93  ? 1.689   21.582  71.017  1.00 10.56 ? 93  PHE C CD1 1 
ATOM   5014 C  CD2 . PHE C 1 93  ? 1.457   23.437  72.623  1.00 10.26 ? 93  PHE C CD2 1 
ATOM   5015 C  CE1 . PHE C 1 93  ? 0.404   21.152  71.329  1.00 10.07 ? 93  PHE C CE1 1 
ATOM   5016 C  CE2 . PHE C 1 93  ? 0.180   22.981  72.915  1.00 10.99 ? 93  PHE C CE2 1 
ATOM   5017 C  CZ  . PHE C 1 93  ? -0.318  21.872  72.268  1.00 9.70  ? 93  PHE C CZ  1 
ATOM   5018 N  N   . HIS C 1 94  ? 4.267   22.057  68.535  1.00 8.27  ? 94  HIS C N   1 
ATOM   5019 C  CA  . HIS C 1 94  ? 3.995   21.101  67.479  1.00 7.44  ? 94  HIS C CA  1 
ATOM   5020 C  C   . HIS C 1 94  ? 4.683   19.805  67.815  1.00 7.06  ? 94  HIS C C   1 
ATOM   5021 O  O   . HIS C 1 94  ? 5.456   19.734  68.767  1.00 8.00  ? 94  HIS C O   1 
ATOM   5022 C  CB  . HIS C 1 94  ? 4.460   21.580  66.067  1.00 8.13  ? 94  HIS C CB  1 
ATOM   5023 C  CG  . HIS C 1 94  ? 5.906   21.863  66.066  1.00 6.79  ? 94  HIS C CG  1 
ATOM   5024 N  ND1 . HIS C 1 94  ? 6.490   23.059  66.460  1.00 7.46  ? 94  HIS C ND1 1 
ATOM   5025 C  CD2 . HIS C 1 94  ? 6.948   21.024  65.760  1.00 7.02  ? 94  HIS C CD2 1 
ATOM   5026 C  CE1 . HIS C 1 94  ? 7.841   22.911  66.413  1.00 8.22  ? 94  HIS C CE1 1 
ATOM   5027 N  NE2 . HIS C 1 94  ? 8.142   21.659  65.982  1.00 7.32  ? 94  HIS C NE2 1 
ATOM   5028 N  N   . PHE C 1 95  ? 4.446   18.784  67.012  1.00 7.79  ? 95  PHE C N   1 
ATOM   5029 C  CA  . PHE C 1 95  ? 5.075   17.457  67.208  1.00 7.54  ? 95  PHE C CA  1 
ATOM   5030 C  C   . PHE C 1 95  ? 5.710   16.984  65.894  1.00 7.26  ? 95  PHE C C   1 
ATOM   5031 O  O   . PHE C 1 95  ? 5.443   17.456  64.803  1.00 8.50  ? 95  PHE C O   1 
ATOM   5032 C  CB  . PHE C 1 95  ? 4.027   16.391  67.605  1.00 8.77  ? 95  PHE C CB  1 
ATOM   5033 C  CG  . PHE C 1 95  ? 3.281   16.688  68.904  1.00 8.42  ? 95  PHE C CG  1 
ATOM   5034 C  CD1 . PHE C 1 95  ? 2.177   17.567  68.879  1.00 8.29  ? 95  PHE C CD1 1 
ATOM   5035 C  CD2 . PHE C 1 95  ? 3.553   16.003  70.062  1.00 8.85  ? 95  PHE C CD2 1 
ATOM   5036 C  CE1 . PHE C 1 95  ? 1.408   17.760  70.003  1.00 9.56  ? 95  PHE C CE1 1 
ATOM   5037 C  CE2 . PHE C 1 95  ? 2.811   16.188  71.219  1.00 9.70  ? 95  PHE C CE2 1 
ATOM   5038 C  CZ  . PHE C 1 95  ? 1.725   17.099  71.150  1.00 10.13 ? 95  PHE C CZ  1 
ATOM   5039 N  N   . HIS C 1 96  ? 6.647   16.024  66.076  1.00 7.71  ? 96  HIS C N   1 
ATOM   5040 C  CA  . HIS C 1 96  ? 7.163   15.242  64.978  1.00 6.64  ? 96  HIS C CA  1 
ATOM   5041 C  C   . HIS C 1 96  ? 6.918   13.776  65.351  1.00 7.44  ? 96  HIS C C   1 
ATOM   5042 O  O   . HIS C 1 96  ? 7.043   13.421  66.538  1.00 7.73  ? 96  HIS C O   1 
ATOM   5043 C  CB  . HIS C 1 96  ? 8.696   15.437  64.846  1.00 8.07  ? 96  HIS C CB  1 
ATOM   5044 C  CG  . HIS C 1 96  ? 9.085   16.877  64.638  1.00 7.64  ? 96  HIS C CG  1 
ATOM   5045 N  ND1 . HIS C 1 96  ? 9.295   17.449  63.422  1.00 8.21  ? 96  HIS C ND1 1 
ATOM   5046 C  CD2 . HIS C 1 96  ? 9.223   17.867  65.543  1.00 7.65  ? 96  HIS C CD2 1 
ATOM   5047 C  CE1 . HIS C 1 96  ? 9.593   18.766  63.592  1.00 8.24  ? 96  HIS C CE1 1 
ATOM   5048 N  NE2 . HIS C 1 96  ? 9.528   19.040  64.912  1.00 7.24  ? 96  HIS C NE2 1 
ATOM   5049 N  N   . TRP C 1 97  ? 6.535   12.908  64.407  1.00 6.76  ? 97  TRP C N   1 
ATOM   5050 C  CA  . TRP C 1 97  ? 6.251   11.544  64.752  1.00 7.15  ? 97  TRP C CA  1 
ATOM   5051 C  C   . TRP C 1 97  ? 6.491   10.651  63.555  1.00 6.86  ? 97  TRP C C   1 
ATOM   5052 O  O   . TRP C 1 97  ? 6.816   11.067  62.425  1.00 7.99  ? 97  TRP C O   1 
ATOM   5053 C  CB  . TRP C 1 97  ? 4.780   11.375  65.196  1.00 8.39  ? 97  TRP C CB  1 
ATOM   5054 C  CG  . TRP C 1 97  ? 3.785   11.799  64.151  1.00 7.64  ? 97  TRP C CG  1 
ATOM   5055 C  CD1 . TRP C 1 97  ? 3.202   10.969  63.204  1.00 8.82  ? 97  TRP C CD1 1 
ATOM   5056 C  CD2 . TRP C 1 97  ? 3.225   13.104  63.946  1.00 8.68  ? 97  TRP C CD2 1 
ATOM   5057 N  NE1 . TRP C 1 97  ? 2.273   11.658  62.447  1.00 9.70  ? 97  TRP C NE1 1 
ATOM   5058 C  CE2 . TRP C 1 97  ? 2.288   12.999  62.826  1.00 8.27  ? 97  TRP C CE2 1 
ATOM   5059 C  CE3 . TRP C 1 97  ? 3.472   14.375  64.519  1.00 7.87  ? 97  TRP C CE3 1 
ATOM   5060 C  CZ2 . TRP C 1 97  ? 1.612   14.076  62.372  1.00 9.64  ? 97  TRP C CZ2 1 
ATOM   5061 C  CZ3 . TRP C 1 97  ? 2.756   15.494  64.043  1.00 8.39  ? 97  TRP C CZ3 1 
ATOM   5062 C  CH2 . TRP C 1 97  ? 1.816   15.325  62.983  1.00 9.26  ? 97  TRP C CH2 1 
ATOM   5063 N  N   . GLY C 1 98  ? 6.418   9.322   63.828  1.00 7.68  ? 98  GLY C N   1 
ATOM   5064 C  CA  . GLY C 1 98  ? 6.803   8.310   62.867  1.00 8.54  ? 98  GLY C CA  1 
ATOM   5065 C  C   . GLY C 1 98  ? 5.613   7.612   62.210  1.00 9.17  ? 98  GLY C C   1 
ATOM   5066 O  O   . GLY C 1 98  ? 4.452   7.742   62.615  1.00 9.47  ? 98  GLY C O   1 
ATOM   5067 N  N   . SER C 1 99  ? 5.951   6.741   61.250  1.00 10.62 ? 99  SER C N   1 
ATOM   5068 C  CA  . SER C 1 99  ? 4.957   5.805   60.678  1.00 10.83 ? 99  SER C CA  1 
ATOM   5069 C  C   . SER C 1 99  ? 4.826   4.547   61.542  1.00 11.20 ? 99  SER C C   1 
ATOM   5070 O  O   . SER C 1 99  ? 3.893   3.769   61.330  1.00 15.08 ? 99  SER C O   1 
ATOM   5071 C  CB  . SER C 1 99  ? 5.417   5.491   59.287  1.00 11.37 ? 99  SER C CB  1 
ATOM   5072 O  OG  . SER C 1 99  ? 6.740   4.927   59.291  1.00 12.63 ? 99  SER C OG  1 
ATOM   5073 N  N   . LEU C 1 100 ? 5.780   4.312   62.476  1.00 10.56 ? 100 LEU C N   1 
ATOM   5074 C  CA  . LEU C 1 100 ? 5.825   3.168   63.348  1.00 13.53 ? 100 LEU C CA  1 
ATOM   5075 C  C   . LEU C 1 100 ? 6.266   3.633   64.688  1.00 12.07 ? 100 LEU C C   1 
ATOM   5076 O  O   . LEU C 1 100 ? 6.930   4.649   64.788  1.00 10.89 ? 100 LEU C O   1 
ATOM   5077 C  CB  . LEU C 1 100 ? 6.965   2.186   62.893  1.00 17.41 ? 100 LEU C CB  1 
ATOM   5078 C  CG  . LEU C 1 100 ? 6.860   1.807   61.409  1.00 18.08 ? 100 LEU C CG  1 
ATOM   5079 C  CD1 . LEU C 1 100 ? 8.130   1.363   60.741  1.00 28.95 ? 100 LEU C CD1 1 
ATOM   5080 C  CD2 . LEU C 1 100 ? 5.807   0.733   61.316  1.00 22.71 ? 100 LEU C CD2 1 
ATOM   5081 N  N   . ASP C 1 101 ? 5.978   2.909   65.746  1.00 11.81 ? 101 ASP C N   1 
ATOM   5082 C  CA  . ASP C 1 101 ? 6.280   3.383   67.109  1.00 11.45 ? 101 ASP C CA  1 
ATOM   5083 C  C   . ASP C 1 101 ? 7.785   3.450   67.336  1.00 11.55 ? 101 ASP C C   1 
ATOM   5084 O  O   . ASP C 1 101 ? 8.208   4.178   68.230  1.00 12.61 ? 101 ASP C O   1 
ATOM   5085 C  CB  . ASP C 1 101 ? 5.673   2.469   68.192  1.00 12.81 ? 101 ASP C CB  1 
ATOM   5086 C  CG  . ASP C 1 101 ? 4.160   2.386   68.117  1.00 13.39 ? 101 ASP C CG  1 
ATOM   5087 O  OD1 . ASP C 1 101 ? 3.471   3.316   67.627  1.00 14.80 ? 101 ASP C OD1 1 
ATOM   5088 O  OD2 . ASP C 1 101 ? 3.648   1.409   68.695  1.00 19.44 ? 101 ASP C OD2 1 
ATOM   5089 N  N   . GLY C 1 102 ? 8.573   2.693   66.519  1.00 11.55 ? 102 GLY C N   1 
ATOM   5090 C  CA  . GLY C 1 102 ? 10.037  2.728   66.712  1.00 12.14 ? 102 GLY C CA  1 
ATOM   5091 C  C   . GLY C 1 102 ? 10.821  3.869   66.082  1.00 11.42 ? 102 GLY C C   1 
ATOM   5092 O  O   . GLY C 1 102 ? 12.020  3.896   66.159  1.00 12.53 ? 102 GLY C O   1 
ATOM   5093 N  N   . GLN C 1 103 ? 10.097  4.893   65.636  1.00 10.52 ? 103 GLN C N   1 
ATOM   5094 C  CA  . GLN C 1 103 ? 10.777  6.071   65.085  1.00 8.98  ? 103 GLN C CA  1 
ATOM   5095 C  C   . GLN C 1 103 ? 9.815   7.217   65.200  1.00 7.99  ? 103 GLN C C   1 
ATOM   5096 O  O   . GLN C 1 103 ? 8.606   7.038   65.330  1.00 9.27  ? 103 GLN C O   1 
ATOM   5097 C  CB  . GLN C 1 103 ? 11.256  5.818   63.643  1.00 9.41  ? 103 GLN C CB  1 
ATOM   5098 C  CG  . GLN C 1 103 ? 10.101  5.627   62.669  1.00 9.65  ? 103 GLN C CG  1 
ATOM   5099 C  CD  . GLN C 1 103 ? 10.591  5.001   61.391  1.00 13.45 ? 103 GLN C CD  1 
ATOM   5100 O  OE1 . GLN C 1 103 ? 11.334  4.030   61.441  1.00 19.48 ? 103 GLN C OE1 1 
ATOM   5101 N  NE2 . GLN C 1 103 ? 10.185  5.506   60.242  1.00 14.66 ? 103 GLN C NE2 1 
ATOM   5102 N  N   . GLY C 1 104 ? 10.349  8.431   65.022  1.00 7.40  ? 104 GLY C N   1 
ATOM   5103 C  CA  . GLY C 1 104 ? 9.503   9.649   65.039  1.00 8.16  ? 104 GLY C CA  1 
ATOM   5104 C  C   . GLY C 1 104 ? 10.199  10.793  65.734  1.00 7.27  ? 104 GLY C C   1 
ATOM   5105 O  O   . GLY C 1 104 ? 9.925   11.935  65.365  1.00 8.97  ? 104 GLY C O   1 
ATOM   5106 N  N   . SER C 1 105 ? 11.016  10.554  66.764  1.00 6.80  ? 105 SER C N   1 
ATOM   5107 C  CA  . SER C 1 105 ? 11.670  11.676  67.404  1.00 7.85  ? 105 SER C CA  1 
ATOM   5108 C  C   . SER C 1 105 ? 12.787  12.220  66.507  1.00 7.42  ? 105 SER C C   1 
ATOM   5109 O  O   . SER C 1 105 ? 13.302  11.541  65.579  1.00 8.20  ? 105 SER C O   1 
ATOM   5110 C  CB  . SER C 1 105 ? 12.212  11.330  68.797  1.00 8.29  ? 105 SER C CB  1 
ATOM   5111 O  OG  . SER C 1 105 ? 13.240  10.346  68.754  1.00 7.63  ? 105 SER C OG  1 
ATOM   5112 N  N   . GLU C 1 106 ? 13.109  13.467  66.734  1.00 6.99  ? 106 GLU C N   1 
ATOM   5113 C  CA  . GLU C 1 106 ? 14.211  14.194  66.058  1.00 7.01  ? 106 GLU C CA  1 
ATOM   5114 C  C   . GLU C 1 106 ? 15.520  13.980  66.851  1.00 7.24  ? 106 GLU C C   1 
ATOM   5115 O  O   . GLU C 1 106 ? 16.494  13.410  66.328  1.00 7.74  ? 106 GLU C O   1 
ATOM   5116 C  CB  . GLU C 1 106 ? 13.841  15.660  65.864  1.00 7.17  ? 106 GLU C CB  1 
ATOM   5117 C  CG  . GLU C 1 106 ? 12.624  15.787  64.972  1.00 9.19  ? 106 GLU C CG  1 
ATOM   5118 C  CD  . GLU C 1 106 ? 12.582  17.052  64.260  1.00 9.18  ? 106 GLU C CD  1 
ATOM   5119 O  OE1 . GLU C 1 106 ? 12.630  18.137  64.903  1.00 9.30  ? 106 GLU C OE1 1 
ATOM   5120 O  OE2 . GLU C 1 106 ? 12.533  17.060  63.020  1.00 9.46  ? 106 GLU C OE2 1 
ATOM   5121 N  N   . HIS C 1 107 ? 15.517  14.412  68.099  1.00 7.28  ? 107 HIS C N   1 
ATOM   5122 C  CA  . HIS C 1 107 ? 16.631  14.045  68.964  1.00 6.86  ? 107 HIS C CA  1 
ATOM   5123 C  C   . HIS C 1 107 ? 16.548  12.548  69.252  1.00 7.61  ? 107 HIS C C   1 
ATOM   5124 O  O   . HIS C 1 107 ? 15.478  11.987  69.252  1.00 8.39  ? 107 HIS C O   1 
ATOM   5125 C  CB  . HIS C 1 107 ? 16.587  14.844  70.300  1.00 6.95  ? 107 HIS C CB  1 
ATOM   5126 C  CG  . HIS C 1 107 ? 16.835  16.303  70.033  1.00 7.52  ? 107 HIS C CG  1 
ATOM   5127 N  ND1 . HIS C 1 107 ? 15.828  17.190  69.758  1.00 7.27  ? 107 HIS C ND1 1 
ATOM   5128 C  CD2 . HIS C 1 107 ? 18.009  17.015  69.885  1.00 7.72  ? 107 HIS C CD2 1 
ATOM   5129 C  CE1 . HIS C 1 107 ? 16.400  18.407  69.432  1.00 7.28  ? 107 HIS C CE1 1 
ATOM   5130 N  NE2 . HIS C 1 107 ? 17.722  18.320  69.552  1.00 7.44  ? 107 HIS C NE2 1 
ATOM   5131 N  N   . THR C 1 108 ? 17.752  11.994  69.524  1.00 8.00  ? 108 THR C N   1 
ATOM   5132 C  CA  . THR C 1 108 ? 17.843  10.606  69.939  1.00 8.20  ? 108 THR C CA  1 
ATOM   5133 C  C   . THR C 1 108 ? 18.685  10.602  71.224  1.00 8.03  ? 108 THR C C   1 
ATOM   5134 O  O   . THR C 1 108 ? 19.415  11.584  71.499  1.00 9.11  ? 108 THR C O   1 
ATOM   5135 C  CB  . THR C 1 108 ? 18.440  9.681   68.838  1.00 8.44  ? 108 THR C CB  1 
ATOM   5136 O  OG1 . THR C 1 108 ? 19.700  10.184  68.387  1.00 9.11  ? 108 THR C OG1 1 
ATOM   5137 C  CG2 . THR C 1 108 ? 17.414  9.659   67.686  1.00 8.92  ? 108 THR C CG2 1 
ATOM   5138 N  N   . VAL C 1 109 ? 18.547  9.542   71.991  1.00 8.39  ? 109 VAL C N   1 
ATOM   5139 C  CA  . VAL C 1 109 ? 19.275  9.442   73.293  1.00 8.71  ? 109 VAL C CA  1 
ATOM   5140 C  C   . VAL C 1 109 ? 20.102  8.119   73.249  1.00 9.57  ? 109 VAL C C   1 
ATOM   5141 O  O   . VAL C 1 109 ? 19.497  7.036   73.220  1.00 9.81  ? 109 VAL C O   1 
ATOM   5142 C  CB  . VAL C 1 109 ? 18.280  9.417   74.445  1.00 9.71  ? 109 VAL C CB  1 
ATOM   5143 C  CG1 . VAL C 1 109 ? 19.025  9.292   75.786  1.00 12.32 ? 109 VAL C CG1 1 
ATOM   5144 C  CG2 . VAL C 1 109 ? 17.383  10.668  74.461  1.00 12.14 ? 109 VAL C CG2 1 
ATOM   5145 N  N   . ASP C 1 110 ? 21.418  8.253   73.136  1.00 9.78  ? 110 ASP C N   1 
ATOM   5146 C  CA  . ASP C 1 110 ? 22.248  7.057   72.894  1.00 12.52 ? 110 ASP C CA  1 
ATOM   5147 C  C   . ASP C 1 110 ? 21.708  6.254   71.709  1.00 10.40 ? 110 ASP C C   1 
ATOM   5148 O  O   . ASP C 1 110 ? 21.647  4.985   71.763  1.00 11.74 ? 110 ASP C O   1 
ATOM   5149 C  CB  . ASP C 1 110 ? 22.375  6.237   74.164  1.00 12.75 ? 110 ASP C CB  1 
ATOM   5150 C  CG  . ASP C 1 110 ? 23.045  7.075   75.306  1.00 12.10 ? 110 ASP C CG  1 
ATOM   5151 O  OD1 . ASP C 1 110 ? 23.908  7.876   74.977  1.00 14.27 ? 110 ASP C OD1 1 
ATOM   5152 O  OD2 . ASP C 1 110 ? 22.720  6.796   76.449  1.00 17.36 ? 110 ASP C OD2 1 
ATOM   5153 N  N   . LYS C 1 111 ? 21.303  6.936   70.642  1.00 9.86  ? 111 LYS C N   1 
ATOM   5154 C  CA  . LYS C 1 111 ? 20.785  6.427   69.384  1.00 10.29 ? 111 LYS C CA  1 
ATOM   5155 C  C   . LYS C 1 111 ? 19.344  5.891   69.481  1.00 10.19 ? 111 LYS C C   1 
ATOM   5156 O  O   . LYS C 1 111 ? 18.753  5.523   68.480  1.00 11.23 ? 111 LYS C O   1 
ATOM   5157 C  CB  . LYS C 1 111 ? 21.710  5.353   68.764  1.00 12.03 ? 111 LYS C CB  1 
ATOM   5158 C  CG  . LYS C 1 111 ? 23.115  5.917   68.476  1.00 14.79 ? 111 LYS C CG  1 
ATOM   5159 C  CD  . LYS C 1 111 ? 23.091  7.050   67.455  1.00 20.69 ? 111 LYS C CD  1 
ATOM   5160 C  CE  . LYS C 1 111 ? 24.458  7.674   67.181  1.00 20.51 ? 111 LYS C CE  1 
ATOM   5161 N  NZ  . LYS C 1 111 ? 24.968  7.016   66.008  1.00 23.84 ? 111 LYS C NZ  1 
ATOM   5162 N  N   . LYS C 1 112 ? 18.759  5.959   70.660  1.00 9.11  ? 112 LYS C N   1 
ATOM   5163 C  CA  . LYS C 1 112 ? 17.335  5.530   70.835  1.00 9.87  ? 112 LYS C CA  1 
ATOM   5164 C  C   . LYS C 1 112 ? 16.427  6.583   70.192  1.00 8.83  ? 112 LYS C C   1 
ATOM   5165 O  O   . LYS C 1 112 ? 16.558  7.804   70.482  1.00 9.19  ? 112 LYS C O   1 
ATOM   5166 C  CB  . LYS C 1 112 ? 16.949  5.464   72.341  1.00 10.83 ? 112 LYS C CB  1 
ATOM   5167 C  CG  . LYS C 1 112 ? 15.499  5.056   72.546  1.00 12.30 ? 112 LYS C CG  1 
ATOM   5168 C  CD  . LYS C 1 112 ? 15.097  5.040   74.017  1.00 15.65 ? 112 LYS C CD  1 
ATOM   5169 C  CE  . LYS C 1 112 ? 13.604  4.882   74.175  1.00 16.43 ? 112 LYS C CE  1 
ATOM   5170 N  NZ  . LYS C 1 112 ? 13.180  3.560   73.792  1.00 16.83 ? 112 LYS C NZ  1 
ATOM   5171 N  N   A LYS C 1 113 ? 15.542  6.135   69.312  0.50 8.55  ? 113 LYS C N   1 
ATOM   5172 N  N   B LYS C 1 113 ? 15.510  6.134   69.346  0.50 8.50  ? 113 LYS C N   1 
ATOM   5173 C  CA  A LYS C 1 113 ? 14.438  6.884   68.785  0.50 8.84  ? 113 LYS C CA  1 
ATOM   5174 C  CA  B LYS C 1 113 ? 14.467  6.938   68.776  0.50 9.06  ? 113 LYS C CA  1 
ATOM   5175 C  C   A LYS C 1 113 ? 13.208  6.693   69.640  0.50 8.65  ? 113 LYS C C   1 
ATOM   5176 C  C   B LYS C 1 113 ? 13.118  6.696   69.446  0.50 8.98  ? 113 LYS C C   1 
ATOM   5177 O  O   A LYS C 1 113 ? 12.921  5.569   70.055  0.50 8.60  ? 113 LYS C O   1 
ATOM   5178 O  O   B LYS C 1 113 ? 12.667  5.535   69.557  0.50 8.74  ? 113 LYS C O   1 
ATOM   5179 C  CB  A LYS C 1 113 ? 14.120  6.400   67.352  0.50 9.11  ? 113 LYS C CB  1 
ATOM   5180 C  CB  B LYS C 1 113 ? 14.319  6.626   67.281  0.50 8.95  ? 113 LYS C CB  1 
ATOM   5181 C  CG  A LYS C 1 113 ? 15.245  6.675   66.366  0.50 8.75  ? 113 LYS C CG  1 
ATOM   5182 C  CG  B LYS C 1 113 ? 15.531  6.950   66.420  0.50 10.53 ? 113 LYS C CG  1 
ATOM   5183 C  CD  A LYS C 1 113 ? 15.029  5.995   64.998  0.50 9.76  ? 113 LYS C CD  1 
ATOM   5184 C  CD  B LYS C 1 113 ? 15.328  6.418   65.000  0.50 9.13  ? 113 LYS C CD  1 
ATOM   5185 C  CE  A LYS C 1 113 ? 15.920  6.566   63.887  0.50 9.78  ? 113 LYS C CE  1 
ATOM   5186 C  CE  B LYS C 1 113 ? 16.420  6.968   64.076  0.50 10.54 ? 113 LYS C CE  1 
ATOM   5187 N  NZ  A LYS C 1 113 ? 17.337  6.111   63.875  0.50 11.63 ? 113 LYS C NZ  1 
ATOM   5188 N  NZ  B LYS C 1 113 ? 16.535  6.205   62.825  0.50 13.28 ? 113 LYS C NZ  1 
ATOM   5189 N  N   . TYR C 1 114 ? 12.487  7.791   69.890  1.00 7.95  ? 114 TYR C N   1 
ATOM   5190 C  CA  . TYR C 1 114 ? 11.197  7.714   70.532  1.00 7.63  ? 114 TYR C CA  1 
ATOM   5191 C  C   . TYR C 1 114 ? 10.077  7.759   69.466  1.00 7.48  ? 114 TYR C C   1 
ATOM   5192 O  O   . TYR C 1 114 ? 10.381  8.057   68.278  1.00 8.12  ? 114 TYR C O   1 
ATOM   5193 C  CB  . TYR C 1 114 ? 10.996  8.837   71.557  1.00 8.47  ? 114 TYR C CB  1 
ATOM   5194 C  CG  . TYR C 1 114 ? 11.769  8.617   72.834  1.00 8.36  ? 114 TYR C CG  1 
ATOM   5195 C  CD1 . TYR C 1 114 ? 13.092  9.021   72.953  1.00 9.26  ? 114 TYR C CD1 1 
ATOM   5196 C  CD2 . TYR C 1 114 ? 11.176  8.003   73.921  1.00 9.32  ? 114 TYR C CD2 1 
ATOM   5197 C  CE1 . TYR C 1 114 ? 13.798  8.818   74.124  1.00 10.99 ? 114 TYR C CE1 1 
ATOM   5198 C  CE2 . TYR C 1 114 ? 11.877  7.793   75.094  1.00 11.82 ? 114 TYR C CE2 1 
ATOM   5199 C  CZ  . TYR C 1 114 ? 13.188  8.210   75.188  1.00 12.33 ? 114 TYR C CZ  1 
ATOM   5200 O  OH  . TYR C 1 114 ? 13.908  8.019   76.344  1.00 16.47 ? 114 TYR C OH  1 
ATOM   5201 N  N   . ALA C 1 115 ? 8.819   7.458   69.796  1.00 7.65  ? 115 ALA C N   1 
ATOM   5202 C  CA  . ALA C 1 115 ? 7.742   7.449   68.839  1.00 8.01  ? 115 ALA C CA  1 
ATOM   5203 C  C   . ALA C 1 115 ? 7.425   8.828   68.338  1.00 7.80  ? 115 ALA C C   1 
ATOM   5204 O  O   . ALA C 1 115 ? 6.829   9.008   67.265  1.00 8.42  ? 115 ALA C O   1 
ATOM   5205 C  CB  . ALA C 1 115 ? 6.523   6.810   69.533  1.00 9.99  ? 115 ALA C CB  1 
ATOM   5206 N  N   . ALA C 1 116 ? 7.692   9.864   69.153  1.00 8.06  ? 116 ALA C N   1 
ATOM   5207 C  CA  . ALA C 1 116 ? 7.356   11.248  68.701  1.00 8.06  ? 116 ALA C CA  1 
ATOM   5208 C  C   . ALA C 1 116 ? 8.131   12.169  69.595  1.00 7.62  ? 116 ALA C C   1 
ATOM   5209 O  O   . ALA C 1 116 ? 8.773   11.787  70.593  1.00 7.60  ? 116 ALA C O   1 
ATOM   5210 C  CB  . ALA C 1 116 ? 5.811   11.497  68.776  1.00 8.04  ? 116 ALA C CB  1 
ATOM   5211 N  N   . GLU C 1 117 ? 8.074   13.470  69.249  1.00 7.41  ? 117 GLU C N   1 
ATOM   5212 C  CA  . GLU C 1 117 ? 8.784   14.513  70.049  1.00 7.43  ? 117 GLU C CA  1 
ATOM   5213 C  C   . GLU C 1 117 ? 7.900   15.784  69.956  1.00 6.85  ? 117 GLU C C   1 
ATOM   5214 O  O   . GLU C 1 117 ? 7.523   16.196  68.850  1.00 8.79  ? 117 GLU C O   1 
ATOM   5215 C  CB  . GLU C 1 117 ? 10.186  14.728  69.486  1.00 8.26  ? 117 GLU C CB  1 
ATOM   5216 C  CG  . GLU C 1 117 ? 11.058  15.640  70.346  1.00 8.38  ? 117 GLU C CG  1 
ATOM   5217 C  CD  . GLU C 1 117 ? 12.519  15.734  69.911  1.00 8.15  ? 117 GLU C CD  1 
ATOM   5218 O  OE1 . GLU C 1 117 ? 13.000  14.726  69.313  1.00 8.47  ? 117 GLU C OE1 1 
ATOM   5219 O  OE2 . GLU C 1 117 ? 13.126  16.804  70.113  1.00 7.82  ? 117 GLU C OE2 1 
ATOM   5220 N  N   . LEU C 1 118 ? 7.631   16.350  71.109  1.00 7.40  ? 118 LEU C N   1 
ATOM   5221 C  CA  . LEU C 1 118 ? 6.876   17.602  71.278  1.00 6.75  ? 118 LEU C CA  1 
ATOM   5222 C  C   . LEU C 1 118 ? 7.867   18.747  71.378  1.00 6.66  ? 118 LEU C C   1 
ATOM   5223 O  O   . LEU C 1 118 ? 8.829   18.653  72.180  1.00 7.04  ? 118 LEU C O   1 
ATOM   5224 C  CB  . LEU C 1 118 ? 6.083   17.482  72.598  1.00 7.88  ? 118 LEU C CB  1 
ATOM   5225 C  CG  . LEU C 1 118 ? 5.474   18.799  73.181  1.00 8.05  ? 118 LEU C CG  1 
ATOM   5226 C  CD1 . LEU C 1 118 ? 4.474   19.431  72.206  1.00 9.23  ? 118 LEU C CD1 1 
ATOM   5227 C  CD2 . LEU C 1 118 ? 4.733   18.439  74.462  1.00 10.06 ? 118 LEU C CD2 1 
ATOM   5228 N  N   . HIS C 1 119 ? 7.647   19.838  70.604  1.00 6.45  ? 119 HIS C N   1 
ATOM   5229 C  CA  . HIS C 1 119 ? 8.451   21.044  70.649  1.00 6.90  ? 119 HIS C CA  1 
ATOM   5230 C  C   . HIS C 1 119 ? 7.608   22.231  71.051  1.00 6.75  ? 119 HIS C C   1 
ATOM   5231 O  O   . HIS C 1 119 ? 6.634   22.570  70.344  1.00 7.35  ? 119 HIS C O   1 
ATOM   5232 C  CB  . HIS C 1 119 ? 9.049   21.296  69.280  1.00 7.14  ? 119 HIS C CB  1 
ATOM   5233 C  CG  . HIS C 1 119 ? 10.118  20.289  68.960  1.00 6.47  ? 119 HIS C CG  1 
ATOM   5234 N  ND1 . HIS C 1 119 ? 10.541  20.038  67.675  1.00 7.42  ? 119 HIS C ND1 1 
ATOM   5235 C  CD2 . HIS C 1 119 ? 10.864  19.486  69.761  1.00 7.63  ? 119 HIS C CD2 1 
ATOM   5236 C  CE1 . HIS C 1 119 ? 11.514  19.147  67.682  1.00 7.22  ? 119 HIS C CE1 1 
ATOM   5237 N  NE2 . HIS C 1 119 ? 11.682  18.758  68.938  1.00 7.96  ? 119 HIS C NE2 1 
ATOM   5238 N  N   . LEU C 1 120 ? 7.919   22.837  72.204  1.00 7.51  ? 120 LEU C N   1 
ATOM   5239 C  CA  . LEU C 1 120 ? 7.308   24.081  72.632  1.00 7.82  ? 120 LEU C CA  1 
ATOM   5240 C  C   . LEU C 1 120 ? 8.269   25.211  72.333  1.00 7.22  ? 120 LEU C C   1 
ATOM   5241 O  O   . LEU C 1 120 ? 9.401   25.240  72.828  1.00 7.42  ? 120 LEU C O   1 
ATOM   5242 C  CB  . LEU C 1 120 ? 7.006   23.990  74.136  1.00 8.90  ? 120 LEU C CB  1 
ATOM   5243 C  CG  . LEU C 1 120 ? 5.922   22.944  74.473  1.00 9.24  ? 120 LEU C CG  1 
ATOM   5244 C  CD1 . LEU C 1 120 ? 6.423   21.994  75.507  1.00 13.00 ? 120 LEU C CD1 1 
ATOM   5245 C  CD2 . LEU C 1 120 ? 4.588   23.596  74.921  1.00 12.73 ? 120 LEU C CD2 1 
ATOM   5246 N  N   . VAL C 1 121 ? 7.809   26.045  71.377  1.00 7.75  ? 121 VAL C N   1 
ATOM   5247 C  CA  . VAL C 1 121 ? 8.708   27.095  70.819  1.00 8.20  ? 121 VAL C CA  1 
ATOM   5248 C  C   . VAL C 1 121 ? 8.448   28.450  71.497  1.00 7.45  ? 121 VAL C C   1 
ATOM   5249 O  O   . VAL C 1 121 ? 7.318   28.874  71.627  1.00 8.53  ? 121 VAL C O   1 
ATOM   5250 C  CB  . VAL C 1 121 ? 8.423   27.244  69.277  1.00 8.90  ? 121 VAL C CB  1 
ATOM   5251 C  CG1 . VAL C 1 121 ? 9.323   28.274  68.631  1.00 9.43  ? 121 VAL C CG1 1 
ATOM   5252 C  CG2 . VAL C 1 121 ? 8.473   25.868  68.562  1.00 9.29  ? 121 VAL C CG2 1 
ATOM   5253 N  N   . HIS C 1 122 ? 9.555   29.052  71.961  1.00 7.44  ? 122 HIS C N   1 
ATOM   5254 C  CA  . HIS C 1 122 ? 9.523   30.328  72.713  1.00 8.47  ? 122 HIS C CA  1 
ATOM   5255 C  C   . HIS C 1 122 ? 10.508  31.294  72.070  1.00 8.52  ? 122 HIS C C   1 
ATOM   5256 O  O   . HIS C 1 122 ? 11.605  30.901  71.654  1.00 8.49  ? 122 HIS C O   1 
ATOM   5257 C  CB  . HIS C 1 122 ? 9.957   30.118  74.184  1.00 8.60  ? 122 HIS C CB  1 
ATOM   5258 C  CG  . HIS C 1 122 ? 9.261   28.984  74.892  1.00 8.24  ? 122 HIS C CG  1 
ATOM   5259 N  ND1 . HIS C 1 122 ? 9.589   27.635  74.654  1.00 8.41  ? 122 HIS C ND1 1 
ATOM   5260 C  CD2 . HIS C 1 122 ? 8.278   28.941  75.901  1.00 9.10  ? 122 HIS C CD2 1 
ATOM   5261 C  CE1 . HIS C 1 122 ? 8.863   26.849  75.451  1.00 9.12  ? 122 HIS C CE1 1 
ATOM   5262 N  NE2 . HIS C 1 122 ? 8.052   27.619  76.206  1.00 8.89  ? 122 HIS C NE2 1 
ATOM   5263 N  N   . TRP C 1 123 ? 10.131  32.575  72.050  1.00 8.15  ? 123 TRP C N   1 
ATOM   5264 C  CA  . TRP C 1 123 ? 11.051  33.583  71.494  1.00 8.00  ? 123 TRP C CA  1 
ATOM   5265 C  C   . TRP C 1 123 ? 11.515  34.565  72.548  1.00 7.32  ? 123 TRP C C   1 
ATOM   5266 O  O   . TRP C 1 123 ? 10.812  34.903  73.542  1.00 9.11  ? 123 TRP C O   1 
ATOM   5267 C  CB  . TRP C 1 123 ? 10.405  34.367  70.322  1.00 10.36 ? 123 TRP C CB  1 
ATOM   5268 C  CG  . TRP C 1 123 ? 9.102   34.989  70.618  1.00 9.72  ? 123 TRP C CG  1 
ATOM   5269 C  CD1 . TRP C 1 123 ? 7.859   34.422  70.469  1.00 11.23 ? 123 TRP C CD1 1 
ATOM   5270 C  CD2 . TRP C 1 123 ? 8.855   36.356  71.005  1.00 10.89 ? 123 TRP C CD2 1 
ATOM   5271 N  NE1 . TRP C 1 123 ? 6.872   35.290  70.805  1.00 10.75 ? 123 TRP C NE1 1 
ATOM   5272 C  CE2 . TRP C 1 123 ? 7.422   36.481  71.173  1.00 11.86 ? 123 TRP C CE2 1 
ATOM   5273 C  CE3 . TRP C 1 123 ? 9.680   37.451  71.332  1.00 10.76 ? 123 TRP C CE3 1 
ATOM   5274 C  CZ2 . TRP C 1 123 ? 6.822   37.682  71.566  1.00 13.05 ? 123 TRP C CZ2 1 
ATOM   5275 C  CZ3 . TRP C 1 123 ? 9.064   38.648  71.732  1.00 11.53 ? 123 TRP C CZ3 1 
ATOM   5276 C  CH2 . TRP C 1 123 ? 7.682   38.750  71.837  1.00 13.06 ? 123 TRP C CH2 1 
ATOM   5277 N  N   . ASN C 1 124 ? 12.777  34.968  72.423  1.00 8.40  ? 124 ASN C N   1 
ATOM   5278 C  CA  . ASN C 1 124 ? 13.421  35.896  73.394  1.00 8.94  ? 124 ASN C CA  1 
ATOM   5279 C  C   . ASN C 1 124 ? 12.794  37.253  73.334  1.00 9.25  ? 124 ASN C C   1 
ATOM   5280 O  O   . ASN C 1 124 ? 12.872  37.945  72.334  1.00 9.54  ? 124 ASN C O   1 
ATOM   5281 C  CB  . ASN C 1 124 ? 14.904  35.925  73.046  1.00 9.85  ? 124 ASN C CB  1 
ATOM   5282 C  CG  . ASN C 1 124 ? 15.744  36.513  74.110  1.00 9.35  ? 124 ASN C CG  1 
ATOM   5283 O  OD1 . ASN C 1 124 ? 15.277  37.414  74.845  1.00 11.64 ? 124 ASN C OD1 1 
ATOM   5284 N  ND2 . ASN C 1 124 ? 16.975  36.048  74.228  1.00 11.11 ? 124 ASN C ND2 1 
ATOM   5285 N  N   . THR C 1 125 ? 12.225  37.685  74.452  1.00 10.40 ? 125 THR C N   1 
ATOM   5286 C  CA  . THR C 1 125 ? 11.500  38.984  74.480  1.00 11.20 ? 125 THR C CA  1 
ATOM   5287 C  C   . THR C 1 125 ? 12.388  40.170  74.274  1.00 11.59 ? 125 THR C C   1 
ATOM   5288 O  O   . THR C 1 125 ? 11.842  41.210  73.881  1.00 13.32 ? 125 THR C O   1 
ATOM   5289 C  CB  . THR C 1 125 ? 10.752  39.137  75.813  1.00 14.99 ? 125 THR C CB  1 
ATOM   5290 O  OG1 . THR C 1 125 ? 11.724  39.120  76.850  1.00 17.85 ? 125 THR C OG1 1 
ATOM   5291 C  CG2 . THR C 1 125 ? 9.664   38.024  75.929  1.00 17.54 ? 125 THR C CG2 1 
ATOM   5292 N  N   . LYS C 1 126 ? 13.709  40.012  74.330  1.00 11.41 ? 127 LYS C N   1 
ATOM   5293 C  CA  . LYS C 1 126 ? 14.564  41.155  74.037  1.00 13.34 ? 127 LYS C CA  1 
ATOM   5294 C  C   . LYS C 1 126 ? 14.533  41.517  72.573  1.00 11.51 ? 127 LYS C C   1 
ATOM   5295 O  O   . LYS C 1 126 ? 15.034  42.589  72.220  1.00 13.47 ? 127 LYS C O   1 
ATOM   5296 C  CB  . LYS C 1 126 ? 15.958  40.909  74.604  1.00 14.33 ? 127 LYS C CB  1 
ATOM   5297 C  CG  . LYS C 1 126 ? 16.808  40.019  73.780  1.00 15.06 ? 127 LYS C CG  1 
ATOM   5298 C  CD  . LYS C 1 126 ? 18.005  39.674  74.661  1.00 20.58 ? 127 LYS C CD  1 
ATOM   5299 C  CE  . LYS C 1 126 ? 18.988  39.042  73.809  1.00 25.76 ? 127 LYS C CE  1 
ATOM   5300 N  NZ  . LYS C 1 126 ? 20.363  39.671  73.848  1.00 38.54 ? 127 LYS C NZ  1 
ATOM   5301 N  N   . TYR C 1 127 ? 13.994  40.662  71.689  1.00 11.34 ? 128 TYR C N   1 
ATOM   5302 C  CA  . TYR C 1 127 ? 13.961  40.961  70.268  1.00 10.50 ? 128 TYR C CA  1 
ATOM   5303 C  C   . TYR C 1 127 ? 12.567  41.364  69.769  1.00 10.80 ? 128 TYR C C   1 
ATOM   5304 O  O   . TYR C 1 127 ? 12.367  41.596  68.575  1.00 11.12 ? 128 TYR C O   1 
ATOM   5305 C  CB  . TYR C 1 127 ? 14.525  39.785  69.425  1.00 11.02 ? 128 TYR C CB  1 
ATOM   5306 C  CG  . TYR C 1 127 ? 15.903  39.475  69.788  1.00 10.18 ? 128 TYR C CG  1 
ATOM   5307 C  CD1 . TYR C 1 127 ? 16.918  40.453  69.734  1.00 11.26 ? 128 TYR C CD1 1 
ATOM   5308 C  CD2 . TYR C 1 127 ? 16.260  38.200  70.259  1.00 10.65 ? 128 TYR C CD2 1 
ATOM   5309 C  CE1 . TYR C 1 127 ? 18.238  40.158  70.092  1.00 13.02 ? 128 TYR C CE1 1 
ATOM   5310 C  CE2 . TYR C 1 127 ? 17.551  37.890  70.606  1.00 10.75 ? 128 TYR C CE2 1 
ATOM   5311 C  CZ  . TYR C 1 127 ? 18.558  38.902  70.530  1.00 11.43 ? 128 TYR C CZ  1 
ATOM   5312 O  OH  . TYR C 1 127 ? 19.839  38.707  70.891  1.00 13.73 ? 128 TYR C OH  1 
ATOM   5313 N  N   . GLY C 1 128 ? 11.622  41.435  70.690  1.00 10.53 ? 129 GLY C N   1 
ATOM   5314 C  CA  . GLY C 1 128 ? 10.345  42.146  70.421  1.00 11.42 ? 129 GLY C CA  1 
ATOM   5315 C  C   . GLY C 1 128 ? 9.321   41.302  69.686  1.00 10.02 ? 129 GLY C C   1 
ATOM   5316 O  O   . GLY C 1 128 ? 8.095   41.412  69.960  1.00 12.63 ? 129 GLY C O   1 
ATOM   5317 N  N   . ASP C 1 129 ? 9.724   40.445  68.743  1.00 11.10 ? 130 ASP C N   1 
ATOM   5318 C  CA  . ASP C 1 129 ? 8.780   39.519  68.125  1.00 12.62 ? 130 ASP C CA  1 
ATOM   5319 C  C   . ASP C 1 129 ? 9.551   38.343  67.563  1.00 12.71 ? 130 ASP C C   1 
ATOM   5320 O  O   . ASP C 1 129 ? 10.778  38.353  67.504  1.00 12.63 ? 130 ASP C O   1 
ATOM   5321 C  CB  . ASP C 1 129 ? 7.800   40.191  67.161  1.00 15.07 ? 130 ASP C CB  1 
ATOM   5322 C  CG  . ASP C 1 129 ? 8.443   40.586  65.848  1.00 15.75 ? 130 ASP C CG  1 
ATOM   5323 O  OD1 . ASP C 1 129 ? 9.626   40.300  65.610  1.00 20.26 ? 130 ASP C OD1 1 
ATOM   5324 O  OD2 . ASP C 1 129 ? 7.734   41.182  65.031  1.00 22.09 ? 130 ASP C OD2 1 
ATOM   5325 N  N   . PHE C 1 130 ? 8.814   37.284  67.204  1.00 11.71 ? 131 PHE C N   1 
ATOM   5326 C  CA  . PHE C 1 130 ? 9.494   36.063  66.786  1.00 12.07 ? 131 PHE C CA  1 
ATOM   5327 C  C   . PHE C 1 130 ? 10.218  36.244  65.479  1.00 11.41 ? 131 PHE C C   1 
ATOM   5328 O  O   . PHE C 1 130 ? 11.255  35.608  65.276  1.00 11.15 ? 131 PHE C O   1 
ATOM   5329 C  CB  . PHE C 1 130 ? 8.551   34.857  66.738  1.00 15.29 ? 131 PHE C CB  1 
ATOM   5330 C  CG  . PHE C 1 130 ? 7.602   34.853  65.571  1.00 18.83 ? 131 PHE C CG  1 
ATOM   5331 C  CD1 . PHE C 1 130 ? 6.295   35.422  65.629  1.00 26.00 ? 131 PHE C CD1 1 
ATOM   5332 C  CD2 . PHE C 1 130 ? 7.999   34.247  64.370  1.00 21.53 ? 131 PHE C CD2 1 
ATOM   5333 C  CE1 . PHE C 1 130 ? 5.434   35.386  64.483  1.00 24.02 ? 131 PHE C CE1 1 
ATOM   5334 C  CE2 . PHE C 1 130 ? 7.122   34.226  63.248  1.00 26.10 ? 131 PHE C CE2 1 
ATOM   5335 C  CZ  . PHE C 1 130 ? 5.845   34.794  63.330  1.00 26.39 ? 131 PHE C CZ  1 
ATOM   5336 N  N   . GLY C 1 131 ? 9.666   37.069  64.527  1.00 12.35 ? 132 GLY C N   1 
ATOM   5337 C  CA  . GLY C 1 131 ? 10.344  37.159  63.216  1.00 12.46 ? 132 GLY C CA  1 
ATOM   5338 C  C   . GLY C 1 131 ? 11.720  37.816  63.348  1.00 13.65 ? 132 GLY C C   1 
ATOM   5339 O  O   . GLY C 1 131 ? 12.620  37.524  62.621  1.00 15.15 ? 132 GLY C O   1 
ATOM   5340 N  N   . LYS C 1 132 ? 11.876  38.739  64.292  1.00 12.79 ? 133 LYS C N   1 
ATOM   5341 C  CA  . LYS C 1 132 ? 13.210  39.292  64.593  1.00 12.84 ? 133 LYS C CA  1 
ATOM   5342 C  C   . LYS C 1 132 ? 14.075  38.345  65.392  1.00 11.43 ? 133 LYS C C   1 
ATOM   5343 O  O   . LYS C 1 132 ? 15.284  38.239  65.225  1.00 12.17 ? 133 LYS C O   1 
ATOM   5344 C  CB  . LYS C 1 132 ? 13.091  40.671  65.245  1.00 12.67 ? 133 LYS C CB  1 
ATOM   5345 C  CG  . LYS C 1 132 ? 12.302  41.717  64.373  1.00 17.94 ? 133 LYS C CG  1 
ATOM   5346 C  CD  . LYS C 1 132 ? 12.818  41.887  62.942  1.00 24.12 ? 133 LYS C CD  1 
ATOM   5347 C  CE  . LYS C 1 132 ? 14.237  42.405  63.233  1.00 25.63 ? 133 LYS C CE  1 
ATOM   5348 N  NZ  . LYS C 1 132 ? 14.315  43.756  63.883  1.00 41.77 ? 133 LYS C NZ  1 
ATOM   5349 N  N   . ALA C 1 133 ? 13.451  37.635  66.327  1.00 11.35 ? 134 ALA C N   1 
ATOM   5350 C  CA  . ALA C 1 133 ? 14.173  36.675  67.138  1.00 11.53 ? 134 ALA C CA  1 
ATOM   5351 C  C   . ALA C 1 133 ? 14.886  35.596  66.331  1.00 9.82  ? 134 ALA C C   1 
ATOM   5352 O  O   . ALA C 1 133 ? 16.030  35.241  66.665  1.00 10.39 ? 134 ALA C O   1 
ATOM   5353 C  CB  . ALA C 1 133 ? 13.234  36.056  68.152  1.00 11.03 ? 134 ALA C CB  1 
ATOM   5354 N  N   . VAL C 1 134 ? 14.291  35.117  65.250  1.00 9.61  ? 135 VAL C N   1 
ATOM   5355 C  CA  . VAL C 1 134 ? 14.910  34.005  64.518  1.00 9.87  ? 135 VAL C CA  1 
ATOM   5356 C  C   . VAL C 1 134 ? 16.128  34.423  63.772  1.00 11.33 ? 135 VAL C C   1 
ATOM   5357 O  O   . VAL C 1 134 ? 16.863  33.559  63.298  1.00 12.16 ? 135 VAL C O   1 
ATOM   5358 C  CB  . VAL C 1 134 ? 13.942  33.305  63.531  1.00 11.73 ? 135 VAL C CB  1 
ATOM   5359 C  CG1 . VAL C 1 134 ? 12.785  32.650  64.306  1.00 14.47 ? 135 VAL C CG1 1 
ATOM   5360 C  CG2 . VAL C 1 134 ? 13.426  34.198  62.389  1.00 12.51 ? 135 VAL C CG2 1 
ATOM   5361 N  N   . GLN C 1 135 ? 16.348  35.752  63.678  1.00 11.21 ? 136 GLN C N   1 
ATOM   5362 C  CA  . GLN C 1 135 ? 17.567  36.281  63.065  1.00 12.36 ? 136 GLN C CA  1 
ATOM   5363 C  C   . GLN C 1 135 ? 18.752  36.377  64.041  1.00 12.63 ? 136 GLN C C   1 
ATOM   5364 O  O   . GLN C 1 135 ? 19.821  36.950  63.694  1.00 14.84 ? 136 GLN C O   1 
ATOM   5365 C  CB  . GLN C 1 135 ? 17.251  37.666  62.405  1.00 13.92 ? 136 GLN C CB  1 
ATOM   5366 C  CG  . GLN C 1 135 ? 16.220  37.549  61.335  1.00 16.48 ? 136 GLN C CG  1 
ATOM   5367 C  CD  . GLN C 1 135 ? 15.859  38.914  60.756  1.00 22.37 ? 136 GLN C CD  1 
ATOM   5368 O  OE1 . GLN C 1 135 ? 14.657  39.350  60.773  1.00 31.29 ? 136 GLN C OE1 1 
ATOM   5369 N  NE2 . GLN C 1 135 ? 16.897  39.662  60.354  1.00 29.61 ? 136 GLN C NE2 1 
ATOM   5370 N  N   . GLN C 1 136 ? 18.567  35.913  65.285  1.00 11.38 ? 137 GLN C N   1 
ATOM   5371 C  CA  . GLN C 1 136 ? 19.578  36.099  66.349  1.00 11.35 ? 137 GLN C CA  1 
ATOM   5372 C  C   . GLN C 1 136 ? 20.033  34.765  66.828  1.00 13.13 ? 137 GLN C C   1 
ATOM   5373 O  O   . GLN C 1 136 ? 19.226  33.813  66.980  1.00 11.58 ? 137 GLN C O   1 
ATOM   5374 C  CB  . GLN C 1 136 ? 19.030  36.867  67.552  1.00 11.61 ? 137 GLN C CB  1 
ATOM   5375 C  CG  . GLN C 1 136 ? 18.253  38.070  67.123  1.00 16.26 ? 137 GLN C CG  1 
ATOM   5376 C  CD  . GLN C 1 136 ? 18.994  39.051  66.305  1.00 17.04 ? 137 GLN C CD  1 
ATOM   5377 O  OE1 . GLN C 1 136 ? 20.185  39.228  66.442  1.00 16.47 ? 137 GLN C OE1 1 
ATOM   5378 N  NE2 . GLN C 1 136 ? 18.231  39.761  65.428  1.00 20.50 ? 137 GLN C NE2 1 
ATOM   5379 N  N   . PRO C 1 137 ? 21.286  34.644  67.316  1.00 11.31 ? 138 PRO C N   1 
ATOM   5380 C  CA  . PRO C 1 137 ? 21.822  33.345  67.727  1.00 12.36 ? 138 PRO C CA  1 
ATOM   5381 C  C   . PRO C 1 137 ? 21.145  32.861  68.991  1.00 13.99 ? 138 PRO C C   1 
ATOM   5382 O  O   . PRO C 1 137 ? 21.216  31.660  69.261  1.00 14.18 ? 138 PRO C O   1 
ATOM   5383 C  CB  . PRO C 1 137 ? 23.349  33.570  67.917  1.00 17.07 ? 138 PRO C CB  1 
ATOM   5384 C  CG  . PRO C 1 137 ? 23.483  35.044  67.825  1.00 21.13 ? 138 PRO C CG  1 
ATOM   5385 C  CD  . PRO C 1 137 ? 22.312  35.703  67.173  1.00 15.49 ? 138 PRO C CD  1 
ATOM   5386 N  N   . ASP C 1 138 ? 20.524  33.763  69.774  1.00 10.60 ? 139 ASP C N   1 
ATOM   5387 C  CA  . ASP C 1 138 ? 19.866  33.372  71.002  1.00 11.66 ? 139 ASP C CA  1 
ATOM   5388 C  C   . ASP C 1 138 ? 18.381  33.749  70.885  1.00 10.83 ? 139 ASP C C   1 
ATOM   5389 O  O   . ASP C 1 138 ? 17.776  34.143  71.895  1.00 11.18 ? 139 ASP C O   1 
ATOM   5390 C  CB  . ASP C 1 138 ? 20.549  34.014  72.266  1.00 13.68 ? 139 ASP C CB  1 
ATOM   5391 C  CG  . ASP C 1 138 ? 20.650  35.526  72.193  1.00 13.93 ? 139 ASP C CG  1 
ATOM   5392 O  OD1 . ASP C 1 138 ? 20.378  36.100  71.124  1.00 14.07 ? 139 ASP C OD1 1 
ATOM   5393 O  OD2 . ASP C 1 138 ? 20.999  36.134  73.225  1.00 18.69 ? 139 ASP C OD2 1 
ATOM   5394 N  N   . GLY C 1 139 ? 17.806  33.700  69.684  1.00 10.50 ? 140 GLY C N   1 
ATOM   5395 C  CA  . GLY C 1 139 ? 16.459  34.170  69.497  1.00 10.08 ? 140 GLY C CA  1 
ATOM   5396 C  C   . GLY C 1 139 ? 15.381  33.279  70.042  1.00 8.41  ? 140 GLY C C   1 
ATOM   5397 O  O   . GLY C 1 139 ? 14.349  33.787  70.421  1.00 9.07  ? 140 GLY C O   1 
ATOM   5398 N  N   . LEU C 1 140 ? 15.575  31.954  70.017  1.00 8.37  ? 141 LEU C N   1 
ATOM   5399 C  CA  . LEU C 1 140 ? 14.533  31.030  70.412  1.00 7.46  ? 141 LEU C CA  1 
ATOM   5400 C  C   . LEU C 1 140 ? 15.013  30.085  71.461  1.00 7.66  ? 141 LEU C C   1 
ATOM   5401 O  O   . LEU C 1 140 ? 16.200  29.786  71.531  1.00 8.18  ? 141 LEU C O   1 
ATOM   5402 C  CB  . LEU C 1 140 ? 14.091  30.158  69.238  1.00 8.15  ? 141 LEU C CB  1 
ATOM   5403 C  CG  . LEU C 1 140 ? 13.471  30.872  68.042  1.00 9.24  ? 141 LEU C CG  1 
ATOM   5404 C  CD1 . LEU C 1 140 ? 12.955  29.810  67.035  1.00 10.67 ? 141 LEU C CD1 1 
ATOM   5405 C  CD2 . LEU C 1 140 ? 12.343  31.842  68.390  1.00 10.81 ? 141 LEU C CD2 1 
ATOM   5406 N  N   . ALA C 1 141 ? 14.064  29.575  72.272  1.00 7.50  ? 142 ALA C N   1 
ATOM   5407 C  CA  . ALA C 1 141 ? 14.363  28.444  73.155  1.00 8.22  ? 142 ALA C CA  1 
ATOM   5408 C  C   . ALA C 1 141 ? 13.277  27.468  72.887  1.00 7.46  ? 142 ALA C C   1 
ATOM   5409 O  O   . ALA C 1 141 ? 12.079  27.804  72.909  1.00 8.29  ? 142 ALA C O   1 
ATOM   5410 C  CB  . ALA C 1 141 ? 14.288  28.876  74.636  1.00 8.92  ? 142 ALA C CB  1 
ATOM   5411 N  N   . VAL C 1 142 ? 13.672  26.232  72.471  1.00 7.56  ? 143 VAL C N   1 
ATOM   5412 C  CA  . VAL C 1 142 ? 12.665  25.181  72.183  1.00 7.91  ? 143 VAL C CA  1 
ATOM   5413 C  C   . VAL C 1 142 ? 12.796  24.109  73.270  1.00 7.09  ? 143 VAL C C   1 
ATOM   5414 O  O   . VAL C 1 142 ? 13.909  23.616  73.477  1.00 8.22  ? 143 VAL C O   1 
ATOM   5415 C  CB  . VAL C 1 142 ? 12.778  24.589  70.748  1.00 7.23  ? 143 VAL C CB  1 
ATOM   5416 C  CG1 . VAL C 1 142 ? 11.645  23.598  70.521  1.00 7.94  ? 143 VAL C CG1 1 
ATOM   5417 C  CG2 . VAL C 1 142 ? 12.674  25.707  69.696  1.00 8.66  ? 143 VAL C CG2 1 
ATOM   5418 N  N   . LEU C 1 143 ? 11.688  23.841  73.944  1.00 7.35  ? 144 LEU C N   1 
ATOM   5419 C  CA  . LEU C 1 143 ? 11.606  22.804  74.965  1.00 7.87  ? 144 LEU C CA  1 
ATOM   5420 C  C   . LEU C 1 143 ? 11.121  21.560  74.210  1.00 6.81  ? 144 LEU C C   1 
ATOM   5421 O  O   . LEU C 1 143 ? 10.036  21.506  73.665  1.00 8.51  ? 144 LEU C O   1 
ATOM   5422 C  CB  . LEU C 1 143 ? 10.656  23.272  76.089  1.00 9.99  ? 144 LEU C CB  1 
ATOM   5423 C  CG  . LEU C 1 143 ? 10.461  22.284  77.221  1.00 10.33 ? 144 LEU C CG  1 
ATOM   5424 C  CD1 . LEU C 1 143 ? 11.806  22.011  77.899  1.00 10.55 ? 144 LEU C CD1 1 
ATOM   5425 C  CD2 . LEU C 1 143 ? 9.425   22.934  78.187  1.00 11.43 ? 144 LEU C CD2 1 
ATOM   5426 N  N   . GLY C 1 144 ? 11.992  20.541  74.241  1.00 7.19  ? 145 GLY C N   1 
ATOM   5427 C  CA  . GLY C 1 144 ? 11.680  19.251  73.553  1.00 7.19  ? 145 GLY C CA  1 
ATOM   5428 C  C   . GLY C 1 144 ? 11.337  18.165  74.605  1.00 6.54  ? 145 GLY C C   1 
ATOM   5429 O  O   . GLY C 1 144 ? 12.023  18.006  75.579  1.00 8.39  ? 145 GLY C O   1 
ATOM   5430 N  N   . ILE C 1 145 ? 10.280  17.417  74.291  1.00 7.26  ? 146 ILE C N   1 
ATOM   5431 C  CA  . ILE C 1 145 ? 9.801   16.351  75.211  1.00 7.74  ? 146 ILE C CA  1 
ATOM   5432 C  C   . ILE C 1 145 ? 9.535   15.138  74.372  1.00 7.47  ? 146 ILE C C   1 
ATOM   5433 O  O   . ILE C 1 145 ? 8.814   15.168  73.376  1.00 7.89  ? 146 ILE C O   1 
ATOM   5434 C  CB  . ILE C 1 145 ? 8.515   16.832  75.948  1.00 8.37  ? 146 ILE C CB  1 
ATOM   5435 C  CG1 . ILE C 1 145 ? 8.804   18.105  76.785  1.00 10.42 ? 146 ILE C CG1 1 
ATOM   5436 C  CG2 . ILE C 1 145 ? 7.922   15.755  76.790  1.00 10.00 ? 146 ILE C CG2 1 
ATOM   5437 C  CD1 . ILE C 1 145 ? 7.589   18.797  77.393  1.00 11.24 ? 146 ILE C CD1 1 
ATOM   5438 N  N   . PHE C 1 146 ? 10.113  14.024  74.762  1.00 7.32  ? 147 PHE C N   1 
ATOM   5439 C  CA  . PHE C 1 146 ? 9.922   12.752  74.022  1.00 7.78  ? 147 PHE C CA  1 
ATOM   5440 C  C   . PHE C 1 146 ? 8.565   12.141  74.398  1.00 7.62  ? 147 PHE C C   1 
ATOM   5441 O  O   . PHE C 1 146 ? 8.085   12.309  75.518  1.00 8.73  ? 147 PHE C O   1 
ATOM   5442 C  CB  . PHE C 1 146 ? 11.029  11.789  74.384  1.00 7.91  ? 147 PHE C CB  1 
ATOM   5443 C  CG  . PHE C 1 146 ? 12.394  12.235  73.943  1.00 7.09  ? 147 PHE C CG  1 
ATOM   5444 C  CD1 . PHE C 1 146 ? 12.686  12.410  72.600  1.00 7.32  ? 147 PHE C CD1 1 
ATOM   5445 C  CD2 . PHE C 1 146 ? 13.390  12.470  74.875  1.00 8.36  ? 147 PHE C CD2 1 
ATOM   5446 C  CE1 . PHE C 1 146 ? 13.944  12.816  72.196  1.00 8.22  ? 147 PHE C CE1 1 
ATOM   5447 C  CE2 . PHE C 1 146 ? 14.650  12.876  74.479  1.00 8.85  ? 147 PHE C CE2 1 
ATOM   5448 C  CZ  . PHE C 1 146 ? 14.928  13.049  73.138  1.00 7.92  ? 147 PHE C CZ  1 
ATOM   5449 N  N   . LEU C 1 147 ? 7.998   11.415  73.435  1.00 8.25  ? 148 LEU C N   1 
ATOM   5450 C  CA  . LEU C 1 147 ? 6.772   10.632  73.637  1.00 7.46  ? 148 LEU C CA  1 
ATOM   5451 C  C   . LEU C 1 147 ? 7.127   9.168   73.383  1.00 8.87  ? 148 LEU C C   1 
ATOM   5452 O  O   . LEU C 1 147 ? 7.671   8.809   72.325  1.00 8.82  ? 148 LEU C O   1 
ATOM   5453 C  CB  . LEU C 1 147 ? 5.659   10.974  72.655  1.00 8.29  ? 148 LEU C CB  1 
ATOM   5454 C  CG  . LEU C 1 147 ? 4.900   12.289  72.973  1.00 9.18  ? 148 LEU C CG  1 
ATOM   5455 C  CD1 . LEU C 1 147 ? 5.732   13.579  73.104  1.00 10.50 ? 148 LEU C CD1 1 
ATOM   5456 C  CD2 . LEU C 1 147 ? 3.770   12.500  71.933  1.00 10.21 ? 148 LEU C CD2 1 
ATOM   5457 N  N   . LYS C 1 148 ? 6.705   8.307   74.319  1.00 8.56  ? 149 LYS C N   1 
ATOM   5458 C  CA  . LYS C 1 148 ? 6.752   6.855   74.148  1.00 10.19 ? 149 LYS C CA  1 
ATOM   5459 C  C   . LYS C 1 148 ? 5.320   6.374   74.171  1.00 9.75  ? 149 LYS C C   1 
ATOM   5460 O  O   . LYS C 1 148 ? 4.415   7.007   74.710  1.00 10.81 ? 149 LYS C O   1 
ATOM   5461 C  CB  . LYS C 1 148 ? 7.628   6.172   75.217  1.00 11.83 ? 149 LYS C CB  1 
ATOM   5462 C  CG  . LYS C 1 148 ? 7.033   6.296   76.632  1.00 12.39 ? 149 LYS C CG  1 
ATOM   5463 C  CD  . LYS C 1 148 ? 7.968   5.566   77.617  1.00 18.59 ? 149 LYS C CD  1 
ATOM   5464 C  CE  . LYS C 1 148 ? 7.245   5.175   78.896  1.00 27.95 ? 149 LYS C CE  1 
ATOM   5465 N  NZ  . LYS C 1 148 ? 8.129   4.138   79.457  1.00 41.96 ? 149 LYS C NZ  1 
ATOM   5466 N  N   . VAL C 1 149 ? 5.043   5.199   73.585  1.00 10.65 ? 150 VAL C N   1 
ATOM   5467 C  CA  . VAL C 1 149 ? 3.731   4.644   73.544  1.00 10.64 ? 150 VAL C CA  1 
ATOM   5468 C  C   . VAL C 1 149 ? 3.512   3.689   74.745  1.00 10.59 ? 150 VAL C C   1 
ATOM   5469 O  O   . VAL C 1 149 ? 4.291   2.753   74.984  1.00 12.41 ? 150 VAL C O   1 
ATOM   5470 C  CB  . VAL C 1 149 ? 3.532   3.864   72.215  1.00 10.72 ? 150 VAL C CB  1 
ATOM   5471 C  CG1 . VAL C 1 149 ? 2.227   3.079   72.190  1.00 12.57 ? 150 VAL C CG1 1 
ATOM   5472 C  CG2 . VAL C 1 149 ? 3.567   4.850   71.064  1.00 13.94 ? 150 VAL C CG2 1 
ATOM   5473 N  N   . GLY C 1 150 ? 2.469   3.966   75.511  1.00 9.88  ? 151 GLY C N   1 
ATOM   5474 C  CA  . GLY C 1 150 ? 2.167   3.147   76.701  1.00 11.98 ? 151 GLY C CA  1 
ATOM   5475 C  C   . GLY C 1 150 ? 0.829   3.650   77.181  1.00 10.88 ? 151 GLY C C   1 
ATOM   5476 O  O   . GLY C 1 150 ? -0.162  3.553   76.443  1.00 11.80 ? 151 GLY C O   1 
ATOM   5477 N  N   A SER C 1 151 ? 0.773   4.109   78.444  0.50 12.10 ? 152 SER C N   1 
ATOM   5478 N  N   B SER C 1 151 ? 0.807   4.138   78.432  0.50 12.05 ? 152 SER C N   1 
ATOM   5479 C  CA  A SER C 1 151 ? -0.524  4.658   78.965  0.50 12.71 ? 152 SER C CA  1 
ATOM   5480 C  CA  B SER C 1 151 ? -0.461  4.731   78.952  0.50 13.15 ? 152 SER C CA  1 
ATOM   5481 C  C   A SER C 1 151 ? -0.863  5.993   78.282  0.50 11.45 ? 152 SER C C   1 
ATOM   5482 C  C   B SER C 1 151 ? -0.875  5.985   78.160  0.50 12.56 ? 152 SER C C   1 
ATOM   5483 O  O   A SER C 1 151 ? 0.073   6.724   77.830  0.50 11.55 ? 152 SER C O   1 
ATOM   5484 O  O   B SER C 1 151 ? -0.038  6.650   77.526  0.50 11.58 ? 152 SER C O   1 
ATOM   5485 C  CB  A SER C 1 151 ? -0.422  4.928   80.456  0.50 15.30 ? 152 SER C CB  1 
ATOM   5486 C  CB  B SER C 1 151 ? -0.306  5.134   80.407  0.50 14.56 ? 152 SER C CB  1 
ATOM   5487 O  OG  A SER C 1 151 ? 0.558   5.931   80.713  0.50 17.99 ? 152 SER C OG  1 
ATOM   5488 O  OG  B SER C 1 151 ? 0.104   4.038   81.174  0.50 18.67 ? 152 SER C OG  1 
ATOM   5489 N  N   . ALA C 1 152 ? -2.176  6.258   78.087  1.00 11.80 ? 153 ALA C N   1 
ATOM   5490 C  CA  . ALA C 1 152 ? -2.636  7.516   77.497  1.00 11.78 ? 153 ALA C CA  1 
ATOM   5491 C  C   . ALA C 1 152 ? -2.209  8.723   78.288  1.00 10.54 ? 153 ALA C C   1 
ATOM   5492 O  O   . ALA C 1 152 ? -2.033  8.647   79.562  1.00 13.03 ? 153 ALA C O   1 
ATOM   5493 C  CB  . ALA C 1 152 ? -4.165  7.518   77.384  1.00 13.71 ? 153 ALA C CB  1 
ATOM   5494 N  N   . LYS C 1 153 ? -2.009  9.841   77.578  1.00 11.50 ? 154 LYS C N   1 
ATOM   5495 C  CA  . LYS C 1 153 ? -1.717  11.143  78.283  1.00 10.87 ? 154 LYS C CA  1 
ATOM   5496 C  C   . LYS C 1 153 ? -3.065  11.915  78.273  1.00 11.14 ? 154 LYS C C   1 
ATOM   5497 O  O   . LYS C 1 153 ? -3.520  12.359  77.213  1.00 10.64 ? 154 LYS C O   1 
ATOM   5498 C  CB  . LYS C 1 153 ? -0.613  11.916  77.574  1.00 10.85 ? 154 LYS C CB  1 
ATOM   5499 C  CG  . LYS C 1 153 ? -0.091  13.164  78.335  1.00 13.12 ? 154 LYS C CG  1 
ATOM   5500 C  CD  . LYS C 1 153 ? 0.669   12.731  79.647  1.00 13.47 ? 154 LYS C CD  1 
ATOM   5501 C  CE  . LYS C 1 153 ? 1.432   13.886  80.329  1.00 15.04 ? 154 LYS C CE  1 
ATOM   5502 N  NZ  . LYS C 1 153 ? 1.874   13.585  81.723  1.00 23.52 ? 154 LYS C NZ  1 
ATOM   5503 N  N   . PRO C 1 154 ? -3.748  11.977  79.450  1.00 12.73 ? 155 PRO C N   1 
ATOM   5504 C  CA  . PRO C 1 154 ? -5.112  12.600  79.386  1.00 13.57 ? 155 PRO C CA  1 
ATOM   5505 C  C   . PRO C 1 154 ? -5.067  14.038  78.886  1.00 11.65 ? 155 PRO C C   1 
ATOM   5506 O  O   . PRO C 1 154 ? -5.976  14.400  78.145  1.00 14.60 ? 155 PRO C O   1 
ATOM   5507 C  CB  . PRO C 1 154 ? -5.621  12.488  80.838  1.00 15.28 ? 155 PRO C CB  1 
ATOM   5508 C  CG  . PRO C 1 154 ? -4.776  11.344  81.448  1.00 16.51 ? 155 PRO C CG  1 
ATOM   5509 C  CD  . PRO C 1 154 ? -3.447  11.369  80.765  1.00 12.82 ? 155 PRO C CD  1 
ATOM   5510 N  N   . GLY C 1 155 ? -4.002  14.797  79.174  1.00 12.09 ? 156 GLY C N   1 
ATOM   5511 C  CA  . GLY C 1 155 ? -3.969  16.193  78.773  1.00 13.50 ? 156 GLY C CA  1 
ATOM   5512 C  C   . GLY C 1 155 ? -3.649  16.372  77.305  1.00 11.38 ? 156 GLY C C   1 
ATOM   5513 O  O   . GLY C 1 155 ? -3.766  17.476  76.780  1.00 16.31 ? 156 GLY C O   1 
ATOM   5514 N  N   . LEU C 1 156 ? -3.327  15.286  76.571  1.00 10.39 ? 157 LEU C N   1 
ATOM   5515 C  CA  . LEU C 1 156 ? -3.186  15.335  75.148  1.00 10.18 ? 157 LEU C CA  1 
ATOM   5516 C  C   . LEU C 1 156 ? -4.516  15.127  74.416  1.00 11.25 ? 157 LEU C C   1 
ATOM   5517 O  O   . LEU C 1 156 ? -4.628  15.398  73.180  1.00 10.47 ? 157 LEU C O   1 
ATOM   5518 C  CB  . LEU C 1 156 ? -2.138  14.301  74.717  1.00 11.16 ? 157 LEU C CB  1 
ATOM   5519 C  CG  . LEU C 1 156 ? -1.840  14.157  73.204  1.00 10.83 ? 157 LEU C CG  1 
ATOM   5520 C  CD1 . LEU C 1 156 ? -1.249  15.450  72.634  1.00 12.78 ? 157 LEU C CD1 1 
ATOM   5521 C  CD2 . LEU C 1 156 ? -0.863  12.995  72.935  1.00 12.27 ? 157 LEU C CD2 1 
ATOM   5522 N  N   . GLN C 1 157 ? -5.536  14.559  75.099  1.00 11.11 ? 158 GLN C N   1 
ATOM   5523 C  CA  . GLN C 1 157 ? -6.726  14.092  74.351  1.00 13.03 ? 158 GLN C CA  1 
ATOM   5524 C  C   . GLN C 1 157 ? -7.473  15.210  73.646  1.00 10.95 ? 158 GLN C C   1 
ATOM   5525 O  O   . GLN C 1 157 ? -7.910  14.982  72.537  1.00 11.53 ? 158 GLN C O   1 
ATOM   5526 C  CB  . GLN C 1 157 ? -7.640  13.306  75.265  1.00 13.64 ? 158 GLN C CB  1 
ATOM   5527 C  CG  . GLN C 1 157 ? -8.759  12.533  74.498  1.00 15.21 ? 158 GLN C CG  1 
ATOM   5528 C  CD  . GLN C 1 157 ? -8.172  11.504  73.544  1.00 14.12 ? 158 GLN C CD  1 
ATOM   5529 O  OE1 . GLN C 1 157 ? -7.057  10.919  73.772  1.00 13.84 ? 158 GLN C OE1 1 
ATOM   5530 N  NE2 . GLN C 1 157 ? -8.831  11.281  72.449  1.00 14.58 ? 158 GLN C NE2 1 
ATOM   5531 N  N   . LYS C 1 158 ? -7.506  16.446  74.177  1.00 13.48 ? 159 LYS C N   1 
ATOM   5532 C  CA  . LYS C 1 158 ? -8.176  17.554  73.489  1.00 13.55 ? 159 LYS C CA  1 
ATOM   5533 C  C   . LYS C 1 158 ? -7.550  17.847  72.137  1.00 13.77 ? 159 LYS C C   1 
ATOM   5534 O  O   . LYS C 1 158 ? -8.235  18.174  71.178  1.00 13.88 ? 159 LYS C O   1 
ATOM   5535 C  CB  . LYS C 1 158 ? -8.284  18.742  74.464  1.00 15.76 ? 159 LYS C CB  1 
ATOM   5536 C  CG  . LYS C 1 158 ? -9.467  18.567  75.429  1.00 26.00 ? 159 LYS C CG  1 
ATOM   5537 C  CD  . LYS C 1 158 ? -9.807  19.838  76.224  1.00 33.75 ? 159 LYS C CD  1 
ATOM   5538 C  CE  . LYS C 1 158 ? -10.513 19.579  77.588  1.00 41.91 ? 159 LYS C CE  1 
ATOM   5539 N  NZ  . LYS C 1 158 ? -10.699 20.815  78.469  1.00 36.61 ? 159 LYS C NZ  1 
ATOM   5540 N  N   . VAL C 1 159 ? -6.200  17.700  72.075  1.00 12.12 ? 160 VAL C N   1 
ATOM   5541 C  CA  . VAL C 1 159 ? -5.507  17.867  70.825  1.00 10.56 ? 160 VAL C CA  1 
ATOM   5542 C  C   . VAL C 1 159 ? -5.910  16.759  69.842  1.00 11.19 ? 160 VAL C C   1 
ATOM   5543 O  O   . VAL C 1 159 ? -6.263  17.001  68.675  1.00 13.01 ? 160 VAL C O   1 
ATOM   5544 C  CB  . VAL C 1 159 ? -3.971  17.860  71.024  1.00 11.00 ? 160 VAL C CB  1 
ATOM   5545 C  CG1 . VAL C 1 159 ? -3.288  17.864  69.669  1.00 12.40 ? 160 VAL C CG1 1 
ATOM   5546 C  CG2 . VAL C 1 159 ? -3.556  19.076  71.828  1.00 14.56 ? 160 VAL C CG2 1 
ATOM   5547 N  N   . VAL C 1 160 ? -5.804  15.513  70.276  1.00 10.66 ? 161 VAL C N   1 
ATOM   5548 C  CA  . VAL C 1 160 ? -6.153  14.353  69.461  1.00 13.79 ? 161 VAL C CA  1 
ATOM   5549 C  C   . VAL C 1 160 ? -7.534  14.477  68.895  1.00 12.36 ? 161 VAL C C   1 
ATOM   5550 O  O   . VAL C 1 160 ? -7.713  14.186  67.699  1.00 13.17 ? 161 VAL C O   1 
ATOM   5551 C  CB  . VAL C 1 160 ? -6.041  12.980  70.315  1.00 15.07 ? 161 VAL C CB  1 
ATOM   5552 C  CG1 . VAL C 1 160 ? -6.701  11.789  69.613  1.00 16.68 ? 161 VAL C CG1 1 
ATOM   5553 C  CG2 . VAL C 1 160 ? -4.604  12.768  70.674  1.00 17.49 ? 161 VAL C CG2 1 
ATOM   5554 N  N   . ASP C 1 161 ? -8.475  14.884  69.741  1.00 11.85 ? 162 ASP C N   1 
ATOM   5555 C  CA  . ASP C 1 161 ? -9.844  14.938  69.287  1.00 14.95 ? 162 ASP C CA  1 
ATOM   5556 C  C   . ASP C 1 161 ? -10.170 15.941  68.233  1.00 15.69 ? 162 ASP C C   1 
ATOM   5557 O  O   . ASP C 1 161 ? -11.177 15.800  67.493  1.00 20.47 ? 162 ASP C O   1 
ATOM   5558 C  CB  . ASP C 1 161 ? -10.778 14.990  70.454  1.00 19.83 ? 162 ASP C CB  1 
ATOM   5559 C  CG  . ASP C 1 161 ? -10.941 13.639  71.103  1.00 17.88 ? 162 ASP C CG  1 
ATOM   5560 O  OD1 . ASP C 1 161 ? -10.804 12.620  70.389  1.00 22.65 ? 162 ASP C OD1 1 
ATOM   5561 O  OD2 . ASP C 1 161 ? -11.163 13.592  72.328  1.00 20.39 ? 162 ASP C OD2 1 
ATOM   5562 N  N   . VAL C 1 162 ? -9.386  17.024  68.146  1.00 14.21 ? 163 VAL C N   1 
ATOM   5563 C  CA  . VAL C 1 162 ? -9.700  18.045  67.134  1.00 14.09 ? 163 VAL C CA  1 
ATOM   5564 C  C   . VAL C 1 162 ? -9.042  17.727  65.799  1.00 12.01 ? 163 VAL C C   1 
ATOM   5565 O  O   . VAL C 1 162 ? -9.265  18.405  64.802  1.00 13.86 ? 163 VAL C O   1 
ATOM   5566 C  CB  . VAL C 1 162 ? -9.226  19.451  67.654  1.00 14.57 ? 163 VAL C CB  1 
ATOM   5567 C  CG1 . VAL C 1 162 ? -7.703  19.629  67.614  1.00 14.75 ? 163 VAL C CG1 1 
ATOM   5568 C  CG2 . VAL C 1 162 ? -9.938  20.646  66.987  1.00 16.30 ? 163 VAL C CG2 1 
ATOM   5569 N  N   . LEU C 1 163 ? -8.105  16.736  65.748  1.00 14.14 ? 164 LEU C N   1 
ATOM   5570 C  CA  . LEU C 1 163 ? -7.363  16.512  64.507  1.00 12.27 ? 164 LEU C CA  1 
ATOM   5571 C  C   . LEU C 1 163 ? -8.242  16.192  63.307  1.00 14.04 ? 164 LEU C C   1 
ATOM   5572 O  O   . LEU C 1 163 ? -7.851  16.467  62.142  1.00 14.29 ? 164 LEU C O   1 
ATOM   5573 C  CB  . LEU C 1 163 ? -6.274  15.430  64.687  1.00 12.64 ? 164 LEU C CB  1 
ATOM   5574 C  CG  . LEU C 1 163 ? -5.208  15.813  65.741  1.00 11.95 ? 164 LEU C CG  1 
ATOM   5575 C  CD1 . LEU C 1 163 ? -4.194  14.635  65.805  1.00 14.19 ? 164 LEU C CD1 1 
ATOM   5576 C  CD2 . LEU C 1 163 ? -4.532  17.146  65.406  1.00 12.88 ? 164 LEU C CD2 1 
ATOM   5577 N  N   . ASP C 1 164 ? -9.338  15.496  63.540  1.00 15.50 ? 165 ASP C N   1 
ATOM   5578 C  CA  . ASP C 1 164 ? -10.199 15.111  62.389  1.00 17.60 ? 165 ASP C CA  1 
ATOM   5579 C  C   . ASP C 1 164 ? -10.746 16.388  61.656  1.00 18.78 ? 165 ASP C C   1 
ATOM   5580 O  O   . ASP C 1 164 ? -11.132 16.312  60.483  1.00 22.51 ? 165 ASP C O   1 
ATOM   5581 C  CB  . ASP C 1 164 ? -11.340 14.232  62.857  1.00 22.31 ? 165 ASP C CB  1 
ATOM   5582 C  CG  . ASP C 1 164 ? -12.493 15.057  63.410  1.00 28.01 ? 165 ASP C CG  1 
ATOM   5583 O  OD1 . ASP C 1 164 ? -12.213 15.699  64.479  1.00 39.13 ? 165 ASP C OD1 1 
ATOM   5584 O  OD2 . ASP C 1 164 ? -13.634 15.112  62.746  1.00 66.97 ? 165 ASP C OD2 1 
ATOM   5585 N  N   . SER C 1 165 ? -10.749 17.541  62.352  1.00 14.60 ? 166 SER C N   1 
ATOM   5586 C  CA  . SER C 1 165 ? -11.252 18.780  61.735  1.00 15.60 ? 166 SER C CA  1 
ATOM   5587 C  C   . SER C 1 165 ? -10.136 19.533  61.009  1.00 14.64 ? 166 SER C C   1 
ATOM   5588 O  O   . SER C 1 165 ? -10.411 20.538  60.350  1.00 15.46 ? 166 SER C O   1 
ATOM   5589 C  CB  . SER C 1 165 ? -11.937 19.650  62.779  1.00 20.31 ? 166 SER C CB  1 
ATOM   5590 O  OG  . SER C 1 165 ? -10.956 20.227  63.596  1.00 19.91 ? 166 SER C OG  1 
ATOM   5591 N  N   . ILE C 1 166 ? -8.879  19.089  61.156  1.00 12.97 ? 167 ILE C N   1 
ATOM   5592 C  CA  . ILE C 1 166 ? -7.794  19.745  60.395  1.00 12.50 ? 167 ILE C CA  1 
ATOM   5593 C  C   . ILE C 1 166 ? -6.996  18.701  59.598  1.00 11.20 ? 167 ILE C C   1 
ATOM   5594 O  O   . ILE C 1 166 ? -5.767  18.724  59.613  1.00 12.56 ? 167 ILE C O   1 
ATOM   5595 C  CB  . ILE C 1 166 ? -6.871  20.587  61.340  1.00 13.09 ? 167 ILE C CB  1 
ATOM   5596 C  CG1 . ILE C 1 166 ? -6.258  19.726  62.473  1.00 11.43 ? 167 ILE C CG1 1 
ATOM   5597 C  CG2 . ILE C 1 166 ? -7.597  21.855  61.830  1.00 13.73 ? 167 ILE C CG2 1 
ATOM   5598 C  CD1 . ILE C 1 166 ? -4.965  20.356  62.935  1.00 12.88 ? 167 ILE C CD1 1 
ATOM   5599 N  N   . LYS C 1 167 ? -7.671  17.783  58.871  1.00 12.96 ? 168 LYS C N   1 
ATOM   5600 C  CA  . LYS C 1 167 ? -7.009  16.653  58.279  1.00 11.94 ? 168 LYS C CA  1 
ATOM   5601 C  C   . LYS C 1 167 ? -5.961  17.051  57.283  1.00 13.56 ? 168 LYS C C   1 
ATOM   5602 O  O   . LYS C 1 167 ? -4.919  16.369  57.148  1.00 12.81 ? 168 LYS C O   1 
ATOM   5603 C  CB  . LYS C 1 167 ? -8.018  15.724  57.610  1.00 15.15 ? 168 LYS C CB  1 
ATOM   5604 C  CG  . LYS C 1 167 ? -7.377  14.466  56.982  1.00 17.04 ? 168 LYS C CG  1 
ATOM   5605 C  CD  . LYS C 1 167 ? -8.508  13.622  56.337  1.00 22.37 ? 168 LYS C CD  1 
ATOM   5606 C  CE  . LYS C 1 167 ? -7.865  12.480  55.578  1.00 29.05 ? 168 LYS C CE  1 
ATOM   5607 N  NZ  . LYS C 1 167 ? -8.732  11.357  55.140  1.00 33.54 ? 168 LYS C NZ  1 
ATOM   5608 N  N   . THR C 1 168 ? -6.239  18.136  56.526  1.00 13.69 ? 169 THR C N   1 
ATOM   5609 C  CA  . THR C 1 168 ? -5.416  18.397  55.343  1.00 13.43 ? 169 THR C CA  1 
ATOM   5610 C  C   . THR C 1 168 ? -4.751  19.817  55.460  1.00 12.84 ? 169 THR C C   1 
ATOM   5611 O  O   . THR C 1 168 ? -5.160  20.659  56.255  1.00 13.13 ? 169 THR C O   1 
ATOM   5612 C  CB  . THR C 1 168 ? -6.246  18.358  53.997  1.00 13.90 ? 169 THR C CB  1 
ATOM   5613 O  OG1 . THR C 1 168 ? -7.414  19.163  54.197  1.00 15.27 ? 169 THR C OG1 1 
ATOM   5614 C  CG2 . THR C 1 168 ? -6.568  16.931  53.735  1.00 14.79 ? 169 THR C CG2 1 
ATOM   5615 N  N   . LYS C 1 169 ? -3.700  19.964  54.678  1.00 13.20 ? 170 LYS C N   1 
ATOM   5616 C  CA  . LYS C 1 169 ? -2.908  21.165  54.675  1.00 13.57 ? 170 LYS C CA  1 
ATOM   5617 C  C   . LYS C 1 169 ? -3.698  22.438  54.505  1.00 14.38 ? 170 LYS C C   1 
ATOM   5618 O  O   . LYS C 1 169 ? -4.579  22.468  53.576  1.00 17.99 ? 170 LYS C O   1 
ATOM   5619 C  CB  . LYS C 1 169 ? -1.928  21.069  53.557  1.00 13.99 ? 170 LYS C CB  1 
ATOM   5620 C  CG  . LYS C 1 169 ? -1.034  22.336  53.389  1.00 16.51 ? 170 LYS C CG  1 
ATOM   5621 C  CD  . LYS C 1 169 ? 0.072   22.139  52.317  1.00 17.92 ? 170 LYS C CD  1 
ATOM   5622 C  CE  . LYS C 1 169 ? -0.360  21.529  51.026  1.00 23.02 ? 170 LYS C CE  1 
ATOM   5623 N  NZ  . LYS C 1 169 ? 0.669   21.901  50.011  1.00 41.22 ? 170 LYS C NZ  1 
ATOM   5624 N  N   . GLY C 1 170 ? -3.489  23.386  55.393  1.00 14.75 ? 171 GLY C N   1 
ATOM   5625 C  CA  . GLY C 1 170 ? -4.121  24.673  55.354  1.00 14.29 ? 171 GLY C CA  1 
ATOM   5626 C  C   . GLY C 1 170 ? -5.439  24.784  56.172  1.00 17.12 ? 171 GLY C C   1 
ATOM   5627 O  O   . GLY C 1 170 ? -5.997  25.913  56.383  1.00 19.07 ? 171 GLY C O   1 
ATOM   5628 N  N   . LYS C 1 171 ? -5.953  23.635  56.709  1.00 12.66 ? 172 LYS C N   1 
ATOM   5629 C  CA  . LYS C 1 171 ? -7.079  23.657  57.609  1.00 13.79 ? 172 LYS C CA  1 
ATOM   5630 C  C   . LYS C 1 171 ? -6.690  24.144  58.999  1.00 13.34 ? 172 LYS C C   1 
ATOM   5631 O  O   . LYS C 1 171 ? -5.658  23.699  59.554  1.00 12.04 ? 172 LYS C O   1 
ATOM   5632 C  CB  . LYS C 1 171 ? -7.783  22.282  57.665  1.00 15.36 ? 172 LYS C CB  1 
ATOM   5633 C  CG  . LYS C 1 171 ? -8.405  21.927  56.290  1.00 17.98 ? 172 LYS C CG  1 
ATOM   5634 C  CD  . LYS C 1 171 ? -9.529  20.881  56.356  1.00 24.63 ? 172 LYS C CD  1 
ATOM   5635 C  CE  . LYS C 1 171 ? -10.783 21.370  57.123  1.00 31.48 ? 172 LYS C CE  1 
ATOM   5636 N  NZ  . LYS C 1 171 ? -11.775 20.255  57.416  1.00 31.01 ? 172 LYS C NZ  1 
ATOM   5637 N  N   . SER C 1 172 ? -7.500  24.986  59.599  1.00 13.18 ? 173 SER C N   1 
ATOM   5638 C  CA  . SER C 1 172 ? -7.347  25.398  61.006  1.00 14.83 ? 173 SER C CA  1 
ATOM   5639 C  C   . SER C 1 172 ? -8.642  25.304  61.754  1.00 12.49 ? 173 SER C C   1 
ATOM   5640 O  O   . SER C 1 172 ? -9.758  25.250  61.110  1.00 15.37 ? 173 SER C O   1 
ATOM   5641 C  CB  . SER C 1 172 ? -6.785  26.836  61.097  1.00 14.43 ? 173 SER C CB  1 
ATOM   5642 O  OG  . SER C 1 172 ? -7.689  27.706  60.411  1.00 20.22 ? 173 SER C OG  1 
ATOM   5643 N  N   . ALA C 1 173 ? -8.585  25.333  63.084  1.00 14.97 ? 174 ALA C N   1 
ATOM   5644 C  CA  . ALA C 1 173 ? -9.777  25.300  63.955  1.00 14.34 ? 174 ALA C CA  1 
ATOM   5645 C  C   . ALA C 1 173 ? -9.515  26.129  65.191  1.00 15.54 ? 174 ALA C C   1 
ATOM   5646 O  O   . ALA C 1 173 ? -8.374  26.186  65.684  1.00 14.30 ? 174 ALA C O   1 
ATOM   5647 C  CB  . ALA C 1 173 ? -10.093 23.855  64.366  1.00 18.48 ? 174 ALA C CB  1 
ATOM   5648 N  N   . ASP C 1 174 ? -10.510 26.806  65.743  1.00 14.43 ? 175 ASP C N   1 
ATOM   5649 C  CA  . ASP C 1 174 ? -10.361 27.464  67.029  1.00 16.37 ? 175 ASP C CA  1 
ATOM   5650 C  C   . ASP C 1 174 ? -9.927  26.446  68.047  1.00 18.55 ? 175 ASP C C   1 
ATOM   5651 O  O   . ASP C 1 174 ? -10.393 25.318  68.083  1.00 18.59 ? 175 ASP C O   1 
ATOM   5652 C  CB  . ASP C 1 174 ? -11.721 28.099  67.448  1.00 19.79 ? 175 ASP C CB  1 
ATOM   5653 C  CG  . ASP C 1 174 ? -12.164 29.092  66.436  1.00 29.99 ? 175 ASP C CG  1 
ATOM   5654 O  OD1 . ASP C 1 174 ? -11.254 29.779  65.827  1.00 33.00 ? 175 ASP C OD1 1 
ATOM   5655 O  OD2 . ASP C 1 174 ? -13.397 29.107  66.158  1.00 29.49 ? 175 ASP C OD2 1 
ATOM   5656 N  N   . PHE C 1 175 ? -9.013  26.870  68.893  1.00 13.38 ? 176 PHE C N   1 
ATOM   5657 C  CA  . PHE C 1 175 ? -8.482  25.955  69.917  1.00 15.01 ? 176 PHE C CA  1 
ATOM   5658 C  C   . PHE C 1 175 ? -8.118  26.730  71.122  1.00 15.66 ? 176 PHE C C   1 
ATOM   5659 O  O   . PHE C 1 175 ? -6.957  27.007  71.334  1.00 16.46 ? 176 PHE C O   1 
ATOM   5660 C  CB  . PHE C 1 175 ? -7.310  25.140  69.351  1.00 14.13 ? 176 PHE C CB  1 
ATOM   5661 C  CG  . PHE C 1 175 ? -7.046  23.873  70.101  1.00 13.36 ? 176 PHE C CG  1 
ATOM   5662 C  CD1 . PHE C 1 175 ? -7.923  22.838  70.095  1.00 14.12 ? 176 PHE C CD1 1 
ATOM   5663 C  CD2 . PHE C 1 175 ? -5.862  23.740  70.818  1.00 15.05 ? 176 PHE C CD2 1 
ATOM   5664 C  CE1 . PHE C 1 175 ? -7.658  21.632  70.810  1.00 15.76 ? 176 PHE C CE1 1 
ATOM   5665 C  CE2 . PHE C 1 175 ? -5.492  22.527  71.502  1.00 15.00 ? 176 PHE C CE2 1 
ATOM   5666 C  CZ  . PHE C 1 175 ? -6.443  21.503  71.512  1.00 14.43 ? 176 PHE C CZ  1 
ATOM   5667 N  N   . THR C 1 176 ? -9.107  27.138  71.909  1.00 15.70 ? 177 THR C N   1 
ATOM   5668 C  CA  . THR C 1 176 ? -8.915  27.948  73.068  1.00 14.41 ? 177 THR C CA  1 
ATOM   5669 C  C   . THR C 1 176 ? -8.895  27.161  74.345  1.00 10.95 ? 177 THR C C   1 
ATOM   5670 O  O   . THR C 1 176 ? -9.362  25.997  74.414  1.00 13.10 ? 177 THR C O   1 
ATOM   5671 C  CB  . THR C 1 176 ? -10.015 29.019  73.149  1.00 15.63 ? 177 THR C CB  1 
ATOM   5672 O  OG1 . THR C 1 176 ? -11.299 28.395  73.154  1.00 20.03 ? 177 THR C OG1 1 
ATOM   5673 C  CG2 . THR C 1 176 ? -9.934  29.944  71.938  1.00 19.50 ? 177 THR C CG2 1 
ATOM   5674 N  N   . ASN C 1 177 ? -8.299  27.699  75.378  1.00 12.15 ? 178 ASN C N   1 
ATOM   5675 C  CA  . ASN C 1 177 ? -8.309  27.172  76.731  1.00 13.74 ? 178 ASN C CA  1 
ATOM   5676 C  C   . ASN C 1 177 ? -7.572  25.850  76.858  1.00 15.02 ? 178 ASN C C   1 
ATOM   5677 O  O   . ASN C 1 177 ? -7.809  25.110  77.801  1.00 18.19 ? 178 ASN C O   1 
ATOM   5678 C  CB  . ASN C 1 177 ? -9.741  27.090  77.246  1.00 15.75 ? 178 ASN C CB  1 
ATOM   5679 C  CG  . ASN C 1 177 ? -10.368 28.474  77.284  1.00 17.03 ? 178 ASN C CG  1 
ATOM   5680 O  OD1 . ASN C 1 177 ? -9.988  29.298  78.111  1.00 18.80 ? 178 ASN C OD1 1 
ATOM   5681 N  ND2 . ASN C 1 177 ? -11.254 28.749  76.325  1.00 16.40 ? 178 ASN C ND2 1 
ATOM   5682 N  N   . PHE C 1 178 ? -6.648  25.606  75.946  1.00 12.40 ? 179 PHE C N   1 
ATOM   5683 C  CA  . PHE C 1 178 ? -5.823  24.410  76.123  1.00 11.16 ? 179 PHE C CA  1 
ATOM   5684 C  C   . PHE C 1 178 ? -4.652  24.637  76.992  1.00 11.40 ? 179 PHE C C   1 
ATOM   5685 O  O   . PHE C 1 178 ? -3.913  25.623  76.761  1.00 13.33 ? 179 PHE C O   1 
ATOM   5686 C  CB  . PHE C 1 178 ? -5.334  23.955  74.749  1.00 12.59 ? 179 PHE C CB  1 
ATOM   5687 C  CG  . PHE C 1 178 ? -4.475  22.720  74.883  1.00 11.71 ? 179 PHE C CG  1 
ATOM   5688 C  CD1 . PHE C 1 178 ? -5.123  21.483  75.120  1.00 13.20 ? 179 PHE C CD1 1 
ATOM   5689 C  CD2 . PHE C 1 178 ? -3.097  22.761  74.966  1.00 11.10 ? 179 PHE C CD2 1 
ATOM   5690 C  CE1 . PHE C 1 178 ? -4.365  20.329  75.352  1.00 14.08 ? 179 PHE C CE1 1 
ATOM   5691 C  CE2 . PHE C 1 178 ? -2.345  21.579  75.195  1.00 12.53 ? 179 PHE C CE2 1 
ATOM   5692 C  CZ  . PHE C 1 178 ? -2.980  20.388  75.407  1.00 12.27 ? 179 PHE C CZ  1 
ATOM   5693 N  N   . ASP C 1 179 ? -4.455  23.824  78.018  1.00 11.95 ? 180 ASP C N   1 
ATOM   5694 C  CA  . ASP C 1 179 ? -3.395  24.066  78.982  1.00 11.38 ? 180 ASP C CA  1 
ATOM   5695 C  C   . ASP C 1 179 ? -2.212  23.155  78.699  1.00 11.30 ? 180 ASP C C   1 
ATOM   5696 O  O   . ASP C 1 179 ? -2.258  21.933  78.881  1.00 11.84 ? 180 ASP C O   1 
ATOM   5697 C  CB  . ASP C 1 179 ? -3.983  23.767  80.363  1.00 13.75 ? 180 ASP C CB  1 
ATOM   5698 C  CG  . ASP C 1 179 ? -3.068  24.164  81.504  1.00 15.61 ? 180 ASP C CG  1 
ATOM   5699 O  OD1 . ASP C 1 179 ? -1.837  24.267  81.307  1.00 15.00 ? 180 ASP C OD1 1 
ATOM   5700 O  OD2 . ASP C 1 179 ? -3.597  24.356  82.618  1.00 22.88 ? 180 ASP C OD2 1 
ATOM   5701 N  N   . PRO C 1 180 ? -1.104  23.755  78.223  1.00 11.28 ? 181 PRO C N   1 
ATOM   5702 C  CA  . PRO C 1 180 ? 0.062   22.884  77.834  1.00 12.42 ? 181 PRO C CA  1 
ATOM   5703 C  C   . PRO C 1 180 ? 0.728   22.300  79.053  1.00 10.30 ? 181 PRO C C   1 
ATOM   5704 O  O   . PRO C 1 180 ? 1.586   21.372  78.889  1.00 11.20 ? 181 PRO C O   1 
ATOM   5705 C  CB  . PRO C 1 180 ? 0.962   23.880  77.083  1.00 12.88 ? 181 PRO C CB  1 
ATOM   5706 C  CG  . PRO C 1 180 ? 0.652   25.251  77.706  1.00 13.71 ? 181 PRO C CG  1 
ATOM   5707 C  CD  . PRO C 1 180 ? -0.873  25.181  77.915  1.00 12.80 ? 181 PRO C CD  1 
ATOM   5708 N  N   . ARG C 1 181 ? 0.391   22.712  80.283  1.00 11.12 ? 182 ARG C N   1 
ATOM   5709 C  CA  . ARG C 1 181 ? 0.943   22.015  81.494  1.00 11.48 ? 182 ARG C CA  1 
ATOM   5710 C  C   . ARG C 1 181 ? 0.554   20.566  81.511  1.00 11.90 ? 182 ARG C C   1 
ATOM   5711 O  O   . ARG C 1 181 ? 1.279   19.760  82.138  1.00 12.38 ? 182 ARG C O   1 
ATOM   5712 C  CB  . ARG C 1 181 ? 0.548   22.702  82.815  1.00 12.24 ? 182 ARG C CB  1 
ATOM   5713 C  CG  . ARG C 1 181 ? 1.138   24.099  82.902  1.00 13.98 ? 182 ARG C CG  1 
ATOM   5714 C  CD  . ARG C 1 181 ? 0.631   24.828  84.148  1.00 16.15 ? 182 ARG C CD  1 
ATOM   5715 N  NE  . ARG C 1 181 ? -0.789  25.106  83.995  1.00 15.99 ? 182 ARG C NE  1 
ATOM   5716 C  CZ  . ARG C 1 181 ? -1.493  25.845  84.864  1.00 19.23 ? 182 ARG C CZ  1 
ATOM   5717 N  NH1 . ARG C 1 181 ? -0.895  26.373  85.951  1.00 22.18 ? 182 ARG C NH1 1 
ATOM   5718 N  NH2 . ARG C 1 181 ? -2.795  26.027  84.654  1.00 21.54 ? 182 ARG C NH2 1 
ATOM   5719 N  N   . GLY C 1 182 ? -0.548  20.186  80.862  1.00 12.14 ? 183 GLY C N   1 
ATOM   5720 C  CA  . GLY C 1 182 ? -0.915  18.785  80.893  1.00 13.55 ? 183 GLY C CA  1 
ATOM   5721 C  C   . GLY C 1 182 ? -0.097  17.891  79.949  1.00 12.05 ? 183 GLY C C   1 
ATOM   5722 O  O   . GLY C 1 182 ? -0.375  16.671  79.801  1.00 13.86 ? 183 GLY C O   1 
ATOM   5723 N  N   . LEU C 1 183 ? 0.912   18.478  79.255  1.00 10.74 ? 184 LEU C N   1 
ATOM   5724 C  CA  . LEU C 1 183 ? 1.788   17.712  78.359  1.00 11.81 ? 184 LEU C CA  1 
ATOM   5725 C  C   . LEU C 1 183 ? 3.178   17.544  78.949  1.00 11.34 ? 184 LEU C C   1 
ATOM   5726 O  O   . LEU C 1 183 ? 4.091   16.968  78.298  1.00 12.32 ? 184 LEU C O   1 
ATOM   5727 C  CB  . LEU C 1 183 ? 1.984   18.377  77.033  1.00 10.94 ? 184 LEU C CB  1 
ATOM   5728 C  CG  . LEU C 1 183 ? 0.703   18.572  76.253  1.00 10.74 ? 184 LEU C CG  1 
ATOM   5729 C  CD1 . LEU C 1 183 ? 0.952   19.400  75.013  1.00 12.45 ? 184 LEU C CD1 1 
ATOM   5730 C  CD2 . LEU C 1 183 ? -0.029  17.287  75.850  1.00 14.92 ? 184 LEU C CD2 1 
ATOM   5731 N  N   . LEU C 1 184 ? 3.427   17.969  80.191  1.00 12.06 ? 185 LEU C N   1 
ATOM   5732 C  CA  . LEU C 1 184 ? 4.746   17.951  80.802  1.00 11.20 ? 185 LEU C CA  1 
ATOM   5733 C  C   . LEU C 1 184 ? 4.985   16.751  81.718  1.00 11.68 ? 185 LEU C C   1 
ATOM   5734 O  O   . LEU C 1 184 ? 4.136   16.423  82.576  1.00 14.24 ? 185 LEU C O   1 
ATOM   5735 C  CB  . LEU C 1 184 ? 5.011   19.243  81.633  1.00 11.15 ? 185 LEU C CB  1 
ATOM   5736 C  CG  . LEU C 1 184 ? 4.818   20.560  80.868  1.00 11.56 ? 185 LEU C CG  1 
ATOM   5737 C  CD1 . LEU C 1 184 ? 5.012   21.716  81.836  1.00 14.00 ? 185 LEU C CD1 1 
ATOM   5738 C  CD2 . LEU C 1 184 ? 5.697   20.699  79.629  1.00 12.83 ? 185 LEU C CD2 1 
ATOM   5739 N  N   . PRO C 1 185 ? 6.180   16.129  81.625  1.00 11.49 ? 186 PRO C N   1 
ATOM   5740 C  CA  . PRO C 1 185 ? 6.487   15.027  82.550  1.00 10.94 ? 186 PRO C CA  1 
ATOM   5741 C  C   . PRO C 1 185 ? 6.762   15.581  83.975  1.00 11.46 ? 186 PRO C C   1 
ATOM   5742 O  O   . PRO C 1 185 ? 6.848   16.820  84.190  1.00 12.43 ? 186 PRO C O   1 
ATOM   5743 C  CB  . PRO C 1 185 ? 7.745   14.421  81.918  1.00 10.59 ? 186 PRO C CB  1 
ATOM   5744 C  CG  . PRO C 1 185 ? 8.450   15.637  81.341  1.00 11.33 ? 186 PRO C CG  1 
ATOM   5745 C  CD  . PRO C 1 185 ? 7.322   16.533  80.780  1.00 10.74 ? 186 PRO C CD  1 
ATOM   5746 N  N   . GLU C 1 186 ? 6.948   14.670  84.929  1.00 11.29 ? 187 GLU C N   1 
ATOM   5747 C  CA  . GLU C 1 186 ? 7.190   15.106  86.319  1.00 12.09 ? 187 GLU C CA  1 
ATOM   5748 C  C   . GLU C 1 186 ? 8.442   15.849  86.456  1.00 12.95 ? 187 GLU C C   1 
ATOM   5749 O  O   . GLU C 1 186 ? 8.450   16.904  87.088  1.00 17.42 ? 187 GLU C O   1 
ATOM   5750 C  CB  . GLU C 1 186 ? 7.331   13.859  87.257  1.00 17.27 ? 187 GLU C CB  1 
ATOM   5751 C  CG  . GLU C 1 186 ? 6.047   13.185  87.493  1.00 21.74 ? 187 GLU C CG  1 
ATOM   5752 C  CD  . GLU C 1 186 ? 6.267   11.898  88.336  1.00 17.76 ? 187 GLU C CD  1 
ATOM   5753 O  OE1 . GLU C 1 186 ? 7.390   11.690  88.824  1.00 21.61 ? 187 GLU C OE1 1 
ATOM   5754 O  OE2 . GLU C 1 186 ? 5.308   11.146  88.461  1.00 24.60 ? 187 GLU C OE2 1 
ATOM   5755 N  N   . SER C 1 187 ? 9.555   15.333  85.922  1.00 13.92 ? 188 SER C N   1 
ATOM   5756 C  CA  . SER C 1 187 ? 10.849  15.917  86.129  1.00 14.76 ? 188 SER C CA  1 
ATOM   5757 C  C   . SER C 1 187 ? 11.146  16.951  85.016  1.00 14.13 ? 188 SER C C   1 
ATOM   5758 O  O   . SER C 1 187 ? 10.907  16.700  83.831  1.00 14.84 ? 188 SER C O   1 
ATOM   5759 C  CB  . SER C 1 187 ? 11.955  14.867  86.075  1.00 13.78 ? 188 SER C CB  1 
ATOM   5760 O  OG  . SER C 1 187 ? 13.236  15.401  86.265  1.00 15.82 ? 188 SER C OG  1 
ATOM   5761 N  N   . LEU C 1 188 ? 11.820  18.015  85.419  1.00 12.68 ? 189 LEU C N   1 
ATOM   5762 C  CA  . LEU C 1 188 ? 12.384  18.995  84.476  1.00 13.08 ? 189 LEU C CA  1 
ATOM   5763 C  C   . LEU C 1 188 ? 13.891  18.826  84.335  1.00 12.21 ? 189 LEU C C   1 
ATOM   5764 O  O   . LEU C 1 188 ? 14.572  19.697  83.791  1.00 15.77 ? 189 LEU C O   1 
ATOM   5765 C  CB  . LEU C 1 188 ? 12.027  20.425  84.902  1.00 17.77 ? 189 LEU C CB  1 
ATOM   5766 C  CG  . LEU C 1 188 ? 10.603  20.845  84.803  1.00 16.97 ? 189 LEU C CG  1 
ATOM   5767 C  CD1 . LEU C 1 188 ? 10.470  22.317  85.296  1.00 21.78 ? 189 LEU C CD1 1 
ATOM   5768 C  CD2 . LEU C 1 188 ? 10.015  20.644  83.393  1.00 18.70 ? 189 LEU C CD2 1 
ATOM   5769 N  N   . ASP C 1 189 ? 14.461  17.661  84.656  1.00 13.11 ? 190 ASP C N   1 
ATOM   5770 C  CA  . ASP C 1 189 ? 15.831  17.370  84.287  1.00 13.80 ? 190 ASP C CA  1 
ATOM   5771 C  C   . ASP C 1 189 ? 16.025  17.454  82.746  1.00 10.08 ? 190 ASP C C   1 
ATOM   5772 O  O   . ASP C 1 189 ? 15.126  16.954  82.028  1.00 11.49 ? 190 ASP C O   1 
ATOM   5773 C  CB  . ASP C 1 189 ? 16.265  15.974  84.733  1.00 15.28 ? 190 ASP C CB  1 
ATOM   5774 C  CG  . ASP C 1 189 ? 16.438  15.805  86.289  1.00 20.78 ? 190 ASP C CG  1 
ATOM   5775 O  OD1 . ASP C 1 189 ? 16.616  16.812  86.950  1.00 24.96 ? 190 ASP C OD1 1 
ATOM   5776 O  OD2 . ASP C 1 189 ? 16.514  14.633  86.707  1.00 28.18 ? 190 ASP C OD2 1 
ATOM   5777 N  N   . TYR C 1 190 ? 17.144  18.056  82.319  1.00 10.27 ? 191 TYR C N   1 
ATOM   5778 C  CA  . TYR C 1 190 ? 17.244  18.313  80.866  1.00 10.01 ? 191 TYR C CA  1 
ATOM   5779 C  C   . TYR C 1 190 ? 18.659  18.271  80.401  1.00 10.65 ? 191 TYR C C   1 
ATOM   5780 O  O   . TYR C 1 190 ? 19.661  18.382  81.167  1.00 10.59 ? 191 TYR C O   1 
ATOM   5781 C  CB  . TYR C 1 190 ? 16.613  19.706  80.531  1.00 11.31 ? 191 TYR C CB  1 
ATOM   5782 C  CG  . TYR C 1 190 ? 17.359  20.873  81.167  1.00 10.83 ? 191 TYR C CG  1 
ATOM   5783 C  CD1 . TYR C 1 190 ? 18.469  21.476  80.566  1.00 11.53 ? 191 TYR C CD1 1 
ATOM   5784 C  CD2 . TYR C 1 190 ? 16.923  21.389  82.372  1.00 11.62 ? 191 TYR C CD2 1 
ATOM   5785 C  CE1 . TYR C 1 190 ? 19.129  22.552  81.236  1.00 12.33 ? 191 TYR C CE1 1 
ATOM   5786 C  CE2 . TYR C 1 190 ? 17.498  22.500  82.992  1.00 13.31 ? 191 TYR C CE2 1 
ATOM   5787 C  CZ  . TYR C 1 190 ? 18.600  23.067  82.416  1.00 13.10 ? 191 TYR C CZ  1 
ATOM   5788 O  OH  . TYR C 1 190 ? 19.331  24.042  83.057  1.00 15.21 ? 191 TYR C OH  1 
ATOM   5789 N  N   . TRP C 1 191 ? 18.791  18.125  79.074  1.00 8.57  ? 192 TRP C N   1 
ATOM   5790 C  CA  . TRP C 1 191 ? 20.052  18.379  78.379  1.00 9.16  ? 192 TRP C CA  1 
ATOM   5791 C  C   . TRP C 1 191 ? 19.894  19.671  77.570  1.00 8.64  ? 192 TRP C C   1 
ATOM   5792 O  O   . TRP C 1 191 ? 18.777  20.004  77.156  1.00 9.87  ? 192 TRP C O   1 
ATOM   5793 C  CB  . TRP C 1 191 ? 20.383  17.270  77.393  1.00 10.26 ? 192 TRP C CB  1 
ATOM   5794 C  CG  . TRP C 1 191 ? 20.598  15.962  78.021  1.00 9.27  ? 192 TRP C CG  1 
ATOM   5795 C  CD1 . TRP C 1 191 ? 21.768  15.524  78.656  1.00 9.73  ? 192 TRP C CD1 1 
ATOM   5796 C  CD2 . TRP C 1 191 ? 19.678  14.845  78.017  1.00 9.97  ? 192 TRP C CD2 1 
ATOM   5797 N  NE1 . TRP C 1 191 ? 21.578  14.213  79.069  1.00 12.09 ? 192 TRP C NE1 1 
ATOM   5798 C  CE2 . TRP C 1 191 ? 20.360  13.740  78.641  1.00 11.42 ? 192 TRP C CE2 1 
ATOM   5799 C  CE3 . TRP C 1 191 ? 18.396  14.638  77.488  1.00 10.86 ? 192 TRP C CE3 1 
ATOM   5800 C  CZ2 . TRP C 1 191 ? 19.728  12.485  78.798  1.00 10.82 ? 192 TRP C CZ2 1 
ATOM   5801 C  CZ3 . TRP C 1 191 ? 17.787  13.380  77.598  1.00 11.93 ? 192 TRP C CZ3 1 
ATOM   5802 C  CH2 . TRP C 1 191 ? 18.430  12.340  78.217  1.00 12.42 ? 192 TRP C CH2 1 
ATOM   5803 N  N   . THR C 1 192 ? 20.962  20.408  77.332  1.00 9.01  ? 193 THR C N   1 
ATOM   5804 C  CA  . THR C 1 192 ? 20.874  21.644  76.538  1.00 8.59  ? 193 THR C CA  1 
ATOM   5805 C  C   . THR C 1 192 ? 22.059  21.824  75.642  1.00 8.40  ? 193 THR C C   1 
ATOM   5806 O  O   . THR C 1 192 ? 23.182  21.382  76.011  1.00 9.66  ? 193 THR C O   1 
ATOM   5807 C  CB  . THR C 1 192 ? 20.615  22.820  77.479  1.00 9.02  ? 193 THR C CB  1 
ATOM   5808 O  OG1 . THR C 1 192 ? 20.441  24.034  76.682  1.00 9.92  ? 193 THR C OG1 1 
ATOM   5809 C  CG2 . THR C 1 192 ? 21.822  23.087  78.428  1.00 10.55 ? 193 THR C CG2 1 
ATOM   5810 N  N   . TYR C 1 193 ? 21.858  22.427  74.456  1.00 9.10  ? 194 TYR C N   1 
ATOM   5811 C  CA  . TYR C 1 193 ? 22.942  22.684  73.564  1.00 9.26  ? 194 TYR C CA  1 
ATOM   5812 C  C   . TYR C 1 193 ? 22.465  23.761  72.583  1.00 8.82  ? 194 TYR C C   1 
ATOM   5813 O  O   . TYR C 1 193 ? 21.268  23.948  72.389  1.00 8.88  ? 194 TYR C O   1 
ATOM   5814 C  CB  . TYR C 1 193 ? 23.429  21.382  72.793  1.00 9.69  ? 194 TYR C CB  1 
ATOM   5815 C  CG  . TYR C 1 193 ? 22.440  20.889  71.737  1.00 8.70  ? 194 TYR C CG  1 
ATOM   5816 C  CD1 . TYR C 1 193 ? 21.295  20.144  72.100  1.00 8.50  ? 194 TYR C CD1 1 
ATOM   5817 C  CD2 . TYR C 1 193 ? 22.639  21.245  70.410  1.00 9.01  ? 194 TYR C CD2 1 
ATOM   5818 C  CE1 . TYR C 1 193 ? 20.354  19.843  71.146  1.00 7.81  ? 194 TYR C CE1 1 
ATOM   5819 C  CE2 . TYR C 1 193 ? 21.704  20.876  69.451  1.00 8.78  ? 194 TYR C CE2 1 
ATOM   5820 C  CZ  . TYR C 1 193 ? 20.573  20.205  69.837  1.00 7.15  ? 194 TYR C CZ  1 
ATOM   5821 O  OH  . TYR C 1 193 ? 19.651  19.923  68.808  1.00 8.05  ? 194 TYR C OH  1 
ATOM   5822 N  N   . PRO C 1 194 ? 23.382  24.434  71.896  1.00 8.41  ? 195 PRO C N   1 
ATOM   5823 C  CA  . PRO C 1 194 ? 23.004  25.438  70.891  1.00 9.81  ? 195 PRO C CA  1 
ATOM   5824 C  C   . PRO C 1 194 ? 22.765  24.783  69.542  1.00 7.90  ? 195 PRO C C   1 
ATOM   5825 O  O   . PRO C 1 194 ? 23.646  24.016  69.026  1.00 9.84  ? 195 PRO C O   1 
ATOM   5826 C  CB  . PRO C 1 194 ? 24.237  26.361  70.789  1.00 11.26 ? 195 PRO C CB  1 
ATOM   5827 C  CG  . PRO C 1 194 ? 25.416  25.403  71.201  1.00 10.69 ? 195 PRO C CG  1 
ATOM   5828 C  CD  . PRO C 1 194 ? 24.841  24.456  72.198  1.00 11.47 ? 195 PRO C CD  1 
ATOM   5829 N  N   . GLY C 1 195 ? 21.660  25.094  68.908  1.00 8.03  ? 196 GLY C N   1 
ATOM   5830 C  CA  . GLY C 1 195 ? 21.332  24.460  67.617  1.00 8.38  ? 196 GLY C CA  1 
ATOM   5831 C  C   . GLY C 1 195 ? 20.456  25.338  66.757  1.00 8.22  ? 196 GLY C C   1 
ATOM   5832 O  O   . GLY C 1 195 ? 20.609  26.568  66.698  1.00 8.77  ? 196 GLY C O   1 
ATOM   5833 N  N   . SER C 1 196 ? 19.596  24.686  65.998  1.00 7.09  ? 197 SER C N   1 
ATOM   5834 C  CA  . SER C 1 196 ? 18.895  25.327  64.881  1.00 7.90  ? 197 SER C CA  1 
ATOM   5835 C  C   . SER C 1 196 ? 17.418  24.919  64.873  1.00 8.31  ? 197 SER C C   1 
ATOM   5836 O  O   . SER C 1 196 ? 16.999  23.960  65.548  1.00 7.83  ? 197 SER C O   1 
ATOM   5837 C  CB  . SER C 1 196 ? 19.474  24.910  63.529  1.00 8.59  ? 197 SER C CB  1 
ATOM   5838 O  OG  . SER C 1 196 ? 19.180  23.554  63.209  1.00 8.31  ? 197 SER C OG  1 
ATOM   5839 N  N   . LEU C 1 197 ? 16.601  25.575  64.032  1.00 7.30  ? 198 LEU C N   1 
ATOM   5840 C  CA  . LEU C 1 197 ? 15.360  24.986  63.604  1.00 7.28  ? 198 LEU C CA  1 
ATOM   5841 C  C   . LEU C 1 197 ? 15.605  23.683  62.975  1.00 8.10  ? 198 LEU C C   1 
ATOM   5842 O  O   . LEU C 1 197 ? 16.617  23.526  62.238  1.00 8.22  ? 198 LEU C O   1 
ATOM   5843 C  CB  . LEU C 1 197 ? 14.679  25.924  62.615  1.00 10.60 ? 198 LEU C CB  1 
ATOM   5844 C  CG  . LEU C 1 197 ? 14.372  27.343  63.082  1.00 9.22  ? 198 LEU C CG  1 
ATOM   5845 C  CD1 . LEU C 1 197 ? 13.721  28.193  61.972  1.00 12.33 ? 198 LEU C CD1 1 
ATOM   5846 C  CD2 . LEU C 1 197 ? 13.532  27.384  64.307  1.00 12.79 ? 198 LEU C CD2 1 
ATOM   5847 N  N   . THR C 1 198 ? 14.678  22.746  63.037  1.00 8.36  ? 199 THR C N   1 
ATOM   5848 C  CA  . THR C 1 198 ? 14.878  21.451  62.465  1.00 8.76  ? 199 THR C CA  1 
ATOM   5849 C  C   . THR C 1 198 ? 14.130  21.351  61.103  1.00 9.02  ? 199 THR C C   1 
ATOM   5850 O  O   . THR C 1 198 ? 14.158  20.284  60.488  1.00 8.99  ? 199 THR C O   1 
ATOM   5851 C  CB  . THR C 1 198 ? 14.453  20.291  63.361  1.00 7.58  ? 199 THR C CB  1 
ATOM   5852 O  OG1 . THR C 1 198 ? 13.031  20.324  63.489  1.00 8.35  ? 199 THR C OG1 1 
ATOM   5853 C  CG2 . THR C 1 198 ? 15.149  20.269  64.688  1.00 8.74  ? 199 THR C CG2 1 
ATOM   5854 N  N   . THR C 1 199 ? 13.449  22.447  60.695  1.00 9.36  ? 200 THR C N   1 
ATOM   5855 C  CA  . THR C 1 199 ? 12.786  22.534  59.417  1.00 10.01 ? 200 THR C CA  1 
ATOM   5856 C  C   . THR C 1 199 ? 13.353  23.758  58.683  1.00 10.01 ? 200 THR C C   1 
ATOM   5857 O  O   . THR C 1 199 ? 13.758  24.694  59.316  1.00 10.71 ? 200 THR C O   1 
ATOM   5858 C  CB  . THR C 1 199 ? 11.267  22.763  59.516  1.00 12.75 ? 200 THR C CB  1 
ATOM   5859 O  OG1 . THR C 1 199 ? 11.028  23.824  60.514  1.00 16.82 ? 200 THR C OG1 1 
ATOM   5860 C  CG2 . THR C 1 199 ? 10.610  21.503  60.073  1.00 12.50 ? 200 THR C CG2 1 
ATOM   5861 N  N   . PRO C 1 200 ? 13.408  23.707  57.332  1.00 10.41 ? 201 PRO C N   1 
ATOM   5862 C  CA  . PRO C 1 200 ? 13.697  24.954  56.604  1.00 11.75 ? 201 PRO C CA  1 
ATOM   5863 C  C   . PRO C 1 200 ? 12.913  26.128  57.246  1.00 11.59 ? 201 PRO C C   1 
ATOM   5864 O  O   . PRO C 1 200 ? 11.691  25.981  57.504  1.00 13.31 ? 201 PRO C O   1 
ATOM   5865 C  CB  . PRO C 1 200 ? 13.256  24.601  55.167  1.00 12.30 ? 201 PRO C CB  1 
ATOM   5866 C  CG  . PRO C 1 200 ? 13.557  23.140  55.083  1.00 13.16 ? 201 PRO C CG  1 
ATOM   5867 C  CD  . PRO C 1 200 ? 13.067  22.592  56.415  1.00 11.04 ? 201 PRO C CD  1 
ATOM   5868 N  N   . PRO C 1 201 ? 13.543  27.288  57.421  1.00 11.33 ? 202 PRO C N   1 
ATOM   5869 C  CA  . PRO C 1 201 ? 14.826  27.676  56.839  1.00 12.26 ? 202 PRO C CA  1 
ATOM   5870 C  C   . PRO C 1 201 ? 16.046  27.266  57.684  1.00 11.65 ? 202 PRO C C   1 
ATOM   5871 O  O   . PRO C 1 201 ? 17.179  27.692  57.410  1.00 11.54 ? 202 PRO C O   1 
ATOM   5872 C  CB  . PRO C 1 201 ? 14.681  29.201  56.778  1.00 13.50 ? 202 PRO C CB  1 
ATOM   5873 C  CG  . PRO C 1 201 ? 13.800  29.557  57.975  1.00 14.69 ? 202 PRO C CG  1 
ATOM   5874 C  CD  . PRO C 1 201 ? 12.776  28.463  57.935  1.00 13.55 ? 202 PRO C CD  1 
ATOM   5875 N  N   . LEU C 1 202 ? 15.871  26.425  58.746  1.00 8.99  ? 203 LEU C N   1 
ATOM   5876 C  CA  . LEU C 1 202 ? 17.050  25.799  59.430  1.00 9.71  ? 203 LEU C CA  1 
ATOM   5877 C  C   . LEU C 1 202 ? 17.973  26.830  60.134  1.00 9.79  ? 203 LEU C C   1 
ATOM   5878 O  O   . LEU C 1 202 ? 19.129  26.565  60.362  1.00 9.23  ? 203 LEU C O   1 
ATOM   5879 C  CB  . LEU C 1 202 ? 17.862  24.923  58.445  1.00 9.14  ? 203 LEU C CB  1 
ATOM   5880 C  CG  . LEU C 1 202 ? 17.035  23.724  57.875  1.00 9.82  ? 203 LEU C CG  1 
ATOM   5881 C  CD1 . LEU C 1 202 ? 17.905  23.089  56.792  1.00 12.24 ? 203 LEU C CD1 1 
ATOM   5882 C  CD2 . LEU C 1 202 ? 16.686  22.690  58.890  1.00 11.04 ? 203 LEU C CD2 1 
ATOM   5883 N  N   . LEU C 1 203 ? 17.356  27.944  60.557  1.00 9.79  ? 204 LEU C N   1 
ATOM   5884 C  CA  . LEU C 1 203 ? 18.118  29.059  61.107  1.00 10.16 ? 204 LEU C CA  1 
ATOM   5885 C  C   . LEU C 1 203 ? 18.761  28.623  62.435  1.00 10.35 ? 204 LEU C C   1 
ATOM   5886 O  O   . LEU C 1 203 ? 18.143  27.892  63.266  1.00 9.49  ? 204 LEU C O   1 
ATOM   5887 C  CB  . LEU C 1 203 ? 17.215  30.279  61.368  1.00 11.47 ? 204 LEU C CB  1 
ATOM   5888 C  CG  . LEU C 1 203 ? 16.604  30.826  60.068  1.00 13.82 ? 204 LEU C CG  1 
ATOM   5889 C  CD1 . LEU C 1 203 ? 15.480  31.839  60.357  1.00 14.22 ? 204 LEU C CD1 1 
ATOM   5890 C  CD2 . LEU C 1 203 ? 17.653  31.485  59.186  1.00 16.97 ? 204 LEU C CD2 1 
ATOM   5891 N  N   . GLU C 1 204 ? 19.996  29.089  62.651  1.00 10.22 ? 205 GLU C N   1 
ATOM   5892 C  CA  . GLU C 1 204 ? 20.787  28.734  63.782  1.00 9.44  ? 205 GLU C CA  1 
ATOM   5893 C  C   . GLU C 1 204 ? 20.508  29.706  64.909  1.00 10.37 ? 205 GLU C C   1 
ATOM   5894 O  O   . GLU C 1 204 ? 21.402  30.486  65.344  1.00 12.20 ? 205 GLU C O   1 
ATOM   5895 C  CB  . GLU C 1 204 ? 22.266  28.634  63.369  1.00 11.50 ? 205 GLU C CB  1 
ATOM   5896 C  CG  . GLU C 1 204 ? 22.448  27.418  62.506  1.00 10.77 ? 205 GLU C CG  1 
ATOM   5897 C  CD  . GLU C 1 204 ? 23.842  27.137  61.979  1.00 12.44 ? 205 GLU C CD  1 
ATOM   5898 O  OE1 . GLU C 1 204 ? 24.677  28.095  61.885  1.00 15.47 ? 205 GLU C OE1 1 
ATOM   5899 O  OE2 . GLU C 1 204 ? 24.119  25.944  61.681  1.00 12.20 ? 205 GLU C OE2 1 
ATOM   5900 N  N   . CYS C 1 205 ? 19.324  29.631  65.480  1.00 8.78  ? 206 CYS C N   1 
ATOM   5901 C  CA  . CYS C 1 205 ? 18.848  30.610  66.440  1.00 9.36  ? 206 CYS C CA  1 
ATOM   5902 C  C   . CYS C 1 205 ? 18.300  29.990  67.684  1.00 9.02  ? 206 CYS C C   1 
ATOM   5903 O  O   . CYS C 1 205 ? 17.637  30.672  68.465  1.00 10.28 ? 206 CYS C O   1 
ATOM   5904 C  CB  . CYS C 1 205 ? 17.743  31.434  65.781  1.00 10.85 ? 206 CYS C CB  1 
ATOM   5905 S  SG  . CYS C 1 205 ? 16.301  30.470  65.198  1.00 10.77 ? 206 CYS C SG  1 
ATOM   5906 N  N   . VAL C 1 206 ? 18.484  28.672  67.927  1.00 8.64  ? 207 VAL C N   1 
ATOM   5907 C  CA  . VAL C 1 206 ? 17.763  27.970  68.979  1.00 8.35  ? 207 VAL C CA  1 
ATOM   5908 C  C   . VAL C 1 206 ? 18.705  27.531  70.094  1.00 7.42  ? 207 VAL C C   1 
ATOM   5909 O  O   . VAL C 1 206 ? 19.710  26.874  69.849  1.00 9.82  ? 207 VAL C O   1 
ATOM   5910 C  CB  . VAL C 1 206 ? 17.063  26.712  68.404  1.00 7.96  ? 207 VAL C CB  1 
ATOM   5911 C  CG1 . VAL C 1 206 ? 16.343  25.969  69.597  1.00 8.54  ? 207 VAL C CG1 1 
ATOM   5912 C  CG2 . VAL C 1 206 ? 16.077  27.095  67.293  1.00 9.52  ? 207 VAL C CG2 1 
ATOM   5913 N  N   . THR C 1 207 ? 18.333  27.831  71.347  1.00 8.04  ? 208 THR C N   1 
ATOM   5914 C  CA  . THR C 1 207 ? 18.830  27.080  72.492  1.00 8.44  ? 208 THR C CA  1 
ATOM   5915 C  C   . THR C 1 207 ? 17.866  25.945  72.774  1.00 8.21  ? 208 THR C C   1 
ATOM   5916 O  O   . THR C 1 207 ? 16.688  26.143  73.060  1.00 8.30  ? 208 THR C O   1 
ATOM   5917 C  CB  . THR C 1 207 ? 18.895  27.955  73.765  1.00 9.19  ? 208 THR C CB  1 
ATOM   5918 O  OG1 . THR C 1 207 ? 19.775  29.059  73.544  1.00 9.53  ? 208 THR C OG1 1 
ATOM   5919 C  CG2 . THR C 1 207 ? 19.450  27.108  74.959  1.00 11.10 ? 208 THR C CG2 1 
ATOM   5920 N  N   . TRP C 1 208 ? 18.371  24.723  72.549  1.00 7.99  ? 209 TRP C N   1 
ATOM   5921 C  CA  . TRP C 1 208 ? 17.573  23.529  72.738  1.00 7.64  ? 209 TRP C CA  1 
ATOM   5922 C  C   . TRP C 1 208 ? 17.588  23.101  74.230  1.00 7.31  ? 209 TRP C C   1 
ATOM   5923 O  O   . TRP C 1 208 ? 18.677  23.033  74.842  1.00 7.96  ? 209 TRP C O   1 
ATOM   5924 C  CB  . TRP C 1 208 ? 18.091  22.334  71.858  1.00 8.17  ? 209 TRP C CB  1 
ATOM   5925 C  CG  . TRP C 1 208 ? 17.558  22.447  70.476  1.00 7.13  ? 209 TRP C CG  1 
ATOM   5926 C  CD1 . TRP C 1 208 ? 18.128  23.072  69.365  1.00 7.38  ? 209 TRP C CD1 1 
ATOM   5927 C  CD2 . TRP C 1 208 ? 16.223  22.071  70.096  1.00 7.57  ? 209 TRP C CD2 1 
ATOM   5928 N  NE1 . TRP C 1 208 ? 17.212  23.059  68.344  1.00 8.09  ? 209 TRP C NE1 1 
ATOM   5929 C  CE2 . TRP C 1 208 ? 16.071  22.448  68.727  1.00 7.75  ? 209 TRP C CE2 1 
ATOM   5930 C  CE3 . TRP C 1 208 ? 15.146  21.430  70.759  1.00 6.96  ? 209 TRP C CE3 1 
ATOM   5931 C  CZ2 . TRP C 1 208 ? 14.885  22.249  68.039  1.00 8.05  ? 209 TRP C CZ2 1 
ATOM   5932 C  CZ3 . TRP C 1 208 ? 13.983  21.216  70.063  1.00 8.47  ? 209 TRP C CZ3 1 
ATOM   5933 C  CH2 . TRP C 1 208 ? 13.873  21.565  68.710  1.00 8.54  ? 209 TRP C CH2 1 
ATOM   5934 N  N   . ILE C 1 209 ? 16.446  22.764  74.752  1.00 7.63  ? 210 ILE C N   1 
ATOM   5935 C  CA  . ILE C 1 209 ? 16.348  22.221  76.141  1.00 8.07  ? 210 ILE C CA  1 
ATOM   5936 C  C   . ILE C 1 209 ? 15.481  20.973  75.966  1.00 7.56  ? 210 ILE C C   1 
ATOM   5937 O  O   . ILE C 1 209 ? 14.309  21.052  75.668  1.00 8.48  ? 210 ILE C O   1 
ATOM   5938 C  CB  . ILE C 1 209 ? 15.672  23.257  77.054  1.00 8.85  ? 210 ILE C CB  1 
ATOM   5939 C  CG1 . ILE C 1 209 ? 16.543  24.503  77.094  1.00 10.59 ? 210 ILE C CG1 1 
ATOM   5940 C  CG2 . ILE C 1 209 ? 15.479  22.658  78.459  1.00 9.87  ? 210 ILE C CG2 1 
ATOM   5941 C  CD1 . ILE C 1 209 ? 15.850  25.711  77.774  1.00 12.38 ? 210 ILE C CD1 1 
ATOM   5942 N  N   . VAL C 1 210 ? 16.111  19.805  76.124  1.00 7.92  ? 211 VAL C N   1 
ATOM   5943 C  CA  . VAL C 1 210 ? 15.449  18.494  75.859  1.00 7.64  ? 211 VAL C CA  1 
ATOM   5944 C  C   . VAL C 1 210 ? 15.257  17.802  77.200  1.00 6.68  ? 211 VAL C C   1 
ATOM   5945 O  O   . VAL C 1 210 ? 16.280  17.518  77.857  1.00 8.87  ? 211 VAL C O   1 
ATOM   5946 C  CB  . VAL C 1 210 ? 16.257  17.675  74.834  1.00 8.20  ? 211 VAL C CB  1 
ATOM   5947 C  CG1 . VAL C 1 210 ? 15.576  16.300  74.655  1.00 8.65  ? 211 VAL C CG1 1 
ATOM   5948 C  CG2 . VAL C 1 210 ? 16.423  18.436  73.509  1.00 9.40  ? 211 VAL C CG2 1 
ATOM   5949 N  N   . LEU C 1 211 ? 14.053  17.520  77.593  1.00 8.30  ? 212 LEU C N   1 
ATOM   5950 C  CA  . LEU C 1 211 ? 13.837  16.882  78.860  1.00 8.43  ? 212 LEU C CA  1 
ATOM   5951 C  C   . LEU C 1 211 ? 14.178  15.392  78.806  1.00 9.14  ? 212 LEU C C   1 
ATOM   5952 O  O   . LEU C 1 211 ? 13.950  14.689  77.829  1.00 9.74  ? 212 LEU C O   1 
ATOM   5953 C  CB  . LEU C 1 211 ? 12.344  17.004  79.221  1.00 8.76  ? 212 LEU C CB  1 
ATOM   5954 C  CG  . LEU C 1 211 ? 11.829  18.454  79.482  1.00 10.18 ? 212 LEU C CG  1 
ATOM   5955 C  CD1 . LEU C 1 211 ? 10.439  18.396  80.145  1.00 12.51 ? 212 LEU C CD1 1 
ATOM   5956 C  CD2 . LEU C 1 211 ? 12.797  19.259  80.328  1.00 11.79 ? 212 LEU C CD2 1 
ATOM   5957 N  N   . LYS C 1 212 ? 14.759  14.899  79.920  1.00 9.33  ? 213 LYS C N   1 
ATOM   5958 C  CA  . LYS C 1 212 ? 15.126  13.528  79.985  1.00 10.10 ? 213 LYS C CA  1 
ATOM   5959 C  C   . LYS C 1 212 ? 13.967  12.595  80.104  1.00 9.72  ? 213 LYS C C   1 
ATOM   5960 O  O   . LYS C 1 212 ? 14.003  11.503  79.516  1.00 11.84 ? 213 LYS C O   1 
ATOM   5961 C  CB  . LYS C 1 212 ? 16.110  13.283  81.165  1.00 12.21 ? 213 LYS C CB  1 
ATOM   5962 C  CG  . LYS C 1 212 ? 16.461  11.815  81.476  1.00 15.47 ? 213 LYS C CG  1 
ATOM   5963 C  CD  . LYS C 1 212 ? 16.842  11.772  83.003  1.00 33.86 ? 213 LYS C CD  1 
ATOM   5964 C  CE  . LYS C 1 212 ? 16.038  12.785  83.799  1.00 32.77 ? 213 LYS C CE  1 
ATOM   5965 N  NZ  . LYS C 1 212 ? 14.581  12.489  83.725  1.00 21.89 ? 213 LYS C NZ  1 
ATOM   5966 N  N   . GLU C 1 213 ? 12.935  12.966  80.840  1.00 9.06  ? 214 GLU C N   1 
ATOM   5967 C  CA  . GLU C 1 213 ? 11.830  12.094  81.086  1.00 10.36 ? 214 GLU C CA  1 
ATOM   5968 C  C   . GLU C 1 213 ? 10.815  12.187  79.976  1.00 9.51  ? 214 GLU C C   1 
ATOM   5969 O  O   . GLU C 1 213 ? 10.269  13.286  79.733  1.00 9.36  ? 214 GLU C O   1 
ATOM   5970 C  CB  . GLU C 1 213 ? 11.175  12.474  82.437  1.00 10.84 ? 214 GLU C CB  1 
ATOM   5971 C  CG  . GLU C 1 213 ? 10.043  11.537  82.808  1.00 13.80 ? 214 GLU C CG  1 
ATOM   5972 C  CD  . GLU C 1 213 ? 9.363   11.790  84.131  1.00 15.35 ? 214 GLU C CD  1 
ATOM   5973 O  OE1 . GLU C 1 213 ? 9.820   12.656  84.901  1.00 15.85 ? 214 GLU C OE1 1 
ATOM   5974 O  OE2 . GLU C 1 213 ? 8.356   11.093  84.391  1.00 32.32 ? 214 GLU C OE2 1 
ATOM   5975 N  N   . PRO C 1 214 ? 10.504  11.080  79.266  1.00 9.05  ? 215 PRO C N   1 
ATOM   5976 C  CA  . PRO C 1 214 ? 9.431   11.137  78.265  1.00 9.43  ? 215 PRO C CA  1 
ATOM   5977 C  C   . PRO C 1 214 ? 8.076   11.149  78.880  1.00 9.95  ? 215 PRO C C   1 
ATOM   5978 O  O   . PRO C 1 214 ? 7.933   10.776  80.064  1.00 11.55 ? 215 PRO C O   1 
ATOM   5979 C  CB  . PRO C 1 214 ? 9.567   9.779   77.507  1.00 9.79  ? 215 PRO C CB  1 
ATOM   5980 C  CG  . PRO C 1 214 ? 10.152  8.849   78.521  1.00 16.62 ? 215 PRO C CG  1 
ATOM   5981 C  CD  . PRO C 1 214 ? 11.044  9.727   79.440  1.00 10.12 ? 215 PRO C CD  1 
ATOM   5982 N  N   . ILE C 1 215 ? 7.075   11.598  78.132  1.00 8.98  ? 216 ILE C N   1 
ATOM   5983 C  CA  . ILE C 1 215 ? 5.683   11.344  78.530  1.00 9.57  ? 216 ILE C CA  1 
ATOM   5984 C  C   . ILE C 1 215 ? 5.200   10.107  77.781  1.00 9.73  ? 216 ILE C C   1 
ATOM   5985 O  O   . ILE C 1 215 ? 5.747   9.747   76.687  1.00 10.19 ? 216 ILE C O   1 
ATOM   5986 C  CB  . ILE C 1 215 ? 4.764   12.553  78.244  1.00 10.61 ? 216 ILE C CB  1 
ATOM   5987 C  CG1 . ILE C 1 215 ? 4.699   12.881  76.743  1.00 10.72 ? 216 ILE C CG1 1 
ATOM   5988 C  CG2 . ILE C 1 215 ? 5.209   13.771  79.090  1.00 11.99 ? 216 ILE C CG2 1 
ATOM   5989 C  CD1 . ILE C 1 215 ? 3.609   13.905  76.373  1.00 11.49 ? 216 ILE C CD1 1 
ATOM   5990 N  N   . SER C 1 216 ? 4.228   9.404   78.352  0.50 5.56  ? 217 SER C N   1 
ATOM   5991 C  CA  . SER C 1 216 ? 3.577   8.301   77.663  0.50 4.54  ? 217 SER C CA  1 
ATOM   5992 C  C   . SER C 1 216 ? 2.297   8.754   77.021  0.50 4.53  ? 217 SER C C   1 
ATOM   5993 O  O   . SER C 1 216 ? 1.527   9.473   77.663  0.50 4.70  ? 217 SER C O   1 
ATOM   5994 C  CB  . SER C 1 216 ? 3.287   7.192   78.685  0.50 7.44  ? 217 SER C CB  1 
ATOM   5995 O  OG  . SER C 1 216 ? 4.442   6.582   79.136  0.50 11.60 ? 217 SER C OG  1 
ATOM   5996 N  N   . VAL C 1 217 ? 2.074   8.293   75.784  1.00 9.65  ? 218 VAL C N   1 
ATOM   5997 C  CA  . VAL C 1 217 ? 0.849   8.507   75.085  1.00 9.59  ? 218 VAL C CA  1 
ATOM   5998 C  C   . VAL C 1 217 ? 0.331   7.140   74.702  1.00 9.81  ? 218 VAL C C   1 
ATOM   5999 O  O   . VAL C 1 217 ? 1.136   6.197   74.572  1.00 9.91  ? 218 VAL C O   1 
ATOM   6000 C  CB  . VAL C 1 217 ? 0.998   9.445   73.880  1.00 10.37 ? 218 VAL C CB  1 
ATOM   6001 C  CG1 . VAL C 1 217 ? 1.576   10.805  74.369  1.00 10.51 ? 218 VAL C CG1 1 
ATOM   6002 C  CG2 . VAL C 1 217 ? 1.904   8.847   72.777  1.00 11.70 ? 218 VAL C CG2 1 
ATOM   6003 N  N   . SER C 1 218 ? -0.949  6.992   74.393  1.00 10.24 ? 219 SER C N   1 
ATOM   6004 C  CA  . SER C 1 218 ? -1.398  5.652   74.004  1.00 10.31 ? 219 SER C CA  1 
ATOM   6005 C  C   . SER C 1 218 ? -1.181  5.409   72.547  1.00 9.85  ? 219 SER C C   1 
ATOM   6006 O  O   . SER C 1 218 ? -1.053  6.324   71.692  1.00 11.09 ? 219 SER C O   1 
ATOM   6007 C  CB  . SER C 1 218 ? -2.875  5.486   74.397  1.00 10.75 ? 219 SER C CB  1 
ATOM   6008 O  OG  . SER C 1 218 ? -3.711  6.359   73.650  1.00 11.21 ? 219 SER C OG  1 
ATOM   6009 N  N   A SER C 1 219 ? -1.249  4.120   72.199  0.50 10.72 ? 220 SER C N   1 
ATOM   6010 N  N   B SER C 1 219 ? -1.219  4.139   72.182  0.50 10.82 ? 220 SER C N   1 
ATOM   6011 C  CA  A SER C 1 219 ? -1.220  3.721   70.802  0.50 11.72 ? 220 SER C CA  1 
ATOM   6012 C  CA  B SER C 1 219 ? -1.123  3.800   70.784  0.50 11.75 ? 220 SER C CA  1 
ATOM   6013 C  C   A SER C 1 219 ? -2.281  4.461   70.032  0.50 11.45 ? 220 SER C C   1 
ATOM   6014 C  C   B SER C 1 219 ? -2.321  4.385   69.981  0.50 11.80 ? 220 SER C C   1 
ATOM   6015 O  O   A SER C 1 219 ? -1.998  5.020   68.950  0.50 11.90 ? 220 SER C O   1 
ATOM   6016 O  O   B SER C 1 219 ? -2.175  4.808   68.825  0.50 12.63 ? 220 SER C O   1 
ATOM   6017 C  CB  A SER C 1 219 ? -1.406  2.182   70.659  0.50 15.66 ? 220 SER C CB  1 
ATOM   6018 C  CB  B SER C 1 219 ? -0.995  2.263   70.695  0.50 14.60 ? 220 SER C CB  1 
ATOM   6019 O  OG  A SER C 1 219 ? -2.530  1.650   71.348  0.50 13.92 ? 220 SER C OG  1 
ATOM   6020 O  OG  B SER C 1 219 ? -1.050  1.818   69.363  0.50 15.63 ? 220 SER C OG  1 
ATOM   6021 N  N   . GLU C 1 220 ? -3.509  4.500   70.592  1.00 11.41 ? 221 GLU C N   1 
ATOM   6022 C  CA  . GLU C 1 220 ? -4.642  5.172   69.960  1.00 13.20 ? 221 GLU C CA  1 
ATOM   6023 C  C   . GLU C 1 220 ? -4.361  6.652   69.689  1.00 11.28 ? 221 GLU C C   1 
ATOM   6024 O  O   . GLU C 1 220 ? -4.771  7.217   68.623  1.00 12.69 ? 221 GLU C O   1 
ATOM   6025 C  CB  . GLU C 1 220 ? -5.960  5.031   70.708  1.00 15.58 ? 221 GLU C CB  1 
ATOM   6026 C  CG  . GLU C 1 220 ? -6.484  3.562   70.687  1.00 20.29 ? 221 GLU C CG  1 
ATOM   6027 C  CD  . GLU C 1 220 ? -5.948  2.733   71.874  1.00 23.53 ? 221 GLU C CD  1 
ATOM   6028 O  OE1 . GLU C 1 220 ? -4.978  3.125   72.625  1.00 19.71 ? 221 GLU C OE1 1 
ATOM   6029 O  OE2 . GLU C 1 220 ? -6.545  1.639   72.142  1.00 35.59 ? 221 GLU C OE2 1 
ATOM   6030 N  N   . GLN C 1 221 ? -3.765  7.320   70.672  1.00 10.60 ? 222 GLN C N   1 
ATOM   6031 C  CA  . GLN C 1 221 ? -3.484  8.765   70.463  1.00 10.70 ? 222 GLN C CA  1 
ATOM   6032 C  C   . GLN C 1 221 ? -2.487  8.973   69.266  1.00 10.08 ? 222 GLN C C   1 
ATOM   6033 O  O   . GLN C 1 221 ? -2.729  9.817   68.414  1.00 11.44 ? 222 GLN C O   1 
ATOM   6034 C  CB  . GLN C 1 221 ? -2.892  9.373   71.753  1.00 10.80 ? 222 GLN C CB  1 
ATOM   6035 C  CG  . GLN C 1 221 ? -3.974  9.460   72.866  1.00 10.96 ? 222 GLN C CG  1 
ATOM   6036 C  CD  . GLN C 1 221 ? -3.476  10.005  74.193  1.00 10.24 ? 222 GLN C CD  1 
ATOM   6037 O  OE1 . GLN C 1 221 ? -2.384  9.626   74.650  1.00 10.21 ? 222 GLN C OE1 1 
ATOM   6038 N  NE2 . GLN C 1 221 ? -4.277  10.920  74.774  1.00 10.92 ? 222 GLN C NE2 1 
ATOM   6039 N  N   . VAL C 1 222 ? -1.378  8.196   69.227  1.00 10.98 ? 223 VAL C N   1 
ATOM   6040 C  CA  . VAL C 1 222 ? -0.423  8.422   68.110  1.00 11.18 ? 223 VAL C CA  1 
ATOM   6041 C  C   . VAL C 1 222 ? -1.011  7.942   66.776  1.00 12.71 ? 223 VAL C C   1 
ATOM   6042 O  O   . VAL C 1 222 ? -0.728  8.522   65.696  1.00 12.04 ? 223 VAL C O   1 
ATOM   6043 C  CB  . VAL C 1 222 ? 0.969   7.842   68.455  1.00 14.56 ? 223 VAL C CB  1 
ATOM   6044 C  CG1 . VAL C 1 222 ? 0.910   6.324   68.538  1.00 15.63 ? 223 VAL C CG1 1 
ATOM   6045 C  CG2 . VAL C 1 222 ? 2.011   8.342   67.449  1.00 16.29 ? 223 VAL C CG2 1 
ATOM   6046 N  N   . LEU C 1 223 ? -1.859  6.916   66.814  1.00 11.87 ? 224 LEU C N   1 
ATOM   6047 C  CA  . LEU C 1 223 ? -2.488  6.496   65.554  1.00 13.38 ? 224 LEU C CA  1 
ATOM   6048 C  C   . LEU C 1 223 ? -3.298  7.640   64.968  1.00 13.18 ? 224 LEU C C   1 
ATOM   6049 O  O   . LEU C 1 223 ? -3.400  7.753   63.737  1.00 13.88 ? 224 LEU C O   1 
ATOM   6050 C  CB  . LEU C 1 223 ? -3.386  5.280   65.752  1.00 17.26 ? 224 LEU C CB  1 
ATOM   6051 C  CG  . LEU C 1 223 ? -2.550  3.972   65.886  1.00 17.42 ? 224 LEU C CG  1 
ATOM   6052 C  CD1 . LEU C 1 223 ? -3.364  2.802   66.467  1.00 22.79 ? 224 LEU C CD1 1 
ATOM   6053 C  CD2 . LEU C 1 223 ? -2.037  3.532   64.533  1.00 19.14 ? 224 LEU C CD2 1 
ATOM   6054 N  N   . LYS C 1 224 ? -3.933  8.463   65.801  1.00 12.36 ? 225 LYS C N   1 
ATOM   6055 C  CA  . LYS C 1 224 ? -4.692  9.613   65.286  1.00 13.75 ? 225 LYS C CA  1 
ATOM   6056 C  C   . LYS C 1 224 ? -3.776  10.680  64.679  1.00 12.29 ? 225 LYS C C   1 
ATOM   6057 O  O   . LYS C 1 224 ? -4.126  11.286  63.662  1.00 12.23 ? 225 LYS C O   1 
ATOM   6058 C  CB  . LYS C 1 224 ? -5.657  10.114  66.367  1.00 16.06 ? 225 LYS C CB  1 
ATOM   6059 C  CG  . LYS C 1 224 ? -6.799  9.060   66.540  1.00 18.27 ? 225 LYS C CG  1 
ATOM   6060 C  CD  . LYS C 1 224 ? -7.857  9.387   67.579  1.00 26.97 ? 225 LYS C CD  1 
ATOM   6061 C  CE  . LYS C 1 224 ? -9.023  8.337   67.648  1.00 25.19 ? 225 LYS C CE  1 
ATOM   6062 N  NZ  . LYS C 1 224 ? -9.899  8.655   68.847  1.00 28.75 ? 225 LYS C NZ  1 
ATOM   6063 N  N   . PHE C 1 225 ? -2.556  10.887  65.206  1.00 10.66 ? 226 PHE C N   1 
ATOM   6064 C  CA  . PHE C 1 225 ? -1.618  11.780  64.561  1.00 10.02 ? 226 PHE C CA  1 
ATOM   6065 C  C   . PHE C 1 225 ? -1.359  11.245  63.113  1.00 10.95 ? 226 PHE C C   1 
ATOM   6066 O  O   . PHE C 1 225 ? -1.257  12.047  62.163  1.00 11.50 ? 226 PHE C O   1 
ATOM   6067 C  CB  . PHE C 1 225 ? -0.241  11.756  65.248  1.00 10.81 ? 226 PHE C CB  1 
ATOM   6068 C  CG  . PHE C 1 225 ? -0.126  12.537  66.549  1.00 11.42 ? 226 PHE C CG  1 
ATOM   6069 C  CD1 . PHE C 1 225 ? -1.224  12.961  67.288  1.00 14.63 ? 226 PHE C CD1 1 
ATOM   6070 C  CD2 . PHE C 1 225 ? 1.143   12.811  67.049  1.00 13.10 ? 226 PHE C CD2 1 
ATOM   6071 C  CE1 . PHE C 1 225 ? -1.041  13.655  68.485  1.00 15.74 ? 226 PHE C CE1 1 
ATOM   6072 C  CE2 . PHE C 1 225 ? 1.326   13.499  68.235  1.00 16.06 ? 226 PHE C CE2 1 
ATOM   6073 C  CZ  . PHE C 1 225 ? 0.234   13.921  68.958  1.00 14.00 ? 226 PHE C CZ  1 
ATOM   6074 N  N   . ARG C 1 226 ? -1.231  9.906   62.949  1.00 9.79  ? 227 ARG C N   1 
ATOM   6075 C  CA  . ARG C 1 226 ? -0.847  9.324   61.663  1.00 11.60 ? 227 ARG C CA  1 
ATOM   6076 C  C   . ARG C 1 226 ? -1.988  9.278   60.651  1.00 11.77 ? 227 ARG C C   1 
ATOM   6077 O  O   . ARG C 1 226 ? -1.754  8.900   59.503  1.00 12.50 ? 227 ARG C O   1 
ATOM   6078 C  CB  . ARG C 1 226 ? -0.373  7.871   61.898  1.00 11.79 ? 227 ARG C CB  1 
ATOM   6079 C  CG  . ARG C 1 226 ? 0.867   7.754   62.804  1.00 11.80 ? 227 ARG C CG  1 
ATOM   6080 C  CD  . ARG C 1 226 ? 1.391   6.327   62.829  1.00 14.22 ? 227 ARG C CD  1 
ATOM   6081 N  NE  . ARG C 1 226 ? 2.485   6.187   63.817  1.00 13.16 ? 227 ARG C NE  1 
ATOM   6082 C  CZ  . ARG C 1 226 ? 2.482   5.334   64.836  1.00 12.33 ? 227 ARG C CZ  1 
ATOM   6083 N  NH1 . ARG C 1 226 ? 1.496   4.403   64.987  1.00 15.45 ? 227 ARG C NH1 1 
ATOM   6084 N  NH2 . ARG C 1 226 ? 3.455   5.372   65.695  1.00 14.12 ? 227 ARG C NH2 1 
ATOM   6085 N  N   . LYS C 1 227 ? -3.185  9.725   61.036  1.00 11.53 ? 228 LYS C N   1 
ATOM   6086 C  CA  . LYS C 1 227 ? -4.339  9.941   60.094  1.00 12.54 ? 228 LYS C CA  1 
ATOM   6087 C  C   . LYS C 1 227 ? -4.319  11.300  59.415  1.00 11.16 ? 228 LYS C C   1 
ATOM   6088 O  O   . LYS C 1 227 ? -5.095  11.552  58.461  1.00 13.65 ? 228 LYS C O   1 
ATOM   6089 C  CB  . LYS C 1 227 ? -5.698  9.706   60.805  1.00 15.37 ? 228 LYS C CB  1 
ATOM   6090 C  CG  . LYS C 1 227 ? -5.849  8.242   61.140  1.00 18.12 ? 228 LYS C CG  1 
ATOM   6091 C  CD  . LYS C 1 227 ? -7.095  8.019   61.997  1.00 27.37 ? 228 LYS C CD  1 
ATOM   6092 C  CE  . LYS C 1 227 ? -8.430  8.393   61.326  1.00 37.35 ? 228 LYS C CE  1 
ATOM   6093 N  NZ  . LYS C 1 227 ? -9.067  7.306   60.509  1.00 40.51 ? 228 LYS C NZ  1 
ATOM   6094 N  N   . LEU C 1 228 ? -3.532  12.247  59.911  1.00 12.09 ? 229 LEU C N   1 
ATOM   6095 C  CA  . LEU C 1 228 ? -3.415  13.533  59.286  1.00 10.81 ? 229 LEU C CA  1 
ATOM   6096 C  C   . LEU C 1 228 ? -2.756  13.361  57.898  1.00 10.44 ? 229 LEU C C   1 
ATOM   6097 O  O   . LEU C 1 228 ? -2.178  12.300  57.560  1.00 11.40 ? 229 LEU C O   1 
ATOM   6098 C  CB  . LEU C 1 228 ? -2.521  14.445  60.137  1.00 11.21 ? 229 LEU C CB  1 
ATOM   6099 C  CG  . LEU C 1 228 ? -3.176  14.913  61.416  1.00 11.51 ? 229 LEU C CG  1 
ATOM   6100 C  CD1 . LEU C 1 228 ? -2.093  15.588  62.275  1.00 12.47 ? 229 LEU C CD1 1 
ATOM   6101 C  CD2 . LEU C 1 228 ? -4.215  15.962  61.097  1.00 13.97 ? 229 LEU C CD2 1 
ATOM   6102 N  N   . ASN C 1 229 ? -2.896  14.415  57.099  1.00 12.26 ? 230 ASN C N   1 
ATOM   6103 C  CA  . ASN C 1 229 ? -2.388  14.350  55.721  1.00 11.40 ? 230 ASN C CA  1 
ATOM   6104 C  C   . ASN C 1 229 ? -1.417  15.544  55.503  1.00 12.85 ? 230 ASN C C   1 
ATOM   6105 O  O   . ASN C 1 229 ? -1.685  16.661  55.933  1.00 13.01 ? 230 ASN C O   1 
ATOM   6106 C  CB  . ASN C 1 229 ? -3.586  14.568  54.694  1.00 12.85 ? 230 ASN C CB  1 
ATOM   6107 C  CG  . ASN C 1 229 ? -4.437  13.371  54.442  1.00 15.25 ? 230 ASN C CG  1 
ATOM   6108 O  OD1 . ASN C 1 229 ? -5.306  13.529  53.537  1.00 18.95 ? 230 ASN C OD1 1 
ATOM   6109 N  ND2 . ASN C 1 229 ? -4.300  12.246  55.179  1.00 15.51 ? 230 ASN C ND2 1 
ATOM   6110 N  N   . PHE C 1 230 ? -0.375  15.260  54.700  1.00 11.88 ? 231 PHE C N   1 
ATOM   6111 C  CA  . PHE C 1 230 ? 0.517   16.341  54.254  1.00 12.33 ? 231 PHE C CA  1 
ATOM   6112 C  C   . PHE C 1 230 ? -0.117  17.181  53.159  1.00 14.64 ? 231 PHE C C   1 
ATOM   6113 O  O   . PHE C 1 230 ? 0.159   18.403  53.025  1.00 14.94 ? 231 PHE C O   1 
ATOM   6114 C  CB  . PHE C 1 230 ? 1.784   15.784  53.627  1.00 13.84 ? 231 PHE C CB  1 
ATOM   6115 C  CG  . PHE C 1 230 ? 2.841   15.187  54.606  1.00 12.18 ? 231 PHE C CG  1 
ATOM   6116 C  CD1 . PHE C 1 230 ? 3.383   15.977  55.644  1.00 12.70 ? 231 PHE C CD1 1 
ATOM   6117 C  CD2 . PHE C 1 230 ? 3.323   13.920  54.411  1.00 14.03 ? 231 PHE C CD2 1 
ATOM   6118 C  CE1 . PHE C 1 230 ? 4.399   15.440  56.442  1.00 11.97 ? 231 PHE C CE1 1 
ATOM   6119 C  CE2 . PHE C 1 230 ? 4.343   13.365  55.215  1.00 12.31 ? 231 PHE C CE2 1 
ATOM   6120 C  CZ  . PHE C 1 230 ? 4.880   14.140  56.226  1.00 11.04 ? 231 PHE C CZ  1 
ATOM   6121 N  N   . ASN C 1 231 ? -0.909  16.523  52.321  1.00 13.11 ? 232 ASN C N   1 
ATOM   6122 C  CA  . ASN C 1 231 ? -1.564  17.128  51.096  1.00 14.50 ? 232 ASN C CA  1 
ATOM   6123 C  C   . ASN C 1 231 ? -2.759  17.977  51.478  1.00 14.63 ? 232 ASN C C   1 
ATOM   6124 O  O   . ASN C 1 231 ? -3.327  17.912  52.628  1.00 14.50 ? 232 ASN C O   1 
ATOM   6125 C  CB  . ASN C 1 231 ? -2.077  15.999  50.216  1.00 16.04 ? 232 ASN C CB  1 
ATOM   6126 C  CG  . ASN C 1 231 ? -3.001  15.103  50.988  1.00 15.72 ? 232 ASN C CG  1 
ATOM   6127 O  OD1 . ASN C 1 231 ? -2.521  14.212  51.707  1.00 15.77 ? 232 ASN C OD1 1 
ATOM   6128 N  ND2 . ASN C 1 231 ? -4.315  15.256  50.795  1.00 17.23 ? 232 ASN C ND2 1 
ATOM   6129 N  N   . GLY C 1 232 ? -3.077  18.953  50.571  1.00 15.94 ? 233 GLY C N   1 
ATOM   6130 C  CA  . GLY C 1 232 ? -4.348  19.721  50.718  1.00 19.64 ? 233 GLY C CA  1 
ATOM   6131 C  C   . GLY C 1 232 ? -5.554  18.862  50.359  1.00 15.68 ? 233 GLY C C   1 
ATOM   6132 O  O   . GLY C 1 232 ? -5.413  17.842  49.697  1.00 17.50 ? 233 GLY C O   1 
ATOM   6133 N  N   . GLU C 1 233 ? -6.746  19.360  50.747  1.00 16.48 ? 234 GLU C N   1 
ATOM   6134 C  CA  . GLU C 1 233 ? -8.034  18.839  50.305  1.00 18.23 ? 234 GLU C CA  1 
ATOM   6135 C  C   . GLU C 1 233 ? -8.063  18.769  48.780  1.00 16.33 ? 234 GLU C C   1 
ATOM   6136 O  O   . GLU C 1 233 ? -7.692  19.665  48.102  1.00 20.41 ? 234 GLU C O   1 
ATOM   6137 C  CB  . GLU C 1 233 ? -9.141  19.681  50.895  1.00 15.87 ? 234 GLU C CB  1 
ATOM   6138 C  CG  . GLU C 1 233 ? -10.489 19.072  50.744  1.00 17.45 ? 234 GLU C CG  1 
ATOM   6139 C  CD  . GLU C 1 233 ? -11.609 19.970  51.208  1.00 24.67 ? 234 GLU C CD  1 
ATOM   6140 O  OE1 . GLU C 1 233 ? -11.345 21.141  51.642  1.00 28.53 ? 234 GLU C OE1 1 
ATOM   6141 O  OE2 . GLU C 1 233 ? -12.755 19.518  51.015  1.00 27.10 ? 234 GLU C OE2 1 
ATOM   6142 N  N   . GLY C 1 234 ? -8.456  17.610  48.275  1.00 18.49 ? 235 GLY C N   1 
ATOM   6143 C  CA  . GLY C 1 234 ? -8.609  17.406  46.837  1.00 22.73 ? 235 GLY C CA  1 
ATOM   6144 C  C   . GLY C 1 234 ? -7.381  17.002  46.102  1.00 22.06 ? 235 GLY C C   1 
ATOM   6145 O  O   . GLY C 1 234 ? -7.361  16.927  44.855  1.00 25.86 ? 235 GLY C O   1 
ATOM   6146 N  N   . GLU C 1 235 ? -6.317  16.738  46.846  1.00 21.55 ? 236 GLU C N   1 
ATOM   6147 C  CA  . GLU C 1 235 ? -5.026  16.248  46.338  1.00 18.39 ? 236 GLU C CA  1 
ATOM   6148 C  C   . GLU C 1 235 ? -4.844  14.789  46.769  1.00 23.60 ? 236 GLU C C   1 
ATOM   6149 O  O   . GLU C 1 235 ? -5.528  14.344  47.759  1.00 23.59 ? 236 GLU C O   1 
ATOM   6150 C  CB  . GLU C 1 235 ? -3.911  17.106  46.892  1.00 20.04 ? 236 GLU C CB  1 
ATOM   6151 C  CG  . GLU C 1 235 ? -3.803  18.456  46.278  1.00 24.77 ? 236 GLU C CG  1 
ATOM   6152 C  CD  . GLU C 1 235 ? -2.896  19.360  47.058  1.00 27.14 ? 236 GLU C CD  1 
ATOM   6153 O  OE1 . GLU C 1 235 ? -2.147  18.920  48.015  1.00 27.47 ? 236 GLU C OE1 1 
ATOM   6154 O  OE2 . GLU C 1 235 ? -3.007  20.543  46.740  1.00 34.31 ? 236 GLU C OE2 1 
ATOM   6155 N  N   . PRO C 1 236 ? -3.983  14.032  46.072  1.00 20.28 ? 237 PRO C N   1 
ATOM   6156 C  CA  . PRO C 1 236 ? -3.723  12.612  46.365  1.00 22.13 ? 237 PRO C CA  1 
ATOM   6157 C  C   . PRO C 1 236 ? -3.309  12.484  47.866  1.00 21.26 ? 237 PRO C C   1 
ATOM   6158 O  O   . PRO C 1 236 ? -2.519  13.301  48.328  1.00 20.67 ? 237 PRO C O   1 
ATOM   6159 C  CB  . PRO C 1 236 ? -2.512  12.285  45.443  1.00 23.90 ? 237 PRO C CB  1 
ATOM   6160 C  CG  . PRO C 1 236 ? -2.659  13.262  44.313  1.00 27.99 ? 237 PRO C CG  1 
ATOM   6161 C  CD  . PRO C 1 236 ? -3.230  14.523  44.906  1.00 24.99 ? 237 PRO C CD  1 
ATOM   6162 N  N   . GLU C 1 237 ? -3.808  11.457  48.579  1.00 21.24 ? 238 GLU C N   1 
ATOM   6163 C  CA  . GLU C 1 237 ? -3.563  11.323  49.980  1.00 16.87 ? 238 GLU C CA  1 
ATOM   6164 C  C   . GLU C 1 237 ? -2.112  10.910  50.226  1.00 16.66 ? 238 GLU C C   1 
ATOM   6165 O  O   . GLU C 1 237 ? -1.659  9.901   49.767  1.00 16.16 ? 238 GLU C O   1 
ATOM   6166 C  CB  . GLU C 1 237 ? -4.449  10.241  50.586  1.00 19.69 ? 238 GLU C CB  1 
ATOM   6167 C  CG  . GLU C 1 237 ? -4.660  10.564  52.043  1.00 25.61 ? 238 GLU C CG  1 
ATOM   6168 C  CD  . GLU C 1 237 ? -5.406  9.581   52.892  1.00 28.97 ? 238 GLU C CD  1 
ATOM   6169 O  OE1 . GLU C 1 237 ? -5.683  8.427   52.403  1.00 38.20 ? 238 GLU C OE1 1 
ATOM   6170 O  OE2 . GLU C 1 237 ? -5.700  10.026  54.047  1.00 25.27 ? 238 GLU C OE2 1 
ATOM   6171 N  N   . GLU C 1 238 ? -1.430  11.676  51.085  1.00 15.68 ? 239 GLU C N   1 
ATOM   6172 C  CA  . GLU C 1 238 ? -0.123  11.377  51.567  1.00 16.73 ? 239 GLU C CA  1 
ATOM   6173 C  C   . GLU C 1 238 ? -0.160  11.510  53.118  1.00 14.20 ? 239 GLU C C   1 
ATOM   6174 O  O   . GLU C 1 238 ? -0.244  12.616  53.639  1.00 16.25 ? 239 GLU C O   1 
ATOM   6175 C  CB  . GLU C 1 238 ? 0.921   12.334  51.091  1.00 19.97 ? 239 GLU C CB  1 
ATOM   6176 C  CG  . GLU C 1 238 ? 1.023   12.797  49.614  1.00 27.58 ? 239 GLU C CG  1 
ATOM   6177 C  CD  . GLU C 1 238 ? 1.783   14.102  49.481  1.00 30.37 ? 239 GLU C CD  1 
ATOM   6178 O  OE1 . GLU C 1 238 ? 1.215   15.086  48.975  1.00 74.26 ? 239 GLU C OE1 1 
ATOM   6179 O  OE2 . GLU C 1 238 ? 2.963   14.158  49.886  1.00 51.07 ? 239 GLU C OE2 1 
ATOM   6180 N  N   . LEU C 1 239 ? -0.124  10.355  53.831  1.00 13.55 ? 240 LEU C N   1 
ATOM   6181 C  CA  . LEU C 1 239 ? -0.292  10.401  55.297  1.00 12.99 ? 240 LEU C CA  1 
ATOM   6182 C  C   . LEU C 1 239 ? 0.874   11.244  55.869  1.00 11.56 ? 240 LEU C C   1 
ATOM   6183 O  O   . LEU C 1 239 ? 2.046   11.064  55.482  1.00 12.85 ? 240 LEU C O   1 
ATOM   6184 C  CB  . LEU C 1 239 ? -0.263  8.992   55.862  1.00 12.88 ? 240 LEU C CB  1 
ATOM   6185 C  CG  . LEU C 1 239 ? -1.418  8.099   55.463  1.00 14.50 ? 240 LEU C CG  1 
ATOM   6186 C  CD1 . LEU C 1 239 ? -1.191  6.718   56.087  1.00 17.86 ? 240 LEU C CD1 1 
ATOM   6187 C  CD2 . LEU C 1 239 ? -2.757  8.692   55.900  1.00 14.49 ? 240 LEU C CD2 1 
ATOM   6188 N  N   . MET C 1 240 ? 0.528   12.038  56.857  1.00 10.81 ? 241 MET C N   1 
ATOM   6189 C  CA  . MET C 1 240 ? 1.501   12.870  57.595  1.00 11.74 ? 241 MET C CA  1 
ATOM   6190 C  C   . MET C 1 240 ? 2.146   11.950  58.657  1.00 9.11  ? 241 MET C C   1 
ATOM   6191 O  O   . MET C 1 240 ? 1.630   11.778  59.741  1.00 10.89 ? 241 MET C O   1 
ATOM   6192 C  CB  . MET C 1 240 ? 0.734   14.068  58.239  1.00 12.27 ? 241 MET C CB  1 
ATOM   6193 C  CG  . MET C 1 240 ? 1.768   15.049  58.955  1.00 11.43 ? 241 MET C CG  1 
ATOM   6194 S  SD  . MET C 1 240 ? 0.930   16.455  59.722  1.00 12.30 ? 241 MET C SD  1 
ATOM   6195 C  CE  . MET C 1 240 ? 0.803   17.534  58.262  1.00 12.33 ? 241 MET C CE  1 
ATOM   6196 N  N   . VAL C 1 241 ? 3.262   11.370  58.213  1.00 9.85  ? 242 VAL C N   1 
ATOM   6197 C  CA  . VAL C 1 241 ? 4.060   10.477  59.032  1.00 9.45  ? 242 VAL C CA  1 
ATOM   6198 C  C   . VAL C 1 241 ? 5.516   10.692  58.697  1.00 9.54  ? 242 VAL C C   1 
ATOM   6199 O  O   . VAL C 1 241 ? 5.842   11.073  57.578  1.00 10.46 ? 242 VAL C O   1 
ATOM   6200 C  CB  . VAL C 1 241 ? 3.729   8.918   58.881  1.00 9.79  ? 242 VAL C CB  1 
ATOM   6201 C  CG1 . VAL C 1 241 ? 2.281   8.664   59.303  1.00 11.78 ? 242 VAL C CG1 1 
ATOM   6202 C  CG2 . VAL C 1 241 ? 3.948   8.473   57.433  1.00 11.02 ? 242 VAL C CG2 1 
ATOM   6203 N  N   . ASP C 1 242 ? 6.409   10.371  59.637  1.00 8.45  ? 243 ASP C N   1 
ATOM   6204 C  CA  . ASP C 1 242 ? 7.817   10.526  59.447  1.00 8.75  ? 243 ASP C CA  1 
ATOM   6205 C  C   . ASP C 1 242 ? 8.213   11.938  59.048  1.00 8.62  ? 243 ASP C C   1 
ATOM   6206 O  O   . ASP C 1 242 ? 9.039   12.173  58.158  1.00 10.01 ? 243 ASP C O   1 
ATOM   6207 C  CB  . ASP C 1 242 ? 8.389   9.464   58.444  1.00 8.93  ? 243 ASP C CB  1 
ATOM   6208 C  CG  . ASP C 1 242 ? 8.308   8.077   59.023  1.00 9.61  ? 243 ASP C CG  1 
ATOM   6209 O  OD1 . ASP C 1 242 ? 8.550   7.872   60.238  1.00 9.47  ? 243 ASP C OD1 1 
ATOM   6210 O  OD2 . ASP C 1 242 ? 7.889   7.132   58.251  1.00 11.60 ? 243 ASP C OD2 1 
ATOM   6211 N  N   . ASN C 1 243 ? 7.688   12.889  59.803  1.00 8.12  ? 244 ASN C N   1 
ATOM   6212 C  CA  . ASN C 1 243 ? 7.983   14.315  59.608  1.00 9.05  ? 244 ASN C CA  1 
ATOM   6213 C  C   . ASN C 1 243 ? 9.080   14.753  60.572  1.00 8.00  ? 244 ASN C C   1 
ATOM   6214 O  O   . ASN C 1 243 ? 8.943   15.758  61.251  1.00 8.68  ? 244 ASN C O   1 
ATOM   6215 C  CB  . ASN C 1 243 ? 6.687   15.179  59.727  1.00 8.87  ? 244 ASN C CB  1 
ATOM   6216 C  CG  . ASN C 1 243 ? 5.983   15.015  61.060  1.00 9.57  ? 244 ASN C CG  1 
ATOM   6217 O  OD1 . ASN C 1 243 ? 6.348   14.141  61.869  1.00 10.02 ? 244 ASN C OD1 1 
ATOM   6218 N  ND2 . ASN C 1 243 ? 5.005   15.849  61.305  1.00 13.13 ? 244 ASN C ND2 1 
ATOM   6219 N  N   . TRP C 1 244 ? 10.163  13.983  60.601  1.00 7.65  ? 245 TRP C N   1 
ATOM   6220 C  CA  . TRP C 1 244 ? 11.307  14.192  61.472  1.00 7.16  ? 245 TRP C CA  1 
ATOM   6221 C  C   . TRP C 1 244 ? 12.571  14.300  60.677  1.00 8.68  ? 245 TRP C C   1 
ATOM   6222 O  O   . TRP C 1 244 ? 12.750  13.582  59.682  1.00 9.09  ? 245 TRP C O   1 
ATOM   6223 C  CB  . TRP C 1 244 ? 11.470  13.119  62.555  1.00 7.65  ? 245 TRP C CB  1 
ATOM   6224 C  CG  . TRP C 1 244 ? 11.421  11.709  62.075  1.00 7.12  ? 245 TRP C CG  1 
ATOM   6225 C  CD1 . TRP C 1 244 ? 10.280  10.940  61.833  1.00 7.69  ? 245 TRP C CD1 1 
ATOM   6226 C  CD2 . TRP C 1 244 ? 12.549  10.849  61.826  1.00 7.84  ? 245 TRP C CD2 1 
ATOM   6227 N  NE1 . TRP C 1 244 ? 10.633  9.670   61.396  1.00 8.64  ? 245 TRP C NE1 1 
ATOM   6228 C  CE2 . TRP C 1 244 ? 12.007  9.568   61.408  1.00 8.25  ? 245 TRP C CE2 1 
ATOM   6229 C  CE3 . TRP C 1 244 ? 13.932  10.995  61.948  1.00 9.30  ? 245 TRP C CE3 1 
ATOM   6230 C  CZ2 . TRP C 1 244 ? 12.845  8.486   61.043  1.00 9.77  ? 245 TRP C CZ2 1 
ATOM   6231 C  CZ3 . TRP C 1 244 ? 14.774  9.886   61.624  1.00 10.42 ? 245 TRP C CZ3 1 
ATOM   6232 C  CH2 . TRP C 1 244 ? 14.220  8.651   61.228  1.00 10.44 ? 245 TRP C CH2 1 
ATOM   6233 N  N   . ARG C 1 245 ? 13.465  15.194  61.107  1.00 7.54  ? 246 ARG C N   1 
ATOM   6234 C  CA  . ARG C 1 245 ? 14.822  15.327  60.516  1.00 8.43  ? 246 ARG C CA  1 
ATOM   6235 C  C   . ARG C 1 245 ? 15.721  14.389  61.340  1.00 8.69  ? 246 ARG C C   1 
ATOM   6236 O  O   . ARG C 1 245 ? 15.644  14.377  62.538  1.00 9.30  ? 246 ARG C O   1 
ATOM   6237 C  CB  . ARG C 1 245 ? 15.302  16.767  60.596  1.00 8.60  ? 246 ARG C CB  1 
ATOM   6238 C  CG  . ARG C 1 245 ? 16.630  16.949  59.865  1.00 8.74  ? 246 ARG C CG  1 
ATOM   6239 C  CD  . ARG C 1 245 ? 17.179  18.351  60.147  1.00 9.22  ? 246 ARG C CD  1 
ATOM   6240 N  NE  . ARG C 1 245 ? 18.192  18.715  59.148  1.00 9.50  ? 246 ARG C NE  1 
ATOM   6241 C  CZ  . ARG C 1 245 ? 19.079  19.707  59.247  1.00 9.82  ? 246 ARG C CZ  1 
ATOM   6242 N  NH1 . ARG C 1 245 ? 19.121  20.492  60.316  1.00 9.63  ? 246 ARG C NH1 1 
ATOM   6243 N  NH2 . ARG C 1 245 ? 19.937  19.910  58.256  1.00 11.61 ? 246 ARG C NH2 1 
ATOM   6244 N  N   . PRO C 1 246 ? 16.596  13.597  60.675  1.00 9.07  ? 247 PRO C N   1 
ATOM   6245 C  CA  . PRO C 1 246 ? 17.519  12.768  61.421  1.00 9.27  ? 247 PRO C CA  1 
ATOM   6246 C  C   . PRO C 1 246 ? 18.573  13.591  62.140  1.00 9.00  ? 247 PRO C C   1 
ATOM   6247 O  O   . PRO C 1 246 ? 18.813  14.773  61.831  1.00 9.15  ? 247 PRO C O   1 
ATOM   6248 C  CB  . PRO C 1 246 ? 18.130  11.878  60.373  1.00 12.27 ? 247 PRO C CB  1 
ATOM   6249 C  CG  . PRO C 1 246 ? 17.304  12.046  59.142  1.00 17.64 ? 247 PRO C CG  1 
ATOM   6250 C  CD  . PRO C 1 246 ? 16.745  13.398  59.237  1.00 11.03 ? 247 PRO C CD  1 
ATOM   6251 N  N   . ALA C 1 247 ? 19.250  12.918  63.046  1.00 9.22  ? 248 ALA C N   1 
ATOM   6252 C  CA  . ALA C 1 247 ? 20.325  13.556  63.791  1.00 9.84  ? 248 ALA C CA  1 
ATOM   6253 C  C   . ALA C 1 247 ? 21.400  14.066  62.874  1.00 9.36  ? 248 ALA C C   1 
ATOM   6254 O  O   . ALA C 1 247 ? 21.805  13.393  61.918  1.00 11.47 ? 248 ALA C O   1 
ATOM   6255 C  CB  . ALA C 1 247 ? 20.935  12.530  64.726  1.00 11.74 ? 248 ALA C CB  1 
ATOM   6256 N  N   . GLN C 1 248 ? 21.950  15.236  63.196  1.00 9.54  ? 249 GLN C N   1 
ATOM   6257 C  CA  . GLN C 1 248 ? 22.954  15.967  62.436  1.00 9.13  ? 249 GLN C CA  1 
ATOM   6258 C  C   . GLN C 1 248 ? 24.297  15.947  63.186  1.00 9.49  ? 249 GLN C C   1 
ATOM   6259 O  O   . GLN C 1 248 ? 24.359  15.751  64.395  1.00 10.87 ? 249 GLN C O   1 
ATOM   6260 C  CB  . GLN C 1 248 ? 22.495  17.397  62.223  1.00 9.44  ? 249 GLN C CB  1 
ATOM   6261 C  CG  . GLN C 1 248 ? 21.172  17.500  61.436  1.00 10.35 ? 249 GLN C CG  1 
ATOM   6262 C  CD  . GLN C 1 248 ? 21.279  16.828  60.050  1.00 11.29 ? 249 GLN C CD  1 
ATOM   6263 O  OE1 . GLN C 1 248 ? 22.168  17.150  59.279  1.00 13.61 ? 249 GLN C OE1 1 
ATOM   6264 N  NE2 . GLN C 1 248 ? 20.414  15.907  59.725  1.00 10.88 ? 249 GLN C NE2 1 
ATOM   6265 N  N   . PRO C 1 249 ? 25.415  16.240  62.487  1.00 12.60 ? 250 PRO C N   1 
ATOM   6266 C  CA  . PRO C 1 249 ? 26.708  16.190  63.129  1.00 13.44 ? 250 PRO C CA  1 
ATOM   6267 C  C   . PRO C 1 249 ? 26.776  17.210  64.274  1.00 11.39 ? 250 PRO C C   1 
ATOM   6268 O  O   . PRO C 1 249 ? 26.432  18.390  64.150  1.00 12.28 ? 250 PRO C O   1 
ATOM   6269 C  CB  . PRO C 1 249 ? 27.691  16.588  62.015  1.00 18.76 ? 250 PRO C CB  1 
ATOM   6270 C  CG  . PRO C 1 249 ? 27.008  16.195  60.752  1.00 19.71 ? 250 PRO C CG  1 
ATOM   6271 C  CD  . PRO C 1 249 ? 25.534  16.461  61.040  1.00 14.18 ? 250 PRO C CD  1 
ATOM   6272 N  N   . LEU C 1 250 ? 27.309  16.772  65.388  1.00 12.45 ? 251 LEU C N   1 
ATOM   6273 C  CA  . LEU C 1 250 ? 27.472  17.619  66.589  1.00 12.07 ? 251 LEU C CA  1 
ATOM   6274 C  C   . LEU C 1 250 ? 28.509  18.705  66.371  1.00 13.92 ? 251 LEU C C   1 
ATOM   6275 O  O   . LEU C 1 250 ? 28.416  19.790  66.936  1.00 13.00 ? 251 LEU C O   1 
ATOM   6276 C  CB  . LEU C 1 250 ? 27.870  16.769  67.805  1.00 12.76 ? 251 LEU C CB  1 
ATOM   6277 C  CG  . LEU C 1 250 ? 27.834  17.409  69.173  1.00 14.09 ? 251 LEU C CG  1 
ATOM   6278 C  CD1 . LEU C 1 250 ? 26.453  18.047  69.588  1.00 14.90 ? 251 LEU C CD1 1 
ATOM   6279 C  CD2 . LEU C 1 250 ? 28.316  16.493  70.316  1.00 16.90 ? 251 LEU C CD2 1 
ATOM   6280 N  N   . LYS C 1 251 ? 29.534  18.405  65.557  1.00 14.43 ? 252 LYS C N   1 
ATOM   6281 C  CA  . LYS C 1 251 ? 30.608  19.419  65.246  1.00 13.73 ? 252 LYS C CA  1 
ATOM   6282 C  C   . LYS C 1 251 ? 31.176  19.959  66.556  1.00 16.38 ? 252 LYS C C   1 
ATOM   6283 O  O   . LYS C 1 251 ? 31.448  19.171  67.472  1.00 20.17 ? 252 LYS C O   1 
ATOM   6284 C  CB  . LYS C 1 251 ? 30.160  20.482  64.228  1.00 16.42 ? 252 LYS C CB  1 
ATOM   6285 C  CG  . LYS C 1 251 ? 29.787  19.772  62.941  1.00 20.13 ? 252 LYS C CG  1 
ATOM   6286 C  CD  . LYS C 1 251 ? 29.460  20.731  61.808  1.00 24.24 ? 252 LYS C CD  1 
ATOM   6287 C  CE  . LYS C 1 251 ? 29.158  20.004  60.516  1.00 23.49 ? 252 LYS C CE  1 
ATOM   6288 N  NZ  . LYS C 1 251 ? 28.879  21.013  59.461  1.00 28.14 ? 252 LYS C NZ  1 
ATOM   6289 N  N   . ASN C 1 252 ? 31.379  21.254  66.687  1.00 14.47 ? 253 ASN C N   1 
ATOM   6290 C  CA  . ASN C 1 252 ? 32.182  21.587  67.849  1.00 24.27 ? 253 ASN C CA  1 
ATOM   6291 C  C   . ASN C 1 252 ? 31.563  21.464  69.331  1.00 30.41 ? 253 ASN C C   1 
ATOM   6292 O  O   . ASN C 1 252 ? 32.248  21.558  70.384  1.00 34.20 ? 253 ASN C O   1 
ATOM   6293 C  CB  . ASN C 1 252 ? 33.077  22.808  67.495  1.00 29.75 ? 253 ASN C CB  1 
ATOM   6294 C  CG  . ASN C 1 252 ? 34.512  22.376  67.176  1.00 48.94 ? 253 ASN C CG  1 
ATOM   6295 O  OD1 . ASN C 1 252 ? 34.852  21.171  67.248  1.00 47.27 ? 253 ASN C OD1 1 
ATOM   6296 N  ND2 . ASN C 1 252 ? 35.360  23.337  66.824  1.00 76.34 ? 253 ASN C ND2 1 
ATOM   6297 N  N   . ARG C 1 253 ? 30.305  21.150  69.384  1.00 16.58 ? 254 ARG C N   1 
ATOM   6298 C  CA  . ARG C 1 253 ? 29.439  21.516  70.495  1.00 12.98 ? 254 ARG C CA  1 
ATOM   6299 C  C   . ARG C 1 253 ? 29.564  20.584  71.642  1.00 14.53 ? 254 ARG C C   1 
ATOM   6300 O  O   . ARG C 1 253 ? 29.810  19.374  71.437  1.00 17.78 ? 254 ARG C O   1 
ATOM   6301 C  CB  . ARG C 1 253 ? 27.990  21.582  69.950  1.00 12.56 ? 254 ARG C CB  1 
ATOM   6302 C  CG  . ARG C 1 253 ? 27.819  22.706  68.930  1.00 11.83 ? 254 ARG C CG  1 
ATOM   6303 C  CD  . ARG C 1 253 ? 26.425  22.726  68.305  1.00 11.27 ? 254 ARG C CD  1 
ATOM   6304 N  NE  . ARG C 1 253 ? 26.242  21.574  67.356  1.00 11.24 ? 254 ARG C NE  1 
ATOM   6305 C  CZ  . ARG C 1 253 ? 25.113  21.294  66.727  1.00 9.06  ? 254 ARG C CZ  1 
ATOM   6306 N  NH1 . ARG C 1 253 ? 24.000  21.973  67.025  1.00 9.12  ? 254 ARG C NH1 1 
ATOM   6307 N  NH2 . ARG C 1 253 ? 25.082  20.280  65.870  1.00 9.83  ? 254 ARG C NH2 1 
ATOM   6308 N  N   . GLN C 1 254 ? 29.162  21.071  72.813  1.00 13.71 ? 255 GLN C N   1 
ATOM   6309 C  CA  . GLN C 1 254 ? 29.066  20.309  74.022  1.00 17.00 ? 255 GLN C CA  1 
ATOM   6310 C  C   . GLN C 1 254 ? 27.605  20.346  74.428  1.00 15.68 ? 255 GLN C C   1 
ATOM   6311 O  O   . GLN C 1 254 ? 26.892  21.375  74.388  1.00 18.33 ? 255 GLN C O   1 
ATOM   6312 C  CB  . GLN C 1 254 ? 29.908  21.022  75.105  1.00 22.08 ? 255 GLN C CB  1 
ATOM   6313 C  CG  . GLN C 1 254 ? 29.751  20.578  76.556  1.00 32.49 ? 255 GLN C CG  1 
ATOM   6314 C  CD  . GLN C 1 254 ? 30.583  19.374  76.967  1.00 51.08 ? 255 GLN C CD  1 
ATOM   6315 O  OE1 . GLN C 1 254 ? 31.680  19.492  77.680  1.00 81.52 ? 255 GLN C OE1 1 
ATOM   6316 N  NE2 . GLN C 1 254 ? 30.040  18.147  76.554  1.00 73.62 ? 255 GLN C NE2 1 
ATOM   6317 N  N   . ILE C 1 255 ? 27.089  19.186  74.760  1.00 11.80 ? 256 ILE C N   1 
ATOM   6318 C  CA  . ILE C 1 255 ? 25.753  19.077  75.335  1.00 12.25 ? 256 ILE C CA  1 
ATOM   6319 C  C   . ILE C 1 255 ? 25.922  19.059  76.887  1.00 12.75 ? 256 ILE C C   1 
ATOM   6320 O  O   . ILE C 1 255 ? 26.836  18.388  77.390  1.00 12.52 ? 256 ILE C O   1 
ATOM   6321 C  CB  . ILE C 1 255 ? 25.027  17.798  74.883  1.00 11.57 ? 256 ILE C CB  1 
ATOM   6322 C  CG1 . ILE C 1 255 ? 24.996  17.771  73.318  1.00 11.83 ? 256 ILE C CG1 1 
ATOM   6323 C  CG2 . ILE C 1 255 ? 23.662  17.694  75.527  1.00 13.99 ? 256 ILE C CG2 1 
ATOM   6324 C  CD1 . ILE C 1 255 ? 24.286  16.511  72.843  1.00 14.02 ? 256 ILE C CD1 1 
ATOM   6325 N  N   . LYS C 1 256 ? 25.200  19.922  77.590  1.00 11.74 ? 257 LYS C N   1 
ATOM   6326 C  CA  . LYS C 1 256 ? 25.227  19.989  79.027  1.00 11.07 ? 257 LYS C CA  1 
ATOM   6327 C  C   . LYS C 1 256 ? 24.052  19.308  79.635  1.00 11.99 ? 257 LYS C C   1 
ATOM   6328 O  O   . LYS C 1 256 ? 22.950  19.390  79.059  1.00 13.56 ? 257 LYS C O   1 
ATOM   6329 C  CB  . LYS C 1 256 ? 25.344  21.470  79.465  1.00 15.41 ? 257 LYS C CB  1 
ATOM   6330 C  CG  . LYS C 1 256 ? 26.629  22.127  78.939  1.00 20.44 ? 257 LYS C CG  1 
ATOM   6331 C  CD  . LYS C 1 256 ? 26.564  23.620  79.187  1.00 28.09 ? 257 LYS C CD  1 
ATOM   6332 C  CE  . LYS C 1 256 ? 27.928  24.285  79.013  1.00 41.60 ? 257 LYS C CE  1 
ATOM   6333 N  NZ  . LYS C 1 256 ? 27.829  25.715  78.520  1.00 39.55 ? 257 LYS C NZ  1 
ATOM   6334 N  N   . ALA C 1 257 ? 24.222  18.701  80.803  1.00 12.36 ? 258 ALA C N   1 
ATOM   6335 C  CA  . ALA C 1 257 ? 23.138  18.115  81.577  1.00 12.40 ? 258 ALA C CA  1 
ATOM   6336 C  C   . ALA C 1 257 ? 22.838  18.884  82.869  1.00 13.20 ? 258 ALA C C   1 
ATOM   6337 O  O   . ALA C 1 257 ? 23.750  19.355  83.554  1.00 14.94 ? 258 ALA C O   1 
ATOM   6338 C  CB  . ALA C 1 257 ? 23.422  16.632  81.951  1.00 14.32 ? 258 ALA C CB  1 
ATOM   6339 N  N   . SER C 1 258 ? 21.577  19.014  83.218  1.00 12.57 ? 259 SER C N   1 
ATOM   6340 C  CA  . SER C 1 258 ? 21.203  19.715  84.439  1.00 15.58 ? 259 SER C CA  1 
ATOM   6341 C  C   . SER C 1 258 ? 21.269  18.788  85.660  1.00 14.66 ? 259 SER C C   1 
ATOM   6342 O  O   . SER C 1 258 ? 20.988  19.244  86.781  1.00 19.40 ? 259 SER C O   1 
ATOM   6343 C  CB  . SER C 1 258 ? 19.808  20.259  84.296  1.00 14.44 ? 259 SER C CB  1 
ATOM   6344 O  OG  . SER C 1 258 ? 18.847  19.252  84.346  1.00 12.31 ? 259 SER C OG  1 
ATOM   6345 N  N   . PHE C 1 259 ? 21.629  17.534  85.455  1.00 15.89 ? 260 PHE C N   1 
ATOM   6346 C  CA  . PHE C 1 259 ? 21.472  16.516  86.475  1.00 20.12 ? 260 PHE C CA  1 
ATOM   6347 C  C   . PHE C 1 259 ? 22.614  15.493  86.363  1.00 19.84 ? 260 PHE C C   1 
ATOM   6348 O  O   . PHE C 1 259 ? 23.302  15.387  85.304  1.00 21.12 ? 260 PHE C O   1 
ATOM   6349 C  CB  . PHE C 1 259 ? 20.126  15.775  86.266  1.00 19.19 ? 260 PHE C CB  1 
ATOM   6350 C  CG  . PHE C 1 259 ? 20.108  14.998  84.951  1.00 19.04 ? 260 PHE C CG  1 
ATOM   6351 C  CD1 . PHE C 1 259 ? 19.784  15.664  83.749  1.00 16.62 ? 260 PHE C CD1 1 
ATOM   6352 C  CD2 . PHE C 1 259 ? 20.554  13.662  84.883  1.00 22.26 ? 260 PHE C CD2 1 
ATOM   6353 C  CE1 . PHE C 1 259 ? 19.872  14.979  82.532  1.00 16.88 ? 260 PHE C CE1 1 
ATOM   6354 C  CE2 . PHE C 1 259 ? 20.634  12.988  83.648  1.00 20.98 ? 260 PHE C CE2 1 
ATOM   6355 C  CZ  . PHE C 1 259 ? 20.267  13.628  82.467  1.00 18.69 ? 260 PHE C CZ  1 
ATOM   6356 N  N   . LYS C 1 260 ? 22.825  14.739  87.437  1.00 31.77 ? 261 LYS C N   1 
ATOM   6357 C  CA  . LYS C 1 260 ? 23.875  13.728  87.470  1.00 34.61 ? 261 LYS C CA  1 
ATOM   6358 C  C   . LYS C 1 260 ? 25.064  14.140  86.608  1.00 39.95 ? 261 LYS C C   1 
ATOM   6359 O  O   . LYS C 1 260 ? 26.186  13.681  86.822  1.00 60.54 ? 261 LYS C O   1 
ATOM   6360 C  CB  . LYS C 1 260 ? 23.331  12.376  87.003  1.00 45.77 ? 261 LYS C CB  1 
ATOM   6361 N  N   . HIS D 1 3   ? 22.202  22.524  4.078   1.00 25.60 ? 3   HIS D N   1 
ATOM   6362 C  CA  . HIS D 1 3   ? 23.075  21.433  4.670   1.00 35.67 ? 3   HIS D CA  1 
ATOM   6363 C  C   . HIS D 1 3   ? 23.768  21.922  5.930   1.00 39.53 ? 3   HIS D C   1 
ATOM   6364 O  O   . HIS D 1 3   ? 25.028  22.006  6.018   1.00 45.42 ? 3   HIS D O   1 
ATOM   6365 C  CB  . HIS D 1 3   ? 24.118  20.960  3.718   1.00 32.74 ? 3   HIS D CB  1 
ATOM   6366 C  CG  . HIS D 1 3   ? 24.935  19.802  4.267   1.00 33.81 ? 3   HIS D CG  1 
ATOM   6367 N  ND1 . HIS D 1 3   ? 24.617  18.493  4.024   1.00 35.55 ? 3   HIS D ND1 1 
ATOM   6368 C  CD2 . HIS D 1 3   ? 26.094  19.791  5.097   1.00 25.71 ? 3   HIS D CD2 1 
ATOM   6369 C  CE1 . HIS D 1 3   ? 25.542  17.703  4.642   1.00 33.96 ? 3   HIS D CE1 1 
ATOM   6370 N  NE2 . HIS D 1 3   ? 26.445  18.511  5.274   1.00 30.05 ? 3   HIS D NE2 1 
ATOM   6371 N  N   . HIS D 1 4   ? 22.945  22.273  6.921   1.00 46.89 ? 4   HIS D N   1 
ATOM   6372 C  CA  . HIS D 1 4   ? 23.475  22.763  8.155   1.00 32.84 ? 4   HIS D CA  1 
ATOM   6373 C  C   . HIS D 1 4   ? 23.839  21.631  9.036   1.00 21.40 ? 4   HIS D C   1 
ATOM   6374 O  O   . HIS D 1 4   ? 23.613  20.443  8.753   1.00 19.42 ? 4   HIS D O   1 
ATOM   6375 C  CB  . HIS D 1 4   ? 22.510  23.771  8.771   1.00 38.26 ? 4   HIS D CB  1 
ATOM   6376 C  CG  . HIS D 1 4   ? 23.079  25.173  8.842   1.00 56.90 ? 4   HIS D CG  1 
ATOM   6377 N  ND1 . HIS D 1 4   ? 22.557  26.219  8.151   1.00 72.56 ? 4   HIS D ND1 1 
ATOM   6378 C  CD2 . HIS D 1 4   ? 24.176  25.677  9.550   1.00 46.01 ? 4   HIS D CD2 1 
ATOM   6379 C  CE1 . HIS D 1 4   ? 23.279  27.338  8.413   1.00 74.24 ? 4   HIS D CE1 1 
ATOM   6380 N  NE2 . HIS D 1 4   ? 24.266  27.005  9.272   1.00 74.66 ? 4   HIS D NE2 1 
ATOM   6381 N  N   . TRP D 1 5   ? 24.521  21.961  10.095  1.00 19.22 ? 5   TRP D N   1 
ATOM   6382 C  CA  . TRP D 1 5   ? 24.981  20.987  11.038  1.00 15.44 ? 5   TRP D CA  1 
ATOM   6383 C  C   . TRP D 1 5   ? 23.916  20.194  11.725  1.00 14.79 ? 5   TRP D C   1 
ATOM   6384 O  O   . TRP D 1 5   ? 22.770  20.611  11.900  1.00 15.27 ? 5   TRP D O   1 
ATOM   6385 C  CB  . TRP D 1 5   ? 25.903  21.694  12.020  1.00 17.10 ? 5   TRP D CB  1 
ATOM   6386 C  CG  . TRP D 1 5   ? 25.164  22.496  13.069  1.00 16.24 ? 5   TRP D CG  1 
ATOM   6387 C  CD1 . TRP D 1 5   ? 24.870  23.864  13.010  1.00 18.73 ? 5   TRP D CD1 1 
ATOM   6388 C  CD2 . TRP D 1 5   ? 24.662  22.002  14.355  1.00 15.10 ? 5   TRP D CD2 1 
ATOM   6389 N  NE1 . TRP D 1 5   ? 24.212  24.264  14.157  1.00 16.11 ? 5   TRP D NE1 1 
ATOM   6390 C  CE2 . TRP D 1 5   ? 24.051  23.146  15.016  1.00 16.49 ? 5   TRP D CE2 1 
ATOM   6391 C  CE3 . TRP D 1 5   ? 24.651  20.754  14.972  1.00 12.52 ? 5   TRP D CE3 1 
ATOM   6392 C  CZ2 . TRP D 1 5   ? 23.443  23.049  16.255  1.00 16.71 ? 5   TRP D CZ2 1 
ATOM   6393 C  CZ3 . TRP D 1 5   ? 24.035  20.678  16.276  1.00 13.10 ? 5   TRP D CZ3 1 
ATOM   6394 C  CH2 . TRP D 1 5   ? 23.472  21.811  16.885  1.00 14.63 ? 5   TRP D CH2 1 
ATOM   6395 N  N   . GLY D 1 6   ? 24.292  18.965  12.089  1.00 15.02 ? 6   GLY D N   1 
ATOM   6396 C  CA  . GLY D 1 6   ? 23.372  18.166  12.893  1.00 15.78 ? 6   GLY D CA  1 
ATOM   6397 C  C   . GLY D 1 6   ? 24.217  17.085  13.555  1.00 13.49 ? 6   GLY D C   1 
ATOM   6398 O  O   . GLY D 1 6   ? 25.362  17.248  13.889  1.00 13.80 ? 6   GLY D O   1 
ATOM   6399 N  N   . TYR D 1 7   ? 23.636  15.900  13.600  1.00 14.05 ? 7   TYR D N   1 
ATOM   6400 C  CA  . TYR D 1 7   ? 24.221  14.746  14.255  1.00 14.09 ? 7   TYR D CA  1 
ATOM   6401 C  C   . TYR D 1 7   ? 24.403  13.491  13.426  1.00 17.78 ? 7   TYR D C   1 
ATOM   6402 O  O   . TYR D 1 7   ? 24.936  12.468  13.912  1.00 19.46 ? 7   TYR D O   1 
ATOM   6403 C  CB  . TYR D 1 7   ? 23.390  14.404  15.520  1.00 13.96 ? 7   TYR D CB  1 
ATOM   6404 C  CG  . TYR D 1 7   ? 23.546  15.491  16.602  1.00 12.24 ? 7   TYR D CG  1 
ATOM   6405 C  CD1 . TYR D 1 7   ? 24.678  15.467  17.463  1.00 11.09 ? 7   TYR D CD1 1 
ATOM   6406 C  CD2 . TYR D 1 7   ? 22.578  16.480  16.803  1.00 14.90 ? 7   TYR D CD2 1 
ATOM   6407 C  CE1 . TYR D 1 7   ? 24.802  16.464  18.474  1.00 10.78 ? 7   TYR D CE1 1 
ATOM   6408 C  CE2 . TYR D 1 7   ? 22.724  17.446  17.803  1.00 13.35 ? 7   TYR D CE2 1 
ATOM   6409 C  CZ  . TYR D 1 7   ? 23.853  17.378  18.617  1.00 10.54 ? 7   TYR D CZ  1 
ATOM   6410 O  OH  . TYR D 1 7   ? 23.966  18.384  19.608  1.00 12.84 ? 7   TYR D OH  1 
ATOM   6411 N  N   . GLY D 1 8   ? 24.128  13.619  12.132  1.00 19.54 ? 8   GLY D N   1 
ATOM   6412 C  CA  . GLY D 1 8   ? 24.250  12.429  11.232  1.00 17.16 ? 8   GLY D CA  1 
ATOM   6413 C  C   . GLY D 1 8   ? 25.615  12.218  10.605  1.00 18.33 ? 8   GLY D C   1 
ATOM   6414 O  O   . GLY D 1 8   ? 26.619  12.936  10.899  1.00 18.03 ? 8   GLY D O   1 
ATOM   6415 N  N   . LYS D 1 9   ? 25.697  11.240  9.685   1.00 19.40 ? 9   LYS D N   1 
ATOM   6416 C  CA  . LYS D 1 9   ? 26.967  10.803  9.083   1.00 22.25 ? 9   LYS D CA  1 
ATOM   6417 C  C   . LYS D 1 9   ? 27.584  11.942  8.305   1.00 15.42 ? 9   LYS D C   1 
ATOM   6418 O  O   . LYS D 1 9   ? 28.768  12.100  8.299   1.00 17.01 ? 9   LYS D O   1 
ATOM   6419 C  CB  . LYS D 1 9   ? 26.718  9.683   8.062   1.00 22.22 ? 9   LYS D CB  1 
ATOM   6420 C  CG  . LYS D 1 9   ? 28.014  9.217   7.381   1.00 26.18 ? 9   LYS D CG  1 
ATOM   6421 C  CD  . LYS D 1 9   ? 27.813  8.066   6.375   1.00 41.46 ? 9   LYS D CD  1 
ATOM   6422 C  CE  . LYS D 1 9   ? 29.141  7.610   5.744   1.00 49.71 ? 9   LYS D CE  1 
ATOM   6423 N  NZ  . LYS D 1 9   ? 29.062  6.869   4.435   1.00 51.42 ? 9   LYS D NZ  1 
ATOM   6424 N  N   . HIS D 1 10  ? 26.749  12.696  7.610   1.00 17.54 ? 10  HIS D N   1 
ATOM   6425 C  CA  . HIS D 1 10  ? 27.263  13.766  6.707   1.00 16.08 ? 10  HIS D CA  1 
ATOM   6426 C  C   . HIS D 1 10  ? 27.311  15.135  7.236   1.00 16.75 ? 10  HIS D C   1 
ATOM   6427 O  O   . HIS D 1 10  ? 28.003  15.967  6.647   1.00 16.67 ? 10  HIS D O   1 
ATOM   6428 C  CB  . HIS D 1 10  ? 26.445  13.756  5.408   1.00 15.31 ? 10  HIS D CB  1 
ATOM   6429 C  CG  . HIS D 1 10  ? 26.431  12.401  4.758   1.00 15.80 ? 10  HIS D CG  1 
ATOM   6430 N  ND1 . HIS D 1 10  ? 27.515  11.883  4.077   1.00 17.73 ? 10  HIS D ND1 1 
ATOM   6431 C  CD2 . HIS D 1 10  ? 25.492  11.436  4.810   1.00 15.94 ? 10  HIS D CD2 1 
ATOM   6432 C  CE1 . HIS D 1 10  ? 27.218  10.627  3.671   1.00 19.56 ? 10  HIS D CE1 1 
ATOM   6433 N  NE2 . HIS D 1 10  ? 25.955  10.339  4.110   1.00 17.58 ? 10  HIS D NE2 1 
ATOM   6434 N  N   . ASN D 1 11  ? 26.757  15.333  8.452   1.00 14.98 ? 11  ASN D N   1 
ATOM   6435 C  CA  . ASN D 1 11  ? 26.707  16.699  9.015   1.00 14.36 ? 11  ASN D CA  1 
ATOM   6436 C  C   . ASN D 1 11  ? 27.009  16.712  10.543  1.00 15.18 ? 11  ASN D C   1 
ATOM   6437 O  O   . ASN D 1 11  ? 26.836  17.800  11.183  1.00 15.75 ? 11  ASN D O   1 
ATOM   6438 C  CB  . ASN D 1 11  ? 25.363  17.358  8.786   1.00 13.47 ? 11  ASN D CB  1 
ATOM   6439 C  CG  . ASN D 1 11  ? 24.238  16.724  9.511   1.00 15.57 ? 11  ASN D CG  1 
ATOM   6440 O  OD1 . ASN D 1 11  ? 24.393  15.689  10.177  1.00 18.77 ? 11  ASN D OD1 1 
ATOM   6441 N  ND2 . ASN D 1 11  ? 23.083  17.309  9.385   1.00 17.86 ? 11  ASN D ND2 1 
ATOM   6442 N  N   . GLY D 1 12  ? 27.490  15.584  11.104  1.00 13.22 ? 12  GLY D N   1 
ATOM   6443 C  CA  . GLY D 1 12  ? 27.649  15.450  12.554  1.00 14.13 ? 12  GLY D CA  1 
ATOM   6444 C  C   . GLY D 1 12  ? 28.944  15.972  13.025  1.00 13.17 ? 12  GLY D C   1 
ATOM   6445 O  O   . GLY D 1 12  ? 29.695  16.672  12.370  1.00 13.29 ? 12  GLY D O   1 
ATOM   6446 N  N   . PRO D 1 13  ? 29.262  15.610  14.308  1.00 12.05 ? 13  PRO D N   1 
ATOM   6447 C  CA  . PRO D 1 13  ? 30.424  16.159  14.997  1.00 12.51 ? 13  PRO D CA  1 
ATOM   6448 C  C   . PRO D 1 13  ? 31.708  16.161  14.235  1.00 14.04 ? 13  PRO D C   1 
ATOM   6449 O  O   . PRO D 1 13  ? 32.526  17.074  14.435  1.00 13.79 ? 13  PRO D O   1 
ATOM   6450 C  CB  . PRO D 1 13  ? 30.466  15.318  16.276  1.00 14.29 ? 13  PRO D CB  1 
ATOM   6451 C  CG  . PRO D 1 13  ? 29.020  15.103  16.595  1.00 13.87 ? 13  PRO D CG  1 
ATOM   6452 C  CD  . PRO D 1 13  ? 28.356  14.865  15.240  1.00 14.48 ? 13  PRO D CD  1 
ATOM   6453 N  N   . GLU D 1 14  ? 31.964  15.125  13.397  1.00 13.78 ? 14  GLU D N   1 
ATOM   6454 C  CA  . GLU D 1 14  ? 33.256  15.060  12.673  1.00 15.61 ? 14  GLU D CA  1 
ATOM   6455 C  C   . GLU D 1 14  ? 33.308  16.066  11.542  1.00 12.56 ? 14  GLU D C   1 
ATOM   6456 O  O   . GLU D 1 14  ? 34.420  16.252  10.986  1.00 15.54 ? 14  GLU D O   1 
ATOM   6457 C  CB  . GLU D 1 14  ? 33.630  13.634  12.181  1.00 18.86 ? 14  GLU D CB  1 
ATOM   6458 C  CG  . GLU D 1 14  ? 33.425  12.497  13.225  1.00 23.62 ? 14  GLU D CG  1 
ATOM   6459 C  CD  . GLU D 1 14  ? 34.101  12.791  14.556  1.00 40.22 ? 14  GLU D CD  1 
ATOM   6460 O  OE1 . GLU D 1 14  ? 35.274  13.220  14.558  1.00 33.76 ? 14  GLU D OE1 1 
ATOM   6461 O  OE2 . GLU D 1 14  ? 33.455  12.596  15.606  1.00 40.63 ? 14  GLU D OE2 1 
ATOM   6462 N  N   . HIS D 1 15  ? 32.170  16.688  11.232  1.00 12.31 ? 15  HIS D N   1 
ATOM   6463 C  CA  . HIS D 1 15  ? 32.112  17.663  10.138  1.00 14.43 ? 15  HIS D CA  1 
ATOM   6464 C  C   . HIS D 1 15  ? 32.122  19.090  10.646  1.00 14.68 ? 15  HIS D C   1 
ATOM   6465 O  O   . HIS D 1 15  ? 32.399  20.047  9.868   1.00 13.48 ? 15  HIS D O   1 
ATOM   6466 C  CB  . HIS D 1 15  ? 30.821  17.488  9.388   1.00 15.34 ? 15  HIS D CB  1 
ATOM   6467 C  CG  . HIS D 1 15  ? 30.797  16.238  8.566   1.00 14.59 ? 15  HIS D CG  1 
ATOM   6468 N  ND1 . HIS D 1 15  ? 31.328  16.189  7.266   1.00 16.44 ? 15  HIS D ND1 1 
ATOM   6469 C  CD2 . HIS D 1 15  ? 30.331  14.968  8.848   1.00 16.51 ? 15  HIS D CD2 1 
ATOM   6470 C  CE1 . HIS D 1 15  ? 31.203  14.952  6.789   1.00 16.25 ? 15  HIS D CE1 1 
ATOM   6471 N  NE2 . HIS D 1 15  ? 30.621  14.183  7.717   1.00 16.68 ? 15  HIS D NE2 1 
ATOM   6472 N  N   . TRP D 1 16  ? 31.843  19.309  11.972  1.00 12.41 ? 16  TRP D N   1 
ATOM   6473 C  CA  . TRP D 1 16  ? 31.551  20.654  12.454  1.00 11.69 ? 16  TRP D CA  1 
ATOM   6474 C  C   . TRP D 1 16  ? 32.692  21.626  12.271  1.00 10.39 ? 16  TRP D C   1 
ATOM   6475 O  O   . TRP D 1 16  ? 32.478  22.830  12.113  1.00 12.25 ? 16  TRP D O   1 
ATOM   6476 C  CB  . TRP D 1 16  ? 31.165  20.590  13.944  1.00 11.72 ? 16  TRP D CB  1 
ATOM   6477 C  CG  . TRP D 1 16  ? 29.877  19.923  14.154  1.00 11.53 ? 16  TRP D CG  1 
ATOM   6478 C  CD1 . TRP D 1 16  ? 28.891  19.526  13.247  1.00 12.11 ? 16  TRP D CD1 1 
ATOM   6479 C  CD2 . TRP D 1 16  ? 29.342  19.538  15.482  1.00 11.81 ? 16  TRP D CD2 1 
ATOM   6480 N  NE1 . TRP D 1 16  ? 27.800  18.931  13.878  1.00 11.49 ? 16  TRP D NE1 1 
ATOM   6481 C  CE2 . TRP D 1 16  ? 28.033  18.961  15.262  1.00 11.55 ? 16  TRP D CE2 1 
ATOM   6482 C  CE3 . TRP D 1 16  ? 29.816  19.682  16.820  1.00 11.73 ? 16  TRP D CE3 1 
ATOM   6483 C  CZ2 . TRP D 1 16  ? 27.271  18.508  16.336  1.00 13.17 ? 16  TRP D CZ2 1 
ATOM   6484 C  CZ3 . TRP D 1 16  ? 29.033  19.226  17.860  1.00 12.60 ? 16  TRP D CZ3 1 
ATOM   6485 C  CH2 . TRP D 1 16  ? 27.831  18.669  17.642  1.00 13.74 ? 16  TRP D CH2 1 
ATOM   6486 N  N   . HIS D 1 17  ? 33.926  21.122  12.301  1.00 12.03 ? 17  HIS D N   1 
ATOM   6487 C  CA  . HIS D 1 17  ? 35.128  21.957  12.229  1.00 13.16 ? 17  HIS D CA  1 
ATOM   6488 C  C   . HIS D 1 17  ? 35.227  22.767  10.899  1.00 14.94 ? 17  HIS D C   1 
ATOM   6489 O  O   . HIS D 1 17  ? 35.858  23.830  10.903  1.00 13.61 ? 17  HIS D O   1 
ATOM   6490 C  CB  . HIS D 1 17  ? 36.420  21.183  12.416  1.00 13.49 ? 17  HIS D CB  1 
ATOM   6491 C  CG  . HIS D 1 17  ? 36.770  20.350  11.227  1.00 14.06 ? 17  HIS D CG  1 
ATOM   6492 N  ND1 . HIS D 1 17  ? 37.691  20.757  10.261  1.00 17.96 ? 17  HIS D ND1 1 
ATOM   6493 C  CD2 . HIS D 1 17  ? 36.269  19.131  10.814  1.00 14.58 ? 17  HIS D CD2 1 
ATOM   6494 C  CE1 . HIS D 1 17  ? 37.743  19.819  9.294   1.00 18.45 ? 17  HIS D CE1 1 
ATOM   6495 N  NE2 . HIS D 1 17  ? 36.888  18.839  9.583   1.00 16.37 ? 17  HIS D NE2 1 
ATOM   6496 N  N   . LYS D 1 18  ? 34.512  22.322  9.828   1.00 14.04 ? 18  LYS D N   1 
ATOM   6497 C  CA  . LYS D 1 18  ? 34.598  23.066  8.547   1.00 13.83 ? 18  LYS D CA  1 
ATOM   6498 C  C   . LYS D 1 18  ? 33.881  24.425  8.656   1.00 17.44 ? 18  LYS D C   1 
ATOM   6499 O  O   . LYS D 1 18  ? 34.464  25.466  8.294   1.00 19.83 ? 18  LYS D O   1 
ATOM   6500 C  CB  . LYS D 1 18  ? 33.979  22.192  7.472   1.00 13.90 ? 18  LYS D CB  1 
ATOM   6501 C  CG  . LYS D 1 18  ? 34.965  21.080  7.078   1.00 16.14 ? 18  LYS D CG  1 
ATOM   6502 C  CD  . LYS D 1 18  ? 34.303  20.093  6.141   1.00 15.13 ? 18  LYS D CD  1 
ATOM   6503 C  CE  . LYS D 1 18  ? 33.361  19.125  6.788   1.00 15.20 ? 18  LYS D CE  1 
ATOM   6504 N  NZ  . LYS D 1 18  ? 32.511  18.262  5.847   1.00 14.74 ? 18  LYS D NZ  1 
ATOM   6505 N  N   . ASP D 1 19  ? 32.728  24.448  9.289   1.00 16.77 ? 19  ASP D N   1 
ATOM   6506 C  CA  . ASP D 1 19  ? 32.069  25.707  9.505   1.00 20.00 ? 19  ASP D CA  1 
ATOM   6507 C  C   . ASP D 1 19  ? 32.554  26.394  10.795  1.00 16.98 ? 19  ASP D C   1 
ATOM   6508 O  O   . ASP D 1 19  ? 32.402  27.605  10.910  1.00 18.04 ? 19  ASP D O   1 
ATOM   6509 C  CB  . ASP D 1 19  ? 30.555  25.508  9.604   1.00 21.13 ? 19  ASP D CB  1 
ATOM   6510 C  CG  . ASP D 1 19  ? 29.824  25.637  8.266   1.00 31.01 ? 19  ASP D CG  1 
ATOM   6511 O  OD1 . ASP D 1 19  ? 30.357  26.204  7.279   1.00 29.29 ? 19  ASP D OD1 1 
ATOM   6512 O  OD2 . ASP D 1 19  ? 28.680  25.190  8.232   1.00 42.56 ? 19  ASP D OD2 1 
ATOM   6513 N  N   . PHE D 1 20  ? 33.072  25.649  11.758  1.00 14.23 ? 20  PHE D N   1 
ATOM   6514 C  CA  . PHE D 1 20  ? 33.360  26.187  13.084  1.00 12.83 ? 20  PHE D CA  1 
ATOM   6515 C  C   . PHE D 1 20  ? 34.717  25.701  13.506  1.00 14.15 ? 20  PHE D C   1 
ATOM   6516 O  O   . PHE D 1 20  ? 34.839  24.645  14.172  1.00 14.97 ? 20  PHE D O   1 
ATOM   6517 C  CB  . PHE D 1 20  ? 32.292  25.751  14.098  1.00 14.50 ? 20  PHE D CB  1 
ATOM   6518 C  CG  . PHE D 1 20  ? 30.876  26.192  13.671  1.00 15.12 ? 20  PHE D CG  1 
ATOM   6519 C  CD1 . PHE D 1 20  ? 30.421  27.502  13.840  1.00 17.99 ? 20  PHE D CD1 1 
ATOM   6520 C  CD2 . PHE D 1 20  ? 30.043  25.276  13.006  1.00 17.86 ? 20  PHE D CD2 1 
ATOM   6521 C  CE1 . PHE D 1 20  ? 29.153  27.887  13.348  1.00 18.06 ? 20  PHE D CE1 1 
ATOM   6522 C  CE2 . PHE D 1 20  ? 28.769  25.600  12.516  1.00 17.44 ? 20  PHE D CE2 1 
ATOM   6523 C  CZ  . PHE D 1 20  ? 28.317  26.921  12.762  1.00 17.50 ? 20  PHE D CZ  1 
ATOM   6524 N  N   . PRO D 1 21  ? 35.820  26.307  12.981  1.00 14.23 ? 21  PRO D N   1 
ATOM   6525 C  CA  . PRO D 1 21  ? 37.101  25.721  13.143  1.00 15.58 ? 21  PRO D CA  1 
ATOM   6526 C  C   . PRO D 1 21  ? 37.564  25.607  14.626  1.00 15.59 ? 21  PRO D C   1 
ATOM   6527 O  O   . PRO D 1 21  ? 38.482  24.854  14.913  1.00 14.82 ? 21  PRO D O   1 
ATOM   6528 C  CB  . PRO D 1 21  ? 38.050  26.688  12.364  1.00 17.42 ? 21  PRO D CB  1 
ATOM   6529 C  CG  . PRO D 1 21  ? 37.189  27.852  12.071  1.00 24.62 ? 21  PRO D CG  1 
ATOM   6530 C  CD  . PRO D 1 21  ? 35.805  27.356  11.936  1.00 17.78 ? 21  PRO D CD  1 
ATOM   6531 N  N   . ILE D 1 22  ? 36.953  26.383  15.534  1.00 13.67 ? 22  ILE D N   1 
ATOM   6532 C  CA  . ILE D 1 22  ? 37.218  26.257  17.000  1.00 14.10 ? 22  ILE D CA  1 
ATOM   6533 C  C   . ILE D 1 22  ? 36.828  24.855  17.472  1.00 12.04 ? 22  ILE D C   1 
ATOM   6534 O  O   . ILE D 1 22  ? 37.245  24.489  18.573  1.00 14.03 ? 22  ILE D O   1 
ATOM   6535 C  CB  . ILE D 1 22  ? 36.393  27.355  17.797  1.00 14.08 ? 22  ILE D CB  1 
ATOM   6536 C  CG1 . ILE D 1 22  ? 37.029  27.661  19.183  1.00 15.24 ? 22  ILE D CG1 1 
ATOM   6537 C  CG2 . ILE D 1 22  ? 34.900  26.972  17.858  1.00 14.65 ? 22  ILE D CG2 1 
ATOM   6538 C  CD1 . ILE D 1 22  ? 38.316  28.442  19.214  1.00 23.22 ? 22  ILE D CD1 1 
ATOM   6539 N  N   . ALA D 1 23  ? 36.082  24.033  16.657  1.00 12.81 ? 23  ALA D N   1 
ATOM   6540 C  CA  . ALA D 1 23  ? 35.893  22.640  17.000  1.00 12.43 ? 23  ALA D CA  1 
ATOM   6541 C  C   . ALA D 1 23  ? 37.167  21.934  17.358  1.00 12.41 ? 23  ALA D C   1 
ATOM   6542 O  O   . ALA D 1 23  ? 37.063  20.923  18.060  1.00 13.25 ? 23  ALA D O   1 
ATOM   6543 C  CB  . ALA D 1 23  ? 35.111  21.879  15.892  1.00 12.67 ? 23  ALA D CB  1 
ATOM   6544 N  N   . LYS D 1 24  ? 38.335  22.326  16.831  1.00 14.07 ? 24  LYS D N   1 
ATOM   6545 C  CA  . LYS D 1 24  ? 39.603  21.648  17.094  1.00 14.39 ? 24  LYS D CA  1 
ATOM   6546 C  C   . LYS D 1 24  ? 40.445  22.543  18.046  1.00 16.62 ? 24  LYS D C   1 
ATOM   6547 O  O   . LYS D 1 24  ? 41.702  22.413  18.075  1.00 18.71 ? 24  LYS D O   1 
ATOM   6548 C  CB  . LYS D 1 24  ? 40.389  21.459  15.768  1.00 16.74 ? 24  LYS D CB  1 
ATOM   6549 C  CG  . LYS D 1 24  ? 39.694  20.522  14.828  1.00 18.80 ? 24  LYS D CG  1 
ATOM   6550 C  CD  . LYS D 1 24  ? 40.575  20.304  13.582  1.00 25.50 ? 24  LYS D CD  1 
ATOM   6551 C  CE  . LYS D 1 24  ? 39.931  19.354  12.595  1.00 26.30 ? 24  LYS D CE  1 
ATOM   6552 N  NZ  . LYS D 1 24  ? 40.165  17.980  13.050  1.00 27.13 ? 24  LYS D NZ  1 
ATOM   6553 N  N   . GLY D 1 25  ? 39.753  23.403  18.846  1.00 15.67 ? 25  GLY D N   1 
ATOM   6554 C  CA  . GLY D 1 25  ? 40.418  24.336  19.783  1.00 16.89 ? 25  GLY D CA  1 
ATOM   6555 C  C   . GLY D 1 25  ? 40.948  23.659  21.033  1.00 15.86 ? 25  GLY D C   1 
ATOM   6556 O  O   . GLY D 1 25  ? 40.986  22.444  21.213  1.00 15.21 ? 25  GLY D O   1 
ATOM   6557 N  N   . GLU D 1 26  ? 41.439  24.532  21.877  1.00 15.63 ? 26  GLU D N   1 
ATOM   6558 C  CA  . GLU D 1 26  ? 42.128  24.148  23.070  1.00 15.14 ? 26  GLU D CA  1 
ATOM   6559 C  C   . GLU D 1 26  ? 41.256  23.913  24.309  1.00 13.29 ? 26  GLU D C   1 
ATOM   6560 O  O   . GLU D 1 26  ? 41.760  23.375  25.290  1.00 14.43 ? 26  GLU D O   1 
ATOM   6561 C  CB  . GLU D 1 26  ? 43.162  25.258  23.399  1.00 19.60 ? 26  GLU D CB  1 
ATOM   6562 C  CG  . GLU D 1 26  ? 44.229  25.460  22.306  1.00 24.73 ? 26  GLU D CG  1 
ATOM   6563 C  CD  . GLU D 1 26  ? 44.939  24.150  21.917  1.00 28.12 ? 26  GLU D CD  1 
ATOM   6564 O  OE1 . GLU D 1 26  ? 45.490  23.421  22.784  1.00 28.51 ? 26  GLU D OE1 1 
ATOM   6565 O  OE2 . GLU D 1 26  ? 44.934  23.831  20.709  1.00 37.09 ? 26  GLU D OE2 1 
ATOM   6566 N  N   . ARG D 1 27  ? 39.971  24.318  24.254  1.00 11.02 ? 27  ARG D N   1 
ATOM   6567 C  CA  . ARG D 1 27  ? 39.095  24.112  25.442  1.00 10.65 ? 27  ARG D CA  1 
ATOM   6568 C  C   . ARG D 1 27  ? 37.731  23.642  24.977  1.00 10.31 ? 27  ARG D C   1 
ATOM   6569 O  O   . ARG D 1 27  ? 36.727  24.264  25.321  1.00 10.89 ? 27  ARG D O   1 
ATOM   6570 C  CB  . ARG D 1 27  ? 39.033  25.366  26.324  1.00 13.21 ? 27  ARG D CB  1 
ATOM   6571 C  CG  . ARG D 1 27  ? 38.571  26.605  25.698  1.00 16.64 ? 27  ARG D CG  1 
ATOM   6572 C  CD  . ARG D 1 27  ? 38.477  27.798  26.686  1.00 22.86 ? 27  ARG D CD  1 
ATOM   6573 N  NE  . ARG D 1 27  ? 37.285  27.714  27.526  1.00 19.29 ? 27  ARG D NE  1 
ATOM   6574 C  CZ  . ARG D 1 27  ? 36.833  28.706  28.285  1.00 16.47 ? 27  ARG D CZ  1 
ATOM   6575 N  NH1 . ARG D 1 27  ? 37.473  29.868  28.314  1.00 16.81 ? 27  ARG D NH1 1 
ATOM   6576 N  NH2 . ARG D 1 27  ? 35.741  28.538  29.016  1.00 16.40 ? 27  ARG D NH2 1 
ATOM   6577 N  N   . GLN D 1 28  ? 37.748  22.531  24.187  1.00 9.62  ? 28  GLN D N   1 
ATOM   6578 C  CA  . GLN D 1 28  ? 36.435  22.052  23.690  1.00 9.84  ? 28  GLN D CA  1 
ATOM   6579 C  C   . GLN D 1 28  ? 35.783  21.072  24.692  1.00 8.70  ? 28  GLN D C   1 
ATOM   6580 O  O   . GLN D 1 28  ? 36.461  20.386  25.475  1.00 9.42  ? 28  GLN D O   1 
ATOM   6581 C  CB  . GLN D 1 28  ? 36.650  21.361  22.316  1.00 10.43 ? 28  GLN D CB  1 
ATOM   6582 C  CG  . GLN D 1 28  ? 36.984  22.402  21.264  1.00 11.12 ? 28  GLN D CG  1 
ATOM   6583 C  CD  . GLN D 1 28  ? 35.726  23.206  20.929  1.00 10.33 ? 28  GLN D CD  1 
ATOM   6584 O  OE1 . GLN D 1 28  ? 34.762  22.689  20.388  1.00 11.51 ? 28  GLN D OE1 1 
ATOM   6585 N  NE2 . GLN D 1 28  ? 35.735  24.539  21.290  1.00 9.94  ? 28  GLN D NE2 1 
ATOM   6586 N  N   . SER D 1 29  ? 34.451  21.001  24.583  1.00 8.22  ? 29  SER D N   1 
ATOM   6587 C  CA  . SER D 1 29  ? 33.652  20.131  25.446  1.00 8.31  ? 29  SER D CA  1 
ATOM   6588 C  C   . SER D 1 29  ? 32.781  19.221  24.565  1.00 9.01  ? 29  SER D C   1 
ATOM   6589 O  O   . SER D 1 29  ? 32.487  19.599  23.426  1.00 9.22  ? 29  SER D O   1 
ATOM   6590 C  CB  . SER D 1 29  ? 32.746  20.986  26.346  1.00 9.00  ? 29  SER D CB  1 
ATOM   6591 O  OG  . SER D 1 29  ? 33.546  21.735  27.263  1.00 8.85  ? 29  SER D OG  1 
ATOM   6592 N  N   . PRO D 1 30  ? 32.291  18.107  25.075  1.00 7.40  ? 30  PRO D N   1 
ATOM   6593 C  CA  . PRO D 1 30  ? 32.566  17.578  26.454  1.00 8.85  ? 30  PRO D CA  1 
ATOM   6594 C  C   . PRO D 1 30  ? 33.949  16.943  26.507  1.00 7.58  ? 30  PRO D C   1 
ATOM   6595 O  O   . PRO D 1 30  ? 34.678  16.879  25.502  1.00 7.91  ? 30  PRO D O   1 
ATOM   6596 C  CB  . PRO D 1 30  ? 31.432  16.558  26.616  1.00 8.26  ? 30  PRO D CB  1 
ATOM   6597 C  CG  . PRO D 1 30  ? 31.320  16.002  25.171  1.00 9.77  ? 30  PRO D CG  1 
ATOM   6598 C  CD  . PRO D 1 30  ? 31.430  17.201  24.247  1.00 8.12  ? 30  PRO D CD  1 
ATOM   6599 N  N   . VAL D 1 31  ? 34.228  16.344  27.656  1.00 7.55  ? 31  VAL D N   1 
ATOM   6600 C  CA  . VAL D 1 31  ? 35.459  15.599  27.920  1.00 8.38  ? 31  VAL D CA  1 
ATOM   6601 C  C   . VAL D 1 31  ? 35.139  14.383  28.722  1.00 8.38  ? 31  VAL D C   1 
ATOM   6602 O  O   . VAL D 1 31  ? 34.054  14.321  29.379  1.00 8.95  ? 31  VAL D O   1 
ATOM   6603 C  CB  . VAL D 1 31  ? 36.534  16.450  28.659  1.00 7.68  ? 31  VAL D CB  1 
ATOM   6604 C  CG1 . VAL D 1 31  ? 36.944  17.639  27.840  1.00 9.72  ? 31  VAL D CG1 1 
ATOM   6605 C  CG2 . VAL D 1 31  ? 36.112  16.844  30.039  1.00 8.82  ? 31  VAL D CG2 1 
ATOM   6606 N  N   . ASP D 1 32  ? 36.015  13.381  28.712  1.00 9.24  ? 32  ASP D N   1 
ATOM   6607 C  CA  . ASP D 1 32  ? 35.989  12.285  29.683  1.00 8.85  ? 32  ASP D CA  1 
ATOM   6608 C  C   . ASP D 1 32  ? 36.515  12.827  31.012  1.00 8.81  ? 32  ASP D C   1 
ATOM   6609 O  O   . ASP D 1 32  ? 37.602  13.441  31.079  1.00 10.41 ? 32  ASP D O   1 
ATOM   6610 C  CB  . ASP D 1 32  ? 36.820  11.128  29.190  1.00 11.14 ? 32  ASP D CB  1 
ATOM   6611 C  CG  . ASP D 1 32  ? 36.777  9.963   30.166  1.00 11.37 ? 32  ASP D CG  1 
ATOM   6612 O  OD1 . ASP D 1 32  ? 35.660  9.516   30.552  1.00 9.71  ? 32  ASP D OD1 1 
ATOM   6613 O  OD2 . ASP D 1 32  ? 37.890  9.536   30.634  1.00 14.62 ? 32  ASP D OD2 1 
ATOM   6614 N  N   . ILE D 1 33  ? 35.809  12.557  32.086  1.00 8.58  ? 33  ILE D N   1 
ATOM   6615 C  CA  . ILE D 1 33  ? 36.226  12.946  33.446  1.00 9.99  ? 33  ILE D CA  1 
ATOM   6616 C  C   . ILE D 1 33  ? 36.907  11.684  33.994  1.00 10.70 ? 33  ILE D C   1 
ATOM   6617 O  O   . ILE D 1 33  ? 36.269  10.680  34.377  1.00 11.47 ? 33  ILE D O   1 
ATOM   6618 C  CB  . ILE D 1 33  ? 35.023  13.366  34.283  1.00 10.09 ? 33  ILE D CB  1 
ATOM   6619 C  CG1 . ILE D 1 33  ? 34.374  14.627  33.632  1.00 9.83  ? 33  ILE D CG1 1 
ATOM   6620 C  CG2 . ILE D 1 33  ? 35.482  13.669  35.727  1.00 11.00 ? 33  ILE D CG2 1 
ATOM   6621 C  CD1 . ILE D 1 33  ? 32.978  14.895  34.250  1.00 12.07 ? 33  ILE D CD1 1 
ATOM   6622 N  N   . ASP D 1 34  ? 38.234  11.767  34.103  1.00 10.63 ? 34  ASP D N   1 
ATOM   6623 C  CA  . ASP D 1 34  ? 39.034  10.689  34.698  1.00 12.87 ? 34  ASP D CA  1 
ATOM   6624 C  C   . ASP D 1 34  ? 39.000  10.948  36.221  1.00 11.11 ? 34  ASP D C   1 
ATOM   6625 O  O   . ASP D 1 34  ? 39.666  11.937  36.684  1.00 13.81 ? 34  ASP D O   1 
ATOM   6626 C  CB  . ASP D 1 34  ? 40.433  10.673  34.005  1.00 14.95 ? 34  ASP D CB  1 
ATOM   6627 C  CG  . ASP D 1 34  ? 41.429  9.696   34.675  1.00 19.57 ? 34  ASP D CG  1 
ATOM   6628 O  OD1 . ASP D 1 34  ? 41.345  9.384   35.846  1.00 20.38 ? 34  ASP D OD1 1 
ATOM   6629 O  OD2 . ASP D 1 34  ? 42.352  9.252   33.978  1.00 31.75 ? 34  ASP D OD2 1 
ATOM   6630 N  N   . THR D 1 35  ? 38.240  10.209  36.946  1.00 11.44 ? 35  THR D N   1 
ATOM   6631 C  CA  . THR D 1 35  ? 37.974  10.537  38.348  1.00 12.60 ? 35  THR D CA  1 
ATOM   6632 C  C   . THR D 1 35  ? 39.182  10.438  39.224  1.00 13.01 ? 35  THR D C   1 
ATOM   6633 O  O   . THR D 1 35  ? 39.237  11.111  40.270  1.00 16.19 ? 35  THR D O   1 
ATOM   6634 C  CB  . THR D 1 35  ? 36.899  9.639   38.883  1.00 12.91 ? 35  THR D CB  1 
ATOM   6635 O  OG1 . THR D 1 35  ? 37.376  8.296   38.979  1.00 15.96 ? 35  THR D OG1 1 
ATOM   6636 C  CG2 . THR D 1 35  ? 35.571  9.760   38.040  1.00 15.54 ? 35  THR D CG2 1 
ATOM   6637 N  N   . HIS D 1 36  ? 40.117  9.550   38.872  1.00 14.59 ? 36  HIS D N   1 
ATOM   6638 C  CA  . HIS D 1 36  ? 41.358  9.378   39.597  1.00 14.81 ? 36  HIS D CA  1 
ATOM   6639 C  C   . HIS D 1 36  ? 42.281  10.533  39.407  1.00 16.35 ? 36  HIS D C   1 
ATOM   6640 O  O   . HIS D 1 36  ? 43.044  10.877  40.395  1.00 17.35 ? 36  HIS D O   1 
ATOM   6641 C  CB  . HIS D 1 36  ? 41.901  7.970   39.233  1.00 17.88 ? 36  HIS D CB  1 
ATOM   6642 C  CG  . HIS D 1 36  ? 41.107  6.886   39.914  1.00 17.31 ? 36  HIS D CG  1 
ATOM   6643 N  ND1 . HIS D 1 36  ? 41.036  6.846   41.294  1.00 21.36 ? 36  HIS D ND1 1 
ATOM   6644 C  CD2 . HIS D 1 36  ? 40.196  5.924   39.433  1.00 16.57 ? 36  HIS D CD2 1 
ATOM   6645 C  CE1 . HIS D 1 36  ? 40.220  5.831   41.673  1.00 26.86 ? 36  HIS D CE1 1 
ATOM   6646 N  NE2 . HIS D 1 36  ? 39.707  5.271   40.538  1.00 23.28 ? 36  HIS D NE2 1 
ATOM   6647 N  N   A THR D 1 37  ? 42.357  11.149  38.214  0.50 16.94 ? 37  THR D N   1 
ATOM   6648 N  N   B THR D 1 37  ? 42.256  11.151  38.230  0.50 17.31 ? 37  THR D N   1 
ATOM   6649 C  CA  A THR D 1 37  ? 43.224  12.309  37.992  0.50 18.29 ? 37  THR D CA  1 
ATOM   6650 C  CA  B THR D 1 37  ? 43.117  12.243  37.897  0.50 16.89 ? 37  THR D CA  1 
ATOM   6651 C  C   A THR D 1 37  ? 42.576  13.715  38.099  0.50 15.17 ? 37  THR D C   1 
ATOM   6652 C  C   B THR D 1 37  ? 42.604  13.616  38.375  0.50 13.90 ? 37  THR D C   1 
ATOM   6653 O  O   A THR D 1 37  ? 43.289  14.760  37.851  0.50 18.50 ? 37  THR D O   1 
ATOM   6654 O  O   B THR D 1 37  ? 43.413  14.527  38.665  0.50 12.36 ? 37  THR D O   1 
ATOM   6655 C  CB  A THR D 1 37  ? 43.988  12.225  36.658  0.50 18.31 ? 37  THR D CB  1 
ATOM   6656 C  CB  B THR D 1 37  ? 43.397  12.230  36.390  0.50 17.39 ? 37  THR D CB  1 
ATOM   6657 O  OG1 A THR D 1 37  ? 43.048  12.299  35.593  0.50 18.53 ? 37  THR D OG1 1 
ATOM   6658 O  OG1 B THR D 1 37  ? 43.988  10.984  36.049  0.50 20.06 ? 37  THR D OG1 1 
ATOM   6659 C  CG2 A THR D 1 37  ? 44.683  10.927  36.527  0.50 20.10 ? 37  THR D CG2 1 
ATOM   6660 C  CG2 B THR D 1 37  ? 44.338  13.381  35.982  0.50 16.59 ? 37  THR D CG2 1 
ATOM   6661 N  N   . ALA D 1 38  ? 41.287  13.737  38.491  1.00 13.29 ? 38  ALA D N   1 
ATOM   6662 C  CA  . ALA D 1 38  ? 40.674  14.974  38.925  1.00 12.81 ? 38  ALA D CA  1 
ATOM   6663 C  C   . ALA D 1 38  ? 41.243  15.311  40.276  1.00 15.55 ? 38  ALA D C   1 
ATOM   6664 O  O   . ALA D 1 38  ? 41.420  14.495  41.147  1.00 20.84 ? 38  ALA D O   1 
ATOM   6665 C  CB  . ALA D 1 38  ? 39.186  14.882  38.940  1.00 14.22 ? 38  ALA D CB  1 
ATOM   6666 N  N   . LYS D 1 39  ? 41.603  16.576  40.413  1.00 15.51 ? 39  LYS D N   1 
ATOM   6667 C  CA  . LYS D 1 39  ? 42.248  17.077  41.641  1.00 17.75 ? 39  LYS D CA  1 
ATOM   6668 C  C   . LYS D 1 39  ? 41.186  17.601  42.669  1.00 14.06 ? 39  LYS D C   1 
ATOM   6669 O  O   . LYS D 1 39  ? 40.516  18.593  42.349  1.00 14.04 ? 39  LYS D O   1 
ATOM   6670 C  CB  . LYS D 1 39  ? 43.132  18.248  41.117  1.00 18.04 ? 39  LYS D CB  1 
ATOM   6671 C  CG  . LYS D 1 39  ? 43.849  19.106  42.159  1.00 22.90 ? 39  LYS D CG  1 
ATOM   6672 C  CD  . LYS D 1 39  ? 45.037  18.381  42.866  1.00 20.93 ? 39  LYS D CD  1 
ATOM   6673 C  CE  . LYS D 1 39  ? 45.673  19.243  43.922  1.00 30.16 ? 39  LYS D CE  1 
ATOM   6674 N  NZ  . LYS D 1 39  ? 46.596  18.402  44.732  1.00 28.96 ? 39  LYS D NZ  1 
ATOM   6675 N  N   . TYR D 1 40  ? 41.107  17.040  43.879  1.00 15.33 ? 40  TYR D N   1 
ATOM   6676 C  CA  . TYR D 1 40  ? 40.298  17.661  44.912  1.00 15.10 ? 40  TYR D CA  1 
ATOM   6677 C  C   . TYR D 1 40  ? 40.846  19.084  45.205  1.00 13.82 ? 40  TYR D C   1 
ATOM   6678 O  O   . TYR D 1 40  ? 42.067  19.272  45.484  1.00 15.54 ? 40  TYR D O   1 
ATOM   6679 C  CB  . TYR D 1 40  ? 40.235  16.793  46.176  1.00 18.27 ? 40  TYR D CB  1 
ATOM   6680 C  CG  . TYR D 1 40  ? 39.688  17.495  47.377  1.00 20.28 ? 40  TYR D CG  1 
ATOM   6681 C  CD1 . TYR D 1 40  ? 38.387  17.983  47.360  1.00 18.28 ? 40  TYR D CD1 1 
ATOM   6682 C  CD2 . TYR D 1 40  ? 40.448  17.641  48.574  1.00 24.38 ? 40  TYR D CD2 1 
ATOM   6683 C  CE1 . TYR D 1 40  ? 37.820  18.575  48.422  1.00 24.23 ? 40  TYR D CE1 1 
ATOM   6684 C  CE2 . TYR D 1 40  ? 39.867  18.313  49.659  1.00 25.97 ? 40  TYR D CE2 1 
ATOM   6685 C  CZ  . TYR D 1 40  ? 38.582  18.744  49.568  1.00 24.19 ? 40  TYR D CZ  1 
ATOM   6686 O  OH  . TYR D 1 40  ? 38.017  19.396  50.620  1.00 26.61 ? 40  TYR D OH  1 
ATOM   6687 N  N   . ASP D 1 41  ? 40.006  20.075  45.131  1.00 14.20 ? 41  ASP D N   1 
ATOM   6688 C  CA  . ASP D 1 41  ? 40.420  21.464  45.412  1.00 14.22 ? 41  ASP D CA  1 
ATOM   6689 C  C   . ASP D 1 41  ? 39.696  21.937  46.645  1.00 18.82 ? 41  ASP D C   1 
ATOM   6690 O  O   . ASP D 1 41  ? 38.529  22.332  46.522  1.00 19.99 ? 41  ASP D O   1 
ATOM   6691 C  CB  . ASP D 1 41  ? 40.094  22.390  44.245  1.00 16.80 ? 41  ASP D CB  1 
ATOM   6692 C  CG  . ASP D 1 41  ? 40.655  23.736  44.392  1.00 25.13 ? 41  ASP D CG  1 
ATOM   6693 O  OD1 . ASP D 1 41  ? 41.134  24.082  45.505  1.00 22.94 ? 41  ASP D OD1 1 
ATOM   6694 O  OD2 . ASP D 1 41  ? 40.630  24.433  43.345  1.00 27.02 ? 41  ASP D OD2 1 
ATOM   6695 N  N   . PRO D 1 42  ? 40.402  21.963  47.805  1.00 20.29 ? 42  PRO D N   1 
ATOM   6696 C  CA  . PRO D 1 42  ? 39.722  22.420  49.028  1.00 21.91 ? 42  PRO D CA  1 
ATOM   6697 C  C   . PRO D 1 42  ? 39.365  23.905  48.978  1.00 21.81 ? 42  PRO D C   1 
ATOM   6698 O  O   . PRO D 1 42  ? 38.555  24.363  49.822  1.00 26.78 ? 42  PRO D O   1 
ATOM   6699 C  CB  . PRO D 1 42  ? 40.767  22.134  50.135  1.00 31.24 ? 42  PRO D CB  1 
ATOM   6700 C  CG  . PRO D 1 42  ? 42.105  22.184  49.398  1.00 31.12 ? 42  PRO D CG  1 
ATOM   6701 C  CD  . PRO D 1 42  ? 41.778  21.473  48.091  1.00 21.95 ? 42  PRO D CD  1 
ATOM   6702 N  N   . SER D 1 43  ? 39.942  24.689  48.037  1.00 21.38 ? 43  SER D N   1 
ATOM   6703 C  CA  . SER D 1 43  ? 39.524  26.108  47.880  1.00 25.00 ? 43  SER D CA  1 
ATOM   6704 C  C   . SER D 1 43  ? 38.149  26.301  47.105  1.00 25.07 ? 43  SER D C   1 
ATOM   6705 O  O   . SER D 1 43  ? 37.626  27.436  47.034  1.00 29.05 ? 43  SER D O   1 
ATOM   6706 C  CB  . SER D 1 43  ? 40.591  26.945  47.157  1.00 28.67 ? 43  SER D CB  1 
ATOM   6707 O  OG  . SER D 1 43  ? 40.560  26.731  45.759  1.00 28.92 ? 43  SER D OG  1 
ATOM   6708 N  N   . LEU D 1 44  ? 37.616  25.237  46.497  1.00 18.86 ? 44  LEU D N   1 
ATOM   6709 C  CA  . LEU D 1 44  ? 36.273  25.285  45.813  1.00 19.26 ? 44  LEU D CA  1 
ATOM   6710 C  C   . LEU D 1 44  ? 35.193  25.476  46.862  1.00 22.45 ? 44  LEU D C   1 
ATOM   6711 O  O   . LEU D 1 44  ? 35.300  24.979  47.977  1.00 28.17 ? 44  LEU D O   1 
ATOM   6712 C  CB  . LEU D 1 44  ? 36.013  24.001  44.994  1.00 17.72 ? 44  LEU D CB  1 
ATOM   6713 C  CG  . LEU D 1 44  ? 36.767  23.969  43.686  1.00 15.73 ? 44  LEU D CG  1 
ATOM   6714 C  CD1 . LEU D 1 44  ? 36.635  22.571  43.090  1.00 21.29 ? 44  LEU D CD1 1 
ATOM   6715 C  CD2 . LEU D 1 44  ? 36.359  25.101  42.728  1.00 18.30 ? 44  LEU D CD2 1 
ATOM   6716 N  N   . LYS D 1 45  ? 34.213  26.314  46.533  1.00 21.79 ? 45  LYS D N   1 
ATOM   6717 C  CA  . LYS D 1 45  ? 33.082  26.511  47.436  1.00 20.42 ? 45  LYS D CA  1 
ATOM   6718 C  C   . LYS D 1 45  ? 31.924  25.618  47.089  1.00 18.99 ? 45  LYS D C   1 
ATOM   6719 O  O   . LYS D 1 45  ? 31.882  25.029  45.995  1.00 19.49 ? 45  LYS D O   1 
ATOM   6720 C  CB  . LYS D 1 45  ? 32.656  27.907  47.323  1.00 23.24 ? 45  LYS D CB  1 
ATOM   6721 C  CG  . LYS D 1 45  ? 33.728  28.891  47.645  1.00 28.20 ? 45  LYS D CG  1 
ATOM   6722 C  CD  . LYS D 1 45  ? 33.128  30.271  47.521  1.00 44.07 ? 45  LYS D CD  1 
ATOM   6723 N  N   . PRO D 1 46  ? 31.047  25.337  48.073  1.00 17.80 ? 46  PRO D N   1 
ATOM   6724 C  CA  . PRO D 1 46  ? 29.817  24.640  47.666  1.00 17.36 ? 46  PRO D CA  1 
ATOM   6725 C  C   . PRO D 1 46  ? 29.148  25.413  46.593  1.00 14.84 ? 46  PRO D C   1 
ATOM   6726 O  O   . PRO D 1 46  ? 29.243  26.644  46.565  1.00 16.24 ? 46  PRO D O   1 
ATOM   6727 C  CB  . PRO D 1 46  ? 28.939  24.635  48.959  1.00 19.48 ? 46  PRO D CB  1 
ATOM   6728 C  CG  . PRO D 1 46  ? 29.907  24.837  50.081  1.00 22.51 ? 46  PRO D CG  1 
ATOM   6729 C  CD  . PRO D 1 46  ? 31.082  25.666  49.520  1.00 18.99 ? 46  PRO D CD  1 
ATOM   6730 N  N   . LEU D 1 47  ? 28.492  24.680  45.680  1.00 17.28 ? 47  LEU D N   1 
ATOM   6731 C  CA  . LEU D 1 47  ? 27.761  25.347  44.672  1.00 16.72 ? 47  LEU D CA  1 
ATOM   6732 C  C   . LEU D 1 47  ? 26.477  25.931  45.304  1.00 17.85 ? 47  LEU D C   1 
ATOM   6733 O  O   . LEU D 1 47  ? 25.815  25.239  46.107  1.00 21.29 ? 47  LEU D O   1 
ATOM   6734 C  CB  . LEU D 1 47  ? 27.458  24.289  43.638  1.00 22.43 ? 47  LEU D CB  1 
ATOM   6735 C  CG  . LEU D 1 47  ? 26.776  24.677  42.372  1.00 20.46 ? 47  LEU D CG  1 
ATOM   6736 C  CD1 . LEU D 1 47  ? 27.709  25.635  41.598  1.00 22.47 ? 47  LEU D CD1 1 
ATOM   6737 C  CD2 . LEU D 1 47  ? 26.502  23.377  41.592  1.00 23.13 ? 47  LEU D CD2 1 
ATOM   6738 N  N   . SER D 1 48  ? 26.085  27.120  44.914  1.00 14.88 ? 48  SER D N   1 
ATOM   6739 C  CA  . SER D 1 48  ? 24.826  27.735  45.356  1.00 15.08 ? 48  SER D CA  1 
ATOM   6740 C  C   . SER D 1 48  ? 23.839  27.737  44.152  1.00 13.86 ? 48  SER D C   1 
ATOM   6741 O  O   . SER D 1 48  ? 24.060  28.443  43.170  1.00 14.80 ? 48  SER D O   1 
ATOM   6742 C  CB  . SER D 1 48  ? 25.141  29.170  45.800  1.00 18.44 ? 48  SER D CB  1 
ATOM   6743 O  OG  . SER D 1 48  ? 23.995  29.958  46.020  1.00 20.09 ? 48  SER D OG  1 
ATOM   6744 N  N   . VAL D 1 49  ? 22.806  26.929  44.182  1.00 15.19 ? 49  VAL D N   1 
ATOM   6745 C  CA  . VAL D 1 49  ? 21.766  26.889  43.213  1.00 16.60 ? 49  VAL D CA  1 
ATOM   6746 C  C   . VAL D 1 49  ? 20.503  27.501  43.801  1.00 18.07 ? 49  VAL D C   1 
ATOM   6747 O  O   . VAL D 1 49  ? 19.915  26.887  44.686  1.00 21.97 ? 49  VAL D O   1 
ATOM   6748 C  CB  . VAL D 1 49  ? 21.491  25.415  42.842  1.00 19.00 ? 49  VAL D CB  1 
ATOM   6749 C  CG1 . VAL D 1 49  ? 20.617  25.344  41.605  1.00 24.76 ? 49  VAL D CG1 1 
ATOM   6750 C  CG2 . VAL D 1 49  ? 22.778  24.705  42.521  1.00 21.80 ? 49  VAL D CG2 1 
ATOM   6751 N  N   . SER D 1 50  ? 20.060  28.645  43.304  1.00 17.39 ? 50  SER D N   1 
ATOM   6752 C  CA  . SER D 1 50  ? 18.862  29.321  43.875  1.00 18.49 ? 50  SER D CA  1 
ATOM   6753 C  C   . SER D 1 50  ? 17.852  29.417  42.820  1.00 18.62 ? 50  SER D C   1 
ATOM   6754 O  O   . SER D 1 50  ? 17.823  30.385  42.081  1.00 20.60 ? 50  SER D O   1 
ATOM   6755 C  CB  . SER D 1 50  ? 19.231  30.717  44.454  1.00 24.30 ? 50  SER D CB  1 
ATOM   6756 O  OG  . SER D 1 50  ? 20.325  30.555  45.373  1.00 29.58 ? 50  SER D OG  1 
ATOM   6757 N  N   . TYR D 1 51  ? 17.000  28.395  42.760  1.00 16.55 ? 51  TYR D N   1 
ATOM   6758 C  CA  . TYR D 1 51  ? 15.974  28.225  41.731  1.00 17.23 ? 51  TYR D CA  1 
ATOM   6759 C  C   . TYR D 1 51  ? 14.515  28.462  42.231  1.00 16.56 ? 51  TYR D C   1 
ATOM   6760 O  O   . TYR D 1 51  ? 13.571  28.277  41.442  1.00 21.09 ? 51  TYR D O   1 
ATOM   6761 C  CB  . TYR D 1 51  ? 16.063  26.847  41.090  1.00 18.11 ? 51  TYR D CB  1 
ATOM   6762 C  CG  . TYR D 1 51  ? 17.208  26.590  40.144  1.00 14.23 ? 51  TYR D CG  1 
ATOM   6763 C  CD1 . TYR D 1 51  ? 18.040  27.604  39.661  1.00 14.53 ? 51  TYR D CD1 1 
ATOM   6764 C  CD2 . TYR D 1 51  ? 17.452  25.289  39.734  1.00 15.20 ? 51  TYR D CD2 1 
ATOM   6765 C  CE1 . TYR D 1 51  ? 19.151  27.311  38.816  1.00 12.82 ? 51  TYR D CE1 1 
ATOM   6766 C  CE2 . TYR D 1 51  ? 18.508  24.989  38.875  1.00 14.06 ? 51  TYR D CE2 1 
ATOM   6767 C  CZ  . TYR D 1 51  ? 19.354  26.007  38.404  1.00 11.78 ? 51  TYR D CZ  1 
ATOM   6768 O  OH  . TYR D 1 51  ? 20.342  25.652  37.529  1.00 13.65 ? 51  TYR D OH  1 
ATOM   6769 N  N   . ASP D 1 52  ? 14.354  28.891  43.496  1.00 18.25 ? 52  ASP D N   1 
ATOM   6770 C  CA  . ASP D 1 52  ? 13.012  29.107  44.039  1.00 24.31 ? 52  ASP D CA  1 
ATOM   6771 C  C   . ASP D 1 52  ? 12.117  30.051  43.242  1.00 24.79 ? 52  ASP D C   1 
ATOM   6772 O  O   . ASP D 1 52  ? 10.888  29.813  43.144  1.00 29.09 ? 52  ASP D O   1 
ATOM   6773 C  CB  . ASP D 1 52  ? 13.079  29.488  45.510  1.00 23.74 ? 52  ASP D CB  1 
ATOM   6774 C  CG  . ASP D 1 52  ? 14.116  30.529  45.778  1.00 40.77 ? 52  ASP D CG  1 
ATOM   6775 O  OD1 . ASP D 1 52  ? 15.332  30.222  45.609  1.00 54.94 ? 52  ASP D OD1 1 
ATOM   6776 O  OD2 . ASP D 1 52  ? 13.719  31.652  46.159  1.00 59.50 ? 52  ASP D OD2 1 
ATOM   6777 N  N   . GLN D 1 53  ? 12.701  31.046  42.603  1.00 20.91 ? 53  GLN D N   1 
ATOM   6778 C  CA  . GLN D 1 53  ? 11.802  31.996  41.860  1.00 21.06 ? 53  GLN D CA  1 
ATOM   6779 C  C   . GLN D 1 53  ? 11.859  31.832  40.352  1.00 16.94 ? 53  GLN D C   1 
ATOM   6780 O  O   . GLN D 1 53  ? 11.517  32.747  39.615  1.00 20.81 ? 53  GLN D O   1 
ATOM   6781 C  CB  . GLN D 1 53  ? 12.247  33.439  42.178  1.00 24.46 ? 53  GLN D CB  1 
ATOM   6782 C  CG  . GLN D 1 53  ? 12.152  33.805  43.641  1.00 30.24 ? 53  GLN D CG  1 
ATOM   6783 C  CD  . GLN D 1 53  ? 10.693  33.962  44.045  1.00 43.20 ? 53  GLN D CD  1 
ATOM   6784 O  OE1 . GLN D 1 53  ? 9.974   34.809  43.494  1.00 52.91 ? 53  GLN D OE1 1 
ATOM   6785 N  NE2 . GLN D 1 53  ? 10.238  33.131  44.985  1.00 60.93 ? 53  GLN D NE2 1 
ATOM   6786 N  N   . ALA D 1 54  ? 12.366  30.684  39.891  1.00 15.61 ? 54  ALA D N   1 
ATOM   6787 C  CA  . ALA D 1 54  ? 12.542  30.517  38.449  1.00 14.93 ? 54  ALA D CA  1 
ATOM   6788 C  C   . ALA D 1 54  ? 11.191  30.615  37.757  1.00 15.36 ? 54  ALA D C   1 
ATOM   6789 O  O   . ALA D 1 54  ? 10.183  30.060  38.246  1.00 20.58 ? 54  ALA D O   1 
ATOM   6790 C  CB  . ALA D 1 54  ? 13.162  29.110  38.124  1.00 15.95 ? 54  ALA D CB  1 
ATOM   6791 N  N   . THR D 1 55  ? 11.182  31.225  36.565  1.00 12.95 ? 55  THR D N   1 
ATOM   6792 C  CA  . THR D 1 55  ? 9.926   31.394  35.778  1.00 14.55 ? 55  THR D CA  1 
ATOM   6793 C  C   . THR D 1 55  ? 10.142  30.862  34.382  1.00 12.15 ? 55  THR D C   1 
ATOM   6794 O  O   . THR D 1 55  ? 10.765  31.525  33.575  1.00 13.83 ? 55  THR D O   1 
ATOM   6795 C  CB  . THR D 1 55  ? 9.637   32.929  35.501  1.00 21.92 ? 55  THR D CB  1 
ATOM   6796 O  OG1 . THR D 1 55  ? 9.426   33.574  36.677  1.00 27.18 ? 55  THR D OG1 1 
ATOM   6797 C  CG2 . THR D 1 55  ? 8.361   33.109  34.738  1.00 23.73 ? 55  THR D CG2 1 
ATOM   6798 N  N   . SER D 1 56  ? 9.629   29.648  34.081  1.00 12.87 ? 56  SER D N   1 
ATOM   6799 C  CA  . SER D 1 56  ? 9.803   29.091  32.719  1.00 11.93 ? 56  SER D CA  1 
ATOM   6800 C  C   . SER D 1 56  ? 8.798   29.771  31.796  1.00 10.56 ? 56  SER D C   1 
ATOM   6801 O  O   . SER D 1 56  ? 7.729   30.261  32.253  1.00 13.70 ? 56  SER D O   1 
ATOM   6802 C  CB  . SER D 1 56  ? 9.574   27.603  32.727  1.00 11.86 ? 56  SER D CB  1 
ATOM   6803 O  OG  . SER D 1 56  ? 8.243   27.206  33.164  1.00 12.24 ? 56  SER D OG  1 
ATOM   6804 N  N   . LEU D 1 57  ? 9.101   29.873  30.504  1.00 12.08 ? 57  LEU D N   1 
ATOM   6805 C  CA  . LEU D 1 57  ? 8.212   30.568  29.520  1.00 13.74 ? 57  LEU D CA  1 
ATOM   6806 C  C   . LEU D 1 57  ? 7.699   29.601  28.467  1.00 12.95 ? 57  LEU D C   1 
ATOM   6807 O  O   . LEU D 1 57  ? 6.460   29.507  28.237  1.00 14.57 ? 57  LEU D O   1 
ATOM   6808 C  CB  . LEU D 1 57  ? 8.950   31.704  28.807  1.00 15.89 ? 57  LEU D CB  1 
ATOM   6809 C  CG  . LEU D 1 57  ? 9.244   32.871  29.784  1.00 16.17 ? 57  LEU D CG  1 
ATOM   6810 C  CD1 . LEU D 1 57  ? 10.146  33.816  28.958  1.00 18.57 ? 57  LEU D CD1 1 
ATOM   6811 C  CD2 . LEU D 1 57  ? 7.916   33.517  30.315  1.00 25.94 ? 57  LEU D CD2 1 
ATOM   6812 N  N   A ARG D 1 58  ? 8.539   28.803  27.833  0.50 14.58 ? 58  ARG D N   1 
ATOM   6813 N  N   B ARG D 1 58  ? 8.652   28.990  27.744  0.50 12.49 ? 58  ARG D N   1 
ATOM   6814 C  CA  A ARG D 1 58  ? 8.007   27.962  26.763  0.50 12.16 ? 58  ARG D CA  1 
ATOM   6815 C  CA  B ARG D 1 58  ? 8.320   28.264  26.494  0.50 11.27 ? 58  ARG D CA  1 
ATOM   6816 C  C   A ARG D 1 58  ? 8.972   26.808  26.638  0.50 13.19 ? 58  ARG D C   1 
ATOM   6817 C  C   B ARG D 1 58  ? 9.187   27.016  26.295  0.50 8.92  ? 58  ARG D C   1 
ATOM   6818 O  O   A ARG D 1 58  ? 9.990   26.740  27.391  0.50 13.54 ? 58  ARG D O   1 
ATOM   6819 O  O   B ARG D 1 58  ? 10.322  27.009  26.766  0.50 8.05  ? 58  ARG D O   1 
ATOM   6820 C  CB  A ARG D 1 58  ? 8.120   28.723  25.393  0.50 14.88 ? 58  ARG D CB  1 
ATOM   6821 C  CB  B ARG D 1 58  ? 8.497   29.199  25.230  0.50 9.67  ? 58  ARG D CB  1 
ATOM   6822 C  CG  A ARG D 1 58  ? 7.173   29.839  25.058  0.50 18.33 ? 58  ARG D CG  1 
ATOM   6823 C  CG  B ARG D 1 58  ? 7.420   30.288  25.179  0.50 10.07 ? 58  ARG D CG  1 
ATOM   6824 C  CD  A ARG D 1 58  ? 7.555   30.126  23.625  0.50 20.99 ? 58  ARG D CD  1 
ATOM   6825 C  CD  B ARG D 1 58  ? 7.252   30.972  23.809  0.50 9.03  ? 58  ARG D CD  1 
ATOM   6826 N  NE  A ARG D 1 58  ? 9.011   30.141  23.484  0.50 23.05 ? 58  ARG D NE  1 
ATOM   6827 N  NE  B ARG D 1 58  ? 6.752   30.033  22.819  0.50 10.07 ? 58  ARG D NE  1 
ATOM   6828 C  CZ  A ARG D 1 58  ? 9.674   29.560  22.486  0.50 17.59 ? 58  ARG D CZ  1 
ATOM   6829 C  CZ  B ARG D 1 58  ? 5.466   29.732  22.706  0.50 11.60 ? 58  ARG D CZ  1 
ATOM   6830 N  NH1 A ARG D 1 58  ? 9.000   28.932  21.531  0.50 22.61 ? 58  ARG D NH1 1 
ATOM   6831 N  NH1 B ARG D 1 58  ? 4.609   30.316  23.531  0.50 13.93 ? 58  ARG D NH1 1 
ATOM   6832 N  NH2 A ARG D 1 58  ? 10.999  29.614  22.437  0.50 25.05 ? 58  ARG D NH2 1 
ATOM   6833 N  NH2 B ARG D 1 58  ? 5.038   28.868  21.796  0.50 10.84 ? 58  ARG D NH2 1 
ATOM   6834 N  N   . ILE D 1 59  ? 8.640   25.939  25.666  1.00 12.80 ? 59  ILE D N   1 
ATOM   6835 C  CA  . ILE D 1 59  ? 9.432   24.782  25.268  1.00 12.63 ? 59  ILE D CA  1 
ATOM   6836 C  C   . ILE D 1 59  ? 9.464   24.683  23.753  1.00 13.72 ? 59  ILE D C   1 
ATOM   6837 O  O   . ILE D 1 59  ? 8.390   24.899  23.132  1.00 13.72 ? 59  ILE D O   1 
ATOM   6838 C  CB  . ILE D 1 59  ? 8.942   23.493  25.938  1.00 13.49 ? 59  ILE D CB  1 
ATOM   6839 C  CG1 . ILE D 1 59  ? 9.930   22.327  25.706  1.00 13.67 ? 59  ILE D CG1 1 
ATOM   6840 C  CG2 . ILE D 1 59  ? 7.472   23.108  25.498  1.00 13.09 ? 59  ILE D CG2 1 
ATOM   6841 C  CD1 . ILE D 1 59  ? 9.572   21.090  26.501  1.00 14.54 ? 59  ILE D CD1 1 
ATOM   6842 N  N   . LEU D 1 60  ? 10.599  24.433  23.089  1.00 11.74 ? 60  LEU D N   1 
ATOM   6843 C  CA  . LEU D 1 60  ? 10.739  24.467  21.677  1.00 13.73 ? 60  LEU D CA  1 
ATOM   6844 C  C   . LEU D 1 60  ? 11.499  23.201  21.252  1.00 11.88 ? 60  LEU D C   1 
ATOM   6845 O  O   . LEU D 1 60  ? 12.541  22.855  21.860  1.00 13.95 ? 60  LEU D O   1 
ATOM   6846 C  CB  . LEU D 1 60  ? 11.604  25.726  21.295  1.00 14.64 ? 60  LEU D CB  1 
ATOM   6847 C  CG  . LEU D 1 60  ? 12.170  25.780  19.917  1.00 19.20 ? 60  LEU D CG  1 
ATOM   6848 C  CD1 . LEU D 1 60  ? 10.978  26.000  19.020  1.00 22.21 ? 60  LEU D CD1 1 
ATOM   6849 C  CD2 . LEU D 1 60  ? 13.118  26.996  19.912  1.00 22.71 ? 60  LEU D CD2 1 
ATOM   6850 N  N   . ASN D 1 61  ? 11.111  22.560  20.172  1.00 11.76 ? 61  ASN D N   1 
ATOM   6851 C  CA  . ASN D 1 61  ? 11.927  21.596  19.430  1.00 13.10 ? 61  ASN D CA  1 
ATOM   6852 C  C   . ASN D 1 61  ? 12.695  22.382  18.373  1.00 14.53 ? 61  ASN D C   1 
ATOM   6853 O  O   . ASN D 1 61  ? 12.104  22.903  17.401  1.00 14.60 ? 61  ASN D O   1 
ATOM   6854 C  CB  . ASN D 1 61  ? 11.040  20.553  18.792  1.00 12.73 ? 61  ASN D CB  1 
ATOM   6855 C  CG  . ASN D 1 61  ? 11.809  19.565  17.962  1.00 11.80 ? 61  ASN D CG  1 
ATOM   6856 O  OD1 . ASN D 1 61  ? 12.895  19.826  17.438  1.00 13.93 ? 61  ASN D OD1 1 
ATOM   6857 N  ND2 . ASN D 1 61  ? 11.218  18.368  17.816  1.00 14.50 ? 61  ASN D ND2 1 
ATOM   6858 N  N   . ASN D 1 62  ? 13.970  22.546  18.572  1.00 14.42 ? 62  ASN D N   1 
ATOM   6859 C  CA  . ASN D 1 62  ? 14.799  23.317  17.620  1.00 13.03 ? 62  ASN D CA  1 
ATOM   6860 C  C   . ASN D 1 62  ? 15.441  22.475  16.516  1.00 17.85 ? 62  ASN D C   1 
ATOM   6861 O  O   . ASN D 1 62  ? 16.278  22.981  15.727  1.00 18.80 ? 62  ASN D O   1 
ATOM   6862 C  CB  . ASN D 1 62  ? 15.798  24.134  18.404  1.00 16.68 ? 62  ASN D CB  1 
ATOM   6863 C  CG  . ASN D 1 62  ? 16.657  23.242  19.332  1.00 18.08 ? 62  ASN D CG  1 
ATOM   6864 O  OD1 . ASN D 1 62  ? 17.188  22.241  18.864  1.00 17.20 ? 62  ASN D OD1 1 
ATOM   6865 N  ND2 . ASN D 1 62  ? 16.682  23.543  20.658  1.00 22.13 ? 62  ASN D ND2 1 
ATOM   6866 N  N   . GLY D 1 63  ? 15.092  21.185  16.424  1.00 13.70 ? 63  GLY D N   1 
ATOM   6867 C  CA  . GLY D 1 63  ? 15.617  20.317  15.359  1.00 16.81 ? 63  GLY D CA  1 
ATOM   6868 C  C   . GLY D 1 63  ? 16.872  19.640  15.832  1.00 11.91 ? 63  GLY D C   1 
ATOM   6869 O  O   . GLY D 1 63  ? 17.379  18.736  15.121  1.00 15.73 ? 63  GLY D O   1 
ATOM   6870 N  N   . HIS D 1 64  ? 17.465  20.076  16.970  1.00 14.64 ? 64  HIS D N   1 
ATOM   6871 C  CA  . HIS D 1 64  ? 18.677  19.416  17.564  1.00 15.24 ? 64  HIS D CA  1 
ATOM   6872 C  C   . HIS D 1 64  ? 18.359  18.762  18.889  1.00 14.43 ? 64  HIS D C   1 
ATOM   6873 O  O   . HIS D 1 64  ? 18.792  17.636  19.164  1.00 16.24 ? 64  HIS D O   1 
ATOM   6874 C  CB  . HIS D 1 64  ? 19.849  20.400  17.778  1.00 15.85 ? 64  HIS D CB  1 
ATOM   6875 C  CG  . HIS D 1 64  ? 20.184  21.175  16.521  1.00 14.87 ? 64  HIS D CG  1 
ATOM   6876 N  ND1 . HIS D 1 64  ? 20.735  20.551  15.427  1.00 17.47 ? 64  HIS D ND1 1 
ATOM   6877 C  CD2 . HIS D 1 64  ? 20.036  22.508  16.203  1.00 17.98 ? 64  HIS D CD2 1 
ATOM   6878 C  CE1 . HIS D 1 64  ? 20.905  21.449  14.453  1.00 18.39 ? 64  HIS D CE1 1 
ATOM   6879 N  NE2 . HIS D 1 64  ? 20.459  22.659  14.930  1.00 18.30 ? 64  HIS D NE2 1 
ATOM   6880 N  N   . ALA D 1 65  ? 17.595  19.448  19.727  1.00 13.25 ? 65  ALA D N   1 
ATOM   6881 C  CA  . ALA D 1 65  ? 17.132  18.972  21.028  1.00 12.84 ? 65  ALA D CA  1 
ATOM   6882 C  C   . ALA D 1 65  ? 15.801  19.700  21.273  1.00 13.20 ? 65  ALA D C   1 
ATOM   6883 O  O   . ALA D 1 65  ? 15.262  20.374  20.386  1.00 13.53 ? 65  ALA D O   1 
ATOM   6884 C  CB  . ALA D 1 65  ? 18.212  19.224  22.092  1.00 14.51 ? 65  ALA D CB  1 
ATOM   6885 N  N   . PHE D 1 66  ? 15.304  19.647  22.492  1.00 10.76 ? 66  PHE D N   1 
ATOM   6886 C  CA  . PHE D 1 66  ? 14.282  20.573  22.939  1.00 12.41 ? 66  PHE D CA  1 
ATOM   6887 C  C   . PHE D 1 66  ? 14.820  21.464  24.062  1.00 12.26 ? 66  PHE D C   1 
ATOM   6888 O  O   . PHE D 1 66  ? 15.675  21.031  24.882  1.00 14.58 ? 66  PHE D O   1 
ATOM   6889 C  CB  . PHE D 1 66  ? 12.939  19.889  23.361  1.00 13.75 ? 66  PHE D CB  1 
ATOM   6890 C  CG  . PHE D 1 66  ? 13.082  19.011  24.566  1.00 11.95 ? 66  PHE D CG  1 
ATOM   6891 C  CD1 . PHE D 1 66  ? 12.895  19.532  25.829  1.00 10.96 ? 66  PHE D CD1 1 
ATOM   6892 C  CD2 . PHE D 1 66  ? 13.347  17.657  24.509  1.00 13.46 ? 66  PHE D CD2 1 
ATOM   6893 C  CE1 . PHE D 1 66  ? 12.982  18.789  27.008  1.00 12.56 ? 66  PHE D CE1 1 
ATOM   6894 C  CE2 . PHE D 1 66  ? 13.449  16.868  25.677  1.00 13.83 ? 66  PHE D CE2 1 
ATOM   6895 C  CZ  . PHE D 1 66  ? 13.274  17.394  26.927  1.00 12.68 ? 66  PHE D CZ  1 
ATOM   6896 N  N   . ASN D 1 67  ? 14.339  22.684  24.112  1.00 13.22 ? 67  ASN D N   1 
ATOM   6897 C  CA  . ASN D 1 67  ? 14.849  23.523  25.161  1.00 14.34 ? 67  ASN D CA  1 
ATOM   6898 C  C   . ASN D 1 67  ? 13.695  24.160  25.834  1.00 13.44 ? 67  ASN D C   1 
ATOM   6899 O  O   . ASN D 1 67  ? 12.708  24.594  25.175  1.00 15.61 ? 67  ASN D O   1 
ATOM   6900 C  CB  . ASN D 1 67  ? 15.843  24.582  24.664  1.00 22.05 ? 67  ASN D CB  1 
ATOM   6901 C  CG  . ASN D 1 67  ? 15.916  24.669  23.161  1.00 23.03 ? 67  ASN D CG  1 
ATOM   6902 O  OD1 . ASN D 1 67  ? 15.012  25.197  22.510  1.00 37.86 ? 67  ASN D OD1 1 
ATOM   6903 N  ND2 . ASN D 1 67  ? 17.008  24.173  22.587  1.00 60.99 ? 67  ASN D ND2 1 
ATOM   6904 N  N   . VAL D 1 68  ? 13.791  24.245  27.141  1.00 11.99 ? 68  VAL D N   1 
ATOM   6905 C  CA  . VAL D 1 68  ? 12.912  25.013  27.992  1.00 11.81 ? 68  VAL D CA  1 
ATOM   6906 C  C   . VAL D 1 68  ? 13.572  26.360  28.296  1.00 12.06 ? 68  VAL D C   1 
ATOM   6907 O  O   . VAL D 1 68  ? 14.652  26.385  28.894  1.00 12.12 ? 68  VAL D O   1 
ATOM   6908 C  CB  . VAL D 1 68  ? 12.560  24.278  29.262  1.00 12.40 ? 68  VAL D CB  1 
ATOM   6909 C  CG1 . VAL D 1 68  ? 11.723  25.213  30.145  1.00 14.34 ? 68  VAL D CG1 1 
ATOM   6910 C  CG2 . VAL D 1 68  ? 11.791  22.938  28.953  1.00 14.91 ? 68  VAL D CG2 1 
ATOM   6911 N  N   A GLU D 1 69  ? 12.901  27.439  27.928  0.50 13.32 ? 69  GLU D N   1 
ATOM   6912 N  N   B GLU D 1 69  ? 12.986  27.458  27.815  0.50 11.66 ? 69  GLU D N   1 
ATOM   6913 C  CA  A GLU D 1 69  ? 13.418  28.779  28.018  0.50 11.90 ? 69  GLU D CA  1 
ATOM   6914 C  CA  B GLU D 1 69  ? 13.513  28.778  28.116  0.50 10.71 ? 69  GLU D CA  1 
ATOM   6915 C  C   A GLU D 1 69  ? 12.798  29.522  29.162  0.50 11.63 ? 69  GLU D C   1 
ATOM   6916 C  C   B GLU D 1 69  ? 12.808  29.363  29.390  0.50 12.26 ? 69  GLU D C   1 
ATOM   6917 O  O   A GLU D 1 69  ? 11.556  29.494  29.248  0.50 9.61  ? 69  GLU D O   1 
ATOM   6918 O  O   B GLU D 1 69  ? 11.598  29.077  29.831  0.50 13.58 ? 69  GLU D O   1 
ATOM   6919 C  CB  A GLU D 1 69  ? 13.003  29.444  26.692  0.50 18.62 ? 69  GLU D CB  1 
ATOM   6920 C  CB  B GLU D 1 69  ? 13.628  29.788  26.883  0.50 12.29 ? 69  GLU D CB  1 
ATOM   6921 C  CG  A GLU D 1 69  ? 13.507  28.628  25.516  0.50 26.48 ? 69  GLU D CG  1 
ATOM   6922 C  CG  B GLU D 1 69  ? 14.648  30.923  27.001  0.50 16.45 ? 69  GLU D CG  1 
ATOM   6923 C  CD  A GLU D 1 69  ? 12.778  28.815  24.208  0.50 25.40 ? 69  GLU D CD  1 
ATOM   6924 C  CD  B GLU D 1 69  ? 14.943  31.639  25.675  0.50 17.81 ? 69  GLU D CD  1 
ATOM   6925 O  OE1 A GLU D 1 69  ? 11.675  28.251  23.995  0.50 14.53 ? 69  GLU D OE1 1 
ATOM   6926 O  OE1 B GLU D 1 69  ? 15.308  30.990  24.667  0.50 20.72 ? 69  GLU D OE1 1 
ATOM   6927 O  OE2 A GLU D 1 69  ? 13.349  29.513  23.364  0.50 29.08 ? 69  GLU D OE2 1 
ATOM   6928 O  OE2 B GLU D 1 69  ? 14.826  32.880  25.642  0.50 19.44 ? 69  GLU D OE2 1 
ATOM   6929 N  N   . PHE D 1 70  ? 13.597  30.228  29.985  1.00 12.21 ? 70  PHE D N   1 
ATOM   6930 C  CA  . PHE D 1 70  ? 13.142  30.940  31.230  1.00 11.34 ? 70  PHE D CA  1 
ATOM   6931 C  C   . PHE D 1 70  ? 13.164  32.478  31.035  1.00 11.95 ? 70  PHE D C   1 
ATOM   6932 O  O   . PHE D 1 70  ? 13.878  32.973  30.212  1.00 14.81 ? 70  PHE D O   1 
ATOM   6933 C  CB  . PHE D 1 70  ? 14.071  30.608  32.419  1.00 12.09 ? 70  PHE D CB  1 
ATOM   6934 C  CG  . PHE D 1 70  ? 13.861  29.223  32.899  1.00 12.15 ? 70  PHE D CG  1 
ATOM   6935 C  CD1 . PHE D 1 70  ? 14.350  28.108  32.193  1.00 13.14 ? 70  PHE D CD1 1 
ATOM   6936 C  CD2 . PHE D 1 70  ? 13.149  29.052  34.066  1.00 11.91 ? 70  PHE D CD2 1 
ATOM   6937 C  CE1 . PHE D 1 70  ? 14.090  26.800  32.645  1.00 16.12 ? 70  PHE D CE1 1 
ATOM   6938 C  CE2 . PHE D 1 70  ? 12.853  27.748  34.535  1.00 12.80 ? 70  PHE D CE2 1 
ATOM   6939 C  CZ  . PHE D 1 70  ? 13.364  26.621  33.826  1.00 13.49 ? 70  PHE D CZ  1 
ATOM   6940 N  N   A ASP D 1 71  ? 12.420  33.163  31.916  0.50 15.20 ? 71  ASP D N   1 
ATOM   6941 N  N   B ASP D 1 71  ? 12.281  33.200  31.695  0.50 13.58 ? 71  ASP D N   1 
ATOM   6942 C  CA  A ASP D 1 71  ? 12.554  34.612  32.105  0.50 14.99 ? 71  ASP D CA  1 
ATOM   6943 C  CA  B ASP D 1 71  ? 12.351  34.663  31.676  0.50 12.93 ? 71  ASP D CA  1 
ATOM   6944 C  C   A ASP D 1 71  ? 13.833  34.903  32.829  0.50 15.85 ? 71  ASP D C   1 
ATOM   6945 C  C   B ASP D 1 71  ? 13.502  35.054  32.631  0.50 15.64 ? 71  ASP D C   1 
ATOM   6946 O  O   A ASP D 1 71  ? 14.055  34.650  34.003  0.50 17.40 ? 71  ASP D O   1 
ATOM   6947 O  O   B ASP D 1 71  ? 13.273  34.875  33.844  0.50 14.35 ? 71  ASP D O   1 
ATOM   6948 C  CB  A ASP D 1 71  ? 11.419  35.204  32.914  0.50 16.97 ? 71  ASP D CB  1 
ATOM   6949 C  CB  B ASP D 1 71  ? 10.980  35.177  32.149  0.50 12.79 ? 71  ASP D CB  1 
ATOM   6950 C  CG  A ASP D 1 71  ? 11.547  36.741  33.114  0.50 16.08 ? 71  ASP D CG  1 
ATOM   6951 C  CG  B ASP D 1 71  ? 10.897  36.701  32.271  0.50 14.93 ? 71  ASP D CG  1 
ATOM   6952 O  OD1 A ASP D 1 71  ? 12.425  37.400  32.539  0.50 17.45 ? 71  ASP D OD1 1 
ATOM   6953 O  OD1 B ASP D 1 71  ? 9.779   37.201  32.637  0.50 19.57 ? 71  ASP D OD1 1 
ATOM   6954 O  OD2 A ASP D 1 71  ? 10.807  37.221  33.982  0.50 18.53 ? 71  ASP D OD2 1 
ATOM   6955 O  OD2 B ASP D 1 71  ? 11.879  37.358  31.861  0.50 21.35 ? 71  ASP D OD2 1 
ATOM   6956 N  N   . ASP D 1 72  ? 14.672  35.518  32.117  1.00 15.79 ? 72  ASP D N   1 
ATOM   6957 C  CA  . ASP D 1 72  ? 15.921  35.871  32.780  1.00 15.60 ? 72  ASP D CA  1 
ATOM   6958 C  C   . ASP D 1 72  ? 16.016  37.397  32.891  1.00 22.39 ? 72  ASP D C   1 
ATOM   6959 O  O   . ASP D 1 72  ? 17.132  37.897  32.877  1.00 20.96 ? 72  ASP D O   1 
ATOM   6960 C  CB  . ASP D 1 72  ? 17.129  35.273  31.988  1.00 17.91 ? 72  ASP D CB  1 
ATOM   6961 C  CG  . ASP D 1 72  ? 17.250  35.828  30.582  1.00 18.72 ? 72  ASP D CG  1 
ATOM   6962 O  OD1 . ASP D 1 72  ? 16.292  36.485  30.054  1.00 18.95 ? 72  ASP D OD1 1 
ATOM   6963 O  OD2 . ASP D 1 72  ? 18.270  35.660  29.953  1.00 19.32 ? 72  ASP D OD2 1 
ATOM   6964 N  N   . SER D 1 73  ? 14.889  38.109  32.942  1.00 20.42 ? 73  SER D N   1 
ATOM   6965 C  CA  . SER D 1 73  ? 14.992  39.655  32.927  1.00 22.80 ? 73  SER D CA  1 
ATOM   6966 C  C   . SER D 1 73  ? 15.050  40.173  34.353  1.00 25.13 ? 73  SER D C   1 
ATOM   6967 O  O   . SER D 1 73  ? 15.194  41.376  34.525  1.00 22.13 ? 73  SER D O   1 
ATOM   6968 C  CB  . SER D 1 73  ? 13.824  40.268  32.183  1.00 25.86 ? 73  SER D CB  1 
ATOM   6969 O  OG  . SER D 1 73  ? 12.650  39.946  32.880  1.00 23.70 ? 73  SER D OG  1 
ATOM   6970 N  N   . GLN D 1 74  ? 14.917  39.313  35.370  1.00 25.07 ? 74  GLN D N   1 
ATOM   6971 C  CA  . GLN D 1 74  ? 15.152  39.722  36.772  1.00 25.72 ? 74  GLN D CA  1 
ATOM   6972 C  C   . GLN D 1 74  ? 16.138  38.799  37.406  1.00 25.68 ? 74  GLN D C   1 
ATOM   6973 O  O   . GLN D 1 74  ? 16.390  37.694  36.863  1.00 21.29 ? 74  GLN D O   1 
ATOM   6974 C  CB  . GLN D 1 74  ? 13.844  39.752  37.601  1.00 27.76 ? 74  GLN D CB  1 
ATOM   6975 C  CG  . GLN D 1 74  ? 12.979  40.944  37.248  1.00 35.92 ? 74  GLN D CG  1 
ATOM   6976 C  CD  . GLN D 1 74  ? 11.686  40.976  38.003  1.00 39.92 ? 74  GLN D CD  1 
ATOM   6977 O  OE1 . GLN D 1 74  ? 11.663  41.247  39.216  1.00 58.95 ? 74  GLN D OE1 1 
ATOM   6978 N  NE2 . GLN D 1 74  ? 10.592  40.704  37.298  1.00 41.45 ? 74  GLN D NE2 1 
ATOM   6979 N  N   . ASP D 1 75  ? 16.628  39.174  38.599  1.00 24.90 ? 75  ASP D N   1 
ATOM   6980 C  CA  . ASP D 1 75  ? 17.632  38.352  39.210  1.00 26.52 ? 75  ASP D CA  1 
ATOM   6981 C  C   . ASP D 1 75  ? 16.888  37.275  40.044  1.00 25.21 ? 75  ASP D C   1 
ATOM   6982 O  O   . ASP D 1 75  ? 16.625  37.497  41.238  1.00 33.83 ? 75  ASP D O   1 
ATOM   6983 C  CB  . ASP D 1 75  ? 18.695  39.177  39.988  1.00 40.44 ? 75  ASP D CB  1 
ATOM   6984 C  CG  . ASP D 1 75  ? 20.046  38.424  40.096  1.00 52.59 ? 75  ASP D CG  1 
ATOM   6985 O  OD1 . ASP D 1 75  ? 20.665  37.945  39.015  1.00 32.82 ? 75  ASP D OD1 1 
ATOM   6986 O  OD2 . ASP D 1 75  ? 20.441  38.254  41.273  1.00 55.23 ? 75  ASP D OD2 1 
ATOM   6987 N  N   . LYS D 1 76  ? 16.511  36.161  39.400  1.00 23.28 ? 76  LYS D N   1 
ATOM   6988 C  CA  . LYS D 1 76  ? 15.656  35.175  40.068  1.00 34.21 ? 76  LYS D CA  1 
ATOM   6989 C  C   . LYS D 1 76  ? 16.504  33.889  40.296  1.00 36.44 ? 76  LYS D C   1 
ATOM   6990 O  O   . LYS D 1 76  ? 17.145  33.718  41.391  1.00 41.72 ? 76  LYS D O   1 
ATOM   6991 C  CB  . LYS D 1 76  ? 14.286  35.031  39.255  1.00 26.65 ? 76  LYS D CB  1 
ATOM   6992 N  N   . ALA D 1 77  ? 16.579  33.079  39.256  1.00 24.64 ? 77  ALA D N   1 
ATOM   6993 C  CA  . ALA D 1 77  ? 17.114  31.700  39.270  1.00 22.25 ? 77  ALA D CA  1 
ATOM   6994 C  C   . ALA D 1 77  ? 18.589  31.901  38.994  1.00 18.44 ? 77  ALA D C   1 
ATOM   6995 O  O   . ALA D 1 77  ? 18.969  32.119  37.854  1.00 22.32 ? 77  ALA D O   1 
ATOM   6996 C  CB  . ALA D 1 77  ? 16.460  30.969  38.077  1.00 22.13 ? 77  ALA D CB  1 
ATOM   6997 N  N   . VAL D 1 78  ? 19.436  31.740  40.002  1.00 15.51 ? 78  VAL D N   1 
ATOM   6998 C  CA  . VAL D 1 78  ? 20.867  32.037  39.831  1.00 17.10 ? 78  VAL D CA  1 
ATOM   6999 C  C   . VAL D 1 78  ? 21.799  30.966  40.377  1.00 15.28 ? 78  VAL D C   1 
ATOM   7000 O  O   . VAL D 1 78  ? 21.483  30.269  41.310  1.00 16.05 ? 78  VAL D O   1 
ATOM   7001 C  CB  . VAL D 1 78  ? 21.273  33.403  40.377  1.00 20.76 ? 78  VAL D CB  1 
ATOM   7002 C  CG1 . VAL D 1 78  ? 20.368  34.539  39.936  1.00 23.67 ? 78  VAL D CG1 1 
ATOM   7003 C  CG2 . VAL D 1 78  ? 21.265  33.416  41.821  1.00 21.79 ? 78  VAL D CG2 1 
ATOM   7004 N  N   . LEU D 1 79  ? 22.917  30.784  39.676  1.00 12.64 ? 79  LEU D N   1 
ATOM   7005 C  CA  . LEU D 1 79  ? 23.975  29.874  40.085  1.00 13.40 ? 79  LEU D CA  1 
ATOM   7006 C  C   . LEU D 1 79  ? 25.129  30.736  40.537  1.00 13.81 ? 79  LEU D C   1 
ATOM   7007 O  O   . LEU D 1 79  ? 25.508  31.702  39.774  1.00 14.97 ? 79  LEU D O   1 
ATOM   7008 C  CB  . LEU D 1 79  ? 24.292  28.958  38.885  1.00 16.05 ? 79  LEU D CB  1 
ATOM   7009 C  CG  . LEU D 1 79  ? 25.295  27.891  39.099  1.00 15.34 ? 79  LEU D CG  1 
ATOM   7010 C  CD1 . LEU D 1 79  ? 24.779  26.864  40.069  1.00 18.88 ? 79  LEU D CD1 1 
ATOM   7011 C  CD2 . LEU D 1 79  ? 25.630  27.254  37.765  1.00 14.23 ? 79  LEU D CD2 1 
ATOM   7012 N  N   . LYS D 1 80  ? 25.692  30.442  41.721  1.00 14.28 ? 80  LYS D N   1 
ATOM   7013 C  CA  . LYS D 1 80  ? 26.899  31.123  42.105  1.00 15.53 ? 80  LYS D CA  1 
ATOM   7014 C  C   . LYS D 1 80  ? 27.738  30.246  43.001  1.00 15.59 ? 80  LYS D C   1 
ATOM   7015 O  O   . LYS D 1 80  ? 27.367  29.084  43.216  1.00 15.10 ? 80  LYS D O   1 
ATOM   7016 C  CB  . LYS D 1 80  ? 26.650  32.484  42.773  1.00 18.49 ? 80  LYS D CB  1 
ATOM   7017 C  CG  . LYS D 1 80  ? 25.872  32.263  44.056  1.00 19.99 ? 80  LYS D CG  1 
ATOM   7018 C  CD  . LYS D 1 80  ? 25.354  33.601  44.657  1.00 25.12 ? 80  LYS D CD  1 
ATOM   7019 N  N   . GLY D 1 81  ? 28.833  30.762  43.543  1.00 15.50 ? 81  GLY D N   1 
ATOM   7020 C  CA  . GLY D 1 81  ? 29.694  29.932  44.365  1.00 16.32 ? 81  GLY D CA  1 
ATOM   7021 C  C   . GLY D 1 81  ? 30.379  28.846  43.569  1.00 16.06 ? 81  GLY D C   1 
ATOM   7022 O  O   . GLY D 1 81  ? 30.556  29.011  42.354  1.00 14.92 ? 81  GLY D O   1 
ATOM   7023 N  N   . GLY D 1 82  ? 30.696  27.719  44.163  1.00 17.62 ? 82  GLY D N   1 
ATOM   7024 C  CA  . GLY D 1 82  ? 31.425  26.737  43.415  1.00 21.30 ? 82  GLY D CA  1 
ATOM   7025 C  C   . GLY D 1 82  ? 32.721  27.361  42.943  1.00 17.44 ? 82  GLY D C   1 
ATOM   7026 O  O   . GLY D 1 82  ? 33.424  28.041  43.688  1.00 21.98 ? 82  GLY D O   1 
ATOM   7027 N  N   . PRO D 1 83  ? 33.067  27.156  41.635  1.00 15.04 ? 83  PRO D N   1 
ATOM   7028 C  CA  . PRO D 1 83  ? 34.245  27.742  41.064  1.00 13.91 ? 83  PRO D CA  1 
ATOM   7029 C  C   . PRO D 1 83  ? 34.011  29.157  40.524  1.00 16.90 ? 83  PRO D C   1 
ATOM   7030 O  O   . PRO D 1 83  ? 34.933  29.753  40.025  1.00 17.83 ? 83  PRO D O   1 
ATOM   7031 C  CB  . PRO D 1 83  ? 34.510  26.816  39.855  1.00 15.79 ? 83  PRO D CB  1 
ATOM   7032 C  CG  . PRO D 1 83  ? 33.146  26.396  39.416  1.00 14.37 ? 83  PRO D CG  1 
ATOM   7033 C  CD  . PRO D 1 83  ? 32.355  26.231  40.715  1.00 15.62 ? 83  PRO D CD  1 
ATOM   7034 N  N   . LEU D 1 84  ? 32.792  29.639  40.603  1.00 12.34 ? 84  LEU D N   1 
ATOM   7035 C  CA  . LEU D 1 84  ? 32.360  30.837  39.875  1.00 12.16 ? 84  LEU D CA  1 
ATOM   7036 C  C   . LEU D 1 84  ? 32.700  32.108  40.636  1.00 14.44 ? 84  LEU D C   1 
ATOM   7037 O  O   . LEU D 1 84  ? 32.566  32.151  41.883  1.00 16.00 ? 84  LEU D O   1 
ATOM   7038 C  CB  . LEU D 1 84  ? 30.863  30.799  39.635  1.00 11.90 ? 84  LEU D CB  1 
ATOM   7039 C  CG  . LEU D 1 84  ? 30.369  29.555  38.815  1.00 11.49 ? 84  LEU D CG  1 
ATOM   7040 C  CD1 . LEU D 1 84  ? 28.850  29.524  38.752  1.00 13.57 ? 84  LEU D CD1 1 
ATOM   7041 C  CD2 . LEU D 1 84  ? 31.000  29.520  37.381  1.00 11.09 ? 84  LEU D CD2 1 
ATOM   7042 N  N   . ASP D 1 85  ? 33.008  33.125  39.873  1.00 16.06 ? 85  ASP D N   1 
ATOM   7043 C  CA  . ASP D 1 85  ? 33.131  34.493  40.440  1.00 15.45 ? 85  ASP D CA  1 
ATOM   7044 C  C   . ASP D 1 85  ? 31.885  35.187  39.965  1.00 17.66 ? 85  ASP D C   1 
ATOM   7045 O  O   . ASP D 1 85  ? 31.506  35.102  38.833  1.00 22.26 ? 85  ASP D O   1 
ATOM   7046 C  CB  . ASP D 1 85  ? 34.400  35.179  39.912  1.00 17.12 ? 85  ASP D CB  1 
ATOM   7047 C  CG  . ASP D 1 85  ? 35.652  34.647  40.545  0.50 16.26 ? 85  ASP D CG  1 
ATOM   7048 O  OD1 . ASP D 1 85  ? 35.665  34.144  41.658  0.50 17.22 ? 85  ASP D OD1 1 
ATOM   7049 O  OD2 . ASP D 1 85  ? 36.683  34.789  39.950  0.50 18.09 ? 85  ASP D OD2 1 
ATOM   7050 N  N   . GLY D 1 86  ? 31.216  35.898  40.847  1.00 20.23 ? 86  GLY D N   1 
ATOM   7051 C  CA  . GLY D 1 86  ? 30.032  36.617  40.437  1.00 18.64 ? 86  GLY D CA  1 
ATOM   7052 C  C   . GLY D 1 86  ? 28.766  35.711  40.321  1.00 18.30 ? 86  GLY D C   1 
ATOM   7053 O  O   . GLY D 1 86  ? 28.669  34.647  40.935  1.00 20.73 ? 86  GLY D O   1 
ATOM   7054 N  N   A THR D 1 87  ? 27.763  36.204  39.577  0.50 17.89 ? 87  THR D N   1 
ATOM   7055 N  N   B THR D 1 87  ? 27.783  36.138  39.556  0.50 17.10 ? 87  THR D N   1 
ATOM   7056 C  CA  A THR D 1 87  ? 26.395  35.622  39.533  0.50 15.99 ? 87  THR D CA  1 
ATOM   7057 C  CA  B THR D 1 87  ? 26.520  35.433  39.577  0.50 14.27 ? 87  THR D CA  1 
ATOM   7058 C  C   A THR D 1 87  ? 25.951  35.248  38.135  0.50 13.71 ? 87  THR D C   1 
ATOM   7059 C  C   B THR D 1 87  ? 26.124  35.163  38.159  0.50 12.93 ? 87  THR D C   1 
ATOM   7060 O  O   A THR D 1 87  ? 26.020  36.047  37.202  0.50 12.94 ? 87  THR D O   1 
ATOM   7061 O  O   B THR D 1 87  ? 26.461  35.926  37.239  0.50 12.43 ? 87  THR D O   1 
ATOM   7062 C  CB  A THR D 1 87  ? 25.295  36.603  40.073  0.50 18.75 ? 87  THR D CB  1 
ATOM   7063 C  CB  B THR D 1 87  ? 25.458  36.281  40.292  0.50 17.93 ? 87  THR D CB  1 
ATOM   7064 O  OG1 A THR D 1 87  ? 25.664  37.102  41.376  0.50 19.05 ? 87  THR D OG1 1 
ATOM   7065 O  OG1 B THR D 1 87  ? 25.503  37.598  39.738  0.50 14.57 ? 87  THR D OG1 1 
ATOM   7066 C  CG2 A THR D 1 87  ? 23.892  35.892  40.123  0.50 20.19 ? 87  THR D CG2 1 
ATOM   7067 C  CG2 B THR D 1 87  ? 25.775  36.372  41.814  0.50 16.99 ? 87  THR D CG2 1 
ATOM   7068 N  N   . TYR D 1 88  ? 25.451  34.032  37.983  1.00 12.92 ? 88  TYR D N   1 
ATOM   7069 C  CA  . TYR D 1 88  ? 25.062  33.559  36.618  1.00 11.92 ? 88  TYR D CA  1 
ATOM   7070 C  C   . TYR D 1 88  ? 23.584  33.253  36.634  1.00 11.73 ? 88  TYR D C   1 
ATOM   7071 O  O   . TYR D 1 88  ? 23.076  32.611  37.581  1.00 15.37 ? 88  TYR D O   1 
ATOM   7072 C  CB  . TYR D 1 88  ? 25.868  32.313  36.256  1.00 11.65 ? 88  TYR D CB  1 
ATOM   7073 C  CG  . TYR D 1 88  ? 27.325  32.530  35.986  1.00 10.21 ? 88  TYR D CG  1 
ATOM   7074 C  CD1 . TYR D 1 88  ? 28.207  32.865  36.979  1.00 11.32 ? 88  TYR D CD1 1 
ATOM   7075 C  CD2 . TYR D 1 88  ? 27.820  32.372  34.698  1.00 9.90  ? 88  TYR D CD2 1 
ATOM   7076 C  CE1 . TYR D 1 88  ? 29.545  33.025  36.741  1.00 11.34 ? 88  TYR D CE1 1 
ATOM   7077 C  CE2 . TYR D 1 88  ? 29.143  32.497  34.406  1.00 9.95  ? 88  TYR D CE2 1 
ATOM   7078 C  CZ  . TYR D 1 88  ? 30.043  32.833  35.406  1.00 10.13 ? 88  TYR D CZ  1 
ATOM   7079 O  OH  . TYR D 1 88  ? 31.346  32.894  35.126  1.00 10.71 ? 88  TYR D OH  1 
ATOM   7080 N  N   . ARG D 1 89  ? 22.854  33.768  35.676  1.00 10.92 ? 89  ARG D N   1 
ATOM   7081 C  CA  . ARG D 1 89  ? 21.449  33.654  35.601  1.00 11.00 ? 89  ARG D CA  1 
ATOM   7082 C  C   . ARG D 1 89  ? 20.942  32.521  34.673  1.00 9.60  ? 89  ARG D C   1 
ATOM   7083 O  O   . ARG D 1 89  ? 21.385  32.430  33.508  1.00 10.04 ? 89  ARG D O   1 
ATOM   7084 C  CB  . ARG D 1 89  ? 20.853  34.959  35.136  1.00 15.04 ? 89  ARG D CB  1 
ATOM   7085 C  CG  . ARG D 1 89  ? 19.395  35.132  35.514  1.00 18.95 ? 89  ARG D CG  1 
ATOM   7086 C  CD  . ARG D 1 89  ? 19.018  36.600  35.183  1.00 18.22 ? 89  ARG D CD  1 
ATOM   7087 N  NE  . ARG D 1 89  ? 19.595  37.589  36.108  1.00 19.25 ? 89  ARG D NE  1 
ATOM   7088 C  CZ  . ARG D 1 89  ? 19.473  38.918  35.962  1.00 18.91 ? 89  ARG D CZ  1 
ATOM   7089 N  NH1 . ARG D 1 89  ? 18.805  39.396  34.901  1.00 20.77 ? 89  ARG D NH1 1 
ATOM   7090 N  NH2 . ARG D 1 89  ? 20.062  39.752  36.822  1.00 18.57 ? 89  ARG D NH2 1 
ATOM   7091 N  N   . LEU D 1 90  ? 19.984  31.718  35.139  1.00 11.13 ? 90  LEU D N   1 
ATOM   7092 C  CA  . LEU D 1 90  ? 19.466  30.611  34.336  1.00 10.85 ? 90  LEU D CA  1 
ATOM   7093 C  C   . LEU D 1 90  ? 18.671  31.139  33.143  1.00 10.34 ? 90  LEU D C   1 
ATOM   7094 O  O   . LEU D 1 90  ? 17.781  32.012  33.331  1.00 13.88 ? 90  LEU D O   1 
ATOM   7095 C  CB  . LEU D 1 90  ? 18.495  29.784  35.208  1.00 11.62 ? 90  LEU D CB  1 
ATOM   7096 C  CG  . LEU D 1 90  ? 17.819  28.625  34.487  1.00 11.89 ? 90  LEU D CG  1 
ATOM   7097 C  CD1 . LEU D 1 90  ? 18.784  27.554  33.980  1.00 12.99 ? 90  LEU D CD1 1 
ATOM   7098 C  CD2 . LEU D 1 90  ? 16.775  28.005  35.416  1.00 14.02 ? 90  LEU D CD2 1 
ATOM   7099 N  N   . ILE D 1 91  ? 18.990  30.710  31.950  1.00 10.40 ? 91  ILE D N   1 
ATOM   7100 C  CA  . ILE D 1 91  ? 18.241  31.070  30.751  1.00 10.41 ? 91  ILE D CA  1 
ATOM   7101 C  C   . ILE D 1 91  ? 17.508  29.907  30.122  1.00 11.14 ? 91  ILE D C   1 
ATOM   7102 O  O   . ILE D 1 91  ? 16.349  30.084  29.680  1.00 10.79 ? 91  ILE D O   1 
ATOM   7103 C  CB  . ILE D 1 91  ? 19.128  31.804  29.710  1.00 11.45 ? 91  ILE D CB  1 
ATOM   7104 C  CG1 . ILE D 1 91  ? 18.380  32.105  28.420  1.00 14.92 ? 91  ILE D CG1 1 
ATOM   7105 C  CG2 . ILE D 1 91  ? 20.427  31.002  29.415  1.00 12.36 ? 91  ILE D CG2 1 
ATOM   7106 C  CD1 . ILE D 1 91  ? 19.099  33.168  27.568  1.00 19.01 ? 91  ILE D CD1 1 
ATOM   7107 N  N   . GLN D 1 92  ? 18.084  28.671  30.088  1.00 10.49 ? 92  GLN D N   1 
ATOM   7108 C  CA  . GLN D 1 92  ? 17.327  27.542  29.494  1.00 11.22 ? 92  GLN D CA  1 
ATOM   7109 C  C   . GLN D 1 92  ? 17.969  26.281  30.007  1.00 9.34  ? 92  GLN D C   1 
ATOM   7110 O  O   . GLN D 1 92  ? 19.051  26.276  30.566  1.00 10.21 ? 92  GLN D O   1 
ATOM   7111 C  CB  . GLN D 1 92  ? 17.390  27.569  27.977  1.00 13.09 ? 92  GLN D CB  1 
ATOM   7112 C  CG  . GLN D 1 92  ? 18.788  27.550  27.346  1.00 14.06 ? 92  GLN D CG  1 
ATOM   7113 C  CD  . GLN D 1 92  ? 19.012  26.202  26.647  1.00 14.31 ? 92  GLN D CD  1 
ATOM   7114 O  OE1 . GLN D 1 92  ? 19.179  25.213  27.314  1.00 15.74 ? 92  GLN D OE1 1 
ATOM   7115 N  NE2 . GLN D 1 92  ? 19.002  26.144  25.329  1.00 20.22 ? 92  GLN D NE2 1 
ATOM   7116 N  N   . PHE D 1 93  ? 17.234  25.184  29.848  1.00 9.61  ? 93  PHE D N   1 
ATOM   7117 C  CA  . PHE D 1 93  ? 17.836  23.866  29.892  1.00 9.21  ? 93  PHE D CA  1 
ATOM   7118 C  C   . PHE D 1 93  ? 17.423  23.029  28.720  1.00 8.77  ? 93  PHE D C   1 
ATOM   7119 O  O   . PHE D 1 93  ? 16.411  23.271  28.056  1.00 10.18 ? 93  PHE D O   1 
ATOM   7120 C  CB  . PHE D 1 93  ? 17.553  23.184  31.232  1.00 9.73  ? 93  PHE D CB  1 
ATOM   7121 C  CG  . PHE D 1 93  ? 16.130  22.762  31.481  1.00 10.12 ? 93  PHE D CG  1 
ATOM   7122 C  CD1 . PHE D 1 93  ? 15.581  21.633  30.818  1.00 11.46 ? 93  PHE D CD1 1 
ATOM   7123 C  CD2 . PHE D 1 93  ? 15.333  23.441  32.433  1.00 11.33 ? 93  PHE D CD2 1 
ATOM   7124 C  CE1 . PHE D 1 93  ? 14.237  21.241  31.042  1.00 12.03 ? 93  PHE D CE1 1 
ATOM   7125 C  CE2 . PHE D 1 93  ? 14.012  23.006  32.655  1.00 12.07 ? 93  PHE D CE2 1 
ATOM   7126 C  CZ  . PHE D 1 93  ? 13.476  21.894  31.996  1.00 11.38 ? 93  PHE D CZ  1 
ATOM   7127 N  N   . HIS D 1 94  ? 18.224  21.979  28.478  1.00 9.07  ? 94  HIS D N   1 
ATOM   7128 C  CA  . HIS D 1 94  ? 17.947  21.027  27.426  1.00 8.32  ? 94  HIS D CA  1 
ATOM   7129 C  C   . HIS D 1 94  ? 18.665  19.744  27.841  1.00 8.14  ? 94  HIS D C   1 
ATOM   7130 O  O   . HIS D 1 94  ? 19.395  19.691  28.829  1.00 8.50  ? 94  HIS D O   1 
ATOM   7131 C  CB  . HIS D 1 94  ? 18.496  21.526  26.053  1.00 8.16  ? 94  HIS D CB  1 
ATOM   7132 C  CG  . HIS D 1 94  ? 19.987  21.787  26.099  1.00 7.45  ? 94  HIS D CG  1 
ATOM   7133 N  ND1 . HIS D 1 94  ? 20.529  22.992  26.526  1.00 8.72  ? 94  HIS D ND1 1 
ATOM   7134 C  CD2 . HIS D 1 94  ? 21.030  20.947  25.861  1.00 8.00  ? 94  HIS D CD2 1 
ATOM   7135 C  CE1 . HIS D 1 94  ? 21.866  22.854  26.516  1.00 8.67  ? 94  HIS D CE1 1 
ATOM   7136 N  NE2 . HIS D 1 94  ? 22.164  21.596  26.137  1.00 8.39  ? 94  HIS D NE2 1 
ATOM   7137 N  N   . PHE D 1 95  ? 18.457  18.706  27.019  1.00 8.45  ? 95  PHE D N   1 
ATOM   7138 C  CA  . PHE D 1 95  ? 19.077  17.385  27.264  1.00 8.08  ? 95  PHE D CA  1 
ATOM   7139 C  C   . PHE D 1 95  ? 19.744  16.926  25.995  1.00 8.15  ? 95  PHE D C   1 
ATOM   7140 O  O   . PHE D 1 95  ? 19.439  17.388  24.860  1.00 8.84  ? 95  PHE D O   1 
ATOM   7141 C  CB  . PHE D 1 95  ? 17.992  16.339  27.590  1.00 8.59  ? 95  PHE D CB  1 
ATOM   7142 C  CG  . PHE D 1 95  ? 17.228  16.637  28.870  1.00 7.66  ? 95  PHE D CG  1 
ATOM   7143 C  CD1 . PHE D 1 95  ? 16.142  17.524  28.844  1.00 9.49  ? 95  PHE D CD1 1 
ATOM   7144 C  CD2 . PHE D 1 95  ? 17.435  15.961  30.079  1.00 8.80  ? 95  PHE D CD2 1 
ATOM   7145 C  CE1 . PHE D 1 95  ? 15.368  17.764  29.980  1.00 9.62  ? 95  PHE D CE1 1 
ATOM   7146 C  CE2 . PHE D 1 95  ? 16.682  16.156  31.203  1.00 9.77  ? 95  PHE D CE2 1 
ATOM   7147 C  CZ  . PHE D 1 95  ? 15.620  17.078  31.153  1.00 9.65  ? 95  PHE D CZ  1 
ATOM   7148 N  N   . HIS D 1 96  ? 20.647  15.942  26.194  1.00 7.98  ? 96  HIS D N   1 
ATOM   7149 C  CA  . HIS D 1 96  ? 21.223  15.162  25.130  1.00 8.59  ? 96  HIS D CA  1 
ATOM   7150 C  C   . HIS D 1 96  ? 20.945  13.702  25.500  1.00 8.50  ? 96  HIS D C   1 
ATOM   7151 O  O   . HIS D 1 96  ? 21.016  13.346  26.686  1.00 9.00  ? 96  HIS D O   1 
ATOM   7152 C  CB  . HIS D 1 96  ? 22.709  15.360  24.984  1.00 8.27  ? 96  HIS D CB  1 
ATOM   7153 C  CG  . HIS D 1 96  ? 23.106  16.784  24.799  1.00 7.66  ? 96  HIS D CG  1 
ATOM   7154 N  ND1 . HIS D 1 96  ? 23.409  17.338  23.591  1.00 8.59  ? 96  HIS D ND1 1 
ATOM   7155 C  CD2 . HIS D 1 96  ? 23.224  17.779  25.723  1.00 9.09  ? 96  HIS D CD2 1 
ATOM   7156 C  CE1 . HIS D 1 96  ? 23.734  18.654  23.740  1.00 9.17  ? 96  HIS D CE1 1 
ATOM   7157 N  NE2 . HIS D 1 96  ? 23.572  18.961  25.064  1.00 7.84  ? 96  HIS D NE2 1 
ATOM   7158 N  N   . TRP D 1 97  ? 20.593  12.826  24.549  1.00 7.81  ? 97  TRP D N   1 
ATOM   7159 C  CA  . TRP D 1 97  ? 20.263  11.429  24.878  1.00 8.91  ? 97  TRP D CA  1 
ATOM   7160 C  C   . TRP D 1 97  ? 20.531  10.527  23.741  1.00 9.04  ? 97  TRP D C   1 
ATOM   7161 O  O   . TRP D 1 97  ? 20.891  10.963  22.603  1.00 9.40  ? 97  TRP D O   1 
ATOM   7162 C  CB  . TRP D 1 97  ? 18.796  11.322  25.304  1.00 8.57  ? 97  TRP D CB  1 
ATOM   7163 C  CG  . TRP D 1 97  ? 17.790  11.696  24.250  1.00 8.68  ? 97  TRP D CG  1 
ATOM   7164 C  CD1 . TRP D 1 97  ? 17.262  10.869  23.285  1.00 9.42  ? 97  TRP D CD1 1 
ATOM   7165 C  CD2 . TRP D 1 97  ? 17.286  13.000  23.949  1.00 9.29  ? 97  TRP D CD2 1 
ATOM   7166 N  NE1 . TRP D 1 97  ? 16.399  11.563  22.460  1.00 10.29 ? 97  TRP D NE1 1 
ATOM   7167 C  CE2 . TRP D 1 97  ? 16.400  12.887  22.804  1.00 9.61  ? 97  TRP D CE2 1 
ATOM   7168 C  CE3 . TRP D 1 97  ? 17.465  14.282  24.535  1.00 9.22  ? 97  TRP D CE3 1 
ATOM   7169 C  CZ2 . TRP D 1 97  ? 15.694  13.982  22.302  1.00 10.89 ? 97  TRP D CZ2 1 
ATOM   7170 C  CZ3 . TRP D 1 97  ? 16.816  15.390  24.015  1.00 11.01 ? 97  TRP D CZ3 1 
ATOM   7171 C  CH2 . TRP D 1 97  ? 15.891  15.249  22.919  1.00 10.97 ? 97  TRP D CH2 1 
ATOM   7172 N  N   . GLY D 1 98  ? 20.451  9.210   23.999  1.00 9.11  ? 98  GLY D N   1 
ATOM   7173 C  CA  . GLY D 1 98  ? 20.852  8.190   23.027  1.00 9.41  ? 98  GLY D CA  1 
ATOM   7174 C  C   . GLY D 1 98  ? 19.683  7.449   22.402  1.00 9.80  ? 98  GLY D C   1 
ATOM   7175 O  O   . GLY D 1 98  ? 18.534  7.619   22.781  1.00 10.62 ? 98  GLY D O   1 
ATOM   7176 N  N   . SER D 1 99  ? 20.087  6.581   21.440  1.00 11.33 ? 99  SER D N   1 
ATOM   7177 C  CA  . SER D 1 99  ? 19.127  5.653   20.854  1.00 13.03 ? 99  SER D CA  1 
ATOM   7178 C  C   . SER D 1 99  ? 18.941  4.416   21.767  1.00 12.69 ? 99  SER D C   1 
ATOM   7179 O  O   . SER D 1 99  ? 17.945  3.678   21.568  1.00 16.44 ? 99  SER D O   1 
ATOM   7180 C  CB  . SER D 1 99  ? 19.647  5.308   19.493  1.00 14.27 ? 99  SER D CB  1 
ATOM   7181 O  OG  . SER D 1 99  ? 20.955  4.768   19.587  1.00 14.11 ? 99  SER D OG  1 
ATOM   7182 N  N   . LEU D 1 100 ? 19.810  4.180   22.747  1.00 11.73 ? 100 LEU D N   1 
ATOM   7183 C  CA  . LEU D 1 100 ? 19.733  3.049   23.657  1.00 14.40 ? 100 LEU D CA  1 
ATOM   7184 C  C   . LEU D 1 100 ? 20.220  3.526   25.005  1.00 12.97 ? 100 LEU D C   1 
ATOM   7185 O  O   . LEU D 1 100 ? 20.963  4.544   25.086  1.00 12.94 ? 100 LEU D O   1 
ATOM   7186 C  CB  . LEU D 1 100 ? 20.765  1.960   23.286  1.00 18.60 ? 100 LEU D CB  1 
ATOM   7187 C  CG  . LEU D 1 100 ? 20.599  1.590   21.853  1.00 24.88 ? 100 LEU D CG  1 
ATOM   7188 C  CD1 . LEU D 1 100 ? 21.908  1.140   21.196  1.00 42.63 ? 100 LEU D CD1 1 
ATOM   7189 C  CD2 . LEU D 1 100 ? 19.521  0.544   21.845  1.00 27.48 ? 100 LEU D CD2 1 
ATOM   7190 N  N   . ASP D 1 101 ? 19.919  2.829   26.070  1.00 13.11 ? 101 ASP D N   1 
ATOM   7191 C  CA  . ASP D 1 101 ? 20.285  3.283   27.438  1.00 12.98 ? 101 ASP D CA  1 
ATOM   7192 C  C   . ASP D 1 101 ? 21.743  3.393   27.667  1.00 12.10 ? 101 ASP D C   1 
ATOM   7193 O  O   . ASP D 1 101 ? 22.140  4.138   28.533  1.00 14.63 ? 101 ASP D O   1 
ATOM   7194 C  CB  . ASP D 1 101 ? 19.635  2.437   28.556  1.00 15.89 ? 101 ASP D CB  1 
ATOM   7195 C  CG  . ASP D 1 101 ? 18.115  2.371   28.481  1.00 16.69 ? 101 ASP D CG  1 
ATOM   7196 O  OD1 . ASP D 1 101 ? 17.483  3.201   27.797  1.00 15.98 ? 101 ASP D OD1 1 
ATOM   7197 O  OD2 . ASP D 1 101 ? 17.550  1.463   29.130  1.00 21.21 ? 101 ASP D OD2 1 
ATOM   7198 N  N   . GLY D 1 102 ? 22.577  2.630   26.923  1.00 13.02 ? 102 GLY D N   1 
ATOM   7199 C  CA  . GLY D 1 102 ? 24.029  2.706   27.143  1.00 13.71 ? 102 GLY D CA  1 
ATOM   7200 C  C   . GLY D 1 102 ? 24.799  3.809   26.458  1.00 12.47 ? 102 GLY D C   1 
ATOM   7201 O  O   . GLY D 1 102 ? 26.027  3.823   26.516  1.00 13.78 ? 102 GLY D O   1 
ATOM   7202 N  N   . GLN D 1 103 ? 24.095  4.808   25.928  1.00 11.67 ? 103 GLN D N   1 
ATOM   7203 C  CA  . GLN D 1 103 ? 24.791  5.995   25.412  1.00 10.07 ? 103 GLN D CA  1 
ATOM   7204 C  C   . GLN D 1 103 ? 23.831  7.130   25.445  1.00 9.17  ? 103 GLN D C   1 
ATOM   7205 O  O   . GLN D 1 103 ? 22.622  6.920   25.570  1.00 10.51 ? 103 GLN D O   1 
ATOM   7206 C  CB  . GLN D 1 103 ? 25.297  5.745   23.966  1.00 11.25 ? 103 GLN D CB  1 
ATOM   7207 C  CG  . GLN D 1 103 ? 24.192  5.510   22.965  1.00 11.18 ? 103 GLN D CG  1 
ATOM   7208 C  CD  . GLN D 1 103 ? 24.684  4.858   21.696  1.00 16.54 ? 103 GLN D CD  1 
ATOM   7209 O  OE1 . GLN D 1 103 ? 25.436  3.888   21.767  1.00 25.02 ? 103 GLN D OE1 1 
ATOM   7210 N  NE2 . GLN D 1 103 ? 24.307  5.390   20.547  1.00 14.83 ? 103 GLN D NE2 1 
ATOM   7211 N  N   . GLY D 1 104 ? 24.348  8.363   25.274  1.00 8.84  ? 104 GLY D N   1 
ATOM   7212 C  CA  . GLY D 1 104 ? 23.514  9.560   25.282  1.00 8.91  ? 104 GLY D CA  1 
ATOM   7213 C  C   . GLY D 1 104 ? 24.161  10.718  25.981  1.00 7.96  ? 104 GLY D C   1 
ATOM   7214 O  O   . GLY D 1 104 ? 23.893  11.847  25.593  1.00 9.12  ? 104 GLY D O   1 
ATOM   7215 N  N   . SER D 1 105 ? 24.976  10.484  27.035  1.00 7.99  ? 105 SER D N   1 
ATOM   7216 C  CA  . SER D 1 105 ? 25.607  11.609  27.694  1.00 7.58  ? 105 SER D CA  1 
ATOM   7217 C  C   . SER D 1 105 ? 26.729  12.140  26.815  1.00 7.96  ? 105 SER D C   1 
ATOM   7218 O  O   . SER D 1 105 ? 27.292  11.451  25.910  1.00 9.53  ? 105 SER D O   1 
ATOM   7219 C  CB  . SER D 1 105 ? 26.133  11.260  29.084  1.00 8.32  ? 105 SER D CB  1 
ATOM   7220 O  OG  . SER D 1 105 ? 27.158  10.276  29.108  1.00 8.44  ? 105 SER D OG  1 
ATOM   7221 N  N   . GLU D 1 106 ? 27.094  13.389  27.069  1.00 7.58  ? 106 GLU D N   1 
ATOM   7222 C  CA  . GLU D 1 106 ? 28.204  14.114  26.393  1.00 7.94  ? 106 GLU D CA  1 
ATOM   7223 C  C   . GLU D 1 106 ? 29.489  13.929  27.219  1.00 7.46  ? 106 GLU D C   1 
ATOM   7224 O  O   . GLU D 1 106 ? 30.458  13.290  26.740  1.00 7.96  ? 106 GLU D O   1 
ATOM   7225 C  CB  . GLU D 1 106 ? 27.820  15.562  26.214  1.00 8.05  ? 106 GLU D CB  1 
ATOM   7226 C  CG  . GLU D 1 106 ? 26.591  15.688  25.302  1.00 9.76  ? 106 GLU D CG  1 
ATOM   7227 C  CD  . GLU D 1 106 ? 26.608  16.961  24.556  1.00 8.71  ? 106 GLU D CD  1 
ATOM   7228 O  OE1 . GLU D 1 106 ? 26.685  18.047  25.195  1.00 9.33  ? 106 GLU D OE1 1 
ATOM   7229 O  OE2 . GLU D 1 106 ? 26.632  16.945  23.299  1.00 10.04 ? 106 GLU D OE2 1 
ATOM   7230 N  N   . HIS D 1 107 ? 29.489  14.341  28.506  1.00 7.27  ? 107 HIS D N   1 
ATOM   7231 C  CA  . HIS D 1 107 ? 30.597  13.952  29.356  1.00 7.00  ? 107 HIS D CA  1 
ATOM   7232 C  C   . HIS D 1 107 ? 30.483  12.475  29.659  1.00 7.95  ? 107 HIS D C   1 
ATOM   7233 O  O   . HIS D 1 107 ? 29.365  11.897  29.631  1.00 8.00  ? 107 HIS D O   1 
ATOM   7234 C  CB  . HIS D 1 107 ? 30.502  14.752  30.676  1.00 7.76  ? 107 HIS D CB  1 
ATOM   7235 C  CG  . HIS D 1 107 ? 30.718  16.228  30.418  1.00 7.73  ? 107 HIS D CG  1 
ATOM   7236 N  ND1 . HIS D 1 107 ? 29.719  17.098  30.104  1.00 7.20  ? 107 HIS D ND1 1 
ATOM   7237 C  CD2 . HIS D 1 107 ? 31.901  16.939  30.346  1.00 7.71  ? 107 HIS D CD2 1 
ATOM   7238 C  CE1 . HIS D 1 107 ? 30.285  18.338  29.850  1.00 7.56  ? 107 HIS D CE1 1 
ATOM   7239 N  NE2 . HIS D 1 107 ? 31.606  18.237  30.011  1.00 7.57  ? 107 HIS D NE2 1 
ATOM   7240 N  N   . THR D 1 108 ? 31.663  11.892  29.946  1.00 8.09  ? 108 THR D N   1 
ATOM   7241 C  CA  . THR D 1 108 ? 31.714  10.521  30.403  1.00 8.03  ? 108 THR D CA  1 
ATOM   7242 C  C   . THR D 1 108 ? 32.536  10.512  31.701  1.00 7.13  ? 108 THR D C   1 
ATOM   7243 O  O   . THR D 1 108 ? 33.258  11.479  32.021  1.00 7.92  ? 108 THR D O   1 
ATOM   7244 C  CB  . THR D 1 108 ? 32.333  9.604   29.337  1.00 8.80  ? 108 THR D CB  1 
ATOM   7245 O  OG1 . THR D 1 108 ? 33.606  10.090  28.917  1.00 9.51  ? 108 THR D OG1 1 
ATOM   7246 C  CG2 . THR D 1 108 ? 31.411  9.518   28.112  1.00 9.60  ? 108 THR D CG2 1 
ATOM   7247 N  N   . VAL D 1 109 ? 32.376  9.466   32.444  1.00 8.29  ? 109 VAL D N   1 
ATOM   7248 C  CA  . VAL D 1 109 ? 33.030  9.363   33.793  1.00 8.74  ? 109 VAL D CA  1 
ATOM   7249 C  C   . VAL D 1 109 ? 33.852  8.047   33.781  1.00 9.46  ? 109 VAL D C   1 
ATOM   7250 O  O   . VAL D 1 109 ? 33.239  6.961   33.719  1.00 9.88  ? 109 VAL D O   1 
ATOM   7251 C  CB  . VAL D 1 109 ? 32.010  9.338   34.937  1.00 9.51  ? 109 VAL D CB  1 
ATOM   7252 C  CG1 . VAL D 1 109 ? 32.764  9.181   36.271  1.00 11.48 ? 109 VAL D CG1 1 
ATOM   7253 C  CG2 . VAL D 1 109 ? 31.184  10.611  34.917  1.00 10.63 ? 109 VAL D CG2 1 
ATOM   7254 N  N   . ASP D 1 110 ? 35.180  8.157   33.721  1.00 9.71  ? 110 ASP D N   1 
ATOM   7255 C  CA  . ASP D 1 110 ? 35.987  6.946   33.527  1.00 11.03 ? 110 ASP D CA  1 
ATOM   7256 C  C   . ASP D 1 110 ? 35.466  6.154   32.330  1.00 10.55 ? 110 ASP D C   1 
ATOM   7257 O  O   . ASP D 1 110 ? 35.407  4.883   32.366  1.00 12.27 ? 110 ASP D O   1 
ATOM   7258 C  CB  . ASP D 1 110 ? 36.053  6.128   34.799  1.00 13.12 ? 110 ASP D CB  1 
ATOM   7259 C  CG  . ASP D 1 110 ? 36.774  6.913   35.934  1.00 12.91 ? 110 ASP D CG  1 
ATOM   7260 O  OD1 . ASP D 1 110 ? 37.580  7.766   35.649  1.00 14.39 ? 110 ASP D OD1 1 
ATOM   7261 O  OD2 . ASP D 1 110 ? 36.483  6.653   37.122  1.00 16.89 ? 110 ASP D OD2 1 
ATOM   7262 N  N   . LYS D 1 111 ? 35.166  6.852   31.259  1.00 10.29 ? 111 LYS D N   1 
ATOM   7263 C  CA  . LYS D 1 111 ? 34.703  6.343   29.969  1.00 10.10 ? 111 LYS D CA  1 
ATOM   7264 C  C   . LYS D 1 111 ? 33.225  5.818   30.026  1.00 10.00 ? 111 LYS D C   1 
ATOM   7265 O  O   . LYS D 1 111 ? 32.661  5.458   29.007  1.00 11.24 ? 111 LYS D O   1 
ATOM   7266 C  CB  . LYS D 1 111 ? 35.648  5.261   29.375  1.00 13.14 ? 111 LYS D CB  1 
ATOM   7267 C  CG  . LYS D 1 111 ? 37.064  5.735   29.270  1.00 16.22 ? 111 LYS D CG  1 
ATOM   7268 C  CD  . LYS D 1 111 ? 37.182  6.708   28.174  1.00 20.12 ? 111 LYS D CD  1 
ATOM   7269 C  CE  . LYS D 1 111 ? 38.592  7.329   27.989  1.00 24.63 ? 111 LYS D CE  1 
ATOM   7270 N  NZ  . LYS D 1 111 ? 38.934  7.158   26.572  1.00 23.69 ? 111 LYS D NZ  1 
ATOM   7271 N  N   . LYS D 1 112 ? 32.590  5.850   31.186  1.00 9.72  ? 112 LYS D N   1 
ATOM   7272 C  CA  . LYS D 1 112 ? 31.189  5.454   31.307  1.00 10.33 ? 112 LYS D CA  1 
ATOM   7273 C  C   . LYS D 1 112 ? 30.303  6.509   30.647  1.00 9.04  ? 112 LYS D C   1 
ATOM   7274 O  O   . LYS D 1 112 ? 30.411  7.721   30.930  1.00 9.66  ? 112 LYS D O   1 
ATOM   7275 C  CB  . LYS D 1 112 ? 30.753  5.356   32.798  1.00 11.35 ? 112 LYS D CB  1 
ATOM   7276 C  CG  . LYS D 1 112 ? 29.264  5.007   32.926  1.00 12.85 ? 112 LYS D CG  1 
ATOM   7277 C  CD  . LYS D 1 112 ? 28.837  4.845   34.377  1.00 14.14 ? 112 LYS D CD  1 
ATOM   7278 C  CE  . LYS D 1 112 ? 27.343  4.717   34.559  1.00 16.70 ? 112 LYS D CE  1 
ATOM   7279 N  NZ  . LYS D 1 112 ? 27.013  3.419   34.139  1.00 20.32 ? 112 LYS D NZ  1 
ATOM   7280 N  N   A LYS D 1 113 ? 29.431  6.045   29.748  0.50 9.43  ? 113 LYS D N   1 
ATOM   7281 N  N   B LYS D 1 113 ? 29.469  6.095   29.678  0.50 9.55  ? 113 LYS D N   1 
ATOM   7282 C  CA  A LYS D 1 113 ? 28.374  6.836   29.155  0.50 8.76  ? 113 LYS D CA  1 
ATOM   7283 C  CA  B LYS D 1 113 ? 28.408  6.928   29.076  0.50 9.26  ? 113 LYS D CA  1 
ATOM   7284 C  C   A LYS D 1 113 ? 27.106  6.652   29.978  0.50 8.23  ? 113 LYS D C   1 
ATOM   7285 C  C   B LYS D 1 113 ? 27.054  6.657   29.747  0.50 9.61  ? 113 LYS D C   1 
ATOM   7286 O  O   A LYS D 1 113 ? 26.762  5.546   30.374  0.50 7.98  ? 113 LYS D O   1 
ATOM   7287 O  O   B LYS D 1 113 ? 26.618  5.491   29.804  0.50 10.43 ? 113 LYS D O   1 
ATOM   7288 C  CB  A LYS D 1 113 ? 28.125  6.349   27.704  0.50 9.53  ? 113 LYS D CB  1 
ATOM   7289 C  CB  B LYS D 1 113 ? 28.253  6.592   27.567  0.50 9.52  ? 113 LYS D CB  1 
ATOM   7290 C  CG  A LYS D 1 113 ? 29.314  6.572   26.786  0.50 9.22  ? 113 LYS D CG  1 
ATOM   7291 C  CG  B LYS D 1 113 ? 29.381  7.086   26.688  0.50 9.81  ? 113 LYS D CG  1 
ATOM   7292 C  CD  A LYS D 1 113 ? 29.091  5.928   25.414  0.50 10.95 ? 113 LYS D CD  1 
ATOM   7293 C  CD  B LYS D 1 113 ? 29.352  6.311   25.378  0.50 9.24  ? 113 LYS D CD  1 
ATOM   7294 C  CE  A LYS D 1 113 ? 29.986  6.469   24.305  0.50 13.37 ? 113 LYS D CE  1 
ATOM   7295 C  CE  B LYS D 1 113 ? 30.488  6.845   24.518  0.50 11.66 ? 113 LYS D CE  1 
ATOM   7296 N  NZ  A LYS D 1 113 ? 31.420  6.094   24.446  0.50 15.31 ? 113 LYS D NZ  1 
ATOM   7297 N  NZ  B LYS D 1 113 ? 30.603  6.122   23.227  0.50 17.04 ? 113 LYS D NZ  1 
ATOM   7298 N  N   . TYR D 1 114 ? 26.365  7.729   30.169  1.00 9.32  ? 114 TYR D N   1 
ATOM   7299 C  CA  . TYR D 1 114 ? 25.037  7.644   30.759  1.00 8.75  ? 114 TYR D CA  1 
ATOM   7300 C  C   . TYR D 1 114 ? 23.992  7.680   29.669  1.00 8.87  ? 114 TYR D C   1 
ATOM   7301 O  O   . TYR D 1 114 ? 24.286  7.974   28.507  1.00 9.29  ? 114 TYR D O   1 
ATOM   7302 C  CB  . TYR D 1 114 ? 24.840  8.783   31.808  1.00 9.91  ? 114 TYR D CB  1 
ATOM   7303 C  CG  . TYR D 1 114 ? 25.622  8.528   33.071  1.00 9.47  ? 114 TYR D CG  1 
ATOM   7304 C  CD1 . TYR D 1 114 ? 26.914  8.954   33.236  1.00 11.43 ? 114 TYR D CD1 1 
ATOM   7305 C  CD2 . TYR D 1 114 ? 24.972  7.926   34.157  1.00 10.81 ? 114 TYR D CD2 1 
ATOM   7306 C  CE1 . TYR D 1 114 ? 27.578  8.745   34.438  1.00 13.53 ? 114 TYR D CE1 1 
ATOM   7307 C  CE2 . TYR D 1 114 ? 25.622  7.695   35.382  1.00 13.14 ? 114 TYR D CE2 1 
ATOM   7308 C  CZ  . TYR D 1 114 ? 26.939  8.162   35.527  1.00 13.55 ? 114 TYR D CZ  1 
ATOM   7309 O  OH  . TYR D 1 114 ? 27.698  7.977   36.721  1.00 17.78 ? 114 TYR D OH  1 
ATOM   7310 N  N   . ALA D 1 115 ? 22.750  7.379   30.030  1.00 9.47  ? 115 ALA D N   1 
ATOM   7311 C  CA  . ALA D 1 115 ? 21.673  7.397   29.063  1.00 9.11  ? 115 ALA D CA  1 
ATOM   7312 C  C   . ALA D 1 115 ? 21.366  8.783   28.536  1.00 8.22  ? 115 ALA D C   1 
ATOM   7313 O  O   . ALA D 1 115 ? 20.790  8.918   27.446  1.00 9.18  ? 115 ALA D O   1 
ATOM   7314 C  CB  . ALA D 1 115 ? 20.440  6.765   29.739  1.00 11.02 ? 115 ALA D CB  1 
ATOM   7315 N  N   . ALA D 1 116 ? 21.648  9.822   29.340  1.00 8.43  ? 116 ALA D N   1 
ATOM   7316 C  CA  . ALA D 1 116 ? 21.295  11.181  28.839  1.00 7.95  ? 116 ALA D CA  1 
ATOM   7317 C  C   . ALA D 1 116 ? 22.067  12.105  29.756  1.00 7.42  ? 116 ALA D C   1 
ATOM   7318 O  O   . ALA D 1 116 ? 22.651  11.728  30.796  1.00 7.81  ? 116 ALA D O   1 
ATOM   7319 C  CB  . ALA D 1 116 ? 19.756  11.439  28.847  1.00 8.82  ? 116 ALA D CB  1 
ATOM   7320 N  N   . GLU D 1 117 ? 22.017  13.399  29.376  1.00 8.03  ? 117 GLU D N   1 
ATOM   7321 C  CA  . GLU D 1 117 ? 22.660  14.445  30.217  1.00 8.07  ? 117 GLU D CA  1 
ATOM   7322 C  C   . GLU D 1 117 ? 21.819  15.700  30.075  1.00 6.81  ? 117 GLU D C   1 
ATOM   7323 O  O   . GLU D 1 117 ? 21.475  16.117  28.951  1.00 8.72  ? 117 GLU D O   1 
ATOM   7324 C  CB  . GLU D 1 117 ? 24.090  14.663  29.752  1.00 7.88  ? 117 GLU D CB  1 
ATOM   7325 C  CG  . GLU D 1 117 ? 24.979  15.606  30.606  1.00 8.92  ? 117 GLU D CG  1 
ATOM   7326 C  CD  . GLU D 1 117 ? 26.424  15.654  30.178  1.00 8.66  ? 117 GLU D CD  1 
ATOM   7327 O  OE1 . GLU D 1 117 ? 26.895  14.657  29.603  1.00 8.50  ? 117 GLU D OE1 1 
ATOM   7328 O  OE2 . GLU D 1 117 ? 27.026  16.730  30.434  1.00 8.99  ? 117 GLU D OE2 1 
ATOM   7329 N  N   . LEU D 1 118 ? 21.518  16.300  31.223  1.00 8.01  ? 118 LEU D N   1 
ATOM   7330 C  CA  . LEU D 1 118 ? 20.756  17.550  31.334  1.00 7.52  ? 118 LEU D CA  1 
ATOM   7331 C  C   . LEU D 1 118 ? 21.775  18.691  31.495  1.00 7.61  ? 118 LEU D C   1 
ATOM   7332 O  O   . LEU D 1 118 ? 22.717  18.610  32.298  1.00 8.00  ? 118 LEU D O   1 
ATOM   7333 C  CB  . LEU D 1 118 ? 19.922  17.453  32.636  1.00 8.20  ? 118 LEU D CB  1 
ATOM   7334 C  CG  . LEU D 1 118 ? 19.310  18.764  33.188  1.00 8.99  ? 118 LEU D CG  1 
ATOM   7335 C  CD1 . LEU D 1 118 ? 18.375  19.432  32.202  1.00 9.99  ? 118 LEU D CD1 1 
ATOM   7336 C  CD2 . LEU D 1 118 ? 18.586  18.473  34.502  1.00 10.40 ? 118 LEU D CD2 1 
ATOM   7337 N  N   . HIS D 1 119 ? 21.551  19.778  30.724  1.00 7.23  ? 119 HIS D N   1 
ATOM   7338 C  CA  . HIS D 1 119 ? 22.341  21.002  30.757  1.00 7.35  ? 119 HIS D CA  1 
ATOM   7339 C  C   . HIS D 1 119 ? 21.475  22.156  31.147  1.00 7.60  ? 119 HIS D C   1 
ATOM   7340 O  O   . HIS D 1 119 ? 20.537  22.525  30.408  1.00 8.89  ? 119 HIS D O   1 
ATOM   7341 C  CB  . HIS D 1 119 ? 22.998  21.229  29.394  1.00 8.25  ? 119 HIS D CB  1 
ATOM   7342 C  CG  . HIS D 1 119 ? 24.079  20.223  29.128  1.00 6.29  ? 119 HIS D CG  1 
ATOM   7343 N  ND1 . HIS D 1 119 ? 24.537  19.950  27.864  1.00 7.19  ? 119 HIS D ND1 1 
ATOM   7344 C  CD2 . HIS D 1 119 ? 24.773  19.423  29.958  1.00 7.99  ? 119 HIS D CD2 1 
ATOM   7345 C  CE1 . HIS D 1 119 ? 25.466  19.032  27.899  1.00 7.99  ? 119 HIS D CE1 1 
ATOM   7346 N  NE2 . HIS D 1 119 ? 25.637  18.688  29.187  1.00 8.72  ? 119 HIS D NE2 1 
ATOM   7347 N  N   . LEU D 1 120 ? 21.799  22.772  32.302  1.00 7.08  ? 120 LEU D N   1 
ATOM   7348 C  CA  . LEU D 1 120 ? 21.143  24.033  32.709  1.00 8.17  ? 120 LEU D CA  1 
ATOM   7349 C  C   . LEU D 1 120 ? 22.156  25.165  32.448  1.00 7.90  ? 120 LEU D C   1 
ATOM   7350 O  O   . LEU D 1 120 ? 23.262  25.175  32.998  1.00 8.18  ? 120 LEU D O   1 
ATOM   7351 C  CB  . LEU D 1 120 ? 20.812  23.958  34.197  1.00 8.77  ? 120 LEU D CB  1 
ATOM   7352 C  CG  . LEU D 1 120 ? 19.720  22.906  34.530  1.00 9.98  ? 120 LEU D CG  1 
ATOM   7353 C  CD1 . LEU D 1 120 ? 20.207  21.960  35.623  1.00 13.70 ? 120 LEU D CD1 1 
ATOM   7354 C  CD2 . LEU D 1 120 ? 18.385  23.623  34.900  1.00 12.34 ? 120 LEU D CD2 1 
ATOM   7355 N  N   . VAL D 1 121 ? 21.747  26.020  31.503  1.00 8.80  ? 121 VAL D N   1 
ATOM   7356 C  CA  . VAL D 1 121 ? 22.655  27.044  30.935  1.00 8.79  ? 121 VAL D CA  1 
ATOM   7357 C  C   . VAL D 1 121 ? 22.388  28.406  31.608  1.00 9.23  ? 121 VAL D C   1 
ATOM   7358 O  O   . VAL D 1 121 ? 21.235  28.832  31.729  1.00 10.17 ? 121 VAL D O   1 
ATOM   7359 C  CB  . VAL D 1 121 ? 22.379  27.185  29.388  1.00 8.67  ? 121 VAL D CB  1 
ATOM   7360 C  CG1 . VAL D 1 121 ? 23.317  28.244  28.807  1.00 10.46 ? 121 VAL D CG1 1 
ATOM   7361 C  CG2 . VAL D 1 121 ? 22.497  25.815  28.668  1.00 11.07 ? 121 VAL D CG2 1 
ATOM   7362 N  N   . HIS D 1 122 ? 23.452  29.009  32.148  1.00 8.72  ? 122 HIS D N   1 
ATOM   7363 C  CA  . HIS D 1 122 ? 23.387  30.275  32.918  1.00 9.89  ? 122 HIS D CA  1 
ATOM   7364 C  C   . HIS D 1 122 ? 24.411  31.248  32.331  1.00 9.61  ? 122 HIS D C   1 
ATOM   7365 O  O   . HIS D 1 122 ? 25.515  30.845  31.918  1.00 9.60  ? 122 HIS D O   1 
ATOM   7366 C  CB  . HIS D 1 122 ? 23.777  30.081  34.394  1.00 9.44  ? 122 HIS D CB  1 
ATOM   7367 C  CG  . HIS D 1 122 ? 23.091  28.925  35.074  1.00 9.54  ? 122 HIS D CG  1 
ATOM   7368 N  ND1 . HIS D 1 122 ? 23.420  27.582  34.817  1.00 8.80  ? 122 HIS D ND1 1 
ATOM   7369 C  CD2 . HIS D 1 122 ? 22.034  28.878  36.005  1.00 10.30 ? 122 HIS D CD2 1 
ATOM   7370 C  CE1 . HIS D 1 122 ? 22.684  26.790  35.592  1.00 10.81 ? 122 HIS D CE1 1 
ATOM   7371 N  NE2 . HIS D 1 122 ? 21.821  27.545  36.313  1.00 10.58 ? 122 HIS D NE2 1 
ATOM   7372 N  N   . TRP D 1 123 ? 24.025  32.525  32.305  1.00 9.44  ? 123 TRP D N   1 
ATOM   7373 C  CA  . TRP D 1 123 ? 24.966  33.530  31.780  1.00 10.33 ? 123 TRP D CA  1 
ATOM   7374 C  C   . TRP D 1 123 ? 25.428  34.507  32.864  1.00 9.36  ? 123 TRP D C   1 
ATOM   7375 O  O   . TRP D 1 123 ? 24.676  34.852  33.805  1.00 10.54 ? 123 TRP D O   1 
ATOM   7376 C  CB  . TRP D 1 123 ? 24.389  34.308  30.563  1.00 11.74 ? 123 TRP D CB  1 
ATOM   7377 C  CG  . TRP D 1 123 ? 23.053  34.940  30.860  1.00 12.35 ? 123 TRP D CG  1 
ATOM   7378 C  CD1 . TRP D 1 123 ? 21.788  34.374  30.740  1.00 13.73 ? 123 TRP D CD1 1 
ATOM   7379 C  CD2 . TRP D 1 123 ? 22.801  36.337  31.244  1.00 12.14 ? 123 TRP D CD2 1 
ATOM   7380 N  NE1 . TRP D 1 123 ? 20.791  35.276  31.029  1.00 14.93 ? 123 TRP D NE1 1 
ATOM   7381 C  CE2 . TRP D 1 123 ? 21.354  36.483  31.391  1.00 13.56 ? 123 TRP D CE2 1 
ATOM   7382 C  CE3 . TRP D 1 123 ? 23.630  37.423  31.599  1.00 13.03 ? 123 TRP D CE3 1 
ATOM   7383 C  CZ2 . TRP D 1 123 ? 20.761  37.659  31.784  1.00 16.16 ? 123 TRP D CZ2 1 
ATOM   7384 C  CZ3 . TRP D 1 123 ? 22.997  38.619  32.003  1.00 14.89 ? 123 TRP D CZ3 1 
ATOM   7385 C  CH2 . TRP D 1 123 ? 21.584  38.736  32.063  1.00 16.45 ? 123 TRP D CH2 1 
ATOM   7386 N  N   . ASN D 1 124 ? 26.673  34.904  32.722  1.00 10.70 ? 124 ASN D N   1 
ATOM   7387 C  CA  . ASN D 1 124 ? 27.295  35.819  33.712  1.00 11.58 ? 124 ASN D CA  1 
ATOM   7388 C  C   . ASN D 1 124 ? 26.672  37.218  33.670  1.00 10.42 ? 124 ASN D C   1 
ATOM   7389 O  O   . ASN D 1 124 ? 26.712  37.895  32.599  1.00 11.35 ? 124 ASN D O   1 
ATOM   7390 C  CB  . ASN D 1 124 ? 28.761  35.884  33.381  1.00 12.05 ? 124 ASN D CB  1 
ATOM   7391 C  CG  . ASN D 1 124 ? 29.617  36.477  34.490  1.00 10.40 ? 124 ASN D CG  1 
ATOM   7392 O  OD1 . ASN D 1 124 ? 29.127  37.340  35.260  1.00 12.82 ? 124 ASN D OD1 1 
ATOM   7393 N  ND2 . ASN D 1 124 ? 30.852  36.001  34.628  1.00 12.26 ? 124 ASN D ND2 1 
ATOM   7394 N  N   . THR D 1 125 ? 26.068  37.602  34.801  1.00 11.48 ? 125 THR D N   1 
ATOM   7395 C  CA  . THR D 1 125 ? 25.324  38.882  34.812  1.00 13.71 ? 125 THR D CA  1 
ATOM   7396 C  C   . THR D 1 125 ? 26.227  40.088  34.642  1.00 13.88 ? 125 THR D C   1 
ATOM   7397 O  O   . THR D 1 125 ? 25.702  41.134  34.217  1.00 15.25 ? 125 THR D O   1 
ATOM   7398 C  CB  . THR D 1 125 ? 24.542  39.059  36.117  1.00 15.19 ? 125 THR D CB  1 
ATOM   7399 O  OG1 . THR D 1 125 ? 25.479  39.060  37.181  1.00 18.67 ? 125 THR D OG1 1 
ATOM   7400 C  CG2 . THR D 1 125 ? 23.487  37.947  36.293  1.00 17.68 ? 125 THR D CG2 1 
ATOM   7401 N  N   . LYS D 1 126 ? 27.548  39.954  34.660  1.00 14.05 ? 127 LYS D N   1 
ATOM   7402 C  CA  . LYS D 1 126 ? 28.392  41.112  34.394  1.00 14.83 ? 127 LYS D CA  1 
ATOM   7403 C  C   . LYS D 1 126 ? 28.379  41.452  32.892  1.00 13.49 ? 127 LYS D C   1 
ATOM   7404 O  O   . LYS D 1 126 ? 28.875  42.541  32.494  1.00 16.42 ? 127 LYS D O   1 
ATOM   7405 C  CB  . LYS D 1 126 ? 29.765  40.902  34.993  1.00 16.01 ? 127 LYS D CB  1 
ATOM   7406 C  CG  . LYS D 1 126 ? 30.628  40.056  34.140  1.00 16.03 ? 127 LYS D CG  1 
ATOM   7407 C  CD  . LYS D 1 126 ? 31.840  39.680  35.026  1.00 21.60 ? 127 LYS D CD  1 
ATOM   7408 C  CE  . LYS D 1 126 ? 32.853  38.852  34.253  1.00 26.04 ? 127 LYS D CE  1 
ATOM   7409 N  NZ  . LYS D 1 126 ? 34.182  39.521  34.185  1.00 29.27 ? 127 LYS D NZ  1 
ATOM   7410 N  N   . TYR D 1 127 ? 27.843  40.593  32.009  1.00 13.49 ? 128 TYR D N   1 
ATOM   7411 C  CA  . TYR D 1 127 ? 27.829  40.885  30.580  1.00 12.64 ? 128 TYR D CA  1 
ATOM   7412 C  C   . TYR D 1 127 ? 26.440  41.307  30.072  1.00 11.81 ? 128 TYR D C   1 
ATOM   7413 O  O   . TYR D 1 127 ? 26.306  41.525  28.885  1.00 13.45 ? 128 TYR D O   1 
ATOM   7414 C  CB  . TYR D 1 127 ? 28.420  39.717  29.759  1.00 13.01 ? 128 TYR D CB  1 
ATOM   7415 C  CG  . TYR D 1 127 ? 29.794  39.401  30.163  1.00 12.55 ? 128 TYR D CG  1 
ATOM   7416 C  CD1 . TYR D 1 127 ? 30.796  40.397  30.116  1.00 13.81 ? 128 TYR D CD1 1 
ATOM   7417 C  CD2 . TYR D 1 127 ? 30.168  38.118  30.636  1.00 12.71 ? 128 TYR D CD2 1 
ATOM   7418 C  CE1 . TYR D 1 127 ? 32.090  40.084  30.539  1.00 14.07 ? 128 TYR D CE1 1 
ATOM   7419 C  CE2 . TYR D 1 127 ? 31.432  37.811  31.043  1.00 13.39 ? 128 TYR D CE2 1 
ATOM   7420 C  CZ  . TYR D 1 127 ? 32.428  38.834  30.952  1.00 12.37 ? 128 TYR D CZ  1 
ATOM   7421 O  OH  . TYR D 1 127 ? 33.686  38.608  31.383  1.00 14.24 ? 128 TYR D OH  1 
ATOM   7422 N  N   . GLY D 1 128 ? 25.480  41.376  31.005  1.00 12.11 ? 129 GLY D N   1 
ATOM   7423 C  CA  . GLY D 1 128 ? 24.231  42.059  30.661  1.00 12.84 ? 129 GLY D CA  1 
ATOM   7424 C  C   . GLY D 1 128 ? 23.199  41.218  29.915  1.00 12.66 ? 129 GLY D C   1 
ATOM   7425 O  O   . GLY D 1 128 ? 22.001  41.371  30.158  1.00 14.78 ? 129 GLY D O   1 
ATOM   7426 N  N   . ASP D 1 129 ? 23.619  40.366  28.971  1.00 14.20 ? 130 ASP D N   1 
ATOM   7427 C  CA  . ASP D 1 129 ? 22.667  39.511  28.303  1.00 14.30 ? 130 ASP D CA  1 
ATOM   7428 C  C   . ASP D 1 129 ? 23.433  38.300  27.781  1.00 14.43 ? 130 ASP D C   1 
ATOM   7429 O  O   . ASP D 1 129 ? 24.674  38.323  27.712  1.00 14.97 ? 130 ASP D O   1 
ATOM   7430 C  CB  . ASP D 1 129 ? 21.783  40.198  27.261  1.00 17.74 ? 130 ASP D CB  1 
ATOM   7431 C  CG  . ASP D 1 129 ? 22.506  40.547  25.974  1.00 19.99 ? 130 ASP D CG  1 
ATOM   7432 O  OD1 . ASP D 1 129 ? 23.597  40.012  25.666  1.00 30.67 ? 130 ASP D OD1 1 
ATOM   7433 O  OD2 . ASP D 1 129 ? 21.932  41.384  25.250  1.00 34.02 ? 130 ASP D OD2 1 
ATOM   7434 N  N   . PHE D 1 130 ? 22.724  37.218  27.446  1.00 14.94 ? 131 PHE D N   1 
ATOM   7435 C  CA  . PHE D 1 130 ? 23.422  36.000  27.054  1.00 16.19 ? 131 PHE D CA  1 
ATOM   7436 C  C   . PHE D 1 130 ? 24.159  36.137  25.742  1.00 15.05 ? 131 PHE D C   1 
ATOM   7437 O  O   . PHE D 1 130 ? 25.202  35.506  25.572  1.00 13.69 ? 131 PHE D O   1 
ATOM   7438 C  CB  . PHE D 1 130 ? 22.469  34.790  27.001  1.00 19.08 ? 131 PHE D CB  1 
ATOM   7439 C  CG  . PHE D 1 130 ? 21.489  34.788  25.879  1.00 20.83 ? 131 PHE D CG  1 
ATOM   7440 C  CD1 . PHE D 1 130 ? 20.174  35.293  26.058  1.00 28.90 ? 131 PHE D CD1 1 
ATOM   7441 C  CD2 . PHE D 1 130 ? 21.824  34.280  24.614  1.00 21.48 ? 131 PHE D CD2 1 
ATOM   7442 C  CE1 . PHE D 1 130 ? 19.216  35.253  25.005  1.00 38.44 ? 131 PHE D CE1 1 
ATOM   7443 C  CE2 . PHE D 1 130 ? 20.857  34.216  23.572  1.00 29.97 ? 131 PHE D CE2 1 
ATOM   7444 C  CZ  . PHE D 1 130 ? 19.561  34.745  23.769  1.00 35.19 ? 131 PHE D CZ  1 
ATOM   7445 N  N   . GLY D 1 131 ? 23.640  36.986  24.791  1.00 15.41 ? 132 GLY D N   1 
ATOM   7446 C  CA  . GLY D 1 131 ? 24.319  37.091  23.470  1.00 13.89 ? 132 GLY D CA  1 
ATOM   7447 C  C   . GLY D 1 131 ? 25.727  37.727  23.629  1.00 13.64 ? 132 GLY D C   1 
ATOM   7448 O  O   . GLY D 1 131 ? 26.698  37.425  22.952  1.00 16.90 ? 132 GLY D O   1 
ATOM   7449 N  N   . LYS D 1 132 ? 25.804  38.669  24.548  1.00 14.54 ? 133 LYS D N   1 
ATOM   7450 C  CA  . LYS D 1 132 ? 27.151  39.197  24.868  1.00 14.74 ? 133 LYS D CA  1 
ATOM   7451 C  C   . LYS D 1 132 ? 27.981  38.229  25.697  1.00 12.89 ? 133 LYS D C   1 
ATOM   7452 O  O   . LYS D 1 132 ? 29.199  38.135  25.490  1.00 13.58 ? 133 LYS D O   1 
ATOM   7453 C  CB  . LYS D 1 132 ? 27.017  40.566  25.573  1.00 14.92 ? 133 LYS D CB  1 
ATOM   7454 C  CG  . LYS D 1 132 ? 26.512  41.731  24.741  1.00 20.24 ? 133 LYS D CG  1 
ATOM   7455 C  CD  . LYS D 1 132 ? 27.626  42.128  23.724  1.00 27.44 ? 133 LYS D CD  1 
ATOM   7456 C  CE  . LYS D 1 132 ? 27.876  43.644  23.742  1.00 31.92 ? 133 LYS D CE  1 
ATOM   7457 N  NZ  . LYS D 1 132 ? 28.887  44.095  22.700  1.00 61.16 ? 133 LYS D NZ  1 
ATOM   7458 N  N   . ALA D 1 133 ? 27.336  37.547  26.671  1.00 11.81 ? 134 ALA D N   1 
ATOM   7459 C  CA  . ALA D 1 133 ? 28.102  36.600  27.517  1.00 12.20 ? 134 ALA D CA  1 
ATOM   7460 C  C   . ALA D 1 133 ? 28.835  35.546  26.705  1.00 11.19 ? 134 ALA D C   1 
ATOM   7461 O  O   . ALA D 1 133 ? 29.958  35.172  27.028  1.00 11.31 ? 134 ALA D O   1 
ATOM   7462 C  CB  . ALA D 1 133 ? 27.148  35.967  28.502  1.00 13.04 ? 134 ALA D CB  1 
ATOM   7463 N  N   . VAL D 1 134 ? 28.227  35.031  25.626  1.00 11.71 ? 135 VAL D N   1 
ATOM   7464 C  CA  . VAL D 1 134 ? 28.879  33.936  24.885  1.00 12.43 ? 135 VAL D CA  1 
ATOM   7465 C  C   . VAL D 1 134 ? 30.122  34.348  24.177  1.00 13.02 ? 135 VAL D C   1 
ATOM   7466 O  O   . VAL D 1 134 ? 30.879  33.501  23.750  1.00 13.23 ? 135 VAL D O   1 
ATOM   7467 C  CB  . VAL D 1 134 ? 28.009  33.217  23.845  1.00 13.41 ? 135 VAL D CB  1 
ATOM   7468 C  CG1 . VAL D 1 134 ? 26.818  32.583  24.494  1.00 15.69 ? 135 VAL D CG1 1 
ATOM   7469 C  CG2 . VAL D 1 134 ? 27.543  34.097  22.673  1.00 15.79 ? 135 VAL D CG2 1 
ATOM   7470 N  N   . GLN D 1 135 ? 30.309  35.677  24.079  1.00 13.22 ? 136 GLN D N   1 
ATOM   7471 C  CA  . GLN D 1 135 ? 31.537  36.210  23.502  1.00 13.59 ? 136 GLN D CA  1 
ATOM   7472 C  C   . GLN D 1 135 ? 32.697  36.316  24.491  1.00 13.11 ? 136 GLN D C   1 
ATOM   7473 O  O   . GLN D 1 135 ? 33.781  36.880  24.172  1.00 16.78 ? 136 GLN D O   1 
ATOM   7474 C  CB  . GLN D 1 135 ? 31.268  37.570  22.804  1.00 14.75 ? 136 GLN D CB  1 
ATOM   7475 C  CG  . GLN D 1 135 ? 30.203  37.474  21.758  1.00 17.82 ? 136 GLN D CG  1 
ATOM   7476 C  CD  . GLN D 1 135 ? 29.939  38.843  21.113  1.00 24.59 ? 136 GLN D CD  1 
ATOM   7477 O  OE1 . GLN D 1 135 ? 30.889  39.495  20.646  1.00 41.24 ? 136 GLN D OE1 1 
ATOM   7478 N  NE2 . GLN D 1 135 ? 28.679  39.317  21.172  1.00 33.58 ? 136 GLN D NE2 1 
ATOM   7479 N  N   . GLN D 1 136 ? 32.432  35.844  25.718  1.00 11.84 ? 137 GLN D N   1 
ATOM   7480 C  CA  . GLN D 1 136 ? 33.441  36.041  26.797  1.00 11.98 ? 137 GLN D CA  1 
ATOM   7481 C  C   . GLN D 1 136 ? 33.950  34.707  27.298  1.00 11.65 ? 137 GLN D C   1 
ATOM   7482 O  O   . GLN D 1 136 ? 33.176  33.735  27.389  1.00 12.81 ? 137 GLN D O   1 
ATOM   7483 C  CB  . GLN D 1 136 ? 32.878  36.844  27.945  1.00 12.72 ? 137 GLN D CB  1 
ATOM   7484 C  CG  . GLN D 1 136 ? 32.037  38.077  27.561  1.00 18.30 ? 137 GLN D CG  1 
ATOM   7485 C  CD  . GLN D 1 136 ? 32.786  39.065  26.728  1.00 20.63 ? 137 GLN D CD  1 
ATOM   7486 O  OE1 . GLN D 1 136 ? 33.990  39.227  26.890  1.00 19.64 ? 137 GLN D OE1 1 
ATOM   7487 N  NE2 . GLN D 1 136 ? 32.045  39.747  25.796  1.00 23.69 ? 137 GLN D NE2 1 
ATOM   7488 N  N   . PRO D 1 137 ? 35.214  34.649  27.796  1.00 10.75 ? 138 PRO D N   1 
ATOM   7489 C  CA  . PRO D 1 137 ? 35.776  33.356  28.207  1.00 13.41 ? 138 PRO D CA  1 
ATOM   7490 C  C   . PRO D 1 137 ? 35.093  32.805  29.474  1.00 12.51 ? 138 PRO D C   1 
ATOM   7491 O  O   . PRO D 1 137 ? 35.179  31.611  29.714  1.00 13.96 ? 138 PRO D O   1 
ATOM   7492 C  CB  . PRO D 1 137 ? 37.281  33.580  28.337  1.00 18.09 ? 138 PRO D CB  1 
ATOM   7493 C  CG  . PRO D 1 137 ? 37.341  35.027  28.561  1.00 19.24 ? 138 PRO D CG  1 
ATOM   7494 C  CD  . PRO D 1 137 ? 36.248  35.713  27.739  1.00 15.56 ? 138 PRO D CD  1 
ATOM   7495 N  N   . ASP D 1 138 ? 34.468  33.690  30.270  1.00 10.57 ? 139 ASP D N   1 
ATOM   7496 C  CA  . ASP D 1 138 ? 33.797  33.320  31.500  1.00 10.91 ? 139 ASP D CA  1 
ATOM   7497 C  C   . ASP D 1 138 ? 32.310  33.764  31.342  1.00 10.47 ? 139 ASP D C   1 
ATOM   7498 O  O   . ASP D 1 138 ? 31.698  34.149  32.298  1.00 11.11 ? 139 ASP D O   1 
ATOM   7499 C  CB  . ASP D 1 138 ? 34.459  33.962  32.724  1.00 13.03 ? 139 ASP D CB  1 
ATOM   7500 C  CG  . ASP D 1 138 ? 34.477  35.469  32.669  1.00 14.52 ? 139 ASP D CG  1 
ATOM   7501 O  OD1 . ASP D 1 138 ? 34.269  36.084  31.573  1.00 14.10 ? 139 ASP D OD1 1 
ATOM   7502 O  OD2 . ASP D 1 138 ? 34.781  36.056  33.722  1.00 17.63 ? 139 ASP D OD2 1 
ATOM   7503 N  N   . GLY D 1 139 ? 31.744  33.664  30.143  1.00 10.31 ? 140 GLY D N   1 
ATOM   7504 C  CA  . GLY D 1 139 ? 30.411  34.120  29.898  1.00 10.51 ? 140 GLY D CA  1 
ATOM   7505 C  C   . GLY D 1 139 ? 29.304  33.216  30.449  1.00 8.76  ? 140 GLY D C   1 
ATOM   7506 O  O   . GLY D 1 139 ? 28.262  33.724  30.777  1.00 10.08 ? 140 GLY D O   1 
ATOM   7507 N  N   . LEU D 1 140 ? 29.521  31.879  30.417  1.00 9.28  ? 141 LEU D N   1 
ATOM   7508 C  CA  . LEU D 1 140 ? 28.469  30.924  30.748  1.00 9.22  ? 141 LEU D CA  1 
ATOM   7509 C  C   . LEU D 1 140 ? 28.942  29.992  31.826  1.00 8.72  ? 141 LEU D C   1 
ATOM   7510 O  O   . LEU D 1 140 ? 30.121  29.708  31.965  1.00 8.59  ? 141 LEU D O   1 
ATOM   7511 C  CB  . LEU D 1 140 ? 28.037  30.060  29.556  1.00 9.89  ? 141 LEU D CB  1 
ATOM   7512 C  CG  . LEU D 1 140 ? 27.491  30.783  28.314  1.00 11.83 ? 141 LEU D CG  1 
ATOM   7513 C  CD1 . LEU D 1 140 ? 26.965  29.747  27.319  1.00 12.94 ? 141 LEU D CD1 1 
ATOM   7514 C  CD2 . LEU D 1 140 ? 26.361  31.729  28.605  1.00 13.26 ? 141 LEU D CD2 1 
ATOM   7515 N  N   . ALA D 1 141 ? 27.963  29.516  32.599  1.00 8.60  ? 142 ALA D N   1 
ATOM   7516 C  CA  . ALA D 1 141 ? 28.239  28.376  33.497  1.00 8.71  ? 142 ALA D CA  1 
ATOM   7517 C  C   . ALA D 1 141 ? 27.121  27.395  33.175  1.00 8.25  ? 142 ALA D C   1 
ATOM   7518 O  O   . ALA D 1 141 ? 25.945  27.742  33.136  1.00 9.18  ? 142 ALA D O   1 
ATOM   7519 C  CB  . ALA D 1 141 ? 28.133  28.789  34.970  1.00 9.10  ? 142 ALA D CB  1 
ATOM   7520 N  N   . VAL D 1 142 ? 27.513  26.170  32.765  1.00 8.14  ? 143 VAL D N   1 
ATOM   7521 C  CA  . VAL D 1 142 ? 26.567  25.118  32.415  1.00 8.30  ? 143 VAL D CA  1 
ATOM   7522 C  C   . VAL D 1 142 ? 26.681  24.065  33.543  1.00 7.54  ? 143 VAL D C   1 
ATOM   7523 O  O   . VAL D 1 142 ? 27.761  23.516  33.795  1.00 8.75  ? 143 VAL D O   1 
ATOM   7524 C  CB  . VAL D 1 142 ? 26.723  24.538  31.005  1.00 8.69  ? 143 VAL D CB  1 
ATOM   7525 C  CG1 . VAL D 1 142 ? 25.575  23.502  30.775  1.00 9.18  ? 143 VAL D CG1 1 
ATOM   7526 C  CG2 . VAL D 1 142 ? 26.635  25.668  29.969  1.00 9.77  ? 143 VAL D CG2 1 
ATOM   7527 N  N   . LEU D 1 143 ? 25.557  23.811  34.215  1.00 8.21  ? 144 LEU D N   1 
ATOM   7528 C  CA  . LEU D 1 143 ? 25.408  22.730  35.152  1.00 8.16  ? 144 LEU D CA  1 
ATOM   7529 C  C   . LEU D 1 143 ? 24.950  21.477  34.409  1.00 6.77  ? 144 LEU D C   1 
ATOM   7530 O  O   . LEU D 1 143 ? 23.844  21.460  33.864  1.00 8.80  ? 144 LEU D O   1 
ATOM   7531 C  CB  . LEU D 1 143 ? 24.413  23.218  36.263  1.00 9.09  ? 144 LEU D CB  1 
ATOM   7532 C  CG  . LEU D 1 143 ? 24.173  22.194  37.421  1.00 9.52  ? 144 LEU D CG  1 
ATOM   7533 C  CD1 . LEU D 1 143 ? 25.464  21.900  38.178  1.00 11.89 ? 144 LEU D CD1 1 
ATOM   7534 C  CD2 . LEU D 1 143 ? 23.106  22.850  38.314  1.00 11.08 ? 144 LEU D CD2 1 
ATOM   7535 N  N   . GLY D 1 144 ? 25.800  20.451  34.491  1.00 7.72  ? 145 GLY D N   1 
ATOM   7536 C  CA  . GLY D 1 144 ? 25.478  19.183  33.821  1.00 6.82  ? 145 GLY D CA  1 
ATOM   7537 C  C   . GLY D 1 144 ? 25.129  18.112  34.840  1.00 7.37  ? 145 GLY D C   1 
ATOM   7538 O  O   . GLY D 1 144 ? 25.814  17.978  35.833  1.00 8.69  ? 145 GLY D O   1 
ATOM   7539 N  N   . ILE D 1 145 ? 24.082  17.366  34.490  1.00 7.19  ? 146 ILE D N   1 
ATOM   7540 C  CA  . ILE D 1 145 ? 23.572  16.332  35.409  1.00 7.38  ? 146 ILE D CA  1 
ATOM   7541 C  C   . ILE D 1 145 ? 23.331  15.096  34.541  1.00 7.87  ? 146 ILE D C   1 
ATOM   7542 O  O   . ILE D 1 145 ? 22.594  15.130  33.539  1.00 8.42  ? 146 ILE D O   1 
ATOM   7543 C  CB  . ILE D 1 145 ? 22.254  16.812  36.101  1.00 8.48  ? 146 ILE D CB  1 
ATOM   7544 C  CG1 . ILE D 1 145 ? 22.510  18.134  36.862  1.00 10.88 ? 146 ILE D CG1 1 
ATOM   7545 C  CG2 . ILE D 1 145 ? 21.698  15.716  36.993  1.00 10.70 ? 146 ILE D CG2 1 
ATOM   7546 C  CD1 . ILE D 1 145 ? 21.289  18.741  37.509  1.00 11.37 ? 146 ILE D CD1 1 
ATOM   7547 N  N   . PHE D 1 146 ? 23.913  13.979  34.984  1.00 7.35  ? 147 PHE D N   1 
ATOM   7548 C  CA  . PHE D 1 146 ? 23.744  12.705  34.232  1.00 7.36  ? 147 PHE D CA  1 
ATOM   7549 C  C   . PHE D 1 146 ? 22.370  12.103  34.554  1.00 8.05  ? 147 PHE D C   1 
ATOM   7550 O  O   . PHE D 1 146 ? 21.879  12.236  35.672  1.00 9.38  ? 147 PHE D O   1 
ATOM   7551 C  CB  . PHE D 1 146 ? 24.809  11.751  34.644  1.00 8.29  ? 147 PHE D CB  1 
ATOM   7552 C  CG  . PHE D 1 146 ? 26.185  12.189  34.285  1.00 6.94  ? 147 PHE D CG  1 
ATOM   7553 C  CD1 . PHE D 1 146 ? 26.502  12.355  32.945  1.00 7.60  ? 147 PHE D CD1 1 
ATOM   7554 C  CD2 . PHE D 1 146 ? 27.153  12.460  35.201  1.00 8.25  ? 147 PHE D CD2 1 
ATOM   7555 C  CE1 . PHE D 1 146 ? 27.786  12.741  32.543  1.00 7.74  ? 147 PHE D CE1 1 
ATOM   7556 C  CE2 . PHE D 1 146 ? 28.476  12.810  34.829  1.00 7.93  ? 147 PHE D CE2 1 
ATOM   7557 C  CZ  . PHE D 1 146 ? 28.800  12.954  33.467  1.00 7.72  ? 147 PHE D CZ  1 
ATOM   7558 N  N   . LEU D 1 147 ? 21.799  11.383  33.581  1.00 8.01  ? 148 LEU D N   1 
ATOM   7559 C  CA  . LEU D 1 147 ? 20.600  10.566  33.768  1.00 8.49  ? 148 LEU D CA  1 
ATOM   7560 C  C   . LEU D 1 147 ? 20.959  9.089   33.550  1.00 8.65  ? 148 LEU D C   1 
ATOM   7561 O  O   . LEU D 1 147 ? 21.531  8.758   32.526  1.00 9.34  ? 148 LEU D O   1 
ATOM   7562 C  CB  . LEU D 1 147 ? 19.490  10.958  32.766  1.00 9.91  ? 148 LEU D CB  1 
ATOM   7563 C  CG  . LEU D 1 147 ? 18.701  12.232  32.978  1.00 10.54 ? 148 LEU D CG  1 
ATOM   7564 C  CD1 . LEU D 1 147 ? 19.608  13.528  33.096  1.00 10.76 ? 148 LEU D CD1 1 
ATOM   7565 C  CD2 . LEU D 1 147 ? 17.543  12.430  31.980  1.00 10.96 ? 148 LEU D CD2 1 
ATOM   7566 N  N   . LYS D 1 148 ? 20.509  8.262   34.506  1.00 9.36  ? 149 LYS D N   1 
ATOM   7567 C  CA  . LYS D 1 148 ? 20.565  6.835   34.348  1.00 10.20 ? 149 LYS D CA  1 
ATOM   7568 C  C   . LYS D 1 148 ? 19.114  6.321   34.372  1.00 11.16 ? 149 LYS D C   1 
ATOM   7569 O  O   . LYS D 1 148 ? 18.236  6.963   34.935  1.00 11.95 ? 149 LYS D O   1 
ATOM   7570 C  CB  . LYS D 1 148 ? 21.426  6.185   35.456  1.00 11.99 ? 149 LYS D CB  1 
ATOM   7571 C  CG  . LYS D 1 148 ? 20.804  6.280   36.881  1.00 13.54 ? 149 LYS D CG  1 
ATOM   7572 C  CD  . LYS D 1 148 ? 21.722  5.585   37.909  1.00 20.06 ? 149 LYS D CD  1 
ATOM   7573 C  CE  . LYS D 1 148 ? 21.014  5.395   39.245  1.00 24.46 ? 149 LYS D CE  1 
ATOM   7574 N  NZ  . LYS D 1 148 ? 21.847  4.409   40.006  1.00 41.65 ? 149 LYS D NZ  1 
ATOM   7575 N  N   . VAL D 1 149 ? 18.901  5.151   33.783  1.00 10.93 ? 150 VAL D N   1 
ATOM   7576 C  CA  . VAL D 1 149 ? 17.577  4.599   33.727  1.00 12.27 ? 150 VAL D CA  1 
ATOM   7577 C  C   . VAL D 1 149 ? 17.341  3.709   34.972  1.00 13.37 ? 150 VAL D C   1 
ATOM   7578 O  O   . VAL D 1 149 ? 18.082  2.748   35.216  1.00 13.39 ? 150 VAL D O   1 
ATOM   7579 C  CB  . VAL D 1 149 ? 17.390  3.828   32.384  1.00 13.86 ? 150 VAL D CB  1 
ATOM   7580 C  CG1 . VAL D 1 149 ? 16.097  3.043   32.376  1.00 15.14 ? 150 VAL D CG1 1 
ATOM   7581 C  CG2 . VAL D 1 149 ? 17.399  4.821   31.253  1.00 15.30 ? 150 VAL D CG2 1 
ATOM   7582 N  N   . GLY D 1 150 ? 16.258  3.948   35.692  1.00 12.90 ? 151 GLY D N   1 
ATOM   7583 C  CA  . GLY D 1 150 ? 15.884  3.145   36.873  1.00 14.66 ? 151 GLY D CA  1 
ATOM   7584 C  C   . GLY D 1 150 ? 14.547  3.647   37.288  1.00 13.03 ? 151 GLY D C   1 
ATOM   7585 O  O   . GLY D 1 150 ? 13.578  3.574   36.493  1.00 14.23 ? 151 GLY D O   1 
ATOM   7586 N  N   A SER D 1 151 ? 14.449  4.153   38.519  0.50 13.55 ? 152 SER D N   1 
ATOM   7587 N  N   B SER D 1 151 ? 14.459  4.158   38.519  0.50 13.67 ? 152 SER D N   1 
ATOM   7588 C  CA  A SER D 1 151 ? 13.160  4.696   39.014  0.50 14.36 ? 152 SER D CA  1 
ATOM   7589 C  CA  B SER D 1 151 ? 13.184  4.746   38.997  0.50 14.63 ? 152 SER D CA  1 
ATOM   7590 C  C   A SER D 1 151 ? 12.840  6.043   38.328  0.50 13.67 ? 152 SER D C   1 
ATOM   7591 C  C   B SER D 1 151 ? 12.838  5.995   38.180  0.50 14.47 ? 152 SER D C   1 
ATOM   7592 O  O   A SER D 1 151 ? 13.770  6.772   37.924  0.50 13.57 ? 152 SER D O   1 
ATOM   7593 O  O   B SER D 1 151 ? 13.726  6.600   37.552  0.50 13.56 ? 152 SER D O   1 
ATOM   7594 C  CB  A SER D 1 151 ? 13.246  4.898   40.509  0.50 17.72 ? 152 SER D CB  1 
ATOM   7595 C  CB  B SER D 1 151 ? 13.291  5.151   40.449  0.50 17.30 ? 152 SER D CB  1 
ATOM   7596 O  OG  A SER D 1 151 ? 14.185  5.925   40.787  0.50 19.81 ? 152 SER D OG  1 
ATOM   7597 O  OG  B SER D 1 151 ? 13.766  4.094   41.233  0.50 20.69 ? 152 SER D OG  1 
ATOM   7598 N  N   . ALA D 1 152 ? 11.551  6.323   38.107  1.00 13.42 ? 153 ALA D N   1 
ATOM   7599 C  CA  . ALA D 1 152 ? 11.134  7.557   37.518  1.00 13.71 ? 153 ALA D CA  1 
ATOM   7600 C  C   . ALA D 1 152 ? 11.557  8.764   38.288  1.00 14.07 ? 153 ALA D C   1 
ATOM   7601 O  O   . ALA D 1 152 ? 11.727  8.721   39.500  1.00 15.20 ? 153 ALA D O   1 
ATOM   7602 C  CB  . ALA D 1 152 ? 9.608   7.555   37.367  1.00 15.01 ? 153 ALA D CB  1 
ATOM   7603 N  N   . LYS D 1 153 ? 11.733  9.869   37.556  1.00 12.55 ? 154 LYS D N   1 
ATOM   7604 C  CA  . LYS D 1 153 ? 12.014  11.191  38.161  1.00 13.92 ? 154 LYS D CA  1 
ATOM   7605 C  C   . LYS D 1 153 ? 10.689  12.005  38.105  1.00 11.26 ? 154 LYS D C   1 
ATOM   7606 O  O   . LYS D 1 153 ? 10.234  12.418  37.035  1.00 12.46 ? 154 LYS D O   1 
ATOM   7607 C  CB  . LYS D 1 153 ? 13.116  11.954  37.384  1.00 13.35 ? 154 LYS D CB  1 
ATOM   7608 C  CG  . LYS D 1 153 ? 13.568  13.212  38.044  1.00 13.74 ? 154 LYS D CG  1 
ATOM   7609 C  CD  . LYS D 1 153 ? 14.380  12.846  39.306  1.00 14.58 ? 154 LYS D CD  1 
ATOM   7610 C  CE  . LYS D 1 153 ? 15.223  14.054  39.667  1.00 15.46 ? 154 LYS D CE  1 
ATOM   7611 N  NZ  . LYS D 1 153 ? 15.810  13.713  40.986  1.00 15.68 ? 154 LYS D NZ  1 
ATOM   7612 N  N   . PRO D 1 154 ? 9.993   12.058  39.213  1.00 12.61 ? 155 PRO D N   1 
ATOM   7613 C  CA  . PRO D 1 154 ? 8.624   12.629  39.173  1.00 13.68 ? 155 PRO D CA  1 
ATOM   7614 C  C   . PRO D 1 154 ? 8.633   14.111  38.639  1.00 13.95 ? 155 PRO D C   1 
ATOM   7615 O  O   . PRO D 1 154 ? 7.748   14.504  37.847  1.00 16.12 ? 155 PRO D O   1 
ATOM   7616 C  CB  . PRO D 1 154 ? 8.186   12.583  40.654  1.00 15.74 ? 155 PRO D CB  1 
ATOM   7617 C  CG  . PRO D 1 154 ? 9.012   11.543  41.275  1.00 21.33 ? 155 PRO D CG  1 
ATOM   7618 C  CD  . PRO D 1 154 ? 10.341  11.562  40.571  1.00 13.70 ? 155 PRO D CD  1 
ATOM   7619 N  N   . GLY D 1 155 ? 9.705   14.860  38.950  1.00 12.78 ? 156 GLY D N   1 
ATOM   7620 C  CA  . GLY D 1 155 ? 9.870   16.255  38.533  1.00 14.23 ? 156 GLY D CA  1 
ATOM   7621 C  C   . GLY D 1 155 ? 10.123  16.397  37.051  1.00 15.29 ? 156 GLY D C   1 
ATOM   7622 O  O   . GLY D 1 155 ? 10.044  17.516  36.531  1.00 17.90 ? 156 GLY D O   1 
ATOM   7623 N  N   . LEU D 1 156 ? 10.444  15.328  36.334  1.00 12.62 ? 157 LEU D N   1 
ATOM   7624 C  CA  . LEU D 1 156 ? 10.623  15.326  34.890  1.00 13.37 ? 157 LEU D CA  1 
ATOM   7625 C  C   . LEU D 1 156 ? 9.300   15.162  34.127  1.00 10.52 ? 157 LEU D C   1 
ATOM   7626 O  O   . LEU D 1 156 ? 9.202   15.430  32.905  1.00 12.04 ? 157 LEU D O   1 
ATOM   7627 C  CB  . LEU D 1 156 ? 11.636  14.218  34.496  1.00 13.66 ? 157 LEU D CB  1 
ATOM   7628 C  CG  . LEU D 1 156 ? 11.992  14.103  32.989  1.00 13.29 ? 157 LEU D CG  1 
ATOM   7629 C  CD1 . LEU D 1 156 ? 12.610  15.433  32.527  1.00 15.46 ? 157 LEU D CD1 1 
ATOM   7630 C  CD2 . LEU D 1 156 ? 12.993  12.959  32.848  1.00 13.65 ? 157 LEU D CD2 1 
ATOM   7631 N  N   . GLN D 1 157 ? 8.304   14.583  34.792  1.00 13.49 ? 158 GLN D N   1 
ATOM   7632 C  CA  . GLN D 1 157 ? 7.089   14.138  34.062  1.00 13.90 ? 158 GLN D CA  1 
ATOM   7633 C  C   . GLN D 1 157 ? 6.341   15.264  33.329  1.00 13.32 ? 158 GLN D C   1 
ATOM   7634 O  O   . GLN D 1 157 ? 5.902   15.056  32.207  1.00 13.90 ? 158 GLN D O   1 
ATOM   7635 C  CB  . GLN D 1 157 ? 6.199   13.285  34.972  1.00 14.81 ? 158 GLN D CB  1 
ATOM   7636 C  CG  . GLN D 1 157 ? 5.107   12.584  34.165  1.00 16.72 ? 158 GLN D CG  1 
ATOM   7637 C  CD  . GLN D 1 157 ? 5.662   11.538  33.214  1.00 16.26 ? 158 GLN D CD  1 
ATOM   7638 O  OE1 . GLN D 1 157 ? 6.779   10.937  33.447  1.00 14.96 ? 158 GLN D OE1 1 
ATOM   7639 N  NE2 . GLN D 1 157 ? 4.978   11.345  32.082  1.00 16.35 ? 158 GLN D NE2 1 
ATOM   7640 N  N   . LYS D 1 158 ? 6.319   16.493  33.902  1.00 13.96 ? 159 LYS D N   1 
ATOM   7641 C  CA  . LYS D 1 158 ? 5.719   17.614  33.215  1.00 14.84 ? 159 LYS D CA  1 
ATOM   7642 C  C   . LYS D 1 158 ? 6.329   17.883  31.825  1.00 14.20 ? 159 LYS D C   1 
ATOM   7643 O  O   . LYS D 1 158 ? 5.671   18.207  30.843  1.00 15.14 ? 159 LYS D O   1 
ATOM   7644 C  CB  . LYS D 1 158 ? 5.650   18.796  34.139  1.00 17.96 ? 159 LYS D CB  1 
ATOM   7645 C  CG  . LYS D 1 158 ? 4.521   18.557  35.149  1.00 25.42 ? 159 LYS D CG  1 
ATOM   7646 C  CD  . LYS D 1 158 ? 4.116   19.838  35.901  1.00 40.40 ? 159 LYS D CD  1 
ATOM   7647 C  CE  . LYS D 1 158 ? 3.158   19.545  37.069  1.00 44.31 ? 159 LYS D CE  1 
ATOM   7648 N  NZ  . LYS D 1 158 ? 3.006   20.609  38.152  1.00 41.49 ? 159 LYS D NZ  1 
ATOM   7649 N  N   . VAL D 1 159 ? 7.693   17.765  31.770  1.00 11.96 ? 160 VAL D N   1 
ATOM   7650 C  CA  . VAL D 1 159 ? 8.420   17.868  30.520  1.00 12.66 ? 160 VAL D CA  1 
ATOM   7651 C  C   . VAL D 1 159 ? 7.966   16.753  29.548  1.00 10.96 ? 160 VAL D C   1 
ATOM   7652 O  O   . VAL D 1 159 ? 7.622   16.989  28.364  1.00 13.43 ? 160 VAL D O   1 
ATOM   7653 C  CB  . VAL D 1 159 ? 9.950   17.890  30.753  1.00 11.95 ? 160 VAL D CB  1 
ATOM   7654 C  CG1 . VAL D 1 159 ? 10.667  17.838  29.390  1.00 14.57 ? 160 VAL D CG1 1 
ATOM   7655 C  CG2 . VAL D 1 159 ? 10.326  19.127  31.596  1.00 16.30 ? 160 VAL D CG2 1 
ATOM   7656 N  N   . VAL D 1 160 ? 8.051   15.506  30.019  1.00 11.79 ? 161 VAL D N   1 
ATOM   7657 C  CA  . VAL D 1 160 ? 7.754   14.318  29.218  1.00 15.88 ? 161 VAL D CA  1 
ATOM   7658 C  C   . VAL D 1 160 ? 6.378   14.427  28.638  1.00 12.93 ? 161 VAL D C   1 
ATOM   7659 O  O   . VAL D 1 160 ? 6.175   14.184  27.450  1.00 15.98 ? 161 VAL D O   1 
ATOM   7660 C  CB  . VAL D 1 160 ? 7.864   12.995  30.128  1.00 16.43 ? 161 VAL D CB  1 
ATOM   7661 C  CG1 . VAL D 1 160 ? 7.185   11.799  29.456  1.00 17.39 ? 161 VAL D CG1 1 
ATOM   7662 C  CG2 . VAL D 1 160 ? 9.295   12.804  30.543  1.00 19.08 ? 161 VAL D CG2 1 
ATOM   7663 N  N   . ASP D 1 161 ? 5.426   14.890  29.431  1.00 15.39 ? 162 ASP D N   1 
ATOM   7664 C  CA  . ASP D 1 161 ? 4.040   14.908  28.916  1.00 16.23 ? 162 ASP D CA  1 
ATOM   7665 C  C   . ASP D 1 161 ? 3.756   15.966  27.855  1.00 17.66 ? 162 ASP D C   1 
ATOM   7666 O  O   . ASP D 1 161 ? 2.719   15.848  27.205  1.00 20.68 ? 162 ASP D O   1 
ATOM   7667 C  CB  . ASP D 1 161 ? 3.165   15.098  30.131  1.00 21.72 ? 162 ASP D CB  1 
ATOM   7668 C  CG  . ASP D 1 161 ? 2.919   13.729  30.893  1.00 21.42 ? 162 ASP D CG  1 
ATOM   7669 O  OD1 . ASP D 1 161 ? 3.004   12.638  30.233  1.00 24.66 ? 162 ASP D OD1 1 
ATOM   7670 O  OD2 . ASP D 1 161 ? 2.663   13.741  32.074  1.00 29.12 ? 162 ASP D OD2 1 
ATOM   7671 N  N   . VAL D 1 162 ? 4.579   17.013  27.703  1.00 14.21 ? 163 VAL D N   1 
ATOM   7672 C  CA  . VAL D 1 162 ? 4.352   18.040  26.670  1.00 15.23 ? 163 VAL D CA  1 
ATOM   7673 C  C   . VAL D 1 162 ? 5.045   17.707  25.371  1.00 14.38 ? 163 VAL D C   1 
ATOM   7674 O  O   . VAL D 1 162 ? 4.828   18.389  24.358  1.00 15.61 ? 163 VAL D O   1 
ATOM   7675 C  CB  . VAL D 1 162 ? 4.786   19.464  27.247  1.00 19.01 ? 163 VAL D CB  1 
ATOM   7676 C  CG1 . VAL D 1 162 ? 6.245   19.715  27.158  1.00 16.61 ? 163 VAL D CG1 1 
ATOM   7677 C  CG2 . VAL D 1 162 ? 3.923   20.669  26.886  1.00 23.36 ? 163 VAL D CG2 1 
ATOM   7678 N  N   . LEU D 1 163 ? 5.947   16.672  25.361  1.00 13.49 ? 164 LEU D N   1 
ATOM   7679 C  CA  . LEU D 1 163 ? 6.736   16.458  24.168  1.00 15.23 ? 164 LEU D CA  1 
ATOM   7680 C  C   . LEU D 1 163 ? 5.864   16.102  22.974  1.00 14.42 ? 164 LEU D C   1 
ATOM   7681 O  O   . LEU D 1 163 ? 6.256   16.392  21.841  1.00 15.40 ? 164 LEU D O   1 
ATOM   7682 C  CB  . LEU D 1 163 ? 7.773   15.408  24.425  1.00 13.40 ? 164 LEU D CB  1 
ATOM   7683 C  CG  . LEU D 1 163 ? 8.806   15.727  25.508  1.00 13.20 ? 164 LEU D CG  1 
ATOM   7684 C  CD1 . LEU D 1 163 ? 9.797   14.566  25.651  1.00 14.57 ? 164 LEU D CD1 1 
ATOM   7685 C  CD2 . LEU D 1 163 ? 9.508   17.043  25.213  1.00 12.28 ? 164 LEU D CD2 1 
ATOM   7686 N  N   . ASP D 1 164 ? 4.712   15.433  23.218  1.00 18.14 ? 165 ASP D N   1 
ATOM   7687 C  CA  . ASP D 1 164 ? 3.843   15.064  22.051  1.00 20.28 ? 165 ASP D CA  1 
ATOM   7688 C  C   . ASP D 1 164 ? 3.365   16.340  21.295  1.00 18.26 ? 165 ASP D C   1 
ATOM   7689 O  O   . ASP D 1 164 ? 3.023   16.282  20.116  1.00 24.72 ? 165 ASP D O   1 
ATOM   7690 C  CB  . ASP D 1 164 ? 2.682   14.156  22.467  1.00 26.22 ? 165 ASP D CB  1 
ATOM   7691 C  CG  . ASP D 1 164 ? 1.604   14.922  23.182  1.00 32.00 ? 165 ASP D CG  1 
ATOM   7692 O  OD1 . ASP D 1 164 ? 1.952   15.638  24.164  1.00 43.33 ? 165 ASP D OD1 1 
ATOM   7693 O  OD2 . ASP D 1 164 ? 0.397   14.807  22.767  1.00 79.41 ? 165 ASP D OD2 1 
ATOM   7694 N  N   . SER D 1 165 ? 3.351   17.486  21.952  1.00 16.62 ? 166 SER D N   1 
ATOM   7695 C  CA  . SER D 1 165 ? 2.918   18.702  21.283  1.00 17.60 ? 166 SER D CA  1 
ATOM   7696 C  C   . SER D 1 165 ? 4.048   19.432  20.525  1.00 17.72 ? 166 SER D C   1 
ATOM   7697 O  O   . SER D 1 165 ? 3.801   20.424  19.834  1.00 17.04 ? 166 SER D O   1 
ATOM   7698 C  CB  . SER D 1 165 ? 2.293   19.622  22.257  1.00 19.38 ? 166 SER D CB  1 
ATOM   7699 O  OG  . SER D 1 165 ? 3.304   20.231  23.079  1.00 19.84 ? 166 SER D OG  1 
ATOM   7700 N  N   . ILE D 1 166 ? 5.303   18.996  20.680  1.00 14.13 ? 167 ILE D N   1 
ATOM   7701 C  CA  . ILE D 1 166 ? 6.430   19.630  19.958  1.00 14.57 ? 167 ILE D CA  1 
ATOM   7702 C  C   . ILE D 1 166 ? 7.235   18.541  19.248  1.00 15.12 ? 167 ILE D C   1 
ATOM   7703 O  O   . ILE D 1 166 ? 8.501   18.529  19.258  1.00 14.41 ? 167 ILE D O   1 
ATOM   7704 C  CB  . ILE D 1 166 ? 7.323   20.482  20.932  1.00 14.15 ? 167 ILE D CB  1 
ATOM   7705 C  CG1 . ILE D 1 166 ? 7.864   19.601  22.093  1.00 12.82 ? 167 ILE D CG1 1 
ATOM   7706 C  CG2 . ILE D 1 166 ? 6.538   21.698  21.446  1.00 17.00 ? 167 ILE D CG2 1 
ATOM   7707 C  CD1 . ILE D 1 166 ? 9.109   20.254  22.713  1.00 14.02 ? 167 ILE D CD1 1 
ATOM   7708 N  N   . LYS D 1 167 ? 6.511   17.621  18.587  1.00 15.14 ? 168 LYS D N   1 
ATOM   7709 C  CA  . LYS D 1 167 ? 7.189   16.497  18.020  1.00 14.30 ? 168 LYS D CA  1 
ATOM   7710 C  C   . LYS D 1 167 ? 8.272   16.832  16.935  1.00 15.08 ? 168 LYS D C   1 
ATOM   7711 O  O   . LYS D 1 167 ? 9.313   16.140  16.887  1.00 14.63 ? 168 LYS D O   1 
ATOM   7712 C  CB  . LYS D 1 167 ? 6.147   15.516  17.448  1.00 17.53 ? 168 LYS D CB  1 
ATOM   7713 C  CG  . LYS D 1 167 ? 6.728   14.183  16.983  1.00 19.07 ? 168 LYS D CG  1 
ATOM   7714 C  CD  . LYS D 1 167 ? 5.607   13.356  16.325  1.00 26.82 ? 168 LYS D CD  1 
ATOM   7715 C  CE  . LYS D 1 167 ? 6.234   12.118  15.702  1.00 38.24 ? 168 LYS D CE  1 
ATOM   7716 N  NZ  . LYS D 1 167 ? 5.211   11.226  15.089  1.00 37.03 ? 168 LYS D NZ  1 
ATOM   7717 N  N   . THR D 1 168 ? 8.026   17.886  16.077  1.00 14.66 ? 169 THR D N   1 
ATOM   7718 C  CA  . THR D 1 168 ? 8.928   18.135  14.933  1.00 14.20 ? 169 THR D CA  1 
ATOM   7719 C  C   . THR D 1 168 ? 9.625   19.497  15.101  1.00 14.06 ? 169 THR D C   1 
ATOM   7720 O  O   . THR D 1 168 ? 9.122   20.357  15.828  1.00 14.82 ? 169 THR D O   1 
ATOM   7721 C  CB  . THR D 1 168 ? 8.134   18.044  13.639  1.00 17.09 ? 169 THR D CB  1 
ATOM   7722 O  OG1 . THR D 1 168 ? 6.972   18.861  13.760  1.00 19.06 ? 169 THR D OG1 1 
ATOM   7723 C  CG2 . THR D 1 168 ? 7.689   16.555  13.407  1.00 17.62 ? 169 THR D CG2 1 
ATOM   7724 N  N   A LYS D 1 169 ? 10.747  19.654  14.413  0.50 15.42 ? 170 LYS D N   1 
ATOM   7725 N  N   B LYS D 1 169 ? 10.732  19.666  14.392  0.50 15.51 ? 170 LYS D N   1 
ATOM   7726 C  CA  A LYS D 1 169 ? 11.507  20.892  14.334  0.50 13.12 ? 170 LYS D CA  1 
ATOM   7727 C  CA  B LYS D 1 169 ? 11.486  20.905  14.320  0.50 13.26 ? 170 LYS D CA  1 
ATOM   7728 C  C   A LYS D 1 169 ? 10.639  22.093  14.064  0.50 15.65 ? 170 LYS D C   1 
ATOM   7729 C  C   B LYS D 1 169 ? 10.620  22.103  14.064  0.50 16.08 ? 170 LYS D C   1 
ATOM   7730 O  O   A LYS D 1 169 ? 9.831   22.092  13.111  0.50 18.33 ? 170 LYS D O   1 
ATOM   7731 O  O   B LYS D 1 169 ? 9.810   22.122  13.115  0.50 18.92 ? 170 LYS D O   1 
ATOM   7732 C  CB  A LYS D 1 169 ? 12.562  20.759  13.241  0.50 14.53 ? 170 LYS D CB  1 
ATOM   7733 C  CB  B LYS D 1 169 ? 12.534  20.797  13.220  0.50 14.99 ? 170 LYS D CB  1 
ATOM   7734 C  CG  A LYS D 1 169 ? 13.428  21.995  13.100  0.50 15.41 ? 170 LYS D CG  1 
ATOM   7735 C  CG  B LYS D 1 169 ? 13.379  22.053  13.086  0.50 16.01 ? 170 LYS D CG  1 
ATOM   7736 C  CD  A LYS D 1 169 ? 14.442  21.812  11.989  0.50 16.65 ? 170 LYS D CD  1 
ATOM   7737 C  CD  B LYS D 1 169 ? 14.543  21.809  12.148  0.50 16.95 ? 170 LYS D CD  1 
ATOM   7738 C  CE  A LYS D 1 169 ? 15.342  23.034  11.878  0.50 22.76 ? 170 LYS D CE  1 
ATOM   7739 C  CE  B LYS D 1 169 ? 14.076  21.743  10.715  0.50 23.80 ? 170 LYS D CE  1 
ATOM   7740 N  NZ  A LYS D 1 169 ? 15.464  23.386  10.447  0.50 29.41 ? 170 LYS D NZ  1 
ATOM   7741 N  NZ  B LYS D 1 169 ? 15.146  21.114  9.872   0.50 30.49 ? 170 LYS D NZ  1 
ATOM   7742 N  N   . GLY D 1 170 ? 10.741  23.091  14.948  1.00 13.97 ? 171 GLY D N   1 
ATOM   7743 C  CA  . GLY D 1 170 ? 10.052  24.376  14.801  1.00 17.84 ? 171 GLY D CA  1 
ATOM   7744 C  C   . GLY D 1 170 ? 8.848   24.474  15.686  1.00 17.12 ? 171 GLY D C   1 
ATOM   7745 O  O   . GLY D 1 170 ? 8.253   25.574  15.811  1.00 21.35 ? 171 GLY D O   1 
ATOM   7746 N  N   . LYS D 1 171 ? 8.358   23.344  16.224  1.00 15.74 ? 172 LYS D N   1 
ATOM   7747 C  CA  . LYS D 1 171 ? 7.198   23.430  17.088  1.00 12.22 ? 172 LYS D CA  1 
ATOM   7748 C  C   . LYS D 1 171 ? 7.533   23.902  18.447  1.00 13.37 ? 172 LYS D C   1 
ATOM   7749 O  O   . LYS D 1 171 ? 8.588   23.524  19.015  1.00 14.56 ? 172 LYS D O   1 
ATOM   7750 C  CB  . LYS D 1 171 ? 6.380   22.139  17.180  1.00 13.09 ? 172 LYS D CB  1 
ATOM   7751 C  CG  . LYS D 1 171 ? 5.868   21.728  15.792  1.00 18.75 ? 172 LYS D CG  1 
ATOM   7752 C  CD  . LYS D 1 171 ? 4.835   20.605  15.911  1.00 21.96 ? 172 LYS D CD  1 
ATOM   7753 C  CE  . LYS D 1 171 ? 3.381   21.092  15.921  1.00 41.14 ? 172 LYS D CE  1 
ATOM   7754 N  NZ  . LYS D 1 171 ? 2.505   20.039  16.557  1.00 42.49 ? 172 LYS D NZ  1 
ATOM   7755 N  N   . SER D 1 172 ? 6.697   24.765  19.017  1.00 14.70 ? 173 SER D N   1 
ATOM   7756 C  CA  . SER D 1 172 ? 6.899   25.259  20.343  1.00 13.89 ? 173 SER D CA  1 
ATOM   7757 C  C   . SER D 1 172 ? 5.590   25.272  21.101  1.00 14.93 ? 173 SER D C   1 
ATOM   7758 O  O   . SER D 1 172 ? 4.485   25.272  20.488  1.00 16.10 ? 173 SER D O   1 
ATOM   7759 C  CB  . SER D 1 172 ? 7.606   26.643  20.326  1.00 13.21 ? 173 SER D CB  1 
ATOM   7760 O  OG  . SER D 1 172 ? 6.733   27.672  19.823  1.00 18.17 ? 173 SER D OG  1 
ATOM   7761 N  N   . ALA D 1 173 ? 5.618   25.403  22.412  1.00 13.36 ? 174 ALA D N   1 
ATOM   7762 C  CA  . ALA D 1 173 ? 4.454   25.567  23.271  1.00 15.42 ? 174 ALA D CA  1 
ATOM   7763 C  C   . ALA D 1 173 ? 4.745   26.440  24.411  1.00 14.70 ? 174 ALA D C   1 
ATOM   7764 O  O   . ALA D 1 173 ? 5.907   26.462  24.891  1.00 14.46 ? 174 ALA D O   1 
ATOM   7765 C  CB  . ALA D 1 173 ? 4.009   24.209  23.751  1.00 18.41 ? 174 ALA D CB  1 
ATOM   7766 N  N   A ASP D 1 174 ? 3.651   26.886  25.044  0.50 20.13 ? 175 ASP D N   1 
ATOM   7767 N  N   B ASP D 1 174 ? 3.816   27.300  24.867  0.50 13.19 ? 175 ASP D N   1 
ATOM   7768 C  CA  A ASP D 1 174 ? 3.744   27.568  26.287  0.50 16.52 ? 175 ASP D CA  1 
ATOM   7769 C  CA  B ASP D 1 174 ? 4.018   27.858  26.213  0.50 14.51 ? 175 ASP D CA  1 
ATOM   7770 C  C   A ASP D 1 174 ? 4.114   26.630  27.443  0.50 16.05 ? 175 ASP D C   1 
ATOM   7771 C  C   B ASP D 1 174 ? 4.256   26.755  27.274  0.50 13.67 ? 175 ASP D C   1 
ATOM   7772 O  O   A ASP D 1 174 ? 3.641   25.493  27.519  0.50 20.51 ? 175 ASP D O   1 
ATOM   7773 O  O   B ASP D 1 174 ? 3.812   25.640  27.112  0.50 12.98 ? 175 ASP D O   1 
ATOM   7774 C  CB  A ASP D 1 174 ? 2.474   28.444  26.525  0.50 21.55 ? 175 ASP D CB  1 
ATOM   7775 C  CB  B ASP D 1 174 ? 2.908   28.880  26.625  0.50 15.87 ? 175 ASP D CB  1 
ATOM   7776 C  CG  A ASP D 1 174 ? 2.397   29.653  25.556  0.50 21.73 ? 175 ASP D CG  1 
ATOM   7777 C  CG  B ASP D 1 174 ? 1.560   28.218  26.924  0.50 19.09 ? 175 ASP D CG  1 
ATOM   7778 O  OD1 A ASP D 1 174 ? 3.303   30.503  25.636  0.50 37.53 ? 175 ASP D OD1 1 
ATOM   7779 O  OD1 B ASP D 1 174 ? 1.314   27.721  28.056  0.50 20.02 ? 175 ASP D OD1 1 
ATOM   7780 O  OD2 A ASP D 1 174 ? 1.441   29.774  24.712  0.50 28.77 ? 175 ASP D OD2 1 
ATOM   7781 O  OD2 B ASP D 1 174 ? 0.718   28.267  26.014  0.50 26.51 ? 175 ASP D OD2 1 
ATOM   7782 N  N   . PHE D 1 175 ? 5.036   27.039  28.317  1.00 15.36 ? 176 PHE D N   1 
ATOM   7783 C  CA  . PHE D 1 175 ? 5.470   26.033  29.297  1.00 14.31 ? 176 PHE D CA  1 
ATOM   7784 C  C   . PHE D 1 175 ? 5.829   26.770  30.533  1.00 14.44 ? 176 PHE D C   1 
ATOM   7785 O  O   . PHE D 1 175 ? 6.999   27.071  30.766  1.00 15.70 ? 176 PHE D O   1 
ATOM   7786 C  CB  . PHE D 1 175 ? 6.676   25.228  28.754  1.00 15.46 ? 176 PHE D CB  1 
ATOM   7787 C  CG  . PHE D 1 175 ? 6.969   23.980  29.550  1.00 14.10 ? 176 PHE D CG  1 
ATOM   7788 C  CD1 . PHE D 1 175 ? 6.085   22.935  29.557  1.00 17.24 ? 176 PHE D CD1 1 
ATOM   7789 C  CD2 . PHE D 1 175 ? 8.114   23.844  30.322  1.00 14.62 ? 176 PHE D CD2 1 
ATOM   7790 C  CE1 . PHE D 1 175 ? 6.320   21.734  30.238  1.00 15.70 ? 176 PHE D CE1 1 
ATOM   7791 C  CE2 . PHE D 1 175 ? 8.404   22.621  31.008  1.00 14.46 ? 176 PHE D CE2 1 
ATOM   7792 C  CZ  . PHE D 1 175 ? 7.483   21.576  31.006  1.00 15.77 ? 176 PHE D CZ  1 
ATOM   7793 N  N   . THR D 1 176 ? 4.825   27.161  31.323  1.00 14.96 ? 177 THR D N   1 
ATOM   7794 C  CA  . THR D 1 176 ? 4.980   27.987  32.505  1.00 14.70 ? 177 THR D CA  1 
ATOM   7795 C  C   . THR D 1 176 ? 4.939   27.185  33.805  1.00 11.79 ? 177 THR D C   1 
ATOM   7796 O  O   . THR D 1 176 ? 4.485   26.017  33.832  1.00 13.43 ? 177 THR D O   1 
ATOM   7797 C  CB  . THR D 1 176 ? 3.861   29.127  32.598  1.00 15.83 ? 177 THR D CB  1 
ATOM   7798 O  OG1 . THR D 1 176 ? 2.584   28.461  32.549  1.00 17.50 ? 177 THR D OG1 1 
ATOM   7799 C  CG2 . THR D 1 176 ? 4.050   30.188  31.464  1.00 18.83 ? 177 THR D CG2 1 
ATOM   7800 N  N   . ASN D 1 177 ? 5.549   27.714  34.841  1.00 11.39 ? 178 ASN D N   1 
ATOM   7801 C  CA  . ASN D 1 177 ? 5.523   27.206  36.201  1.00 12.43 ? 178 ASN D CA  1 
ATOM   7802 C  C   . ASN D 1 177 ? 6.297   25.874  36.339  1.00 15.26 ? 178 ASN D C   1 
ATOM   7803 O  O   . ASN D 1 177 ? 5.976   25.101  37.264  1.00 17.46 ? 178 ASN D O   1 
ATOM   7804 C  CB  . ASN D 1 177 ? 4.077   27.071  36.802  1.00 13.93 ? 178 ASN D CB  1 
ATOM   7805 C  CG  . ASN D 1 177 ? 3.423   28.418  36.868  1.00 14.63 ? 178 ASN D CG  1 
ATOM   7806 O  OD1 . ASN D 1 177 ? 3.808   29.236  37.695  1.00 18.26 ? 178 ASN D OD1 1 
ATOM   7807 N  ND2 . ASN D 1 177 ? 2.532   28.702  35.932  1.00 14.26 ? 178 ASN D ND2 1 
ATOM   7808 N  N   . PHE D 1 178 ? 7.222   25.570  35.445  1.00 12.38 ? 179 PHE D N   1 
ATOM   7809 C  CA  . PHE D 1 178 ? 8.052   24.366  35.604  1.00 11.79 ? 179 PHE D CA  1 
ATOM   7810 C  C   . PHE D 1 178 ? 9.153   24.683  36.588  1.00 12.16 ? 179 PHE D C   1 
ATOM   7811 O  O   . PHE D 1 178 ? 9.890   25.642  36.438  1.00 13.09 ? 179 PHE D O   1 
ATOM   7812 C  CB  . PHE D 1 178 ? 8.606   23.928  34.307  1.00 14.22 ? 179 PHE D CB  1 
ATOM   7813 C  CG  . PHE D 1 178 ? 9.413   22.676  34.480  1.00 12.92 ? 179 PHE D CG  1 
ATOM   7814 C  CD1 . PHE D 1 178 ? 8.798   21.448  34.692  1.00 16.65 ? 179 PHE D CD1 1 
ATOM   7815 C  CD2 . PHE D 1 178 ? 10.821  22.754  34.671  1.00 12.97 ? 179 PHE D CD2 1 
ATOM   7816 C  CE1 . PHE D 1 178 ? 9.535   20.292  34.928  1.00 14.23 ? 179 PHE D CE1 1 
ATOM   7817 C  CE2 . PHE D 1 178 ? 11.558  21.584  34.906  1.00 12.22 ? 179 PHE D CE2 1 
ATOM   7818 C  CZ  . PHE D 1 178 ? 10.933  20.385  35.072  1.00 12.58 ? 179 PHE D CZ  1 
ATOM   7819 N  N   . ASP D 1 179 ? 9.278   23.870  37.627  1.00 12.80 ? 180 ASP D N   1 
ATOM   7820 C  CA  . ASP D 1 179 ? 10.286  24.047  38.688  1.00 13.11 ? 180 ASP D CA  1 
ATOM   7821 C  C   . ASP D 1 179 ? 11.525  23.170  38.479  1.00 12.45 ? 180 ASP D C   1 
ATOM   7822 O  O   . ASP D 1 179 ? 11.505  21.940  38.676  1.00 12.63 ? 180 ASP D O   1 
ATOM   7823 C  CB  . ASP D 1 179 ? 9.654   23.717  40.043  1.00 13.81 ? 180 ASP D CB  1 
ATOM   7824 C  CG  . ASP D 1 179 ? 10.548  24.085  41.216  1.00 16.70 ? 180 ASP D CG  1 
ATOM   7825 O  OD1 . ASP D 1 179 ? 11.758  24.311  41.001  1.00 14.65 ? 180 ASP D OD1 1 
ATOM   7826 O  OD2 . ASP D 1 179 ? 10.038  24.146  42.355  1.00 25.21 ? 180 ASP D OD2 1 
ATOM   7827 N  N   . PRO D 1 180 ? 12.649  23.796  38.049  1.00 12.18 ? 181 PRO D N   1 
ATOM   7828 C  CA  . PRO D 1 180 ? 13.822  22.946  37.752  1.00 12.10 ? 181 PRO D CA  1 
ATOM   7829 C  C   . PRO D 1 180 ? 14.495  22.370  38.991  1.00 11.20 ? 181 PRO D C   1 
ATOM   7830 O  O   . PRO D 1 180 ? 15.354  21.435  38.854  1.00 12.09 ? 181 PRO D O   1 
ATOM   7831 C  CB  . PRO D 1 180 ? 14.703  23.918  37.009  1.00 13.24 ? 181 PRO D CB  1 
ATOM   7832 C  CG  . PRO D 1 180 ? 14.404  25.279  37.586  1.00 13.07 ? 181 PRO D CG  1 
ATOM   7833 C  CD  . PRO D 1 180 ? 12.867  25.214  37.764  1.00 12.47 ? 181 PRO D CD  1 
ATOM   7834 N  N   . ARG D 1 181 ? 14.088  22.762  40.203  1.00 10.79 ? 182 ARG D N   1 
ATOM   7835 C  CA  . ARG D 1 181 ? 14.610  22.075  41.368  1.00 11.74 ? 182 ARG D CA  1 
ATOM   7836 C  C   . ARG D 1 181 ? 14.219  20.575  41.355  1.00 11.39 ? 182 ARG D C   1 
ATOM   7837 O  O   . ARG D 1 181 ? 14.935  19.745  41.976  1.00 14.18 ? 182 ARG D O   1 
ATOM   7838 C  CB  . ARG D 1 181 ? 14.037  22.687  42.669  1.00 12.89 ? 182 ARG D CB  1 
ATOM   7839 C  CG  . ARG D 1 181 ? 14.574  24.104  42.867  1.00 14.68 ? 182 ARG D CG  1 
ATOM   7840 C  CD  . ARG D 1 181 ? 13.997  24.709  44.118  1.00 15.98 ? 182 ARG D CD  1 
ATOM   7841 N  NE  . ARG D 1 181 ? 12.594  24.994  43.925  1.00 17.26 ? 182 ARG D NE  1 
ATOM   7842 C  CZ  . ARG D 1 181 ? 11.880  25.700  44.813  1.00 24.31 ? 182 ARG D CZ  1 
ATOM   7843 N  NH1 . ARG D 1 181 ? 12.424  26.135  45.947  1.00 23.12 ? 182 ARG D NH1 1 
ATOM   7844 N  NH2 . ARG D 1 181 ? 10.609  25.905  44.591  1.00 26.88 ? 182 ARG D NH2 1 
ATOM   7845 N  N   . GLY D 1 182 ? 13.154  20.241  40.635  1.00 12.41 ? 183 GLY D N   1 
ATOM   7846 C  CA  . GLY D 1 182 ? 12.731  18.816  40.506  1.00 13.46 ? 183 GLY D CA  1 
ATOM   7847 C  C   . GLY D 1 182 ? 13.615  17.942  39.669  1.00 14.60 ? 183 GLY D C   1 
ATOM   7848 O  O   . GLY D 1 182 ? 13.324  16.729  39.527  1.00 14.60 ? 183 GLY D O   1 
ATOM   7849 N  N   . LEU D 1 183 ? 14.635  18.534  39.008  1.00 11.78 ? 184 LEU D N   1 
ATOM   7850 C  CA  . LEU D 1 183 ? 15.553  17.801  38.171  1.00 10.06 ? 184 LEU D CA  1 
ATOM   7851 C  C   . LEU D 1 183 ? 16.897  17.566  38.850  1.00 11.24 ? 184 LEU D C   1 
ATOM   7852 O  O   . LEU D 1 183 ? 17.809  16.977  38.245  1.00 12.47 ? 184 LEU D O   1 
ATOM   7853 C  CB  . LEU D 1 183 ? 15.751  18.531  36.863  1.00 11.96 ? 184 LEU D CB  1 
ATOM   7854 C  CG  . LEU D 1 183 ? 14.524  18.713  35.980  1.00 13.25 ? 184 LEU D CG  1 
ATOM   7855 C  CD1 . LEU D 1 183 ? 14.775  19.564  34.763  1.00 14.70 ? 184 LEU D CD1 1 
ATOM   7856 C  CD2 . LEU D 1 183 ? 13.845  17.356  35.648  1.00 14.58 ? 184 LEU D CD2 1 
ATOM   7857 N  N   . LEU D 1 184 ? 17.084  17.985  40.113  1.00 11.12 ? 185 LEU D N   1 
ATOM   7858 C  CA  . LEU D 1 184 ? 18.428  17.919  40.749  1.00 10.89 ? 185 LEU D CA  1 
ATOM   7859 C  C   . LEU D 1 184 ? 18.549  16.636  41.522  1.00 14.68 ? 185 LEU D C   1 
ATOM   7860 O  O   . LEU D 1 184 ? 17.523  16.096  41.993  1.00 18.79 ? 185 LEU D O   1 
ATOM   7861 C  CB  . LEU D 1 184 ? 18.659  19.147  41.687  1.00 12.59 ? 185 LEU D CB  1 
ATOM   7862 C  CG  . LEU D 1 184 ? 18.459  20.541  41.056  1.00 12.96 ? 185 LEU D CG  1 
ATOM   7863 C  CD1 . LEU D 1 184 ? 18.607  21.621  42.099  1.00 14.72 ? 185 LEU D CD1 1 
ATOM   7864 C  CD2 . LEU D 1 184 ? 19.532  20.707  39.949  1.00 13.85 ? 185 LEU D CD2 1 
ATOM   7865 N  N   . PRO D 1 185 ? 19.764  16.108  41.686  1.00 11.22 ? 186 PRO D N   1 
ATOM   7866 C  CA  . PRO D 1 185 ? 20.006  14.962  42.578  1.00 11.47 ? 186 PRO D CA  1 
ATOM   7867 C  C   . PRO D 1 185 ? 20.133  15.499  43.978  1.00 11.65 ? 186 PRO D C   1 
ATOM   7868 O  O   . PRO D 1 185 ? 20.073  16.702  44.194  1.00 12.22 ? 186 PRO D O   1 
ATOM   7869 C  CB  . PRO D 1 185 ? 21.330  14.376  42.017  1.00 11.46 ? 186 PRO D CB  1 
ATOM   7870 C  CG  . PRO D 1 185 ? 22.071  15.623  41.533  1.00 10.61 ? 186 PRO D CG  1 
ATOM   7871 C  CD  . PRO D 1 185 ? 20.958  16.509  40.898  1.00 10.12 ? 186 PRO D CD  1 
ATOM   7872 N  N   A GLU D 1 186 ? 20.308  14.528  44.855  0.50 12.24 ? 187 GLU D N   1 
ATOM   7873 N  N   B GLU D 1 186 ? 20.350  14.647  45.009  0.50 13.45 ? 187 GLU D N   1 
ATOM   7874 C  CA  A GLU D 1 186 ? 20.452  14.806  46.238  0.50 12.79 ? 187 GLU D CA  1 
ATOM   7875 C  CA  B GLU D 1 186 ? 20.547  15.157  46.408  0.50 13.12 ? 187 GLU D CA  1 
ATOM   7876 C  C   A GLU D 1 186 ? 21.679  15.709  46.499  0.50 10.77 ? 187 GLU D C   1 
ATOM   7877 C  C   B GLU D 1 186 ? 21.868  15.838  46.623  0.50 12.52 ? 187 GLU D C   1 
ATOM   7878 O  O   A GLU D 1 186 ? 21.531  16.785  47.134  0.50 12.51 ? 187 GLU D O   1 
ATOM   7879 O  O   B GLU D 1 186 ? 22.021  16.835  47.310  0.50 12.35 ? 187 GLU D O   1 
ATOM   7880 C  CB  A GLU D 1 186 ? 20.513  13.467  46.952  0.50 13.74 ? 187 GLU D CB  1 
ATOM   7881 C  CB  B GLU D 1 186 ? 20.587  14.045  47.446  0.50 13.83 ? 187 GLU D CB  1 
ATOM   7882 C  CG  A GLU D 1 186 ? 20.735  13.610  48.429  0.50 19.55 ? 187 GLU D CG  1 
ATOM   7883 C  CG  B GLU D 1 186 ? 19.358  13.189  47.466  0.50 15.39 ? 187 GLU D CG  1 
ATOM   7884 C  CD  A GLU D 1 186 ? 20.765  12.275  49.145  0.50 18.83 ? 187 GLU D CD  1 
ATOM   7885 C  CD  B GLU D 1 186 ? 19.507  11.969  48.354  0.50 16.01 ? 187 GLU D CD  1 
ATOM   7886 O  OE1 A GLU D 1 186 ? 19.925  11.409  48.823  0.50 20.43 ? 187 GLU D OE1 1 
ATOM   7887 O  OE1 B GLU D 1 186 ? 20.629  11.720  48.841  0.50 16.89 ? 187 GLU D OE1 1 
ATOM   7888 O  OE2 A GLU D 1 186 ? 21.628  12.092  50.030  0.50 27.96 ? 187 GLU D OE2 1 
ATOM   7889 O  OE2 B GLU D 1 186 ? 18.501  11.259  48.563  0.50 20.61 ? 187 GLU D OE2 1 
ATOM   7890 N  N   . SER D 1 187 ? 22.890  15.276  46.018  1.00 12.15 ? 188 SER D N   1 
ATOM   7891 C  CA  . SER D 1 187 ? 24.150  15.883  46.310  1.00 13.11 ? 188 SER D CA  1 
ATOM   7892 C  C   . SER D 1 187 ? 24.533  16.913  45.246  1.00 12.01 ? 188 SER D C   1 
ATOM   7893 O  O   . SER D 1 187 ? 24.270  16.669  44.067  1.00 14.27 ? 188 SER D O   1 
ATOM   7894 C  CB  . SER D 1 187 ? 25.226  14.795  46.318  1.00 14.57 ? 188 SER D CB  1 
ATOM   7895 O  OG  . SER D 1 187 ? 26.532  15.342  46.490  1.00 14.84 ? 188 SER D OG  1 
ATOM   7896 N  N   . LEU D 1 188 ? 25.245  17.959  45.673  1.00 12.21 ? 189 LEU D N   1 
ATOM   7897 C  CA  . LEU D 1 188 ? 25.798  18.964  44.778  1.00 12.06 ? 189 LEU D CA  1 
ATOM   7898 C  C   . LEU D 1 188 ? 27.315  18.834  44.676  1.00 11.90 ? 189 LEU D C   1 
ATOM   7899 O  O   . LEU D 1 188 ? 27.959  19.752  44.165  1.00 14.02 ? 189 LEU D O   1 
ATOM   7900 C  CB  . LEU D 1 188 ? 25.335  20.414  45.140  1.00 13.20 ? 189 LEU D CB  1 
ATOM   7901 C  CG  . LEU D 1 188 ? 23.871  20.759  45.023  1.00 14.04 ? 189 LEU D CG  1 
ATOM   7902 C  CD1 . LEU D 1 188 ? 23.620  22.217  45.481  1.00 17.10 ? 189 LEU D CD1 1 
ATOM   7903 C  CD2 . LEU D 1 188 ? 23.353  20.573  43.594  1.00 15.60 ? 189 LEU D CD2 1 
ATOM   7904 N  N   . ASP D 1 189 ? 27.858  17.652  45.020  1.00 13.01 ? 190 ASP D N   1 
ATOM   7905 C  CA  . ASP D 1 189 ? 29.246  17.421  44.726  1.00 11.69 ? 190 ASP D CA  1 
ATOM   7906 C  C   . ASP D 1 189 ? 29.518  17.454  43.194  1.00 8.69  ? 190 ASP D C   1 
ATOM   7907 O  O   . ASP D 1 189 ? 28.682  16.958  42.427  1.00 10.04 ? 190 ASP D O   1 
ATOM   7908 C  CB  . ASP D 1 189 ? 29.719  16.050  45.216  1.00 14.82 ? 190 ASP D CB  1 
ATOM   7909 C  CG  . ASP D 1 189 ? 29.852  15.923  46.780  1.00 18.85 ? 190 ASP D CG  1 
ATOM   7910 O  OD1 . ASP D 1 189 ? 29.906  16.939  47.433  1.00 23.74 ? 190 ASP D OD1 1 
ATOM   7911 O  OD2 . ASP D 1 189 ? 30.024  14.772  47.214  1.00 30.80 ? 190 ASP D OD2 1 
ATOM   7912 N  N   . TYR D 1 190 ? 30.617  18.066  42.788  1.00 10.09 ? 191 TYR D N   1 
ATOM   7913 C  CA  . TYR D 1 190 ? 30.844  18.284  41.342  1.00 8.63  ? 191 TYR D CA  1 
ATOM   7914 C  C   . TYR D 1 190 ? 32.278  18.234  40.934  1.00 9.12  ? 191 TYR D C   1 
ATOM   7915 O  O   . TYR D 1 190 ? 33.207  18.345  41.705  1.00 9.19  ? 191 TYR D O   1 
ATOM   7916 C  CB  . TYR D 1 190 ? 30.230  19.673  40.996  1.00 9.76  ? 191 TYR D CB  1 
ATOM   7917 C  CG  . TYR D 1 190 ? 30.943  20.854  41.663  1.00 9.32  ? 191 TYR D CG  1 
ATOM   7918 C  CD1 . TYR D 1 190 ? 32.075  21.436  41.097  1.00 10.46 ? 191 TYR D CD1 1 
ATOM   7919 C  CD2 . TYR D 1 190 ? 30.478  21.367  42.866  1.00 11.29 ? 191 TYR D CD2 1 
ATOM   7920 C  CE1 . TYR D 1 190 ? 32.721  22.491  41.708  1.00 10.67 ? 191 TYR D CE1 1 
ATOM   7921 C  CE2 . TYR D 1 190 ? 31.116  22.422  43.492  1.00 10.89 ? 191 TYR D CE2 1 
ATOM   7922 C  CZ  . TYR D 1 190 ? 32.237  22.979  42.907  1.00 10.61 ? 191 TYR D CZ  1 
ATOM   7923 O  OH  . TYR D 1 190 ? 32.884  24.029  43.512  1.00 12.89 ? 191 TYR D OH  1 
ATOM   7924 N  N   . TRP D 1 191 ? 32.438  18.063  39.611  1.00 8.65  ? 192 TRP D N   1 
ATOM   7925 C  CA  . TRP D 1 191 ? 33.683  18.324  38.908  1.00 7.84  ? 192 TRP D CA  1 
ATOM   7926 C  C   . TRP D 1 191 ? 33.572  19.613  38.124  1.00 7.06  ? 192 TRP D C   1 
ATOM   7927 O  O   . TRP D 1 191 ? 32.457  19.971  37.661  1.00 8.33  ? 192 TRP D O   1 
ATOM   7928 C  CB  . TRP D 1 191 ? 34.001  17.218  37.922  1.00 8.60  ? 192 TRP D CB  1 
ATOM   7929 C  CG  . TRP D 1 191 ? 34.218  15.905  38.560  1.00 8.33  ? 192 TRP D CG  1 
ATOM   7930 C  CD1 . TRP D 1 191 ? 35.351  15.480  39.242  1.00 9.99  ? 192 TRP D CD1 1 
ATOM   7931 C  CD2 . TRP D 1 191 ? 33.330  14.769  38.524  1.00 9.28  ? 192 TRP D CD2 1 
ATOM   7932 N  NE1 . TRP D 1 191 ? 35.182  14.145  39.657  1.00 11.14 ? 192 TRP D NE1 1 
ATOM   7933 C  CE2 . TRP D 1 191 ? 33.983  13.690  39.197  1.00 9.97  ? 192 TRP D CE2 1 
ATOM   7934 C  CE3 . TRP D 1 191 ? 32.051  14.531  37.944  1.00 10.21 ? 192 TRP D CE3 1 
ATOM   7935 C  CZ2 . TRP D 1 191 ? 33.402  12.420  39.311  1.00 11.38 ? 192 TRP D CZ2 1 
ATOM   7936 C  CZ3 . TRP D 1 191 ? 31.487  13.263  38.045  1.00 10.36 ? 192 TRP D CZ3 1 
ATOM   7937 C  CH2 . TRP D 1 191 ? 32.159  12.217  38.741  1.00 11.85 ? 192 TRP D CH2 1 
ATOM   7938 N  N   . THR D 1 192 ? 34.667  20.320  37.886  1.00 7.93  ? 193 THR D N   1 
ATOM   7939 C  CA  . THR D 1 192 ? 34.582  21.590  37.087  1.00 7.89  ? 193 THR D CA  1 
ATOM   7940 C  C   . THR D 1 192 ? 35.829  21.713  36.223  1.00 7.91  ? 193 THR D C   1 
ATOM   7941 O  O   . THR D 1 192 ? 36.954  21.257  36.625  1.00 8.45  ? 193 THR D O   1 
ATOM   7942 C  CB  . THR D 1 192 ? 34.382  22.773  38.011  1.00 8.19  ? 193 THR D CB  1 
ATOM   7943 O  OG1 . THR D 1 192 ? 34.226  23.985  37.239  1.00 8.80  ? 193 THR D OG1 1 
ATOM   7944 C  CG2 . THR D 1 192 ? 35.489  22.965  39.064  1.00 9.55  ? 193 THR D CG2 1 
ATOM   7945 N  N   . TYR D 1 193 ? 35.670  22.329  35.052  1.00 8.47  ? 194 TYR D N   1 
ATOM   7946 C  CA  . TYR D 1 193 ? 36.799  22.534  34.166  1.00 7.90  ? 194 TYR D CA  1 
ATOM   7947 C  C   . TYR D 1 193 ? 36.340  23.624  33.179  1.00 7.72  ? 194 TYR D C   1 
ATOM   7948 O  O   . TYR D 1 193 ? 35.110  23.885  32.988  1.00 8.20  ? 194 TYR D O   1 
ATOM   7949 C  CB  . TYR D 1 193 ? 37.256  21.255  33.444  1.00 9.74  ? 194 TYR D CB  1 
ATOM   7950 C  CG  . TYR D 1 193 ? 36.286  20.839  32.346  1.00 8.75  ? 194 TYR D CG  1 
ATOM   7951 C  CD1 . TYR D 1 193 ? 35.122  20.131  32.639  1.00 7.61  ? 194 TYR D CD1 1 
ATOM   7952 C  CD2 . TYR D 1 193 ? 36.523  21.180  31.020  1.00 8.24  ? 194 TYR D CD2 1 
ATOM   7953 C  CE1 . TYR D 1 193 ? 34.235  19.763  31.638  1.00 7.26  ? 194 TYR D CE1 1 
ATOM   7954 C  CE2 . TYR D 1 193 ? 35.643  20.816  30.016  1.00 9.81  ? 194 TYR D CE2 1 
ATOM   7955 C  CZ  . TYR D 1 193 ? 34.503  20.110  30.327  1.00 7.09  ? 194 TYR D CZ  1 
ATOM   7956 O  OH  . TYR D 1 193 ? 33.636  19.755  29.316  1.00 8.35  ? 194 TYR D OH  1 
ATOM   7957 N  N   . PRO D 1 194 ? 37.285  24.278  32.457  1.00 8.52  ? 195 PRO D N   1 
ATOM   7958 C  CA  . PRO D 1 194 ? 36.944  25.265  31.477  1.00 8.68  ? 195 PRO D CA  1 
ATOM   7959 C  C   . PRO D 1 194 ? 36.733  24.648  30.109  1.00 8.16  ? 195 PRO D C   1 
ATOM   7960 O  O   . PRO D 1 194 ? 37.580  23.841  29.672  1.00 9.39  ? 195 PRO D O   1 
ATOM   7961 C  CB  . PRO D 1 194 ? 38.188  26.160  31.444  1.00 12.20 ? 195 PRO D CB  1 
ATOM   7962 C  CG  . PRO D 1 194 ? 39.313  25.223  31.807  1.00 11.74 ? 195 PRO D CG  1 
ATOM   7963 C  CD  . PRO D 1 194 ? 38.742  24.250  32.784  1.00 10.39 ? 195 PRO D CD  1 
ATOM   7964 N  N   . GLY D 1 195 ? 35.600  24.988  29.478  1.00 7.95  ? 196 GLY D N   1 
ATOM   7965 C  CA  . GLY D 1 195 ? 35.301  24.367  28.183  1.00 9.20  ? 196 GLY D CA  1 
ATOM   7966 C  C   . GLY D 1 195 ? 34.457  25.254  27.301  1.00 8.27  ? 196 GLY D C   1 
ATOM   7967 O  O   . GLY D 1 195 ? 34.618  26.485  27.256  1.00 8.39  ? 196 GLY D O   1 
ATOM   7968 N  N   . SER D 1 196 ? 33.597  24.584  26.532  1.00 7.56  ? 197 SER D N   1 
ATOM   7969 C  CA  . SER D 1 196 ? 32.913  25.235  25.409  1.00 8.20  ? 197 SER D CA  1 
ATOM   7970 C  C   . SER D 1 196 ? 31.460  24.823  25.337  1.00 9.06  ? 197 SER D C   1 
ATOM   7971 O  O   . SER D 1 196 ? 31.036  23.840  25.973  1.00 8.80  ? 197 SER D O   1 
ATOM   7972 C  CB  . SER D 1 196 ? 33.556  24.811  24.079  1.00 9.22  ? 197 SER D CB  1 
ATOM   7973 O  OG  . SER D 1 196 ? 33.262  23.453  23.712  1.00 8.47  ? 197 SER D OG  1 
ATOM   7974 N  N   . LEU D 1 197 ? 30.680  25.478  24.468  1.00 8.52  ? 198 LEU D N   1 
ATOM   7975 C  CA  . LEU D 1 197 ? 29.428  24.917  24.009  1.00 8.20  ? 198 LEU D CA  1 
ATOM   7976 C  C   . LEU D 1 197 ? 29.720  23.595  23.384  1.00 8.40  ? 198 LEU D C   1 
ATOM   7977 O  O   . LEU D 1 197 ? 30.736  23.448  22.642  1.00 9.18  ? 198 LEU D O   1 
ATOM   7978 C  CB  . LEU D 1 197 ? 28.774  25.868  23.014  1.00 11.49 ? 198 LEU D CB  1 
ATOM   7979 C  CG  . LEU D 1 197 ? 28.471  27.292  23.436  1.00 10.72 ? 198 LEU D CG  1 
ATOM   7980 C  CD1 . LEU D 1 197 ? 27.864  28.060  22.280  1.00 14.65 ? 198 LEU D CD1 1 
ATOM   7981 C  CD2 . LEU D 1 197 ? 27.581  27.316  24.628  1.00 12.95 ? 198 LEU D CD2 1 
ATOM   7982 N  N   . THR D 1 198 ? 28.795  22.644  23.446  1.00 9.34  ? 199 THR D N   1 
ATOM   7983 C  CA  . THR D 1 198 ? 29.011  21.328  22.824  1.00 9.03  ? 199 THR D CA  1 
ATOM   7984 C  C   . THR D 1 198 ? 28.290  21.249  21.468  1.00 9.44  ? 199 THR D C   1 
ATOM   7985 O  O   . THR D 1 198 ? 28.328  20.198  20.860  1.00 10.11 ? 199 THR D O   1 
ATOM   7986 C  CB  . THR D 1 198 ? 28.558  20.198  23.726  1.00 8.37  ? 199 THR D CB  1 
ATOM   7987 O  OG1 . THR D 1 198 ? 27.131  20.251  23.790  1.00 9.17  ? 199 THR D OG1 1 
ATOM   7988 C  CG2 . THR D 1 198 ? 29.204  20.204  25.101  1.00 9.91  ? 199 THR D CG2 1 
ATOM   7989 N  N   . THR D 1 199 ? 27.585  22.334  21.073  1.00 10.66 ? 200 THR D N   1 
ATOM   7990 C  CA  . THR D 1 199 ? 26.974  22.435  19.740  1.00 11.08 ? 200 THR D CA  1 
ATOM   7991 C  C   . THR D 1 199 ? 27.599  23.664  19.064  1.00 13.00 ? 200 THR D C   1 
ATOM   7992 O  O   . THR D 1 199 ? 28.006  24.613  19.693  1.00 11.86 ? 200 THR D O   1 
ATOM   7993 C  CB  . THR D 1 199 ? 25.453  22.682  19.822  1.00 14.64 ? 200 THR D CB  1 
ATOM   7994 O  OG1 . THR D 1 199 ? 25.236  23.747  20.813  1.00 18.33 ? 200 THR D OG1 1 
ATOM   7995 C  CG2 . THR D 1 199 ? 24.790  21.431  20.399  1.00 15.09 ? 200 THR D CG2 1 
ATOM   7996 N  N   . PRO D 1 200 ? 27.687  23.620  17.699  1.00 12.76 ? 201 PRO D N   1 
ATOM   7997 C  CA  . PRO D 1 200 ? 27.970  24.866  16.968  1.00 12.25 ? 201 PRO D CA  1 
ATOM   7998 C  C   . PRO D 1 200 ? 27.161  26.032  17.582  1.00 13.55 ? 201 PRO D C   1 
ATOM   7999 O  O   . PRO D 1 200 ? 25.924  25.902  17.832  1.00 14.72 ? 201 PRO D O   1 
ATOM   8000 C  CB  . PRO D 1 200 ? 27.498  24.486  15.557  1.00 14.23 ? 201 PRO D CB  1 
ATOM   8001 C  CG  . PRO D 1 200 ? 27.795  23.005  15.455  1.00 15.80 ? 201 PRO D CG  1 
ATOM   8002 C  CD  . PRO D 1 200 ? 27.341  22.497  16.787  1.00 14.14 ? 201 PRO D CD  1 
ATOM   8003 N  N   . PRO D 1 201 ? 27.786  27.198  17.797  1.00 12.79 ? 202 PRO D N   1 
ATOM   8004 C  CA  . PRO D 1 201 ? 29.148  27.620  17.270  1.00 12.97 ? 202 PRO D CA  1 
ATOM   8005 C  C   . PRO D 1 201 ? 30.332  27.223  18.160  1.00 12.35 ? 202 PRO D C   1 
ATOM   8006 O  O   . PRO D 1 201 ? 31.458  27.605  17.880  1.00 12.77 ? 202 PRO D O   1 
ATOM   8007 C  CB  . PRO D 1 201 ? 28.996  29.112  17.176  1.00 16.10 ? 202 PRO D CB  1 
ATOM   8008 C  CG  . PRO D 1 201 ? 28.075  29.430  18.313  1.00 17.05 ? 202 PRO D CG  1 
ATOM   8009 C  CD  . PRO D 1 201 ? 26.991  28.360  18.245  1.00 15.75 ? 202 PRO D CD  1 
ATOM   8010 N  N   . LEU D 1 202 ? 30.079  26.326  19.164  1.00 10.49 ? 203 LEU D N   1 
ATOM   8011 C  CA  . LEU D 1 202 ? 31.269  25.684  19.875  1.00 10.35 ? 203 LEU D CA  1 
ATOM   8012 C  C   . LEU D 1 202 ? 32.183  26.706  20.645  1.00 9.39  ? 203 LEU D C   1 
ATOM   8013 O  O   . LEU D 1 202 ? 33.320  26.458  20.898  1.00 11.01 ? 203 LEU D O   1 
ATOM   8014 C  CB  . LEU D 1 202 ? 32.141  24.814  18.932  1.00 10.64 ? 203 LEU D CB  1 
ATOM   8015 C  CG  . LEU D 1 202 ? 31.299  23.651  18.329  1.00 10.44 ? 203 LEU D CG  1 
ATOM   8016 C  CD1 . LEU D 1 202 ? 32.199  22.979  17.265  1.00 12.97 ? 203 LEU D CD1 1 
ATOM   8017 C  CD2 . LEU D 1 202 ? 30.810  22.633  19.316  1.00 11.40 ? 203 LEU D CD2 1 
ATOM   8018 N  N   . LEU D 1 203 ? 31.567  27.847  20.990  1.00 11.43 ? 204 LEU D N   1 
ATOM   8019 C  CA  . LEU D 1 203 ? 32.289  28.926  21.597  1.00 12.45 ? 204 LEU D CA  1 
ATOM   8020 C  C   . LEU D 1 203 ? 32.916  28.526  22.943  1.00 11.00 ? 204 LEU D C   1 
ATOM   8021 O  O   . LEU D 1 203 ? 32.282  27.822  23.777  1.00 10.23 ? 204 LEU D O   1 
ATOM   8022 C  CB  . LEU D 1 203 ? 31.367  30.133  21.801  1.00 14.21 ? 204 LEU D CB  1 
ATOM   8023 C  CG  . LEU D 1 203 ? 30.874  30.741  20.480  1.00 16.25 ? 204 LEU D CG  1 
ATOM   8024 C  CD1 . LEU D 1 203 ? 29.735  31.717  20.748  1.00 18.57 ? 204 LEU D CD1 1 
ATOM   8025 C  CD2 . LEU D 1 203 ? 32.007  31.414  19.654  1.00 19.79 ? 204 LEU D CD2 1 
ATOM   8026 N  N   . GLU D 1 204 ? 34.146  28.965  23.170  1.00 12.18 ? 205 GLU D N   1 
ATOM   8027 C  CA  . GLU D 1 204 ? 34.943  28.609  24.363  1.00 10.98 ? 205 GLU D CA  1 
ATOM   8028 C  C   . GLU D 1 204 ? 34.650  29.592  25.507  1.00 12.82 ? 205 GLU D C   1 
ATOM   8029 O  O   . GLU D 1 204 ? 35.502  30.359  25.927  1.00 14.72 ? 205 GLU D O   1 
ATOM   8030 C  CB  . GLU D 1 204 ? 36.418  28.470  23.981  1.00 12.08 ? 205 GLU D CB  1 
ATOM   8031 C  CG  . GLU D 1 204 ? 36.546  27.247  23.094  1.00 12.96 ? 205 GLU D CG  1 
ATOM   8032 C  CD  . GLU D 1 204 ? 37.967  26.951  22.629  1.00 14.65 ? 205 GLU D CD  1 
ATOM   8033 O  OE1 . GLU D 1 204 ? 38.822  27.916  22.624  1.00 17.70 ? 205 GLU D OE1 1 
ATOM   8034 O  OE2 . GLU D 1 204 ? 38.296  25.755  22.383  1.00 12.80 ? 205 GLU D OE2 1 
ATOM   8035 N  N   . CYS D 1 205 ? 33.417  29.542  25.966  1.00 9.84  ? 206 CYS D N   1 
ATOM   8036 C  CA  . CYS D 1 205 ? 32.878  30.503  26.898  1.00 9.58  ? 206 CYS D CA  1 
ATOM   8037 C  C   . CYS D 1 205 ? 32.306  29.909  28.151  1.00 9.97  ? 206 CYS D C   1 
ATOM   8038 O  O   . CYS D 1 205 ? 31.628  30.598  28.935  1.00 11.20 ? 206 CYS D O   1 
ATOM   8039 C  CB  . CYS D 1 205 ? 31.770  31.321  26.202  1.00 10.91 ? 206 CYS D CB  1 
ATOM   8040 S  SG  . CYS D 1 205 ? 30.353  30.386  25.624  1.00 12.38 ? 206 CYS D SG  1 
ATOM   8041 N  N   . VAL D 1 206 ? 32.483  28.597  28.396  1.00 9.11  ? 207 VAL D N   1 
ATOM   8042 C  CA  . VAL D 1 206 ? 31.752  27.891  29.451  1.00 8.18  ? 207 VAL D CA  1 
ATOM   8043 C  C   . VAL D 1 206 ? 32.678  27.458  30.575  1.00 7.89  ? 207 VAL D C   1 
ATOM   8044 O  O   . VAL D 1 206 ? 33.665  26.777  30.384  1.00 10.04 ? 207 VAL D O   1 
ATOM   8045 C  CB  . VAL D 1 206 ? 31.068  26.641  28.864  1.00 8.36  ? 207 VAL D CB  1 
ATOM   8046 C  CG1 . VAL D 1 206 ? 30.267  25.912  29.994  1.00 8.72  ? 207 VAL D CG1 1 
ATOM   8047 C  CG2 . VAL D 1 206 ? 30.117  27.009  27.749  1.00 10.56 ? 207 VAL D CG2 1 
ATOM   8048 N  N   . THR D 1 207 ? 32.267  27.772  31.826  1.00 8.25  ? 208 THR D N   1 
ATOM   8049 C  CA  . THR D 1 207 ? 32.696  27.025  33.000  1.00 8.91  ? 208 THR D CA  1 
ATOM   8050 C  C   . THR D 1 207 ? 31.736  25.879  33.258  1.00 7.69  ? 208 THR D C   1 
ATOM   8051 O  O   . THR D 1 207 ? 30.553  26.071  33.485  1.00 8.30  ? 208 THR D O   1 
ATOM   8052 C  CB  . THR D 1 207 ? 32.768  27.898  34.265  1.00 8.78  ? 208 THR D CB  1 
ATOM   8053 O  OG1 . THR D 1 207 ? 33.642  29.018  34.042  1.00 10.14 ? 208 THR D OG1 1 
ATOM   8054 C  CG2 . THR D 1 207 ? 33.252  27.059  35.501  1.00 10.54 ? 208 THR D CG2 1 
ATOM   8055 N  N   . TRP D 1 208 ? 32.264  24.673  33.015  1.00 7.80  ? 209 TRP D N   1 
ATOM   8056 C  CA  . TRP D 1 208 ? 31.468  23.465  33.199  1.00 7.75  ? 209 TRP D CA  1 
ATOM   8057 C  C   . TRP D 1 208 ? 31.430  23.048  34.658  1.00 7.08  ? 209 TRP D C   1 
ATOM   8058 O  O   . TRP D 1 208 ? 32.499  23.003  35.311  1.00 7.47  ? 209 TRP D O   1 
ATOM   8059 C  CB  . TRP D 1 208 ? 31.989  22.280  32.353  1.00 7.60  ? 209 TRP D CB  1 
ATOM   8060 C  CG  . TRP D 1 208 ? 31.488  22.405  30.954  1.00 6.69  ? 209 TRP D CG  1 
ATOM   8061 C  CD1 . TRP D 1 208 ? 32.078  22.986  29.838  1.00 8.49  ? 209 TRP D CD1 1 
ATOM   8062 C  CD2 . TRP D 1 208 ? 30.191  21.996  30.525  1.00 7.61  ? 209 TRP D CD2 1 
ATOM   8063 N  NE1 . TRP D 1 208 ? 31.208  22.971  28.783  1.00 8.36  ? 209 TRP D NE1 1 
ATOM   8064 C  CE2 . TRP D 1 208 ? 30.049  22.366  29.129  1.00 7.74  ? 209 TRP D CE2 1 
ATOM   8065 C  CE3 . TRP D 1 208 ? 29.110  21.364  31.189  1.00 7.15  ? 209 TRP D CE3 1 
ATOM   8066 C  CZ2 . TRP D 1 208 ? 28.886  22.141  28.435  1.00 9.00  ? 209 TRP D CZ2 1 
ATOM   8067 C  CZ3 . TRP D 1 208 ? 27.972  21.111  30.489  1.00 8.22  ? 209 TRP D CZ3 1 
ATOM   8068 C  CH2 . TRP D 1 208 ? 27.850  21.443  29.132  1.00 8.69  ? 209 TRP D CH2 1 
ATOM   8069 N  N   . ILE D 1 209 ? 30.256  22.682  35.167  1.00 7.31  ? 210 ILE D N   1 
ATOM   8070 C  CA  . ILE D 1 209 ? 30.104  22.144  36.530  1.00 7.55  ? 210 ILE D CA  1 
ATOM   8071 C  C   . ILE D 1 209 ? 29.272  20.898  36.329  1.00 7.49  ? 210 ILE D C   1 
ATOM   8072 O  O   . ILE D 1 209 ? 28.118  20.993  35.971  1.00 8.24  ? 210 ILE D O   1 
ATOM   8073 C  CB  . ILE D 1 209 ? 29.424  23.174  37.458  1.00 8.60  ? 210 ILE D CB  1 
ATOM   8074 C  CG1 . ILE D 1 209 ? 30.230  24.473  37.479  1.00 10.67 ? 210 ILE D CG1 1 
ATOM   8075 C  CG2 . ILE D 1 209 ? 29.182  22.586  38.844  1.00 10.02 ? 210 ILE D CG2 1 
ATOM   8076 C  CD1 . ILE D 1 209 ? 29.503  25.631  38.161  1.00 13.19 ? 210 ILE D CD1 1 
ATOM   8077 N  N   . VAL D 1 210 ? 29.880  19.728  36.560  1.00 7.47  ? 211 VAL D N   1 
ATOM   8078 C  CA  . VAL D 1 210 ? 29.228  18.449  36.293  1.00 7.11  ? 211 VAL D CA  1 
ATOM   8079 C  C   . VAL D 1 210 ? 28.985  17.761  37.610  1.00 6.62  ? 211 VAL D C   1 
ATOM   8080 O  O   . VAL D 1 210 ? 29.950  17.471  38.303  1.00 8.35  ? 211 VAL D O   1 
ATOM   8081 C  CB  . VAL D 1 210 ? 30.050  17.590  35.293  1.00 7.54  ? 211 VAL D CB  1 
ATOM   8082 C  CG1 . VAL D 1 210 ? 29.356  16.222  35.078  1.00 8.59  ? 211 VAL D CG1 1 
ATOM   8083 C  CG2 . VAL D 1 210 ? 30.251  18.347  33.947  1.00 8.84  ? 211 VAL D CG2 1 
ATOM   8084 N  N   . LEU D 1 211 ? 27.728  17.460  37.923  1.00 7.85  ? 212 LEU D N   1 
ATOM   8085 C  CA  . LEU D 1 211 ? 27.454  16.834  39.204  1.00 8.10  ? 212 LEU D CA  1 
ATOM   8086 C  C   . LEU D 1 211 ? 27.879  15.370  39.184  1.00 9.01  ? 212 LEU D C   1 
ATOM   8087 O  O   . LEU D 1 211 ? 27.645  14.641  38.207  1.00 9.29  ? 212 LEU D O   1 
ATOM   8088 C  CB  . LEU D 1 211 ? 25.975  16.984  39.531  1.00 8.43  ? 212 LEU D CB  1 
ATOM   8089 C  CG  . LEU D 1 211 ? 25.437  18.418  39.699  1.00 9.02  ? 212 LEU D CG  1 
ATOM   8090 C  CD1 . LEU D 1 211 ? 24.019  18.358  40.326  1.00 10.98 ? 212 LEU D CD1 1 
ATOM   8091 C  CD2 . LEU D 1 211 ? 26.383  19.260  40.611  1.00 9.31  ? 212 LEU D CD2 1 
ATOM   8092 N  N   . LYS D 1 212 ? 28.496  14.922  40.289  1.00 9.26  ? 213 LYS D N   1 
ATOM   8093 C  CA  . LYS D 1 212 ? 28.868  13.532  40.351  1.00 10.15 ? 213 LYS D CA  1 
ATOM   8094 C  C   . LYS D 1 212 ? 27.640  12.585  40.454  1.00 9.48  ? 213 LYS D C   1 
ATOM   8095 O  O   . LYS D 1 212 ? 27.681  11.507  39.932  1.00 12.50 ? 213 LYS D O   1 
ATOM   8096 C  CB  . LYS D 1 212 ? 29.769  13.326  41.541  1.00 13.03 ? 213 LYS D CB  1 
ATOM   8097 C  CG  . LYS D 1 212 ? 30.142  11.877  41.890  1.00 16.07 ? 213 LYS D CG  1 
ATOM   8098 C  CD  . LYS D 1 212 ? 30.412  11.631  43.371  1.00 29.00 ? 213 LYS D CD  1 
ATOM   8099 C  CE  . LYS D 1 212 ? 29.721  12.619  44.301  1.00 34.65 ? 213 LYS D CE  1 
ATOM   8100 N  NZ  . LYS D 1 212 ? 28.233  12.596  44.235  1.00 24.20 ? 213 LYS D NZ  1 
ATOM   8101 N  N   . GLU D 1 213 ? 26.561  12.979  41.130  1.00 8.99  ? 214 GLU D N   1 
ATOM   8102 C  CA  . GLU D 1 213 ? 25.430  12.054  41.378  1.00 10.57 ? 214 GLU D CA  1 
ATOM   8103 C  C   . GLU D 1 213 ? 24.427  12.153  40.208  1.00 9.37  ? 214 GLU D C   1 
ATOM   8104 O  O   . GLU D 1 213 ? 23.925  13.261  39.952  1.00 9.25  ? 214 GLU D O   1 
ATOM   8105 C  CB  . GLU D 1 213 ? 24.749  12.423  42.687  1.00 12.08 ? 214 GLU D CB  1 
ATOM   8106 C  CG  . GLU D 1 213 ? 23.577  11.474  42.960  1.00 16.95 ? 214 GLU D CG  1 
ATOM   8107 C  CD  . GLU D 1 213 ? 22.930  11.617  44.303  1.00 19.12 ? 214 GLU D CD  1 
ATOM   8108 O  OE1 . GLU D 1 213 ? 23.225  12.533  45.046  1.00 15.52 ? 214 GLU D OE1 1 
ATOM   8109 O  OE2 . GLU D 1 213 ? 22.156  10.634  44.620  1.00 30.56 ? 214 GLU D OE2 1 
ATOM   8110 N  N   . PRO D 1 214 ? 24.191  11.073  39.480  1.00 9.15  ? 215 PRO D N   1 
ATOM   8111 C  CA  . PRO D 1 214 ? 23.178  11.112  38.422  1.00 10.06 ? 215 PRO D CA  1 
ATOM   8112 C  C   . PRO D 1 214 ? 21.778  11.182  39.022  1.00 10.86 ? 215 PRO D C   1 
ATOM   8113 O  O   . PRO D 1 214 ? 21.564  10.761  40.195  1.00 12.21 ? 215 PRO D O   1 
ATOM   8114 C  CB  . PRO D 1 214 ? 23.292  9.760   37.726  1.00 9.65  ? 215 PRO D CB  1 
ATOM   8115 C  CG  . PRO D 1 214 ? 23.924  8.900   38.705  1.00 16.89 ? 215 PRO D CG  1 
ATOM   8116 C  CD  . PRO D 1 214 ? 24.796  9.715   39.649  1.00 10.64 ? 215 PRO D CD  1 
ATOM   8117 N  N   . ILE D 1 215 ? 20.834  11.630  38.205  1.00 9.69  ? 216 ILE D N   1 
ATOM   8118 C  CA  . ILE D 1 215 ? 19.414  11.416  38.570  1.00 11.68 ? 216 ILE D CA  1 
ATOM   8119 C  C   . ILE D 1 215 ? 18.962  10.131  37.872  1.00 10.46 ? 216 ILE D C   1 
ATOM   8120 O  O   . ILE D 1 215 ? 19.503  9.734   36.819  1.00 11.12 ? 216 ILE D O   1 
ATOM   8121 C  CB  . ILE D 1 215 ? 18.531  12.607  38.203  1.00 10.81 ? 216 ILE D CB  1 
ATOM   8122 C  CG1 . ILE D 1 215 ? 18.532  12.917  36.700  1.00 12.06 ? 216 ILE D CG1 1 
ATOM   8123 C  CG2 . ILE D 1 215 ? 18.857  13.862  39.084  1.00 13.19 ? 216 ILE D CG2 1 
ATOM   8124 C  CD1 . ILE D 1 215 ? 17.400  13.907  36.309  1.00 12.27 ? 216 ILE D CD1 1 
ATOM   8125 N  N   . SER D 1 216 ? 17.953  9.448   38.446  0.50 5.71  ? 217 SER D N   1 
ATOM   8126 C  CA  . SER D 1 216 ? 17.306  8.304   37.794  0.50 6.02  ? 217 SER D CA  1 
ATOM   8127 C  C   . SER D 1 216 ? 16.051  8.771   37.127  0.50 5.37  ? 217 SER D C   1 
ATOM   8128 O  O   . SER D 1 216 ? 15.225  9.477   37.739  0.50 6.21  ? 217 SER D O   1 
ATOM   8129 C  CB  . SER D 1 216 ? 16.982  7.212   38.826  0.50 10.75 ? 217 SER D CB  1 
ATOM   8130 O  OG  . SER D 1 216 ? 18.120  6.607   39.339  0.50 11.27 ? 217 SER D OG  1 
ATOM   8131 N  N   . VAL D 1 217 ? 15.834  8.288   35.921  1.00 10.58 ? 218 VAL D N   1 
ATOM   8132 C  CA  . VAL D 1 217 ? 14.621  8.502   35.208  1.00 11.20 ? 218 VAL D CA  1 
ATOM   8133 C  C   . VAL D 1 217 ? 14.103  7.123   34.811  1.00 12.15 ? 218 VAL D C   1 
ATOM   8134 O  O   . VAL D 1 217 ? 14.882  6.186   34.669  1.00 11.36 ? 218 VAL D O   1 
ATOM   8135 C  CB  . VAL D 1 217 ? 14.815  9.394   33.979  1.00 12.18 ? 218 VAL D CB  1 
ATOM   8136 C  CG1 . VAL D 1 217 ? 15.353  10.760  34.423  1.00 12.71 ? 218 VAL D CG1 1 
ATOM   8137 C  CG2 . VAL D 1 217 ? 15.774  8.753   32.940  1.00 13.52 ? 218 VAL D CG2 1 
ATOM   8138 N  N   . SER D 1 218 ? 12.862  6.978   34.479  1.00 11.80 ? 219 SER D N   1 
ATOM   8139 C  CA  . SER D 1 218 ? 12.397  5.655   34.039  1.00 12.29 ? 219 SER D CA  1 
ATOM   8140 C  C   . SER D 1 218 ? 12.608  5.395   32.600  1.00 12.11 ? 219 SER D C   1 
ATOM   8141 O  O   . SER D 1 218 ? 12.783  6.294   31.763  1.00 12.77 ? 219 SER D O   1 
ATOM   8142 C  CB  . SER D 1 218 ? 10.925  5.468   34.406  1.00 12.14 ? 219 SER D CB  1 
ATOM   8143 O  OG  . SER D 1 218 ? 10.112  6.338   33.595  1.00 14.15 ? 219 SER D OG  1 
ATOM   8144 N  N   A SER D 1 219 ? 12.554  4.108   32.211  0.50 11.99 ? 220 SER D N   1 
ATOM   8145 N  N   B SER D 1 219 ? 12.565  4.104   32.298  0.50 12.46 ? 220 SER D N   1 
ATOM   8146 C  CA  A SER D 1 219 ? 12.641  3.727   30.794  0.50 14.11 ? 220 SER D CA  1 
ATOM   8147 C  CA  B SER D 1 219 ? 12.708  3.718   30.953  0.50 13.92 ? 220 SER D CA  1 
ATOM   8148 C  C   A SER D 1 219 ? 11.549  4.381   29.963  0.50 13.01 ? 220 SER D C   1 
ATOM   8149 C  C   B SER D 1 219 ? 11.644  4.412   30.096  0.50 13.59 ? 220 SER D C   1 
ATOM   8150 O  O   A SER D 1 219 ? 11.731  4.778   28.791  0.50 13.46 ? 220 SER D O   1 
ATOM   8151 O  O   B SER D 1 219 ? 12.005  4.925   29.036  0.50 15.54 ? 220 SER D O   1 
ATOM   8152 C  CB  A SER D 1 219 ? 12.560  2.178   30.636  0.50 15.56 ? 220 SER D CB  1 
ATOM   8153 C  CB  B SER D 1 219 ? 12.731  2.175   30.831  0.50 15.35 ? 220 SER D CB  1 
ATOM   8154 O  OG  A SER D 1 219 ? 11.388  1.623   31.273  0.50 15.80 ? 220 SER D OG  1 
ATOM   8155 O  OG  B SER D 1 219 ? 12.918  1.776   29.494  0.50 15.52 ? 220 SER D OG  1 
ATOM   8156 N  N   . GLU D 1 220 ? 10.372  4.486   30.568  1.00 13.78 ? 221 GLU D N   1 
ATOM   8157 C  CA  . GLU D 1 220 ? 9.260   5.115   29.825  1.00 16.39 ? 221 GLU D CA  1 
ATOM   8158 C  C   . GLU D 1 220 ? 9.524   6.621   29.567  1.00 13.63 ? 221 GLU D C   1 
ATOM   8159 O  O   . GLU D 1 220 ? 9.161   7.165   28.518  1.00 15.39 ? 221 GLU D O   1 
ATOM   8160 C  CB  . GLU D 1 220 ? 7.899   4.970   30.520  1.00 17.62 ? 221 GLU D CB  1 
ATOM   8161 C  CG  . GLU D 1 220 ? 7.456   3.456   30.566  1.00 20.53 ? 221 GLU D CG  1 
ATOM   8162 C  CD  . GLU D 1 220 ? 7.876   2.753   31.849  1.00 23.99 ? 221 GLU D CD  1 
ATOM   8163 O  OE1 . GLU D 1 220 ? 8.833   3.236   32.500  1.00 21.22 ? 221 GLU D OE1 1 
ATOM   8164 O  OE2 . GLU D 1 220 ? 7.257   1.714   32.191  1.00 37.26 ? 221 GLU D OE2 1 
ATOM   8165 N  N   . GLN D 1 221 ? 10.150  7.278   30.558  1.00 13.42 ? 222 GLN D N   1 
ATOM   8166 C  CA  . GLN D 1 221 ? 10.407  8.700   30.351  1.00 12.10 ? 222 GLN D CA  1 
ATOM   8167 C  C   . GLN D 1 221 ? 11.431  8.913   29.247  1.00 13.45 ? 222 GLN D C   1 
ATOM   8168 O  O   . GLN D 1 221 ? 11.230  9.714   28.367  1.00 13.43 ? 222 GLN D O   1 
ATOM   8169 C  CB  . GLN D 1 221 ? 10.957  9.227   31.653  1.00 11.82 ? 222 GLN D CB  1 
ATOM   8170 C  CG  . GLN D 1 221 ? 9.862   9.398   32.709  1.00 12.85 ? 222 GLN D CG  1 
ATOM   8171 C  CD  . GLN D 1 221 ? 10.320  9.987   34.050  1.00 11.72 ? 222 GLN D CD  1 
ATOM   8172 O  OE1 . GLN D 1 221 ? 11.391  9.611   34.591  1.00 11.79 ? 222 GLN D OE1 1 
ATOM   8173 N  NE2 . GLN D 1 221 ? 9.523   10.920  34.642  1.00 11.18 ? 222 GLN D NE2 1 
ATOM   8174 N  N   . VAL D 1 222 ? 12.526  8.165   29.217  1.00 12.70 ? 223 VAL D N   1 
ATOM   8175 C  CA  . VAL D 1 222 ? 13.486  8.350   28.117  1.00 13.00 ? 223 VAL D CA  1 
ATOM   8176 C  C   . VAL D 1 222 ? 12.950  7.875   26.756  1.00 14.37 ? 223 VAL D C   1 
ATOM   8177 O  O   . VAL D 1 222 ? 13.328  8.437   25.734  1.00 14.44 ? 223 VAL D O   1 
ATOM   8178 C  CB  . VAL D 1 222 ? 14.896  7.793   28.514  1.00 17.88 ? 223 VAL D CB  1 
ATOM   8179 C  CG1 . VAL D 1 222 ? 14.885  6.275   28.636  1.00 19.45 ? 223 VAL D CG1 1 
ATOM   8180 C  CG2 . VAL D 1 222 ? 15.979  8.296   27.572  1.00 19.73 ? 223 VAL D CG2 1 
ATOM   8181 N  N   . LEU D 1 223 ? 12.066  6.857   26.775  1.00 13.41 ? 224 LEU D N   1 
ATOM   8182 C  CA  . LEU D 1 223 ? 11.446  6.426   25.552  1.00 14.80 ? 224 LEU D CA  1 
ATOM   8183 C  C   . LEU D 1 223 ? 10.638  7.536   24.925  1.00 15.11 ? 224 LEU D C   1 
ATOM   8184 O  O   . LEU D 1 223 ? 10.661  7.644   23.708  1.00 16.28 ? 224 LEU D O   1 
ATOM   8185 C  CB  . LEU D 1 223 ? 10.586  5.183   25.757  1.00 18.74 ? 224 LEU D CB  1 
ATOM   8186 C  CG  . LEU D 1 223 ? 11.450  3.896   25.817  1.00 20.58 ? 224 LEU D CG  1 
ATOM   8187 C  CD1 . LEU D 1 223 ? 10.632  2.752   26.491  1.00 27.39 ? 224 LEU D CD1 1 
ATOM   8188 C  CD2 . LEU D 1 223 ? 11.945  3.491   24.405  1.00 25.41 ? 224 LEU D CD2 1 
ATOM   8189 N  N   . LYS D 1 224 ? 10.057  8.414   25.748  1.00 15.01 ? 225 LYS D N   1 
ATOM   8190 C  CA  . LYS D 1 224 ? 9.312   9.569   25.181  1.00 15.49 ? 225 LYS D CA  1 
ATOM   8191 C  C   . LYS D 1 224 ? 10.239  10.631  24.574  1.00 13.65 ? 225 LYS D C   1 
ATOM   8192 O  O   . LYS D 1 224 ? 9.932   11.222  23.555  1.00 13.56 ? 225 LYS D O   1 
ATOM   8193 C  CB  . LYS D 1 224 ? 8.312   10.095  26.266  1.00 16.88 ? 225 LYS D CB  1 
ATOM   8194 C  CG  . LYS D 1 224 ? 7.192   9.031   26.468  1.00 19.22 ? 225 LYS D CG  1 
ATOM   8195 C  CD  . LYS D 1 224 ? 6.006   9.464   27.248  1.00 26.53 ? 225 LYS D CD  1 
ATOM   8196 C  CE  . LYS D 1 224 ? 4.968   8.317   27.379  1.00 28.47 ? 225 LYS D CE  1 
ATOM   8197 N  NZ  . LYS D 1 224 ? 3.960   8.568   28.438  1.00 27.06 ? 225 LYS D NZ  1 
ATOM   8198 N  N   . PHE D 1 225 ? 11.444  10.829  25.132  1.00 11.75 ? 226 PHE D N   1 
ATOM   8199 C  CA  . PHE D 1 225 ? 12.405  11.665  24.450  1.00 11.08 ? 226 PHE D CA  1 
ATOM   8200 C  C   . PHE D 1 225 ? 12.702  11.124  23.048  1.00 13.50 ? 226 PHE D C   1 
ATOM   8201 O  O   . PHE D 1 225 ? 12.853  11.924  22.104  1.00 12.35 ? 226 PHE D O   1 
ATOM   8202 C  CB  . PHE D 1 225 ? 13.772  11.676  25.192  1.00 12.45 ? 226 PHE D CB  1 
ATOM   8203 C  CG  . PHE D 1 225 ? 13.866  12.452  26.503  1.00 11.74 ? 226 PHE D CG  1 
ATOM   8204 C  CD1 . PHE D 1 225 ? 12.781  12.926  27.202  1.00 16.69 ? 226 PHE D CD1 1 
ATOM   8205 C  CD2 . PHE D 1 225 ? 15.140  12.690  27.025  1.00 17.00 ? 226 PHE D CD2 1 
ATOM   8206 C  CE1 . PHE D 1 225 ? 12.970  13.610  28.407  1.00 16.17 ? 226 PHE D CE1 1 
ATOM   8207 C  CE2 . PHE D 1 225 ? 15.328  13.372  28.209  1.00 18.25 ? 226 PHE D CE2 1 
ATOM   8208 C  CZ  . PHE D 1 225 ? 14.236  13.825  28.908  1.00 18.85 ? 226 PHE D CZ  1 
ATOM   8209 N  N   . ARG D 1 226 ? 12.800  9.777   22.959  1.00 11.40 ? 227 ARG D N   1 
ATOM   8210 C  CA  . ARG D 1 226 ? 13.219  9.168   21.677  1.00 13.63 ? 227 ARG D CA  1 
ATOM   8211 C  C   . ARG D 1 226 ? 12.083  9.111   20.639  1.00 11.52 ? 227 ARG D C   1 
ATOM   8212 O  O   . ARG D 1 226 ? 12.328  8.720   19.487  1.00 13.87 ? 227 ARG D O   1 
ATOM   8213 C  CB  . ARG D 1 226 ? 13.705  7.758   21.928  1.00 12.28 ? 227 ARG D CB  1 
ATOM   8214 C  CG  . ARG D 1 226 ? 14.918  7.648   22.850  1.00 11.91 ? 227 ARG D CG  1 
ATOM   8215 C  CD  . ARG D 1 226 ? 15.390  6.222   22.898  1.00 14.03 ? 227 ARG D CD  1 
ATOM   8216 N  NE  . ARG D 1 226 ? 16.460  6.068   23.903  1.00 12.30 ? 227 ARG D NE  1 
ATOM   8217 C  CZ  . ARG D 1 226 ? 16.484  5.201   24.889  1.00 11.90 ? 227 ARG D CZ  1 
ATOM   8218 N  NH1 . ARG D 1 226 ? 15.535  4.265   24.991  1.00 17.34 ? 227 ARG D NH1 1 
ATOM   8219 N  NH2 . ARG D 1 226 ? 17.457  5.272   25.803  1.00 14.61 ? 227 ARG D NH2 1 
ATOM   8220 N  N   . LYS D 1 227 ? 10.896  9.591   21.014  1.00 13.63 ? 228 LYS D N   1 
ATOM   8221 C  CA  . LYS D 1 227 ? 9.801   9.788   20.001  1.00 14.26 ? 228 LYS D CA  1 
ATOM   8222 C  C   . LYS D 1 227 ? 9.863   11.143  19.297  1.00 13.43 ? 228 LYS D C   1 
ATOM   8223 O  O   . LYS D 1 227 ? 9.157   11.332  18.286  1.00 14.39 ? 228 LYS D O   1 
ATOM   8224 C  CB  . LYS D 1 227 ? 8.442   9.619   20.713  1.00 16.93 ? 228 LYS D CB  1 
ATOM   8225 C  CG  . LYS D 1 227 ? 8.206   8.173   21.126  1.00 19.51 ? 228 LYS D CG  1 
ATOM   8226 C  CD  . LYS D 1 227 ? 6.969   7.931   21.978  1.00 24.71 ? 228 LYS D CD  1 
ATOM   8227 C  CE  . LYS D 1 227 ? 5.681   8.513   21.411  1.00 45.93 ? 228 LYS D CE  1 
ATOM   8228 N  NZ  . LYS D 1 227 ? 4.788   7.495   20.787  1.00 51.79 ? 228 LYS D NZ  1 
ATOM   8229 N  N   . LEU D 1 228 ? 10.626  12.099  19.818  1.00 14.21 ? 229 LEU D N   1 
ATOM   8230 C  CA  . LEU D 1 228 ? 10.840  13.372  19.111  1.00 11.73 ? 229 LEU D CA  1 
ATOM   8231 C  C   . LEU D 1 228 ? 11.501  13.150  17.737  1.00 12.66 ? 229 LEU D C   1 
ATOM   8232 O  O   . LEU D 1 228 ? 12.049  12.116  17.490  1.00 12.33 ? 229 LEU D O   1 
ATOM   8233 C  CB  . LEU D 1 228 ? 11.668  14.330  19.973  1.00 11.22 ? 229 LEU D CB  1 
ATOM   8234 C  CG  . LEU D 1 228 ? 10.996  14.787  21.275  1.00 10.59 ? 229 LEU D CG  1 
ATOM   8235 C  CD1 . LEU D 1 228 ? 12.040  15.424  22.181  1.00 12.39 ? 229 LEU D CD1 1 
ATOM   8236 C  CD2 . LEU D 1 228 ? 9.899   15.825  20.970  1.00 15.34 ? 229 LEU D CD2 1 
ATOM   8237 N  N   . ASN D 1 229 ? 11.353  14.147  16.833  1.00 12.81 ? 230 ASN D N   1 
ATOM   8238 C  CA  . ASN D 1 229 ? 11.901  14.094  15.486  1.00 13.33 ? 230 ASN D CA  1 
ATOM   8239 C  C   . ASN D 1 229 ? 12.904  15.252  15.283  1.00 13.86 ? 230 ASN D C   1 
ATOM   8240 O  O   . ASN D 1 229 ? 12.641  16.382  15.720  1.00 15.53 ? 230 ASN D O   1 
ATOM   8241 C  CB  . ASN D 1 229 ? 10.730  14.332  14.473  1.00 14.72 ? 230 ASN D CB  1 
ATOM   8242 C  CG  . ASN D 1 229 ? 9.788   13.150  14.270  1.00 15.38 ? 230 ASN D CG  1 
ATOM   8243 O  OD1 . ASN D 1 229 ? 8.929   13.252  13.399  1.00 21.59 ? 230 ASN D OD1 1 
ATOM   8244 N  ND2 . ASN D 1 229 ? 9.898   12.063  15.031  1.00 16.97 ? 230 ASN D ND2 1 
ATOM   8245 N  N   . PHE D 1 230 ? 13.991  14.964  14.563  1.00 14.29 ? 231 PHE D N   1 
ATOM   8246 C  CA  . PHE D 1 230 ? 14.920  15.998  14.093  1.00 13.42 ? 231 PHE D CA  1 
ATOM   8247 C  C   . PHE D 1 230 ? 14.251  16.803  12.944  1.00 15.88 ? 231 PHE D C   1 
ATOM   8248 O  O   . PHE D 1 230 ? 14.515  17.990  12.795  1.00 16.95 ? 231 PHE D O   1 
ATOM   8249 C  CB  . PHE D 1 230 ? 16.172  15.372  13.466  1.00 15.86 ? 231 PHE D CB  1 
ATOM   8250 C  CG  . PHE D 1 230 ? 17.162  14.764  14.463  1.00 14.95 ? 231 PHE D CG  1 
ATOM   8251 C  CD1 . PHE D 1 230 ? 17.680  15.567  15.510  1.00 15.94 ? 231 PHE D CD1 1 
ATOM   8252 C  CD2 . PHE D 1 230 ? 17.679  13.484  14.278  1.00 15.02 ? 231 PHE D CD2 1 
ATOM   8253 C  CE1 . PHE D 1 230 ? 18.675  15.031  16.370  1.00 15.38 ? 231 PHE D CE1 1 
ATOM   8254 C  CE2 . PHE D 1 230 ? 18.649  12.932  15.095  1.00 14.32 ? 231 PHE D CE2 1 
ATOM   8255 C  CZ  . PHE D 1 230 ? 19.151  13.748  16.142  1.00 14.28 ? 231 PHE D CZ  1 
ATOM   8256 N  N   . ASN D 1 231 ? 13.496  16.110  12.081  1.00 15.98 ? 232 ASN D N   1 
ATOM   8257 C  CA  . ASN D 1 231 ? 12.867  16.706  10.863  1.00 14.74 ? 232 ASN D CA  1 
ATOM   8258 C  C   . ASN D 1 231 ? 11.745  17.648  11.233  1.00 15.93 ? 232 ASN D C   1 
ATOM   8259 O  O   . ASN D 1 231 ? 11.126  17.540  12.294  1.00 14.71 ? 232 ASN D O   1 
ATOM   8260 C  CB  . ASN D 1 231 ? 12.318  15.585  9.979   1.00 16.16 ? 232 ASN D CB  1 
ATOM   8261 C  CG  . ASN D 1 231 ? 11.412  14.664  10.735  1.00 17.79 ? 232 ASN D CG  1 
ATOM   8262 O  OD1 . ASN D 1 231 ? 11.884  13.814  11.492  1.00 16.67 ? 232 ASN D OD1 1 
ATOM   8263 N  ND2 . ASN D 1 231 ? 10.102  14.791  10.526  1.00 18.99 ? 232 ASN D ND2 1 
ATOM   8264 N  N   . GLY D 1 232 ? 11.450  18.584  10.336  1.00 15.54 ? 233 GLY D N   1 
ATOM   8265 C  CA  . GLY D 1 232 ? 10.215  19.306  10.429  1.00 18.17 ? 233 GLY D CA  1 
ATOM   8266 C  C   . GLY D 1 232 ? 8.951   18.484  10.014  1.00 18.80 ? 233 GLY D C   1 
ATOM   8267 O  O   . GLY D 1 232 ? 9.095   17.451  9.355   1.00 24.76 ? 233 GLY D O   1 
ATOM   8268 N  N   . GLU D 1 233 ? 7.758   18.956  10.411  1.00 24.39 ? 234 GLU D N   1 
ATOM   8269 C  CA  . GLU D 1 233 ? 6.446   18.440  9.992   1.00 28.22 ? 234 GLU D CA  1 
ATOM   8270 C  C   . GLU D 1 233 ? 6.409   18.314  8.469   1.00 33.85 ? 234 GLU D C   1 
ATOM   8271 O  O   . GLU D 1 233 ? 6.799   19.219  7.744   1.00 28.90 ? 234 GLU D O   1 
ATOM   8272 C  CB  . GLU D 1 233 ? 5.302   19.304  10.596  1.00 28.38 ? 234 GLU D CB  1 
ATOM   8273 C  CG  . GLU D 1 233 ? 3.893   18.679  10.575  1.00 27.92 ? 234 GLU D CG  1 
ATOM   8274 C  CD  . GLU D 1 233 ? 2.819   19.559  11.204  1.00 31.89 ? 234 GLU D CD  1 
ATOM   8275 O  OE1 . GLU D 1 233 ? 3.041   20.740  11.646  1.00 37.96 ? 234 GLU D OE1 1 
ATOM   8276 O  OE2 . GLU D 1 233 ? 1.676   19.072  11.186  1.00 48.43 ? 234 GLU D OE2 1 
ATOM   8277 N  N   . GLY D 1 234 ? 6.051   17.115  8.004   1.00 33.14 ? 235 GLY D N   1 
ATOM   8278 C  CA  . GLY D 1 234 ? 6.047   16.764  6.574   1.00 43.87 ? 235 GLY D CA  1 
ATOM   8279 C  C   . GLY D 1 234 ? 7.377   16.608  5.813   1.00 43.12 ? 235 GLY D C   1 
ATOM   8280 O  O   . GLY D 1 234 ? 7.349   16.807  4.574   1.00 70.48 ? 235 GLY D O   1 
ATOM   8281 N  N   . GLU D 1 235 ? 8.506   16.269  6.506   1.00 41.18 ? 236 GLU D N   1 
ATOM   8282 C  CA  . GLU D 1 235 ? 9.750   15.815  5.845   1.00 29.04 ? 236 GLU D CA  1 
ATOM   8283 C  C   . GLU D 1 235 ? 9.906   14.372  6.339   1.00 24.14 ? 236 GLU D C   1 
ATOM   8284 O  O   . GLU D 1 235 ? 9.237   14.009  7.253   1.00 25.31 ? 236 GLU D O   1 
ATOM   8285 C  CB  . GLU D 1 235 ? 11.000  16.588  6.225   1.00 29.54 ? 236 GLU D CB  1 
ATOM   8286 C  CG  . GLU D 1 235 ? 10.848  18.081  6.002   1.00 34.93 ? 236 GLU D CG  1 
ATOM   8287 C  CD  . GLU D 1 235 ? 11.577  18.964  7.006   1.00 46.50 ? 236 GLU D CD  1 
ATOM   8288 O  OE1 . GLU D 1 235 ? 12.551  18.550  7.680   1.00 35.20 ? 236 GLU D OE1 1 
ATOM   8289 O  OE2 . GLU D 1 235 ? 11.147  20.123  7.086   1.00 36.58 ? 236 GLU D OE2 1 
ATOM   8290 N  N   . PRO D 1 236 ? 10.739  13.539  5.684   1.00 23.09 ? 237 PRO D N   1 
ATOM   8291 C  CA  . PRO D 1 236 ? 10.740  12.172  6.232   1.00 20.00 ? 237 PRO D CA  1 
ATOM   8292 C  C   . PRO D 1 236 ? 11.116  12.064  7.746   1.00 16.28 ? 237 PRO D C   1 
ATOM   8293 O  O   . PRO D 1 236 ? 12.030  12.772  8.209   1.00 17.44 ? 237 PRO D O   1 
ATOM   8294 C  CB  . PRO D 1 236 ? 11.795  11.446  5.348   1.00 19.91 ? 237 PRO D CB  1 
ATOM   8295 C  CG  . PRO D 1 236 ? 11.821  12.236  4.076   1.00 23.88 ? 237 PRO D CG  1 
ATOM   8296 C  CD  . PRO D 1 236 ? 11.606  13.670  4.505   1.00 24.62 ? 237 PRO D CD  1 
ATOM   8297 N  N   . GLU D 1 237 ? 10.469  11.169  8.498   1.00 19.16 ? 238 GLU D N   1 
ATOM   8298 C  CA  . GLU D 1 237 ? 10.624  11.082  9.967   1.00 17.75 ? 238 GLU D CA  1 
ATOM   8299 C  C   . GLU D 1 237 ? 12.006  10.483  10.315  1.00 16.14 ? 238 GLU D C   1 
ATOM   8300 O  O   . GLU D 1 237 ? 12.387  9.401   9.877   1.00 18.80 ? 238 GLU D O   1 
ATOM   8301 C  CB  . GLU D 1 237 ? 9.578   10.181  10.600  1.00 20.98 ? 238 GLU D CB  1 
ATOM   8302 C  CG  . GLU D 1 237 ? 9.866   10.047  12.064  1.00 23.74 ? 238 GLU D CG  1 
ATOM   8303 C  CD  . GLU D 1 237 ? 8.728   9.433   12.890  1.00 24.53 ? 238 GLU D CD  1 
ATOM   8304 O  OE1 . GLU D 1 237 ? 8.096   8.511   12.343  1.00 34.35 ? 238 GLU D OE1 1 
ATOM   8305 O  OE2 . GLU D 1 237 ? 8.419   9.859   14.060  1.00 22.06 ? 238 GLU D OE2 1 
ATOM   8306 N  N   . GLU D 1 238 ? 12.815  11.272  11.054  1.00 15.08 ? 239 GLU D N   1 
ATOM   8307 C  CA  . GLU D 1 238 ? 14.142  10.864  11.563  1.00 17.07 ? 239 GLU D CA  1 
ATOM   8308 C  C   . GLU D 1 238 ? 14.080  11.091  13.072  1.00 15.93 ? 239 GLU D C   1 
ATOM   8309 O  O   . GLU D 1 238 ? 13.930  12.222  13.524  1.00 15.84 ? 239 GLU D O   1 
ATOM   8310 C  CB  . GLU D 1 238 ? 15.352  11.660  10.920  1.00 17.25 ? 239 GLU D CB  1 
ATOM   8311 C  CG  . GLU D 1 238 ? 15.645  11.246  9.397   1.00 17.18 ? 239 GLU D CG  1 
ATOM   8312 C  CD  . GLU D 1 238 ? 16.846  11.965  8.868   1.00 20.09 ? 239 GLU D CD  1 
ATOM   8313 O  OE1 . GLU D 1 238 ? 17.969  11.611  9.321   1.00 28.45 ? 239 GLU D OE1 1 
ATOM   8314 O  OE2 . GLU D 1 238 ? 16.696  12.824  7.965   1.00 22.33 ? 239 GLU D OE2 1 
ATOM   8315 N  N   . LEU D 1 239 ? 14.094  10.010  13.846  1.00 14.33 ? 240 LEU D N   1 
ATOM   8316 C  CA  . LEU D 1 239 ? 13.906  10.127  15.291  1.00 14.41 ? 240 LEU D CA  1 
ATOM   8317 C  C   . LEU D 1 239 ? 15.066  10.952  15.895  1.00 14.19 ? 240 LEU D C   1 
ATOM   8318 O  O   . LEU D 1 239 ? 16.211  10.756  15.529  1.00 14.04 ? 240 LEU D O   1 
ATOM   8319 C  CB  . LEU D 1 239 ? 13.851  8.760   15.985  1.00 17.07 ? 240 LEU D CB  1 
ATOM   8320 C  CG  . LEU D 1 239 ? 12.656  7.900   15.710  1.00 16.97 ? 240 LEU D CG  1 
ATOM   8321 C  CD1 . LEU D 1 239 ? 12.868  6.636   16.544  1.00 23.79 ? 240 LEU D CD1 1 
ATOM   8322 C  CD2 . LEU D 1 239 ? 11.356  8.640   16.035  1.00 16.66 ? 240 LEU D CD2 1 
ATOM   8323 N  N   . MET D 1 240 ? 14.720  11.830  16.841  1.00 12.13 ? 241 MET D N   1 
ATOM   8324 C  CA  . MET D 1 240 ? 15.735  12.621  17.547  1.00 12.89 ? 241 MET D CA  1 
ATOM   8325 C  C   . MET D 1 240 ? 16.366  11.770  18.627  1.00 12.30 ? 241 MET D C   1 
ATOM   8326 O  O   . MET D 1 240 ? 15.781  11.638  19.696  1.00 11.22 ? 241 MET D O   1 
ATOM   8327 C  CB  . MET D 1 240 ? 15.057  13.826  18.184  1.00 14.26 ? 241 MET D CB  1 
ATOM   8328 C  CG  . MET D 1 240 ? 16.022  14.820  18.867  1.00 13.56 ? 241 MET D CG  1 
ATOM   8329 S  SD  . MET D 1 240 ? 15.195  16.255  19.550  1.00 14.51 ? 241 MET D SD  1 
ATOM   8330 C  CE  . MET D 1 240 ? 15.032  17.252  18.076  1.00 13.87 ? 241 MET D CE  1 
ATOM   8331 N  N   . VAL D 1 241 ? 17.463  11.136  18.262  1.00 10.94 ? 242 VAL D N   1 
ATOM   8332 C  CA  . VAL D 1 241 ? 18.219  10.287  19.192  1.00 11.13 ? 242 VAL D CA  1 
ATOM   8333 C  C   . VAL D 1 241 ? 19.698  10.520  18.865  1.00 10.22 ? 242 VAL D C   1 
ATOM   8334 O  O   . VAL D 1 241 ? 20.041  10.887  17.706  1.00 11.64 ? 242 VAL D O   1 
ATOM   8335 C  CB  . VAL D 1 241 ? 17.899  8.765   19.040  1.00 11.12 ? 242 VAL D CB  1 
ATOM   8336 C  CG1 . VAL D 1 241 ? 16.450  8.533   19.479  1.00 14.70 ? 242 VAL D CG1 1 
ATOM   8337 C  CG2 . VAL D 1 241 ? 18.153  8.304   17.605  1.00 13.46 ? 242 VAL D CG2 1 
ATOM   8338 N  N   . ASP D 1 242 ? 20.582  10.274  19.832  1.00 10.42 ? 243 ASP D N   1 
ATOM   8339 C  CA  . ASP D 1 242 ? 22.024  10.389  19.589  1.00 10.58 ? 243 ASP D CA  1 
ATOM   8340 C  C   . ASP D 1 242 ? 22.399  11.794  19.227  1.00 9.96  ? 243 ASP D C   1 
ATOM   8341 O  O   . ASP D 1 242 ? 23.252  12.003  18.359  1.00 12.13 ? 243 ASP D O   1 
ATOM   8342 C  CB  . ASP D 1 242 ? 22.599  9.296   18.638  1.00 10.86 ? 243 ASP D CB  1 
ATOM   8343 C  CG  . ASP D 1 242 ? 22.457  7.919   19.263  1.00 9.65  ? 243 ASP D CG  1 
ATOM   8344 O  OD1 . ASP D 1 242 ? 22.699  7.744   20.493  1.00 10.91 ? 243 ASP D OD1 1 
ATOM   8345 O  OD2 . ASP D 1 242 ? 22.064  6.956   18.535  1.00 14.02 ? 243 ASP D OD2 1 
ATOM   8346 N  N   . ASN D 1 243 ? 21.820  12.728  19.979  1.00 8.55  ? 244 ASN D N   1 
ATOM   8347 C  CA  . ASN D 1 243 ? 22.145  14.140  19.763  1.00 9.92  ? 244 ASN D CA  1 
ATOM   8348 C  C   . ASN D 1 243 ? 23.249  14.621  20.767  1.00 8.47  ? 244 ASN D C   1 
ATOM   8349 O  O   . ASN D 1 243 ? 23.050  15.654  21.420  1.00 9.52  ? 244 ASN D O   1 
ATOM   8350 C  CB  . ASN D 1 243 ? 20.871  15.015  19.830  1.00 9.75  ? 244 ASN D CB  1 
ATOM   8351 C  CG  . ASN D 1 243 ? 20.109  14.856  21.109  1.00 9.91  ? 244 ASN D CG  1 
ATOM   8352 O  OD1 . ASN D 1 243 ? 20.463  14.029  21.985  1.00 10.89 ? 244 ASN D OD1 1 
ATOM   8353 N  ND2 . ASN D 1 243 ? 19.100  15.643  21.284  1.00 13.45 ? 244 ASN D ND2 1 
ATOM   8354 N  N   . TRP D 1 244 ? 24.333  13.866  20.844  1.00 8.59  ? 245 TRP D N   1 
ATOM   8355 C  CA  . TRP D 1 244 ? 25.457  14.114  21.740  1.00 8.16  ? 245 TRP D CA  1 
ATOM   8356 C  C   . TRP D 1 244 ? 26.710  14.195  20.942  1.00 9.34  ? 245 TRP D C   1 
ATOM   8357 O  O   . TRP D 1 244 ? 26.884  13.480  19.978  1.00 10.10 ? 245 TRP D O   1 
ATOM   8358 C  CB  . TRP D 1 244 ? 25.586  13.013  22.833  1.00 8.69  ? 245 TRP D CB  1 
ATOM   8359 C  CG  . TRP D 1 244 ? 25.511  11.597  22.367  1.00 8.49  ? 245 TRP D CG  1 
ATOM   8360 C  CD1 . TRP D 1 244 ? 24.349  10.849  22.055  1.00 9.30  ? 245 TRP D CD1 1 
ATOM   8361 C  CD2 . TRP D 1 244 ? 26.652  10.722  22.134  1.00 8.93  ? 245 TRP D CD2 1 
ATOM   8362 N  NE1 . TRP D 1 244 ? 24.764  9.577   21.671  1.00 9.49  ? 245 TRP D NE1 1 
ATOM   8363 C  CE2 . TRP D 1 244 ? 26.124  9.453   21.701  1.00 8.99  ? 245 TRP D CE2 1 
ATOM   8364 C  CE3 . TRP D 1 244 ? 28.039  10.853  22.339  1.00 10.06 ? 245 TRP D CE3 1 
ATOM   8365 C  CZ2 . TRP D 1 244 ? 26.961  8.356   21.401  1.00 9.74  ? 245 TRP D CZ2 1 
ATOM   8366 C  CZ3 . TRP D 1 244 ? 28.857  9.769   22.028  1.00 10.69 ? 245 TRP D CZ3 1 
ATOM   8367 C  CH2 . TRP D 1 244 ? 28.318  8.527   21.585  1.00 11.95 ? 245 TRP D CH2 1 
ATOM   8368 N  N   . ARG D 1 245 ? 27.581  15.104  21.375  1.00 8.40  ? 246 ARG D N   1 
ATOM   8369 C  CA  . ARG D 1 245 ? 28.971  15.225  20.853  1.00 8.88  ? 246 ARG D CA  1 
ATOM   8370 C  C   . ARG D 1 245 ? 29.816  14.261  21.683  1.00 8.71  ? 246 ARG D C   1 
ATOM   8371 O  O   . ARG D 1 245 ? 29.701  14.292  22.908  1.00 10.48 ? 246 ARG D O   1 
ATOM   8372 C  CB  . ARG D 1 245 ? 29.471  16.675  20.965  1.00 9.02  ? 246 ARG D CB  1 
ATOM   8373 C  CG  . ARG D 1 245 ? 30.801  16.868  20.279  1.00 9.28  ? 246 ARG D CG  1 
ATOM   8374 C  CD  . ARG D 1 245 ? 31.359  18.224  20.608  1.00 9.60  ? 246 ARG D CD  1 
ATOM   8375 N  NE  . ARG D 1 245 ? 32.412  18.591  19.639  1.00 9.86  ? 246 ARG D NE  1 
ATOM   8376 C  CZ  . ARG D 1 245 ? 33.278  19.597  19.724  1.00 10.53 ? 246 ARG D CZ  1 
ATOM   8377 N  NH1 . ARG D 1 245 ? 33.278  20.409  20.778  1.00 11.71 ? 246 ARG D NH1 1 
ATOM   8378 N  NH2 . ARG D 1 245 ? 34.162  19.806  18.758  1.00 11.75 ? 246 ARG D NH2 1 
ATOM   8379 N  N   . PRO D 1 246 ? 30.724  13.482  21.074  1.00 10.15 ? 247 PRO D N   1 
ATOM   8380 C  CA  . PRO D 1 246 ? 31.612  12.669  21.841  1.00 10.00 ? 247 PRO D CA  1 
ATOM   8381 C  C   . PRO D 1 246 ? 32.631  13.512  22.626  1.00 8.94  ? 247 PRO D C   1 
ATOM   8382 O  O   . PRO D 1 246 ? 32.906  14.684  22.322  1.00 9.61  ? 247 PRO D O   1 
ATOM   8383 C  CB  . PRO D 1 246 ? 32.288  11.760  20.825  1.00 14.07 ? 247 PRO D CB  1 
ATOM   8384 C  CG  . PRO D 1 246 ? 31.427  11.833  19.604  1.00 18.27 ? 247 PRO D CG  1 
ATOM   8385 C  CD  . PRO D 1 246 ? 30.882  13.243  19.625  1.00 12.42 ? 247 PRO D CD  1 
ATOM   8386 N  N   . ALA D 1 247 ? 33.311  12.825  23.549  1.00 10.40 ? 248 ALA D N   1 
ATOM   8387 C  CA  . ALA D 1 247 ? 34.406  13.447  24.348  1.00 9.65  ? 248 ALA D CA  1 
ATOM   8388 C  C   . ALA D 1 247 ? 35.483  13.979  23.453  1.00 10.69 ? 248 ALA D C   1 
ATOM   8389 O  O   . ALA D 1 247 ? 35.886  13.321  22.476  1.00 12.34 ? 248 ALA D O   1 
ATOM   8390 C  CB  . ALA D 1 247 ? 34.986  12.419  25.306  1.00 12.46 ? 248 ALA D CB  1 
ATOM   8391 N  N   . GLN D 1 248 ? 36.026  15.162  23.771  1.00 9.89  ? 249 GLN D N   1 
ATOM   8392 C  CA  . GLN D 1 248 ? 37.050  15.882  22.971  1.00 9.74  ? 249 GLN D CA  1 
ATOM   8393 C  C   . GLN D 1 248 ? 38.335  15.856  23.792  1.00 10.91 ? 249 GLN D C   1 
ATOM   8394 O  O   . GLN D 1 248 ? 38.368  15.664  25.009  1.00 11.69 ? 249 GLN D O   1 
ATOM   8395 C  CB  . GLN D 1 248 ? 36.620  17.319  22.750  1.00 10.47 ? 249 GLN D CB  1 
ATOM   8396 C  CG  . GLN D 1 248 ? 35.325  17.404  21.986  1.00 11.69 ? 249 GLN D CG  1 
ATOM   8397 C  CD  . GLN D 1 248 ? 35.404  16.717  20.593  1.00 12.18 ? 249 GLN D CD  1 
ATOM   8398 O  OE1 . GLN D 1 248 ? 36.299  17.056  19.821  1.00 15.16 ? 249 GLN D OE1 1 
ATOM   8399 N  NE2 . GLN D 1 248 ? 34.542  15.755  20.281  1.00 12.31 ? 249 GLN D NE2 1 
ATOM   8400 N  N   . PRO D 1 249 ? 39.487  16.147  23.146  1.00 13.09 ? 250 PRO D N   1 
ATOM   8401 C  CA  . PRO D 1 249 ? 40.760  16.131  23.823  1.00 14.48 ? 250 PRO D CA  1 
ATOM   8402 C  C   . PRO D 1 249 ? 40.816  17.121  24.994  1.00 10.73 ? 250 PRO D C   1 
ATOM   8403 O  O   . PRO D 1 249 ? 40.512  18.294  24.845  1.00 13.32 ? 250 PRO D O   1 
ATOM   8404 C  CB  . PRO D 1 249 ? 41.751  16.522  22.688  1.00 19.13 ? 250 PRO D CB  1 
ATOM   8405 C  CG  . PRO D 1 249 ? 41.086  16.024  21.461  1.00 21.54 ? 250 PRO D CG  1 
ATOM   8406 C  CD  . PRO D 1 249 ? 39.642  16.373  21.721  1.00 16.03 ? 250 PRO D CD  1 
ATOM   8407 N  N   . LEU D 1 250 ? 41.319  16.651  26.108  1.00 12.81 ? 251 LEU D N   1 
ATOM   8408 C  CA  . LEU D 1 250 ? 41.445  17.546  27.287  1.00 12.54 ? 251 LEU D CA  1 
ATOM   8409 C  C   . LEU D 1 250 ? 42.535  18.568  27.157  1.00 12.58 ? 251 LEU D C   1 
ATOM   8410 O  O   . LEU D 1 250 ? 42.434  19.705  27.641  1.00 12.60 ? 251 LEU D O   1 
ATOM   8411 C  CB  . LEU D 1 250 ? 41.708  16.664  28.508  1.00 12.78 ? 251 LEU D CB  1 
ATOM   8412 C  CG  . LEU D 1 250 ? 41.703  17.314  29.910  1.00 13.91 ? 251 LEU D CG  1 
ATOM   8413 C  CD1 . LEU D 1 250 ? 40.301  17.935  30.230  1.00 13.57 ? 251 LEU D CD1 1 
ATOM   8414 C  CD2 . LEU D 1 250 ? 42.122  16.357  31.047  1.00 16.69 ? 251 LEU D CD2 1 
ATOM   8415 N  N   . LYS D 1 251 ? 43.600  18.221  26.437  1.00 16.24 ? 252 LYS D N   1 
ATOM   8416 C  CA  . LYS D 1 251 ? 44.697  19.130  26.119  1.00 16.34 ? 252 LYS D CA  1 
ATOM   8417 C  C   . LYS D 1 251 ? 45.322  19.585  27.424  1.00 17.76 ? 252 LYS D C   1 
ATOM   8418 O  O   . LYS D 1 251 ? 45.565  18.708  28.255  1.00 26.07 ? 252 LYS D O   1 
ATOM   8419 C  CB  . LYS D 1 251 ? 44.275  20.195  25.116  1.00 19.69 ? 252 LYS D CB  1 
ATOM   8420 C  CG  . LYS D 1 251 ? 43.953  19.535  23.779  1.00 22.11 ? 252 LYS D CG  1 
ATOM   8421 C  CD  . LYS D 1 251 ? 43.731  20.514  22.639  1.00 30.01 ? 252 LYS D CD  1 
ATOM   8422 C  CE  . LYS D 1 251 ? 43.493  19.743  21.346  1.00 32.16 ? 252 LYS D CE  1 
ATOM   8423 N  NZ  . LYS D 1 251 ? 42.975  20.626  20.277  1.00 31.02 ? 252 LYS D NZ  1 
ATOM   8424 N  N   . ASN D 1 252 ? 45.615  20.843  27.656  1.00 18.25 ? 253 ASN D N   1 
ATOM   8425 C  CA  . ASN D 1 252 ? 46.341  21.094  28.880  1.00 28.32 ? 253 ASN D CA  1 
ATOM   8426 C  C   . ASN D 1 252 ? 45.501  21.164  30.157  1.00 24.48 ? 253 ASN D C   1 
ATOM   8427 O  O   . ASN D 1 252 ? 46.058  21.412  31.259  1.00 24.39 ? 253 ASN D O   1 
ATOM   8428 C  CB  . ASN D 1 252 ? 47.282  22.288  28.707  1.00 38.19 ? 253 ASN D CB  1 
ATOM   8429 C  CG  . ASN D 1 252 ? 48.447  21.955  27.795  1.00 48.45 ? 253 ASN D CG  1 
ATOM   8430 O  OD1 . ASN D 1 252 ? 48.783  20.783  27.623  1.00 45.43 ? 253 ASN D OD1 1 
ATOM   8431 N  ND2 . ASN D 1 252 ? 49.054  22.970  27.195  1.00 59.92 ? 253 ASN D ND2 1 
ATOM   8432 N  N   . ARG D 1 253 ? 44.198  20.955  30.080  1.00 16.56 ? 254 ARG D N   1 
ATOM   8433 C  CA  . ARG D 1 253 ? 43.324  21.365  31.168  1.00 11.16 ? 254 ARG D CA  1 
ATOM   8434 C  C   . ARG D 1 253 ? 43.361  20.439  32.344  1.00 12.87 ? 254 ARG D C   1 
ATOM   8435 O  O   . ARG D 1 253 ? 43.576  19.232  32.214  1.00 17.48 ? 254 ARG D O   1 
ATOM   8436 C  CB  . ARG D 1 253 ? 41.898  21.490  30.603  1.00 9.95  ? 254 ARG D CB  1 
ATOM   8437 C  CG  . ARG D 1 253 ? 41.770  22.598  29.569  1.00 10.78 ? 254 ARG D CG  1 
ATOM   8438 C  CD  . ARG D 1 253 ? 40.406  22.639  28.911  1.00 9.88  ? 254 ARG D CD  1 
ATOM   8439 N  NE  . ARG D 1 253 ? 40.235  21.443  28.058  1.00 10.19 ? 254 ARG D NE  1 
ATOM   8440 C  CZ  . ARG D 1 253 ? 39.118  21.177  27.396  1.00 9.31  ? 254 ARG D CZ  1 
ATOM   8441 N  NH1 . ARG D 1 253 ? 37.991  21.876  27.610  1.00 10.18 ? 254 ARG D NH1 1 
ATOM   8442 N  NH2 . ARG D 1 253 ? 39.077  20.153  26.549  1.00 10.16 ? 254 ARG D NH2 1 
ATOM   8443 N  N   . GLN D 1 254 ? 42.989  20.984  33.505  1.00 12.43 ? 255 GLN D N   1 
ATOM   8444 C  CA  . GLN D 1 254 ? 42.814  20.237  34.759  1.00 14.14 ? 255 GLN D CA  1 
ATOM   8445 C  C   . GLN D 1 254 ? 41.331  20.251  35.078  1.00 13.59 ? 255 GLN D C   1 
ATOM   8446 O  O   . GLN D 1 254 ? 40.657  21.291  34.983  1.00 14.73 ? 255 GLN D O   1 
ATOM   8447 C  CB  . GLN D 1 254 ? 43.549  20.934  35.898  1.00 17.37 ? 255 GLN D CB  1 
ATOM   8448 C  CG  . GLN D 1 254 ? 43.607  20.266  37.275  1.00 30.79 ? 255 GLN D CG  1 
ATOM   8449 C  CD  . GLN D 1 254 ? 44.566  19.099  37.410  1.00 70.75 ? 255 GLN D CD  1 
ATOM   8450 O  OE1 . GLN D 1 254 ? 44.166  17.896  37.294  1.00 65.47 ? 255 GLN D OE1 1 
ATOM   8451 N  NE2 . GLN D 1 254 ? 45.838  19.425  37.718  1.00 54.36 ? 255 GLN D NE2 1 
ATOM   8452 N  N   . ILE D 1 255 ? 40.846  19.093  35.443  1.00 11.42 ? 256 ILE D N   1 
ATOM   8453 C  CA  . ILE D 1 255 ? 39.497  18.952  36.034  1.00 11.24 ? 256 ILE D CA  1 
ATOM   8454 C  C   . ILE D 1 255 ? 39.654  18.883  37.560  1.00 11.10 ? 256 ILE D C   1 
ATOM   8455 O  O   . ILE D 1 255 ? 40.547  18.203  38.091  1.00 12.00 ? 256 ILE D O   1 
ATOM   8456 C  CB  . ILE D 1 255 ? 38.804  17.691  35.519  1.00 10.67 ? 256 ILE D CB  1 
ATOM   8457 C  CG1 . ILE D 1 255 ? 38.754  17.721  33.903  1.00 11.66 ? 256 ILE D CG1 1 
ATOM   8458 C  CG2 . ILE D 1 255 ? 37.357  17.622  36.161  1.00 12.94 ? 256 ILE D CG2 1 
ATOM   8459 C  CD1 . ILE D 1 255 ? 38.114  16.444  33.399  1.00 12.79 ? 256 ILE D CD1 1 
ATOM   8460 N  N   . LYS D 1 256 ? 38.909  19.756  38.227  1.00 10.00 ? 257 LYS D N   1 
ATOM   8461 C  CA  . LYS D 1 256 ? 38.941  19.860  39.686  1.00 11.06 ? 257 LYS D CA  1 
ATOM   8462 C  C   . LYS D 1 256 ? 37.696  19.247  40.297  1.00 10.44 ? 257 LYS D C   1 
ATOM   8463 O  O   . LYS D 1 256 ? 36.612  19.329  39.701  1.00 12.30 ? 257 LYS D O   1 
ATOM   8464 C  CB  . LYS D 1 256 ? 39.080  21.359  40.106  1.00 13.10 ? 257 LYS D CB  1 
ATOM   8465 C  CG  . LYS D 1 256 ? 40.439  21.900  39.574  1.00 18.36 ? 257 LYS D CG  1 
ATOM   8466 C  CD  . LYS D 1 256 ? 40.708  23.318  39.839  1.00 25.27 ? 257 LYS D CD  1 
ATOM   8467 C  CE  . LYS D 1 256 ? 42.089  23.691  39.262  1.00 37.45 ? 257 LYS D CE  1 
ATOM   8468 N  NZ  . LYS D 1 256 ? 42.335  25.178  39.352  1.00 34.42 ? 257 LYS D NZ  1 
ATOM   8469 N  N   . ALA D 1 257 ? 37.779  18.584  41.431  1.00 11.31 ? 258 ALA D N   1 
ATOM   8470 C  CA  . ALA D 1 257 ? 36.719  17.991  42.211  1.00 11.33 ? 258 ALA D CA  1 
ATOM   8471 C  C   . ALA D 1 257 ? 36.435  18.795  43.445  1.00 11.26 ? 258 ALA D C   1 
ATOM   8472 O  O   . ALA D 1 257 ? 37.401  19.251  44.162  1.00 11.57 ? 258 ALA D O   1 
ATOM   8473 C  CB  . ALA D 1 257 ? 36.999  16.521  42.540  1.00 12.27 ? 258 ALA D CB  1 
ATOM   8474 N  N   . SER D 1 258 ? 35.153  18.957  43.750  1.00 10.72 ? 259 SER D N   1 
ATOM   8475 C  CA  . SER D 1 258 ? 34.737  19.674  44.967  1.00 11.43 ? 259 SER D CA  1 
ATOM   8476 C  C   . SER D 1 258 ? 34.765  18.777  46.208  1.00 12.72 ? 259 SER D C   1 
ATOM   8477 O  O   . SER D 1 258 ? 34.466  19.243  47.303  1.00 17.27 ? 259 SER D O   1 
ATOM   8478 C  CB  . SER D 1 258 ? 33.325  20.210  44.790  1.00 12.29 ? 259 SER D CB  1 
ATOM   8479 O  OG  . SER D 1 258 ? 32.353  19.168  44.860  1.00 11.50 ? 259 SER D OG  1 
ATOM   8480 N  N   . PHE D 1 259 ? 35.100  17.495  46.049  1.00 15.06 ? 260 PHE D N   1 
ATOM   8481 C  CA  . PHE D 1 259 ? 34.896  16.470  47.056  1.00 15.68 ? 260 PHE D CA  1 
ATOM   8482 C  C   . PHE D 1 259 ? 36.127  15.485  46.967  1.00 17.99 ? 260 PHE D C   1 
ATOM   8483 O  O   . PHE D 1 259 ? 36.806  15.376  45.901  1.00 17.79 ? 260 PHE D O   1 
ATOM   8484 C  CB  . PHE D 1 259 ? 33.577  15.700  46.809  1.00 16.54 ? 260 PHE D CB  1 
ATOM   8485 C  CG  . PHE D 1 259 ? 33.570  14.951  45.462  1.00 15.32 ? 260 PHE D CG  1 
ATOM   8486 C  CD1 . PHE D 1 259 ? 33.290  15.645  44.265  1.00 13.65 ? 260 PHE D CD1 1 
ATOM   8487 C  CD2 . PHE D 1 259 ? 33.992  13.634  45.375  1.00 18.47 ? 260 PHE D CD2 1 
ATOM   8488 C  CE1 . PHE D 1 259 ? 33.332  14.965  43.054  1.00 16.87 ? 260 PHE D CE1 1 
ATOM   8489 C  CE2 . PHE D 1 259 ? 34.078  12.981  44.158  1.00 18.63 ? 260 PHE D CE2 1 
ATOM   8490 C  CZ  . PHE D 1 259 ? 33.726  13.637  42.995  1.00 18.31 ? 260 PHE D CZ  1 
ATOM   8491 N  N   . LYS D 1 260 ? 36.286  14.749  48.106  1.00 27.56 ? 261 LYS D N   1 
ATOM   8492 C  CA  . LYS D 1 260 ? 36.979  13.458  48.363  1.00 34.11 ? 261 LYS D CA  1 
ATOM   8493 C  C   . LYS D 1 260 ? 38.454  13.403  48.197  1.00 45.72 ? 261 LYS D C   1 
ATOM   8494 O  O   . LYS D 1 260 ? 39.148  13.560  49.202  1.00 58.18 ? 261 LYS D O   1 
ATOM   8495 C  CB  . LYS D 1 260 ? 36.237  12.185  47.846  1.00 35.40 ? 261 LYS D CB  1 
ATOM   8496 C  CG  . LYS D 1 260 ? 35.073  11.715  48.747  1.00 52.81 ? 261 LYS D CG  1 
ATOM   8497 C  CD  . LYS D 1 260 ? 33.797  11.272  47.984  1.00 45.46 ? 261 LYS D CD  1 
ATOM   8498 C  CE  . LYS D 1 260 ? 33.930  9.957   47.190  1.00 64.01 ? 261 LYS D CE  1 
ATOM   8499 N  NZ  . LYS D 1 260 ? 34.533  10.086  45.818  1.00 44.61 ? 261 LYS D NZ  1 
HETATM 8500 ZN ZN  . ZN  E 2 .   ? -0.866  0.096   3.546   1.00 8.25  ? 301 ZN  A ZN  1 
HETATM 8501 O  O16 . WWX F 3 .   ? 4.067   3.070   6.902   1.00 25.65 ? 302 WWX A O16 1 
HETATM 8502 S  S14 . WWX F 3 .   ? 3.049   3.984   7.653   1.00 21.62 ? 302 WWX A S14 1 
HETATM 8503 O  O15 . WWX F 3 .   ? 3.557   5.438   7.567   1.00 25.59 ? 302 WWX A O15 1 
HETATM 8504 C  C18 . WWX F 3 .   ? 1.577   3.685   9.953   1.00 25.62 ? 302 WWX A C18 1 
HETATM 8505 O  O20 . WWX F 3 .   ? 1.322   5.036   9.996   1.00 33.62 ? 302 WWX A O20 1 
HETATM 8506 C  C17 . WWX F 3 .   ? 2.950   3.352   9.345   1.00 23.49 ? 302 WWX A C17 1 
HETATM 8507 C  C8  . WWX F 3 .   ? 1.455   3.871   6.830   1.00 18.37 ? 302 WWX A C8  1 
HETATM 8508 C  C7  . WWX F 3 .   ? 0.981   2.541   6.759   1.00 17.17 ? 302 WWX A C7  1 
HETATM 8509 F  F12 . WWX F 3 .   ? 1.693   1.530   7.411   1.00 21.19 ? 302 WWX A F12 1 
HETATM 8510 C  C6  . WWX F 3 .   ? -0.186  2.253   6.138   1.00 15.31 ? 302 WWX A C6  1 
HETATM 8511 F  F11 . WWX F 3 .   ? -0.574  0.937   6.235   1.00 17.01 ? 302 WWX A F11 1 
HETATM 8512 C  C9  . WWX F 3 .   ? 0.686   4.861   6.217   1.00 16.27 ? 302 WWX A C9  1 
HETATM 8513 C  C10 . WWX F 3 .   ? -0.416  4.500   5.438   1.00 17.43 ? 302 WWX A C10 1 
HETATM 8514 F  F13 . WWX F 3 .   ? -1.066  5.494   4.788   1.00 17.90 ? 302 WWX A F13 1 
HETATM 8515 C  C5  . WWX F 3 .   ? -0.953  3.210   5.399   1.00 15.36 ? 302 WWX A C5  1 
HETATM 8516 S  S1  . WWX F 3 .   ? -2.291  2.775   4.169   1.00 13.21 ? 302 WWX A S1  1 
HETATM 8517 O  O3  . WWX F 3 .   ? -3.605  3.250   4.605   1.00 17.48 ? 302 WWX A O3  1 
HETATM 8518 N  N4  . WWX F 3 .   ? -2.249  1.194   4.325   1.00 9.50  ? 302 WWX A N4  1 
HETATM 8519 O  O2  . WWX F 3 .   ? -1.831  3.126   2.893   1.00 12.67 ? 302 WWX A O2  1 
HETATM 8520 N  N19 . WWX F 3 .   ? 1.196   6.221   6.271   1.00 18.99 ? 302 WWX A N19 1 
HETATM 8521 C  C21 . WWX F 3 .   ? 0.300   7.367   6.435   1.00 17.86 ? 302 WWX A C21 1 
HETATM 8522 C  C30 . WWX F 3 .   ? 0.435   8.333   5.331   1.00 15.44 ? 302 WWX A C30 1 
HETATM 8523 C  C35 . WWX F 3 .   ? 1.678   8.605   4.729   1.00 20.08 ? 302 WWX A C35 1 
HETATM 8524 C  C34 . WWX F 3 .   ? 1.747   9.572   3.694   1.00 22.33 ? 302 WWX A C34 1 
HETATM 8525 C  C33 . WWX F 3 .   ? 0.577   10.354  3.305   1.00 18.39 ? 302 WWX A C33 1 
HETATM 8526 C  C32 . WWX F 3 .   ? -0.617  10.088  3.963   1.00 16.27 ? 302 WWX A C32 1 
HETATM 8527 C  C31 . WWX F 3 .   ? -0.740  9.065   4.974   1.00 16.93 ? 302 WWX A C31 1 
HETATM 8528 C  C22 . WWX F 3 .   ? 0.618   8.034   7.812   1.00 24.08 ? 302 WWX A C22 1 
HETATM 8529 O  O29 . WWX F 3 .   ? 2.007   8.367   7.849   1.00 24.14 ? 302 WWX A O29 1 
HETATM 8530 C  C23 . WWX F 3 .   ? -0.240  9.223   8.153   1.00 18.91 ? 302 WWX A C23 1 
HETATM 8531 C  C28 . WWX F 3 .   ? 0.193   10.543  7.957   1.00 21.46 ? 302 WWX A C28 1 
HETATM 8532 C  C27 . WWX F 3 .   ? -0.689  11.617  8.309   1.00 20.41 ? 302 WWX A C27 1 
HETATM 8533 C  C26 . WWX F 3 .   ? -1.939  11.338  8.814   1.00 22.02 ? 302 WWX A C26 1 
HETATM 8534 C  C25 . WWX F 3 .   ? -2.348  10.028  9.008   1.00 21.63 ? 302 WWX A C25 1 
HETATM 8535 C  C24 . WWX F 3 .   ? -1.496  8.996   8.640   1.00 20.63 ? 302 WWX A C24 1 
HETATM 8536 S  S   . DMS G 4 .   ? -3.195  -9.840  11.227  1.00 23.22 ? 303 DMS A S   1 
HETATM 8537 O  O   . DMS G 4 .   ? -2.846  -11.175 11.906  1.00 28.75 ? 303 DMS A O   1 
HETATM 8538 C  C1  . DMS G 4 .   ? -4.858  -9.721  10.900  1.00 20.54 ? 303 DMS A C1  1 
HETATM 8539 C  C2  . DMS G 4 .   ? -3.207  -8.616  12.387  1.00 24.75 ? 303 DMS A C2  1 
HETATM 8540 N  N1  . BCN H 5 .   ? -3.251  -12.095 -12.871 1.00 37.05 ? 304 BCN A N1  1 
HETATM 8541 C  C1  . BCN H 5 .   ? -4.680  -12.046 -12.263 1.00 43.36 ? 304 BCN A C1  1 
HETATM 8542 C  C2  . BCN H 5 .   ? -5.608  -13.215 -12.659 1.00 52.24 ? 304 BCN A C2  1 
HETATM 8543 O  O21 . BCN H 5 .   ? -6.731  -13.293 -12.139 1.00 34.15 ? 304 BCN A O21 1 
HETATM 8544 O  O22 . BCN H 5 .   ? -5.362  -14.100 -13.466 1.00 49.61 ? 304 BCN A O22 1 
HETATM 8545 C  C3  . BCN H 5 .   ? -2.453  -13.257 -12.473 1.00 41.97 ? 304 BCN A C3  1 
HETATM 8546 C  C4  . BCN H 5 .   ? -2.826  -13.990 -11.222 1.00 27.14 ? 304 BCN A C4  1 
HETATM 8547 O  O4  . BCN H 5 .   ? -1.634  -14.696 -10.903 1.00 45.11 ? 304 BCN A O4  1 
HETATM 8548 C  C5  . BCN H 5 .   ? -3.082  -12.028 -14.349 1.00 48.42 ? 304 BCN A C5  1 
HETATM 8549 C  C6  . BCN H 5 .   ? -3.389  -10.742 -15.112 1.00 41.98 ? 304 BCN A C6  1 
HETATM 8550 O  O6  . BCN H 5 .   ? -4.763  -10.550 -14.868 1.00 40.43 ? 304 BCN A O6  1 
HETATM 8551 ZN ZN  . ZN  I 2 .   ? -14.615 0.187   43.041  1.00 7.57  ? 301 ZN  B ZN  1 
HETATM 8552 O  O16 . WWX J 3 .   ? -9.721  3.077   46.398  1.00 26.55 ? 302 WWX B O16 1 
HETATM 8553 S  S14 . WWX J 3 .   ? -10.672 4.097   47.083  1.00 21.54 ? 302 WWX B S14 1 
HETATM 8554 O  O15 . WWX J 3 .   ? -10.145 5.541   46.966  1.00 23.61 ? 302 WWX B O15 1 
HETATM 8555 C  C18 . WWX J 3 .   ? -12.050 3.769   49.405  1.00 22.33 ? 302 WWX B C18 1 
HETATM 8556 O  O20 . WWX J 3 .   ? -12.263 5.146   49.563  1.00 32.89 ? 302 WWX B O20 1 
HETATM 8557 C  C17 . WWX J 3 .   ? -10.679 3.525   48.763  1.00 24.90 ? 302 WWX B C17 1 
HETATM 8558 C  C8  . WWX J 3 .   ? -12.272 3.922   46.309  1.00 17.41 ? 302 WWX B C8  1 
HETATM 8559 C  C7  . WWX J 3 .   ? -12.778 2.600   46.239  1.00 15.97 ? 302 WWX B C7  1 
HETATM 8560 F  F12 . WWX J 3 .   ? -12.079 1.589   46.915  1.00 21.46 ? 302 WWX B F12 1 
HETATM 8561 C  C6  . WWX J 3 .   ? -13.934 2.344   45.629  1.00 13.43 ? 302 WWX B C6  1 
HETATM 8562 F  F11 . WWX J 3 .   ? -14.399 1.028   45.742  1.00 15.04 ? 302 WWX B F11 1 
HETATM 8563 C  C9  . WWX J 3 .   ? -13.025 4.905   45.671  1.00 15.94 ? 302 WWX B C9  1 
HETATM 8564 C  C10 . WWX J 3 .   ? -14.152 4.574   44.922  1.00 14.94 ? 302 WWX B C10 1 
HETATM 8565 F  F13 . WWX J 3 .   ? -14.788 5.580   44.226  1.00 16.23 ? 302 WWX B F13 1 
HETATM 8566 C  C5  . WWX J 3 .   ? -14.706 3.295   44.901  1.00 12.78 ? 302 WWX B C5  1 
HETATM 8567 S  S1  . WWX J 3 .   ? -16.039 2.855   43.683  1.00 10.90 ? 302 WWX B S1  1 
HETATM 8568 O  O3  . WWX J 3 .   ? -17.324 3.314   44.179  1.00 14.89 ? 302 WWX B O3  1 
HETATM 8569 N  N4  . WWX J 3 .   ? -15.972 1.276   43.870  1.00 10.44 ? 302 WWX B N4  1 
HETATM 8570 O  O2  . WWX J 3 .   ? -15.573 3.195   42.342  1.00 12.93 ? 302 WWX B O2  1 
HETATM 8571 N  N19 . WWX J 3 .   ? -12.523 6.246   45.697  1.00 16.59 ? 302 WWX B N19 1 
HETATM 8572 C  C21 . WWX J 3 .   ? -13.411 7.410   45.950  1.00 17.48 ? 302 WWX B C21 1 
HETATM 8573 C  C30 . WWX J 3 .   ? -13.394 8.408   44.823  1.00 14.27 ? 302 WWX B C30 1 
HETATM 8574 C  C35 . WWX J 3 .   ? -12.194 8.659   44.093  1.00 16.93 ? 302 WWX B C35 1 
HETATM 8575 C  C34 . WWX J 3 .   ? -12.134 9.665   43.093  1.00 20.78 ? 302 WWX B C34 1 
HETATM 8576 C  C33 . WWX J 3 .   ? -13.271 10.459  42.746  1.00 16.23 ? 302 WWX B C33 1 
HETATM 8577 C  C32 . WWX J 3 .   ? -14.374 10.236  43.506  1.00 15.40 ? 302 WWX B C32 1 
HETATM 8578 C  C31 . WWX J 3 .   ? -14.515 9.216   44.504  1.00 16.34 ? 302 WWX B C31 1 
HETATM 8579 C  C22 . WWX J 3 .   ? -13.041 8.124   47.247  1.00 19.51 ? 302 WWX B C22 1 
HETATM 8580 O  O29 . WWX J 3 .   ? -11.653 8.471   47.169  1.00 21.87 ? 302 WWX B O29 1 
HETATM 8581 C  C23 . WWX J 3 .   ? -13.932 9.301   47.634  1.00 16.99 ? 302 WWX B C23 1 
HETATM 8582 C  C28 . WWX J 3 .   ? -13.514 10.621  47.393  1.00 19.06 ? 302 WWX B C28 1 
HETATM 8583 C  C27 . WWX J 3 .   ? -14.408 11.687  47.758  1.00 22.92 ? 302 WWX B C27 1 
HETATM 8584 C  C26 . WWX J 3 .   ? -15.627 11.404  48.359  1.00 21.92 ? 302 WWX B C26 1 
HETATM 8585 C  C25 . WWX J 3 .   ? -16.041 10.097  48.617  1.00 21.05 ? 302 WWX B C25 1 
HETATM 8586 C  C24 . WWX J 3 .   ? -15.190 9.079   48.189  1.00 15.19 ? 302 WWX B C24 1 
HETATM 8587 S  S   . DMS K 4 .   ? -16.784 -9.758  50.839  1.00 22.66 ? 303 DMS B S   1 
HETATM 8588 O  O   . DMS K 4 .   ? -16.529 -11.137 51.480  1.00 28.43 ? 303 DMS B O   1 
HETATM 8589 C  C1  . DMS K 4 .   ? -18.414 -9.661  50.566  1.00 17.64 ? 303 DMS B C1  1 
HETATM 8590 C  C2  . DMS K 4 .   ? -16.668 -8.530  52.013  1.00 23.59 ? 303 DMS B C2  1 
HETATM 8591 N  N1  . BCN L 5 .   ? -17.738 -12.758 27.299  1.00 33.47 ? 304 BCN B N1  1 
HETATM 8592 C  C1  . BCN L 5 .   ? -18.989 -12.190 27.913  1.00 30.00 ? 304 BCN B C1  1 
HETATM 8593 C  C2  . BCN L 5 .   ? -19.977 -13.200 27.300  1.00 37.58 ? 304 BCN B C2  1 
HETATM 8594 O  O21 . BCN L 5 .   ? -19.661 -13.976 26.353  1.00 51.06 ? 304 BCN B O21 1 
HETATM 8595 O  O22 . BCN L 5 .   ? -21.105 -13.322 27.715  1.00 38.02 ? 304 BCN B O22 1 
HETATM 8596 C  C3  . BCN L 5 .   ? -16.974 -11.889 26.382  1.00 24.46 ? 304 BCN B C3  1 
HETATM 8597 C  C4  . BCN L 5 .   ? -17.444 -11.363 25.000  1.00 39.70 ? 304 BCN B C4  1 
HETATM 8598 O  O4  . BCN L 5 .   ? -18.588 -10.511 25.048  1.00 28.76 ? 304 BCN B O4  1 
HETATM 8599 C  C5  . BCN L 5 .   ? -17.000 -13.697 28.221  1.00 22.76 ? 304 BCN B C5  1 
HETATM 8600 C  C6  . BCN L 5 .   ? -15.647 -14.206 27.741  1.00 36.90 ? 304 BCN B C6  1 
HETATM 8601 O  O6  . BCN L 5 .   ? -15.113 -14.797 28.892  1.00 44.48 ? 304 BCN B O6  1 
HETATM 8602 ZN ZN  . ZN  M 2 .   ? 9.931   20.784  65.852  1.00 7.62  ? 301 ZN  C ZN  1 
HETATM 8603 O  O16 . WWX N 3 .   ? 5.028   23.719  62.498  1.00 28.01 ? 302 WWX C O16 1 
HETATM 8604 S  S14 . WWX N 3 .   ? 6.003   24.704  61.819  1.00 21.59 ? 302 WWX C S14 1 
HETATM 8605 O  O15 . WWX N 3 .   ? 5.420   26.123  61.985  1.00 24.64 ? 302 WWX C O15 1 
HETATM 8606 C  C18 . WWX N 3 .   ? 7.378   24.374  59.461  1.00 25.19 ? 302 WWX C C18 1 
HETATM 8607 O  O20 . WWX N 3 .   ? 7.585   25.763  59.432  1.00 33.01 ? 302 WWX C O20 1 
HETATM 8608 C  C17 . WWX N 3 .   ? 6.004   24.123  60.114  1.00 27.73 ? 302 WWX C C17 1 
HETATM 8609 C  C8  . WWX N 3 .   ? 7.593   24.506  62.592  1.00 17.79 ? 302 WWX C C8  1 
HETATM 8610 C  C7  . WWX N 3 .   ? 8.143   23.172  62.637  1.00 14.62 ? 302 WWX C C7  1 
HETATM 8611 F  F12 . WWX N 3 .   ? 7.415   22.147  61.999  1.00 20.97 ? 302 WWX C F12 1 
HETATM 8612 C  C6  . WWX N 3 .   ? 9.270   22.916  63.270  1.00 13.04 ? 302 WWX C C6  1 
HETATM 8613 F  F11 . WWX N 3 .   ? 9.720   21.608  63.157  1.00 14.97 ? 302 WWX C F11 1 
HETATM 8614 C  C9  . WWX N 3 .   ? 8.317   25.520  63.229  1.00 17.49 ? 302 WWX C C9  1 
HETATM 8615 C  C10 . WWX N 3 .   ? 9.476   25.194  63.936  1.00 17.45 ? 302 WWX C C10 1 
HETATM 8616 F  F13 . WWX N 3 .   ? 10.137  26.203  64.664  1.00 15.44 ? 302 WWX C F13 1 
HETATM 8617 C  C5  . WWX N 3 .   ? 10.001  23.898  63.991  1.00 13.93 ? 302 WWX C C5  1 
HETATM 8618 S  S1  . WWX N 3 .   ? 11.357  23.452  65.216  1.00 11.09 ? 302 WWX C S1  1 
HETATM 8619 O  O3  . WWX N 3 .   ? 12.616  23.939  64.632  1.00 14.50 ? 302 WWX C O3  1 
HETATM 8620 N  N4  . WWX N 3 .   ? 11.361  21.862  65.051  1.00 11.44 ? 302 WWX C N4  1 
HETATM 8621 O  O2  . WWX N 3 .   ? 10.836  23.813  66.547  1.00 12.77 ? 302 WWX C O2  1 
HETATM 8622 N  N19 . WWX N 3 .   ? 7.788   26.873  63.165  1.00 16.82 ? 302 WWX C N19 1 
HETATM 8623 C  C21 . WWX N 3 .   ? 8.695   28.019  62.937  1.00 18.71 ? 302 WWX C C21 1 
HETATM 8624 C  C30 . WWX N 3 .   ? 8.665   29.016  64.061  1.00 16.24 ? 302 WWX C C30 1 
HETATM 8625 C  C35 . WWX N 3 .   ? 7.472   29.222  64.825  1.00 18.20 ? 302 WWX C C35 1 
HETATM 8626 C  C34 . WWX N 3 .   ? 7.487   30.221  65.819  1.00 20.54 ? 302 WWX C C34 1 
HETATM 8627 C  C33 . WWX N 3 .   ? 8.577   31.012  66.187  1.00 17.93 ? 302 WWX C C33 1 
HETATM 8628 C  C32 . WWX N 3 .   ? 9.718   30.815  65.429  1.00 14.88 ? 302 WWX C C32 1 
HETATM 8629 C  C31 . WWX N 3 .   ? 9.822   29.771  64.419  1.00 17.14 ? 302 WWX C C31 1 
HETATM 8630 C  C22 . WWX N 3 .   ? 8.366   28.727  61.644  1.00 19.34 ? 302 WWX C C22 1 
HETATM 8631 O  O29 . WWX N 3 .   ? 6.991   29.054  61.676  1.00 21.88 ? 302 WWX C O29 1 
HETATM 8632 C  C23 . WWX N 3 .   ? 9.254   29.902  61.267  1.00 17.08 ? 302 WWX C C23 1 
HETATM 8633 C  C28 . WWX N 3 .   ? 8.827   31.229  61.466  1.00 20.58 ? 302 WWX C C28 1 
HETATM 8634 C  C27 . WWX N 3 .   ? 9.723   32.279  61.089  1.00 24.52 ? 302 WWX C C27 1 
HETATM 8635 C  C26 . WWX N 3 .   ? 10.972  31.977  60.546  1.00 20.29 ? 302 WWX C C26 1 
HETATM 8636 C  C25 . WWX N 3 .   ? 11.394  30.655  60.389  1.00 20.69 ? 302 WWX C C25 1 
HETATM 8637 C  C24 . WWX N 3 .   ? 10.541  29.637  60.763  1.00 17.94 ? 302 WWX C C24 1 
HETATM 8638 S  S   . DMS O 4 .   ? 12.135  10.791  58.021  1.00 23.22 ? 303 DMS C S   1 
HETATM 8639 O  O   . DMS O 4 .   ? 12.095  9.465   57.230  1.00 31.22 ? 303 DMS C O   1 
HETATM 8640 C  C1  . DMS O 4 .   ? 13.759  10.994  58.337  1.00 18.85 ? 303 DMS C C1  1 
HETATM 8641 C  C2  . DMS O 4 .   ? 11.868  11.995  56.888  1.00 28.05 ? 303 DMS C C2  1 
HETATM 8642 N  N1  . BCN P 5 .   ? 12.921  7.772   81.676  1.00 34.70 ? 304 BCN C N1  1 
HETATM 8643 C  C1  . BCN P 5 .   ? 14.192  8.369   81.112  1.00 31.90 ? 304 BCN C C1  1 
HETATM 8644 C  C2  . BCN P 5 .   ? 15.221  7.365   81.650  1.00 41.62 ? 304 BCN C C2  1 
HETATM 8645 O  O21 . BCN P 5 .   ? 16.359  7.377   81.180  1.00 42.68 ? 304 BCN C O21 1 
HETATM 8646 O  O22 . BCN P 5 .   ? 14.996  6.536   82.533  1.00 45.20 ? 304 BCN C O22 1 
HETATM 8647 C  C3  . BCN P 5 .   ? 12.182  8.756   82.515  1.00 26.03 ? 304 BCN C C3  1 
HETATM 8648 C  C4  . BCN P 5 .   ? 12.705  9.315   83.884  1.00 39.79 ? 304 BCN C C4  1 
HETATM 8649 O  O4  . BCN P 5 .   ? 13.938  10.050  83.852  1.00 30.33 ? 304 BCN C O4  1 
HETATM 8650 C  C5  . BCN P 5 .   ? 12.303  6.849   80.622  1.00 23.65 ? 304 BCN C C5  1 
HETATM 8651 C  C6  . BCN P 5 .   ? 10.979  6.023   80.537  1.00 34.28 ? 304 BCN C C6  1 
HETATM 8652 O  O6  . BCN P 5 .   ? 10.036  6.309   81.555  1.00 52.63 ? 304 BCN C O6  1 
HETATM 8653 ZN ZN  . ZN  Q 2 .   ? 23.958  20.696  26.031  1.00 8.45  ? 301 ZN  D ZN  1 
HETATM 8654 O  O16 . WWX R 3 .   ? 19.027  23.680  22.688  1.00 27.75 ? 302 WWX D O16 1 
HETATM 8655 S  S14 . WWX R 3 .   ? 20.043  24.605  21.930  1.00 22.16 ? 302 WWX D S14 1 
HETATM 8656 O  O15 . WWX R 3 .   ? 19.509  26.046  21.983  1.00 27.36 ? 302 WWX D O15 1 
HETATM 8657 C  C18 . WWX R 3 .   ? 21.455  24.251  19.620  1.00 23.80 ? 302 WWX D C18 1 
HETATM 8658 O  O20 . WWX R 3 .   ? 21.641  25.610  19.550  1.00 40.69 ? 302 WWX D O20 1 
HETATM 8659 C  C17 . WWX R 3 .   ? 20.078  23.949  20.242  1.00 25.87 ? 302 WWX D C17 1 
HETATM 8660 C  C8  . WWX R 3 .   ? 21.619  24.452  22.735  1.00 17.47 ? 302 WWX D C8  1 
HETATM 8661 C  C7  . WWX R 3 .   ? 22.109  23.110  22.798  1.00 18.61 ? 302 WWX D C7  1 
HETATM 8662 F  F12 . WWX R 3 .   ? 21.385  22.073  22.178  1.00 22.16 ? 302 WWX D F12 1 
HETATM 8663 C  C6  . WWX R 3 .   ? 23.279  22.829  23.436  1.00 14.96 ? 302 WWX D C6  1 
HETATM 8664 F  F11 . WWX R 3 .   ? 23.686  21.525  23.356  1.00 17.14 ? 302 WWX D F11 1 
HETATM 8665 C  C9  . WWX R 3 .   ? 22.335  25.481  23.357  1.00 19.78 ? 302 WWX D C9  1 
HETATM 8666 C  C10 . WWX R 3 .   ? 23.475  25.116  24.059  1.00 17.55 ? 302 WWX D C10 1 
HETATM 8667 F  F13 . WWX R 3 .   ? 24.099  26.132  24.772  1.00 17.90 ? 302 WWX D F13 1 
HETATM 8668 C  C5  . WWX R 3 .   ? 24.012  23.822  24.155  1.00 15.20 ? 302 WWX D C5  1 
HETATM 8669 S  S1  . WWX R 3 .   ? 25.380  23.377  25.403  1.00 13.33 ? 302 WWX D S1  1 
HETATM 8670 O  O3  . WWX R 3 .   ? 26.707  23.869  24.896  1.00 17.97 ? 302 WWX D O3  1 
HETATM 8671 N  N4  . WWX R 3 .   ? 25.352  21.788  25.257  1.00 10.36 ? 302 WWX D N4  1 
HETATM 8672 O  O2  . WWX R 3 .   ? 24.889  23.750  26.703  1.00 14.49 ? 302 WWX D O2  1 
HETATM 8673 N  N19 . WWX R 3 .   ? 21.867  26.853  23.242  1.00 18.41 ? 302 WWX D N19 1 
HETATM 8674 C  C21 . WWX R 3 .   ? 22.817  27.955  23.049  1.00 21.95 ? 302 WWX D C21 1 
HETATM 8675 C  C30 . WWX R 3 .   ? 22.772  28.917  24.175  1.00 15.93 ? 302 WWX D C30 1 
HETATM 8676 C  C35 . WWX R 3 .   ? 21.525  29.175  24.817  1.00 18.92 ? 302 WWX D C35 1 
HETATM 8677 C  C34 . WWX R 3 .   ? 21.438  30.169  25.815  1.00 20.42 ? 302 WWX D C34 1 
HETATM 8678 C  C33 . WWX R 3 .   ? 22.598  30.901  26.292  1.00 19.41 ? 302 WWX D C33 1 
HETATM 8679 C  C32 . WWX R 3 .   ? 23.815  30.679  25.625  1.00 17.91 ? 302 WWX D C32 1 
HETATM 8680 C  C31 . WWX R 3 .   ? 23.925  29.680  24.574  1.00 18.96 ? 302 WWX D C31 1 
HETATM 8681 C  C22 . WWX R 3 .   ? 22.504  28.658  21.719  1.00 22.75 ? 302 WWX D C22 1 
HETATM 8682 O  O29 . WWX R 3 .   ? 21.121  28.936  21.717  1.00 23.62 ? 302 WWX D O29 1 
HETATM 8683 C  C23 . WWX R 3 .   ? 23.363  29.859  21.397  1.00 19.41 ? 302 WWX D C23 1 
HETATM 8684 C  C28 . WWX R 3 .   ? 22.953  31.183  21.601  1.00 23.54 ? 302 WWX D C28 1 
HETATM 8685 C  C27 . WWX R 3 .   ? 23.848  32.231  21.244  1.00 21.07 ? 302 WWX D C27 1 
HETATM 8686 C  C26 . WWX R 3 .   ? 25.113  31.947  20.758  1.00 22.95 ? 302 WWX D C26 1 
HETATM 8687 C  C25 . WWX R 3 .   ? 25.509  30.624  20.604  1.00 22.05 ? 302 WWX D C25 1 
HETATM 8688 C  C24 . WWX R 3 .   ? 24.632  29.596  20.944  1.00 19.99 ? 302 WWX D C24 1 
HETATM 8689 S  S   . DMS S 4 .   ? 26.306  10.749  18.335  1.00 23.28 ? 303 DMS D S   1 
HETATM 8690 O  O   . DMS S 4 .   ? 26.144  9.398   17.586  1.00 29.06 ? 303 DMS D O   1 
HETATM 8691 C  C1  . DMS S 4 .   ? 27.975  10.819  18.666  1.00 19.87 ? 303 DMS D C1  1 
HETATM 8692 C  C2  . DMS S 4 .   ? 26.339  11.981  17.228  1.00 25.93 ? 303 DMS D C2  1 
HETATM 8693 N  N1  . BCN T 5 .   ? 26.621  7.673   42.042  1.00 44.41 ? 304 BCN D N1  1 
HETATM 8694 C  C1  . BCN T 5 .   ? 27.857  8.317   41.478  1.00 38.77 ? 304 BCN D C1  1 
HETATM 8695 C  C2  . BCN T 5 .   ? 28.913  7.578   42.257  1.00 68.59 ? 304 BCN D C2  1 
HETATM 8696 O  O21 . BCN T 5 .   ? 28.725  7.222   43.442  1.00 85.59 ? 304 BCN D O21 1 
HETATM 8697 O  O22 . BCN T 5 .   ? 29.957  7.325   41.731  1.00 42.56 ? 304 BCN D O22 1 
HETATM 8698 C  C3  . BCN T 5 .   ? 25.815  8.654   42.832  1.00 30.40 ? 304 BCN D C3  1 
HETATM 8699 C  C4  . BCN T 5 .   ? 26.228  9.114   44.258  1.00 46.62 ? 304 BCN D C4  1 
HETATM 8700 O  O4  . BCN T 5 .   ? 27.312  10.055  44.377  1.00 36.17 ? 304 BCN D O4  1 
HETATM 8701 C  C5  . BCN T 5 .   ? 25.978  6.818   40.961  1.00 25.79 ? 304 BCN D C5  1 
HETATM 8702 C  C6  . BCN T 5 .   ? 25.102  5.654   41.389  1.00 44.18 ? 304 BCN D C6  1 
HETATM 8703 O  O6  . BCN T 5 .   ? 23.836  5.860   40.785  1.00 54.70 ? 304 BCN D O6  1 
HETATM 8704 O  O   . HOH U 6 .   ? -1.988  -6.531  -7.925  1.00 9.23  ? 401 HOH A O   1 
HETATM 8705 O  O   . HOH U 6 .   ? 14.297  7.582   -6.829  1.00 16.10 ? 402 HOH A O   1 
HETATM 8706 O  O   . HOH U 6 .   ? -14.035 -8.028  -11.649 1.00 17.72 ? 403 HOH A O   1 
HETATM 8707 O  O   . HOH U 6 .   ? -9.230  -15.023 -6.411  1.00 15.80 ? 404 HOH A O   1 
HETATM 8708 O  O   . HOH U 6 .   ? -3.063  -2.280  8.536   1.00 10.26 ? 405 HOH A O   1 
HETATM 8709 O  O   . HOH U 6 .   ? -4.034  -11.702 4.577   1.00 10.17 ? 406 HOH A O   1 
HETATM 8710 O  O   . HOH U 6 .   ? -11.212 -11.471 3.153   1.00 12.38 ? 407 HOH A O   1 
HETATM 8711 O  O   . HOH U 6 .   ? -3.386  -5.293  -13.314 1.00 13.21 ? 408 HOH A O   1 
HETATM 8712 O  O   . HOH U 6 .   ? 10.011  -18.569 -4.719  1.00 16.74 ? 409 HOH A O   1 
HETATM 8713 O  O   . HOH U 6 .   ? 3.455   -13.644 3.645   1.00 11.06 ? 410 HOH A O   1 
HETATM 8714 O  O   . HOH U 6 .   ? -7.085  -9.340  4.550   1.00 11.13 ? 411 HOH A O   1 
HETATM 8715 O  O   . HOH U 6 .   ? -18.114 6.780   8.128   1.00 20.89 ? 412 HOH A O   1 
HETATM 8716 O  O   . HOH U 6 .   ? -9.141  10.530  -3.589  1.00 11.01 ? 413 HOH A O   1 
HETATM 8717 O  O   . HOH U 6 .   ? -10.224 -3.099  12.448  1.00 14.01 ? 414 HOH A O   1 
HETATM 8718 O  O   . HOH U 6 .   ? 7.869   11.362  -12.958 1.00 32.05 ? 415 HOH A O   1 
HETATM 8719 O  O   . HOH U 6 .   ? -6.065  -10.473 -8.469  1.00 15.80 ? 416 HOH A O   1 
HETATM 8720 O  O   . HOH U 6 .   ? -15.192 -6.918  2.657   1.00 12.35 ? 417 HOH A O   1 
HETATM 8721 O  O   . HOH U 6 .   ? -12.641 -9.966  7.619   1.00 22.89 ? 418 HOH A O   1 
HETATM 8722 O  O   . HOH U 6 .   ? -9.432  -10.486 5.226   1.00 11.96 ? 419 HOH A O   1 
HETATM 8723 O  O   . HOH U 6 .   ? -11.567 -1.922  15.898  1.00 15.38 ? 420 HOH A O   1 
HETATM 8724 O  O   . HOH U 6 .   ? 4.429   -20.361 3.686   1.00 22.09 ? 421 HOH A O   1 
HETATM 8725 O  O   . HOH U 6 .   ? 15.574  0.330   17.258  1.00 19.95 ? 422 HOH A O   1 
HETATM 8726 O  O   . HOH U 6 .   ? -6.251  -17.547 -0.032  1.00 16.25 ? 423 HOH A O   1 
HETATM 8727 O  O   . HOH U 6 .   ? 0.590   10.503  -14.481 1.00 23.12 ? 424 HOH A O   1 
HETATM 8728 O  O   . HOH U 6 .   ? -16.837 0.249   6.144   1.00 14.50 ? 425 HOH A O   1 
HETATM 8729 O  O   . HOH U 6 .   ? -0.100  -15.371 -2.944  1.00 16.01 ? 426 HOH A O   1 
HETATM 8730 O  O   . HOH U 6 .   ? -10.292 -14.099 3.079   1.00 14.99 ? 427 HOH A O   1 
HETATM 8731 O  O   . HOH U 6 .   ? -0.923  -7.604  21.822  1.00 27.30 ? 428 HOH A O   1 
HETATM 8732 O  O   . HOH U 6 .   ? -15.500 -9.364  3.987   1.00 20.24 ? 429 HOH A O   1 
HETATM 8733 O  O   . HOH U 6 .   ? -9.459  -12.515 7.178   1.00 22.23 ? 430 HOH A O   1 
HETATM 8734 O  O   . HOH U 6 .   ? 1.773   21.789  -3.121  1.00 18.28 ? 431 HOH A O   1 
HETATM 8735 O  O   . HOH U 6 .   ? 11.333  -5.807  -11.386 1.00 18.63 ? 432 HOH A O   1 
HETATM 8736 O  O   . HOH U 6 .   ? 6.086   -9.747  -11.358 1.00 20.32 ? 433 HOH A O   1 
HETATM 8737 O  O   . HOH U 6 .   ? 19.473  -2.918  11.641  1.00 21.15 ? 434 HOH A O   1 
HETATM 8738 O  O   . HOH U 6 .   ? -1.178  -16.447 -0.718  1.00 14.42 ? 435 HOH A O   1 
HETATM 8739 O  O   . HOH U 6 .   ? -10.327 12.152  -7.455  1.00 15.47 ? 436 HOH A O   1 
HETATM 8740 O  O   . HOH U 6 .   ? 6.786   12.589  -5.710  1.00 16.89 ? 437 HOH A O   1 
HETATM 8741 O  O   . HOH U 6 .   ? 20.240  2.427   9.468   1.00 28.73 ? 438 HOH A O   1 
HETATM 8742 O  O   . HOH U 6 .   ? 6.179   -16.445 -10.508 1.00 23.09 ? 439 HOH A O   1 
HETATM 8743 O  O   . HOH U 6 .   ? -3.325  -14.455 -8.873  1.00 27.41 ? 440 HOH A O   1 
HETATM 8744 O  O   . HOH U 6 .   ? -15.189 -1.683  9.972   1.00 23.78 ? 441 HOH A O   1 
HETATM 8745 O  O   . HOH U 6 .   ? 16.591  -3.956  -7.248  1.00 20.38 ? 442 HOH A O   1 
HETATM 8746 O  O   . HOH U 6 .   ? -11.009 -14.668 -8.477  1.00 22.72 ? 443 HOH A O   1 
HETATM 8747 O  O   . HOH U 6 .   ? 16.698  9.751   -5.134  1.00 15.50 ? 444 HOH A O   1 
HETATM 8748 O  O   . HOH U 6 .   ? -16.858 -13.364 -7.145  1.00 28.69 ? 445 HOH A O   1 
HETATM 8749 O  O   . HOH U 6 .   ? -17.395 -6.149  -5.653  1.00 23.37 ? 446 HOH A O   1 
HETATM 8750 O  O   . HOH U 6 .   ? 15.341  -14.880 -4.674  1.00 26.65 ? 447 HOH A O   1 
HETATM 8751 O  O   . HOH U 6 .   ? -12.036 -15.646 4.343   1.00 31.61 ? 448 HOH A O   1 
HETATM 8752 O  O   . HOH U 6 .   ? 15.757  1.097   -8.376  1.00 21.39 ? 449 HOH A O   1 
HETATM 8753 O  O   . HOH U 6 .   ? -15.950 -13.131 -2.358  1.00 21.56 ? 450 HOH A O   1 
HETATM 8754 O  O   . HOH U 6 .   ? -20.309 -13.530 -5.464  1.00 31.35 ? 451 HOH A O   1 
HETATM 8755 O  O   . HOH U 6 .   ? -19.356 -3.963  -5.881  1.00 17.54 ? 452 HOH A O   1 
HETATM 8756 O  O   . HOH U 6 .   ? -18.648 8.099   -14.849 1.00 30.14 ? 453 HOH A O   1 
HETATM 8757 O  O   . HOH U 6 .   ? -1.206  -16.729 -5.261  1.00 18.22 ? 454 HOH A O   1 
HETATM 8758 O  O   . HOH U 6 .   ? -16.552 -6.779  0.296   1.00 18.81 ? 455 HOH A O   1 
HETATM 8759 O  O   . HOH U 6 .   ? 6.858   -2.010  4.331   1.00 14.85 ? 456 HOH A O   1 
HETATM 8760 O  O   . HOH U 6 .   ? 12.591  -15.024 7.757   1.00 22.76 ? 457 HOH A O   1 
HETATM 8761 O  O   . HOH U 6 .   ? 8.435   -17.591 2.152   1.00 26.61 ? 458 HOH A O   1 
HETATM 8762 O  O   . HOH U 6 .   ? 9.545   11.948  -6.027  1.00 16.05 ? 459 HOH A O   1 
HETATM 8763 O  O   . HOH U 6 .   ? -14.704 -7.182  -14.418 1.00 27.16 ? 460 HOH A O   1 
HETATM 8764 O  O   . HOH U 6 .   ? -16.418 2.249   19.174  1.00 20.51 ? 461 HOH A O   1 
HETATM 8765 O  O   . HOH U 6 .   ? 3.094   -2.569  15.025  1.00 21.89 ? 462 HOH A O   1 
HETATM 8766 O  O   . HOH U 6 .   ? -5.554  17.769  -8.146  1.00 19.73 ? 463 HOH A O   1 
HETATM 8767 O  O   . HOH U 6 .   ? -20.748 -2.237  -17.811 1.00 35.84 ? 464 HOH A O   1 
HETATM 8768 O  O   . HOH U 6 .   ? -0.152  21.820  -5.005  1.00 21.96 ? 465 HOH A O   1 
HETATM 8769 O  O   . HOH U 6 .   ? 4.194   -19.933 -4.032  1.00 20.38 ? 466 HOH A O   1 
HETATM 8770 O  O   . HOH U 6 .   ? 19.171  -4.673  -7.977  1.00 32.26 ? 467 HOH A O   1 
HETATM 8771 O  O   . HOH U 6 .   ? -8.609  5.305   24.557  1.00 25.38 ? 468 HOH A O   1 
HETATM 8772 O  O   . HOH U 6 .   ? 3.264   16.931  1.218   1.00 20.58 ? 469 HOH A O   1 
HETATM 8773 O  O   . HOH U 6 .   ? -13.542 4.638   -6.873  1.00 19.69 ? 470 HOH A O   1 
HETATM 8774 O  O   . HOH U 6 .   ? -11.915 8.041   14.686  1.00 17.34 ? 471 HOH A O   1 
HETATM 8775 O  O   . HOH U 6 .   ? -0.720  -5.111  25.863  1.00 27.60 ? 472 HOH A O   1 
HETATM 8776 O  O   . HOH U 6 .   ? 8.002   -4.113  -13.928 1.00 40.02 ? 473 HOH A O   1 
HETATM 8777 O  O   . HOH U 6 .   ? -17.038 3.141   16.680  1.00 25.40 ? 474 HOH A O   1 
HETATM 8778 O  O   . HOH U 6 .   ? -6.555  8.758   19.636  1.00 36.25 ? 475 HOH A O   1 
HETATM 8779 O  O   . HOH U 6 .   ? 2.160   -16.690 -2.624  1.00 16.81 ? 476 HOH A O   1 
HETATM 8780 O  O   . HOH U 6 .   ? -6.936  12.605  -13.258 1.00 18.04 ? 477 HOH A O   1 
HETATM 8781 O  O   . HOH U 6 .   ? 1.524   -9.721  14.223  1.00 26.10 ? 478 HOH A O   1 
HETATM 8782 O  O   . HOH U 6 .   ? 18.524  5.123   12.351  1.00 24.18 ? 479 HOH A O   1 
HETATM 8783 O  O   . HOH U 6 .   ? -5.272  8.134   -18.529 1.00 24.04 ? 480 HOH A O   1 
HETATM 8784 O  O   . HOH U 6 .   ? -10.514 12.679  6.636   1.00 21.32 ? 481 HOH A O   1 
HETATM 8785 O  O   . HOH U 6 .   ? 13.045  -1.016  -8.911  1.00 18.76 ? 482 HOH A O   1 
HETATM 8786 O  O   . HOH U 6 .   ? -12.005 10.616  8.019   1.00 24.41 ? 483 HOH A O   1 
HETATM 8787 O  O   . HOH U 6 .   ? 17.852  -7.697  -8.739  1.00 21.43 ? 484 HOH A O   1 
HETATM 8788 O  O   . HOH U 6 .   ? -4.697  22.845  2.062   1.00 16.44 ? 485 HOH A O   1 
HETATM 8789 O  O   . HOH U 6 .   ? -3.812  -17.653 -1.804  1.00 23.41 ? 486 HOH A O   1 
HETATM 8790 O  O   . HOH U 6 .   ? -18.539 -7.884  -0.814  1.00 34.16 ? 487 HOH A O   1 
HETATM 8791 O  O   . HOH U 6 .   ? -9.601  16.041  -7.259  1.00 21.93 ? 488 HOH A O   1 
HETATM 8792 O  O   . HOH U 6 .   ? 2.085   -13.765 13.688  1.00 23.79 ? 489 HOH A O   1 
HETATM 8793 O  O   . HOH U 6 .   ? 4.032   -13.183 -12.122 1.00 36.33 ? 490 HOH A O   1 
HETATM 8794 O  O   . HOH U 6 .   ? -17.207 -10.242 -0.440  1.00 20.15 ? 491 HOH A O   1 
HETATM 8795 O  O   . HOH U 6 .   ? -13.130 17.654  -4.335  1.00 29.41 ? 492 HOH A O   1 
HETATM 8796 O  O   . HOH U 6 .   ? -11.387 9.755   -6.871  1.00 21.69 ? 493 HOH A O   1 
HETATM 8797 O  O   . HOH U 6 .   ? -9.725  8.956   13.153  1.00 21.36 ? 494 HOH A O   1 
HETATM 8798 O  O   . HOH U 6 .   ? -16.831 -6.920  -3.134  1.00 17.75 ? 495 HOH A O   1 
HETATM 8799 O  O   . HOH U 6 .   ? -10.780 -18.040 -2.040  1.00 25.00 ? 496 HOH A O   1 
HETATM 8800 O  O   . HOH U 6 .   ? -5.444  1.134   -16.601 1.00 17.09 ? 497 HOH A O   1 
HETATM 8801 O  O   . HOH U 6 .   ? 20.015  -1.699  -1.391  1.00 29.51 ? 498 HOH A O   1 
HETATM 8802 O  O   . HOH U 6 .   ? 6.616   15.719  2.148   1.00 33.26 ? 499 HOH A O   1 
HETATM 8803 O  O   . HOH U 6 .   ? -11.852 14.382  -6.538  1.00 19.12 ? 500 HOH A O   1 
HETATM 8804 O  O   . HOH U 6 .   ? 3.714   19.556  0.082   1.00 21.48 ? 501 HOH A O   1 
HETATM 8805 O  O   . HOH U 6 .   ? -8.812  -12.308 9.834   1.00 31.45 ? 502 HOH A O   1 
HETATM 8806 O  O   . HOH U 6 .   ? 0.896   21.780  -7.667  1.00 26.87 ? 503 HOH A O   1 
HETATM 8807 O  O   . HOH U 6 .   ? 15.783  -8.335  6.690   1.00 23.12 ? 504 HOH A O   1 
HETATM 8808 O  O   . HOH U 6 .   ? 8.983   14.005  1.720   1.00 22.50 ? 505 HOH A O   1 
HETATM 8809 O  O   . HOH U 6 .   ? 2.194   -4.775  16.601  1.00 23.39 ? 506 HOH A O   1 
HETATM 8810 O  O   . HOH U 6 .   ? -3.141  -2.137  -18.773 1.00 20.06 ? 507 HOH A O   1 
HETATM 8811 O  O   . HOH U 6 .   ? 18.647  10.851  1.208   1.00 21.69 ? 508 HOH A O   1 
HETATM 8812 O  O   . HOH U 6 .   ? 20.925  5.963   -0.814  1.00 22.98 ? 509 HOH A O   1 
HETATM 8813 O  O   . HOH U 6 .   ? -1.877  -16.144 -7.924  1.00 27.25 ? 510 HOH A O   1 
HETATM 8814 O  O   . HOH U 6 .   ? -19.056 -6.703  3.377   1.00 23.96 ? 511 HOH A O   1 
HETATM 8815 O  O   . HOH U 6 .   ? -8.962  23.490  -6.114  1.00 21.34 ? 512 HOH A O   1 
HETATM 8816 O  O   . HOH U 6 .   ? -21.463 -3.457  -4.125  1.00 19.43 ? 513 HOH A O   1 
HETATM 8817 O  O   . HOH U 6 .   ? -14.118 15.088  -7.944  1.00 22.48 ? 514 HOH A O   1 
HETATM 8818 O  O   . HOH U 6 .   ? 8.826   -6.771  22.551  1.00 24.00 ? 515 HOH A O   1 
HETATM 8819 O  O   . HOH U 6 .   ? -17.540 -0.744  9.410   1.00 23.67 ? 516 HOH A O   1 
HETATM 8820 O  O   . HOH U 6 .   ? 18.724  -7.120  4.169   1.00 24.30 ? 517 HOH A O   1 
HETATM 8821 O  O   . HOH U 6 .   ? 3.759   -19.170 -7.537  1.00 28.81 ? 518 HOH A O   1 
HETATM 8822 O  O   . HOH U 6 .   ? 15.339  7.343   12.420  1.00 22.76 ? 519 HOH A O   1 
HETATM 8823 O  O   . HOH U 6 .   ? -12.983 7.760   -3.502  1.00 20.33 ? 520 HOH A O   1 
HETATM 8824 O  O   . HOH U 6 .   ? 8.713   -11.409 -10.892 1.00 22.28 ? 521 HOH A O   1 
HETATM 8825 O  O   . HOH U 6 .   ? 1.273   12.974  -15.495 1.00 33.79 ? 522 HOH A O   1 
HETATM 8826 O  O   . HOH U 6 .   ? -13.865 -2.828  15.154  1.00 27.03 ? 523 HOH A O   1 
HETATM 8827 O  O   . HOH U 6 .   ? 12.447  -17.812 -7.177  1.00 25.53 ? 524 HOH A O   1 
HETATM 8828 O  O   . HOH U 6 .   ? -16.201 -3.874  18.959  1.00 26.46 ? 525 HOH A O   1 
HETATM 8829 O  O   . HOH U 6 .   ? -1.350  4.353   -18.995 1.00 37.63 ? 526 HOH A O   1 
HETATM 8830 O  O   . HOH U 6 .   ? 12.800  -19.001 -4.898  1.00 27.30 ? 527 HOH A O   1 
HETATM 8831 O  O   . HOH U 6 .   ? -17.492 -10.115 2.178   1.00 33.08 ? 528 HOH A O   1 
HETATM 8832 O  O   . HOH U 6 .   ? 15.402  -11.321 12.484  1.00 28.06 ? 529 HOH A O   1 
HETATM 8833 O  O   . HOH U 6 .   ? 7.749   -20.325 -0.193  1.00 26.96 ? 530 HOH A O   1 
HETATM 8834 O  O   . HOH U 6 .   ? -25.662 2.610   -8.105  1.00 23.03 ? 531 HOH A O   1 
HETATM 8835 O  O   . HOH U 6 .   ? -21.842 3.565   -7.713  1.00 29.52 ? 532 HOH A O   1 
HETATM 8836 O  O   . HOH U 6 .   ? -5.672  -1.849  22.586  1.00 22.96 ? 533 HOH A O   1 
HETATM 8837 O  O   . HOH U 6 .   ? 20.411  3.574   12.248  1.00 38.45 ? 534 HOH A O   1 
HETATM 8838 O  O   . HOH U 6 .   ? -12.879 0.789   -21.116 1.00 29.60 ? 535 HOH A O   1 
HETATM 8839 O  O   . HOH U 6 .   ? -18.405 -8.313  -12.354 1.00 34.20 ? 536 HOH A O   1 
HETATM 8840 O  O   . HOH U 6 .   ? -5.274  -15.849 7.755   1.00 30.03 ? 537 HOH A O   1 
HETATM 8841 O  O   . HOH U 6 .   ? -14.538 11.194  4.616   1.00 25.40 ? 538 HOH A O   1 
HETATM 8842 O  O   . HOH U 6 .   ? -8.507  22.658  -3.450  1.00 23.92 ? 539 HOH A O   1 
HETATM 8843 O  O   . HOH U 6 .   ? -10.745 14.271  8.935   1.00 29.18 ? 540 HOH A O   1 
HETATM 8844 O  O   . HOH U 6 .   ? 2.218   17.454  5.265   1.00 31.38 ? 541 HOH A O   1 
HETATM 8845 O  O   . HOH U 6 .   ? 19.598  7.216   10.735  1.00 31.46 ? 542 HOH A O   1 
HETATM 8846 O  O   . HOH U 6 .   ? -16.386 2.913   -6.774  1.00 26.59 ? 543 HOH A O   1 
HETATM 8847 O  O   . HOH U 6 .   ? -17.632 5.170   13.254  1.00 34.63 ? 544 HOH A O   1 
HETATM 8848 O  O   . HOH U 6 .   ? 18.104  -5.667  -10.389 1.00 40.23 ? 545 HOH A O   1 
HETATM 8849 O  O   . HOH U 6 .   ? 16.132  -6.900  8.935   1.00 26.88 ? 546 HOH A O   1 
HETATM 8850 O  O   . HOH U 6 .   ? 9.677   7.538   -19.337 1.00 37.63 ? 547 HOH A O   1 
HETATM 8851 O  O   . HOH U 6 .   ? -21.112 2.779   3.018   1.00 29.50 ? 548 HOH A O   1 
HETATM 8852 O  O   . HOH U 6 .   ? -7.675  -0.410  -17.463 1.00 23.94 ? 549 HOH A O   1 
HETATM 8853 O  O   . HOH U 6 .   ? -8.904  -17.820 1.170   1.00 25.41 ? 550 HOH A O   1 
HETATM 8854 O  O   . HOH U 6 .   ? 3.292   -9.399  -12.639 1.00 28.09 ? 551 HOH A O   1 
HETATM 8855 O  O   . HOH U 6 .   ? -1.702  -18.918 5.975   1.00 32.33 ? 552 HOH A O   1 
HETATM 8856 O  O   . HOH U 6 .   ? -10.059 10.229  -14.586 1.00 24.49 ? 553 HOH A O   1 
HETATM 8857 O  O   . HOH U 6 .   ? 1.045   -12.235 -12.034 1.00 32.55 ? 554 HOH A O   1 
HETATM 8858 O  O   . HOH U 6 .   ? -13.785 -11.410 4.210   1.00 25.43 ? 555 HOH A O   1 
HETATM 8859 O  O   . HOH U 6 .   ? -17.153 -13.161 -4.552  1.00 32.53 ? 556 HOH A O   1 
HETATM 8860 O  O   . HOH U 6 .   ? -8.343  -9.296  13.515  1.00 34.59 ? 557 HOH A O   1 
HETATM 8861 O  O   . HOH U 6 .   ? 13.516  -15.851 -9.765  1.00 35.45 ? 558 HOH A O   1 
HETATM 8862 O  O   . HOH U 6 .   ? -22.813 -2.759  -1.198  1.00 32.60 ? 559 HOH A O   1 
HETATM 8863 O  O   . HOH U 6 .   ? -2.889  6.788   -19.748 1.00 29.16 ? 560 HOH A O   1 
HETATM 8864 O  O   . HOH U 6 .   ? 8.593   -4.014  22.431  1.00 34.70 ? 561 HOH A O   1 
HETATM 8865 O  O   . HOH U 6 .   ? 21.073  -14.434 0.883   1.00 34.11 ? 562 HOH A O   1 
HETATM 8866 O  O   . HOH U 6 .   ? 6.369   8.337   -16.909 1.00 46.70 ? 563 HOH A O   1 
HETATM 8867 O  O   . HOH U 6 .   ? -7.768  1.617   20.501  1.00 25.82 ? 564 HOH A O   1 
HETATM 8868 O  O   . HOH U 6 .   ? -14.003 -13.000 -11.967 1.00 35.78 ? 565 HOH A O   1 
HETATM 8869 O  O   . HOH U 6 .   ? -21.507 -4.443  4.834   1.00 27.38 ? 566 HOH A O   1 
HETATM 8870 O  O   . HOH U 6 .   ? -9.268  15.993  -13.859 1.00 32.55 ? 567 HOH A O   1 
HETATM 8871 O  O   . HOH U 6 .   ? -1.939  -18.858 9.900   1.00 44.39 ? 568 HOH A O   1 
HETATM 8872 O  O   . HOH U 6 .   ? -11.483 -4.988  -20.759 1.00 34.98 ? 569 HOH A O   1 
HETATM 8873 O  O   . HOH U 6 .   ? 1.681   -6.183  20.070  1.00 37.68 ? 570 HOH A O   1 
HETATM 8874 O  O   . HOH U 6 .   ? 24.368  7.178   1.984   1.00 40.59 ? 571 HOH A O   1 
HETATM 8875 O  O   . HOH U 6 .   ? -5.160  -3.553  -19.939 1.00 32.07 ? 572 HOH A O   1 
HETATM 8876 O  O   . HOH U 6 .   ? -16.177 13.261  -11.209 1.00 29.57 ? 573 HOH A O   1 
HETATM 8877 O  O   . HOH U 6 .   ? -11.725 16.744  8.040   1.00 36.36 ? 574 HOH A O   1 
HETATM 8878 O  O   . HOH U 6 .   ? 4.849   -0.819  17.067  1.00 40.52 ? 575 HOH A O   1 
HETATM 8879 O  O   . HOH U 6 .   ? 21.081  -10.513 -1.250  1.00 24.13 ? 576 HOH A O   1 
HETATM 8880 O  O   . HOH U 6 .   ? -3.532  15.907  9.181   1.00 29.43 ? 577 HOH A O   1 
HETATM 8881 O  O   . HOH U 6 .   ? -11.591 7.763   21.393  1.00 28.90 ? 578 HOH A O   1 
HETATM 8882 O  O   . HOH U 6 .   ? -24.892 -1.146  -17.521 1.00 38.84 ? 579 HOH A O   1 
HETATM 8883 O  O   . HOH U 6 .   ? 21.583  1.238   4.743   1.00 30.09 ? 580 HOH A O   1 
HETATM 8884 O  O   . HOH U 6 .   ? 5.110   9.692   4.511   1.00 30.48 ? 581 HOH A O   1 
HETATM 8885 O  O   . HOH U 6 .   ? -7.232  -8.463  24.070  1.00 27.11 ? 582 HOH A O   1 
HETATM 8886 O  O   . HOH U 6 .   ? 12.266  -14.186 10.207  1.00 30.01 ? 583 HOH A O   1 
HETATM 8887 O  O   . HOH U 6 .   ? -13.708 -5.242  18.356  1.00 33.64 ? 584 HOH A O   1 
HETATM 8888 O  O   . HOH U 6 .   ? -15.569 9.896   7.266   1.00 34.82 ? 585 HOH A O   1 
HETATM 8889 O  O   . HOH U 6 .   ? -16.987 -9.633  -13.500 1.00 35.90 ? 586 HOH A O   1 
HETATM 8890 O  O   . HOH U 6 .   ? -13.105 1.414   -18.623 1.00 27.85 ? 587 HOH A O   1 
HETATM 8891 O  O   . HOH U 6 .   ? 5.154   -6.403  18.910  1.00 38.12 ? 588 HOH A O   1 
HETATM 8892 O  O   . HOH U 6 .   ? 7.386   11.236  7.422   1.00 39.43 ? 589 HOH A O   1 
HETATM 8893 O  O   . HOH U 6 .   ? 12.062  6.589   -10.686 1.00 40.04 ? 590 HOH A O   1 
HETATM 8894 O  O   . HOH U 6 .   ? 17.733  2.207   17.593  1.00 30.69 ? 591 HOH A O   1 
HETATM 8895 O  O   . HOH U 6 .   ? -5.084  -0.675  19.901  1.00 25.18 ? 592 HOH A O   1 
HETATM 8896 O  O   . HOH U 6 .   ? -17.863 -12.170 -13.892 1.00 28.14 ? 593 HOH A O   1 
HETATM 8897 O  O   . HOH U 6 .   ? -13.560 11.099  -9.488  1.00 31.56 ? 594 HOH A O   1 
HETATM 8898 O  O   . HOH U 6 .   ? -11.509 -5.460  12.287  1.00 29.80 ? 595 HOH A O   1 
HETATM 8899 O  O   . HOH U 6 .   ? 15.304  17.726  -6.303  1.00 33.03 ? 596 HOH A O   1 
HETATM 8900 O  O   . HOH U 6 .   ? 2.258   7.844   -18.035 1.00 35.86 ? 597 HOH A O   1 
HETATM 8901 O  O   . HOH U 6 .   ? -8.444  -5.802  -20.079 1.00 33.93 ? 598 HOH A O   1 
HETATM 8902 O  O   . HOH U 6 .   ? 1.401   -17.855 11.534  1.00 34.30 ? 599 HOH A O   1 
HETATM 8903 O  O   . HOH U 6 .   ? -24.229 4.929   9.832   1.00 42.23 ? 600 HOH A O   1 
HETATM 8904 O  O   . HOH U 6 .   ? -19.487 3.327   -3.685  1.00 30.19 ? 601 HOH A O   1 
HETATM 8905 O  O   . HOH U 6 .   ? -19.064 -11.799 -1.868  1.00 38.75 ? 602 HOH A O   1 
HETATM 8906 O  O   . HOH U 6 .   ? 8.583   -17.603 6.969   1.00 31.75 ? 603 HOH A O   1 
HETATM 8907 O  O   . HOH U 6 .   ? 2.481   -6.981  17.625  1.00 32.25 ? 604 HOH A O   1 
HETATM 8908 O  O   . HOH U 6 .   ? 6.808   -1.795  18.531  1.00 36.09 ? 605 HOH A O   1 
HETATM 8909 O  O   . HOH U 6 .   ? 13.421  -21.317 -2.442  1.00 36.11 ? 606 HOH A O   1 
HETATM 8910 O  O   . HOH U 6 .   ? 16.026  14.886  -3.119  1.00 37.95 ? 607 HOH A O   1 
HETATM 8911 O  O   . HOH U 6 .   ? -14.760 -17.296 -2.731  1.00 32.33 ? 608 HOH A O   1 
HETATM 8912 O  O   . HOH U 6 .   ? 6.044   4.883   14.461  1.00 39.94 ? 609 HOH A O   1 
HETATM 8913 O  O   . HOH U 6 .   ? -11.423 -0.549  -20.245 1.00 40.57 ? 610 HOH A O   1 
HETATM 8914 O  O   . HOH U 6 .   ? 18.488  11.577  3.818   1.00 31.27 ? 611 HOH A O   1 
HETATM 8915 O  O   . HOH U 6 .   ? -19.745 4.259   -12.347 1.00 30.19 ? 612 HOH A O   1 
HETATM 8916 O  O   . HOH U 6 .   ? -3.317  3.787   19.758  1.00 47.58 ? 613 HOH A O   1 
HETATM 8917 O  O   . HOH U 6 .   ? 20.533  -4.798  -3.817  1.00 38.57 ? 614 HOH A O   1 
HETATM 8918 O  O   . HOH U 6 .   ? 22.664  2.701   6.707   1.00 35.18 ? 615 HOH A O   1 
HETATM 8919 O  O   . HOH U 6 .   ? -0.961  -10.611 14.109  1.00 39.30 ? 616 HOH A O   1 
HETATM 8920 O  O   . HOH U 6 .   ? 7.852   -0.227  20.395  1.00 45.59 ? 617 HOH A O   1 
HETATM 8921 O  O   . HOH U 6 .   ? -22.198 -0.135  -18.267 1.00 37.25 ? 618 HOH A O   1 
HETATM 8922 O  O   . HOH U 6 .   ? -18.186 4.902   -5.514  1.00 26.52 ? 619 HOH A O   1 
HETATM 8923 O  O   . HOH U 6 .   ? 5.589   -11.535 15.741  1.00 22.63 ? 620 HOH A O   1 
HETATM 8924 O  O   . HOH U 6 .   ? -4.962  -18.377 -7.158  1.00 28.78 ? 621 HOH A O   1 
HETATM 8925 O  O   . HOH U 6 .   ? 18.637  -3.057  15.458  1.00 42.88 ? 622 HOH A O   1 
HETATM 8926 O  O   . HOH U 6 .   ? -12.597 13.398  4.970   1.00 25.23 ? 623 HOH A O   1 
HETATM 8927 O  O   . HOH U 6 .   ? 18.428  1.982   -7.754  1.00 39.06 ? 624 HOH A O   1 
HETATM 8928 O  O   . HOH U 6 .   ? -9.884  -13.018 -10.433 1.00 29.35 ? 625 HOH A O   1 
HETATM 8929 O  O   . HOH U 6 .   ? -3.772  -5.800  -19.526 1.00 34.68 ? 626 HOH A O   1 
HETATM 8930 O  O   . HOH U 6 .   ? 22.060  5.518   5.443   1.00 39.38 ? 627 HOH A O   1 
HETATM 8931 O  O   . HOH U 6 .   ? -10.390 1.636   -18.261 1.00 34.24 ? 628 HOH A O   1 
HETATM 8932 O  O   . HOH U 6 .   ? 3.516   -8.784  -15.059 1.00 30.82 ? 629 HOH A O   1 
HETATM 8933 O  O   . HOH U 6 .   ? -21.250 4.977   10.684  1.00 55.20 ? 630 HOH A O   1 
HETATM 8934 O  O   . HOH U 6 .   ? 1.807   -4.278  27.687  1.00 35.50 ? 631 HOH A O   1 
HETATM 8935 O  O   . HOH U 6 .   ? 5.728   -7.973  -13.773 1.00 38.24 ? 632 HOH A O   1 
HETATM 8936 O  O   . HOH U 6 .   ? -24.055 2.385   -3.957  1.00 38.98 ? 633 HOH A O   1 
HETATM 8937 O  O   . HOH U 6 .   ? -25.437 1.686   -10.487 1.00 30.86 ? 634 HOH A O   1 
HETATM 8938 O  O   . HOH U 6 .   ? -7.061  -11.116 17.820  1.00 36.68 ? 635 HOH A O   1 
HETATM 8939 O  O   . HOH U 6 .   ? 12.471  -4.615  27.385  1.00 33.73 ? 636 HOH A O   1 
HETATM 8940 O  O   . HOH U 6 .   ? 18.028  -8.420  9.711   1.00 30.85 ? 637 HOH A O   1 
HETATM 8941 O  O   . HOH U 6 .   ? -23.720 2.567   -13.039 1.00 36.81 ? 638 HOH A O   1 
HETATM 8942 O  O   . HOH U 6 .   ? -7.472  -12.238 -9.826  1.00 21.70 ? 639 HOH A O   1 
HETATM 8943 O  O   . HOH U 6 .   ? 8.089   -7.473  25.494  1.00 34.83 ? 640 HOH A O   1 
HETATM 8944 O  O   . HOH U 6 .   ? -5.889  0.733   -20.940 1.00 31.06 ? 641 HOH A O   1 
HETATM 8945 O  O   . HOH U 6 .   ? -28.257 1.727   1.699   1.00 45.68 ? 642 HOH A O   1 
HETATM 8946 O  O   . HOH U 6 .   ? 18.580  -5.482  16.864  1.00 43.07 ? 643 HOH A O   1 
HETATM 8947 O  O   . HOH U 6 .   ? -7.054  -7.526  16.951  1.00 20.31 ? 644 HOH A O   1 
HETATM 8948 O  O   . HOH U 6 .   ? -7.533  -8.958  19.264  1.00 21.09 ? 645 HOH A O   1 
HETATM 8949 O  O   . HOH U 6 .   ? -20.091 -5.414  -14.645 1.00 32.51 ? 646 HOH A O   1 
HETATM 8950 O  O   . HOH U 6 .   ? -21.931 3.307   0.098   1.00 30.71 ? 647 HOH A O   1 
HETATM 8951 O  O   . HOH U 6 .   ? 0.730   1.844   25.548  1.00 29.37 ? 648 HOH A O   1 
HETATM 8952 O  O   . HOH U 6 .   ? -2.920  -2.707  24.474  1.00 42.06 ? 649 HOH A O   1 
HETATM 8953 O  O   . HOH U 6 .   ? 0.371   -6.636  23.831  1.00 29.32 ? 650 HOH A O   1 
HETATM 8954 O  O   . HOH U 6 .   ? -0.028  -4.694  23.413  1.00 30.58 ? 651 HOH A O   1 
HETATM 8955 O  O   . HOH U 6 .   ? 2.292   17.034  -9.115  1.00 29.71 ? 652 HOH A O   1 
HETATM 8956 O  O   . HOH V 6 .   ? -16.028 -6.466  31.630  1.00 9.09  ? 401 HOH B O   1 
HETATM 8957 O  O   . HOH V 6 .   ? 0.325   7.609   32.011  1.00 17.01 ? 402 HOH B O   1 
HETATM 8958 O  O   . HOH V 6 .   ? -28.239 -7.972  28.268  1.00 16.84 ? 403 HOH B O   1 
HETATM 8959 O  O   . HOH V 6 .   ? -23.340 -14.956 33.394  1.00 15.64 ? 404 HOH B O   1 
HETATM 8960 O  O   . HOH V 6 .   ? -16.725 -2.199  48.143  1.00 9.94  ? 405 HOH B O   1 
HETATM 8961 O  O   . HOH V 6 .   ? -17.823 -11.615 44.214  1.00 9.18  ? 406 HOH B O   1 
HETATM 8962 O  O   . HOH V 6 .   ? -24.912 -11.394 43.033  1.00 11.76 ? 407 HOH B O   1 
HETATM 8963 O  O   . HOH V 6 .   ? -17.698 -5.281  26.300  1.00 13.34 ? 408 HOH B O   1 
HETATM 8964 O  O   . HOH V 6 .   ? -3.916  -18.529 34.665  1.00 14.44 ? 409 HOH B O   1 
HETATM 8965 O  O   . HOH V 6 .   ? -10.365 -13.541 43.147  1.00 10.36 ? 410 HOH B O   1 
HETATM 8966 O  O   . HOH V 6 .   ? -20.848 -9.242  44.294  1.00 10.36 ? 411 HOH B O   1 
HETATM 8967 O  O   . HOH V 6 .   ? -31.593 6.944   48.304  1.00 20.22 ? 412 HOH B O   1 
HETATM 8968 O  O   . HOH V 6 .   ? -23.096 10.588  36.148  1.00 10.98 ? 413 HOH B O   1 
HETATM 8969 O  O   . HOH V 6 .   ? -23.629 -3.019  52.271  1.00 13.34 ? 414 HOH B O   1 
HETATM 8970 O  O   . HOH V 6 .   ? -6.482  11.593  26.184  1.00 36.89 ? 415 HOH B O   1 
HETATM 8971 O  O   . HOH V 6 .   ? -20.099 -10.429 31.266  1.00 15.42 ? 416 HOH B O   1 
HETATM 8972 O  O   . HOH V 6 .   ? -28.987 -6.829  42.607  1.00 11.31 ? 417 HOH B O   1 
HETATM 8973 O  O   . HOH V 6 .   ? -26.312 -9.920  47.419  1.00 22.56 ? 418 HOH B O   1 
HETATM 8974 O  O   . HOH V 6 .   ? -23.131 -10.446 45.031  1.00 10.79 ? 419 HOH B O   1 
HETATM 8975 O  O   . HOH V 6 .   ? -24.874 -1.908  55.705  1.00 13.76 ? 420 HOH B O   1 
HETATM 8976 O  O   . HOH V 6 .   ? -9.520  20.897  43.535  1.00 18.10 ? 421 HOH B O   1 
HETATM 8977 O  O   . HOH V 6 .   ? 2.263   0.780   56.017  1.00 16.39 ? 422 HOH B O   1 
HETATM 8978 O  O   . HOH V 6 .   ? -20.176 -17.464 39.608  1.00 15.69 ? 423 HOH B O   1 
HETATM 8979 O  O   . HOH V 6 .   ? -13.648 10.559  24.966  1.00 20.92 ? 424 HOH B O   1 
HETATM 8980 O  O   . HOH V 6 .   ? -30.534 0.392   46.054  1.00 13.73 ? 425 HOH B O   1 
HETATM 8981 O  O   . HOH V 6 .   ? -14.030 -15.322 36.715  1.00 13.41 ? 426 HOH B O   1 
HETATM 8982 O  O   . HOH V 6 .   ? -24.026 -13.999 42.928  1.00 12.72 ? 427 HOH B O   1 
HETATM 8983 O  O   . HOH V 6 .   ? -13.563 -6.923  61.501  1.00 32.49 ? 428 HOH B O   1 
HETATM 8984 O  O   . HOH V 6 .   ? -29.299 -9.286  43.969  1.00 20.26 ? 429 HOH B O   1 
HETATM 8985 O  O   . HOH V 6 .   ? -23.071 -12.447 46.967  1.00 20.51 ? 430 HOH B O   1 
HETATM 8986 O  O   . HOH V 6 .   ? -12.118 21.869  36.487  1.00 14.61 ? 431 HOH B O   1 
HETATM 8987 O  O   . HOH V 6 .   ? -2.728  -5.866  27.702  1.00 15.77 ? 432 HOH B O   1 
HETATM 8988 O  O   . HOH V 6 .   ? -7.993  -10.063 27.964  1.00 21.53 ? 433 HOH B O   1 
HETATM 8989 O  O   . HOH V 6 .   ? 5.890   -2.742  50.516  1.00 20.14 ? 434 HOH B O   1 
HETATM 8990 O  O   . HOH V 6 .   ? -15.062 -16.376 38.997  1.00 12.50 ? 435 HOH B O   1 
HETATM 8991 O  O   . HOH V 6 .   ? -24.333 12.292  32.363  1.00 19.27 ? 436 HOH B O   1 
HETATM 8992 O  O   . HOH V 6 .   ? -7.132  12.696  33.611  1.00 15.87 ? 437 HOH B O   1 
HETATM 8993 O  O   . HOH V 6 .   ? 6.790   2.541   48.160  1.00 25.01 ? 438 HOH B O   1 
HETATM 8994 O  O   . HOH V 6 .   ? -7.921  -16.474 28.984  1.00 21.87 ? 439 HOH B O   1 
HETATM 8995 O  O   . HOH V 6 .   ? -17.528 -14.298 30.742  1.00 20.61 ? 440 HOH B O   1 
HETATM 8996 O  O   . HOH V 6 .   ? -28.745 -1.534  49.878  1.00 19.94 ? 441 HOH B O   1 
HETATM 8997 O  O   . HOH V 6 .   ? 2.716   -3.986  31.781  1.00 20.14 ? 442 HOH B O   1 
HETATM 8998 O  O   . HOH V 6 .   ? -25.217 -14.616 31.484  1.00 27.00 ? 443 HOH B O   1 
HETATM 8999 O  O   . HOH V 6 .   ? 2.794   9.802   33.703  1.00 15.44 ? 444 HOH B O   1 
HETATM 9000 O  O   . HOH V 6 .   ? -30.738 -13.223 33.167  1.00 32.04 ? 445 HOH B O   1 
HETATM 9001 O  O   . HOH V 6 .   ? -31.407 -6.000  34.450  1.00 24.29 ? 446 HOH B O   1 
HETATM 9002 O  O   . HOH V 6 .   ? 1.439   -14.705 34.326  1.00 21.95 ? 447 HOH B O   1 
HETATM 9003 O  O   . HOH V 6 .   ? -25.828 -15.491 44.274  1.00 26.23 ? 448 HOH B O   1 
HETATM 9004 O  O   . HOH V 6 .   ? 1.740   1.160   30.316  1.00 22.10 ? 449 HOH B O   1 
HETATM 9005 O  O   . HOH V 6 .   ? -32.379 7.882   24.822  1.00 38.65 ? 450 HOH B O   1 
HETATM 9006 O  O   . HOH V 6 .   ? -29.895 -13.068 37.818  1.00 23.33 ? 451 HOH B O   1 
HETATM 9007 O  O   . HOH V 6 .   ? -0.738  3.031   57.693  1.00 34.19 ? 452 HOH B O   1 
HETATM 9008 O  O   . HOH V 6 .   ? -35.248 -13.108 34.597  1.00 33.47 ? 453 HOH B O   1 
HETATM 9009 O  O   . HOH V 6 .   ? -33.354 -3.910  34.165  1.00 21.66 ? 454 HOH B O   1 
HETATM 9010 O  O   . HOH V 6 .   ? -15.205 -16.648 34.387  1.00 16.42 ? 455 HOH B O   1 
HETATM 9011 O  O   . HOH V 6 .   ? -30.447 -6.661  40.331  1.00 22.78 ? 456 HOH B O   1 
HETATM 9012 O  O   . HOH V 6 .   ? -6.859  -1.943  43.552  1.00 13.13 ? 457 HOH B O   1 
HETATM 9013 O  O   . HOH V 6 .   ? -1.285  -14.910 47.003  1.00 20.69 ? 458 HOH B O   1 
HETATM 9014 O  O   . HOH V 6 .   ? -5.376  -17.618 41.527  1.00 23.52 ? 459 HOH B O   1 
HETATM 9015 O  O   . HOH V 6 .   ? -4.395  11.987  33.157  1.00 14.65 ? 460 HOH B O   1 
HETATM 9016 O  O   . HOH V 6 .   ? -21.783 -12.134 29.955  1.00 20.77 ? 461 HOH B O   1 
HETATM 9017 O  O   . HOH V 6 .   ? -29.172 -7.073  25.570  1.00 26.53 ? 462 HOH B O   1 
HETATM 9018 O  O   . HOH V 6 .   ? -29.724 2.125   59.132  1.00 19.02 ? 463 HOH B O   1 
HETATM 9019 O  O   . HOH V 6 .   ? 2.959   -15.265 50.698  1.00 35.22 ? 464 HOH B O   1 
HETATM 9020 O  O   . HOH V 6 .   ? -10.376 -2.411  54.544  1.00 21.40 ? 465 HOH B O   1 
HETATM 9021 O  O   . HOH V 6 .   ? -19.534 17.835  31.509  1.00 17.62 ? 466 HOH B O   1 
HETATM 9022 O  O   . HOH V 6 .   ? -35.060 -2.343  22.203  1.00 39.40 ? 467 HOH B O   1 
HETATM 9023 O  O   . HOH V 6 .   ? -14.170 21.899  34.552  1.00 16.25 ? 468 HOH B O   1 
HETATM 9024 O  O   . HOH V 6 .   ? -9.709  -19.924 35.497  1.00 16.13 ? 469 HOH B O   1 
HETATM 9025 O  O   . HOH V 6 .   ? -22.018 5.356   64.518  1.00 25.06 ? 470 HOH B O   1 
HETATM 9026 O  O   . HOH V 6 .   ? 5.292   -4.903  31.205  1.00 35.66 ? 471 HOH B O   1 
HETATM 9027 O  O   . HOH V 6 .   ? -10.582 16.952  40.779  1.00 17.68 ? 472 HOH B O   1 
HETATM 9028 O  O   . HOH V 6 .   ? -27.563 4.721   33.214  1.00 18.50 ? 473 HOH B O   1 
HETATM 9029 O  O   . HOH V 6 .   ? -25.202 8.012   54.687  1.00 17.37 ? 474 HOH B O   1 
HETATM 9030 O  O   . HOH V 6 .   ? -13.975 -5.288  65.881  1.00 38.14 ? 475 HOH B O   1 
HETATM 9031 O  O   . HOH V 6 .   ? -6.124  -4.500  25.662  1.00 20.04 ? 476 HOH B O   1 
HETATM 9032 O  O   . HOH V 6 .   ? -30.363 3.163   56.615  1.00 22.85 ? 477 HOH B O   1 
HETATM 9033 O  O   . HOH V 6 .   ? -20.235 8.729   59.314  1.00 30.23 ? 478 HOH B O   1 
HETATM 9034 O  O   . HOH V 6 .   ? -11.739 -16.634 36.913  1.00 15.81 ? 479 HOH B O   1 
HETATM 9035 O  O   . HOH V 6 .   ? -21.198 12.727  26.535  1.00 18.68 ? 480 HOH B O   1 
HETATM 9036 O  O   . HOH V 6 .   ? -12.027 -9.512  53.699  1.00 19.81 ? 481 HOH B O   1 
HETATM 9037 O  O   . HOH V 6 .   ? -19.484 8.300   21.043  1.00 27.68 ? 482 HOH B O   1 
HETATM 9038 O  O   . HOH V 6 .   ? 5.222   5.113   50.986  1.00 30.18 ? 483 HOH B O   1 
HETATM 9039 O  O   . HOH V 6 .   ? -24.176 12.790  46.444  1.00 18.19 ? 484 HOH B O   1 
HETATM 9040 O  O   . HOH V 6 .   ? -1.089  -1.058  30.102  1.00 20.17 ? 485 HOH B O   1 
HETATM 9041 O  O   . HOH V 6 .   ? -25.567 10.750  47.838  1.00 18.77 ? 486 HOH B O   1 
HETATM 9042 O  O   . HOH V 6 .   ? -21.133 20.114  44.495  1.00 36.13 ? 487 HOH B O   1 
HETATM 9043 O  O   . HOH V 6 .   ? 3.955   -7.755  30.233  1.00 24.23 ? 488 HOH B O   1 
HETATM 9044 O  O   . HOH V 6 .   ? -18.487 -18.295 41.677  1.00 13.96 ? 489 HOH B O   1 
HETATM 9045 O  O   . HOH V 6 .   ? -17.833 -17.565 37.842  1.00 17.95 ? 490 HOH B O   1 
HETATM 9046 O  O   . HOH V 6 .   ? -32.504 -7.800  38.830  1.00 30.19 ? 491 HOH B O   1 
HETATM 9047 O  O   . HOH V 6 .   ? -23.676 16.027  32.587  1.00 20.76 ? 492 HOH B O   1 
HETATM 9048 O  O   . HOH V 6 .   ? -11.664 -13.695 53.189  1.00 20.98 ? 493 HOH B O   1 
HETATM 9049 O  O   . HOH V 6 .   ? -10.054 -13.123 27.529  1.00 32.69 ? 494 HOH B O   1 
HETATM 9050 O  O   . HOH V 6 .   ? -31.113 -10.068 39.517  1.00 20.09 ? 495 HOH B O   1 
HETATM 9051 O  O   . HOH V 6 .   ? -26.951 17.756  35.419  1.00 25.72 ? 496 HOH B O   1 
HETATM 9052 O  O   . HOH V 6 .   ? -25.439 9.775   32.925  1.00 23.27 ? 497 HOH B O   1 
HETATM 9053 O  O   . HOH V 6 .   ? -23.116 8.987   53.087  1.00 17.71 ? 498 HOH B O   1 
HETATM 9054 O  O   . HOH V 6 .   ? -30.737 -6.724  36.860  1.00 17.58 ? 499 HOH B O   1 
HETATM 9055 O  O   . HOH V 6 .   ? -24.726 -17.952 37.750  1.00 23.01 ? 500 HOH B O   1 
HETATM 9056 O  O   . HOH V 6 .   ? -28.534 -16.474 31.884  1.00 27.43 ? 501 HOH B O   1 
HETATM 9057 O  O   . HOH V 6 .   ? -19.626 1.129   23.066  1.00 23.31 ? 502 HOH B O   1 
HETATM 9058 O  O   . HOH V 6 .   ? 6.251   -1.734  37.811  1.00 25.70 ? 503 HOH B O   1 
HETATM 9059 O  O   . HOH V 6 .   ? -7.791  2.027   23.478  1.00 23.66 ? 504 HOH B O   1 
HETATM 9060 O  O   . HOH V 6 .   ? -7.131  15.385  41.614  1.00 25.28 ? 505 HOH B O   1 
HETATM 9061 O  O   . HOH V 6 .   ? -25.800 14.411  33.323  1.00 21.92 ? 506 HOH B O   1 
HETATM 9062 O  O   . HOH V 6 .   ? -10.164 19.610  39.598  1.00 16.87 ? 507 HOH B O   1 
HETATM 9063 O  O   . HOH V 6 .   ? -22.554 -12.256 49.610  1.00 34.16 ? 508 HOH B O   1 
HETATM 9064 O  O   . HOH V 6 .   ? -13.183 21.861  31.885  1.00 21.14 ? 509 HOH B O   1 
HETATM 9065 O  O   . HOH V 6 .   ? -10.244 -19.183 31.949  1.00 22.76 ? 510 HOH B O   1 
HETATM 9066 O  O   . HOH V 6 .   ? -7.367  -0.440  24.416  1.00 15.38 ? 511 HOH B O   1 
HETATM 9067 O  O   . HOH V 6 .   ? -32.854 -6.645  43.339  1.00 23.86 ? 512 HOH B O   1 
HETATM 9068 O  O   . HOH V 6 .   ? -5.326  -11.491 28.621  1.00 17.02 ? 513 HOH B O   1 
HETATM 9069 O  O   . HOH V 6 .   ? -29.417 -4.019  58.693  1.00 22.08 ? 514 HOH B O   1 
HETATM 9070 O  O   . HOH V 6 .   ? -15.821 -16.141 31.758  1.00 22.94 ? 515 HOH B O   1 
HETATM 9071 O  O   . HOH V 6 .   ? -17.681 -1.999  20.861  1.00 19.75 ? 516 HOH B O   1 
HETATM 9072 O  O   . HOH V 6 .   ? -27.419 -11.301 44.218  1.00 22.90 ? 517 HOH B O   1 
HETATM 9073 O  O   . HOH V 6 .   ? 4.840   -2.568  65.589  1.00 25.89 ? 518 HOH B O   1 
HETATM 9074 O  O   . HOH V 6 .   ? -32.681 -8.464  27.939  1.00 22.89 ? 519 HOH B O   1 
HETATM 9075 O  O   . HOH V 6 .   ? 2.016   -8.245  45.936  1.00 22.13 ? 520 HOH B O   1 
HETATM 9076 O  O   . HOH V 6 .   ? -20.877 -0.539  64.346  1.00 21.99 ? 521 HOH B O   1 
HETATM 9077 O  O   . HOH V 6 .   ? -23.007 23.501  33.715  1.00 22.12 ? 522 HOH B O   1 
HETATM 9078 O  O   . HOH V 6 .   ? 10.676  7.169   41.499  1.00 25.54 ? 523 HOH B O   1 
HETATM 9079 O  O   . HOH V 6 .   ? 4.746   10.958  40.305  1.00 23.17 ? 524 HOH B O   1 
HETATM 9080 O  O   . HOH V 6 .   ? -12.968 13.098  24.044  1.00 29.79 ? 525 HOH B O   1 
HETATM 9081 O  O   . HOH V 6 .   ? -6.133  -20.279 39.104  1.00 21.45 ? 526 HOH B O   1 
HETATM 9082 O  O   . HOH V 6 .   ? 5.142   -2.851  54.797  1.00 24.47 ? 527 HOH B O   1 
HETATM 9083 O  O   . HOH V 6 .   ? -10.917 -4.778  55.969  1.00 23.07 ? 528 HOH B O   1 
HETATM 9084 O  O   . HOH V 6 .   ? -1.531  -14.124 49.731  1.00 23.73 ? 529 HOH B O   1 
HETATM 9085 O  O   . HOH V 6 .   ? -22.502 22.750  36.338  1.00 18.97 ? 530 HOH B O   1 
HETATM 9086 O  O   . HOH V 6 .   ? -13.893 4.743   22.643  1.00 23.19 ? 531 HOH B O   1 
HETATM 9087 O  O   . HOH V 6 .   ? -10.959 -9.272  26.616  1.00 22.45 ? 532 HOH B O   1 
HETATM 9088 O  O   . HOH V 6 .   ? -31.398 -9.924  42.222  1.00 28.01 ? 533 HOH B O   1 
HETATM 9089 O  O   . HOH V 6 .   ? 1.681   -11.227 51.655  1.00 26.62 ? 534 HOH B O   1 
HETATM 9090 O  O   . HOH V 6 .   ? -31.100 -0.546  49.192  1.00 24.48 ? 535 HOH B O   1 
HETATM 9091 O  O   . HOH V 6 .   ? -27.147 4.979   62.169  1.00 28.63 ? 536 HOH B O   1 
HETATM 9092 O  O   . HOH V 6 .   ? -35.439 -3.398  35.963  1.00 22.46 ? 537 HOH B O   1 
HETATM 9093 O  O   . HOH V 6 .   ? -35.347 -4.462  44.646  1.00 22.22 ? 538 HOH B O   1 
HETATM 9094 O  O   . HOH V 6 .   ? -27.375 -2.741  54.895  1.00 21.84 ? 539 HOH B O   1 
HETATM 9095 O  O   . HOH V 6 .   ? -0.899  -18.725 34.228  0.50 17.08 ? 540 HOH B O   1 
HETATM 9096 O  O   . HOH V 6 .   ? 5.019   -6.969  43.083  1.00 25.01 ? 541 HOH B O   1 
HETATM 9097 O  O   . HOH V 6 .   ? -0.760  -15.842 29.234  1.00 31.12 ? 542 HOH B O   1 
HETATM 9098 O  O   . HOH V 6 .   ? -34.990 3.008   43.464  1.00 22.34 ? 543 HOH B O   1 
HETATM 9099 O  O   . HOH V 6 .   ? -1.565  -17.768 32.179  1.00 25.71 ? 544 HOH B O   1 
HETATM 9100 O  O   . HOH V 6 .   ? 2.496   -6.851  48.109  1.00 25.60 ? 545 HOH B O   1 
HETATM 9101 O  O   . HOH V 6 .   ? -15.320 4.257   20.327  1.00 31.38 ? 546 HOH B O   1 
HETATM 9102 O  O   . HOH V 6 .   ? -31.119 5.068   53.229  1.00 29.66 ? 547 HOH B O   1 
HETATM 9103 O  O   . HOH V 6 .   ? -28.238 14.994  31.997  1.00 27.09 ? 548 HOH B O   1 
HETATM 9104 O  O   . HOH V 6 .   ? -18.896 -15.691 47.543  1.00 28.02 ? 549 HOH B O   1 
HETATM 9105 O  O   . HOH V 6 .   ? -28.233 11.250  44.425  1.00 25.04 ? 550 HOH B O   1 
HETATM 9106 O  O   . HOH V 6 .   ? -11.654 17.629  44.825  1.00 27.06 ? 551 HOH B O   1 
HETATM 9107 O  O   . HOH V 6 .   ? 8.397   5.516   44.456  1.00 26.24 ? 552 HOH B O   1 
HETATM 9108 O  O   . HOH V 6 .   ? 7.108   5.366   37.285  1.00 28.73 ? 553 HOH B O   1 
HETATM 9109 O  O   . HOH V 6 .   ? 6.614   -4.906  35.235  1.00 33.60 ? 554 HOH B O   1 
HETATM 9110 O  O   . HOH V 6 .   ? -4.426  -12.632 56.768  1.00 28.80 ? 555 HOH B O   1 
HETATM 9111 O  O   . HOH V 6 .   ? -24.331 14.399  48.702  1.00 27.28 ? 556 HOH B O   1 
HETATM 9112 O  O   . HOH V 6 .   ? -30.767 -13.501 35.554  1.00 25.22 ? 557 HOH B O   1 
HETATM 9113 O  O   . HOH V 6 .   ? -4.227  -5.774  61.678  1.00 27.73 ? 558 HOH B O   1 
HETATM 9114 O  O   . HOH V 6 .   ? -12.857 -12.221 27.466  1.00 27.85 ? 559 HOH B O   1 
HETATM 9115 O  O   . HOH V 6 .   ? -26.954 -5.161  57.919  1.00 31.44 ? 560 HOH B O   1 
HETATM 9116 O  O   . HOH V 6 .   ? -22.755 -17.859 40.837  1.00 21.20 ? 561 HOH B O   1 
HETATM 9117 O  O   . HOH V 6 .   ? -31.750 0.614   60.315  1.00 19.47 ? 562 HOH B O   1 
HETATM 9118 O  O   . HOH V 6 .   ? -8.035  -11.411 54.939  1.00 21.35 ? 563 HOH B O   1 
HETATM 9119 O  O   . HOH V 6 .   ? -16.401 -18.608 49.324  1.00 31.89 ? 564 HOH B O   1 
HETATM 9120 O  O   . HOH V 6 .   ? 2.186   -3.067  66.116  1.00 23.15 ? 565 HOH B O   1 
HETATM 9121 O  O   . HOH V 6 .   ? -10.835 -11.508 54.464  1.00 29.79 ? 566 HOH B O   1 
HETATM 9122 O  O   . HOH V 6 .   ? -21.144 1.939   63.391  1.00 27.51 ? 567 HOH B O   1 
HETATM 9123 O  O   . HOH V 6 .   ? 8.852   2.800   46.000  1.00 28.69 ? 568 HOH B O   1 
HETATM 9124 O  O   . HOH V 6 .   ? 4.429   1.765   31.114  1.00 32.60 ? 569 HOH B O   1 
HETATM 9125 O  O   . HOH V 6 .   ? -17.267 16.070  48.729  1.00 29.70 ? 570 HOH B O   1 
HETATM 9126 O  O   . HOH V 6 .   ? -26.207 19.228  40.022  1.00 30.89 ? 571 HOH B O   1 
HETATM 9127 O  O   . HOH V 6 .   ? -22.661 -5.853  19.734  1.00 34.77 ? 572 HOH B O   1 
HETATM 9128 O  O   . HOH V 6 .   ? -4.519  7.451   20.229  1.00 39.09 ? 573 HOH B O   1 
HETATM 9129 O  O   . HOH V 6 .   ? 4.705   8.489   46.168  1.00 41.30 ? 574 HOH B O   1 
HETATM 9130 O  O   . HOH V 6 .   ? -2.457  6.520   28.227  1.00 33.94 ? 575 HOH B O   1 
HETATM 9131 O  O   . HOH V 6 .   ? -29.228 10.327  47.291  1.00 57.90 ? 576 HOH B O   1 
HETATM 9132 O  O   . HOH V 6 .   ? 0.063   7.925   52.156  1.00 29.27 ? 577 HOH B O   1 
HETATM 9133 O  O   . HOH V 6 .   ? -27.029 0.689   18.469  1.00 34.49 ? 578 HOH B O   1 
HETATM 9134 O  O   . HOH V 6 .   ? -30.383 2.898   33.148  1.00 27.87 ? 579 HOH B O   1 
HETATM 9135 O  O   . HOH V 6 .   ? -19.527 -3.446  19.745  1.00 39.29 ? 580 HOH B O   1 
HETATM 9136 O  O   . HOH V 6 .   ? -18.202 -5.742  19.954  1.00 29.36 ? 581 HOH B O   1 
HETATM 9137 O  O   . HOH V 6 .   ? -10.383 -0.942  57.798  1.00 33.74 ? 582 HOH B O   1 
HETATM 9138 O  O   . HOH V 6 .   ? -38.720 -1.138  22.202  1.00 38.43 ? 583 HOH B O   1 
HETATM 9139 O  O   . HOH V 6 .   ? -28.328 -12.782 27.902  1.00 34.39 ? 584 HOH B O   1 
HETATM 9140 O  O   . HOH V 6 .   ? -12.607 -17.541 51.225  1.00 33.15 ? 585 HOH B O   1 
HETATM 9141 O  O   . HOH V 6 .   ? -25.100 -5.356  52.153  1.00 25.38 ? 586 HOH B O   1 
HETATM 9142 O  O   . HOH V 6 .   ? 0.924   -11.107 61.582  1.00 58.27 ? 587 HOH B O   1 
HETATM 9143 O  O   . HOH V 6 .   ? -26.459 -10.256 27.377  1.00 29.26 ? 588 HOH B O   1 
HETATM 9144 O  O   . HOH V 6 .   ? 10.343  0.283   57.677  1.00 43.12 ? 589 HOH B O   1 
HETATM 9145 O  O   . HOH V 6 .   ? -10.583 -8.638  24.492  1.00 27.42 ? 590 HOH B O   1 
HETATM 9146 O  O   . HOH V 6 .   ? 2.833   0.323   63.346  1.00 29.58 ? 591 HOH B O   1 
HETATM 9147 O  O   . HOH V 6 .   ? -0.483  -21.290 36.881  1.00 34.90 ? 592 HOH B O   1 
HETATM 9148 O  O   . HOH V 6 .   ? -36.977 -2.401  38.837  1.00 38.92 ? 593 HOH B O   1 
HETATM 9149 O  O   . HOH V 6 .   ? 4.030   2.479   56.953  1.00 27.60 ? 594 HOH B O   1 
HETATM 9150 O  O   . HOH V 6 .   ? -18.955 -18.292 32.472  1.00 26.66 ? 595 HOH B O   1 
HETATM 9151 O  O   . HOH V 6 .   ? -33.236 3.446   36.444  1.00 23.99 ? 596 HOH B O   1 
HETATM 9152 O  O   . HOH V 6 .   ? -19.115 -1.916  62.313  1.00 29.02 ? 597 HOH B O   1 
HETATM 9153 O  O   . HOH V 6 .   ? -7.627  3.836   55.073  1.00 39.56 ? 598 HOH B O   1 
HETATM 9154 O  O   . HOH V 6 .   ? -4.639  16.037  33.058  1.00 27.15 ? 599 HOH B O   1 
HETATM 9155 O  O   . HOH V 6 .   ? -21.830 -0.361  22.406  1.00 33.74 ? 600 HOH B O   1 
HETATM 9156 O  O   . HOH V 6 .   ? -4.578  13.882  41.073  1.00 33.38 ? 601 HOH B O   1 
HETATM 9157 O  O   . HOH V 6 .   ? -14.008 8.316   20.919  1.00 28.71 ? 602 HOH B O   1 
HETATM 9158 O  O   . HOH V 6 .   ? -8.669  -8.445  26.318  1.00 33.85 ? 603 HOH B O   1 
HETATM 9159 O  O   . HOH V 6 .   ? 8.010   1.069   43.725  1.00 36.68 ? 604 HOH B O   1 
HETATM 9160 O  O   . HOH V 6 .   ? 4.480   -5.168  58.890  1.00 31.66 ? 605 HOH B O   1 
HETATM 9161 O  O   . HOH V 6 .   ? -18.854 -9.269  55.320  1.00 35.29 ? 606 HOH B O   1 
HETATM 9162 O  O   . HOH V 6 .   ? -24.192 10.383  25.235  1.00 28.11 ? 607 HOH B O   1 
HETATM 9163 O  O   . HOH V 6 .   ? -25.650 16.872  47.836  1.00 35.91 ? 608 HOH B O   1 
HETATM 9164 O  O   . HOH V 6 .   ? -36.280 -4.188  41.742  1.00 30.84 ? 609 HOH B O   1 
HETATM 9165 O  O   . HOH V 6 .   ? -1.383  11.348  42.112  1.00 27.41 ? 610 HOH B O   1 
HETATM 9166 O  O   . HOH V 6 .   ? -16.581 3.809   59.600  1.00 32.55 ? 611 HOH B O   1 
HETATM 9167 O  O   . HOH V 6 .   ? 0.809   12.831  43.090  1.00 29.59 ? 612 HOH B O   1 
HETATM 9168 O  O   . HOH V 6 .   ? -24.058 -1.470  19.731  1.00 38.15 ? 613 HOH B O   1 
HETATM 9169 O  O   . HOH V 6 .   ? -5.245  -17.563 46.364  1.00 31.97 ? 614 HOH B O   1 
HETATM 9170 O  O   . HOH V 6 .   ? -18.217 -6.994  66.183  1.00 32.81 ? 615 HOH B O   1 
HETATM 9171 O  O   . HOH V 6 .   ? -6.624  -1.549  57.986  1.00 33.03 ? 616 HOH B O   1 
HETATM 9172 O  O   . HOH V 6 .   ? -4.597  -3.402  62.052  1.00 38.52 ? 617 HOH B O   1 
HETATM 9173 O  O   . HOH V 6 .   ? -28.703 -17.235 37.206  1.00 30.98 ? 618 HOH B O   1 
HETATM 9174 O  O   . HOH V 6 .   ? -26.888 7.745   36.194  1.00 24.43 ? 619 HOH B O   1 
HETATM 9175 O  O   . HOH V 6 .   ? 2.281   -14.825 41.497  1.00 34.80 ? 620 HOH B O   1 
HETATM 9176 O  O   . HOH V 6 .   ? -27.066 1.538   21.329  1.00 32.57 ? 621 HOH B O   1 
HETATM 9177 O  O   . HOH V 6 .   ? -5.939  10.756  41.681  1.00 30.74 ? 622 HOH B O   1 
HETATM 9178 O  O   . HOH V 6 .   ? -12.012 2.838   57.270  1.00 32.05 ? 623 HOH B O   1 
HETATM 9179 O  O   . HOH V 6 .   ? -22.168 -9.236  53.212  1.00 35.02 ? 624 HOH B O   1 
HETATM 9180 O  O   . HOH V 6 .   ? -26.389 13.580  44.849  1.00 26.35 ? 625 HOH B O   1 
HETATM 9181 O  O   . HOH V 6 .   ? 6.692   -6.729  49.816  1.00 35.89 ? 626 HOH B O   1 
HETATM 9182 O  O   . HOH V 6 .   ? -12.881 -10.823 18.118  1.00 51.25 ? 627 HOH B O   1 
HETATM 9183 O  O   . HOH V 6 .   ? -25.295 18.008  31.712  1.00 33.08 ? 628 HOH B O   1 
HETATM 9184 O  O   . HOH V 6 .   ? -5.652  7.660   45.862  1.00 33.99 ? 629 HOH B O   1 
HETATM 9185 O  O   . HOH V 6 .   ? 5.236   -5.379  56.314  1.00 33.65 ? 630 HOH B O   1 
HETATM 9186 O  O   . HOH V 6 .   ? -14.691 -10.976 53.547  1.00 65.13 ? 631 HOH B O   1 
HETATM 9187 O  O   . HOH V 6 .   ? 4.334   -8.328  48.938  1.00 34.49 ? 632 HOH B O   1 
HETATM 9188 O  O   . HOH V 6 .   ? -2.101  21.094  35.482  1.00 21.68 ? 633 HOH B O   1 
HETATM 9189 O  O   . HOH V 6 .   ? 7.093   -10.443 37.665  1.00 23.52 ? 634 HOH B O   1 
HETATM 9190 O  O   . HOH V 6 .   ? -32.081 4.956   34.314  1.00 25.42 ? 635 HOH B O   1 
HETATM 9191 O  O   . HOH V 6 .   ? -21.035 1.556   60.239  1.00 25.17 ? 636 HOH B O   1 
HETATM 9192 O  O   . HOH V 6 .   ? -30.214 13.154  28.803  1.00 30.74 ? 637 HOH B O   1 
HETATM 9193 O  O   . HOH V 6 .   ? -21.000 22.465  42.753  1.00 25.38 ? 638 HOH B O   1 
HETATM 9194 O  O   . HOH V 6 .   ? -16.925 6.691   19.969  1.00 32.87 ? 639 HOH B O   1 
HETATM 9195 O  O   . HOH V 6 .   ? 0.970   -13.726 51.617  1.00 32.17 ? 640 HOH B O   1 
HETATM 9196 O  O   . HOH V 6 .   ? -18.277 0.693   20.565  1.00 23.69 ? 641 HOH B O   1 
HETATM 9197 O  O   . HOH V 6 .   ? -33.229 -11.256 42.421  1.00 27.39 ? 642 HOH B O   1 
HETATM 9198 O  O   . HOH V 6 .   ? -8.622  9.693   43.996  1.00 33.29 ? 643 HOH B O   1 
HETATM 9199 O  O   . HOH V 6 .   ? -23.333 16.154  26.013  1.00 34.77 ? 644 HOH B O   1 
HETATM 9200 O  O   . HOH V 6 .   ? -32.382 -13.088 41.179  1.00 31.67 ? 645 HOH B O   1 
HETATM 9201 O  O   . HOH V 6 .   ? -20.151 -8.722  63.744  1.00 38.17 ? 646 HOH B O   1 
HETATM 9202 O  O   . HOH V 6 .   ? -42.316 1.617   41.008  1.00 35.77 ? 647 HOH B O   1 
HETATM 9203 O  O   . HOH V 6 .   ? -34.146 -5.308  25.210  1.00 30.88 ? 648 HOH B O   1 
HETATM 9204 O  O   . HOH V 6 .   ? -8.535  -21.485 41.628  1.00 27.43 ? 649 HOH B O   1 
HETATM 9205 O  O   . HOH V 6 .   ? -33.503 4.261   27.400  1.00 33.90 ? 650 HOH B O   1 
HETATM 9206 O  O   . HOH V 6 .   ? -8.379  -10.319 22.808  1.00 34.10 ? 651 HOH B O   1 
HETATM 9207 O  O   . HOH V 6 .   ? -13.257 17.187  26.545  1.00 30.68 ? 652 HOH B O   1 
HETATM 9208 O  O   . HOH V 6 .   ? 4.534   2.577   33.695  1.00 37.62 ? 653 HOH B O   1 
HETATM 9209 O  O   . HOH V 6 .   ? -0.170  13.902  28.779  1.00 30.83 ? 654 HOH B O   1 
HETATM 9210 O  O   . HOH V 6 .   ? -4.670  -1.050  60.582  1.00 43.25 ? 655 HOH B O   1 
HETATM 9211 O  O   . HOH V 6 .   ? 6.698   -3.910  52.846  1.00 32.04 ? 656 HOH B O   1 
HETATM 9212 O  O   . HOH V 6 .   ? 7.073   -14.221 39.798  1.00 36.98 ? 657 HOH B O   1 
HETATM 9213 O  O   . HOH V 6 .   ? -11.679 16.912  30.443  1.00 26.10 ? 658 HOH B O   1 
HETATM 9214 O  O   . HOH V 6 .   ? -13.527 -4.704  63.159  1.00 29.76 ? 659 HOH B O   1 
HETATM 9215 O  O   . HOH V 6 .   ? -24.299 -12.184 29.003  1.00 41.17 ? 660 HOH B O   1 
HETATM 9216 O  O   . HOH V 6 .   ? -31.892 -12.366 26.257  1.00 34.34 ? 661 HOH B O   1 
HETATM 9217 O  O   . HOH V 6 .   ? 8.323   -3.041  43.052  1.00 34.18 ? 662 HOH B O   1 
HETATM 9218 O  O   . HOH V 6 .   ? -36.236 -0.224  21.479  1.00 43.32 ? 663 HOH B O   1 
HETATM 9219 O  O   . HOH V 6 .   ? -35.702 3.091   39.924  1.00 24.99 ? 664 HOH B O   1 
HETATM 9220 O  O   . HOH V 6 .   ? -8.476  8.518   21.900  1.00 50.14 ? 665 HOH B O   1 
HETATM 9221 O  O   . HOH W 6 .   ? 11.324  14.106  77.258  1.00 8.92  ? 401 HOH C O   1 
HETATM 9222 O  O   . HOH W 6 .   ? -5.002  28.196  76.868  1.00 16.15 ? 402 HOH C O   1 
HETATM 9223 O  O   . HOH W 6 .   ? 23.583  12.645  80.610  1.00 17.06 ? 403 HOH C O   1 
HETATM 9224 O  O   . HOH W 6 .   ? 13.123  8.997   64.674  1.00 9.31  ? 404 HOH C O   1 
HETATM 9225 O  O   . HOH W 6 .   ? 12.061  18.412  60.751  1.00 10.45 ? 405 HOH C O   1 
HETATM 9226 O  O   . HOH W 6 .   ? 12.970  15.320  82.587  1.00 13.25 ? 406 HOH C O   1 
HETATM 9227 O  O   . HOH W 6 .   ? 18.933  17.591  56.624  1.00 13.23 ? 407 HOH C O   1 
HETATM 9228 O  O   . HOH W 6 .   ? 18.383  31.184  72.748  1.00 10.56 ? 408 HOH C O   1 
HETATM 9229 O  O   . HOH W 6 .   ? 26.926  27.547  60.554  1.00 20.27 ? 409 HOH C O   1 
HETATM 9230 O  O   . HOH W 6 .   ? 18.694  5.629   75.465  1.00 15.42 ? 410 HOH C O   1 
HETATM 9231 O  O   . HOH W 6 .   ? 16.148  11.353  64.577  1.00 10.17 ? 411 HOH C O   1 
HETATM 9232 O  O   . HOH W 6 .   ? 25.815  20.940  62.830  1.00 13.50 ? 412 HOH C O   1 
HETATM 9233 O  O   . HOH W 6 .   ? 19.352  6.612   66.003  1.00 12.72 ? 413 HOH C O   1 
HETATM 9234 O  O   . HOH W 6 .   ? -0.703  2.092   74.195  1.00 13.74 ? 414 HOH C O   1 
HETATM 9235 O  O   . HOH W 6 .   ? 24.320  13.775  66.255  1.00 11.67 ? 415 HOH C O   1 
HETATM 9236 O  O   . HOH W 6 .   ? 5.681   7.061   65.751  1.00 10.17 ? 416 HOH C O   1 
HETATM 9237 O  O   . HOH W 6 .   ? -6.983  21.361  52.863  1.00 17.71 ? 417 HOH C O   1 
HETATM 9238 O  O   . HOH W 6 .   ? 15.463  3.136   69.298  1.00 15.43 ? 418 HOH C O   1 
HETATM 9239 O  O   . HOH W 6 .   ? 20.235  9.216   65.841  1.00 11.95 ? 419 HOH C O   1 
HETATM 9240 O  O   . HOH W 6 .   ? -1.947  14.749  81.165  1.00 16.10 ? 420 HOH C O   1 
HETATM 9241 O  O   . HOH W 6 .   ? 15.406  10.156  77.635  1.00 14.40 ? 421 HOH C O   1 
HETATM 9242 O  O   . HOH W 6 .   ? 21.680  10.681  61.400  1.00 21.62 ? 422 HOH C O   1 
HETATM 9243 O  O   . HOH W 6 .   ? 19.080  36.595  76.219  1.00 21.63 ? 423 HOH C O   1 
HETATM 9244 O  O   . HOH W 6 .   ? 8.749   13.858  47.314  1.00 32.62 ? 424 HOH C O   1 
HETATM 9245 O  O   . HOH W 6 .   ? 7.431   42.480  72.406  1.00 16.29 ? 425 HOH C O   1 
HETATM 9246 O  O   . HOH W 6 .   ? 3.322   10.575  80.951  1.00 20.42 ? 426 HOH C O   1 
HETATM 9247 O  O   . HOH W 6 .   ? 4.886   0.310   65.294  1.00 16.38 ? 427 HOH C O   1 
HETATM 9248 O  O   . HOH W 6 .   ? 9.365   5.288   72.173  1.00 13.41 ? 428 HOH C O   1 
HETATM 9249 O  O   . HOH W 6 .   ? 19.630  32.878  76.520  1.00 17.38 ? 429 HOH C O   1 
HETATM 9250 O  O   . HOH W 6 .   ? 10.365  4.249   69.899  1.00 13.01 ? 430 HOH C O   1 
HETATM 9251 O  O   . HOH W 6 .   ? -6.109  5.878   74.505  1.00 22.88 ? 431 HOH C O   1 
HETATM 9252 O  O   . HOH W 6 .   ? 20.212  18.659  53.183  1.00 13.89 ? 432 HOH C O   1 
HETATM 9253 O  O   . HOH W 6 .   ? 18.472  10.168  63.877  1.00 10.27 ? 433 HOH C O   1 
HETATM 9254 O  O   . HOH W 6 .   ? 5.851   37.580  68.122  1.00 18.25 ? 434 HOH C O   1 
HETATM 9255 O  O   . HOH W 6 .   ? -10.573 17.916  58.441  1.00 20.02 ? 435 HOH C O   1 
HETATM 9256 O  O   . HOH W 6 .   ? 24.001  19.119  59.014  1.00 19.35 ? 436 HOH C O   1 
HETATM 9257 O  O   . HOH W 6 .   ? 3.294   4.183   79.995  1.00 22.30 ? 437 HOH C O   1 
HETATM 9258 O  O   . HOH W 6 .   ? 26.700  14.553  74.499  1.00 23.44 ? 438 HOH C O   1 
HETATM 9259 O  O   . HOH W 6 .   ? 16.554  33.312  82.335  1.00 18.67 ? 439 HOH C O   1 
HETATM 9260 O  O   . HOH W 6 .   ? 17.171  8.534   79.015  1.00 19.99 ? 440 HOH C O   1 
HETATM 9261 O  O   . HOH W 6 .   ? 17.341  25.942  44.470  1.00 27.74 ? 441 HOH C O   1 
HETATM 9262 O  O   . HOH W 6 .   ? 8.962   31.099  83.912  1.00 20.33 ? 442 HOH C O   1 
HETATM 9263 O  O   . HOH W 6 .   ? 30.237  18.103  86.720  1.00 33.92 ? 443 HOH C O   1 
HETATM 9264 O  O   . HOH W 6 .   ? 20.594  6.017   77.433  1.00 24.61 ? 444 HOH C O   1 
HETATM 9265 O  O   . HOH W 6 .   ? 10.555  3.894   74.484  1.00 15.29 ? 445 HOH C O   1 
HETATM 9266 O  O   . HOH W 6 .   ? 2.389   36.041  67.270  1.00 26.06 ? 446 HOH C O   1 
HETATM 9267 O  O   . HOH W 6 .   ? -6.418  21.746  78.501  1.00 21.48 ? 447 HOH C O   1 
HETATM 9268 O  O   . HOH W 6 .   ? -11.441 23.148  60.626  1.00 24.93 ? 448 HOH C O   1 
HETATM 9269 O  O   . HOH W 6 .   ? 29.134  6.896   74.233  1.00 29.19 ? 449 HOH C O   1 
HETATM 9270 O  O   . HOH W 6 .   ? 14.861  38.443  77.403  1.00 19.26 ? 450 HOH C O   1 
HETATM 9271 O  O   . HOH W 6 .   ? -7.433  30.417  75.220  1.00 16.70 ? 451 HOH C O   1 
HETATM 9272 O  O   . HOH W 6 .   ? -3.479  5.689   61.867  1.00 20.14 ? 452 HOH C O   1 
HETATM 9273 O  O   . HOH W 6 .   ? 2.443   33.274  75.270  1.00 16.61 ? 453 HOH C O   1 
HETATM 9274 O  O   . HOH W 6 .   ? 0.659   9.094   80.270  1.00 18.33 ? 454 HOH C O   1 
HETATM 9275 O  O   . HOH W 6 .   ? -9.955  25.625  57.821  1.00 28.16 ? 455 HOH C O   1 
HETATM 9276 O  O   . HOH W 6 .   ? 2.195   18.670  65.287  1.00 13.33 ? 456 HOH C O   1 
HETATM 9277 O  O   . HOH W 6 .   ? -7.349  16.625  77.100  1.00 18.67 ? 457 HOH C O   1 
HETATM 9278 O  O   . HOH W 6 .   ? 28.665  16.699  74.760  1.00 20.73 ? 458 HOH C O   1 
HETATM 9279 O  O   . HOH W 6 .   ? 1.732   32.009  82.664  1.00 33.09 ? 459 HOH C O   1 
HETATM 9280 O  O   . HOH W 6 .   ? 21.093  5.085   64.542  1.00 26.21 ? 460 HOH C O   1 
HETATM 9281 O  O   . HOH W 6 .   ? 14.984  21.814  85.867  1.00 22.85 ? 461 HOH C O   1 
HETATM 9282 O  O   . HOH W 6 .   ? 22.371  15.412  50.920  1.00 29.36 ? 462 HOH C O   1 
HETATM 9283 O  O   . HOH W 6 .   ? 9.456   42.490  74.408  1.00 18.48 ? 463 HOH C O   1 
HETATM 9284 O  O   . HOH W 6 .   ? 26.078  13.928  71.986  1.00 15.84 ? 464 HOH C O   1 
HETATM 9285 O  O   . HOH W 6 .   ? -0.248  32.602  75.748  1.00 14.58 ? 465 HOH C O   1 
HETATM 9286 O  O   . HOH W 6 .   ? 4.990   0.666   73.384  1.00 16.61 ? 466 HOH C O   1 
HETATM 9287 O  O   . HOH W 6 .   ? 11.071  4.403   77.144  1.00 24.53 ? 467 HOH C O   1 
HETATM 9288 O  O   . HOH W 6 .   ? 22.837  25.357  75.684  1.00 19.72 ? 468 HOH C O   1 
HETATM 9289 O  O   . HOH W 6 .   ? 18.443  8.142   61.880  1.00 20.18 ? 469 HOH C O   1 
HETATM 9290 O  O   . HOH W 6 .   ? 26.310  7.432   75.972  1.00 31.95 ? 470 HOH C O   1 
HETATM 9291 O  O   . HOH W 6 .   ? -10.929 18.818  71.158  1.00 21.42 ? 471 HOH C O   1 
HETATM 9292 O  O   . HOH W 6 .   ? 25.683  13.918  68.618  1.00 20.78 ? 472 HOH C O   1 
HETATM 9293 O  O   . HOH W 6 .   ? 26.402  10.548  69.372  1.00 21.80 ? 473 HOH C O   1 
HETATM 9294 O  O   . HOH W 6 .   ? 14.644  28.756  87.740  1.00 30.37 ? 474 HOH C O   1 
HETATM 9295 O  O   . HOH W 6 .   ? 7.349   11.092  55.180  1.00 19.85 ? 475 HOH C O   1 
HETATM 9296 O  O   . HOH W 6 .   ? 18.463  29.613  55.885  1.00 18.23 ? 476 HOH C O   1 
HETATM 9297 O  O   . HOH W 6 .   ? 5.757   18.205  54.336  1.00 21.72 ? 477 HOH C O   1 
HETATM 9298 O  O   . HOH W 6 .   ? 3.840   -0.402  71.251  1.00 31.69 ? 478 HOH C O   1 
HETATM 9299 O  O   . HOH W 6 .   ? 5.370   7.634   81.331  1.00 33.17 ? 479 HOH C O   1 
HETATM 9300 O  O   . HOH W 6 .   ? 7.049   4.029   71.937  1.00 14.79 ? 480 HOH C O   1 
HETATM 9301 O  O   . HOH W 6 .   ? -10.566 28.017  58.642  1.00 51.36 ? 481 HOH C O   1 
HETATM 9302 O  O   . HOH W 6 .   ? 25.277  7.530   71.074  1.00 23.69 ? 482 HOH C O   1 
HETATM 9303 O  O   . HOH W 6 .   ? 4.403   1.950   79.443  1.00 30.67 ? 483 HOH C O   1 
HETATM 9304 O  O   . HOH W 6 .   ? 19.515  33.373  62.480  1.00 18.44 ? 484 HOH C O   1 
HETATM 9305 O  O   . HOH W 6 .   ? 20.533  28.588  54.237  1.00 18.16 ? 485 HOH C O   1 
HETATM 9306 O  O   . HOH W 6 .   ? 14.141  15.846  43.902  1.00 34.76 ? 486 HOH C O   1 
HETATM 9307 O  O   . HOH W 6 .   ? 25.795  23.785  52.283  1.00 22.69 ? 487 HOH C O   1 
HETATM 9308 O  O   . HOH W 6 .   ? 14.294  31.509  86.635  1.00 39.56 ? 488 HOH C O   1 
HETATM 9309 O  O   . HOH W 6 .   ? 7.055   6.929   55.667  1.00 22.59 ? 489 HOH C O   1 
HETATM 9310 O  O   . HOH W 6 .   ? -3.562  19.487  78.754  1.00 21.11 ? 490 HOH C O   1 
HETATM 9311 O  O   . HOH W 6 .   ? 16.009  12.149  45.048  1.00 36.64 ? 491 HOH C O   1 
HETATM 9312 O  O   . HOH W 6 .   ? 0.689   3.009   67.412  1.00 23.79 ? 492 HOH C O   1 
HETATM 9313 O  O   . HOH W 6 .   ? 23.747  4.131   76.910  1.00 28.87 ? 493 HOH C O   1 
HETATM 9314 O  O   . HOH W 6 .   ? 24.991  22.703  49.767  1.00 20.56 ? 494 HOH C O   1 
HETATM 9315 O  O   . HOH W 6 .   ? 18.124  2.773   68.079  1.00 19.49 ? 495 HOH C O   1 
HETATM 9316 O  O   . HOH W 6 .   ? 21.527  34.012  64.126  1.00 28.59 ? 496 HOH C O   1 
HETATM 9317 O  O   . HOH W 6 .   ? 13.053  3.047   71.088  1.00 17.75 ? 497 HOH C O   1 
HETATM 9318 O  O   . HOH W 6 .   ? -9.902  15.420  77.628  1.00 29.17 ? 498 HOH C O   1 
HETATM 9319 O  O   . HOH W 6 .   ? 21.227  34.989  75.551  1.00 21.67 ? 499 HOH C O   1 
HETATM 9320 O  O   . HOH W 6 .   ? -8.709  12.890  78.720  1.00 22.15 ? 500 HOH C O   1 
HETATM 9321 O  O   . HOH W 6 .   ? 31.422  24.523  71.465  1.00 30.16 ? 501 HOH C O   1 
HETATM 9322 O  O   . HOH W 6 .   ? 14.297  4.940   61.266  1.00 26.78 ? 502 HOH C O   1 
HETATM 9323 O  O   . HOH W 6 .   ? -9.533  31.476  68.639  1.00 21.55 ? 503 HOH C O   1 
HETATM 9324 O  O   . HOH W 6 .   ? 23.559  7.764   80.935  1.00 34.20 ? 504 HOH C O   1 
HETATM 9325 O  O   . HOH W 6 .   ? 20.770  10.583  58.023  1.00 37.75 ? 505 HOH C O   1 
HETATM 9326 O  O   . HOH W 6 .   ? 24.546  11.319  64.928  1.00 18.23 ? 506 HOH C O   1 
HETATM 9327 O  O   . HOH W 6 .   ? 2.087   4.003   82.325  1.00 36.72 ? 507 HOH C O   1 
HETATM 9328 O  O   . HOH W 6 .   ? 2.655   20.094  84.499  1.00 15.52 ? 508 HOH C O   1 
HETATM 9329 O  O   . HOH W 6 .   ? 13.830  2.326   67.235  1.00 14.30 ? 509 HOH C O   1 
HETATM 9330 O  O   . HOH W 6 .   ? 16.131  19.976  44.573  1.00 22.38 ? 510 HOH C O   1 
HETATM 9331 O  O   . HOH W 6 .   ? 27.928  12.211  81.059  1.00 20.31 ? 511 HOH C O   1 
HETATM 9332 O  O   . HOH W 6 .   ? 6.158   15.885  52.964  1.00 21.66 ? 512 HOH C O   1 
HETATM 9333 O  O   . HOH W 6 .   ? 5.527   40.255  69.254  1.00 16.66 ? 513 HOH C O   1 
HETATM 9334 O  O   . HOH W 6 .   ? 13.079  18.595  88.026  1.00 19.72 ? 514 HOH C O   1 
HETATM 9335 O  O   . HOH W 6 .   ? 24.910  16.664  50.168  1.00 24.33 ? 515 HOH C O   1 
HETATM 9336 O  O   . HOH W 6 .   ? 28.115  13.929  65.637  1.00 25.33 ? 516 HOH C O   1 
HETATM 9337 O  O   . HOH W 6 .   ? -9.837  17.799  54.068  1.00 25.69 ? 517 HOH C O   1 
HETATM 9338 O  O   . HOH W 6 .   ? 22.660  9.389   64.518  1.00 22.68 ? 518 HOH C O   1 
HETATM 9339 O  O   . HOH W 6 .   ? 18.254  44.155  75.174  1.00 22.55 ? 519 HOH C O   1 
HETATM 9340 O  O   . HOH W 6 .   ? -15.365 27.796  67.361  1.00 25.01 ? 520 HOH C O   1 
HETATM 9341 O  O   . HOH W 6 .   ? 1.461   0.294   69.762  1.00 20.50 ? 521 HOH C O   1 
HETATM 9342 O  O   . HOH W 6 .   ? -3.580  1.671   74.401  1.00 26.68 ? 522 HOH C O   1 
HETATM 9343 O  O   . HOH W 6 .   ? -9.514  17.973  43.263  1.00 26.86 ? 523 HOH C O   1 
HETATM 9344 O  O   . HOH W 6 .   ? -9.694  13.582  65.782  1.00 22.40 ? 524 HOH C O   1 
HETATM 9345 O  O   . HOH W 6 .   ? 20.907  31.352  61.053  1.00 19.73 ? 525 HOH C O   1 
HETATM 9346 O  O   . HOH W 6 .   ? 30.605  16.144  64.204  1.00 23.50 ? 526 HOH C O   1 
HETATM 9347 O  O   . HOH W 6 .   ? 9.232   25.318  86.248  1.00 25.04 ? 527 HOH C O   1 
HETATM 9348 O  O   . HOH W 6 .   ? 24.429  13.469  83.237  1.00 24.89 ? 528 HOH C O   1 
HETATM 9349 O  O   . HOH W 6 .   ? 1.494   16.039  83.268  1.00 23.25 ? 529 HOH C O   1 
HETATM 9350 O  O   . HOH W 6 .   ? 6.299   11.405  82.313  1.00 21.89 ? 530 HOH C O   1 
HETATM 9351 O  O   . HOH W 6 .   ? -7.203  13.740  60.779  1.00 25.89 ? 531 HOH C O   1 
HETATM 9352 O  O   . HOH W 6 .   ? 30.823  17.168  72.913  1.00 20.37 ? 532 HOH C O   1 
HETATM 9353 O  O   . HOH W 6 .   ? 26.776  10.632  66.670  1.00 29.86 ? 533 HOH C O   1 
HETATM 9354 O  O   . HOH W 6 .   ? 27.032  21.239  48.605  1.00 19.53 ? 534 HOH C O   1 
HETATM 9355 O  O   . HOH W 6 .   ? -6.410  9.549   57.161  1.00 26.66 ? 535 HOH C O   1 
HETATM 9356 O  O   . HOH W 6 .   ? 30.275  23.635  65.394  1.00 22.51 ? 536 HOH C O   1 
HETATM 9357 O  O   . HOH W 6 .   ? 3.401   9.249   53.928  1.00 21.58 ? 537 HOH C O   1 
HETATM 9358 O  O   . HOH W 6 .   ? -6.694  12.335  63.006  1.00 22.02 ? 538 HOH C O   1 
HETATM 9359 O  O   . HOH W 6 .   ? 17.798  43.317  72.640  1.00 20.09 ? 539 HOH C O   1 
HETATM 9360 O  O   . HOH W 6 .   ? -3.255  6.544   59.173  1.00 24.34 ? 540 HOH C O   1 
HETATM 9361 O  O   . HOH W 6 .   ? 8.494   42.396  77.004  1.00 22.81 ? 541 HOH C O   1 
HETATM 9362 O  O   . HOH W 6 .   ? 26.299  20.061  59.728  1.00 25.26 ? 542 HOH C O   1 
HETATM 9363 O  O   . HOH W 6 .   ? 20.728  30.404  75.890  1.00 21.51 ? 543 HOH C O   1 
HETATM 9364 O  O   . HOH W 6 .   ? 22.302  38.313  73.323  1.00 24.58 ? 544 HOH C O   1 
HETATM 9365 O  O   . HOH W 6 .   ? 5.624   1.453   76.971  1.00 21.11 ? 545 HOH C O   1 
HETATM 9366 O  O   . HOH W 6 .   ? -12.995 26.169  64.311  1.00 29.74 ? 546 HOH C O   1 
HETATM 9367 O  O   . HOH W 6 .   ? 22.407  25.491  46.627  1.00 29.24 ? 547 HOH C O   1 
HETATM 9368 O  O   . HOH W 6 .   ? -8.659  23.139  51.872  1.00 26.05 ? 548 HOH C O   1 
HETATM 9369 O  O   . HOH W 6 .   ? 23.573  35.538  76.893  1.00 27.90 ? 549 HOH C O   1 
HETATM 9370 O  O   . HOH W 6 .   ? 16.477  22.659  45.511  1.00 29.78 ? 550 HOH C O   1 
HETATM 9371 O  O   . HOH W 6 .   ? 22.707  17.882  53.965  1.00 25.72 ? 551 HOH C O   1 
HETATM 9372 O  O   . HOH W 6 .   ? 19.745  35.057  60.124  1.00 27.12 ? 552 HOH C O   1 
HETATM 9373 O  O   . HOH W 6 .   ? 25.585  33.808  80.048  1.00 32.33 ? 553 HOH C O   1 
HETATM 9374 O  O   . HOH W 6 .   ? 20.423  15.245  56.779  1.00 24.41 ? 554 HOH C O   1 
HETATM 9375 O  O   . HOH W 6 .   ? 27.987  28.571  84.239  1.00 42.47 ? 555 HOH C O   1 
HETATM 9376 O  O   . HOH W 6 .   ? -6.859  17.512  42.780  1.00 22.41 ? 556 HOH C O   1 
HETATM 9377 O  O   . HOH W 6 .   ? 13.562  28.275  48.828  1.00 37.98 ? 557 HOH C O   1 
HETATM 9378 O  O   . HOH W 6 .   ? 6.965   38.310  64.034  1.00 27.07 ? 558 HOH C O   1 
HETATM 9379 O  O   . HOH W 6 .   ? 20.019  28.263  47.404  1.00 31.65 ? 559 HOH C O   1 
HETATM 9380 O  O   . HOH W 6 .   ? -0.409  14.820  47.251  1.00 27.17 ? 560 HOH C O   1 
HETATM 9381 O  O   . HOH W 6 .   ? -11.329 13.972  59.039  1.00 39.81 ? 561 HOH C O   1 
HETATM 9382 O  O   . HOH W 6 .   ? 19.704  30.893  83.581  1.00 30.89 ? 562 HOH C O   1 
HETATM 9383 O  O   . HOH W 6 .   ? 23.234  6.768   63.526  1.00 33.89 ? 563 HOH C O   1 
HETATM 9384 O  O   . HOH W 6 .   ? 23.468  31.902  64.284  1.00 25.45 ? 564 HOH C O   1 
HETATM 9385 O  O   . HOH W 6 .   ? -11.738 25.943  71.618  1.00 31.66 ? 565 HOH C O   1 
HETATM 9386 O  O   . HOH W 6 .   ? 13.881  11.468  53.443  1.00 35.89 ? 566 HOH C O   1 
HETATM 9387 O  O   . HOH W 6 .   ? -9.218  29.102  62.726  1.00 46.71 ? 567 HOH C O   1 
HETATM 9388 O  O   . HOH W 6 .   ? 17.898  14.673  89.137  1.00 33.26 ? 568 HOH C O   1 
HETATM 9389 O  O   . HOH W 6 .   ? -0.104  28.008  88.563  1.00 36.86 ? 569 HOH C O   1 
HETATM 9390 O  O   . HOH W 6 .   ? 18.523  36.544  83.006  1.00 38.40 ? 570 HOH C O   1 
HETATM 9391 O  O   . HOH W 6 .   ? 8.040   2.893   57.842  1.00 32.76 ? 571 HOH C O   1 
HETATM 9392 O  O   . HOH W 6 .   ? -3.957  4.776   79.589  1.00 33.61 ? 572 HOH C O   1 
HETATM 9393 O  O   . HOH W 6 .   ? -0.656  33.730  67.842  1.00 33.03 ? 573 HOH C O   1 
HETATM 9394 O  O   . HOH W 6 .   ? -2.575  27.350  80.632  1.00 38.75 ? 574 HOH C O   1 
HETATM 9395 O  O   . HOH W 6 .   ? 29.370  15.129  83.741  1.00 30.70 ? 575 HOH C O   1 
HETATM 9396 O  O   . HOH W 6 .   ? -9.083  22.455  77.810  1.00 28.97 ? 576 HOH C O   1 
HETATM 9397 O  O   . HOH W 6 .   ? -4.107  -0.522  72.150  1.00 36.36 ? 577 HOH C O   1 
HETATM 9398 O  O   . HOH W 6 .   ? -6.998  5.906   67.307  1.00 35.86 ? 578 HOH C O   1 
HETATM 9399 O  O   . HOH W 6 .   ? 1.842   19.103  50.941  1.00 35.16 ? 579 HOH C O   1 
HETATM 9400 O  O   . HOH W 6 .   ? 33.498  19.085  79.543  1.00 32.30 ? 580 HOH C O   1 
HETATM 9401 O  O   . HOH W 6 .   ? 14.191  2.318   76.359  1.00 27.00 ? 581 HOH C O   1 
HETATM 9402 O  O   . HOH W 6 .   ? -11.202 15.654  73.682  1.00 32.45 ? 582 HOH C O   1 
HETATM 9403 O  O   . HOH W 6 .   ? 6.043   11.900  84.443  1.00 25.45 ? 583 HOH C O   1 
HETATM 9404 O  O   . HOH W 6 .   ? 28.342  8.888   70.655  1.00 30.54 ? 584 HOH C O   1 
HETATM 9405 O  O   . HOH W 6 .   ? 14.561  18.732  46.597  1.00 29.00 ? 585 HOH C O   1 
HETATM 9406 O  O   . HOH W 6 .   ? 5.770   19.484  51.228  1.00 33.61 ? 586 HOH C O   1 
HETATM 9407 O  O   . HOH W 6 .   ? 8.282   8.366   81.302  1.00 30.37 ? 587 HOH C O   1 
HETATM 9408 O  O   . HOH W 6 .   ? 11.631  1.734   59.743  1.00 43.77 ? 588 HOH C O   1 
HETATM 9409 O  O   . HOH W 6 .   ? 8.212   9.941   90.942  1.00 40.48 ? 589 HOH C O   1 
HETATM 9410 O  O   . HOH W 6 .   ? 9.121   28.834  87.944  1.00 30.77 ? 590 HOH C O   1 
HETATM 9411 O  O   . HOH W 6 .   ? 19.272  19.115  89.049  1.00 36.78 ? 591 HOH C O   1 
HETATM 9412 O  O   . HOH W 6 .   ? -5.381  10.046  46.952  1.00 38.85 ? 592 HOH C O   1 
HETATM 9413 O  O   . HOH W 6 .   ? -3.071  2.898   76.780  1.00 29.36 ? 593 HOH C O   1 
HETATM 9414 O  O   . HOH W 6 .   ? -9.453  15.543  49.836  1.00 32.47 ? 594 HOH C O   1 
HETATM 9415 O  O   . HOH W 6 .   ? 8.260   37.733  82.364  1.00 35.48 ? 595 HOH C O   1 
HETATM 9416 O  O   . HOH W 6 .   ? 26.023  7.121   73.272  1.00 26.44 ? 596 HOH C O   1 
HETATM 9417 O  O   . HOH W 6 .   ? -1.660  36.321  67.523  1.00 30.11 ? 597 HOH C O   1 
HETATM 9418 O  O   . HOH W 6 .   ? 20.918  37.453  61.230  1.00 30.30 ? 598 HOH C O   1 
HETATM 9419 O  O   . HOH W 6 .   ? 12.789  36.682  60.054  1.00 28.73 ? 599 HOH C O   1 
HETATM 9420 O  O   . HOH W 6 .   ? -12.676 21.694  65.274  1.00 30.98 ? 600 HOH C O   1 
HETATM 9421 O  O   . HOH W 6 .   ? 26.340  25.653  55.592  1.00 30.54 ? 601 HOH C O   1 
HETATM 9422 O  O   . HOH W 6 .   ? 17.747  19.008  86.841  1.00 30.20 ? 602 HOH C O   1 
HETATM 9423 O  O   . HOH W 6 .   ? 17.247  3.420   63.749  1.00 26.63 ? 603 HOH C O   1 
HETATM 9424 O  O   . HOH W 6 .   ? 25.688  23.549  75.663  1.00 29.07 ? 604 HOH C O   1 
HETATM 9425 O  O   . HOH W 6 .   ? -13.478 23.538  63.028  1.00 30.21 ? 605 HOH C O   1 
HETATM 9426 O  O   . HOH W 6 .   ? 12.298  24.374  49.304  1.00 30.21 ? 606 HOH C O   1 
HETATM 9427 O  O   . HOH W 6 .   ? 20.411  38.706  77.183  1.00 31.98 ? 607 HOH C O   1 
HETATM 9428 O  O   . HOH W 6 .   ? 25.904  19.066  92.432  1.00 37.76 ? 608 HOH C O   1 
HETATM 9429 O  O   . HOH W 6 .   ? 34.041  19.738  86.512  1.00 39.28 ? 609 HOH C O   1 
HETATM 9430 O  O   . HOH W 6 .   ? -4.507  5.006   54.882  1.00 37.25 ? 610 HOH C O   1 
HETATM 9431 O  O   . HOH W 6 .   ? -2.323  7.996   51.928  1.00 33.63 ? 611 HOH C O   1 
HETATM 9432 O  O   . HOH W 6 .   ? -11.751 10.123  71.346  1.00 26.08 ? 612 HOH C O   1 
HETATM 9433 O  O   . HOH W 6 .   ? -3.426  31.955  66.859  1.00 27.14 ? 613 HOH C O   1 
HETATM 9434 O  O   . HOH W 6 .   ? -4.564  34.478  80.001  1.00 28.84 ? 614 HOH C O   1 
HETATM 9435 O  O   . HOH W 6 .   ? 16.455  22.103  48.607  1.00 25.63 ? 615 HOH C O   1 
HETATM 9436 O  O   . HOH W 6 .   ? 3.565   28.815  86.772  1.00 54.69 ? 616 HOH C O   1 
HETATM 9437 O  O   . HOH W 6 .   ? 7.317   23.445  51.678  1.00 28.42 ? 617 HOH C O   1 
HETATM 9438 O  O   . HOH W 6 .   ? 14.934  4.755   78.155  1.00 30.57 ? 618 HOH C O   1 
HETATM 9439 O  O   . HOH W 6 .   ? 9.305   38.470  79.552  1.00 29.18 ? 619 HOH C O   1 
HETATM 9440 O  O   . HOH W 6 .   ? 4.626   33.685  82.851  1.00 43.55 ? 620 HOH C O   1 
HETATM 9441 O  O   . HOH W 6 .   ? 32.278  24.684  64.307  1.00 39.87 ? 621 HOH C O   1 
HETATM 9442 O  O   . HOH W 6 .   ? -9.741  15.288  52.356  1.00 35.07 ? 622 HOH C O   1 
HETATM 9443 O  O   . HOH W 6 .   ? 8.166   33.640  84.786  1.00 30.09 ? 623 HOH C O   1 
HETATM 9444 O  O   . HOH W 6 .   ? 16.803  6.010   77.548  1.00 28.70 ? 624 HOH C O   1 
HETATM 9445 O  O   . HOH W 6 .   ? 31.030  23.721  68.950  1.00 22.59 ? 625 HOH C O   1 
HETATM 9446 O  O   . HOH W 6 .   ? -9.086  12.356  59.885  1.00 30.45 ? 626 HOH C O   1 
HETATM 9447 O  O   . HOH W 6 .   ? 27.920  12.844  70.158  1.00 28.13 ? 627 HOH C O   1 
HETATM 9448 O  O   . HOH W 6 .   ? 3.860   10.446  85.968  1.00 30.44 ? 628 HOH C O   1 
HETATM 9449 O  O   . HOH W 6 .   ? 31.874  17.832  70.420  1.00 37.84 ? 629 HOH C O   1 
HETATM 9450 O  O   . HOH W 6 .   ? 22.416  21.920  87.510  1.00 39.09 ? 630 HOH C O   1 
HETATM 9451 O  O   . HOH W 6 .   ? 21.534  39.925  68.886  1.00 31.40 ? 631 HOH C O   1 
HETATM 9452 O  O   . HOH W 6 .   ? 5.903   16.545  50.431  1.00 29.25 ? 632 HOH C O   1 
HETATM 9453 O  O   . HOH W 6 .   ? 3.868   -0.868  67.322  1.00 24.78 ? 633 HOH C O   1 
HETATM 9454 O  O   . HOH W 6 .   ? 31.692  15.970  84.669  1.00 36.72 ? 634 HOH C O   1 
HETATM 9455 O  O   . HOH W 6 .   ? -12.551 14.099  66.602  1.00 34.29 ? 635 HOH C O   1 
HETATM 9456 O  O   . HOH W 6 .   ? 8.296   40.342  78.679  1.00 37.69 ? 636 HOH C O   1 
HETATM 9457 O  O   . HOH W 6 .   ? 0.591   3.052   62.387  1.00 32.84 ? 637 HOH C O   1 
HETATM 9458 O  O   . HOH W 6 .   ? -3.662  6.340   52.500  1.00 32.91 ? 638 HOH C O   1 
HETATM 9459 O  O   . HOH W 6 .   ? 10.415  8.829   55.334  1.00 33.25 ? 639 HOH C O   1 
HETATM 9460 O  O   . HOH W 6 .   ? 12.829  6.306   78.149  1.00 20.27 ? 640 HOH C O   1 
HETATM 9461 O  O   . HOH W 6 .   ? 16.511  40.807  64.530  1.00 32.30 ? 641 HOH C O   1 
HETATM 9462 O  O   . HOH W 6 .   ? 6.991   37.565  78.490  1.00 29.00 ? 642 HOH C O   1 
HETATM 9463 O  O   . HOH W 6 .   ? 2.861   11.615  89.667  1.00 20.94 ? 643 HOH C O   1 
HETATM 9464 O  O   . HOH W 6 .   ? 9.657   15.575  42.847  1.00 38.02 ? 644 HOH C O   1 
HETATM 9465 O  O   . HOH W 6 .   ? 27.287  8.272   82.641  1.00 33.27 ? 645 HOH C O   1 
HETATM 9466 O  O   . HOH W 6 .   ? 29.084  21.101  50.554  1.00 31.76 ? 646 HOH C O   1 
HETATM 9467 O  O   . HOH W 6 .   ? 28.471  23.114  52.589  1.00 33.06 ? 647 HOH C O   1 
HETATM 9468 O  O   . HOH W 6 .   ? -7.634  20.819  45.540  1.00 30.10 ? 648 HOH C O   1 
HETATM 9469 O  O   . HOH W 6 .   ? 0.008   25.649  53.839  1.00 32.43 ? 649 HOH C O   1 
HETATM 9470 O  O   . HOH W 6 .   ? 28.583  24.057  72.411  1.00 23.45 ? 650 HOH C O   1 
HETATM 9471 O  O   . HOH W 6 .   ? -4.832  30.555  80.921  1.00 37.72 ? 651 HOH C O   1 
HETATM 9472 O  O   . HOH W 6 .   ? -6.474  34.400  82.839  1.00 34.68 ? 652 HOH C O   1 
HETATM 9473 O  O   . HOH W 6 .   ? 12.238  27.361  88.905  1.00 38.49 ? 653 HOH C O   1 
HETATM 9474 O  O   . HOH X 6 .   ? 25.070  14.078  37.504  1.00 9.12  ? 401 HOH D O   1 
HETATM 9475 O  O   . HOH X 6 .   ? 8.815   28.244  36.422  1.00 16.11 ? 402 HOH D O   1 
HETATM 9476 O  O   . HOH X 6 .   ? 37.144  12.579  41.194  1.00 17.68 ? 403 HOH D O   1 
HETATM 9477 O  O   . HOH X 6 .   ? 27.127  8.888   24.985  1.00 10.65 ? 404 HOH D O   1 
HETATM 9478 O  O   . HOH X 6 .   ? 26.169  18.342  21.042  1.00 10.51 ? 405 HOH D O   1 
HETATM 9479 O  O   . HOH X 6 .   ? 26.478  15.344  42.900  1.00 12.94 ? 406 HOH D O   1 
HETATM 9480 O  O   . HOH X 6 .   ? 33.296  17.501  17.128  1.00 13.89 ? 407 HOH D O   1 
HETATM 9481 O  O   . HOH X 6 .   ? 32.253  31.128  33.179  1.00 10.59 ? 408 HOH D O   1 
HETATM 9482 O  O   . HOH X 6 .   ? 41.171  27.337  21.374  1.00 22.59 ? 409 HOH D O   1 
HETATM 9483 O  O   . HOH X 6 .   ? 32.329  5.576   35.948  1.00 16.11 ? 410 HOH D O   1 
HETATM 9484 O  O   . HOH X 6 .   ? 30.194  11.225  25.007  1.00 10.73 ? 411 HOH D O   1 
HETATM 9485 O  O   . HOH X 6 .   ? 39.916  20.822  23.434  1.00 14.00 ? 412 HOH D O   1 
HETATM 9486 O  O   . HOH X 6 .   ? 33.363  6.488   26.482  1.00 14.40 ? 413 HOH D O   1 
HETATM 9487 O  O   . HOH X 6 .   ? 13.095  2.072   34.268  1.00 16.25 ? 414 HOH D O   1 
HETATM 9488 O  O   . HOH X 6 .   ? 38.286  13.708  26.874  1.00 12.42 ? 415 HOH D O   1 
HETATM 9489 O  O   . HOH X 6 .   ? 19.677  6.948   25.927  1.00 10.89 ? 416 HOH D O   1 
HETATM 9490 O  O   . HOH X 6 .   ? 7.506   20.930  12.354  1.00 20.59 ? 417 HOH D O   1 
HETATM 9491 O  O   . HOH X 6 .   ? 29.375  3.045   29.573  1.00 17.85 ? 418 HOH D O   1 
HETATM 9492 O  O   . HOH X 6 .   ? 34.264  9.149   26.394  1.00 12.78 ? 419 HOH D O   1 
HETATM 9493 O  O   . HOH X 6 .   ? 11.756  14.876  40.935  1.00 17.60 ? 420 HOH D O   1 
HETATM 9494 O  O   . HOH X 6 .   ? 29.186  10.114  38.020  1.00 14.49 ? 421 HOH D O   1 
HETATM 9495 O  O   . HOH X 6 .   ? 35.832  10.619  21.887  1.00 21.63 ? 422 HOH D O   1 
HETATM 9496 O  O   . HOH X 6 .   ? 32.727  36.578  36.736  1.00 20.70 ? 423 HOH D O   1 
HETATM 9497 O  O   . HOH X 6 .   ? 24.034  12.886  7.718   1.00 27.35 ? 424 HOH D O   1 
HETATM 9498 O  O   . HOH X 6 .   ? 21.294  42.422  32.613  1.00 17.79 ? 425 HOH D O   1 
HETATM 9499 O  O   . HOH X 6 .   ? 16.991  10.851  40.903  1.00 18.95 ? 426 HOH D O   1 
HETATM 9500 O  O   . HOH X 6 .   ? 18.777  0.251   25.726  1.00 20.85 ? 427 HOH D O   1 
HETATM 9501 O  O   . HOH X 6 .   ? 23.211  5.252   32.466  1.00 15.70 ? 428 HOH D O   1 
HETATM 9502 O  O   . HOH X 6 .   ? 33.417  32.768  37.006  1.00 14.22 ? 429 HOH D O   1 
HETATM 9503 O  O   . HOH X 6 .   ? 24.288  4.186   30.314  1.00 15.37 ? 430 HOH D O   1 
HETATM 9504 O  O   . HOH X 6 .   ? 7.764   5.794   34.294  1.00 27.15 ? 431 HOH D O   1 
HETATM 9505 O  O   . HOH X 6 .   ? 34.661  18.643  13.671  1.00 15.52 ? 432 HOH D O   1 
HETATM 9506 O  O   . HOH X 6 .   ? 32.561  10.086  24.345  1.00 11.43 ? 433 HOH D O   1 
HETATM 9507 O  O   . HOH X 6 .   ? 19.822  37.571  28.337  1.00 19.24 ? 434 HOH D O   1 
HETATM 9508 O  O   . HOH X 6 .   ? 3.632   17.714  17.972  1.00 22.25 ? 435 HOH D O   1 
HETATM 9509 O  O   . HOH X 6 .   ? 38.193  18.995  19.604  1.00 22.37 ? 436 HOH D O   1 
HETATM 9510 O  O   . HOH X 6 .   ? 16.931  4.196   40.126  1.00 24.16 ? 437 HOH D O   1 
HETATM 9511 O  O   . HOH X 6 .   ? 40.553  14.421  35.240  1.00 22.00 ? 438 HOH D O   1 
HETATM 9512 O  O   . HOH X 6 .   ? 30.048  33.211  42.820  1.00 17.68 ? 439 HOH D O   1 
HETATM 9513 O  O   . HOH X 6 .   ? 30.671  8.421   39.403  1.00 21.82 ? 440 HOH D O   1 
HETATM 9514 O  O   . HOH X 6 .   ? 31.690  25.791  5.055   1.00 24.69 ? 441 HOH D O   1 
HETATM 9515 O  O   . HOH X 6 .   ? 22.550  31.058  44.109  1.00 22.62 ? 442 HOH D O   1 
HETATM 9516 O  O   . HOH X 6 .   ? 43.831  18.382  47.415  1.00 30.85 ? 443 HOH D O   1 
HETATM 9517 O  O   . HOH X 6 .   ? 34.123  5.963   38.013  1.00 22.21 ? 444 HOH D O   1 
HETATM 9518 O  O   . HOH X 6 .   ? 24.294  3.840   34.813  1.00 17.32 ? 445 HOH D O   1 
HETATM 9519 O  O   . HOH X 6 .   ? 16.464  36.446  27.487  1.00 31.21 ? 446 HOH D O   1 
HETATM 9520 O  O   . HOH X 6 .   ? 7.412   21.745  37.949  1.00 19.97 ? 447 HOH D O   1 
HETATM 9521 O  O   . HOH X 6 .   ? 2.777   23.002  20.162  1.00 27.47 ? 448 HOH D O   1 
HETATM 9522 O  O   . HOH X 6 .   ? 43.365  7.044   35.083  1.00 28.54 ? 449 HOH D O   1 
HETATM 9523 O  O   . HOH X 6 .   ? 28.631  38.315  37.746  1.00 18.94 ? 450 HOH D O   1 
HETATM 9524 O  O   . HOH X 6 .   ? 6.390   30.371  34.687  1.00 14.49 ? 451 HOH D O   1 
HETATM 9525 O  O   . HOH X 6 .   ? 10.427  5.586   21.857  1.00 24.03 ? 452 HOH D O   1 
HETATM 9526 O  O   . HOH X 6 .   ? 16.289  33.224  35.267  1.00 16.91 ? 453 HOH D O   1 
HETATM 9527 O  O   . HOH X 6 .   ? 14.305  9.221   40.447  1.00 21.66 ? 454 HOH D O   1 
HETATM 9528 O  O   . HOH X 6 .   ? 4.521   25.723  17.293  1.00 24.92 ? 455 HOH D O   1 
HETATM 9529 O  O   . HOH X 6 .   ? 16.260  18.628  25.244  1.00 14.21 ? 456 HOH D O   1 
HETATM 9530 O  O   . HOH X 6 .   ? 6.487   16.634  36.841  1.00 20.93 ? 457 HOH D O   1 
HETATM 9531 O  O   . HOH X 6 .   ? 42.425  16.579  35.430  1.00 17.89 ? 458 HOH D O   1 
HETATM 9532 O  O   . HOH X 6 .   ? 15.344  31.894  42.733  1.00 29.11 ? 459 HOH D O   1 
HETATM 9533 O  O   . HOH X 6 .   ? 35.126  4.962   25.215  1.00 28.54 ? 460 HOH D O   1 
HETATM 9534 O  O   . HOH X 6 .   ? 28.534  21.759  46.195  1.00 17.53 ? 461 HOH D O   1 
HETATM 9535 O  O   . HOH X 6 .   ? 36.614  25.239  36.395  1.00 19.57 ? 462 HOH D O   1 
HETATM 9536 O  O   . HOH X 6 .   ? 36.852  15.382  11.351  1.00 30.49 ? 463 HOH D O   1 
HETATM 9537 O  O   . HOH X 6 .   ? 23.288  42.405  34.662  1.00 22.37 ? 464 HOH D O   1 
HETATM 9538 O  O   . HOH X 6 .   ? 39.924  13.760  32.650  1.00 16.44 ? 465 HOH D O   1 
HETATM 9539 O  O   . HOH X 6 .   ? 13.570  32.563  35.625  1.00 15.63 ? 466 HOH D O   1 
HETATM 9540 O  O   . HOH X 6 .   ? 18.855  0.654   33.638  1.00 19.34 ? 467 HOH D O   1 
HETATM 9541 O  O   . HOH X 6 .   ? 24.861  4.482   37.544  1.00 26.88 ? 468 HOH D O   1 
HETATM 9542 O  O   . HOH X 6 .   ? 32.496  8.060   22.292  1.00 22.68 ? 469 HOH D O   1 
HETATM 9543 O  O   . HOH X 6 .   ? 16.825  25.790  11.150  1.00 34.14 ? 470 HOH D O   1 
HETATM 9544 O  O   . HOH X 6 .   ? 40.037  7.296   36.707  1.00 27.24 ? 471 HOH D O   1 
HETATM 9545 O  O   . HOH X 6 .   ? 2.992   18.677  31.068  1.00 28.31 ? 472 HOH D O   1 
HETATM 9546 O  O   . HOH X 6 .   ? 39.674  13.753  29.259  1.00 18.78 ? 473 HOH D O   1 
HETATM 9547 O  O   . HOH X 6 .   ? 40.276  10.376  29.937  1.00 20.36 ? 474 HOH D O   1 
HETATM 9548 O  O   . HOH X 6 .   ? 28.321  28.684  48.028  1.00 24.69 ? 475 HOH D O   1 
HETATM 9549 O  O   . HOH X 6 .   ? 21.588  10.892  15.335  1.00 25.07 ? 476 HOH D O   1 
HETATM 9550 O  O   . HOH X 6 .   ? 32.744  29.555  16.461  1.00 20.84 ? 477 HOH D O   1 
HETATM 9551 O  O   . HOH X 6 .   ? 20.072  18.123  14.479  1.00 21.99 ? 478 HOH D O   1 
HETATM 9552 O  O   . HOH X 6 .   ? 17.934  -0.111  31.200  1.00 29.94 ? 479 HOH D O   1 
HETATM 9553 O  O   . HOH X 6 .   ? 20.945  3.994   32.183  1.00 16.64 ? 480 HOH D O   1 
HETATM 9554 O  O   . HOH X 6 .   ? 3.553   27.853  18.841  1.00 30.79 ? 481 HOH D O   1 
HETATM 9555 O  O   . HOH X 6 .   ? 39.054  7.399   31.957  1.00 22.00 ? 482 HOH D O   1 
HETATM 9556 O  O   . HOH X 6 .   ? 19.095  7.600   41.603  1.00 33.34 ? 483 HOH D O   1 
HETATM 9557 O  O   . HOH X 6 .   ? 33.624  33.294  22.954  1.00 21.68 ? 484 HOH D O   1 
HETATM 9558 O  O   . HOH X 6 .   ? 34.998  28.620  14.875  1.00 16.86 ? 485 HOH D O   1 
HETATM 9559 O  O   . HOH X 6 .   ? 40.223  23.714  12.921  1.00 22.32 ? 486 HOH D O   1 
HETATM 9560 O  O   . HOH X 6 .   ? 27.847  31.261  46.974  1.00 31.89 ? 487 HOH D O   1 
HETATM 9561 O  O   . HOH X 6 .   ? 21.081  6.784   15.854  1.00 25.30 ? 488 HOH D O   1 
HETATM 9562 O  O   . HOH X 6 .   ? 10.046  19.545  38.466  1.00 20.03 ? 489 HOH D O   1 
HETATM 9563 O  O   . HOH X 6 .   ? 14.570  3.046   27.484  1.00 28.38 ? 490 HOH D O   1 
HETATM 9564 O  O   . HOH X 6 .   ? 37.607  4.129   37.534  1.00 29.35 ? 491 HOH D O   1 
HETATM 9565 O  O   . HOH X 6 .   ? 39.466  22.791  10.351  1.00 22.99 ? 492 HOH D O   1 
HETATM 9566 O  O   . HOH X 6 .   ? 32.046  2.710   28.570  1.00 23.18 ? 493 HOH D O   1 
HETATM 9567 O  O   . HOH X 6 .   ? 35.649  33.916  24.617  1.00 30.54 ? 494 HOH D O   1 
HETATM 9568 O  O   . HOH X 6 .   ? 26.871  2.950   31.381  1.00 22.83 ? 495 HOH D O   1 
HETATM 9569 O  O   . HOH X 6 .   ? 3.917   15.623  37.389  1.00 31.00 ? 496 HOH D O   1 
HETATM 9570 O  O   . HOH X 6 .   ? 35.000  34.976  36.067  1.00 19.07 ? 497 HOH D O   1 
HETATM 9571 O  O   . HOH X 6 .   ? 5.235   12.872  38.382  1.00 23.52 ? 498 HOH D O   1 
HETATM 9572 O  O   . HOH X 6 .   ? 28.360  46.106  21.635  1.00 32.25 ? 499 HOH D O   1 
HETATM 9573 O  O   . HOH X 6 .   ? 36.931  7.133   41.367  1.00 36.13 ? 500 HOH D O   1 
HETATM 9574 O  O   . HOH X 6 .   ? 4.450   31.454  28.351  1.00 21.31 ? 501 HOH D O   1 
HETATM 9575 O  O   . HOH X 6 .   ? 34.844  10.546  18.592  1.00 47.84 ? 502 HOH D O   1 
HETATM 9576 O  O   . HOH X 6 .   ? 38.562  11.233  25.594  1.00 19.78 ? 503 HOH D O   1 
HETATM 9577 O  O   . HOH X 6 .   ? 16.045  4.098   42.410  1.00 37.64 ? 504 HOH D O   1 
HETATM 9578 O  O   . HOH X 6 .   ? 26.216  18.509  48.279  1.00 21.32 ? 505 HOH D O   1 
HETATM 9579 O  O   . HOH X 6 .   ? 14.058  34.528  27.807  1.00 22.92 ? 506 HOH D O   1 
HETATM 9580 O  O   . HOH X 6 .   ? 32.120  2.857   35.671  1.00 23.24 ? 507 HOH D O   1 
HETATM 9581 O  O   . HOH X 6 .   ? 27.807  2.274   27.511  1.00 16.85 ? 508 HOH D O   1 
HETATM 9582 O  O   . HOH X 6 .   ? 20.898  15.753  12.972  1.00 24.32 ? 509 HOH D O   1 
HETATM 9583 O  O   . HOH X 6 .   ? 7.364   12.269  22.848  1.00 23.94 ? 510 HOH D O   1 
HETATM 9584 O  O   . HOH X 6 .   ? 2.183   26.599  30.378  1.00 25.58 ? 511 HOH D O   1 
HETATM 9585 O  O   . HOH X 6 .   ? 28.774  18.764  6.989   1.00 21.75 ? 512 HOH D O   1 
HETATM 9586 O  O   . HOH X 6 .   ? 37.256  35.665  37.524  1.00 21.71 ? 513 HOH D O   1 
HETATM 9587 O  O   . HOH X 6 .   ? 7.753   27.968  17.149  1.00 21.34 ? 514 HOH D O   1 
HETATM 9588 O  O   . HOH X 6 .   ? 42.137  13.836  26.305  1.00 25.14 ? 515 HOH D O   1 
HETATM 9589 O  O   . HOH X 6 .   ? 38.303  24.761  9.250   1.00 28.23 ? 516 HOH D O   1 
HETATM 9590 O  O   . HOH X 6 .   ? 44.594  17.054  33.646  1.00 19.75 ? 517 HOH D O   1 
HETATM 9591 O  O   . HOH X 6 .   ? 30.909  22.639  6.105   1.00 25.20 ? 518 HOH D O   1 
HETATM 9592 O  O   . HOH X 6 .   ? 10.361  1.569   34.377  1.00 28.13 ? 519 HOH D O   1 
HETATM 9593 O  O   . HOH X 6 .   ? 7.772   9.331   17.004  1.00 28.60 ? 520 HOH D O   1 
HETATM 9594 O  O   . HOH X 6 .   ? 14.318  13.784  6.935   1.00 23.29 ? 521 HOH D O   1 
HETATM 9595 O  O   . HOH X 6 .   ? 40.543  19.821  20.286  1.00 24.51 ? 522 HOH D O   1 
HETATM 9596 O  O   . HOH X 6 .   ? 36.743  9.211   25.167  1.00 25.46 ? 523 HOH D O   1 
HETATM 9597 O  O   . HOH X 6 .   ? 34.583  30.361  36.443  1.00 20.17 ? 524 HOH D O   1 
HETATM 9598 O  O   . HOH X 6 .   ? 40.701  10.437  27.266  1.00 32.76 ? 525 HOH D O   1 
HETATM 9599 O  O   . HOH X 6 .   ? 17.487  9.094   13.727  1.00 21.60 ? 526 HOH D O   1 
HETATM 9600 O  O   . HOH X 6 .   ? 6.946   13.647  20.612  1.00 26.26 ? 527 HOH D O   1 
HETATM 9601 O  O   . HOH X 6 .   ? 19.469  40.187  29.433  1.00 21.15 ? 528 HOH D O   1 
HETATM 9602 O  O   . HOH X 6 .   ? 4.280   18.031  3.822   1.00 29.26 ? 529 HOH D O   1 
HETATM 9603 O  O   . HOH X 6 .   ? 39.289  16.729  10.624  1.00 25.43 ? 530 HOH D O   1 
HETATM 9604 O  O   . HOH X 6 .   ? 35.058  31.247  21.596  1.00 23.69 ? 531 HOH D O   1 
HETATM 9605 O  O   . HOH X 6 .   ? 31.668  43.274  33.139  1.00 22.83 ? 532 HOH D O   1 
HETATM 9606 O  O   . HOH X 6 .   ? 24.524  25.143  48.522  1.00 30.75 ? 533 HOH D O   1 
HETATM 9607 O  O   . HOH X 6 .   ? 18.902  -2.493  25.681  1.00 28.58 ? 534 HOH D O   1 
HETATM 9608 O  O   . HOH X 6 .   ? 41.812  28.621  44.483  1.00 29.39 ? 535 HOH D O   1 
HETATM 9609 O  O   . HOH X 6 .   ? 44.204  23.455  26.442  1.00 26.58 ? 536 HOH D O   1 
HETATM 9610 O  O   . HOH X 6 .   ? 4.335   13.469  25.472  1.00 26.35 ? 537 HOH D O   1 
HETATM 9611 O  O   . HOH X 6 .   ? 41.636  12.241  41.988  1.00 30.18 ? 538 HOH D O   1 
HETATM 9612 O  O   . HOH X 6 .   ? 4.551   17.514  13.858  1.00 35.46 ? 539 HOH D O   1 
HETATM 9613 O  O   . HOH X 6 .   ? 34.477  28.306  8.077   1.00 29.73 ? 540 HOH D O   1 
HETATM 9614 O  O   . HOH X 6 .   ? 36.874  17.945  14.419  1.00 27.61 ? 541 HOH D O   1 
HETATM 9615 O  O   . HOH X 6 .   ? 42.676  23.916  33.211  1.00 29.49 ? 542 HOH D O   1 
HETATM 9616 O  O   . HOH X 6 .   ? 33.125  30.757  44.103  1.00 25.85 ? 543 HOH D O   1 
HETATM 9617 O  O   . HOH X 6 .   ? 13.558  13.605  42.514  1.00 25.02 ? 544 HOH D O   1 
HETATM 9618 O  O   . HOH X 6 .   ? 33.744  34.950  20.578  1.00 28.15 ? 545 HOH D O   1 
HETATM 9619 O  O   . HOH X 6 .   ? 5.436   22.781  11.853  1.00 31.69 ? 546 HOH D O   1 
HETATM 9620 O  O   . HOH X 6 .   ? 44.632  16.046  24.932  1.00 29.89 ? 547 HOH D O   1 
HETATM 9621 O  O   . HOH X 6 .   ? 39.231  33.931  40.847  1.00 31.76 ? 548 HOH D O   1 
HETATM 9622 O  O   . HOH X 6 .   ? 33.982  2.590   31.594  1.00 25.69 ? 549 HOH D O   1 
HETATM 9623 O  O   . HOH X 6 .   ? 36.068  38.281  34.007  1.00 27.81 ? 550 HOH D O   1 
HETATM 9624 O  O   . HOH X 6 .   ? 10.764  6.487   19.285  1.00 31.96 ? 551 HOH D O   1 
HETATM 9625 O  O   . HOH X 6 .   ? 31.400  14.724  49.585  1.00 34.60 ? 552 HOH D O   1 
HETATM 9626 O  O   . HOH X 6 .   ? 15.448  17.344  43.091  1.00 29.99 ? 553 HOH D O   1 
HETATM 9627 O  O   . HOH X 6 .   ? 30.395  12.119  5.490   1.00 28.40 ? 554 HOH D O   1 
HETATM 9628 O  O   . HOH X 6 .   ? 41.355  21.303  9.057   1.00 24.91 ? 555 HOH D O   1 
HETATM 9629 O  O   . HOH X 6 .   ? 32.163  36.343  43.559  1.00 34.24 ? 556 HOH D O   1 
HETATM 9630 O  O   . HOH X 6 .   ? 19.338  1.438   37.213  1.00 27.82 ? 557 HOH D O   1 
HETATM 9631 O  O   . HOH X 6 .   ? 37.859  13.446  43.857  1.00 28.88 ? 558 HOH D O   1 
HETATM 9632 O  O   . HOH X 6 .   ? 4.924   14.991  39.990  1.00 34.43 ? 559 HOH D O   1 
HETATM 9633 O  O   . HOH X 6 .   ? 19.810  11.190  42.283  1.00 32.86 ? 560 HOH D O   1 
HETATM 9634 O  O   . HOH X 6 .   ? 37.567  31.836  24.909  1.00 27.92 ? 561 HOH D O   1 
HETATM 9635 O  O   . HOH X 6 .   ? 2.488   13.939  18.587  1.00 38.57 ? 562 HOH D O   1 
HETATM 9636 O  O   . HOH X 6 .   ? 45.756  17.643  30.908  1.00 26.78 ? 563 HOH D O   1 
HETATM 9637 O  O   . HOH X 6 .   ? 34.557  15.040  17.379  1.00 30.29 ? 564 HOH D O   1 
HETATM 9638 O  O   . HOH X 6 .   ? 28.247  17.008  49.532  1.00 34.00 ? 565 HOH D O   1 
HETATM 9639 O  O   . HOH X 6 .   ? 14.733  16.426  7.230   1.00 30.25 ? 566 HOH D O   1 
HETATM 9640 O  O   . HOH X 6 .   ? 20.937  38.113  24.269  1.00 30.64 ? 567 HOH D O   1 
HETATM 9641 O  O   . HOH X 6 .   ? 31.096  22.217  9.071   1.00 23.20 ? 568 HOH D O   1 
HETATM 9642 O  O   . HOH X 6 .   ? 2.051   6.181   28.684  1.00 41.99 ? 569 HOH D O   1 
HETATM 9643 O  O   . HOH X 6 .   ? 16.099  18.880  11.068  1.00 32.57 ? 570 HOH D O   1 
HETATM 9644 O  O   . HOH X 6 .   ? 20.401  19.752  10.611  1.00 36.19 ? 571 HOH D O   1 
HETATM 9645 O  O   . HOH X 6 .   ? 21.758  2.594   18.170  1.00 30.72 ? 572 HOH D O   1 
HETATM 9646 O  O   . HOH X 6 .   ? 36.171  21.900  48.122  1.00 31.03 ? 573 HOH D O   1 
HETATM 9647 O  O   . HOH X 6 .   ? 39.607  23.514  36.351  1.00 30.92 ? 574 HOH D O   1 
HETATM 9648 O  O   . HOH X 6 .   ? 34.736  37.321  21.565  1.00 33.04 ? 575 HOH D O   1 
HETATM 9649 O  O   . HOH X 6 .   ? 1.606   21.797  24.776  1.00 26.87 ? 576 HOH D O   1 
HETATM 9650 O  O   . HOH X 6 .   ? 18.582  9.761   11.263  1.00 28.80 ? 577 HOH D O   1 
HETATM 9651 O  O   . HOH X 6 .   ? 21.728  33.588  44.903  1.00 31.35 ? 578 HOH D O   1 
HETATM 9652 O  O   . HOH X 6 .   ? 26.668  24.443  9.737   1.00 30.98 ? 579 HOH D O   1 
HETATM 9653 O  O   . HOH X 6 .   ? 18.370  14.516  6.788   1.00 35.85 ? 580 HOH D O   1 
HETATM 9654 O  O   . HOH X 6 .   ? 32.974  19.096  49.559  1.00 35.54 ? 581 HOH D O   1 
HETATM 9655 O  O   . HOH X 6 .   ? 26.778  36.570  20.283  1.00 29.11 ? 582 HOH D O   1 
HETATM 9656 O  O   . HOH X 6 .   ? 17.809  14.314  10.531  1.00 43.03 ? 583 HOH D O   1 
HETATM 9657 O  O   . HOH X 6 .   ? 0.441   23.428  22.888  1.00 38.19 ? 584 HOH D O   1 
HETATM 9658 O  O   . HOH X 6 .   ? 43.064  14.965  44.396  1.00 29.25 ? 585 HOH D O   1 
HETATM 9659 O  O   . HOH X 6 .   ? 14.721  27.228  12.340  1.00 32.10 ? 586 HOH D O   1 
HETATM 9660 O  O   . HOH X 6 .   ? 15.345  0.307   29.776  1.00 26.61 ? 587 HOH D O   1 
HETATM 9661 O  O   . HOH X 6 .   ? 20.769  12.524  12.554  1.00 39.42 ? 588 HOH D O   1 
HETATM 9662 O  O   . HOH X 6 .   ? 28.132  2.310   36.721  1.00 29.72 ? 589 HOH D O   1 
HETATM 9663 O  O   . HOH X 6 .   ? 39.700  19.328  52.839  1.00 37.06 ? 590 HOH D O   1 
HETATM 9664 O  O   . HOH X 6 .   ? 30.811  19.927  47.103  1.00 27.61 ? 591 HOH D O   1 
HETATM 9665 O  O   . HOH X 6 .   ? 42.091  18.861  18.392  1.00 39.05 ? 592 HOH D O   1 
HETATM 9666 O  O   . HOH X 6 .   ? 16.392  2.902   19.777  1.00 29.46 ? 593 HOH D O   1 
HETATM 9667 O  O   . HOH X 6 .   ? -1.266  27.743  27.730  1.00 35.38 ? 594 HOH D O   1 
HETATM 9668 O  O   . HOH X 6 .   ? 35.402  39.853  29.398  1.00 29.86 ? 595 HOH D O   1 
HETATM 9669 O  O   . HOH X 6 .   ? 45.627  15.993  45.229  1.00 37.32 ? 596 HOH D O   1 
HETATM 9670 O  O   . HOH X 6 .   ? 9.547   4.801   39.282  1.00 31.54 ? 597 HOH D O   1 
HETATM 9671 O  O   . HOH X 6 .   ? 14.584  3.084   22.274  1.00 31.97 ? 598 HOH D O   1 
HETATM 9672 O  O   . HOH X 6 .   ? 20.358  16.616  10.616  1.00 33.68 ? 599 HOH D O   1 
HETATM 9673 O  O   . HOH X 6 .   ? 40.097  10.989  42.977  1.00 32.66 ? 600 HOH D O   1 
HETATM 9674 O  O   . HOH X 6 .   ? 15.693  4.934   18.661  1.00 35.40 ? 601 HOH D O   1 
HETATM 9675 O  O   . HOH X 6 .   ? 47.763  19.842  46.875  1.00 39.04 ? 602 HOH D O   1 
HETATM 9676 O  O   . HOH X 6 .   ? 5.055   12.153  19.926  1.00 34.38 ? 603 HOH D O   1 
HETATM 9677 O  O   . HOH X 6 .   ? 21.584  14.300  9.517   1.00 37.69 ? 604 HOH D O   1 
HETATM 9678 O  O   . HOH X 6 .   ? 41.069  8.399   43.473  1.00 26.06 ? 605 HOH D O   1 
HETATM 9679 O  O   . HOH X 6 .   ? 23.848  15.567  3.676   1.00 27.24 ? 606 HOH D O   1 
HETATM 9680 O  O   . HOH X 6 .   ? 30.435  6.001   37.961  1.00 27.08 ? 607 HOH D O   1 
HETATM 9681 O  O   . HOH X 6 .   ? 10.694  2.883   36.702  1.00 28.10 ? 608 HOH D O   1 
HETATM 9682 O  O   . HOH X 6 .   ? 4.781   15.038  12.274  1.00 33.92 ? 609 HOH D O   1 
HETATM 9683 O  O   . HOH X 6 .   ? 18.366  2.060   39.695  1.00 34.34 ? 610 HOH D O   1 
HETATM 9684 O  O   . HOH X 6 .   ? 22.204  42.294  37.308  1.00 28.37 ? 611 HOH D O   1 
HETATM 9685 O  O   . HOH X 6 .   ? 13.514  25.348  14.453  1.00 36.19 ? 612 HOH D O   1 
HETATM 9686 O  O   . HOH X 6 .   ? 26.454  6.164   38.444  1.00 24.12 ? 613 HOH D O   1 
HETATM 9687 O  O   . HOH X 6 .   ? 17.081  28.777  46.828  1.00 45.43 ? 614 HOH D O   1 
HETATM 9688 O  O   . HOH X 6 .   ? 37.221  6.719   24.113  1.00 39.81 ? 615 HOH D O   1 
HETATM 9689 O  O   . HOH X 6 .   ? 18.371  19.775  12.488  1.00 41.35 ? 616 HOH D O   1 
HETATM 9690 O  O   . HOH X 6 .   ? 42.238  8.975   31.278  1.00 34.89 ? 617 HOH D O   1 
HETATM 9691 O  O   . HOH X 6 .   ? 40.737  25.729  16.312  1.00 36.38 ? 618 HOH D O   1 
HETATM 9692 O  O   . HOH X 6 .   ? 4.725   22.401  37.826  1.00 34.61 ? 619 HOH D O   1 
HETATM 9693 O  O   . HOH X 6 .   ? 22.026  8.358   41.436  1.00 36.12 ? 620 HOH D O   1 
HETATM 9694 O  O   . HOH X 6 .   ? 27.612  11.385  13.579  1.00 40.58 ? 621 HOH D O   1 
HETATM 9695 O  O   . HOH X 6 .   ? 2.548   15.844  33.357  1.00 36.53 ? 622 HOH D O   1 
HETATM 9696 O  O   . HOH X 6 .   ? 19.672  11.792  44.690  1.00 26.96 ? 623 HOH D O   1 
HETATM 9697 O  O   . HOH X 6 .   ? 28.193  19.916  9.683   1.00 25.26 ? 624 HOH D O   1 
HETATM 9698 O  O   . HOH X 6 .   ? 39.551  26.048  41.527  1.00 35.65 ? 625 HOH D O   1 
HETATM 9699 O  O   . HOH X 6 .   ? 31.335  3.392   24.329  1.00 35.25 ? 626 HOH D O   1 
HETATM 9700 O  O   . HOH X 6 .   ? 22.551  28.761  47.940  1.00 30.39 ? 627 HOH D O   1 
HETATM 9701 O  O   . HOH X 6 .   ? 9.414   34.460  39.789  1.00 30.78 ? 628 HOH D O   1 
HETATM 9702 O  O   . HOH X 6 .   ? 21.615  23.392  11.892  1.00 33.94 ? 629 HOH D O   1 
HETATM 9703 O  O   . HOH X 6 .   ? 7.770   34.569  42.458  1.00 32.26 ? 630 HOH D O   1 
HETATM 9704 O  O   . HOH X 6 .   ? 42.939  24.910  42.021  1.00 29.91 ? 631 HOH D O   1 
HETATM 9705 O  O   . HOH X 6 .   ? 7.068   13.021  11.764  1.00 38.22 ? 632 HOH D O   1 
HETATM 9706 O  O   . HOH X 6 .   ? 11.007  27.387  40.439  1.00 39.55 ? 633 HOH D O   1 
HETATM 9707 O  O   . HOH X 6 .   ? 38.220  25.932  39.236  1.00 30.87 ? 634 HOH D O   1 
HETATM 9708 O  O   . HOH X 6 .   ? 18.051  30.608  24.987  1.00 36.67 ? 635 HOH D O   1 
HETATM 9709 O  O   . HOH X 6 .   ? 30.124  13.058  12.701  1.00 22.63 ? 636 HOH D O   1 
HETATM 9710 O  O   . HOH X 6 .   ? 24.181  9.082   15.455  1.00 42.18 ? 637 HOH D O   1 
HETATM 9711 O  O   . HOH X 6 .   ? 27.343  26.805  51.976  1.00 36.26 ? 638 HOH D O   1 
HETATM 9712 O  O   . HOH X 6 .   ? 25.976  27.520  49.293  1.00 28.28 ? 639 HOH D O   1 
HETATM 9713 O  O   . HOH X 6 .   ? 15.020  13.080  3.945   1.00 28.63 ? 640 HOH D O   1 
HETATM 9714 O  O   . HOH X 6 .   ? 28.795  4.715   38.663  1.00 34.99 ? 641 HOH D O   1 
HETATM 9715 O  O   . HOH X 6 .   ? 37.883  3.455   32.363  1.00 27.56 ? 642 HOH D O   1 
HETATM 9716 O  O   . HOH X 6 .   ? 44.925  23.764  29.457  1.00 28.80 ? 643 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . HIS A 4   ? 0.6539 0.4681 0.2255 -0.1221 -0.1036 0.0149  4   HIS A N   
2    C  CA  . HIS A 4   ? 0.5189 0.3009 0.3016 -0.0256 0.0308  -0.0916 4   HIS A CA  
3    C  C   . HIS A 4   ? 0.2917 0.2757 0.2166 0.0362  -0.0557 0.0074  4   HIS A C   
4    O  O   . HIS A 4   ? 0.3424 0.2748 0.2070 0.0057  -0.0165 -0.0342 4   HIS A O   
5    C  CB  . HIS A 4   ? 0.4855 0.3603 0.2766 -0.0979 -0.0595 -0.0822 4   HIS A CB  
6    C  CG  . HIS A 4   ? 0.4790 0.5375 0.3664 -0.0236 0.2029  0.0120  4   HIS A CG  
7    N  ND1 . HIS A 4   ? 0.7311 0.3368 0.5695 -0.0856 0.0239  -0.1938 4   HIS A ND1 
8    C  CD2 . HIS A 4   ? 0.6777 0.5159 0.2581 -0.0487 0.2166  -0.1036 4   HIS A CD2 
9    C  CE1 . HIS A 4   ? 0.4830 0.7264 0.5857 -0.0917 0.0887  -0.0194 4   HIS A CE1 
10   N  NE2 . HIS A 4   ? 0.4963 0.5266 0.3217 0.0361  0.1832  -0.0908 4   HIS A NE2 
11   N  N   . TRP A 5   ? 0.3120 0.2260 0.1764 -0.0250 -0.0485 -0.0201 5   TRP A N   
12   C  CA  . TRP A 5   ? 0.2687 0.1836 0.1744 -0.0151 -0.0060 -0.0234 5   TRP A CA  
13   C  C   . TRP A 5   ? 0.2129 0.2382 0.1280 -0.0115 -0.0357 0.0051  5   TRP A C   
14   O  O   . TRP A 5   ? 0.2424 0.2161 0.1466 -0.0115 -0.0287 -0.0130 5   TRP A O   
15   C  CB  . TRP A 5   ? 0.2739 0.1915 0.1750 -0.0384 -0.0024 -0.0110 5   TRP A CB  
16   C  CG  . TRP A 5   ? 0.2443 0.2184 0.1453 -0.0331 -0.0015 -0.0157 5   TRP A CG  
17   C  CD1 . TRP A 5   ? 0.2617 0.2021 0.1588 -0.0329 0.0031  -0.0102 5   TRP A CD1 
18   C  CD2 . TRP A 5   ? 0.2476 0.2257 0.1666 -0.0348 0.0185  -0.0172 5   TRP A CD2 
19   N  NE1 . TRP A 5   ? 0.2053 0.2148 0.1919 -0.0377 -0.0030 -0.0094 5   TRP A NE1 
20   C  CE2 . TRP A 5   ? 0.2488 0.2129 0.1874 0.0060  -0.0085 0.0059  5   TRP A CE2 
21   C  CE3 . TRP A 5   ? 0.1939 0.2213 0.1163 0.0315  -0.0020 0.0183  5   TRP A CE3 
22   C  CZ2 . TRP A 5   ? 0.2086 0.2542 0.2041 0.0200  0.0000  0.0096  5   TRP A CZ2 
23   C  CZ3 . TRP A 5   ? 0.1588 0.1836 0.1396 0.0189  -0.0041 0.0173  5   TRP A CZ3 
24   C  CH2 . TRP A 5   ? 0.1944 0.2050 0.1896 0.0228  -0.0218 0.0606  5   TRP A CH2 
25   N  N   . GLY A 6   ? 0.2224 0.1509 0.1468 0.0122  -0.0080 0.0267  6   GLY A N   
26   C  CA  . GLY A 6   ? 0.1996 0.2163 0.1860 0.0091  -0.0244 0.0109  6   GLY A CA  
27   C  C   . GLY A 6   ? 0.1498 0.1990 0.1256 -0.0031 0.0214  0.0244  6   GLY A C   
28   O  O   . GLY A 6   ? 0.1701 0.1969 0.1226 0.0015  0.0060  0.0013  6   GLY A O   
29   N  N   . TYR A 7   ? 0.2454 0.1875 0.1093 0.0161  0.0107  0.0024  7   TYR A N   
30   C  CA  . TYR A 7   ? 0.2563 0.1599 0.1414 0.0230  0.0350  -0.0209 7   TYR A CA  
31   C  C   . TYR A 7   ? 0.3005 0.2159 0.1705 -0.0201 0.0023  0.0293  7   TYR A C   
32   O  O   . TYR A 7   ? 0.3133 0.2366 0.1718 0.0129  0.0342  0.0043  7   TYR A O   
33   C  CB  . TYR A 7   ? 0.2236 0.1964 0.1474 0.0443  0.0467  0.0209  7   TYR A CB  
34   C  CG  . TYR A 7   ? 0.1981 0.1624 0.1098 0.0456  -0.0083 -0.0243 7   TYR A CG  
35   C  CD1 . TYR A 7   ? 0.1707 0.1737 0.1173 0.0289  0.0097  0.0052  7   TYR A CD1 
36   C  CD2 . TYR A 7   ? 0.2150 0.1823 0.1398 0.0381  0.0027  -0.0099 7   TYR A CD2 
37   C  CE1 . TYR A 7   ? 0.1624 0.1486 0.1268 0.0163  0.0306  0.0057  7   TYR A CE1 
38   C  CE2 . TYR A 7   ? 0.1705 0.1651 0.1342 0.0122  -0.0148 -0.0244 7   TYR A CE2 
39   C  CZ  . TYR A 7   ? 0.1493 0.1624 0.1296 0.0109  0.0135  -0.0153 7   TYR A CZ  
40   O  OH  . TYR A 7   ? 0.1847 0.1500 0.1520 0.0148  -0.0153 0.0092  7   TYR A OH  
41   N  N   . GLY A 8   ? 0.2680 0.2212 0.1675 0.0397  -0.0107 0.0383  8   GLY A N   
42   C  CA  . GLY A 8   ? 0.2732 0.1899 0.1730 0.0131  0.0232  0.0342  8   GLY A CA  
43   C  C   . GLY A 8   ? 0.2472 0.2296 0.1689 0.0445  0.0131  0.0046  8   GLY A C   
44   O  O   . GLY A 8   ? 0.2768 0.2415 0.1313 0.0419  0.0103  0.0041  8   GLY A O   
45   N  N   . LYS A 9   ? 0.2845 0.2141 0.1814 0.0262  0.0515  -0.0071 9   LYS A N   
46   C  CA  . LYS A 9   ? 0.2513 0.2321 0.2425 0.0333  0.0285  -0.0204 9   LYS A CA  
47   C  C   . LYS A 9   ? 0.2448 0.2066 0.1651 0.0368  0.0131  0.0320  9   LYS A C   
48   O  O   . LYS A 9   ? 0.2782 0.2606 0.1572 -0.0032 0.0043  -0.0198 9   LYS A O   
49   C  CB  . LYS A 9   ? 0.3497 0.2247 0.2538 0.0296  0.0559  0.0108  9   LYS A CB  
50   C  CG  . LYS A 9   ? 0.3212 0.1861 0.4225 0.0329  0.0087  0.0427  9   LYS A CG  
51   N  N   . HIS A 10  ? 0.2888 0.2060 0.1755 0.0115  0.0285  0.0176  10  HIS A N   
52   C  CA  . HIS A 10  ? 0.2739 0.2111 0.1348 0.0329  0.0037  0.0175  10  HIS A CA  
53   C  C   . HIS A 10  ? 0.2461 0.1822 0.1560 0.0559  0.0114  0.0087  10  HIS A C   
54   O  O   . HIS A 10  ? 0.2685 0.2181 0.1488 0.0177  0.0234  0.0259  10  HIS A O   
55   C  CB  . HIS A 10  ? 0.2775 0.2098 0.1522 -0.0219 -0.0362 0.0149  10  HIS A CB  
56   C  CG  . HIS A 10  ? 0.2073 0.2097 0.1574 -0.0218 0.0125  -0.0052 10  HIS A CG  
57   N  ND1 . HIS A 10  ? 0.2481 0.2293 0.1876 0.0207  0.0476  0.0452  10  HIS A ND1 
58   C  CD2 . HIS A 10  ? 0.2610 0.2204 0.1371 0.0175  -0.0298 0.0219  10  HIS A CD2 
59   C  CE1 . HIS A 10  ? 0.2449 0.2120 0.1941 -0.0046 0.0176  0.0971  10  HIS A CE1 
60   N  NE2 . HIS A 10  ? 0.2508 0.2463 0.1734 0.0104  0.0254  0.0200  10  HIS A NE2 
61   N  N   . ASN A 11  ? 0.2463 0.1800 0.1375 -0.0458 -0.0076 -0.0003 11  ASN A N   
62   C  CA  . ASN A 11  ? 0.2170 0.1762 0.1292 -0.0008 -0.0361 0.0165  11  ASN A CA  
63   C  C   . ASN A 11  ? 0.2418 0.1817 0.1177 -0.0142 0.0006  -0.0190 11  ASN A C   
64   O  O   . ASN A 11  ? 0.2402 0.1987 0.1263 0.0062  0.0052  -0.0031 11  ASN A O   
65   C  CB  . ASN A 11  ? 0.1919 0.1852 0.1477 0.0153  -0.0130 0.0132  11  ASN A CB  
66   C  CG  . ASN A 11  ? 0.2124 0.2157 0.1784 -0.0071 0.0162  0.0138  11  ASN A CG  
67   O  OD1 . ASN A 11  ? 0.2702 0.2567 0.1955 0.0080  0.0116  -0.0337 11  ASN A OD1 
68   N  ND2 . ASN A 11  ? 0.2251 0.2603 0.1974 -0.0188 -0.0244 -0.0189 11  ASN A ND2 
69   N  N   . GLY A 12  ? 0.2269 0.1878 0.1030 -0.0082 0.0140  0.0116  12  GLY A N   
70   C  CA  . GLY A 12  ? 0.1917 0.1938 0.1062 -0.0100 -0.0333 0.0107  12  GLY A CA  
71   C  C   . GLY A 12  ? 0.1897 0.1605 0.1455 -0.0041 -0.0026 0.0038  12  GLY A C   
72   O  O   . GLY A 12  ? 0.2186 0.1696 0.1319 -0.0194 0.0219  0.0054  12  GLY A O   
73   N  N   . PRO A 13  ? 0.1914 0.1515 0.1123 0.0034  0.0041  -0.0032 13  PRO A N   
74   C  CA  . PRO A 13  ? 0.2023 0.1673 0.1328 0.0193  0.0049  -0.0320 13  PRO A CA  
75   C  C   . PRO A 13  ? 0.2034 0.1879 0.1337 0.0220  -0.0063 0.0114  13  PRO A C   
76   O  O   . PRO A 13  ? 0.2375 0.1903 0.1032 0.0221  0.0119  0.0098  13  PRO A O   
77   C  CB  . PRO A 13  ? 0.2127 0.1777 0.1143 0.0483  -0.0096 -0.0260 13  PRO A CB  
78   C  CG  . PRO A 13  ? 0.2000 0.1872 0.1265 0.0152  -0.0161 0.0256  13  PRO A CG  
79   C  CD  . PRO A 13  ? 0.1940 0.2181 0.1249 0.0210  0.0024  0.0195  13  PRO A CD  
80   N  N   . GLU A 14  ? 0.2078 0.1576 0.1324 -0.0120 0.0073  -0.0034 14  GLU A N   
81   C  CA  . GLU A 14  ? 0.2269 0.2096 0.1913 -0.0359 0.0227  -0.0153 14  GLU A CA  
82   C  C   . GLU A 14  ? 0.1856 0.1508 0.1680 -0.0035 0.0192  0.0113  14  GLU A C   
83   O  O   . GLU A 14  ? 0.2184 0.2217 0.1612 -0.0138 0.0104  -0.0027 14  GLU A O   
84   C  CB  . GLU A 14  ? 0.2732 0.1937 0.2300 -0.0549 0.0379  -0.0344 14  GLU A CB  
85   C  CG  . GLU A 14  ? 0.4334 0.2269 0.2391 -0.0507 0.0303  -0.0719 14  GLU A CG  
86   C  CD  . GLU A 14  ? 0.4438 0.4722 0.4702 0.0873  -0.0626 0.0107  14  GLU A CD  
87   O  OE1 . GLU A 14  ? 0.3950 0.5156 0.5540 0.0122  0.0035  -0.0683 14  GLU A OE1 
88   O  OE2 . GLU A 14  ? 0.4783 0.5749 0.3819 -0.1356 -0.1765 0.0895  14  GLU A OE2 
89   N  N   . HIS A 15  ? 0.2179 0.1692 0.1086 -0.0013 0.0060  0.0038  15  HIS A N   
90   C  CA  . HIS A 15  ? 0.2381 0.1648 0.1125 -0.0046 0.0131  -0.0104 15  HIS A CA  
91   C  C   . HIS A 15  ? 0.2447 0.1660 0.1067 0.0208  0.0399  0.0074  15  HIS A C   
92   O  O   . HIS A 15  ? 0.2219 0.1574 0.1109 0.0024  0.0262  0.0057  15  HIS A O   
93   C  CB  . HIS A 15  ? 0.2213 0.1836 0.1278 -0.0188 0.0153  0.0318  15  HIS A CB  
94   C  CG  . HIS A 15  ? 0.2515 0.2091 0.1021 0.0005  0.0035  0.0107  15  HIS A CG  
95   N  ND1 . HIS A 15  ? 0.2335 0.1951 0.1102 -0.0131 0.0219  0.0057  15  HIS A ND1 
96   C  CD2 . HIS A 15  ? 0.3093 0.2174 0.1748 -0.0057 -0.0476 0.0458  15  HIS A CD2 
97   C  CE1 . HIS A 15  ? 0.2363 0.1892 0.2136 -0.0142 -0.0031 0.0395  15  HIS A CE1 
98   N  NE2 . HIS A 15  ? 0.2305 0.2190 0.1678 -0.0115 -0.0038 0.0445  15  HIS A NE2 
99   N  N   . TRP A 16  ? 0.2104 0.1446 0.1053 -0.0054 0.0388  0.0098  16  TRP A N   
100  C  CA  . TRP A 16  ? 0.2190 0.1429 0.0944 0.0049  0.0317  0.0098  16  TRP A CA  
101  C  C   . TRP A 16  ? 0.1678 0.1542 0.0856 -0.0057 0.0181  -0.0026 16  TRP A C   
102  O  O   . TRP A 16  ? 0.1912 0.1446 0.1032 0.0024  0.0300  0.0070  16  TRP A O   
103  C  CB  . TRP A 16  ? 0.2020 0.1967 0.0882 0.0170  0.0395  0.0054  16  TRP A CB  
104  C  CG  . TRP A 16  ? 0.1784 0.1630 0.1228 0.0000  0.0098  -0.0091 16  TRP A CG  
105  C  CD1 . TRP A 16  ? 0.1592 0.1206 0.1515 0.0130  0.0049  0.0215  16  TRP A CD1 
106  C  CD2 . TRP A 16  ? 0.1762 0.1746 0.1140 -0.0044 0.0110  -0.0074 16  TRP A CD2 
107  N  NE1 . TRP A 16  ? 0.1629 0.1355 0.1150 0.0081  -0.0038 -0.0035 16  TRP A NE1 
108  C  CE2 . TRP A 16  ? 0.1675 0.1574 0.1107 -0.0245 0.0129  0.0151  16  TRP A CE2 
109  C  CE3 . TRP A 16  ? 0.1797 0.1459 0.0973 0.0197  0.0165  -0.0073 16  TRP A CE3 
110  C  CZ2 . TRP A 16  ? 0.2093 0.1610 0.1058 0.0298  0.0115  0.0054  16  TRP A CZ2 
111  C  CZ3 . TRP A 16  ? 0.1719 0.1698 0.1145 0.0252  0.0250  -0.0049 16  TRP A CZ3 
112  C  CH2 . TRP A 16  ? 0.1782 0.1601 0.1380 0.0278  -0.0252 0.0194  16  TRP A CH2 
113  N  N   . HIS A 17  ? 0.1782 0.1777 0.1023 -0.0048 0.0146  0.0010  17  HIS A N   
114  C  CA  . HIS A 17  ? 0.1823 0.1849 0.1310 -0.0092 0.0449  -0.0159 17  HIS A CA  
115  C  C   . HIS A 17  ? 0.2108 0.1904 0.1385 0.0386  0.0232  -0.0063 17  HIS A C   
116  O  O   . HIS A 17  ? 0.2351 0.1886 0.1026 0.0077  0.0359  0.0087  17  HIS A O   
117  C  CB  . HIS A 17  ? 0.2081 0.2188 0.1129 -0.0104 0.0120  0.0051  17  HIS A CB  
118  C  CG  . HIS A 17  ? 0.2168 0.1829 0.1355 0.0094  0.0397  -0.0081 17  HIS A CG  
119  N  ND1 . HIS A 17  ? 0.2741 0.2355 0.1912 0.0013  0.0608  0.0280  17  HIS A ND1 
120  C  CD2 . HIS A 17  ? 0.2179 0.1944 0.1277 -0.0237 0.0337  0.0340  17  HIS A CD2 
121  C  CE1 . HIS A 17  ? 0.3023 0.2339 0.1484 0.0003  -0.0109 0.0571  17  HIS A CE1 
122  N  NE2 . HIS A 17  ? 0.2382 0.2319 0.1206 -0.0311 0.0412  0.0154  17  HIS A NE2 
123  N  N   . LYS A 18  ? 0.2323 0.1946 0.1086 -0.0034 0.0439  -0.0115 18  LYS A N   
124  C  CA  . LYS A 18  ? 0.2396 0.1956 0.1152 0.0008  0.0214  -0.0252 18  LYS A CA  
125  C  C   . LYS A 18  ? 0.2682 0.2023 0.2111 0.0012  0.0458  0.0208  18  LYS A C   
126  O  O   . LYS A 18  ? 0.3679 0.2612 0.1911 0.0026  0.1006  -0.0305 18  LYS A O   
127  C  CB  . LYS A 18  ? 0.2353 0.2014 0.1491 -0.0054 0.0230  0.0038  18  LYS A CB  
128  C  CG  . LYS A 18  ? 0.2840 0.2552 0.1435 -0.0504 0.0021  0.0329  18  LYS A CG  
129  C  CD  . LYS A 18  ? 0.2427 0.1949 0.1535 0.0077  0.0008  0.0088  18  LYS A CD  
130  C  CE  . LYS A 18  ? 0.2619 0.1825 0.1826 0.0008  0.0119  0.0423  18  LYS A CE  
131  N  NZ  . LYS A 18  ? 0.2274 0.2086 0.1299 -0.0491 0.0113  0.0155  18  LYS A NZ  
132  N  N   . ASP A 19  ? 0.2912 0.2226 0.1360 -0.0465 0.0328  -0.0419 19  ASP A N   
133  C  CA  . ASP A 19  ? 0.3366 0.2048 0.1360 -0.0163 0.0340  0.0049  19  ASP A CA  
134  C  C   . ASP A 19  ? 0.3005 0.2062 0.1624 -0.0236 0.0010  -0.0027 19  ASP A C   
135  O  O   . ASP A 19  ? 0.3303 0.1817 0.1705 -0.0087 -0.0054 -0.0259 19  ASP A O   
136  C  CB  . ASP A 19  ? 0.3037 0.3142 0.2208 -0.0948 -0.0043 0.0879  19  ASP A CB  
137  C  CG  . ASP A 19  ? 0.3887 0.4002 0.1685 0.0331  -0.0055 0.0173  19  ASP A CG  
138  O  OD1 . ASP A 19  ? 0.4153 0.4061 0.2764 0.0250  0.0308  -0.0269 19  ASP A OD1 
139  O  OD2 . ASP A 19  ? 0.5641 0.7096 0.3950 0.0518  -0.0007 0.1013  19  ASP A OD2 
140  N  N   . PHE A 20  ? 0.2170 0.1753 0.1265 0.0102  0.0401  -0.0111 20  PHE A N   
141  C  CA  . PHE A 20  ? 0.2111 0.2372 0.1050 0.0076  0.0456  -0.0185 20  PHE A CA  
142  C  C   . PHE A 20  ? 0.1886 0.1879 0.1172 0.0031  0.0218  0.0086  20  PHE A C   
143  O  O   . PHE A 20  ? 0.2336 0.1762 0.1276 0.0094  0.0357  -0.0177 20  PHE A O   
144  C  CB  . PHE A 20  ? 0.2166 0.2057 0.1364 -0.0151 0.0654  -0.0232 20  PHE A CB  
145  C  CG  . PHE A 20  ? 0.2122 0.2325 0.1088 -0.0078 0.0665  -0.0331 20  PHE A CG  
146  C  CD1 . PHE A 20  ? 0.3043 0.3057 0.1208 -0.0362 0.0465  -0.0357 20  PHE A CD1 
147  C  CD2 . PHE A 20  ? 0.2635 0.2989 0.1480 0.0148  0.0297  -0.0627 20  PHE A CD2 
148  C  CE1 . PHE A 20  ? 0.2705 0.3282 0.1791 -0.0259 0.0680  -0.0441 20  PHE A CE1 
149  C  CE2 . PHE A 20  ? 0.2515 0.2820 0.2005 -0.0410 0.0551  -0.0204 20  PHE A CE2 
150  C  CZ  . PHE A 20  ? 0.2689 0.2768 0.1377 -0.0562 0.0522  -0.0286 20  PHE A CZ  
151  N  N   . PRO A 21  ? 0.2500 0.1721 0.1699 0.0346  0.0234  -0.0046 21  PRO A N   
152  C  CA  . PRO A 21  ? 0.2490 0.2328 0.1588 0.0414  0.0450  -0.0502 21  PRO A CA  
153  C  C   . PRO A 21  ? 0.1840 0.1955 0.1513 0.0035  0.0511  -0.0243 21  PRO A C   
154  O  O   . PRO A 21  ? 0.2244 0.1921 0.1333 0.0232  0.0650  -0.0091 21  PRO A O   
155  C  CB  . PRO A 21  ? 0.3118 0.2899 0.1391 0.0220  0.1026  -0.1074 21  PRO A CB  
156  C  CG  . PRO A 21  ? 0.2169 0.3235 0.3955 0.0285  0.0772  -0.1254 21  PRO A CG  
157  C  CD  . PRO A 21  ? 0.2768 0.2242 0.1768 0.0264  0.0115  -0.0579 21  PRO A CD  
158  N  N   A ILE A 22  ? 0.2213 0.1624 0.1200 0.0263  0.0531  -0.0137 22  ILE A N   
159  N  N   B ILE A 22  ? 0.2283 0.1606 0.1306 0.0229  0.0630  -0.0168 22  ILE A N   
160  C  CA  A ILE A 22  ? 0.2251 0.1656 0.1374 0.0432  0.0597  -0.0329 22  ILE A CA  
161  C  CA  B ILE A 22  ? 0.2486 0.1687 0.1484 0.0331  0.0789  -0.0285 22  ILE A CA  
162  C  C   A ILE A 22  ? 0.1693 0.1563 0.1224 0.0189  0.0311  -0.0162 22  ILE A C   
163  C  C   B ILE A 22  ? 0.1719 0.1488 0.1203 0.0119  0.0344  -0.0063 22  ILE A C   
164  O  O   A ILE A 22  ? 0.1694 0.1265 0.1136 0.0195  0.0421  -0.0026 22  ILE A O   
165  O  O   B ILE A 22  ? 0.1766 0.1881 0.0901 -0.0226 0.0432  0.0184  22  ILE A O   
166  C  CB  A ILE A 22  ? 0.2035 0.1450 0.1486 0.0458  0.0115  0.0007  22  ILE A CB  
167  C  CB  B ILE A 22  ? 0.1984 0.1798 0.1750 0.0197  0.0248  0.0201  22  ILE A CB  
168  C  CG1 A ILE A 22  ? 0.2380 0.1996 0.1441 0.0432  0.0109  0.0031  22  ILE A CG1 
169  C  CG1 B ILE A 22  ? 0.2348 0.1466 0.1565 0.0656  0.0242  -0.0127 22  ILE A CG1 
170  C  CG2 A ILE A 22  ? 0.2129 0.2160 0.1365 0.0706  0.0529  -0.0551 22  ILE A CG2 
171  C  CG2 B ILE A 22  ? 0.2251 0.2134 0.1825 0.0487  0.0568  -0.0410 22  ILE A CG2 
172  C  CD1 A ILE A 22  ? 0.2187 0.2330 0.1827 0.0297  -0.0113 -0.0335 22  ILE A CD1 
173  C  CD1 B ILE A 22  ? 0.2809 0.1750 0.2098 -0.0144 0.0786  -0.0571 22  ILE A CD1 
174  N  N   . ALA A 23  ? 0.1949 0.1556 0.1430 0.0496  0.0463  -0.0027 23  ALA A N   
175  C  CA  . ALA A 23  ? 0.2152 0.1463 0.1366 0.0434  0.0219  -0.0142 23  ALA A CA  
176  C  C   . ALA A 23  ? 0.2107 0.1730 0.1174 0.0342  0.0469  0.0031  23  ALA A C   
177  O  O   . ALA A 23  ? 0.2199 0.1499 0.1387 -0.0043 0.0364  -0.0185 23  ALA A O   
178  C  CB  . ALA A 23  ? 0.2072 0.1349 0.0989 0.0133  0.0390  0.0071  23  ALA A CB  
179  N  N   . LYS A 24  ? 0.1938 0.1924 0.1499 0.0272  0.0454  0.0049  24  LYS A N   
180  C  CA  . LYS A 24  ? 0.1964 0.2192 0.1093 0.0137  0.0568  -0.0015 24  LYS A CA  
181  C  C   . LYS A 24  ? 0.2120 0.2150 0.2037 0.0266  0.0320  0.0003  24  LYS A C   
182  O  O   . LYS A 24  ? 0.2414 0.2811 0.1887 -0.0037 0.0582  0.0080  24  LYS A O   
183  C  CB  . LYS A 24  ? 0.2263 0.2215 0.1592 -0.0142 0.0614  0.0137  24  LYS A CB  
184  C  CG  . LYS A 24  ? 0.2330 0.2621 0.1896 -0.0005 0.0126  0.0000  24  LYS A CG  
185  C  CD  . LYS A 24  ? 0.4384 0.3792 0.1852 0.0267  0.0832  0.0747  24  LYS A CD  
186  C  CE  . LYS A 24  ? 0.3100 0.3237 0.2257 -0.0368 0.0421  0.0399  24  LYS A CE  
187  N  NZ  . LYS A 24  ? 0.5745 0.3125 0.3183 0.0048  0.0060  0.1084  24  LYS A NZ  
188  N  N   . GLY A 25  ? 0.2133 0.1910 0.1450 0.0494  0.0344  0.0161  25  GLY A N   
189  C  CA  . GLY A 25  ? 0.2107 0.2099 0.1659 0.0778  0.0454  0.0103  25  GLY A CA  
190  C  C   . GLY A 25  ? 0.1592 0.1881 0.1714 0.0447  0.0619  0.0195  25  GLY A C   
191  O  O   . GLY A 25  ? 0.1868 0.2120 0.1590 0.0144  0.0505  0.0140  25  GLY A O   
192  N  N   . GLU A 26  ? 0.1847 0.2370 0.1480 0.0680  0.0560  0.0412  26  GLU A N   
193  C  CA  . GLU A 26  ? 0.1947 0.2238 0.1887 0.0685  0.0412  0.0131  26  GLU A CA  
194  C  C   . GLU A 26  ? 0.1662 0.1466 0.1455 0.0133  0.0147  0.0027  26  GLU A C   
195  O  O   . GLU A 26  ? 0.1256 0.2221 0.1748 0.0146  0.0030  0.0031  26  GLU A O   
196  C  CB  . GLU A 26  ? 0.2168 0.2851 0.2608 0.1290  0.0877  0.0294  26  GLU A CB  
197  C  CG  . GLU A 26  ? 0.3075 0.3998 0.3177 0.1093  0.1217  0.0141  26  GLU A CG  
198  C  CD  . GLU A 26  ? 0.1637 0.4983 0.3986 -0.0005 0.0841  -0.0119 26  GLU A CD  
199  O  OE1 . GLU A 26  ? 0.2673 0.4657 0.4661 0.1093  0.0421  -0.0520 26  GLU A OE1 
200  O  OE2 . GLU A 26  ? 0.4074 0.6565 0.4641 0.0636  0.2538  0.1187  26  GLU A OE2 
201  N  N   . ARG A 27  ? 0.1362 0.1477 0.1402 0.0346  0.0098  -0.0038 27  ARG A N   
202  C  CA  . ARG A 27  ? 0.1184 0.1453 0.1109 0.0142  0.0020  -0.0048 27  ARG A CA  
203  C  C   . ARG A 27  ? 0.1326 0.1297 0.1012 0.0099  -0.0104 -0.0054 27  ARG A C   
204  O  O   . ARG A 27  ? 0.1360 0.1298 0.1317 0.0156  0.0215  0.0076  27  ARG A O   
205  C  CB  . ARG A 27  ? 0.1326 0.1737 0.2073 0.0390  -0.0088 0.0303  27  ARG A CB  
206  C  CG  . ARG A 27  ? 0.1947 0.2493 0.1953 0.0093  0.0465  0.0044  27  ARG A CG  
207  C  CD  . ARG A 27  ? 0.2833 0.2395 0.2136 -0.0222 0.0342  0.0000  27  ARG A CD  
208  N  NE  . ARG A 27  ? 0.2716 0.2290 0.2415 0.0230  0.0028  -0.0021 27  ARG A NE  
209  C  CZ  . ARG A 27  ? 0.1797 0.2023 0.2355 0.0346  -0.0247 0.0368  27  ARG A CZ  
210  N  NH1 . ARG A 27  ? 0.2063 0.1829 0.1601 0.0949  0.0175  0.0449  27  ARG A NH1 
211  N  NH2 . ARG A 27  ? 0.2318 0.1847 0.1832 0.0384  0.0012  -0.0109 27  ARG A NH2 
212  N  N   . GLN A 28  ? 0.1249 0.1407 0.1003 0.0298  0.0208  0.0073  28  GLN A N   
213  C  CA  . GLN A 28  ? 0.1203 0.1419 0.0976 0.0351  0.0115  -0.0115 28  GLN A CA  
214  C  C   . GLN A 28  ? 0.1062 0.0872 0.1098 0.0161  0.0073  0.0068  28  GLN A C   
215  O  O   . GLN A 28  ? 0.1299 0.1221 0.1023 0.0193  0.0031  -0.0010 28  GLN A O   
216  C  CB  . GLN A 28  ? 0.1392 0.1395 0.1037 0.0254  0.0280  0.0071  28  GLN A CB  
217  C  CG  . GLN A 28  ? 0.1516 0.1434 0.1012 0.0253  0.0379  0.0104  28  GLN A CG  
218  C  CD  . GLN A 28  ? 0.1195 0.1416 0.1061 0.0296  0.0458  0.0043  28  GLN A CD  
219  O  OE1 . GLN A 28  ? 0.1484 0.1401 0.1265 0.0353  0.0097  0.0065  28  GLN A OE1 
220  N  NE2 . GLN A 28  ? 0.1571 0.1324 0.0878 0.0136  0.0408  -0.0008 28  GLN A NE2 
221  N  N   . SER A 29  ? 0.1041 0.1120 0.0971 0.0146  0.0153  0.0041  29  SER A N   
222  C  CA  . SER A 29  ? 0.0961 0.1103 0.1064 0.0241  0.0304  -0.0006 29  SER A CA  
223  C  C   . SER A 29  ? 0.1233 0.1086 0.0989 0.0102  0.0065  0.0093  29  SER A C   
224  O  O   . SER A 29  ? 0.1152 0.1109 0.1032 0.0152  0.0044  -0.0005 29  SER A O   
225  C  CB  . SER A 29  ? 0.1395 0.1067 0.1182 0.0043  0.0044  0.0276  29  SER A CB  
226  O  OG  . SER A 29  ? 0.1238 0.1030 0.0983 0.0256  0.0070  -0.0125 29  SER A OG  
227  N  N   . PRO A 30  ? 0.1170 0.1170 0.0892 0.0141  0.0027  0.0055  30  PRO A N   
228  C  CA  . PRO A 30  ? 0.1005 0.1102 0.0949 0.0104  0.0031  -0.0094 30  PRO A CA  
229  C  C   . PRO A 30  ? 0.1014 0.1071 0.0812 0.0138  -0.0008 0.0219  30  PRO A C   
230  O  O   . PRO A 30  ? 0.1033 0.1240 0.0931 0.0133  0.0054  0.0070  30  PRO A O   
231  C  CB  . PRO A 30  ? 0.0994 0.0948 0.0915 0.0200  0.0132  0.0171  30  PRO A CB  
232  C  CG  . PRO A 30  ? 0.1488 0.1228 0.0856 0.0190  0.0120  0.0059  30  PRO A CG  
233  C  CD  . PRO A 30  ? 0.1301 0.1195 0.0927 0.0359  -0.0006 0.0030  30  PRO A CD  
234  N  N   . VAL A 31  ? 0.0965 0.1039 0.1032 -0.0086 0.0026  0.0030  31  VAL A N   
235  C  CA  . VAL A 31  ? 0.0952 0.1089 0.1085 -0.0017 -0.0183 -0.0086 31  VAL A CA  
236  C  C   . VAL A 31  ? 0.0974 0.1102 0.1021 -0.0010 -0.0120 -0.0015 31  VAL A C   
237  O  O   . VAL A 31  ? 0.1174 0.1071 0.1208 0.0082  0.0137  0.0006  31  VAL A O   
238  C  CB  . VAL A 31  ? 0.1172 0.1085 0.0807 0.0074  0.0024  0.0085  31  VAL A CB  
239  C  CG1 . VAL A 31  ? 0.1409 0.1127 0.1346 0.0256  0.0136  -0.0032 31  VAL A CG1 
240  C  CG2 . VAL A 31  ? 0.1411 0.1286 0.0886 0.0094  -0.0078 0.0140  31  VAL A CG2 
241  N  N   . ASP A 32  ? 0.1276 0.1116 0.1177 -0.0102 -0.0006 -0.0028 32  ASP A N   
242  C  CA  . ASP A 32  ? 0.1125 0.0989 0.1136 0.0017  -0.0251 0.0028  32  ASP A CA  
243  C  C   . ASP A 32  ? 0.0931 0.0927 0.1161 0.0041  -0.0048 0.0225  32  ASP A C   
244  O  O   . ASP A 32  ? 0.1146 0.1450 0.1475 0.0271  -0.0037 0.0119  32  ASP A O   
245  C  CB  . ASP A 32  ? 0.1402 0.1167 0.1597 -0.0104 0.0131  -0.0007 32  ASP A CB  
246  C  CG  . ASP A 32  ? 0.1358 0.1452 0.1620 0.0066  -0.0049 -0.0144 32  ASP A CG  
247  O  OD1 . ASP A 32  ? 0.1259 0.1082 0.1321 -0.0088 -0.0041 0.0057  32  ASP A OD1 
248  O  OD2 . ASP A 32  ? 0.1387 0.1579 0.2354 0.0076  -0.0024 -0.0223 32  ASP A OD2 
249  N  N   . ILE A 33  ? 0.1091 0.1127 0.1021 -0.0049 -0.0019 0.0007  33  ILE A N   
250  C  CA  . ILE A 33  ? 0.1315 0.1294 0.1333 0.0041  -0.0044 0.0179  33  ILE A CA  
251  C  C   . ILE A 33  ? 0.1287 0.1188 0.1578 -0.0010 -0.0078 0.0253  33  ILE A C   
252  O  O   . ILE A 33  ? 0.1541 0.1368 0.1366 -0.0089 -0.0055 0.0133  33  ILE A O   
253  C  CB  . ILE A 33  ? 0.1435 0.1344 0.0969 -0.0109 -0.0115 0.0006  33  ILE A CB  
254  C  CG1 . ILE A 33  ? 0.1093 0.1199 0.1301 -0.0159 -0.0048 0.0031  33  ILE A CG1 
255  C  CG2 . ILE A 33  ? 0.1405 0.1597 0.1168 -0.0289 -0.0348 0.0098  33  ILE A CG2 
256  C  CD1 . ILE A 33  ? 0.1457 0.1638 0.1436 -0.0434 0.0307  0.0006  33  ILE A CD1 
257  N  N   . ASP A 34  ? 0.1244 0.1486 0.1635 -0.0142 -0.0472 0.0144  34  ASP A N   
258  C  CA  . ASP A 34  ? 0.1628 0.1543 0.1558 -0.0329 -0.0144 0.0097  34  ASP A CA  
259  C  C   . ASP A 34  ? 0.1570 0.1552 0.1680 -0.0297 -0.0175 0.0080  34  ASP A C   
260  O  O   . ASP A 34  ? 0.1650 0.1745 0.1890 -0.0082 -0.0410 0.0256  34  ASP A O   
261  C  CB  . ASP A 34  ? 0.1574 0.1802 0.2351 0.0013  -0.0204 0.0430  34  ASP A CB  
262  C  CG  . ASP A 34  ? 0.2894 0.2172 0.2484 -0.0800 0.0377  -0.0032 34  ASP A CG  
263  O  OD1 . ASP A 34  ? 0.2933 0.2357 0.2847 -0.0947 -0.0344 0.0170  34  ASP A OD1 
264  O  OD2 . ASP A 34  ? 0.3388 0.5126 0.4332 -0.1489 0.0441  -0.0195 34  ASP A OD2 
265  N  N   . THR A 35  ? 0.1572 0.1563 0.1622 -0.0498 -0.0144 0.0190  35  THR A N   
266  C  CA  . THR A 35  ? 0.1744 0.2099 0.1541 -0.0292 -0.0310 0.0215  35  THR A CA  
267  C  C   . THR A 35  ? 0.1809 0.2145 0.1708 -0.0322 -0.0513 0.0292  35  THR A C   
268  O  O   . THR A 35  ? 0.2228 0.2115 0.2283 -0.0577 -0.0706 0.0511  35  THR A O   
269  C  CB  . THR A 35  ? 0.1696 0.2061 0.1693 -0.0368 -0.0063 0.0309  35  THR A CB  
270  O  OG1 . THR A 35  ? 0.2357 0.2070 0.1906 -0.0277 -0.0450 0.0171  35  THR A OG1 
271  C  CG2 . THR A 35  ? 0.1829 0.2091 0.1860 -0.0625 -0.0173 0.0513  35  THR A CG2 
272  N  N   . HIS A 36  ? 0.1823 0.2188 0.2228 -0.0142 -0.0782 0.0245  36  HIS A N   
273  C  CA  . HIS A 36  ? 0.1921 0.1884 0.2389 -0.0434 -0.0804 0.0116  36  HIS A CA  
274  C  C   . HIS A 36  ? 0.1808 0.2570 0.2305 0.0000  -0.0838 0.0125  36  HIS A C   
275  O  O   . HIS A 36  ? 0.1962 0.2732 0.2248 0.0024  -0.0718 0.0209  36  HIS A O   
276  C  CB  . HIS A 36  ? 0.2084 0.2069 0.2585 -0.1005 -0.0546 -0.0337 36  HIS A CB  
277  C  CG  . HIS A 36  ? 0.1991 0.1657 0.3161 -0.0397 -0.0313 0.0130  36  HIS A CG  
278  N  ND1 . HIS A 36  ? 0.2299 0.2901 0.2797 -0.0162 -0.0043 -0.0024 36  HIS A ND1 
279  C  CD2 . HIS A 36  ? 0.2073 0.2378 0.3485 -0.0778 0.0190  -0.0366 36  HIS A CD2 
280  C  CE1 . HIS A 36  ? 0.3203 0.3483 0.3456 0.0414  0.0049  -0.0178 36  HIS A CE1 
281  N  NE2 . HIS A 36  ? 0.3878 0.3506 0.4582 0.0344  0.0071  -0.0142 36  HIS A NE2 
282  N  N   . THR A 37  ? 0.2449 0.1905 0.2467 -0.0093 -0.0540 0.0320  37  THR A N   
283  C  CA  . THR A 37  ? 0.1795 0.2025 0.2159 -0.0344 -0.0835 0.0054  37  THR A CA  
284  C  C   . THR A 37  ? 0.1721 0.2172 0.2129 -0.0217 0.0247  0.0098  37  THR A C   
285  O  O   . THR A 37  ? 0.1967 0.2422 0.3691 -0.0172 -0.0322 0.0293  37  THR A O   
286  C  CB  . THR A 37  ? 0.3379 0.2481 0.2980 -0.0548 0.1524  0.0156  37  THR A CB  
287  O  OG1 . THR A 37  ? 0.4517 0.2662 0.3558 -0.0916 0.0706  0.0331  37  THR A OG1 
288  C  CG2 . THR A 37  ? 0.2134 0.3310 0.3152 -0.0249 0.0199  0.0210  37  THR A CG2 
289  N  N   . ALA A 38  ? 0.1595 0.1626 0.1653 -0.0203 -0.0307 0.0348  38  ALA A N   
290  C  CA  . ALA A 38  ? 0.1802 0.1692 0.1832 -0.0405 -0.0370 0.0432  38  ALA A CA  
291  C  C   . ALA A 38  ? 0.2493 0.1967 0.1755 -0.0055 -0.0425 0.0003  38  ALA A C   
292  O  O   . ALA A 38  ? 0.3725 0.2269 0.2249 -0.0405 -0.0740 -0.0017 38  ALA A O   
293  C  CB  . ALA A 38  ? 0.1872 0.1585 0.1966 -0.0043 -0.0357 0.0166  38  ALA A CB  
294  N  N   . LYS A 39  ? 0.1371 0.2125 0.2032 -0.0259 -0.0175 0.0507  39  LYS A N   
295  C  CA  . LYS A 39  ? 0.2050 0.2579 0.2181 -0.0226 -0.0258 0.0781  39  LYS A CA  
296  C  C   . LYS A 39  ? 0.2111 0.1660 0.1868 -0.0185 -0.0255 0.0445  39  LYS A C   
297  O  O   . LYS A 39  ? 0.1292 0.1886 0.1689 -0.0140 -0.0236 0.0183  39  LYS A O   
298  C  CB  . LYS A 39  ? 0.1858 0.3158 0.3540 -0.0074 0.0781  0.0668  39  LYS A CB  
299  C  CG  . LYS A 39  ? 0.3282 0.4503 0.3025 0.0146  -0.0284 -0.0133 39  LYS A CG  
300  C  CD  . LYS A 39  ? 0.3190 0.2485 0.2847 -0.0544 0.0337  0.1243  39  LYS A CD  
301  C  CE  . LYS A 39  ? 0.3138 0.3337 0.3070 -0.0850 -0.0828 0.0610  39  LYS A CE  
302  N  NZ  . LYS A 39  ? 0.3657 0.4578 0.2436 -0.2319 0.0197  0.0236  39  LYS A NZ  
303  N  N   . TYR A 40  ? 0.1474 0.2251 0.2402 0.0000  -0.0408 0.0326  40  TYR A N   
304  C  CA  . TYR A 40  ? 0.2037 0.1930 0.1874 -0.0015 -0.0395 -0.0099 40  TYR A CA  
305  C  C   . TYR A 40  ? 0.1800 0.2055 0.1850 0.0245  -0.0160 -0.0054 40  TYR A C   
306  O  O   . TYR A 40  ? 0.1824 0.2892 0.1915 0.0000  -0.0549 0.0274  40  TYR A O   
307  C  CB  . TYR A 40  ? 0.2003 0.2739 0.2172 -0.0136 -0.0160 -0.0562 40  TYR A CB  
308  C  CG  . TYR A 40  ? 0.2361 0.3452 0.2147 -0.0120 -0.0524 -0.0318 40  TYR A CG  
309  C  CD1 . TYR A 40  ? 0.2219 0.3019 0.2303 -0.0008 -0.0331 -0.0357 40  TYR A CD1 
310  C  CD2 . TYR A 40  ? 0.3052 0.5781 0.2502 0.0489  -0.0465 0.0223  40  TYR A CD2 
311  C  CE1 . TYR A 40  ? 0.2344 0.3529 0.2682 0.0200  -0.0496 -0.0149 40  TYR A CE1 
312  C  CE2 . TYR A 40  ? 0.2563 0.4453 0.2788 -0.0125 -0.0390 0.0094  40  TYR A CE2 
313  C  CZ  . TYR A 40  ? 0.2736 0.5562 0.2461 -0.0428 -0.0384 0.0610  40  TYR A CZ  
314  O  OH  . TYR A 40  ? 0.3610 0.4864 0.2325 0.0237  -0.0212 0.0649  40  TYR A OH  
315  N  N   . ASP A 41  ? 0.2129 0.2050 0.1671 0.0220  -0.0175 0.0304  41  ASP A N   
316  C  CA  . ASP A 41  ? 0.1768 0.2118 0.2095 0.0207  -0.0137 0.0104  41  ASP A CA  
317  C  C   . ASP A 41  ? 0.1856 0.2994 0.2129 0.0163  -0.0362 0.0318  41  ASP A C   
318  O  O   . ASP A 41  ? 0.2167 0.2538 0.1878 -0.0170 0.0122  0.0074  41  ASP A O   
319  C  CB  . ASP A 41  ? 0.2351 0.2111 0.2639 0.0379  0.0107  -0.0489 41  ASP A CB  
320  C  CG  . ASP A 41  ? 0.2342 0.2725 0.2944 0.1068  -0.0017 -0.0478 41  ASP A CG  
321  O  OD1 . ASP A 41  ? 0.2748 0.2976 0.3161 0.1035  -0.0038 0.0425  41  ASP A OD1 
322  O  OD2 . ASP A 41  ? 0.3131 0.3147 0.2881 0.0087  0.0553  -0.0476 41  ASP A OD2 
323  N  N   . PRO A 42  ? 0.1978 0.3244 0.2104 -0.0243 -0.0524 0.0557  42  PRO A N   
324  C  CA  . PRO A 42  ? 0.2899 0.4138 0.2078 0.0119  -0.0278 0.0410  42  PRO A CA  
325  C  C   . PRO A 42  ? 0.2915 0.3855 0.2467 -0.0335 -0.0502 0.0100  42  PRO A C   
326  O  O   . PRO A 42  ? 0.4038 0.5099 0.2917 -0.1137 -0.0551 0.1572  42  PRO A O   
327  C  CB  . PRO A 42  ? 0.3569 0.5081 0.2081 -0.0035 -0.0553 0.0276  42  PRO A CB  
328  C  CG  . PRO A 42  ? 0.3088 0.5206 0.2795 -0.0098 -0.0728 0.1044  42  PRO A CG  
329  C  CD  . PRO A 42  ? 0.2159 0.3772 0.2413 -0.0445 -0.1005 0.0593  42  PRO A CD  
330  N  N   . SER A 43  ? 0.2788 0.2973 0.2456 -0.0100 -0.0460 0.0847  43  SER A N   
331  C  CA  . SER A 43  ? 0.2669 0.2601 0.4528 -0.0109 -0.0170 0.0373  43  SER A CA  
332  C  C   . SER A 43  ? 0.2996 0.3093 0.3952 0.0057  -0.0509 0.0781  43  SER A C   
333  O  O   . SER A 43  ? 0.3961 0.2955 0.4487 -0.0120 -0.0080 0.0684  43  SER A O   
334  C  CB  . SER A 43  ? 0.4370 0.4383 0.4442 0.1081  0.0979  0.0992  43  SER A CB  
335  O  OG  . SER A 43  ? 0.3391 0.3332 0.5067 0.0821  0.0395  -0.0024 43  SER A OG  
336  N  N   . LEU A 44  ? 0.1926 0.2892 0.2601 0.0049  0.0205  0.0575  44  LEU A N   
337  C  CA  . LEU A 44  ? 0.1899 0.2675 0.2739 -0.0524 0.0252  0.0728  44  LEU A CA  
338  C  C   . LEU A 44  ? 0.3095 0.3792 0.2272 -0.0839 0.0689  -0.0379 44  LEU A C   
339  O  O   . LEU A 44  ? 0.2576 0.4466 0.2433 -0.0529 0.0790  -0.0993 44  LEU A O   
340  C  CB  . LEU A 44  ? 0.1861 0.2588 0.1984 0.0062  -0.0076 0.0153  44  LEU A CB  
341  C  CG  . LEU A 44  ? 0.1921 0.2149 0.1831 -0.0450 0.0154  -0.0176 44  LEU A CG  
342  C  CD1 . LEU A 44  ? 0.2470 0.2863 0.2204 0.0392  0.0023  0.0238  44  LEU A CD1 
343  C  CD2 . LEU A 44  ? 0.1906 0.2337 0.2165 -0.0355 -0.0003 -0.0366 44  LEU A CD2 
344  N  N   . LYS A 45  ? 0.2445 0.2723 0.2773 -0.0463 0.0640  0.0194  45  LYS A N   
345  C  CA  . LYS A 45  ? 0.2822 0.2899 0.2574 0.0447  0.1080  0.0102  45  LYS A CA  
346  C  C   . LYS A 45  ? 0.2172 0.2892 0.2239 -0.0359 0.0296  0.0295  45  LYS A C   
347  O  O   . LYS A 45  ? 0.2680 0.3188 0.1908 0.0452  0.0348  0.0108  45  LYS A O   
348  C  CB  . LYS A 45  ? 0.3422 0.2824 0.2554 -0.0046 -0.0303 0.0776  45  LYS A CB  
349  C  CG  . LYS A 45  ? 0.3219 0.4940 0.4002 0.1000  0.0340  0.0834  45  LYS A CG  
350  C  CD  . LYS A 45  ? 0.5230 0.5031 0.5487 0.1020  0.0535  0.0710  45  LYS A CD  
351  C  CE  . LYS A 45  ? 0.9996 0.4180 0.7766 0.0443  0.0227  0.2181  45  LYS A CE  
352  N  NZ  . LYS A 45  ? 1.2505 0.6119 0.5877 -0.1846 -0.2766 0.3194  45  LYS A NZ  
353  N  N   . PRO A 46  ? 0.2804 0.2870 0.2069 0.0174  0.0340  -0.0049 46  PRO A N   
354  C  CA  . PRO A 46  ? 0.2278 0.2271 0.2064 -0.0250 0.0198  -0.0540 46  PRO A CA  
355  C  C   . PRO A 46  ? 0.1899 0.1865 0.1308 -0.0093 -0.0031 -0.0010 46  PRO A C   
356  O  O   . PRO A 46  ? 0.2111 0.2172 0.1720 -0.0121 0.0237  -0.0071 46  PRO A O   
357  C  CB  . PRO A 46  ? 0.2493 0.2770 0.1940 0.0190  0.0333  -0.0190 46  PRO A CB  
358  C  CG  . PRO A 46  ? 0.2352 0.3486 0.2513 0.0579  0.0155  0.0302  46  PRO A CG  
359  C  CD  . PRO A 46  ? 0.2781 0.3136 0.2484 0.0212  0.0728  0.0775  46  PRO A CD  
360  N  N   . LEU A 47  ? 0.2289 0.2556 0.1860 -0.0250 0.0186  -0.0054 47  LEU A N   
361  C  CA  . LEU A 47  ? 0.1980 0.1831 0.2129 -0.0388 0.0340  -0.0588 47  LEU A CA  
362  C  C   . LEU A 47  ? 0.2445 0.2242 0.1996 -0.0449 0.0636  -0.0590 47  LEU A C   
363  O  O   . LEU A 47  ? 0.2714 0.2973 0.2558 -0.0329 0.0935  -0.0962 47  LEU A O   
364  C  CB  . LEU A 47  ? 0.2603 0.2554 0.2703 -0.0160 0.0203  -0.0659 47  LEU A CB  
365  C  CG  . LEU A 47  ? 0.2930 0.2300 0.2188 0.0483  0.0593  -0.0397 47  LEU A CG  
366  C  CD1 . LEU A 47  ? 0.3134 0.3323 0.2402 0.1032  0.0903  -0.0419 47  LEU A CD1 
367  C  CD2 . LEU A 47  ? 0.3253 0.2412 0.2300 0.0373  0.1251  0.0643  47  LEU A CD2 
368  N  N   . SER A 48  ? 0.1870 0.1983 0.1890 -0.0288 0.0324  -0.0183 48  SER A N   
369  C  CA  . SER A 48  ? 0.2204 0.1807 0.1468 -0.0410 0.0104  0.0040  48  SER A CA  
370  C  C   . SER A 48  ? 0.1462 0.1747 0.1662 -0.0052 0.0171  0.0010  48  SER A C   
371  O  O   . SER A 48  ? 0.2005 0.2018 0.1599 0.0315  -0.0005 -0.0249 48  SER A O   
372  C  CB  . SER A 48  ? 0.2477 0.2215 0.2116 -0.0010 0.0087  0.0065  48  SER A CB  
373  O  OG  . SER A 48  ? 0.2748 0.2594 0.2269 -0.0421 0.0051  0.0156  48  SER A OG  
374  N  N   . VAL A 49  ? 0.2124 0.2095 0.1481 0.0215  -0.0019 -0.0248 49  VAL A N   
375  C  CA  . VAL A 49  ? 0.2023 0.2143 0.1847 0.0167  -0.0062 -0.0450 49  VAL A CA  
376  C  C   . VAL A 49  ? 0.2226 0.2190 0.1829 0.0251  0.0447  -0.0476 49  VAL A C   
377  O  O   . VAL A 49  ? 0.2879 0.3043 0.2429 0.0494  0.0335  -0.1541 49  VAL A O   
378  C  CB  . VAL A 49  ? 0.2958 0.2187 0.1985 0.0175  -0.0223 -0.0292 49  VAL A CB  
379  C  CG1 . VAL A 49  ? 0.3400 0.2908 0.2851 -0.0126 -0.0799 -0.0969 49  VAL A CG1 
380  C  CG2 . VAL A 49  ? 0.2865 0.2175 0.2260 0.0313  0.0037  -0.0364 49  VAL A CG2 
381  N  N   . SER A 50  ? 0.2197 0.1974 0.2185 -0.0003 0.0285  -0.0182 50  SER A N   
382  C  CA  . SER A 50  ? 0.2111 0.2395 0.1588 -0.0030 0.0333  -0.0120 50  SER A CA  
383  C  C   . SER A 50  ? 0.1583 0.2120 0.1875 -0.0111 0.0513  -0.0093 50  SER A C   
384  O  O   . SER A 50  ? 0.2229 0.2044 0.2460 -0.0179 0.0538  -0.0256 50  SER A O   
385  C  CB  . SER A 50  ? 0.3197 0.2601 0.2676 0.0087  0.0366  -0.0450 50  SER A CB  
386  O  OG  . SER A 50  ? 0.3865 0.3977 0.2892 0.0531  0.0450  0.0553  50  SER A OG  
387  N  N   . TYR A 51  ? 0.2630 0.2312 0.1993 0.0538  0.0485  -0.0035 51  TYR A N   
388  C  CA  . TYR A 51  ? 0.1842 0.1948 0.2662 -0.0005 0.0441  -0.0408 51  TYR A CA  
389  C  C   . TYR A 51  ? 0.2342 0.2642 0.2402 -0.0419 0.0227  0.0108  51  TYR A C   
390  O  O   . TYR A 51  ? 0.2188 0.2856 0.2614 -0.0289 0.0595  -0.0035 51  TYR A O   
391  C  CB  . TYR A 51  ? 0.1856 0.2592 0.1929 0.0000  0.0599  -0.0027 51  TYR A CB  
392  C  CG  . TYR A 51  ? 0.1114 0.1913 0.1773 0.0168  -0.0077 -0.0080 51  TYR A CG  
393  C  CD1 . TYR A 51  ? 0.1893 0.1486 0.1784 0.0175  0.0211  0.0032  51  TYR A CD1 
394  C  CD2 . TYR A 51  ? 0.1897 0.1615 0.1980 -0.0154 0.0373  -0.0292 51  TYR A CD2 
395  C  CE1 . TYR A 51  ? 0.1852 0.1711 0.1735 -0.0390 0.0294  -0.0153 51  TYR A CE1 
396  C  CE2 . TYR A 51  ? 0.1655 0.1590 0.2057 0.0125  0.0148  -0.0217 51  TYR A CE2 
397  C  CZ  . TYR A 51  ? 0.1656 0.1678 0.1484 0.0024  0.0381  -0.0335 51  TYR A CZ  
398  O  OH  . TYR A 51  ? 0.1553 0.1506 0.1644 0.0109  0.0317  -0.0017 51  TYR A OH  
399  N  N   . ASP A 52  ? 0.2339 0.2488 0.2330 -0.0313 0.0564  -0.0416 52  ASP A N   
400  C  CA  . ASP A 52  ? 0.2454 0.3346 0.2657 -0.0776 0.0653  -0.0516 52  ASP A CA  
401  C  C   . ASP A 52  ? 0.3009 0.2833 0.3497 -0.0855 0.0417  -0.0120 52  ASP A C   
402  O  O   . ASP A 52  ? 0.2944 0.4199 0.3655 -0.0987 0.0944  -0.0306 52  ASP A O   
403  C  CB  . ASP A 52  ? 0.2976 0.3995 0.2352 -0.1162 0.0087  -0.0186 52  ASP A CB  
404  C  CG  . ASP A 52  ? 0.5956 0.5544 0.3896 0.0019  -0.1180 0.0573  52  ASP A CG  
405  O  OD1 . ASP A 52  ? 0.6251 0.7257 0.7114 0.0575  -0.0118 0.0247  52  ASP A OD1 
406  O  OD2 . ASP A 52  ? 0.9097 0.8787 0.5034 -0.3564 -0.1512 -0.0315 52  ASP A OD2 
407  N  N   . GLN A 53  ? 0.3513 0.2675 0.2005 -0.0807 0.0668  -0.0035 53  GLN A N   
408  C  CA  . GLN A 53  ? 0.3894 0.3257 0.1730 -0.0351 -0.0187 -0.0340 53  GLN A CA  
409  C  C   . GLN A 53  ? 0.1877 0.2307 0.1915 -0.0436 0.0140  0.0241  53  GLN A C   
410  O  O   . GLN A 53  ? 0.3025 0.2264 0.2698 -0.0487 0.0557  0.0252  53  GLN A O   
411  C  CB  . GLN A 53  ? 0.3722 0.3301 0.3041 -0.1023 0.0280  0.0786  53  GLN A CB  
412  C  CG  . GLN A 53  ? 0.5400 0.3783 0.3926 -0.0208 -0.1174 0.0564  53  GLN A CG  
413  C  CD  . GLN A 53  ? 0.7566 0.6583 0.6006 -0.1097 -0.0077 0.0883  53  GLN A CD  
414  O  OE1 . GLN A 53  ? 0.8597 0.9229 0.7005 -0.0467 -0.0320 0.1624  53  GLN A OE1 
415  N  NE2 . GLN A 53  ? 1.2072 0.9285 0.9095 -0.0626 -0.1316 0.3034  53  GLN A NE2 
416  N  N   . ALA A 54  ? 0.1998 0.1786 0.2159 -0.0071 0.0175  0.0041  54  ALA A N   
417  C  CA  . ALA A 54  ? 0.1800 0.1804 0.2009 0.0000  0.0172  0.0076  54  ALA A CA  
418  C  C   . ALA A 54  ? 0.1793 0.2289 0.1744 0.0298  0.0326  0.0076  54  ALA A C   
419  O  O   . ALA A 54  ? 0.2362 0.2696 0.2364 0.0564  0.0491  -0.0142 54  ALA A O   
420  C  CB  . ALA A 54  ? 0.2445 0.1623 0.1878 -0.0092 0.0092  -0.0124 54  ALA A CB  
421  N  N   . THR A 55  ? 0.1712 0.1800 0.1919 -0.0198 -0.0015 0.0019  55  THR A N   
422  C  CA  . THR A 55  ? 0.1735 0.2211 0.1847 -0.0421 0.0015  0.0214  55  THR A CA  
423  C  C   . THR A 55  ? 0.1389 0.1559 0.1674 -0.0445 0.0135  -0.0114 55  THR A C   
424  O  O   . THR A 55  ? 0.1911 0.1547 0.2204 0.0006  -0.0190 -0.0200 55  THR A O   
425  C  CB  . THR A 55  ? 0.1875 0.2786 0.2967 -0.0710 -0.0756 -0.0184 55  THR A CB  
426  O  OG1 . THR A 55  ? 0.4167 0.2763 0.4066 -0.0537 -0.0194 0.0337  55  THR A OG1 
427  C  CG2 . THR A 55  ? 0.1588 0.2456 0.3269 -0.0186 -0.0619 0.0982  55  THR A CG2 
428  N  N   . SER A 56  ? 0.1238 0.1685 0.1717 -0.0245 0.0026  0.0046  56  SER A N   
429  C  CA  . SER A 56  ? 0.1441 0.1558 0.1777 0.0012  -0.0249 0.0131  56  SER A CA  
430  C  C   . SER A 56  ? 0.1277 0.1281 0.1473 -0.0007 0.0044  -0.0081 56  SER A C   
431  O  O   . SER A 56  ? 0.1509 0.1675 0.2079 -0.0043 0.0196  0.0024  56  SER A O   
432  C  CB  . SER A 56  ? 0.1111 0.1624 0.2147 0.0088  -0.0197 0.0260  56  SER A CB  
433  O  OG  . SER A 56  ? 0.1337 0.1727 0.1994 -0.0065 0.0082  -0.0187 56  SER A OG  
434  N  N   . LEU A 57  ? 0.1418 0.1899 0.1421 -0.0142 -0.0322 0.0140  57  LEU A N   
435  C  CA  . LEU A 57  ? 0.1323 0.1614 0.1942 -0.0173 -0.0252 0.0104  57  LEU A CA  
436  C  C   . LEU A 57  ? 0.1495 0.1723 0.1824 -0.0089 0.0030  0.0436  57  LEU A C   
437  O  O   . LEU A 57  ? 0.1500 0.1655 0.2163 -0.0286 -0.0162 0.0131  57  LEU A O   
438  C  CB  . LEU A 57  ? 0.2129 0.1698 0.2296 -0.0048 -0.0019 0.0068  57  LEU A CB  
439  C  CG  . LEU A 57  ? 0.2127 0.2131 0.2267 0.0175  -0.0015 0.0299  57  LEU A CG  
440  C  CD1 . LEU A 57  ? 0.2971 0.1635 0.2233 0.0294  -0.0329 -0.0119 57  LEU A CD1 
441  C  CD2 . LEU A 57  ? 0.2610 0.2897 0.4542 0.0049  0.0408  0.1133  57  LEU A CD2 
442  N  N   A ARG A 58  ? 0.1752 0.1788 0.1904 -0.0737 -0.0208 0.0265  58  ARG A N   
443  N  N   B ARG A 58  ? 0.1637 0.1660 0.1509 -0.0456 -0.0142 0.0201  58  ARG A N   
444  C  CA  A ARG A 58  ? 0.1937 0.1574 0.1827 -0.0559 -0.0298 -0.0168 58  ARG A CA  
445  C  CA  B ARG A 58  ? 0.1721 0.1650 0.1195 -0.0062 0.0104  -0.0183 58  ARG A CA  
446  C  C   A ARG A 58  ? 0.1721 0.1640 0.1581 -0.0560 -0.0445 0.0137  58  ARG A C   
447  C  C   B ARG A 58  ? 0.1199 0.1540 0.1829 0.0098  -0.0184 -0.0013 58  ARG A C   
448  O  O   A ARG A 58  ? 0.1281 0.1608 0.1917 -0.0392 -0.0206 -0.0104 58  ARG A O   
449  O  O   B ARG A 58  ? 0.1057 0.1299 0.1428 -0.0141 0.0059  -0.0195 58  ARG A O   
450  C  CB  A ARG A 58  ? 0.2709 0.1847 0.1957 -0.0102 -0.0130 -0.0351 58  ARG A CB  
451  C  CB  B ARG A 58  ? 0.1887 0.1412 0.1270 -0.0243 -0.0289 -0.0228 58  ARG A CB  
452  C  CG  A ARG A 58  ? 0.3111 0.2278 0.2292 -0.0357 -0.0200 -0.0465 58  ARG A CG  
453  C  CG  B ARG A 58  ? 0.1678 0.1721 0.1161 -0.0164 -0.0278 -0.0320 58  ARG A CG  
454  C  CD  A ARG A 58  ? 0.2655 0.3084 0.2280 -0.0205 0.0335  0.0276  58  ARG A CD  
455  C  CD  B ARG A 58  ? 0.1836 0.1348 0.1294 -0.0006 -0.0355 -0.0329 58  ARG A CD  
456  N  NE  A ARG A 58  ? 0.3021 0.1984 0.2205 -0.0370 -0.0283 0.0728  58  ARG A NE  
457  N  NE  B ARG A 58  ? 0.1571 0.1233 0.1181 -0.0027 -0.0281 -0.0280 58  ARG A NE  
458  C  CZ  A ARG A 58  ? 0.1621 0.2391 0.1114 0.0388  -0.0060 -0.0518 58  ARG A CZ  
459  C  CZ  B ARG A 58  ? 0.1434 0.1508 0.1143 -0.0063 -0.0054 0.0175  58  ARG A CZ  
460  N  NH1 A ARG A 58  ? 0.3228 0.2894 0.3531 -0.0961 -0.0900 -0.0904 58  ARG A NH1 
461  N  NH1 B ARG A 58  ? 0.1601 0.1263 0.1369 0.0005  -0.0346 0.0142  58  ARG A NH1 
462  N  NH2 A ARG A 58  ? 0.3867 0.3199 0.3152 -0.0538 0.0147  -0.0776 58  ARG A NH2 
463  N  NH2 B ARG A 58  ? 0.1450 0.2030 0.1310 -0.0529 0.0137  -0.0031 58  ARG A NH2 
464  N  N   . ILE A 59  ? 0.1614 0.1427 0.1929 -0.0205 -0.0350 0.0164  59  ILE A N   
465  C  CA  . ILE A 59  ? 0.1384 0.1465 0.1854 -0.0082 -0.0296 0.0368  59  ILE A CA  
466  C  C   . ILE A 59  ? 0.1662 0.1633 0.1969 0.0151  -0.0116 0.0127  59  ILE A C   
467  O  O   . ILE A 59  ? 0.1642 0.1748 0.1752 -0.0065 -0.0346 -0.0093 59  ILE A O   
468  C  CB  . ILE A 59  ? 0.1114 0.1858 0.2617 -0.0164 -0.0144 -0.0107 59  ILE A CB  
469  C  CG1 . ILE A 59  ? 0.1392 0.1806 0.2174 -0.0326 -0.0463 0.0130  59  ILE A CG1 
470  C  CG2 . ILE A 59  ? 0.1262 0.1897 0.2169 -0.0241 -0.0275 0.0138  59  ILE A CG2 
471  C  CD1 . ILE A 59  ? 0.1904 0.1768 0.2192 -0.0248 -0.0298 0.0259  59  ILE A CD1 
472  N  N   . LEU A 60  ? 0.1428 0.1457 0.1698 0.0026  -0.0136 0.0116  60  LEU A N   
473  C  CA  . LEU A 60  ? 0.1568 0.1543 0.1975 -0.0046 -0.0010 0.0031  60  LEU A CA  
474  C  C   . LEU A 60  ? 0.1423 0.1683 0.1570 -0.0218 -0.0226 0.0159  60  LEU A C   
475  O  O   . LEU A 60  ? 0.1407 0.1640 0.2159 -0.0225 -0.0379 0.0099  60  LEU A O   
476  C  CB  . LEU A 60  ? 0.1932 0.1283 0.2373 0.0008  0.0285  -0.0049 60  LEU A CB  
477  C  CG  . LEU A 60  ? 0.2084 0.1757 0.2497 0.0275  0.0189  -0.0178 60  LEU A CG  
478  C  CD1 . LEU A 60  ? 0.2935 0.2237 0.2881 -0.0720 -0.0254 -0.0362 60  LEU A CD1 
479  C  CD2 . LEU A 60  ? 0.2142 0.1933 0.3089 0.0303  0.0419  -0.0049 60  LEU A CD2 
480  N  N   . ASN A 61  ? 0.1459 0.1509 0.1346 0.0093  0.0010  0.0024  61  ASN A N   
481  C  CA  . ASN A 61  ? 0.1471 0.1559 0.1466 0.0077  -0.0167 -0.0155 61  ASN A CA  
482  C  C   . ASN A 61  ? 0.1520 0.1969 0.1676 0.0253  -0.0080 -0.0198 61  ASN A C   
483  O  O   . ASN A 61  ? 0.1874 0.1699 0.1703 -0.0103 -0.0307 -0.0305 61  ASN A O   
484  C  CB  . ASN A 61  ? 0.1753 0.1730 0.1509 0.0166  -0.0220 0.0214  61  ASN A CB  
485  C  CG  . ASN A 61  ? 0.1412 0.1425 0.1872 -0.0038 -0.0300 -0.0368 61  ASN A CG  
486  O  OD1 . ASN A 61  ? 0.1933 0.1658 0.1764 0.0017  -0.0167 -0.0273 61  ASN A OD1 
487  N  ND2 . ASN A 61  ? 0.1560 0.1488 0.1753 0.0043  -0.0087 -0.0203 61  ASN A ND2 
488  N  N   . ASN A 62  ? 0.1500 0.1835 0.1753 -0.0071 0.0066  -0.0368 62  ASN A N   
489  C  CA  . ASN A 62  ? 0.1723 0.1448 0.1942 -0.0044 0.0026  -0.0436 62  ASN A CA  
490  C  C   . ASN A 62  ? 0.1728 0.2123 0.1798 -0.0197 -0.0070 -0.0474 62  ASN A C   
491  O  O   . ASN A 62  ? 0.2105 0.2570 0.2470 0.0399  0.0159  -0.0829 62  ASN A O   
492  C  CB  . ASN A 62  ? 0.1933 0.1700 0.2994 0.0449  0.0032  -0.0305 62  ASN A CB  
493  C  CG  . ASN A 62  ? 0.2442 0.2379 0.2644 0.0074  -0.0478 0.0359  62  ASN A CG  
494  O  OD1 . ASN A 62  ? 0.2346 0.1872 0.2269 0.0148  0.0131  -0.0165 62  ASN A OD1 
495  N  ND2 . ASN A 62  ? 0.2506 0.2308 0.2989 -0.0034 -0.0493 0.0173  62  ASN A ND2 
496  N  N   . GLY A 63  ? 0.1529 0.1768 0.1863 -0.0046 -0.0208 -0.0439 63  GLY A N   
497  C  CA  . GLY A 63  ? 0.2039 0.2275 0.1826 -0.0193 -0.0283 -0.0500 63  GLY A CA  
498  C  C   . GLY A 63  ? 0.1590 0.1635 0.1430 0.0086  0.0129  0.0000  63  GLY A C   
499  O  O   . GLY A 63  ? 0.2468 0.2217 0.1712 -0.0113 0.0141  -0.0052 63  GLY A O   
500  N  N   . HIS A 64  ? 0.1919 0.1912 0.1495 0.0190  -0.0255 -0.0287 64  HIS A N   
501  C  CA  . HIS A 64  ? 0.1852 0.1908 0.1502 0.0208  -0.0184 -0.0207 64  HIS A CA  
502  C  C   . HIS A 64  ? 0.1671 0.1744 0.1827 0.0096  0.0156  -0.0238 64  HIS A C   
503  O  O   . HIS A 64  ? 0.2152 0.2102 0.2029 -0.0315 0.0141  -0.0320 64  HIS A O   
504  C  CB  . HIS A 64  ? 0.1437 0.2087 0.1497 0.0182  0.0326  -0.0091 64  HIS A CB  
505  C  CG  . HIS A 64  ? 0.1800 0.1957 0.1877 0.0137  -0.0019 -0.0266 64  HIS A CG  
506  N  ND1 . HIS A 64  ? 0.2364 0.2353 0.2169 0.0714  -0.0143 0.0264  64  HIS A ND1 
507  C  CD2 . HIS A 64  ? 0.2325 0.2197 0.2017 0.0054  -0.0359 -0.0608 64  HIS A CD2 
508  C  CE1 . HIS A 64  ? 0.2563 0.2549 0.2346 -0.0008 0.0023  -0.0252 64  HIS A CE1 
509  N  NE2 . HIS A 64  ? 0.2372 0.2596 0.1766 -0.0081 -0.0175 -0.0131 64  HIS A NE2 
510  N  N   . ALA A 65  ? 0.1534 0.1739 0.1495 -0.0118 -0.0043 -0.0126 65  ALA A N   
511  C  CA  . ALA A 65  ? 0.1572 0.1592 0.1439 0.0085  -0.0010 -0.0041 65  ALA A CA  
512  C  C   . ALA A 65  ? 0.1651 0.1536 0.1718 0.0193  -0.0037 -0.0294 65  ALA A C   
513  O  O   . ALA A 65  ? 0.1687 0.1766 0.1606 -0.0065 -0.0205 -0.0205 65  ALA A O   
514  C  CB  . ALA A 65  ? 0.1495 0.1899 0.2046 -0.0185 -0.0171 0.0023  65  ALA A CB  
515  N  N   . PHE A 66  ? 0.1195 0.1473 0.1455 -0.0024 -0.0215 -0.0015 66  PHE A N   
516  C  CA  . PHE A 66  ? 0.1446 0.1633 0.1558 -0.0133 -0.0163 0.0023  66  PHE A CA  
517  C  C   . PHE A 66  ? 0.1448 0.1558 0.1462 -0.0151 -0.0059 0.0003  66  PHE A C   
518  O  O   . PHE A 66  ? 0.1552 0.1835 0.1682 -0.0007 -0.0384 -0.0129 66  PHE A O   
519  C  CB  . PHE A 66  ? 0.1515 0.1641 0.1660 0.0244  -0.0264 0.0003  66  PHE A CB  
520  C  CG  . PHE A 66  ? 0.0935 0.1599 0.1693 0.0377  0.0026  -0.0006 66  PHE A CG  
521  C  CD1 . PHE A 66  ? 0.0985 0.1872 0.1421 0.0120  0.0153  -0.0043 66  PHE A CD1 
522  C  CD2 . PHE A 66  ? 0.1453 0.1590 0.1753 0.0172  0.0110  0.0131  66  PHE A CD2 
523  C  CE1 . PHE A 66  ? 0.1259 0.1613 0.1570 0.0308  0.0188  -0.0008 66  PHE A CE1 
524  C  CE2 . PHE A 66  ? 0.1621 0.1628 0.1854 0.0223  0.0048  -0.0160 66  PHE A CE2 
525  C  CZ  . PHE A 66  ? 0.0939 0.1617 0.1642 0.0149  -0.0107 -0.0082 66  PHE A CZ  
526  N  N   A ASN A 67  ? 0.1195 0.1685 0.1757 -0.0184 -0.0087 0.0320  67  ASN A N   
527  N  N   B ASN A 67  ? 0.1132 0.1502 0.1893 0.0038  -0.0142 0.0296  67  ASN A N   
528  C  CA  A ASN A 67  ? 0.1509 0.1836 0.1876 -0.0188 -0.0185 0.0351  67  ASN A CA  
529  C  CA  B ASN A 67  ? 0.1337 0.1831 0.1639 -0.0166 -0.0131 0.0432  67  ASN A CA  
530  C  C   A ASN A 67  ? 0.1197 0.1762 0.1938 0.0379  -0.0155 0.0183  67  ASN A C   
531  C  C   B ASN A 67  ? 0.1410 0.1650 0.1793 -0.0255 -0.0066 0.0153  67  ASN A C   
532  O  O   A ASN A 67  ? 0.1116 0.1626 0.2111 0.0132  -0.0277 -0.0054 67  ASN A O   
533  O  O   B ASN A 67  ? 0.1375 0.1565 0.1254 0.0027  -0.0077 0.0077  67  ASN A O   
534  C  CB  A ASN A 67  ? 0.1678 0.2078 0.2757 0.0212  -0.0091 0.0038  67  ASN A CB  
535  C  CB  B ASN A 67  ? 0.1500 0.2333 0.1471 -0.0086 0.0161  -0.0019 67  ASN A CB  
536  C  CG  A ASN A 67  ? 0.2021 0.2305 0.3052 -0.0511 0.0005  -0.0443 67  ASN A CG  
537  C  CG  B ASN A 67  ? 0.1624 0.1633 0.2413 0.0335  0.0168  -0.0188 67  ASN A CG  
538  O  OD1 A ASN A 67  ? 0.3021 0.2696 0.3357 0.0063  -0.0103 -0.0542 67  ASN A OD1 
539  O  OD1 B ASN A 67  ? 0.2201 0.2319 0.2300 0.0276  0.0122  -0.0465 67  ASN A OD1 
540  N  ND2 A ASN A 67  ? 0.1321 0.2238 0.2750 -0.0070 -0.0286 -0.0666 67  ASN A ND2 
541  N  ND2 B ASN A 67  ? 0.2939 0.2405 0.2529 0.0307  -0.0597 0.0628  67  ASN A ND2 
542  N  N   . VAL A 68  ? 0.1271 0.1109 0.1685 -0.0087 0.0023  0.0126  68  VAL A N   
543  C  CA  . VAL A 68  ? 0.1326 0.1579 0.1660 0.0000  -0.0026 0.0489  68  VAL A CA  
544  C  C   . VAL A 68  ? 0.1594 0.1560 0.1829 -0.0059 -0.0452 0.0230  68  VAL A C   
545  O  O   . VAL A 68  ? 0.1270 0.1592 0.2127 -0.0031 -0.0234 0.0174  68  VAL A O   
546  C  CB  . VAL A 68  ? 0.1199 0.1459 0.1687 -0.0052 -0.0177 0.0261  68  VAL A CB  
547  C  CG1 . VAL A 68  ? 0.1423 0.2230 0.1958 -0.0260 0.0109  0.0410  68  VAL A CG1 
548  C  CG2 . VAL A 68  ? 0.1323 0.1843 0.2188 0.0331  0.0015  0.0130  68  VAL A CG2 
549  N  N   A GLU A 69  ? 0.1272 0.1477 0.1116 0.0188  0.0168  -0.0116 69  GLU A N   
550  N  N   B GLU A 69  ? 0.1638 0.1524 0.2035 -0.0105 -0.0137 0.0170  69  GLU A N   
551  C  CA  A GLU A 69  ? 0.1506 0.1348 0.1170 -0.0006 -0.0020 -0.0097 69  GLU A CA  
552  C  CA  B GLU A 69  ? 0.1367 0.1678 0.1723 0.0157  0.0311  -0.0124 69  GLU A CA  
553  C  C   A GLU A 69  ? 0.1076 0.1597 0.1234 -0.0296 -0.0206 -0.0133 69  GLU A C   
554  C  C   B GLU A 69  ? 0.1499 0.1788 0.1563 -0.0241 -0.0403 0.0081  69  GLU A C   
555  O  O   A GLU A 69  ? 0.1059 0.1179 0.0642 -0.0143 -0.0015 -0.0010 69  GLU A O   
556  O  O   B GLU A 69  ? 0.1994 0.1010 0.2500 -0.0164 -0.0105 -0.0049 69  GLU A O   
557  C  CB  A GLU A 69  ? 0.1012 0.1631 0.0931 -0.0171 -0.0088 -0.0071 69  GLU A CB  
558  C  CB  B GLU A 69  ? 0.2215 0.1736 0.2239 0.0346  -0.0395 -0.0339 69  GLU A CB  
559  C  CG  A GLU A 69  ? 0.2084 0.1106 0.1608 -0.0068 0.0522  -0.0114 69  GLU A CG  
560  C  CG  B GLU A 69  ? 0.3941 0.3118 0.2413 0.0502  0.0167  0.0114  69  GLU A CG  
561  C  CD  A GLU A 69  ? 0.2346 0.2355 0.1377 0.0035  0.0017  -0.0333 69  GLU A CD  
562  C  CD  B GLU A 69  ? 0.2037 0.1994 0.3068 -0.0021 -0.0071 -0.1218 69  GLU A CD  
563  O  OE1 A GLU A 69  ? 0.3059 0.2242 0.1606 0.0280  0.0293  -0.0027 69  GLU A OE1 
564  O  OE1 B GLU A 69  ? 0.1850 0.2371 0.1739 -0.0772 0.0289  0.0313  69  GLU A OE1 
565  O  OE2 A GLU A 69  ? 0.2951 0.2475 0.2388 0.0077  0.0346  0.0162  69  GLU A OE2 
566  O  OE2 B GLU A 69  ? 0.3400 0.2260 0.2192 0.0260  0.0423  -0.0298 69  GLU A OE2 
567  N  N   . PHE A 70  ? 0.1673 0.1497 0.1596 -0.0119 -0.0163 0.0172  70  PHE A N   
568  C  CA  . PHE A 70  ? 0.1513 0.1493 0.1536 -0.0265 0.0023  -0.0076 70  PHE A CA  
569  C  C   . PHE A 70  ? 0.1398 0.1489 0.1574 -0.0078 0.0028  -0.0131 70  PHE A C   
570  O  O   . PHE A 70  ? 0.1777 0.1644 0.2125 -0.0078 0.0164  -0.0197 70  PHE A O   
571  C  CB  . PHE A 70  ? 0.1375 0.1438 0.1737 -0.0294 -0.0010 0.0211  70  PHE A CB  
572  C  CG  . PHE A 70  ? 0.1188 0.1558 0.1714 -0.0207 0.0074  -0.0097 70  PHE A CG  
573  C  CD1 . PHE A 70  ? 0.1678 0.1416 0.2091 -0.0131 -0.0308 -0.0001 70  PHE A CD1 
574  C  CD2 . PHE A 70  ? 0.1863 0.1473 0.1429 -0.0038 0.0170  -0.0125 70  PHE A CD2 
575  C  CE1 . PHE A 70  ? 0.1480 0.1450 0.1951 -0.0135 -0.0229 -0.0204 70  PHE A CE1 
576  C  CE2 . PHE A 70  ? 0.1640 0.1506 0.1646 -0.0161 -0.0129 0.0043  70  PHE A CE2 
577  C  CZ  . PHE A 70  ? 0.1547 0.1188 0.1532 -0.0174 -0.0239 -0.0037 70  PHE A CZ  
578  N  N   . ASP A 71  ? 0.2233 0.1509 0.2002 -0.0220 0.0186  0.0148  71  ASP A N   
579  C  CA  . ASP A 71  ? 0.1989 0.1578 0.1888 -0.0035 0.0266  -0.0162 71  ASP A CA  
580  C  C   . ASP A 71  ? 0.2601 0.1247 0.2267 0.0124  -0.0006 -0.0006 71  ASP A C   
581  O  O   . ASP A 71  ? 0.3300 0.2205 0.2205 -0.0138 0.0074  -0.0206 71  ASP A O   
582  C  CB  . ASP A 71  ? 0.2560 0.1680 0.3093 -0.0073 0.1289  0.0020  71  ASP A CB  
583  C  CG  . ASP A 71  ? 0.3601 0.1624 0.3873 -0.0430 0.1401  -0.0127 71  ASP A CG  
584  O  OD1 . ASP A 71  ? 0.3612 0.1387 0.3776 -0.0496 0.0549  -0.0037 71  ASP A OD1 
585  O  OD2 . ASP A 71  ? 0.5346 0.2545 0.6328 -0.0671 0.2793  0.0077  71  ASP A OD2 
586  N  N   . ASP A 72  ? 0.2104 0.1109 0.2545 -0.0201 -0.0142 -0.0027 72  ASP A N   
587  C  CA  . ASP A 72  ? 0.2321 0.1689 0.2071 0.0463  -0.0322 -0.0588 72  ASP A CA  
588  C  C   . ASP A 72  ? 0.3109 0.1914 0.3043 -0.0102 0.0416  -0.0264 72  ASP A C   
589  O  O   . ASP A 72  ? 0.3384 0.1780 0.3352 -0.0119 -0.0549 -0.0196 72  ASP A O   
590  C  CB  . ASP A 72  ? 0.2064 0.1887 0.2640 0.0216  -0.0458 -0.0604 72  ASP A CB  
591  C  CG  . ASP A 72  ? 0.2244 0.2166 0.2504 -0.0500 -0.0162 -0.0046 72  ASP A CG  
592  O  OD1 . ASP A 72  ? 0.2088 0.2154 0.2633 -0.0507 -0.0153 -0.0507 72  ASP A OD1 
593  O  OD2 . ASP A 72  ? 0.2461 0.1941 0.3436 -0.0028 0.0163  -0.0299 72  ASP A OD2 
594  N  N   . SER A 73  ? 0.3088 0.1632 0.2576 0.0037  -0.0255 0.0189  73  SER A N   
595  C  CA  . SER A 73  ? 0.4075 0.1448 0.2831 0.0377  -0.0386 0.0000  73  SER A CA  
596  C  C   . SER A 73  ? 0.4808 0.1990 0.2906 0.0212  -0.0041 0.0307  73  SER A C   
597  O  O   . SER A 73  ? 0.3422 0.1757 0.3068 -0.0190 0.0099  0.0120  73  SER A O   
598  C  CB  . SER A 73  ? 0.3919 0.1915 0.4532 -0.0621 0.0174  -0.0010 73  SER A CB  
599  O  OG  . SER A 73  ? 0.3623 0.1764 0.4126 -0.0640 -0.0335 0.0010  73  SER A OG  
600  N  N   . GLN A 74  ? 0.4762 0.2089 0.2910 -0.0339 -0.0384 0.0315  74  GLN A N   
601  C  CA  . GLN A 74  ? 0.4031 0.2381 0.3005 0.0485  -0.0034 -0.0261 74  GLN A CA  
602  C  C   . GLN A 74  ? 0.3750 0.3307 0.3138 0.0024  -0.0074 0.0165  74  GLN A C   
603  O  O   . GLN A 74  ? 0.3009 0.2152 0.3102 0.0603  0.0057  -0.0291 74  GLN A O   
604  C  CB  . GLN A 74  ? 0.4494 0.2212 0.2689 -0.0597 -0.0083 0.0822  74  GLN A CB  
605  C  CG  . GLN A 74  ? 0.4775 0.2788 0.3698 -0.0815 0.0080  -0.0057 74  GLN A CG  
606  C  CD  . GLN A 74  ? 0.4016 0.3576 0.4327 -0.1286 -0.0930 -0.0819 74  GLN A CD  
607  O  OE1 . GLN A 74  ? 0.7548 0.6011 0.4442 -0.1741 -0.0048 0.0027  74  GLN A OE1 
608  N  NE2 . GLN A 74  ? 0.3318 0.5623 0.4783 0.1384  -0.0121 -0.0399 74  GLN A NE2 
609  N  N   . ASP A 75  ? 0.3388 0.2904 0.3443 0.0857  -0.0277 -0.0732 75  ASP A N   
610  C  CA  . ASP A 75  ? 0.3418 0.2820 0.2949 0.0436  -0.0175 -0.0110 75  ASP A CA  
611  C  C   . ASP A 75  ? 0.4165 0.3264 0.3034 0.0710  0.1096  0.0806  75  ASP A C   
612  O  O   . ASP A 75  ? 0.4484 0.4063 0.2745 0.0168  0.0802  -0.0428 75  ASP A O   
613  C  CB  . ASP A 75  ? 0.3307 0.3476 0.2836 0.0566  -0.0421 -0.0329 75  ASP A CB  
614  C  CG  . ASP A 75  ? 0.3596 0.3447 0.3481 -0.0728 -0.0381 0.0179  75  ASP A CG  
615  O  OD1 . ASP A 75  ? 0.4599 0.3472 0.3946 -0.0829 0.1116  0.0317  75  ASP A OD1 
616  O  OD2 . ASP A 75  ? 0.6312 0.5080 0.4262 -0.0161 -0.1330 0.0816  75  ASP A OD2 
617  N  N   . LYS A 76  ? 0.2824 0.2239 0.2964 -0.0381 0.0353  -0.0571 76  LYS A N   
618  C  CA  . LYS A 76  ? 0.2910 0.2669 0.4721 -0.0399 0.0339  -0.0993 76  LYS A CA  
619  C  C   . LYS A 76  ? 0.4853 0.3822 0.5408 -0.2087 0.0278  -0.0137 76  LYS A C   
620  O  O   . LYS A 76  ? 0.4271 0.5896 0.6215 -0.0640 0.0654  -0.0938 76  LYS A O   
621  C  CB  . LYS A 76  ? 0.2617 0.2558 0.4700 -0.0324 0.0326  -0.1376 76  LYS A CB  
622  C  CG  . LYS A 76  ? 0.3671 0.2973 0.5656 -0.0763 -0.0245 -0.0125 76  LYS A CG  
623  C  CD  . LYS A 76  ? 0.4354 0.3975 0.5030 0.0684  -0.0329 0.0592  76  LYS A CD  
624  C  CE  . LYS A 76  ? 0.4034 0.4927 0.4718 0.0143  0.1061  0.0357  76  LYS A CE  
625  N  NZ  . LYS A 76  ? 0.4564 0.2336 0.3506 0.0864  -0.0395 -0.0395 76  LYS A NZ  
626  N  N   . ALA A 77  ? 0.2700 0.2949 0.4469 -0.0219 0.1312  -0.0329 77  ALA A N   
627  C  CA  . ALA A 77  ? 0.1856 0.2928 0.2831 -0.0028 0.0388  -0.0231 77  ALA A CA  
628  C  C   . ALA A 77  ? 0.1958 0.2404 0.1811 0.0287  0.0646  -0.0020 77  ALA A C   
629  O  O   . ALA A 77  ? 0.2109 0.3555 0.2321 0.0662  0.0666  -0.0085 77  ALA A O   
630  C  CB  . ALA A 77  ? 0.2012 0.3276 0.3176 0.1023  -0.0046 -0.0675 77  ALA A CB  
631  N  N   . VAL A 78  ? 0.1495 0.1964 0.2185 -0.0197 0.0326  -0.0043 78  VAL A N   
632  C  CA  . VAL A 78  ? 0.1590 0.1974 0.2391 -0.0019 0.0048  -0.0186 78  VAL A CA  
633  C  C   . VAL A 78  ? 0.1921 0.2082 0.2032 0.0184  0.0201  -0.0428 78  VAL A C   
634  O  O   . VAL A 78  ? 0.2221 0.1823 0.2090 0.0015  0.0570  -0.0346 78  VAL A O   
635  C  CB  . VAL A 78  ? 0.2291 0.2236 0.3413 0.0086  -0.0522 0.0062  78  VAL A CB  
636  C  CG1 . VAL A 78  ? 0.2811 0.1915 0.4509 -0.0430 0.0469  -0.0299 78  VAL A CG1 
637  C  CG2 . VAL A 78  ? 0.2486 0.2949 0.2982 -0.0271 -0.0041 0.0245  78  VAL A CG2 
638  N  N   . LEU A 79  ? 0.1605 0.1319 0.1779 -0.0017 0.0081  -0.0054 79  LEU A N   
639  C  CA  . LEU A 79  ? 0.2008 0.1603 0.1532 -0.0073 -0.0046 -0.0201 79  LEU A CA  
640  C  C   . LEU A 79  ? 0.1750 0.1579 0.1622 -0.0074 0.0010  -0.0237 79  LEU A C   
641  O  O   . LEU A 79  ? 0.1942 0.1768 0.1987 0.0231  -0.0074 -0.0434 79  LEU A O   
642  C  CB  . LEU A 79  ? 0.2197 0.2062 0.1775 -0.0252 0.0476  -0.0288 79  LEU A CB  
643  C  CG  . LEU A 79  ? 0.2133 0.1748 0.1836 -0.0092 0.0603  0.0015  79  LEU A CG  
644  C  CD1 . LEU A 79  ? 0.3009 0.2082 0.1617 -0.0144 0.0582  -0.0143 79  LEU A CD1 
645  C  CD2 . LEU A 79  ? 0.1976 0.1763 0.1669 -0.0305 -0.0024 0.0041  79  LEU A CD2 
646  N  N   . LYS A 80  ? 0.1836 0.1795 0.1824 0.0052  -0.0121 -0.0118 80  LYS A N   
647  C  CA  . LYS A 80  ? 0.2012 0.1653 0.2193 -0.0015 -0.0397 -0.0152 80  LYS A CA  
648  C  C   . LYS A 80  ? 0.2127 0.1933 0.1206 0.0155  0.0089  -0.0097 80  LYS A C   
649  O  O   . LYS A 80  ? 0.2136 0.1960 0.1730 -0.0089 0.0034  -0.0372 80  LYS A O   
650  C  CB  . LYS A 80  ? 0.2624 0.2127 0.2728 0.0474  0.0115  0.0408  80  LYS A CB  
651  C  CG  . LYS A 80  ? 0.3023 0.2527 0.2287 0.0148  0.0107  0.0261  80  LYS A CG  
652  C  CD  . LYS A 80  ? 0.5059 0.3109 0.2633 0.0384  0.0416  0.0665  80  LYS A CD  
653  N  N   . GLY A 81  ? 0.1745 0.1872 0.1655 -0.0086 -0.0111 -0.0105 81  GLY A N   
654  C  CA  . GLY A 81  ? 0.2412 0.1921 0.1699 -0.0680 -0.0454 0.0247  81  GLY A CA  
655  C  C   . GLY A 81  ? 0.2109 0.2089 0.1418 -0.0634 -0.0153 -0.0015 81  GLY A C   
656  O  O   . GLY A 81  ? 0.2165 0.1971 0.1642 0.0100  0.0318  -0.0103 81  GLY A O   
657  N  N   . GLY A 82  ? 0.2865 0.1996 0.1919 -0.0335 0.0163  -0.0057 82  GLY A N   
658  C  CA  . GLY A 82  ? 0.3573 0.2115 0.2229 -0.0165 0.0627  0.0102  82  GLY A CA  
659  C  C   . GLY A 82  ? 0.2481 0.2077 0.1917 -0.0156 0.0027  0.0167  82  GLY A C   
660  O  O   . GLY A 82  ? 0.3021 0.2998 0.2239 -0.0219 -0.0727 0.0148  82  GLY A O   
661  N  N   . PRO A 83  ? 0.2506 0.1653 0.1764 -0.0273 -0.0212 0.0046  83  PRO A N   
662  C  CA  . PRO A 83  ? 0.1902 0.1543 0.1939 -0.0397 -0.0131 0.0460  83  PRO A CA  
663  C  C   . PRO A 83  ? 0.2120 0.1958 0.2206 0.0000  -0.0038 0.0115  83  PRO A C   
664  O  O   . PRO A 83  ? 0.2226 0.2099 0.2621 -0.0104 0.0344  0.0174  83  PRO A O   
665  C  CB  . PRO A 83  ? 0.1951 0.1714 0.2018 -0.0089 0.0221  0.0401  83  PRO A CB  
666  C  CG  . PRO A 83  ? 0.1509 0.1726 0.1764 -0.0460 0.0032  0.0209  83  PRO A CG  
667  C  CD  . PRO A 83  ? 0.2312 0.1766 0.1444 0.0149  0.0109  0.0115  83  PRO A CD  
668  N  N   . LEU A 84  ? 0.1705 0.1527 0.1346 0.0120  -0.0259 0.0179  84  LEU A N   
669  C  CA  . LEU A 84  ? 0.2009 0.1277 0.1574 0.0168  -0.0113 0.0129  84  LEU A CA  
670  C  C   . LEU A 84  ? 0.2063 0.1710 0.1660 0.0023  0.0165  0.0399  84  LEU A C   
671  O  O   . LEU A 84  ? 0.2102 0.1705 0.1621 -0.0024 0.0006  0.0253  84  LEU A O   
672  C  CB  . LEU A 84  ? 0.1956 0.1387 0.1407 0.0013  -0.0174 0.0260  84  LEU A CB  
673  C  CG  . LEU A 84  ? 0.1865 0.1428 0.1269 0.0080  -0.0031 0.0269  84  LEU A CG  
674  C  CD1 . LEU A 84  ? 0.1669 0.1624 0.1929 0.0116  0.0125  0.0307  84  LEU A CD1 
675  C  CD2 . LEU A 84  ? 0.1843 0.1190 0.1459 0.0296  0.0241  0.0228  84  LEU A CD2 
676  N  N   . ASP A 85  ? 0.2068 0.1601 0.1804 0.0353  0.0032  0.0260  85  ASP A N   
677  C  CA  . ASP A 85  ? 0.2269 0.1635 0.2354 0.0223  0.0104  0.0012  85  ASP A CA  
678  C  C   . ASP A 85  ? 0.2802 0.1680 0.2251 -0.0027 -0.0221 -0.0052 85  ASP A C   
679  O  O   . ASP A 85  ? 0.3192 0.2971 0.2071 0.0149  -0.0043 0.0208  85  ASP A O   
680  C  CB  . ASP A 85  ? 0.2495 0.2535 0.3003 0.0623  -0.0054 0.0017  85  ASP A CB  
681  C  CG  . ASP A 85  ? 0.3280 0.3510 0.3578 0.0452  -0.0307 -0.0003 85  ASP A CG  
682  O  OD1 . ASP A 85  ? 0.3975 0.4527 0.2845 0.0115  0.0310  0.0164  85  ASP A OD1 
683  O  OD2 . ASP A 85  ? 0.3307 0.4200 0.3400 -0.0750 -0.0074 -0.0612 85  ASP A OD2 
684  N  N   . GLY A 86  ? 0.3023 0.2561 0.2576 -0.0304 0.0189  -0.0263 86  GLY A N   
685  C  CA  . GLY A 86  ? 0.2043 0.2272 0.2416 0.0181  -0.0186 -0.0031 86  GLY A CA  
686  C  C   . GLY A 86  ? 0.2222 0.2260 0.2280 0.0182  -0.0066 -0.0278 86  GLY A C   
687  O  O   . GLY A 86  ? 0.2461 0.2644 0.3402 -0.0185 0.0244  -0.0804 86  GLY A O   
688  N  N   A THR A 87  ? 0.2105 0.2010 0.2172 -0.0283 0.0038  0.0198  87  THR A N   
689  N  N   B THR A 87  ? 0.2011 0.1858 0.2045 -0.0166 0.0100  0.0163  87  THR A N   
690  C  CA  A THR A 87  ? 0.2402 0.2151 0.2019 0.0062  -0.0153 0.0199  87  THR A CA  
691  C  CA  B THR A 87  ? 0.2319 0.1628 0.1829 0.0093  -0.0233 0.0000  87  THR A CA  
692  C  C   A THR A 87  ? 0.1813 0.1421 0.1807 0.0286  0.0074  -0.0124 87  THR A C   
693  C  C   B THR A 87  ? 0.1908 0.1368 0.1660 0.0346  0.0020  -0.0131 87  THR A C   
694  O  O   A THR A 87  ? 0.1412 0.1152 0.1684 0.0008  0.0108  -0.0010 87  THR A O   
695  O  O   B THR A 87  ? 0.1579 0.1252 0.1353 -0.0026 -0.0023 0.0041  87  THR A O   
696  C  CB  A THR A 87  ? 0.2599 0.2273 0.2680 -0.0043 -0.0684 0.0732  87  THR A CB  
697  C  CB  B THR A 87  ? 0.2272 0.2066 0.1703 0.0048  -0.0228 -0.0182 87  THR A CB  
698  O  OG1 A THR A 87  ? 0.2442 0.2662 0.2045 -0.0076 0.0218  0.0553  87  THR A OG1 
699  O  OG1 B THR A 87  ? 0.2522 0.1511 0.2017 -0.0619 0.0130  0.0019  87  THR A OG1 
700  C  CG2 A THR A 87  ? 0.2515 0.2158 0.1938 -0.0051 0.0883  0.0331  87  THR A CG2 
701  C  CG2 B THR A 87  ? 0.2161 0.1795 0.1773 0.0003  -0.0383 -0.0085 87  THR A CG2 
702  N  N   . TYR A 88  ? 0.1676 0.1263 0.1389 0.0149  0.0062  0.0137  88  TYR A N   
703  C  CA  . TYR A 88  ? 0.1647 0.1498 0.1276 -0.0114 0.0000  -0.0060 88  TYR A CA  
704  C  C   . TYR A 88  ? 0.1721 0.1371 0.1518 -0.0021 0.0080  0.0040  88  TYR A C   
705  O  O   . TYR A 88  ? 0.1868 0.1996 0.2060 -0.0043 0.0182  -0.0373 88  TYR A O   
706  C  CB  . TYR A 88  ? 0.1562 0.1267 0.1474 0.0031  0.0174  0.0063  88  TYR A CB  
707  C  CG  . TYR A 88  ? 0.1506 0.0908 0.1308 0.0086  0.0114  0.0099  88  TYR A CG  
708  C  CD1 . TYR A 88  ? 0.1364 0.1392 0.1456 -0.0209 -0.0037 0.0068  88  TYR A CD1 
709  C  CD2 . TYR A 88  ? 0.1376 0.0926 0.1441 -0.0096 0.0153  0.0114  88  TYR A CD2 
710  C  CE1 . TYR A 88  ? 0.1524 0.1450 0.1590 0.0171  0.0012  0.0130  88  TYR A CE1 
711  C  CE2 . TYR A 88  ? 0.1193 0.1159 0.1344 0.0003  -0.0007 0.0006  88  TYR A CE2 
712  C  CZ  . TYR A 88  ? 0.1308 0.0960 0.1434 0.0154  -0.0048 0.0118  88  TYR A CZ  
713  O  OH  . TYR A 88  ? 0.1452 0.1190 0.1523 0.0205  -0.0138 0.0087  88  TYR A OH  
714  N  N   A ARG A 89  ? 0.1513 0.0971 0.1650 -0.0152 0.0054  0.0269  89  ARG A N   
715  N  N   B ARG A 89  ? 0.1508 0.0973 0.1644 -0.0185 0.0059  0.0258  89  ARG A N   
716  C  CA  A ARG A 89  ? 0.1558 0.1369 0.1777 -0.0208 -0.0007 0.0284  89  ARG A CA  
717  C  CA  B ARG A 89  ? 0.1520 0.1184 0.1723 -0.0331 -0.0087 0.0126  89  ARG A CA  
718  C  C   A ARG A 89  ? 0.1280 0.1116 0.1367 -0.0266 0.0043  0.0080  89  ARG A C   
719  C  C   B ARG A 89  ? 0.1301 0.1125 0.1371 -0.0275 0.0054  0.0060  89  ARG A C   
720  O  O   A ARG A 89  ? 0.1520 0.0913 0.1592 0.0063  0.0214  0.0116  89  ARG A O   
721  O  O   B ARG A 89  ? 0.1511 0.0938 0.1610 0.0012  0.0219  0.0103  89  ARG A O   
722  C  CB  A ARG A 89  ? 0.1849 0.1301 0.2442 -0.0088 0.0113  0.0138  89  ARG A CB  
723  C  CB  B ARG A 89  ? 0.1513 0.0918 0.2249 -0.0274 0.0491  0.0098  89  ARG A CB  
724  C  CG  A ARG A 89  ? 0.1694 0.2373 0.1915 0.0242  0.0142  0.0680  89  ARG A CG  
725  C  CG  B ARG A 89  ? 0.1149 0.1447 0.2903 -0.0489 -0.0192 -0.0340 89  ARG A CG  
726  C  CD  A ARG A 89  ? 0.2727 0.1843 0.3506 -0.0813 0.0132  0.0461  89  ARG A CD  
727  C  CD  B ARG A 89  ? 0.2637 0.1614 0.2434 -0.0816 -0.0489 -0.0348 89  ARG A CD  
728  N  NE  A ARG A 89  ? 0.2797 0.2054 0.3016 -0.0456 0.0010  0.0362  89  ARG A NE  
729  N  NE  B ARG A 89  ? 0.2614 0.1818 0.2675 -0.0793 -0.0111 0.0199  89  ARG A NE  
730  C  CZ  A ARG A 89  ? 0.3068 0.2156 0.3192 -0.1264 -0.0680 0.0261  89  ARG A CZ  
731  C  CZ  B ARG A 89  ? 0.3021 0.1825 0.2822 -0.0714 -0.0724 -0.0041 89  ARG A CZ  
732  N  NH1 A ARG A 89  ? 0.3310 0.1789 0.3181 -0.0804 -0.0751 0.0621  89  ARG A NH1 
733  N  NH1 B ARG A 89  ? 0.2969 0.1369 0.2854 -0.0326 -0.0825 0.0038  89  ARG A NH1 
734  N  NH2 A ARG A 89  ? 0.3213 0.2734 0.2186 -0.0417 -0.0443 -0.0208 89  ARG A NH2 
735  N  NH2 B ARG A 89  ? 0.2522 0.1922 0.1991 -0.0967 0.0355  0.0361  89  ARG A NH2 
736  N  N   . LEU A 90  ? 0.1416 0.1289 0.1491 -0.0133 0.0027  0.0040  90  LEU A N   
737  C  CA  . LEU A 90  ? 0.1551 0.1259 0.1583 0.0149  -0.0027 -0.0171 90  LEU A CA  
738  C  C   . LEU A 90  ? 0.1373 0.1084 0.1463 -0.0133 -0.0021 -0.0087 90  LEU A C   
739  O  O   . LEU A 90  ? 0.1450 0.1522 0.1808 -0.0240 0.0038  -0.0010 90  LEU A O   
740  C  CB  . LEU A 90  ? 0.1671 0.1243 0.1599 0.0031  -0.0003 -0.0243 90  LEU A CB  
741  C  CG  . LEU A 90  ? 0.1301 0.1384 0.2009 0.0063  0.0031  -0.0059 90  LEU A CG  
742  C  CD1 . LEU A 90  ? 0.1471 0.1520 0.1926 0.0019  0.0035  -0.0040 90  LEU A CD1 
743  C  CD2 . LEU A 90  ? 0.1635 0.1595 0.1940 0.0086  0.0397  -0.0331 90  LEU A CD2 
744  N  N   . ILE A 91  ? 0.1340 0.1197 0.1531 0.0108  -0.0214 -0.0048 91  ILE A N   
745  C  CA  . ILE A 91  ? 0.1272 0.1351 0.1441 0.0081  -0.0120 -0.0035 91  ILE A CA  
746  C  C   . ILE A 91  ? 0.1342 0.1109 0.1919 -0.0087 -0.0148 0.0078  91  ILE A C   
747  O  O   . ILE A 91  ? 0.1290 0.1134 0.1658 0.0038  -0.0012 -0.0100 91  ILE A O   
748  C  CB  . ILE A 91  ? 0.1339 0.1109 0.1456 0.0153  -0.0163 -0.0207 91  ILE A CB  
749  C  CG1 . ILE A 91  ? 0.2063 0.1621 0.1969 0.0364  -0.0588 -0.0509 91  ILE A CG1 
750  C  CG2 . ILE A 91  ? 0.1463 0.1288 0.2061 0.0088  -0.0241 -0.0107 91  ILE A CG2 
751  C  CD1 . ILE A 91  ? 0.2511 0.1933 0.2402 0.0331  -0.0114 -0.0560 91  ILE A CD1 
752  N  N   . GLN A 92  ? 0.1312 0.1195 0.1572 -0.0164 -0.0135 0.0203  92  GLN A N   
753  C  CA  . GLN A 92  ? 0.1533 0.1000 0.1594 -0.0074 -0.0238 -0.0098 92  GLN A CA  
754  C  C   . GLN A 92  ? 0.1358 0.1109 0.1563 -0.0071 -0.0350 -0.0109 92  GLN A C   
755  O  O   . GLN A 92  ? 0.1191 0.1042 0.1747 -0.0083 -0.0175 -0.0099 92  GLN A O   
756  C  CB  . GLN A 92  ? 0.1595 0.1357 0.1669 -0.0181 -0.0080 -0.0017 92  GLN A CB  
757  C  CG  . GLN A 92  ? 0.1684 0.1583 0.2010 -0.0355 -0.0017 -0.0155 92  GLN A CG  
758  C  CD  . GLN A 92  ? 0.1737 0.1621 0.2012 -0.0315 0.0362  -0.0221 92  GLN A CD  
759  O  OE1 . GLN A 92  ? 0.1685 0.1696 0.2327 -0.0136 0.0000  -0.0399 92  GLN A OE1 
760  N  NE2 . GLN A 92  ? 0.2725 0.3501 0.2269 0.0368  0.0091  0.0262  92  GLN A NE2 
761  N  N   . PHE A 93  ? 0.1229 0.1064 0.1642 -0.0155 -0.0104 -0.0026 93  PHE A N   
762  C  CA  . PHE A 93  ? 0.1301 0.1107 0.1240 -0.0136 -0.0013 -0.0156 93  PHE A CA  
763  C  C   . PHE A 93  ? 0.1134 0.0899 0.1314 -0.0041 -0.0183 -0.0219 93  PHE A C   
764  O  O   . PHE A 93  ? 0.0971 0.1159 0.1465 -0.0017 -0.0124 0.0021  93  PHE A O   
765  C  CB  . PHE A 93  ? 0.1066 0.1315 0.1447 0.0063  0.0307  -0.0211 93  PHE A CB  
766  C  CG  . PHE A 93  ? 0.1121 0.0996 0.1606 0.0027  0.0166  -0.0027 93  PHE A CG  
767  C  CD1 . PHE A 93  ? 0.1091 0.1193 0.2041 0.0152  -0.0119 0.0052  93  PHE A CD1 
768  C  CD2 . PHE A 93  ? 0.1229 0.1394 0.1506 -0.0077 0.0179  0.0035  93  PHE A CD2 
769  C  CE1 . PHE A 93  ? 0.1019 0.1444 0.1606 -0.0017 -0.0076 0.0126  93  PHE A CE1 
770  C  CE2 . PHE A 93  ? 0.1156 0.1439 0.1480 -0.0038 -0.0093 0.0068  93  PHE A CE2 
771  C  CZ  . PHE A 93  ? 0.1378 0.1324 0.1559 0.0197  0.0238  0.0043  93  PHE A CZ  
772  N  N   . HIS A 94  ? 0.1086 0.1026 0.1253 -0.0118 0.0026  -0.0049 94  HIS A N   
773  C  CA  . HIS A 94  ? 0.0994 0.0938 0.1330 -0.0103 -0.0005 0.0100  94  HIS A CA  
774  C  C   . HIS A 94  ? 0.0903 0.1089 0.1106 0.0055  -0.0153 0.0026  94  HIS A C   
775  O  O   . HIS A 94  ? 0.1023 0.0980 0.1037 0.0034  -0.0120 -0.0080 94  HIS A O   
776  C  CB  . HIS A 94  ? 0.0754 0.1134 0.1369 -0.0086 -0.0098 -0.0021 94  HIS A CB  
777  C  CG  . HIS A 94  ? 0.0901 0.0860 0.1234 0.0030  -0.0109 -0.0060 94  HIS A CG  
778  N  ND1 . HIS A 94  ? 0.1215 0.1057 0.1165 0.0186  -0.0087 0.0024  94  HIS A ND1 
779  C  CD2 . HIS A 94  ? 0.0784 0.1134 0.1143 -0.0027 -0.0057 -0.0060 94  HIS A CD2 
780  C  CE1 . HIS A 94  ? 0.1286 0.1026 0.1145 -0.0020 0.0096  -0.0038 94  HIS A CE1 
781  N  NE2 . HIS A 94  ? 0.0988 0.0979 0.1134 0.0046  -0.0226 -0.0068 94  HIS A NE2 
782  N  N   . PHE A 95  ? 0.1331 0.0856 0.1077 0.0008  0.0041  0.0005  95  PHE A N   
783  C  CA  . PHE A 95  ? 0.0953 0.0969 0.1202 0.0007  0.0066  -0.0010 95  PHE A CA  
784  C  C   . PHE A 95  ? 0.1181 0.0987 0.1019 0.0170  -0.0114 -0.0059 95  PHE A C   
785  O  O   . PHE A 95  ? 0.1206 0.1115 0.1127 -0.0032 -0.0104 -0.0127 95  PHE A O   
786  C  CB  . PHE A 95  ? 0.0958 0.1287 0.1229 0.0124  0.0093  0.0121  95  PHE A CB  
787  C  CG  . PHE A 95  ? 0.1071 0.0899 0.1102 0.0120  0.0000  -0.0052 95  PHE A CG  
788  C  CD1 . PHE A 95  ? 0.1172 0.1070 0.1486 0.0088  -0.0054 0.0037  95  PHE A CD1 
789  C  CD2 . PHE A 95  ? 0.1075 0.1444 0.1107 0.0065  0.0043  -0.0093 95  PHE A CD2 
790  C  CE1 . PHE A 95  ? 0.1179 0.1396 0.1594 0.0070  -0.0001 0.0175  95  PHE A CE1 
791  C  CE2 . PHE A 95  ? 0.1495 0.1005 0.1012 0.0221  0.0153  -0.0204 95  PHE A CE2 
792  C  CZ  . PHE A 95  ? 0.1335 0.1341 0.1405 0.0135  0.0197  0.0109  95  PHE A CZ  
793  N  N   . HIS A 96  ? 0.0897 0.1055 0.1206 0.0109  -0.0032 0.0000  96  HIS A N   
794  C  CA  . HIS A 96  ? 0.1073 0.0969 0.1218 0.0013  -0.0031 0.0010  96  HIS A CA  
795  C  C   . HIS A 96  ? 0.1057 0.1001 0.1098 0.0052  -0.0038 0.0006  96  HIS A C   
796  O  O   . HIS A 96  ? 0.1259 0.1088 0.1086 0.0082  -0.0074 0.0124  96  HIS A O   
797  C  CB  . HIS A 96  ? 0.1088 0.0857 0.1412 0.0132  0.0062  0.0054  96  HIS A CB  
798  C  CG  . HIS A 96  ? 0.1039 0.0930 0.1145 0.0100  0.0195  -0.0038 96  HIS A CG  
799  N  ND1 . HIS A 96  ? 0.1261 0.1030 0.1120 0.0066  -0.0003 -0.0099 96  HIS A ND1 
800  C  CD2 . HIS A 96  ? 0.1240 0.0870 0.1238 0.0193  0.0110  0.0041  96  HIS A CD2 
801  C  CE1 . HIS A 96  ? 0.1495 0.1044 0.1145 0.0148  0.0082  -0.0103 96  HIS A CE1 
802  N  NE2 . HIS A 96  ? 0.0924 0.0710 0.1136 0.0005  0.0010  -0.0001 96  HIS A NE2 
803  N  N   . TRP A 97  ? 0.1018 0.1037 0.1240 0.0238  -0.0131 -0.0054 97  TRP A N   
804  C  CA  . TRP A 97  ? 0.1199 0.0944 0.1200 0.0065  -0.0040 0.0028  97  TRP A CA  
805  C  C   . TRP A 97  ? 0.0915 0.1105 0.1085 0.0087  -0.0086 -0.0013 97  TRP A C   
806  O  O   . TRP A 97  ? 0.1224 0.1071 0.1109 0.0034  -0.0164 0.0068  97  TRP A O   
807  C  CB  . TRP A 97  ? 0.1209 0.1055 0.1287 0.0074  -0.0190 -0.0007 97  TRP A CB  
808  C  CG  . TRP A 97  ? 0.1136 0.1037 0.1208 0.0144  -0.0131 -0.0085 97  TRP A CG  
809  C  CD1 . TRP A 97  ? 0.1389 0.1128 0.1398 0.0203  -0.0271 -0.0012 97  TRP A CD1 
810  C  CD2 . TRP A 97  ? 0.1058 0.1008 0.1234 0.0286  -0.0124 -0.0166 97  TRP A CD2 
811  N  NE1 . TRP A 97  ? 0.1295 0.1100 0.1509 0.0031  -0.0171 0.0076  97  TRP A NE1 
812  C  CE2 . TRP A 97  ? 0.1124 0.1018 0.1292 0.0127  -0.0199 0.0024  97  TRP A CE2 
813  C  CE3 . TRP A 97  ? 0.1089 0.0958 0.1441 0.0063  0.0082  0.0000  97  TRP A CE3 
814  C  CZ2 . TRP A 97  ? 0.1532 0.1222 0.1432 -0.0052 -0.0135 -0.0307 97  TRP A CZ2 
815  C  CZ3 . TRP A 97  ? 0.1298 0.1265 0.1529 0.0057  -0.0260 -0.0220 97  TRP A CZ3 
816  C  CH2 . TRP A 97  ? 0.1292 0.1357 0.1118 0.0071  -0.0070 -0.0091 97  TRP A CH2 
817  N  N   . GLY A 98  ? 0.1190 0.1003 0.1240 0.0174  -0.0199 -0.0003 98  GLY A N   
818  C  CA  . GLY A 98  ? 0.1259 0.1068 0.1441 0.0107  -0.0344 0.0238  98  GLY A CA  
819  C  C   . GLY A 98  ? 0.1202 0.1224 0.1351 -0.0041 -0.0184 0.0063  98  GLY A C   
820  O  O   . GLY A 98  ? 0.1204 0.1168 0.1538 0.0295  -0.0104 0.0093  98  GLY A O   
821  N  N   . SER A 99  ? 0.1543 0.1229 0.1481 0.0156  -0.0153 0.0206  99  SER A N   
822  C  CA  . SER A 99  ? 0.1948 0.1265 0.1720 0.0390  -0.0305 0.0296  99  SER A CA  
823  C  C   . SER A 99  ? 0.1466 0.1515 0.1520 0.0359  -0.0189 0.0250  99  SER A C   
824  O  O   . SER A 99  ? 0.1867 0.1721 0.2396 0.0584  -0.0082 0.0141  99  SER A O   
825  C  CB  . SER A 99  ? 0.1966 0.1526 0.1991 0.0076  -0.0113 0.0283  99  SER A CB  
826  O  OG  . SER A 99  ? 0.1960 0.1559 0.1651 -0.0017 0.0000  0.0362  99  SER A OG  
827  N  N   . LEU A 100 ? 0.1913 0.1410 0.1619 0.0206  -0.0278 0.0024  100 LEU A N   
828  C  CA  . LEU A 100 ? 0.2425 0.1400 0.1653 0.0037  -0.0100 -0.0082 100 LEU A CA  
829  C  C   . LEU A 100 ? 0.1545 0.1511 0.1738 0.0156  -0.0275 -0.0163 100 LEU A C   
830  O  O   . LEU A 100 ? 0.1775 0.1150 0.1908 0.0143  -0.0085 0.0103  100 LEU A O   
831  C  CB  . LEU A 100 ? 0.2673 0.2140 0.2533 -0.0315 -0.0148 -0.0041 100 LEU A CB  
832  C  CG  . LEU A 100 ? 0.3244 0.2736 0.2685 0.0361  -0.0046 0.0081  100 LEU A CG  
833  C  CD1 . LEU A 100 ? 0.3352 0.6406 0.3519 -0.1306 -0.0234 0.1333  100 LEU A CD1 
834  C  CD2 . LEU A 100 ? 0.4138 0.3359 0.3867 0.1125  -0.0529 0.1306  100 LEU A CD2 
835  N  N   . ASP A 101 ? 0.1816 0.1340 0.1561 0.0108  0.0147  0.0012  101 ASP A N   
836  C  CA  . ASP A 101 ? 0.1626 0.1486 0.1647 -0.0236 -0.0082 -0.0194 101 ASP A CA  
837  C  C   . ASP A 101 ? 0.1605 0.1420 0.1739 0.0000  -0.0104 -0.0054 101 ASP A C   
838  O  O   . ASP A 101 ? 0.2011 0.1308 0.2087 -0.0092 -0.0197 0.0017  101 ASP A O   
839  C  CB  . ASP A 101 ? 0.2132 0.1606 0.2310 -0.0450 -0.0001 -0.0837 101 ASP A CB  
840  C  CG  . ASP A 101 ? 0.2405 0.2134 0.2186 0.0070  -0.0205 -0.0478 101 ASP A CG  
841  O  OD1 . ASP A 101 ? 0.1732 0.1802 0.2303 0.0238  -0.0285 -0.0516 101 ASP A OD1 
842  O  OD2 . ASP A 101 ? 0.2585 0.2245 0.3330 0.0171  0.0450  -0.0847 101 ASP A OD2 
843  N  N   . GLY A 102 ? 0.1678 0.1299 0.1893 0.0126  0.0074  -0.0175 102 GLY A N   
844  C  CA  . GLY A 102 ? 0.1836 0.1366 0.1996 -0.0020 0.0162  -0.0104 102 GLY A CA  
845  C  C   . GLY A 102 ? 0.1732 0.1143 0.1763 -0.0068 0.0063  -0.0035 102 GLY A C   
846  O  O   . GLY A 102 ? 0.1804 0.1402 0.2017 -0.0027 -0.0296 -0.0190 102 GLY A O   
847  N  N   . GLN A 103 ? 0.1547 0.1290 0.1520 -0.0017 0.0015  -0.0209 103 GLN A N   
848  C  CA  . GLN A 103 ? 0.1396 0.1242 0.1430 0.0063  -0.0043 -0.0120 103 GLN A CA  
849  C  C   . GLN A 103 ? 0.1265 0.1152 0.1085 0.0109  0.0024  -0.0127 103 GLN A C   
850  O  O   . GLN A 103 ? 0.1315 0.1057 0.1595 0.0052  -0.0026 -0.0046 103 GLN A O   
851  C  CB  . GLN A 103 ? 0.1321 0.1333 0.1656 0.0097  -0.0137 -0.0093 103 GLN A CB  
852  C  CG  . GLN A 103 ? 0.1870 0.1211 0.1562 -0.0046 -0.0351 0.0390  103 GLN A CG  
853  C  CD  . GLN A 103 ? 0.2664 0.2179 0.1947 -0.0513 -0.0310 0.0414  103 GLN A CD  
854  O  OE1 . GLN A 103 ? 0.4214 0.3269 0.2411 -0.1639 -0.0797 0.0763  103 GLN A OE1 
855  N  NE2 . GLN A 103 ? 0.2048 0.1802 0.1786 -0.0152 -0.0035 0.0260  103 GLN A NE2 
856  N  N   . GLY A 104 ? 0.1254 0.1057 0.1120 0.0156  -0.0148 0.0142  104 GLY A N   
857  C  CA  . GLY A 104 ? 0.1252 0.1062 0.1234 0.0086  -0.0136 0.0043  104 GLY A CA  
858  C  C   . GLY A 104 ? 0.1037 0.1058 0.1057 -0.0055 -0.0015 0.0082  104 GLY A C   
859  O  O   . GLY A 104 ? 0.1281 0.1249 0.1154 0.0005  0.0007  -0.0102 104 GLY A O   
860  N  N   . SER A 105 ? 0.0933 0.1071 0.0957 0.0171  -0.0040 0.0041  105 SER A N   
861  C  CA  . SER A 105 ? 0.1102 0.0983 0.0996 0.0277  -0.0163 -0.0066 105 SER A CA  
862  C  C   . SER A 105 ? 0.1129 0.1018 0.1003 0.0027  -0.0071 -0.0006 105 SER A C   
863  O  O   . SER A 105 ? 0.1168 0.1048 0.1259 0.0140  0.0044  0.0068  105 SER A O   
864  C  CB  . SER A 105 ? 0.1118 0.1097 0.1073 -0.0032 0.0006  -0.0087 105 SER A CB  
865  O  OG  . SER A 105 ? 0.1308 0.0877 0.1179 -0.0030 -0.0032 -0.0082 105 SER A OG  
866  N  N   . GLU A 106 ? 0.0973 0.1021 0.1046 0.0195  -0.0166 -0.0032 106 GLU A N   
867  C  CA  . GLU A 106 ? 0.1067 0.0987 0.1039 0.0013  0.0076  0.0054  106 GLU A CA  
868  C  C   . GLU A 106 ? 0.1010 0.0908 0.0978 0.0078  0.0111  -0.0049 106 GLU A C   
869  O  O   . GLU A 106 ? 0.1071 0.0949 0.0970 0.0044  0.0063  0.0065  106 GLU A O   
870  C  CB  . GLU A 106 ? 0.1163 0.1033 0.1017 0.0051  -0.0175 -0.0088 106 GLU A CB  
871  C  CG  . GLU A 106 ? 0.1105 0.1103 0.1462 0.0185  -0.0296 -0.0212 106 GLU A CG  
872  C  CD  . GLU A 106 ? 0.1269 0.1238 0.0940 0.0078  -0.0010 -0.0085 106 GLU A CD  
873  O  OE1 . GLU A 106 ? 0.1238 0.1158 0.1093 0.0049  0.0049  0.0007  106 GLU A OE1 
874  O  OE2 . GLU A 106 ? 0.1456 0.1246 0.1000 0.0136  0.0044  0.0059  106 GLU A OE2 
875  N  N   . HIS A 107 ? 0.0935 0.0915 0.0978 -0.0015 0.0021  0.0087  107 HIS A N   
876  C  CA  . HIS A 107 ? 0.0920 0.0772 0.0922 0.0089  -0.0035 0.0057  107 HIS A CA  
877  C  C   . HIS A 107 ? 0.1048 0.0854 0.1039 0.0073  0.0076  0.0007  107 HIS A C   
878  O  O   . HIS A 107 ? 0.1102 0.0958 0.0976 0.0031  0.0083  0.0065  107 HIS A O   
879  C  CB  . HIS A 107 ? 0.1032 0.0854 0.0888 0.0057  -0.0003 0.0057  107 HIS A CB  
880  C  CG  . HIS A 107 ? 0.0918 0.0906 0.0820 0.0040  -0.0098 0.0096  107 HIS A CG  
881  N  ND1 . HIS A 107 ? 0.1073 0.0883 0.1084 0.0007  0.0000  0.0059  107 HIS A ND1 
882  C  CD2 . HIS A 107 ? 0.0949 0.0960 0.1082 0.0048  0.0103  0.0197  107 HIS A CD2 
883  C  CE1 . HIS A 107 ? 0.0944 0.0861 0.1035 0.0087  0.0060  0.0030  107 HIS A CE1 
884  N  NE2 . HIS A 107 ? 0.0994 0.0847 0.1057 0.0097  0.0023  0.0105  107 HIS A NE2 
885  N  N   . THR A 108 ? 0.1143 0.0978 0.1054 0.0037  -0.0157 -0.0125 108 THR A N   
886  C  CA  . THR A 108 ? 0.1247 0.0822 0.1077 -0.0043 -0.0199 0.0141  108 THR A CA  
887  C  C   . THR A 108 ? 0.0906 0.0996 0.0992 0.0060  -0.0023 -0.0020 108 THR A C   
888  O  O   . THR A 108 ? 0.1030 0.1062 0.1130 0.0077  0.0027  0.0152  108 THR A O   
889  C  CB  . THR A 108 ? 0.0958 0.1292 0.1283 -0.0024 0.0077  0.0340  108 THR A CB  
890  O  OG1 . THR A 108 ? 0.1222 0.1237 0.1353 0.0100  0.0141  0.0126  108 THR A OG1 
891  C  CG2 . THR A 108 ? 0.1423 0.1330 0.1238 0.0147  -0.0226 0.0159  108 THR A CG2 
892  N  N   . VAL A 109 ? 0.0960 0.0962 0.1030 -0.0065 -0.0113 -0.0001 109 VAL A N   
893  C  CA  . VAL A 109 ? 0.1235 0.1155 0.1082 -0.0122 -0.0170 0.0035  109 VAL A CA  
894  C  C   . VAL A 109 ? 0.1288 0.1116 0.1062 0.0034  -0.0020 0.0076  109 VAL A C   
895  O  O   . VAL A 109 ? 0.1412 0.1077 0.1218 0.0021  -0.0035 -0.0127 109 VAL A O   
896  C  CB  . VAL A 109 ? 0.1288 0.1164 0.0991 -0.0163 -0.0159 0.0068  109 VAL A CB  
897  C  CG1 . VAL A 109 ? 0.1585 0.1459 0.1215 -0.0074 -0.0399 -0.0152 109 VAL A CG1 
898  C  CG2 . VAL A 109 ? 0.1243 0.1121 0.1331 -0.0174 0.0093  -0.0054 109 VAL A CG2 
899  N  N   . ASP A 110 ? 0.1112 0.1260 0.1632 -0.0081 -0.0242 -0.0043 110 ASP A N   
900  C  CA  . ASP A 110 ? 0.1605 0.1272 0.1559 -0.0086 -0.0216 -0.0037 110 ASP A CA  
901  C  C   . ASP A 110 ? 0.1251 0.1217 0.1526 -0.0181 -0.0083 0.0098  110 ASP A C   
902  O  O   . ASP A 110 ? 0.1518 0.1312 0.1601 -0.0093 -0.0114 0.0030  110 ASP A O   
903  C  CB  . ASP A 110 ? 0.1843 0.1583 0.1635 -0.0427 -0.0487 -0.0015 110 ASP A CB  
904  C  CG  . ASP A 110 ? 0.1764 0.1391 0.1763 -0.0342 -0.0281 -0.0110 110 ASP A CG  
905  O  OD1 . ASP A 110 ? 0.1887 0.1786 0.1814 -0.0172 -0.0238 0.0261  110 ASP A OD1 
906  O  OD2 . ASP A 110 ? 0.2179 0.2443 0.1653 -0.0254 -0.0414 -0.0015 110 ASP A OD2 
907  N  N   . LYS A 111 ? 0.1319 0.1179 0.1208 -0.0013 -0.0107 0.0060  111 LYS A N   
908  C  CA  . LYS A 111 ? 0.1331 0.1500 0.1409 -0.0115 -0.0060 0.0339  111 LYS A CA  
909  C  C   . LYS A 111 ? 0.1378 0.1066 0.1188 0.0073  -0.0035 -0.0041 111 LYS A C   
910  O  O   . LYS A 111 ? 0.1552 0.1395 0.1290 -0.0181 -0.0152 0.0124  111 LYS A O   
911  C  CB  . LYS A 111 ? 0.1414 0.1764 0.1606 -0.0190 -0.0065 0.0326  111 LYS A CB  
912  C  CG  . LYS A 111 ? 0.1427 0.1942 0.2669 -0.0346 0.0176  0.0456  111 LYS A CG  
913  C  CD  . LYS A 111 ? 0.2341 0.3188 0.2413 0.0637  0.0678  0.0496  111 LYS A CD  
914  C  CE  . LYS A 111 ? 0.2276 0.3738 0.3871 0.0644  0.0659  0.0900  111 LYS A CE  
915  N  NZ  . LYS A 111 ? 0.3018 0.4376 0.3406 -0.0879 0.0797  -0.0355 111 LYS A NZ  
916  N  N   . LYS A 112 ? 0.1082 0.0974 0.1356 -0.0130 0.0052  0.0065  112 LYS A N   
917  C  CA  . LYS A 112 ? 0.1322 0.1357 0.1339 0.0190  -0.0132 0.0048  112 LYS A CA  
918  C  C   . LYS A 112 ? 0.1084 0.1182 0.1197 0.0082  0.0074  0.0110  112 LYS A C   
919  O  O   . LYS A 112 ? 0.1263 0.1055 0.1377 0.0097  -0.0023 0.0087  112 LYS A O   
920  C  CB  . LYS A 112 ? 0.1296 0.1574 0.1571 -0.0099 -0.0109 -0.0109 112 LYS A CB  
921  C  CG  . LYS A 112 ? 0.1349 0.1820 0.1473 0.0326  -0.0082 -0.0091 112 LYS A CG  
922  C  CD  . LYS A 112 ? 0.1702 0.2515 0.1696 0.0080  0.0252  0.0221  112 LYS A CD  
923  C  CE  . LYS A 112 ? 0.1942 0.2282 0.2242 0.0217  -0.0046 -0.0010 112 LYS A CE  
924  N  NZ  . LYS A 112 ? 0.2032 0.2157 0.2897 -0.0055 0.0491  -0.0310 112 LYS A NZ  
925  N  N   A LYS A 113 ? 0.1263 0.1177 0.1242 0.0060  -0.0174 0.0032  113 LYS A N   
926  N  N   B LYS A 113 ? 0.1233 0.1145 0.1253 0.0098  -0.0124 0.0024  113 LYS A N   
927  C  CA  A LYS A 113 ? 0.1193 0.0870 0.1339 -0.0019 -0.0054 0.0132  113 LYS A CA  
928  C  CA  B LYS A 113 ? 0.1213 0.1191 0.1369 -0.0120 -0.0021 0.0082  113 LYS A CA  
929  C  C   A LYS A 113 ? 0.1392 0.0931 0.1177 0.0111  -0.0131 0.0000  113 LYS A C   
930  C  C   B LYS A 113 ? 0.1443 0.1010 0.1353 0.0093  -0.0054 -0.0003 113 LYS A C   
931  O  O   A LYS A 113 ? 0.1080 0.0935 0.1033 -0.0023 -0.0043 -0.0098 113 LYS A O   
932  O  O   B LYS A 113 ? 0.1457 0.1008 0.1544 0.0216  0.0038  0.0049  113 LYS A O   
933  C  CB  A LYS A 113 ? 0.1080 0.1357 0.1256 -0.0077 0.0081  0.0109  113 LYS A CB  
934  C  CB  B LYS A 113 ? 0.1292 0.1224 0.1323 0.0043  0.0170  0.0087  113 LYS A CB  
935  C  CG  A LYS A 113 ? 0.1482 0.1225 0.1120 -0.0007 0.0189  0.0098  113 LYS A CG  
936  C  CG  B LYS A 113 ? 0.1044 0.1400 0.1295 -0.0164 0.0054  0.0048  113 LYS A CG  
937  C  CD  A LYS A 113 ? 0.1642 0.1441 0.1159 0.0307  0.0166  0.0255  113 LYS A CD  
938  C  CD  B LYS A 113 ? 0.1623 0.1238 0.1312 0.0155  0.0281  0.0137  113 LYS A CD  
939  C  CE  A LYS A 113 ? 0.1632 0.1136 0.1504 0.0351  0.0077  0.0108  113 LYS A CE  
940  C  CE  B LYS A 113 ? 0.1389 0.1693 0.1524 0.0092  0.0284  -0.0027 113 LYS A CE  
941  N  NZ  A LYS A 113 ? 0.1745 0.2091 0.1802 0.0243  0.0065  0.0184  113 LYS A NZ  
942  N  NZ  B LYS A 113 ? 0.2382 0.1845 0.1457 -0.0082 -0.0093 0.0109  113 LYS A NZ  
943  N  N   . TYR A 114 ? 0.1018 0.1161 0.1193 -0.0032 -0.0188 -0.0027 114 TYR A N   
944  C  CA  . TYR A 114 ? 0.1191 0.0847 0.1197 -0.0103 0.0165  0.0003  114 TYR A CA  
945  C  C   . TYR A 114 ? 0.1249 0.0859 0.1206 0.0031  0.0085  -0.0124 114 TYR A C   
946  O  O   . TYR A 114 ? 0.1262 0.1070 0.1142 0.0166  -0.0005 -0.0076 114 TYR A O   
947  C  CB  . TYR A 114 ? 0.1513 0.0872 0.0951 -0.0171 0.0066  0.0000  114 TYR A CB  
948  C  CG  . TYR A 114 ? 0.1173 0.1161 0.1317 0.0068  0.0054  0.0104  114 TYR A CG  
949  C  CD1 . TYR A 114 ? 0.1430 0.1342 0.1554 0.0041  -0.0068 0.0159  114 TYR A CD1 
950  C  CD2 . TYR A 114 ? 0.1581 0.1261 0.1377 0.0031  -0.0049 -0.0205 114 TYR A CD2 
951  C  CE1 . TYR A 114 ? 0.1447 0.1662 0.1895 -0.0024 -0.0126 0.0059  114 TYR A CE1 
952  C  CE2 . TYR A 114 ? 0.1926 0.1664 0.1523 -0.0063 -0.0208 0.0000  114 TYR A CE2 
953  C  CZ  . TYR A 114 ? 0.1730 0.1687 0.1349 -0.0148 -0.0185 -0.0082 114 TYR A CZ  
954  O  OH  . TYR A 114 ? 0.2777 0.2202 0.1683 -0.0381 -0.0412 0.0155  114 TYR A OH  
955  N  N   . ALA A 115 ? 0.1190 0.0890 0.1274 0.0086  0.0003  0.0000  115 ALA A N   
956  C  CA  . ALA A 115 ? 0.1184 0.0822 0.1362 0.0163  -0.0057 -0.0100 115 ALA A CA  
957  C  C   . ALA A 115 ? 0.1041 0.1010 0.1199 0.0082  -0.0024 -0.0098 115 ALA A C   
958  O  O   . ALA A 115 ? 0.1305 0.0900 0.1310 0.0152  -0.0046 -0.0034 115 ALA A O   
959  C  CB  . ALA A 115 ? 0.1396 0.1212 0.1533 0.0229  0.0155  -0.0057 115 ALA A CB  
960  N  N   . ALA A 116 ? 0.1177 0.0856 0.1299 0.0085  -0.0038 -0.0077 116 ALA A N   
961  C  CA  . ALA A 116 ? 0.1042 0.0836 0.1308 -0.0027 -0.0201 -0.0012 116 ALA A CA  
962  C  C   . ALA A 116 ? 0.1137 0.1012 0.1163 0.0118  -0.0085 -0.0032 116 ALA A C   
963  O  O   . ALA A 116 ? 0.1064 0.0987 0.1150 0.0007  0.0000  -0.0098 116 ALA A O   
964  C  CB  . ALA A 116 ? 0.0979 0.1228 0.1322 -0.0008 0.0023  -0.0107 116 ALA A CB  
965  N  N   . GLU A 117 ? 0.1124 0.0899 0.1112 0.0082  -0.0068 0.0023  117 GLU A N   
966  C  CA  . GLU A 117 ? 0.0906 0.0816 0.1107 0.0043  0.0082  0.0070  117 GLU A CA  
967  C  C   . GLU A 117 ? 0.0890 0.0949 0.0983 0.0138  -0.0166 0.0024  117 GLU A C   
968  O  O   . GLU A 117 ? 0.1317 0.1050 0.0974 -0.0020 -0.0043 -0.0096 117 GLU A O   
969  C  CB  . GLU A 117 ? 0.0833 0.0976 0.1125 0.0052  -0.0010 -0.0038 117 GLU A CB  
970  C  CG  . GLU A 117 ? 0.0908 0.1145 0.1287 0.0247  -0.0083 0.0000  117 GLU A CG  
971  C  CD  . GLU A 117 ? 0.1172 0.1100 0.1044 0.0020  0.0088  0.0114  117 GLU A CD  
972  O  OE1 . GLU A 117 ? 0.1006 0.1089 0.1093 0.0043  0.0120  0.0094  117 GLU A OE1 
973  O  OE2 . GLU A 117 ? 0.1161 0.1111 0.1324 0.0093  -0.0024 -0.0010 117 GLU A OE2 
974  N  N   . LEU A 118 ? 0.0861 0.0987 0.1080 0.0001  0.0023  0.0140  118 LEU A N   
975  C  CA  . LEU A 118 ? 0.1118 0.0753 0.1075 0.0104  -0.0035 0.0089  118 LEU A CA  
976  C  C   . LEU A 118 ? 0.0926 0.1073 0.1035 0.0091  -0.0038 -0.0003 118 LEU A C   
977  O  O   . LEU A 118 ? 0.0870 0.0978 0.0944 0.0023  -0.0037 -0.0116 118 LEU A O   
978  C  CB  . LEU A 118 ? 0.1140 0.1005 0.1018 -0.0108 -0.0032 -0.0097 118 LEU A CB  
979  C  CG  . LEU A 118 ? 0.1283 0.1079 0.1048 -0.0120 0.0057  -0.0032 118 LEU A CG  
980  C  CD1 . LEU A 118 ? 0.1019 0.1285 0.1287 -0.0186 -0.0040 -0.0017 118 LEU A CD1 
981  C  CD2 . LEU A 118 ? 0.1161 0.1351 0.1434 -0.0038 0.0198  -0.0143 118 LEU A CD2 
982  N  N   . HIS A 119 ? 0.0775 0.0842 0.1096 -0.0024 -0.0017 -0.0051 119 HIS A N   
983  C  CA  . HIS A 119 ? 0.0960 0.0847 0.0991 0.0081  0.0005  -0.0044 119 HIS A CA  
984  C  C   . HIS A 119 ? 0.0954 0.0947 0.1155 0.0082  -0.0087 0.0012  119 HIS A C   
985  O  O   . HIS A 119 ? 0.1130 0.0987 0.1299 0.0065  -0.0131 -0.0041 119 HIS A O   
986  C  CB  . HIS A 119 ? 0.1017 0.0926 0.1058 -0.0080 0.0154  -0.0003 119 HIS A CB  
987  C  CG  . HIS A 119 ? 0.0773 0.0891 0.0791 0.0083  -0.0010 0.0121  119 HIS A CG  
988  N  ND1 . HIS A 119 ? 0.1179 0.0978 0.0715 -0.0098 0.0081  -0.0020 119 HIS A ND1 
989  C  CD2 . HIS A 119 ? 0.1023 0.0942 0.0962 0.0051  -0.0043 0.0057  119 HIS A CD2 
990  C  CE1 . HIS A 119 ? 0.1141 0.0976 0.1182 0.0118  -0.0068 0.0024  119 HIS A CE1 
991  N  NE2 . HIS A 119 ? 0.1014 0.1028 0.1121 0.0093  0.0151  -0.0007 119 HIS A NE2 
992  N  N   . LEU A 120 ? 0.0939 0.0872 0.0960 0.0020  -0.0063 -0.0083 120 LEU A N   
993  C  CA  . LEU A 120 ? 0.0996 0.1054 0.1228 0.0052  0.0085  0.0115  120 LEU A CA  
994  C  C   . LEU A 120 ? 0.1076 0.0838 0.1012 -0.0049 -0.0024 0.0176  120 LEU A C   
995  O  O   . LEU A 120 ? 0.1163 0.0933 0.1206 0.0046  -0.0125 0.0062  120 LEU A O   
996  C  CB  . LEU A 120 ? 0.1008 0.0983 0.1093 0.0098  -0.0020 0.0307  120 LEU A CB  
997  C  CG  . LEU A 120 ? 0.1224 0.1259 0.1362 0.0176  0.0087  0.0071  120 LEU A CG  
998  C  CD1 . LEU A 120 ? 0.1870 0.1290 0.2023 0.0200  0.0149  -0.0403 120 LEU A CD1 
999  C  CD2 . LEU A 120 ? 0.1301 0.1567 0.1632 0.0256  0.0148  0.0114  120 LEU A CD2 
1000 N  N   . VAL A 121 ? 0.1206 0.0967 0.1116 0.0054  -0.0005 -0.0040 121 VAL A N   
1001 C  CA  . VAL A 121 ? 0.1204 0.0859 0.1267 0.0055  -0.0121 0.0037  121 VAL A CA  
1002 C  C   . VAL A 121 ? 0.1297 0.0980 0.1290 -0.0037 -0.0103 0.0076  121 VAL A C   
1003 O  O   . VAL A 121 ? 0.1218 0.1128 0.1459 0.0057  -0.0100 0.0031  121 VAL A O   
1004 C  CB  . VAL A 121 ? 0.1240 0.0971 0.1256 0.0019  -0.0065 -0.0068 121 VAL A CB  
1005 C  CG1 . VAL A 121 ? 0.1651 0.1134 0.1176 0.0211  0.0170  -0.0189 121 VAL A CG1 
1006 C  CG2 . VAL A 121 ? 0.1335 0.1021 0.1414 -0.0060 -0.0125 0.0054  121 VAL A CG2 
1007 N  N   . HIS A 122 ? 0.1064 0.0881 0.1298 0.0104  -0.0046 -0.0043 122 HIS A N   
1008 C  CA  . HIS A 122 ? 0.1384 0.0856 0.1129 0.0161  -0.0003 0.0024  122 HIS A CA  
1009 C  C   . HIS A 122 ? 0.1212 0.0958 0.1484 -0.0057 0.0001  -0.0118 122 HIS A C   
1010 O  O   . HIS A 122 ? 0.1233 0.0951 0.1462 0.0031  0.0054  -0.0049 122 HIS A O   
1011 C  CB  . HIS A 122 ? 0.1290 0.0974 0.1138 -0.0129 -0.0098 -0.0055 122 HIS A CB  
1012 C  CG  . HIS A 122 ? 0.1048 0.0952 0.1249 -0.0030 -0.0041 0.0000  122 HIS A CG  
1013 N  ND1 . HIS A 122 ? 0.1150 0.0933 0.1267 -0.0108 -0.0038 0.0037  122 HIS A ND1 
1014 C  CD2 . HIS A 122 ? 0.1199 0.1177 0.1211 -0.0068 0.0021  0.0043  122 HIS A CD2 
1015 C  CE1 . HIS A 122 ? 0.1290 0.1314 0.1326 0.0127  0.0082  0.0133  122 HIS A CE1 
1016 N  NE2 . HIS A 122 ? 0.1230 0.1143 0.1412 -0.0013 0.0086  0.0038  122 HIS A NE2 
1017 N  N   . TRP A 123 ? 0.1299 0.0935 0.1272 -0.0021 0.0055  -0.0026 123 TRP A N   
1018 C  CA  . TRP A 123 ? 0.1387 0.0998 0.1358 0.0176  -0.0055 -0.0082 123 TRP A CA  
1019 C  C   . TRP A 123 ? 0.1233 0.0971 0.1226 -0.0017 0.0038  -0.0109 123 TRP A C   
1020 O  O   . TRP A 123 ? 0.1389 0.1120 0.1490 0.0030  0.0070  -0.0066 123 TRP A O   
1021 C  CB  . TRP A 123 ? 0.1579 0.1179 0.1538 0.0076  -0.0197 -0.0086 123 TRP A CB  
1022 C  CG  . TRP A 123 ? 0.1648 0.1238 0.1822 -0.0052 -0.0119 -0.0049 123 TRP A CG  
1023 C  CD1 . TRP A 123 ? 0.1793 0.1407 0.2196 0.0070  0.0109  -0.0220 123 TRP A CD1 
1024 C  CD2 . TRP A 123 ? 0.1736 0.1280 0.2014 -0.0038 -0.0236 -0.0065 123 TRP A CD2 
1025 N  NE1 . TRP A 123 ? 0.1859 0.1170 0.2424 0.0172  -0.0097 -0.0286 123 TRP A NE1 
1026 C  CE2 . TRP A 123 ? 0.1718 0.1199 0.2170 0.0012  -0.0267 0.0076  123 TRP A CE2 
1027 C  CE3 . TRP A 123 ? 0.1500 0.1084 0.2008 -0.0110 -0.0204 -0.0203 123 TRP A CE3 
1028 C  CZ2 . TRP A 123 ? 0.1972 0.1353 0.2766 -0.0232 -0.0608 0.0034  123 TRP A CZ2 
1029 C  CZ3 . TRP A 123 ? 0.2003 0.1010 0.2583 -0.0099 -0.0262 -0.0167 123 TRP A CZ3 
1030 C  CH2 . TRP A 123 ? 0.2102 0.1439 0.2325 0.0116  -0.0292 -0.0197 123 TRP A CH2 
1031 N  N   . ASN A 124 ? 0.1317 0.1237 0.1574 0.0104  0.0038  0.0130  124 ASN A N   
1032 C  CA  . ASN A 124 ? 0.1335 0.0971 0.1829 -0.0041 -0.0071 0.0253  124 ASN A CA  
1033 C  C   . ASN A 124 ? 0.1367 0.1021 0.1418 0.0157  -0.0041 0.0157  124 ASN A C   
1034 O  O   . ASN A 124 ? 0.1535 0.1089 0.1516 0.0013  0.0041  -0.0031 124 ASN A O   
1035 C  CB  . ASN A 124 ? 0.1288 0.1333 0.1538 0.0110  -0.0093 0.0070  124 ASN A CB  
1036 C  CG  . ASN A 124 ? 0.1840 0.1256 0.1441 0.0120  -0.0103 -0.0187 124 ASN A CG  
1037 O  OD1 . ASN A 124 ? 0.1684 0.1292 0.1858 0.0135  -0.0065 0.0131  124 ASN A OD1 
1038 N  ND2 . ASN A 124 ? 0.1890 0.1211 0.1829 0.0087  -0.0102 0.0048  124 ASN A ND2 
1039 N  N   . THR A 125 ? 0.1477 0.1089 0.1667 0.0099  0.0035  0.0210  125 THR A N   
1040 C  CA  . THR A 125 ? 0.1680 0.1186 0.2075 -0.0114 0.0272  -0.0080 125 THR A CA  
1041 C  C   . THR A 125 ? 0.1775 0.1462 0.1685 -0.0038 -0.0317 0.0204  125 THR A C   
1042 O  O   . THR A 125 ? 0.2359 0.1430 0.2239 -0.0229 -0.0199 -0.0076 125 THR A O   
1043 C  CB  . THR A 125 ? 0.1815 0.1633 0.2104 -0.0230 0.0185  0.0285  125 THR A CB  
1044 O  OG1 . THR A 125 ? 0.3226 0.1790 0.2148 -0.0298 -0.0057 0.0443  125 THR A OG1 
1045 C  CG2 . THR A 125 ? 0.2140 0.2029 0.2317 0.0147  0.0148  0.0156  125 THR A CG2 
1046 N  N   . LYS A 126 ? 0.1978 0.1093 0.1807 0.0234  -0.0261 0.0142  127 LYS A N   
1047 C  CA  . LYS A 126 ? 0.1996 0.1457 0.2190 0.0529  -0.0218 0.0126  127 LYS A CA  
1048 C  C   . LYS A 126 ? 0.1753 0.1305 0.2087 0.0076  -0.0217 -0.0051 127 LYS A C   
1049 O  O   . LYS A 126 ? 0.2676 0.1249 0.2409 0.0436  -0.0311 -0.0148 127 LYS A O   
1050 C  CB  . LYS A 126 ? 0.2542 0.1708 0.2723 0.0143  -0.0344 -0.0013 127 LYS A CB  
1051 C  CG  . LYS A 126 ? 0.2680 0.1958 0.2563 0.0286  -0.0104 0.0035  127 LYS A CG  
1052 C  CD  . LYS A 126 ? 0.3161 0.3323 0.3350 0.0786  -0.0203 -0.0992 127 LYS A CD  
1053 C  CE  . LYS A 126 ? 0.3962 0.3865 0.3145 0.0586  0.0373  0.0126  127 LYS A CE  
1054 N  NZ  . LYS A 126 ? 0.3598 0.4815 0.6037 -0.1026 -0.1806 -0.0615 127 LYS A NZ  
1055 N  N   . TYR A 127 ? 0.1676 0.1313 0.1895 0.0152  -0.0263 0.0060  128 TYR A N   
1056 C  CA  . TYR A 127 ? 0.1360 0.1225 0.1967 0.0159  -0.0155 0.0151  128 TYR A CA  
1057 C  C   . TYR A 127 ? 0.1581 0.1128 0.1583 0.0266  -0.0252 0.0010  128 TYR A C   
1058 O  O   . TYR A 127 ? 0.2197 0.1337 0.1881 0.0089  -0.0229 -0.0068 128 TYR A O   
1059 C  CB  . TYR A 127 ? 0.1854 0.1387 0.1470 0.0023  -0.0221 -0.0113 128 TYR A CB  
1060 C  CG  . TYR A 127 ? 0.1531 0.1136 0.1888 0.0170  -0.0003 -0.0278 128 TYR A CG  
1061 C  CD1 . TYR A 127 ? 0.1579 0.1310 0.1835 0.0395  -0.0138 0.0189  128 TYR A CD1 
1062 C  CD2 . TYR A 127 ? 0.1786 0.1194 0.1685 -0.0038 -0.0115 -0.0181 128 TYR A CD2 
1063 C  CE1 . TYR A 127 ? 0.1631 0.1233 0.2317 0.0188  -0.0329 -0.0083 128 TYR A CE1 
1064 C  CE2 . TYR A 127 ? 0.1628 0.1624 0.1799 0.0229  -0.0005 0.0040  128 TYR A CE2 
1065 C  CZ  . TYR A 127 ? 0.1477 0.1367 0.1996 0.0081  -0.0087 0.0200  128 TYR A CZ  
1066 O  OH  . TYR A 127 ? 0.1576 0.1669 0.2178 0.0185  -0.0259 0.0188  128 TYR A OH  
1067 N  N   . GLY A 128 ? 0.1648 0.1215 0.1915 -0.0038 -0.0091 -0.0140 129 GLY A N   
1068 C  CA  . GLY A 128 ? 0.2057 0.1350 0.2100 -0.0113 -0.0291 -0.0408 129 GLY A CA  
1069 C  C   . GLY A 128 ? 0.1656 0.1579 0.1933 -0.0203 -0.0192 -0.0212 129 GLY A C   
1070 O  O   . GLY A 128 ? 0.1924 0.1375 0.2310 -0.0149 -0.0220 -0.0140 129 GLY A O   
1071 N  N   . ASP A 129 ? 0.1919 0.1342 0.2166 0.0108  -0.0295 -0.0105 130 ASP A N   
1072 C  CA  . ASP A 129 ? 0.1941 0.1411 0.2343 -0.0197 -0.0575 0.0300  130 ASP A CA  
1073 C  C   . ASP A 129 ? 0.1432 0.1552 0.2454 0.0258  -0.0060 0.0024  130 ASP A C   
1074 O  O   . ASP A 129 ? 0.1495 0.1430 0.2612 0.0131  -0.0125 -0.0063 130 ASP A O   
1075 C  CB  . ASP A 129 ? 0.2048 0.2567 0.2470 -0.0447 -0.0562 0.0636  130 ASP A CB  
1076 C  CG  . ASP A 129 ? 0.3072 0.1224 0.2721 -0.0414 -0.0608 0.0640  130 ASP A CG  
1077 O  OD1 . ASP A 129 ? 0.2538 0.2748 0.5601 -0.0441 0.0147  -0.0866 130 ASP A OD1 
1078 O  OD2 . ASP A 129 ? 0.6773 0.2748 0.3610 -0.2143 -0.0496 -0.0467 130 ASP A OD2 
1079 N  N   . PHE A 130 ? 0.1554 0.1376 0.2346 0.0065  -0.0606 0.0310  131 PHE A N   
1080 C  CA  . PHE A 130 ? 0.1884 0.1499 0.2917 0.0043  -0.0361 0.0049  131 PHE A CA  
1081 C  C   . PHE A 130 ? 0.2012 0.1796 0.2425 0.0017  -0.0121 0.0010  131 PHE A C   
1082 O  O   . PHE A 130 ? 0.1581 0.1601 0.2111 0.0076  -0.0273 0.0000  131 PHE A O   
1083 C  CB  . PHE A 130 ? 0.1942 0.1974 0.3156 0.0597  -0.0741 0.0103  131 PHE A CB  
1084 C  CG  . PHE A 130 ? 0.2960 0.2702 0.3380 0.0019  -0.0663 0.0608  131 PHE A CG  
1085 C  CD1 . PHE A 130 ? 0.2632 0.3783 0.4621 -0.0264 -0.0621 0.1074  131 PHE A CD1 
1086 C  CD2 . PHE A 130 ? 0.3499 0.2560 0.3120 0.1620  0.0217  0.0197  131 PHE A CD2 
1087 C  CE1 . PHE A 130 ? 0.3637 0.4453 0.4815 -0.1008 -0.1259 0.0803  131 PHE A CE1 
1088 C  CE2 . PHE A 130 ? 0.4887 0.3788 0.4279 0.0520  -0.1263 0.1503  131 PHE A CE2 
1089 C  CZ  . PHE A 130 ? 0.5156 0.6299 0.5067 -0.0276 -0.1439 0.2418  131 PHE A CZ  
1090 N  N   . GLY A 131 ? 0.2007 0.2068 0.2068 0.0272  -0.0483 0.0044  132 GLY A N   
1091 C  CA  . GLY A 131 ? 0.1960 0.1996 0.2068 0.0000  -0.0266 -0.0102 132 GLY A CA  
1092 C  C   . GLY A 131 ? 0.2310 0.1876 0.1967 0.0015  -0.0467 -0.0274 132 GLY A C   
1093 O  O   . GLY A 131 ? 0.2614 0.1809 0.2413 0.0294  -0.0230 -0.0132 132 GLY A O   
1094 N  N   . LYS A 132 ? 0.2395 0.1504 0.2179 -0.0082 -0.0733 -0.0307 133 LYS A N   
1095 C  CA  . LYS A 132 ? 0.2075 0.1453 0.2328 0.0034  -0.0476 -0.0421 133 LYS A CA  
1096 C  C   . LYS A 132 ? 0.1687 0.1572 0.1922 -0.0105 0.0156  -0.0412 133 LYS A C   
1097 O  O   . LYS A 132 ? 0.1709 0.1448 0.1860 0.0210  -0.0120 -0.0370 133 LYS A O   
1098 C  CB  . LYS A 132 ? 0.2732 0.1380 0.2465 0.0000  -0.0046 -0.0300 133 LYS A CB  
1099 C  CG  . LYS A 132 ? 0.3230 0.2084 0.2876 -0.0795 0.0030  -0.0414 133 LYS A CG  
1100 C  CD  . LYS A 132 ? 0.4277 0.3440 0.3838 -0.0270 0.1212  0.1090  133 LYS A CD  
1101 C  CE  . LYS A 132 ? 0.4671 0.4352 0.5264 0.0687  0.0303  0.0844  133 LYS A CE  
1102 N  NZ  . LYS A 132 ? 0.7347 0.6399 0.5550 0.0452  -0.0261 0.0824  133 LYS A NZ  
1103 N  N   . ALA A 133 ? 0.1608 0.1333 0.1653 0.0285  -0.0248 -0.0291 134 ALA A N   
1104 C  CA  . ALA A 133 ? 0.1457 0.1456 0.1642 -0.0007 -0.0256 -0.0153 134 ALA A CA  
1105 C  C   . ALA A 133 ? 0.1522 0.1365 0.1523 0.0146  -0.0074 -0.0195 134 ALA A C   
1106 O  O   . ALA A 133 ? 0.1376 0.1441 0.1586 0.0129  -0.0135 -0.0129 134 ALA A O   
1107 C  CB  . ALA A 133 ? 0.1622 0.1299 0.1777 0.0160  -0.0162 -0.0243 134 ALA A CB  
1108 N  N   . VAL A 134 ? 0.1596 0.1252 0.1594 0.0239  -0.0096 -0.0219 135 VAL A N   
1109 C  CA  . VAL A 134 ? 0.1646 0.1553 0.1856 -0.0063 -0.0250 0.0089  135 VAL A CA  
1110 C  C   . VAL A 134 ? 0.1872 0.1678 0.1222 -0.0065 -0.0463 -0.0175 135 VAL A C   
1111 O  O   . VAL A 134 ? 0.1987 0.1723 0.1603 0.0092  -0.0276 -0.0003 135 VAL A O   
1112 C  CB  . VAL A 134 ? 0.1712 0.1678 0.1484 0.0234  -0.0450 -0.0178 135 VAL A CB  
1113 C  CG1 . VAL A 134 ? 0.2039 0.2050 0.1633 0.0577  -0.0276 -0.0137 135 VAL A CG1 
1114 C  CG2 . VAL A 134 ? 0.2425 0.1975 0.1456 0.0248  -0.0405 -0.0057 135 VAL A CG2 
1115 N  N   . GLN A 135 ? 0.1815 0.1545 0.1511 0.0197  -0.0372 -0.0205 136 GLN A N   
1116 C  CA  . GLN A 135 ? 0.1892 0.1613 0.1941 0.0198  -0.0226 -0.0153 136 GLN A CA  
1117 C  C   . GLN A 135 ? 0.1867 0.1610 0.1780 0.0399  -0.0164 -0.0035 136 GLN A C   
1118 O  O   . GLN A 135 ? 0.2154 0.2140 0.2143 0.0315  -0.0027 -0.0461 136 GLN A O   
1119 C  CB  . GLN A 135 ? 0.2278 0.1723 0.1834 0.0000  -0.0078 -0.0340 136 GLN A CB  
1120 C  CG  . GLN A 135 ? 0.2608 0.2610 0.2305 -0.0219 -0.0443 -0.0720 136 GLN A CG  
1121 C  CD  . GLN A 135 ? 0.3705 0.3237 0.2379 -0.0118 -0.0472 -0.1080 136 GLN A CD  
1122 O  OE1 . GLN A 135 ? 0.4465 0.4743 0.4251 0.0656  -0.0035 -0.1253 136 GLN A OE1 
1123 N  NE2 . GLN A 135 ? 0.3359 0.3896 0.3887 -0.0582 0.0107  -0.0854 136 GLN A NE2 
1124 N  N   . GLN A 136 ? 0.1791 0.1271 0.1473 -0.0059 -0.0245 -0.0041 137 GLN A N   
1125 C  CA  . GLN A 136 ? 0.1405 0.1595 0.1875 0.0454  -0.0381 -0.0151 137 GLN A CA  
1126 C  C   . GLN A 136 ? 0.1356 0.1571 0.1684 0.0110  0.0046  0.0041  137 GLN A C   
1127 O  O   . GLN A 136 ? 0.1532 0.1477 0.1719 0.0203  -0.0186 0.0114  137 GLN A O   
1128 C  CB  . GLN A 136 ? 0.1773 0.1637 0.2030 0.0164  -0.0082 -0.0320 137 GLN A CB  
1129 C  CG  . GLN A 136 ? 0.2391 0.1883 0.2456 -0.0098 -0.0192 -0.0006 137 GLN A CG  
1130 C  CD  . GLN A 136 ? 0.2639 0.2827 0.2375 -0.0126 0.0226  0.0114  137 GLN A CD  
1131 O  OE1 . GLN A 136 ? 0.2617 0.2240 0.2811 0.0410  -0.0329 -0.0035 137 GLN A OE1 
1132 N  NE2 . GLN A 136 ? 0.3325 0.3303 0.3420 0.0646  -0.0553 -0.0412 137 GLN A NE2 
1133 N  N   . PRO A 137 ? 0.1294 0.1450 0.1256 0.0179  -0.0037 -0.0097 138 PRO A N   
1134 C  CA  . PRO A 137 ? 0.1274 0.1662 0.1750 0.0194  -0.0102 -0.0052 138 PRO A CA  
1135 C  C   . PRO A 137 ? 0.1136 0.1545 0.1393 0.0076  -0.0147 0.0142  138 PRO A C   
1136 O  O   . PRO A 137 ? 0.1829 0.1786 0.1791 -0.0116 -0.0124 0.0379  138 PRO A O   
1137 C  CB  . PRO A 137 ? 0.1357 0.2343 0.2402 0.0034  -0.0595 0.0439  138 PRO A CB  
1138 C  CG  . PRO A 137 ? 0.1851 0.2333 0.2973 0.0220  -0.0179 -0.0344 138 PRO A CG  
1139 C  CD  . PRO A 137 ? 0.2050 0.1992 0.2060 0.0793  -0.0130 -0.0458 138 PRO A CD  
1140 N  N   . ASP A 138 ? 0.1206 0.1378 0.1349 0.0093  0.0093  0.0048  139 ASP A N   
1141 C  CA  . ASP A 138 ? 0.1396 0.1626 0.1199 0.0078  -0.0276 -0.0109 139 ASP A CA  
1142 C  C   . ASP A 138 ? 0.1493 0.1066 0.1254 0.0081  -0.0057 -0.0065 139 ASP A C   
1143 O  O   . ASP A 138 ? 0.1371 0.1290 0.1532 0.0193  0.0038  0.0189  139 ASP A O   
1144 C  CB  . ASP A 138 ? 0.1439 0.1538 0.1644 0.0103  -0.0423 -0.0054 139 ASP A CB  
1145 C  CG  . ASP A 138 ? 0.1360 0.1653 0.1796 0.0467  -0.0217 0.0098  139 ASP A CG  
1146 O  OD1 . ASP A 138 ? 0.1629 0.1568 0.1867 0.0344  -0.0114 0.0231  139 ASP A OD1 
1147 O  OD2 . ASP A 138 ? 0.2025 0.2073 0.2249 0.0467  -0.0461 0.0454  139 ASP A OD2 
1148 N  N   . GLY A 139 ? 0.1195 0.1168 0.1272 0.0208  -0.0201 -0.0195 140 GLY A N   
1149 C  CA  . GLY A 139 ? 0.1030 0.1271 0.1542 0.0076  0.0040  -0.0184 140 GLY A CA  
1150 C  C   . GLY A 139 ? 0.1146 0.0992 0.1389 0.0113  -0.0234 -0.0046 140 GLY A C   
1151 O  O   . GLY A 139 ? 0.1281 0.1096 0.1448 0.0043  0.0023  -0.0046 140 GLY A O   
1152 N  N   . LEU A 140 ? 0.1143 0.0894 0.1296 0.0071  -0.0003 -0.0020 141 LEU A N   
1153 C  CA  . LEU A 140 ? 0.1143 0.1049 0.1030 0.0161  -0.0063 -0.0043 141 LEU A CA  
1154 C  C   . LEU A 140 ? 0.1094 0.1040 0.1319 0.0065  0.0080  -0.0126 141 LEU A C   
1155 O  O   . LEU A 140 ? 0.1141 0.0922 0.1260 0.0070  -0.0083 -0.0076 141 LEU A O   
1156 C  CB  . LEU A 140 ? 0.1333 0.1142 0.1147 0.0057  -0.0221 -0.0027 141 LEU A CB  
1157 C  CG  . LEU A 140 ? 0.1488 0.1301 0.1342 0.0102  -0.0148 0.0024  141 LEU A CG  
1158 C  CD1 . LEU A 140 ? 0.1705 0.1563 0.1479 0.0063  -0.0333 0.0208  141 LEU A CD1 
1159 C  CD2 . LEU A 140 ? 0.1705 0.1310 0.1676 0.0038  -0.0041 0.0092  141 LEU A CD2 
1160 N  N   . ALA A 141 ? 0.1217 0.0933 0.1161 0.0194  0.0156  0.0015  142 ALA A N   
1161 C  CA  . ALA A 141 ? 0.1093 0.1102 0.1279 0.0204  -0.0147 -0.0081 142 ALA A CA  
1162 C  C   . ALA A 141 ? 0.0942 0.1019 0.0991 0.0049  0.0137  0.0100  142 ALA A C   
1163 O  O   . ALA A 141 ? 0.1019 0.0985 0.1425 -0.0015 0.0081  -0.0032 142 ALA A O   
1164 C  CB  . ALA A 141 ? 0.1429 0.1194 0.1230 -0.0174 -0.0091 0.0015  142 ALA A CB  
1165 N  N   . VAL A 142 ? 0.1176 0.0852 0.1041 -0.0015 0.0063  0.0006  143 VAL A N   
1166 C  CA  . VAL A 142 ? 0.1130 0.1086 0.1061 0.0190  -0.0027 -0.0005 143 VAL A CA  
1167 C  C   . VAL A 142 ? 0.0861 0.0710 0.1071 -0.0049 -0.0049 0.0049  143 VAL A C   
1168 O  O   . VAL A 142 ? 0.0922 0.0973 0.1080 -0.0062 0.0013  -0.0078 143 VAL A O   
1169 C  CB  . VAL A 142 ? 0.1107 0.0906 0.1089 0.0035  -0.0030 0.0086  143 VAL A CB  
1170 C  CG1 . VAL A 142 ? 0.1186 0.1146 0.0976 0.0198  -0.0108 0.0066  143 VAL A CG1 
1171 C  CG2 . VAL A 142 ? 0.1277 0.1188 0.1216 0.0066  0.0226  -0.0068 143 VAL A CG2 
1172 N  N   . LEU A 143 ? 0.1014 0.0827 0.0980 0.0019  0.0057  -0.0063 144 LEU A N   
1173 C  CA  . LEU A 143 ? 0.1068 0.0794 0.1172 0.0065  0.0091  0.0024  144 LEU A CA  
1174 C  C   . LEU A 143 ? 0.0798 0.0931 0.0870 0.0071  -0.0041 -0.0085 144 LEU A C   
1175 O  O   . LEU A 143 ? 0.1001 0.1028 0.1080 0.0034  -0.0121 -0.0052 144 LEU A O   
1176 C  CB  . LEU A 143 ? 0.1355 0.1040 0.1185 -0.0144 0.0147  -0.0083 144 LEU A CB  
1177 C  CG  . LEU A 143 ? 0.1134 0.1331 0.0978 0.0113  0.0222  -0.0074 144 LEU A CG  
1178 C  CD1 . LEU A 143 ? 0.1432 0.1587 0.1461 -0.0176 0.0038  -0.0277 144 LEU A CD1 
1179 C  CD2 . LEU A 143 ? 0.1531 0.1605 0.1188 -0.0013 0.0498  -0.0054 144 LEU A CD2 
1180 N  N   . GLY A 144 ? 0.0951 0.0845 0.0939 0.0073  -0.0037 0.0062  145 GLY A N   
1181 C  CA  . GLY A 144 ? 0.1036 0.0724 0.0930 0.0000  -0.0105 -0.0024 145 GLY A CA  
1182 C  C   . GLY A 144 ? 0.0888 0.0847 0.1040 -0.0065 -0.0059 -0.0035 145 GLY A C   
1183 O  O   . GLY A 144 ? 0.1035 0.0985 0.1082 0.0020  -0.0094 0.0038  145 GLY A O   
1184 N  N   . ILE A 145 ? 0.0857 0.0818 0.1021 -0.0026 0.0116  -0.0040 146 ILE A N   
1185 C  CA  . ILE A 145 ? 0.0829 0.1021 0.0845 0.0182  0.0137  -0.0054 146 ILE A CA  
1186 C  C   . ILE A 145 ? 0.0956 0.1015 0.1008 0.0063  0.0019  -0.0041 146 ILE A C   
1187 O  O   . ILE A 145 ? 0.1193 0.1044 0.1185 0.0116  0.0040  -0.0219 146 ILE A O   
1188 C  CB  . ILE A 145 ? 0.1023 0.1012 0.0935 0.0049  0.0253  0.0013  146 ILE A CB  
1189 C  CG1 . ILE A 145 ? 0.1362 0.1294 0.1362 0.0000  0.0081  0.0306  146 ILE A CG1 
1190 C  CG2 . ILE A 145 ? 0.1522 0.1324 0.1353 0.0251  0.0359  -0.0149 146 ILE A CG2 
1191 C  CD1 . ILE A 145 ? 0.1298 0.1660 0.1606 -0.0286 0.0231  -0.0121 146 ILE A CD1 
1192 N  N   . PHE A 146 ? 0.0918 0.0874 0.1136 0.0074  0.0197  0.0092  147 PHE A N   
1193 C  CA  . PHE A 146 ? 0.0987 0.0942 0.1037 0.0142  0.0000  0.0065  147 PHE A CA  
1194 C  C   . PHE A 146 ? 0.1052 0.0927 0.1086 -0.0023 0.0082  -0.0113 147 PHE A C   
1195 O  O   . PHE A 146 ? 0.1228 0.1096 0.1204 0.0109  0.0052  0.0019  147 PHE A O   
1196 C  CB  . PHE A 146 ? 0.0982 0.1107 0.1297 0.0007  0.0171  -0.0063 147 PHE A CB  
1197 C  CG  . PHE A 146 ? 0.0992 0.0863 0.1066 -0.0143 0.0120  -0.0013 147 PHE A CG  
1198 C  CD1 . PHE A 146 ? 0.1193 0.0843 0.1128 0.0015  0.0062  0.0192  147 PHE A CD1 
1199 C  CD2 . PHE A 146 ? 0.1107 0.0847 0.1288 -0.0141 -0.0032 -0.0006 147 PHE A CD2 
1200 C  CE1 . PHE A 146 ? 0.1037 0.0935 0.1044 -0.0146 -0.0027 0.0015  147 PHE A CE1 
1201 C  CE2 . PHE A 146 ? 0.1152 0.0976 0.1121 -0.0015 -0.0099 -0.0219 147 PHE A CE2 
1202 C  CZ  . PHE A 146 ? 0.1096 0.0793 0.1048 -0.0060 -0.0031 -0.0020 147 PHE A CZ  
1203 N  N   . LEU A 147 ? 0.1028 0.1118 0.1314 0.0076  0.0038  0.0030  148 LEU A N   
1204 C  CA  . LEU A 147 ? 0.1003 0.1023 0.1152 0.0065  0.0012  -0.0026 148 LEU A CA  
1205 C  C   . LEU A 147 ? 0.1163 0.1149 0.1030 0.0035  -0.0027 -0.0175 148 LEU A C   
1206 O  O   . LEU A 147 ? 0.1295 0.0983 0.1301 -0.0068 0.0168  -0.0046 148 LEU A O   
1207 C  CB  . LEU A 147 ? 0.1188 0.1077 0.1271 0.0000  -0.0175 -0.0057 148 LEU A CB  
1208 C  CG  . LEU A 147 ? 0.1504 0.0851 0.1298 0.0149  0.0168  -0.0241 148 LEU A CG  
1209 C  CD1 . LEU A 147 ? 0.1351 0.0974 0.1629 0.0195  -0.0062 -0.0177 148 LEU A CD1 
1210 C  CD2 . LEU A 147 ? 0.1319 0.1133 0.1612 0.0028  -0.0161 -0.0089 148 LEU A CD2 
1211 N  N   . LYS A 148 ? 0.1174 0.1040 0.1385 0.0165  0.0027  -0.0176 149 LYS A N   
1212 C  CA  . LYS A 148 ? 0.1197 0.1082 0.1639 -0.0043 0.0087  0.0052  149 LYS A CA  
1213 C  C   . LYS A 148 ? 0.1301 0.1389 0.1353 0.0030  0.0133  0.0109  149 LYS A C   
1214 O  O   . LYS A 148 ? 0.1258 0.1262 0.1852 0.0063  0.0243  0.0141  149 LYS A O   
1215 C  CB  . LYS A 148 ? 0.1299 0.1259 0.1744 -0.0192 -0.0019 0.0019  149 LYS A CB  
1216 C  CG  . LYS A 148 ? 0.1712 0.1693 0.1707 -0.0185 -0.0024 -0.0175 149 LYS A CG  
1217 C  CD  . LYS A 148 ? 0.2120 0.2485 0.2212 -0.0359 0.0008  -0.0595 149 LYS A CD  
1218 C  CE  . LYS A 148 ? 0.2117 0.3700 0.2716 0.0057  -0.0094 -0.0564 149 LYS A CE  
1219 N  NZ  . LYS A 148 ? 0.5859 0.6122 0.4760 0.0100  -0.1439 -0.1976 149 LYS A NZ  
1220 N  N   . VAL A 149 ? 0.1360 0.1097 0.1793 0.0065  0.0021  0.0003  150 VAL A N   
1221 C  CA  . VAL A 149 ? 0.1347 0.1324 0.1972 0.0049  0.0087  -0.0219 150 VAL A CA  
1222 C  C   . VAL A 149 ? 0.1651 0.1315 0.1875 0.0222  0.0155  -0.0109 150 VAL A C   
1223 O  O   . VAL A 149 ? 0.1586 0.1518 0.1976 0.0074  0.0093  -0.0182 150 VAL A O   
1224 C  CB  . VAL A 149 ? 0.1571 0.1702 0.2021 0.0372  0.0153  -0.0164 150 VAL A CB  
1225 C  CG1 . VAL A 149 ? 0.1396 0.1576 0.2486 0.0233  0.0200  0.0133  150 VAL A CG1 
1226 C  CG2 . VAL A 149 ? 0.1901 0.1861 0.2046 -0.0012 0.0406  -0.0329 150 VAL A CG2 
1227 N  N   . GLY A 150 ? 0.1523 0.1259 0.1753 0.0094  -0.0007 -0.0126 151 GLY A N   
1228 C  CA  . GLY A 150 ? 0.1809 0.1588 0.2136 -0.0166 0.0340  -0.0564 151 GLY A CA  
1229 C  C   . GLY A 150 ? 0.1748 0.1382 0.1914 0.0121  0.0136  -0.0456 151 GLY A C   
1230 O  O   . GLY A 150 ? 0.1996 0.1527 0.2012 0.0255  0.0189  -0.0412 151 GLY A O   
1231 N  N   A SER A 151 ? 0.1951 0.1502 0.1965 0.0157  0.0208  -0.0406 152 SER A N   
1232 N  N   B SER A 151 ? 0.2001 0.1529 0.1972 0.0149  0.0207  -0.0401 152 SER A N   
1233 C  CA  A SER A 151 ? 0.1768 0.1723 0.2375 0.0054  0.0263  -0.0520 152 SER A CA  
1234 C  CA  B SER A 151 ? 0.1711 0.1787 0.2421 0.0149  0.0266  -0.0516 152 SER A CA  
1235 C  C   A SER A 151 ? 0.1653 0.1359 0.2535 0.0282  0.0240  -0.0288 152 SER A C   
1236 C  C   B SER A 151 ? 0.1756 0.1437 0.2612 0.0087  0.0298  -0.0263 152 SER A C   
1237 O  O   A SER A 151 ? 0.1479 0.1659 0.1498 0.0399  0.0401  0.0195  152 SER A O   
1238 O  O   B SER A 151 ? 0.1638 0.1620 0.1834 0.0230  -0.0010 -0.0189 152 SER A O   
1239 C  CB  A SER A 151 ? 0.2063 0.2768 0.2621 0.0274  -0.0476 -0.0087 152 SER A CB  
1240 C  CB  B SER A 151 ? 0.2317 0.2456 0.2457 0.0034  -0.0410 -0.0678 152 SER A CB  
1241 O  OG  A SER A 151 ? 0.2160 0.3061 0.2075 0.0379  -0.0450 0.0292  152 SER A OG  
1242 O  OG  B SER A 151 ? 0.2973 0.2872 0.1793 -0.0474 0.0162  -0.0908 152 SER A OG  
1243 N  N   . ALA A 152 ? 0.1590 0.1561 0.2355 0.0092  0.0184  -0.0071 153 ALA A N   
1244 C  CA  . ALA A 152 ? 0.1240 0.1508 0.2129 -0.0027 0.0065  0.0094  153 ALA A CA  
1245 C  C   . ALA A 152 ? 0.1534 0.1798 0.1782 0.0326  0.0024  -0.0100 153 ALA A C   
1246 O  O   . ALA A 152 ? 0.1938 0.1511 0.1806 0.0225  -0.0055 -0.0020 153 ALA A O   
1247 C  CB  . ALA A 152 ? 0.1357 0.1734 0.2224 0.0185  0.0020  -0.0083 153 ALA A CB  
1248 N  N   . LYS A 153 ? 0.1538 0.1242 0.2021 -0.0102 0.0291  -0.0082 154 LYS A N   
1249 C  CA  . LYS A 153 ? 0.1754 0.1694 0.2117 0.0044  0.0208  0.0223  154 LYS A CA  
1250 C  C   . LYS A 153 ? 0.1344 0.1568 0.1547 0.0480  0.0082  0.0000  154 LYS A C   
1251 O  O   . LYS A 153 ? 0.1425 0.1502 0.1805 0.0182  0.0143  -0.0093 154 LYS A O   
1252 C  CB  . LYS A 153 ? 0.1425 0.1491 0.2492 0.0219  0.0197  -0.0013 154 LYS A CB  
1253 C  CG  . LYS A 153 ? 0.1389 0.1815 0.2014 -0.0081 0.0109  0.0023  154 LYS A CG  
1254 C  CD  . LYS A 153 ? 0.1649 0.1637 0.2090 0.0256  0.0077  0.0149  154 LYS A CD  
1255 C  CE  . LYS A 153 ? 0.1849 0.1800 0.2457 0.0008  -0.0672 0.0165  154 LYS A CE  
1256 N  NZ  . LYS A 153 ? 0.2082 0.2199 0.2249 0.0344  -0.0220 0.0049  154 LYS A NZ  
1257 N  N   . PRO A 154 ? 0.1659 0.1710 0.1669 0.0263  0.0241  -0.0107 155 PRO A N   
1258 C  CA  . PRO A 154 ? 0.1601 0.2102 0.1656 -0.0031 0.0412  -0.0359 155 PRO A CA  
1259 C  C   . PRO A 154 ? 0.1398 0.1908 0.1541 -0.0005 0.0055  0.0017  155 PRO A C   
1260 O  O   . PRO A 154 ? 0.1703 0.2314 0.1919 -0.0071 0.0348  -0.0269 155 PRO A O   
1261 C  CB  . PRO A 154 ? 0.2046 0.2206 0.1684 -0.0065 0.0494  0.0006  155 PRO A CB  
1262 C  CG  . PRO A 154 ? 0.2552 0.3357 0.2458 -0.0439 0.0520  -0.0763 155 PRO A CG  
1263 C  CD  . PRO A 154 ? 0.2059 0.1881 0.1725 0.0013  0.0091  -0.0276 155 PRO A CD  
1264 N  N   . GLY A 155 ? 0.1842 0.1542 0.1463 0.0154  0.0381  0.0243  156 GLY A N   
1265 C  CA  . GLY A 155 ? 0.2061 0.1696 0.2041 0.0175  0.0383  0.0098  156 GLY A CA  
1266 C  C   . GLY A 155 ? 0.2002 0.1915 0.2122 -0.0041 0.0619  -0.0231 156 GLY A C   
1267 O  O   . GLY A 155 ? 0.2497 0.2188 0.2565 -0.0293 0.0408  -0.0153 156 GLY A O   
1268 N  N   . LEU A 156 ? 0.1477 0.1726 0.1841 0.0133  0.0322  -0.0023 157 LEU A N   
1269 C  CA  . LEU A 156 ? 0.1480 0.1470 0.1911 -0.0297 -0.0176 0.0031  157 LEU A CA  
1270 C  C   . LEU A 156 ? 0.1313 0.1127 0.1576 0.0073  0.0057  -0.0166 157 LEU A C   
1271 O  O   . LEU A 156 ? 0.1420 0.1418 0.1605 0.0124  0.0130  -0.0082 157 LEU A O   
1272 C  CB  . LEU A 156 ? 0.1342 0.1676 0.2070 -0.0207 0.0350  -0.0370 157 LEU A CB  
1273 C  CG  . LEU A 156 ? 0.1558 0.1547 0.1795 -0.0041 0.0265  -0.0274 157 LEU A CG  
1274 C  CD1 . LEU A 156 ? 0.1747 0.1660 0.2348 0.0057  0.0370  -0.0379 157 LEU A CD1 
1275 C  CD2 . LEU A 156 ? 0.1412 0.1425 0.2030 0.0070  0.0188  -0.0051 157 LEU A CD2 
1276 N  N   . GLN A 157 ? 0.1412 0.1545 0.2375 0.0201  0.0030  -0.0299 158 GLN A N   
1277 C  CA  . GLN A 157 ? 0.1305 0.2251 0.1816 0.0549  0.0120  -0.0357 158 GLN A CA  
1278 C  C   . GLN A 157 ? 0.1568 0.1833 0.1825 -0.0013 0.0215  0.0146  158 GLN A C   
1279 O  O   . GLN A 157 ? 0.1560 0.1967 0.2060 0.0254  0.0255  -0.0046 158 GLN A O   
1280 C  CB  . GLN A 157 ? 0.1893 0.1938 0.1580 0.0566  0.0031  -0.0405 158 GLN A CB  
1281 C  CG  . GLN A 157 ? 0.1703 0.2314 0.2425 0.0557  -0.0024 0.0256  158 GLN A CG  
1282 C  CD  . GLN A 157 ? 0.1633 0.1596 0.1928 0.0163  -0.0296 -0.0100 158 GLN A CD  
1283 O  OE1 . GLN A 157 ? 0.1635 0.1567 0.2547 0.0103  -0.0148 -0.0172 158 GLN A OE1 
1284 N  NE2 . GLN A 157 ? 0.2063 0.2014 0.2479 0.0632  -0.0386 -0.0230 158 GLN A NE2 
1285 N  N   . LYS A 158 ? 0.1244 0.1938 0.2312 0.0074  0.0221  -0.0003 159 LYS A N   
1286 C  CA  . LYS A 158 ? 0.1453 0.2266 0.2082 -0.0296 0.0111  -0.0038 159 LYS A CA  
1287 C  C   . LYS A 158 ? 0.1335 0.1732 0.2071 0.0144  -0.0141 -0.0144 159 LYS A C   
1288 O  O   . LYS A 158 ? 0.1800 0.1930 0.2278 0.0083  0.0024  -0.0193 159 LYS A O   
1289 C  CB  . LYS A 158 ? 0.2114 0.1931 0.3301 -0.0612 0.0359  -0.0007 159 LYS A CB  
1290 C  CG  . LYS A 158 ? 0.3068 0.3458 0.3653 -0.0271 0.0744  -0.0012 159 LYS A CG  
1291 C  CD  . LYS A 158 ? 0.5160 0.4104 0.4083 -0.0138 0.0410  0.0908  159 LYS A CD  
1292 C  CE  . LYS A 158 ? 0.4963 0.4334 0.5997 0.0830  0.1453  0.0230  159 LYS A CE  
1293 N  NZ  . LYS A 158 ? 0.5634 0.7253 0.3984 -0.1169 0.0044  -0.0035 159 LYS A NZ  
1294 N  N   . VAL A 159 ? 0.1170 0.1367 0.1653 -0.0003 0.0044  0.0062  160 VAL A N   
1295 C  CA  . VAL A 159 ? 0.1149 0.1847 0.1684 0.0040  0.0049  0.0149  160 VAL A CA  
1296 C  C   . VAL A 159 ? 0.1412 0.1376 0.1596 -0.0030 0.0125  -0.0115 160 VAL A C   
1297 O  O   . VAL A 159 ? 0.1678 0.1495 0.1764 0.0189  0.0148  -0.0187 160 VAL A O   
1298 C  CB  . VAL A 159 ? 0.1231 0.1714 0.1683 0.0193  -0.0003 0.0003  160 VAL A CB  
1299 C  CG1 . VAL A 159 ? 0.1884 0.2021 0.1685 0.0041  0.0505  -0.0419 160 VAL A CG1 
1300 C  CG2 . VAL A 159 ? 0.1561 0.2087 0.2395 0.0337  0.0041  0.0584  160 VAL A CG2 
1301 N  N   . VAL A 160 ? 0.1538 0.1380 0.2055 0.0302  0.0027  -0.0276 161 VAL A N   
1302 C  CA  . VAL A 160 ? 0.1660 0.1858 0.2157 0.0071  -0.0204 -0.0148 161 VAL A CA  
1303 C  C   . VAL A 160 ? 0.1703 0.1378 0.1737 0.0063  -0.0113 -0.0198 161 VAL A C   
1304 O  O   . VAL A 160 ? 0.2036 0.1729 0.2030 0.0463  -0.0041 -0.0227 161 VAL A O   
1305 C  CB  . VAL A 160 ? 0.2290 0.1536 0.2515 0.0005  -0.0241 -0.0153 161 VAL A CB  
1306 C  CG1 . VAL A 160 ? 0.2167 0.2003 0.2827 0.0747  0.0577  -0.0091 161 VAL A CG1 
1307 C  CG2 . VAL A 160 ? 0.2626 0.1540 0.3240 0.0272  -0.0207 -0.0006 161 VAL A CG2 
1308 N  N   . ASP A 161 ? 0.1653 0.1913 0.2576 0.0351  -0.0010 -0.0270 162 ASP A N   
1309 C  CA  . ASP A 161 ? 0.1642 0.1969 0.2353 0.0425  -0.0012 -0.0181 162 ASP A CA  
1310 C  C   . ASP A 161 ? 0.1757 0.1998 0.2522 0.0315  -0.0245 -0.0083 162 ASP A C   
1311 O  O   . ASP A 161 ? 0.2064 0.2892 0.2597 0.0654  -0.0428 -0.0546 162 ASP A O   
1312 C  CB  . ASP A 161 ? 0.1971 0.2897 0.2303 0.0641  0.0227  -0.0377 162 ASP A CB  
1313 C  CG  . ASP A 161 ? 0.2077 0.2856 0.3188 0.0760  -0.0209 0.0015  162 ASP A CG  
1314 O  OD1 . ASP A 161 ? 0.3314 0.2964 0.3950 0.0756  0.0342  -0.0071 162 ASP A OD1 
1315 O  OD2 . ASP A 161 ? 0.2132 0.3928 0.3637 0.0851  -0.0082 -0.0229 162 ASP A OD2 
1316 N  N   . VAL A 162 ? 0.1378 0.1933 0.1847 0.0098  -0.0104 -0.0271 163 VAL A N   
1317 C  CA  . VAL A 162 ? 0.1588 0.2272 0.2711 -0.0074 -0.0220 -0.0185 163 VAL A CA  
1318 C  C   . VAL A 162 ? 0.1624 0.2073 0.2328 0.0155  -0.0142 -0.0337 163 VAL A C   
1319 O  O   . VAL A 162 ? 0.1893 0.2001 0.2434 0.0098  -0.0372 -0.0337 163 VAL A O   
1320 C  CB  . VAL A 162 ? 0.1969 0.2109 0.3743 -0.0237 -0.0562 -0.0152 163 VAL A CB  
1321 C  CG1 . VAL A 162 ? 0.2292 0.1753 0.2635 0.0370  0.0080  -0.0280 163 VAL A CG1 
1322 C  CG2 . VAL A 162 ? 0.2709 0.2657 0.4347 -0.0496 -0.0749 -0.0262 163 VAL A CG2 
1323 N  N   . LEU A 163 ? 0.1659 0.1709 0.2263 0.0041  0.0104  -0.0163 164 LEU A N   
1324 C  CA  . LEU A 163 ? 0.1906 0.1547 0.1953 -0.0196 -0.0192 -0.0194 164 LEU A CA  
1325 C  C   . LEU A 163 ? 0.1437 0.2030 0.1831 -0.0189 -0.0077 -0.0115 164 LEU A C   
1326 O  O   . LEU A 163 ? 0.1750 0.1773 0.1827 -0.0057 -0.0296 -0.0027 164 LEU A O   
1327 C  CB  . LEU A 163 ? 0.1847 0.1486 0.2018 -0.0115 -0.0143 -0.0007 164 LEU A CB  
1328 C  CG  . LEU A 163 ? 0.1552 0.1188 0.2159 -0.0051 -0.0172 -0.0168 164 LEU A CG  
1329 C  CD1 . LEU A 163 ? 0.1827 0.1694 0.2133 -0.0373 0.0110  0.0086  164 LEU A CD1 
1330 C  CD2 . LEU A 163 ? 0.1590 0.1568 0.1872 0.0170  -0.0236 -0.0220 164 LEU A CD2 
1331 N  N   . ASP A 164 ? 0.1698 0.1938 0.2707 0.0054  -0.0555 -0.0399 165 ASP A N   
1332 C  CA  . ASP A 164 ? 0.2384 0.2415 0.2800 0.0546  -0.0590 -0.0425 165 ASP A CA  
1333 C  C   . ASP A 164 ? 0.1917 0.2402 0.3273 -0.0397 -0.0592 -0.0049 165 ASP A C   
1334 O  O   . ASP A 164 ? 0.3303 0.3291 0.3653 -0.0037 -0.1643 0.0403  165 ASP A O   
1335 C  CB  . ASP A 164 ? 0.3192 0.2414 0.3215 0.1190  -0.0452 -0.0146 165 ASP A CB  
1336 C  CG  . ASP A 164 ? 0.2966 0.4451 0.4668 0.1111  0.0315  -0.0496 165 ASP A CG  
1337 O  OD1 . ASP A 164 ? 0.4826 0.4878 0.5048 0.1178  -0.1202 -0.0344 165 ASP A OD1 
1338 O  OD2 . ASP A 164 ? 0.5225 0.7781 0.6326 0.2275  -0.2255 -0.1309 165 ASP A OD2 
1339 N  N   . SER A 165 ? 0.1486 0.2229 0.2379 -0.0030 -0.0362 -0.0284 166 SER A N   
1340 C  CA  . SER A 165 ? 0.1580 0.2262 0.2628 0.0040  -0.0458 -0.0247 166 SER A CA  
1341 C  C   . SER A 165 ? 0.1969 0.1901 0.2377 0.0137  -0.0507 -0.0265 166 SER A C   
1342 O  O   . SER A 165 ? 0.2041 0.2019 0.2387 -0.0313 -0.0441 -0.0275 166 SER A O   
1343 C  CB  . SER A 165 ? 0.3088 0.2750 0.2330 -0.0298 -0.0281 0.0093  166 SER A CB  
1344 O  OG  . SER A 165 ? 0.2423 0.2393 0.3140 -0.0265 -0.0093 -0.0099 166 SER A OG  
1345 N  N   . ILE A 166 ? 0.1753 0.1989 0.1716 -0.0040 -0.0205 -0.0225 167 ILE A N   
1346 C  CA  . ILE A 166 ? 0.1766 0.1782 0.2517 -0.0055 -0.0126 0.0115  167 ILE A CA  
1347 C  C   . ILE A 166 ? 0.1594 0.1520 0.2230 0.0192  -0.0035 0.0023  167 ILE A C   
1348 O  O   . ILE A 166 ? 0.1657 0.1529 0.1868 -0.0017 -0.0284 -0.0324 167 ILE A O   
1349 C  CB  . ILE A 166 ? 0.1574 0.1529 0.2267 -0.0186 -0.0390 -0.0116 167 ILE A CB  
1350 C  CG1 . ILE A 166 ? 0.1565 0.1683 0.1633 0.0163  -0.0329 -0.0049 167 ILE A CG1 
1351 C  CG2 . ILE A 166 ? 0.2296 0.1892 0.1939 -0.0186 -0.0077 0.0081  167 ILE A CG2 
1352 C  CD1 . ILE A 166 ? 0.1802 0.1612 0.2001 0.0403  -0.0256 -0.0124 167 ILE A CD1 
1353 N  N   . LYS A 167 ? 0.1651 0.1660 0.2122 0.0040  -0.0286 0.0152  168 LYS A N   
1354 C  CA  . LYS A 167 ? 0.1772 0.1850 0.1814 -0.0006 -0.0348 0.0156  168 LYS A CA  
1355 C  C   . LYS A 167 ? 0.1939 0.1558 0.2281 0.0149  -0.0089 -0.0091 168 LYS A C   
1356 O  O   . LYS A 167 ? 0.1763 0.1915 0.1743 0.0165  -0.0299 -0.0141 168 LYS A O   
1357 C  CB  . LYS A 167 ? 0.1709 0.2115 0.2402 0.0438  -0.0078 0.0136  168 LYS A CB  
1358 C  CG  . LYS A 167 ? 0.2459 0.1951 0.3075 0.0173  -0.0344 -0.0114 168 LYS A CG  
1359 C  CD  . LYS A 167 ? 0.2842 0.2910 0.4988 0.0637  -0.0423 0.0965  168 LYS A CD  
1360 C  CE  . LYS A 167 ? 0.3801 0.3488 0.5710 0.0086  0.0129  0.0900  168 LYS A CE  
1361 N  NZ  . LYS A 167 ? 0.6972 0.6363 0.4059 0.1680  -0.0804 0.0262  168 LYS A NZ  
1362 N  N   . THR A 168 ? 0.2003 0.1759 0.1689 -0.0109 -0.0333 -0.0149 169 THR A N   
1363 C  CA  . THR A 168 ? 0.1800 0.2069 0.2052 0.0549  -0.0287 -0.0298 169 THR A CA  
1364 C  C   . THR A 168 ? 0.1798 0.1606 0.1527 -0.0288 -0.0156 -0.0718 169 THR A C   
1365 O  O   . THR A 168 ? 0.1796 0.1844 0.2086 -0.0082 -0.0527 -0.0156 169 THR A O   
1366 C  CB  . THR A 168 ? 0.2246 0.2163 0.2442 0.0162  -0.0781 -0.0278 169 THR A CB  
1367 O  OG1 . THR A 168 ? 0.2226 0.2511 0.2560 -0.0063 -0.0450 -0.0100 169 THR A OG1 
1368 C  CG2 . THR A 168 ? 0.2321 0.2312 0.2156 0.0148  -0.0533 -0.0114 169 THR A CG2 
1369 N  N   . LYS A 169 ? 0.1962 0.2217 0.1827 0.0509  -0.0219 -0.0460 170 LYS A N   
1370 C  CA  . LYS A 169 ? 0.1798 0.1439 0.1705 0.0093  -0.0232 -0.0110 170 LYS A CA  
1371 C  C   . LYS A 169 ? 0.2348 0.2239 0.2125 -0.0294 -0.0175 -0.0003 170 LYS A C   
1372 O  O   . LYS A 169 ? 0.2469 0.2646 0.2244 -0.0553 -0.0496 -0.0263 170 LYS A O   
1373 C  CB  . LYS A 169 ? 0.2271 0.2003 0.1910 0.0034  0.0086  -0.0017 170 LYS A CB  
1374 C  CG  . LYS A 169 ? 0.2104 0.1972 0.2133 0.0066  -0.0141 -0.0118 170 LYS A CG  
1375 C  CD  . LYS A 169 ? 0.2549 0.2402 0.2833 0.0010  0.0392  -0.0458 170 LYS A CD  
1376 C  CE  . LYS A 169 ? 0.3851 0.3456 0.4032 0.0842  0.1053  -0.1005 170 LYS A CE  
1377 N  NZ  . LYS A 169 ? 0.5273 0.6934 0.4330 0.0675  0.1842  0.0159  170 LYS A NZ  
1378 N  N   . GLY A 170 ? 0.1990 0.1588 0.1506 -0.0273 0.0043  -0.0225 171 GLY A N   
1379 C  CA  . GLY A 170 ? 0.2384 0.1953 0.2120 -0.0527 0.0250  -0.0610 171 GLY A CA  
1380 C  C   . GLY A 170 ? 0.2680 0.2023 0.1587 0.0098  0.0177  -0.0337 171 GLY A C   
1381 O  O   . GLY A 170 ? 0.3179 0.1928 0.3670 -0.0220 -0.0074 -0.0795 171 GLY A O   
1382 N  N   . LYS A 171 ? 0.1872 0.1888 0.2163 0.0052  -0.0181 -0.0538 172 LYS A N   
1383 C  CA  . LYS A 171 ? 0.1908 0.1559 0.1457 -0.0131 -0.0249 -0.0337 172 LYS A CA  
1384 C  C   . LYS A 171 ? 0.1865 0.1840 0.1492 -0.0124 -0.0248 -0.0193 172 LYS A C   
1385 O  O   . LYS A 171 ? 0.1572 0.1782 0.1947 -0.0164 -0.0386 -0.0229 172 LYS A O   
1386 C  CB  . LYS A 171 ? 0.1896 0.1402 0.1859 0.0000  -0.0060 0.0131  172 LYS A CB  
1387 C  CG  . LYS A 171 ? 0.2265 0.2658 0.2447 0.0410  -0.0080 0.0505  172 LYS A CG  
1388 C  CD  . LYS A 171 ? 0.3328 0.2481 0.2538 0.0675  -0.0215 0.0264  172 LYS A CD  
1389 C  CE  . LYS A 171 ? 0.4120 0.5274 0.3903 0.1102  -0.1031 0.0483  172 LYS A CE  
1390 N  NZ  . LYS A 171 ? 0.3535 0.4866 0.6772 -0.1107 0.0186  -0.0846 172 LYS A NZ  
1391 N  N   . SER A 172 ? 0.1976 0.1903 0.2141 -0.0083 -0.0080 0.0186  173 SER A N   
1392 C  CA  . SER A 172 ? 0.1646 0.1732 0.1899 -0.0397 -0.0189 0.0041  173 SER A CA  
1393 C  C   . SER A 172 ? 0.1680 0.1969 0.2117 0.0030  -0.0291 -0.0152 173 SER A C   
1394 O  O   . SER A 172 ? 0.1699 0.2678 0.2415 -0.0395 -0.0886 0.0175  173 SER A O   
1395 C  CB  . SER A 172 ? 0.1929 0.1720 0.2208 -0.0200 -0.0296 -0.0452 173 SER A CB  
1396 O  OG  . SER A 172 ? 0.2840 0.2019 0.2294 -0.0649 -0.0353 -0.0284 173 SER A OG  
1397 N  N   . ALA A 173 ? 0.1692 0.1835 0.1861 -0.0653 -0.0093 -0.0034 174 ALA A N   
1398 C  CA  . ALA A 173 ? 0.1908 0.2405 0.1946 0.0196  0.0207  0.0364  174 ALA A CA  
1399 C  C   . ALA A 173 ? 0.1646 0.2434 0.1820 -0.0386 -0.0160 0.0120  174 ALA A C   
1400 O  O   . ALA A 173 ? 0.1597 0.2036 0.1829 -0.0322 -0.0243 0.0185  174 ALA A O   
1401 C  CB  . ALA A 173 ? 0.1921 0.2693 0.1829 0.0195  0.0165  0.0122  174 ALA A CB  
1402 N  N   A ASP A 174 ? 0.1799 0.3018 0.2624 -0.0830 -0.0137 0.0705  175 ASP A N   
1403 N  N   B ASP A 174 ? 0.1748 0.1590 0.1617 -0.0054 0.0019  0.0357  175 ASP A N   
1404 C  CA  A ASP A 174 ? 0.1755 0.2549 0.2114 -0.0684 -0.0195 -0.0063 175 ASP A CA  
1405 C  CA  B ASP A 174 ? 0.1608 0.2070 0.1350 -0.0390 -0.0212 0.0074  175 ASP A CA  
1406 C  C   A ASP A 174 ? 0.2010 0.2484 0.1463 0.0082  0.0026  0.0012  175 ASP A C   
1407 C  C   B ASP A 174 ? 0.2145 0.2099 0.1536 0.0250  0.0074  -0.0201 175 ASP A C   
1408 O  O   A ASP A 174 ? 0.1978 0.2266 0.2958 -0.0467 -0.0223 0.0307  175 ASP A O   
1409 O  O   B ASP A 174 ? 0.1389 0.2077 0.1671 -0.0098 0.0487  0.0220  175 ASP A O   
1410 C  CB  A ASP A 174 ? 0.1387 0.3925 0.3531 -0.0359 -0.0175 0.0306  175 ASP A CB  
1411 C  CB  B ASP A 174 ? 0.1732 0.1817 0.1820 -0.0187 0.0041  0.0148  175 ASP A CB  
1412 C  CG  A ASP A 174 ? 0.3727 0.3768 0.5950 -0.0883 0.0243  -0.0516 175 ASP A CG  
1413 C  CG  B ASP A 174 ? 0.2208 0.2653 0.2422 0.0222  0.0167  -0.0261 175 ASP A CG  
1414 O  OD1 A ASP A 174 ? 0.3088 0.2380 0.4336 -0.1054 0.0073  0.0736  175 ASP A OD1 
1415 O  OD1 B ASP A 174 ? 0.2827 0.4077 0.2536 0.0149  0.0043  0.0065  175 ASP A OD1 
1416 O  OD2 A ASP A 174 ? 0.3684 0.3239 0.7610 -0.0324 -0.0489 0.1489  175 ASP A OD2 
1417 O  OD2 B ASP A 174 ? 0.3061 0.3156 0.2172 -0.0241 0.0472  -0.0178 175 ASP A OD2 
1418 N  N   . PHE A 175 ? 0.1685 0.1890 0.2077 -0.0160 -0.0357 0.0015  176 PHE A N   
1419 C  CA  . PHE A 175 ? 0.1507 0.1777 0.2206 -0.0104 0.0214  -0.0178 176 PHE A CA  
1420 C  C   . PHE A 175 ? 0.1732 0.2276 0.1694 0.0192  0.0138  -0.0078 176 PHE A C   
1421 O  O   . PHE A 175 ? 0.1777 0.2193 0.2099 -0.0240 0.0234  0.0199  176 PHE A O   
1422 C  CB  . PHE A 175 ? 0.1635 0.1888 0.2078 -0.0372 0.0190  0.0130  176 PHE A CB  
1423 C  CG  . PHE A 175 ? 0.1994 0.2055 0.2011 0.0091  -0.0222 -0.0028 176 PHE A CG  
1424 C  CD1 . PHE A 175 ? 0.2005 0.1844 0.2143 -0.0234 -0.0031 -0.0006 176 PHE A CD1 
1425 C  CD2 . PHE A 175 ? 0.1965 0.1915 0.2053 -0.0299 -0.0233 0.0188  176 PHE A CD2 
1426 C  CE1 . PHE A 175 ? 0.1992 0.1901 0.2389 0.0073  -0.0248 -0.0182 176 PHE A CE1 
1427 C  CE2 . PHE A 175 ? 0.2098 0.1719 0.1890 0.0099  0.0260  -0.0027 176 PHE A CE2 
1428 C  CZ  . PHE A 175 ? 0.1854 0.1951 0.2558 0.0104  -0.0121 0.0083  176 PHE A CZ  
1429 N  N   . THR A 176 ? 0.1646 0.1867 0.1981 0.0114  0.0167  0.0168  177 THR A N   
1430 C  CA  . THR A 176 ? 0.1633 0.1886 0.1800 -0.0577 0.0098  0.0092  177 THR A CA  
1431 C  C   . THR A 176 ? 0.0960 0.1671 0.2055 -0.0063 0.0263  -0.0098 177 THR A C   
1432 O  O   . THR A 176 ? 0.1410 0.1547 0.1933 -0.0187 0.0065  -0.0120 177 THR A O   
1433 C  CB  . THR A 176 ? 0.1209 0.2118 0.2063 -0.0373 0.0472  0.0003  177 THR A CB  
1434 O  OG1 . THR A 176 ? 0.1405 0.2346 0.2587 -0.0553 -0.0167 0.0136  177 THR A OG1 
1435 C  CG2 . THR A 176 ? 0.2648 0.2513 0.2915 -0.0635 0.0472  -0.0753 177 THR A CG2 
1436 N  N   . ASN A 177 ? 0.1439 0.1702 0.1391 -0.0160 0.0126  -0.0217 178 ASN A N   
1437 C  CA  . ASN A 177 ? 0.1380 0.1720 0.1486 -0.0186 0.0357  -0.0266 178 ASN A CA  
1438 C  C   . ASN A 177 ? 0.1958 0.1541 0.1480 -0.0115 0.0093  0.0116  178 ASN A C   
1439 O  O   . ASN A 177 ? 0.1906 0.2395 0.2467 -0.0756 0.0454  -0.0788 178 ASN A O   
1440 C  CB  . ASN A 177 ? 0.1351 0.1604 0.1793 -0.0249 0.0318  -0.0231 178 ASN A CB  
1441 C  CG  . ASN A 177 ? 0.2026 0.1818 0.2107 -0.0249 0.0142  -0.0157 178 ASN A CG  
1442 O  OD1 . ASN A 177 ? 0.2352 0.2039 0.2389 -0.0331 0.0078  0.0170  178 ASN A OD1 
1443 N  ND2 . ASN A 177 ? 0.1721 0.1689 0.2204 -0.0200 0.0221  -0.0154 178 ASN A ND2 
1444 N  N   . PHE A 178 ? 0.1290 0.1515 0.1813 -0.0359 -0.0093 0.0049  179 PHE A N   
1445 C  CA  . PHE A 178 ? 0.1540 0.1551 0.1655 -0.0276 -0.0010 -0.0283 179 PHE A CA  
1446 C  C   . PHE A 178 ? 0.1414 0.1297 0.1835 -0.0157 0.0126  0.0038  179 PHE A C   
1447 O  O   . PHE A 178 ? 0.1301 0.1463 0.2032 -0.0115 -0.0046 -0.0041 179 PHE A O   
1448 C  CB  . PHE A 178 ? 0.1590 0.1657 0.2001 -0.0388 0.0037  -0.0100 179 PHE A CB  
1449 C  CG  . PHE A 178 ? 0.1353 0.1475 0.1903 -0.0219 -0.0197 -0.0232 179 PHE A CG  
1450 C  CD1 . PHE A 178 ? 0.1845 0.1538 0.2436 0.0100  -0.0562 0.0322  179 PHE A CD1 
1451 C  CD2 . PHE A 178 ? 0.1298 0.1796 0.1380 -0.0222 -0.0259 -0.0054 179 PHE A CD2 
1452 C  CE1 . PHE A 178 ? 0.1565 0.1624 0.2066 0.0021  -0.0121 -0.0041 179 PHE A CE1 
1453 C  CE2 . PHE A 178 ? 0.1554 0.1592 0.1608 -0.0207 0.0231  0.0000  179 PHE A CE2 
1454 C  CZ  . PHE A 178 ? 0.1457 0.1572 0.1705 -0.0126 0.0137  -0.0196 179 PHE A CZ  
1455 N  N   . ASP A 179 ? 0.1297 0.1856 0.1590 -0.0175 0.0115  -0.0163 180 ASP A N   
1456 C  CA  . ASP A 179 ? 0.1588 0.1585 0.1771 -0.0307 -0.0015 -0.0091 180 ASP A CA  
1457 C  C   . ASP A 179 ? 0.1513 0.1711 0.1895 -0.0245 0.0251  -0.0074 180 ASP A C   
1458 O  O   . ASP A 179 ? 0.1567 0.1712 0.1842 -0.0073 0.0043  -0.0099 180 ASP A O   
1459 C  CB  . ASP A 179 ? 0.1962 0.1637 0.1895 -0.0383 0.0241  -0.0262 180 ASP A CB  
1460 C  CG  . ASP A 179 ? 0.2169 0.2511 0.2018 -0.0184 0.0452  0.0390  180 ASP A CG  
1461 O  OD1 . ASP A 179 ? 0.1926 0.1953 0.1906 -0.0214 0.0085  -0.0024 180 ASP A OD1 
1462 O  OD2 . ASP A 179 ? 0.2759 0.3928 0.1725 -0.0114 0.0538  -0.0073 180 ASP A OD2 
1463 N  N   . PRO A 180 ? 0.1459 0.1614 0.1531 -0.0035 -0.0020 -0.0107 181 PRO A N   
1464 C  CA  . PRO A 180 ? 0.1482 0.1563 0.1447 -0.0076 0.0297  -0.0218 181 PRO A CA  
1465 C  C   . PRO A 180 ? 0.1089 0.1393 0.1421 0.0031  0.0160  -0.0041 181 PRO A C   
1466 O  O   . PRO A 180 ? 0.1359 0.1364 0.1648 -0.0104 0.0147  -0.0110 181 PRO A O   
1467 C  CB  . PRO A 180 ? 0.1786 0.1601 0.1960 0.0209  0.0126  -0.0209 181 PRO A CB  
1468 C  CG  . PRO A 180 ? 0.1461 0.1705 0.2081 -0.0051 0.0496  -0.0233 181 PRO A CG  
1469 C  CD  . PRO A 180 ? 0.1137 0.1725 0.1908 0.0071  0.0026  -0.0172 181 PRO A CD  
1470 N  N   . ARG A 181 ? 0.1468 0.1553 0.1380 -0.0055 0.0151  0.0088  182 ARG A N   
1471 C  CA  . ARG A 181 ? 0.1782 0.1629 0.1603 0.0093  0.0240  0.0105  182 ARG A CA  
1472 C  C   . ARG A 181 ? 0.1285 0.1592 0.1517 0.0020  0.0386  -0.0024 182 ARG A C   
1473 O  O   . ARG A 181 ? 0.1500 0.1854 0.2001 -0.0093 0.0160  -0.0353 182 ARG A O   
1474 C  CB  . ARG A 181 ? 0.1533 0.1757 0.1779 0.0132  0.0368  0.0286  182 ARG A CB  
1475 C  CG  . ARG A 181 ? 0.1703 0.1723 0.1829 0.0088  -0.0133 0.0118  182 ARG A CG  
1476 C  CD  . ARG A 181 ? 0.2497 0.2361 0.1811 0.0270  -0.0190 0.0390  182 ARG A CD  
1477 N  NE  . ARG A 181 ? 0.2393 0.2339 0.1969 -0.0160 0.0401  -0.0317 182 ARG A NE  
1478 C  CZ  . ARG A 181 ? 0.3145 0.3240 0.2800 -0.0687 -0.0160 0.0156  182 ARG A CZ  
1479 N  NH1 . ARG A 181 ? 0.3452 0.3497 0.2698 -0.0566 -0.0701 0.0001  182 ARG A NH1 
1480 N  NH2 . ARG A 181 ? 0.3310 0.3544 0.3208 -0.1282 0.0408  0.0000  182 ARG A NH2 
1481 N  N   . GLY A 182 ? 0.1340 0.1468 0.1942 -0.0194 0.0208  0.0226  183 GLY A N   
1482 C  CA  . GLY A 182 ? 0.1477 0.1364 0.2348 -0.0013 0.0212  0.0063  183 GLY A CA  
1483 C  C   . GLY A 182 ? 0.1827 0.1570 0.2369 -0.0054 0.0747  -0.0183 183 GLY A C   
1484 O  O   . GLY A 182 ? 0.1572 0.1741 0.2633 0.0027  0.0581  0.0076  183 GLY A O   
1485 N  N   . LEU A 183 ? 0.1380 0.1489 0.1605 -0.0041 0.0303  0.0152  184 LEU A N   
1486 C  CA  . LEU A 183 ? 0.1319 0.1371 0.1507 -0.0052 0.0231  0.0143  184 LEU A CA  
1487 C  C   . LEU A 183 ? 0.1418 0.1188 0.1551 -0.0006 0.0189  -0.0054 184 LEU A C   
1488 O  O   . LEU A 183 ? 0.1436 0.1674 0.1509 -0.0153 0.0262  -0.0017 184 LEU A O   
1489 C  CB  . LEU A 183 ? 0.1387 0.1637 0.1587 -0.0041 0.0035  -0.0043 184 LEU A CB  
1490 C  CG  . LEU A 183 ? 0.1403 0.1811 0.1703 -0.0109 -0.0119 0.0222  184 LEU A CG  
1491 C  CD1 . LEU A 183 ? 0.2081 0.1947 0.1981 -0.0621 -0.0038 -0.0140 184 LEU A CD1 
1492 C  CD2 . LEU A 183 ? 0.1796 0.1633 0.2319 -0.0322 -0.0043 0.0264  184 LEU A CD2 
1493 N  N   . LEU A 184 ? 0.1407 0.1525 0.1490 0.0027  -0.0007 -0.0041 185 LEU A N   
1494 C  CA  . LEU A 184 ? 0.1395 0.1374 0.1511 -0.0113 0.0038  -0.0228 185 LEU A CA  
1495 C  C   . LEU A 184 ? 0.1443 0.1463 0.2413 -0.0377 0.0472  -0.0626 185 LEU A C   
1496 O  O   . LEU A 184 ? 0.1860 0.1897 0.3231 -0.0201 0.0775  -0.1022 185 LEU A O   
1497 C  CB  . LEU A 184 ? 0.1411 0.1694 0.1562 0.0154  0.0271  -0.0225 185 LEU A CB  
1498 C  CG  . LEU A 184 ? 0.1771 0.1615 0.1407 0.0097  0.0452  -0.0010 185 LEU A CG  
1499 C  CD1 . LEU A 184 ? 0.1624 0.2095 0.1738 0.0130  -0.0142 0.0149  185 LEU A CD1 
1500 C  CD2 . LEU A 184 ? 0.1502 0.1851 0.1791 0.0082  0.0474  -0.0026 185 LEU A CD2 
1501 N  N   . PRO A 185 ? 0.1203 0.1484 0.1369 -0.0076 0.0264  -0.0178 186 PRO A N   
1502 C  CA  . PRO A 185 ? 0.1268 0.1563 0.1441 -0.0215 0.0146  -0.0252 186 PRO A CA  
1503 C  C   . PRO A 185 ? 0.1520 0.1590 0.1640 -0.0044 0.0388  -0.0179 186 PRO A C   
1504 O  O   . PRO A 185 ? 0.2117 0.1574 0.1199 -0.0219 0.0706  -0.0105 186 PRO A O   
1505 C  CB  . PRO A 185 ? 0.1640 0.1509 0.1488 -0.0241 0.0212  -0.0081 186 PRO A CB  
1506 C  CG  . PRO A 185 ? 0.1466 0.1520 0.1267 -0.0153 0.0204  0.0168  186 PRO A CG  
1507 C  CD  . PRO A 185 ? 0.1123 0.1705 0.1588 -0.0146 0.0392  -0.0102 186 PRO A CD  
1508 N  N   A GLU A 186 ? 0.1450 0.1745 0.1568 0.0001  0.0397  -0.0406 187 GLU A N   
1509 N  N   B GLU A 186 ? 0.1926 0.1747 0.1647 -0.0148 0.0131  -0.0287 187 GLU A N   
1510 C  CA  A GLU A 186 ? 0.1764 0.1729 0.1626 0.0065  0.0293  -0.0357 187 GLU A CA  
1511 C  CA  B GLU A 186 ? 0.1872 0.1818 0.1450 -0.0171 0.0318  -0.0474 187 GLU A CA  
1512 C  C   A GLU A 186 ? 0.1594 0.1495 0.1036 -0.0172 0.0021  -0.0195 187 GLU A C   
1513 C  C   B GLU A 186 ? 0.1940 0.1479 0.1526 -0.0340 0.0399  -0.0010 187 GLU A C   
1514 O  O   A GLU A 186 ? 0.1529 0.1709 0.1179 -0.0168 -0.0110 0.0017  187 GLU A O   
1515 O  O   B GLU A 186 ? 0.2133 0.2048 0.1389 0.0304  0.0292  0.0136  187 GLU A O   
1516 C  CB  A GLU A 186 ? 0.1540 0.1642 0.1734 -0.0149 0.0296  -0.0329 187 GLU A CB  
1517 C  CB  B GLU A 186 ? 0.2005 0.1429 0.1550 -0.0020 0.0538  -0.0295 187 GLU A CB  
1518 C  CG  A GLU A 186 ? 0.3495 0.1835 0.1680 -0.0073 0.0122  -0.0397 187 GLU A CG  
1519 C  CG  B GLU A 186 ? 0.1999 0.1165 0.2202 -0.0120 0.0502  -0.0253 187 GLU A CG  
1520 C  CD  A GLU A 186 ? 0.3569 0.2271 0.1605 0.0094  0.0326  -0.0812 187 GLU A CD  
1521 C  CD  B GLU A 186 ? 0.2163 0.1766 0.1955 -0.0226 0.0688  -0.0551 187 GLU A CD  
1522 O  OE1 A GLU A 186 ? 0.2404 0.2391 0.2337 0.0113  0.0198  -0.0646 187 GLU A OE1 
1523 O  OE1 B GLU A 186 ? 0.2664 0.1444 0.1895 0.0073  0.0115  -0.0439 187 GLU A OE1 
1524 O  OE2 A GLU A 186 ? 0.3032 0.3161 0.2883 -0.1172 0.0177  -0.0579 187 GLU A OE2 
1525 O  OE2 B GLU A 186 ? 0.2788 0.2150 0.2515 0.0048  0.1284  0.0516  187 GLU A OE2 
1526 N  N   . SER A 187 ? 0.1624 0.1771 0.1177 -0.0087 0.0399  -0.0017 188 SER A N   
1527 C  CA  . SER A 187 ? 0.1829 0.1459 0.1353 -0.0040 0.0178  -0.0114 188 SER A CA  
1528 C  C   . SER A 187 ? 0.1628 0.1662 0.1208 0.0159  0.0311  -0.0144 188 SER A C   
1529 O  O   . SER A 187 ? 0.2138 0.2142 0.1511 0.0111  0.0318  0.0142  188 SER A O   
1530 C  CB  . SER A 187 ? 0.1782 0.2251 0.1565 -0.0176 0.0115  -0.0124 188 SER A CB  
1531 O  OG  . SER A 187 ? 0.1818 0.1820 0.1717 0.0020  0.0077  -0.0340 188 SER A OG  
1532 N  N   . LEU A 188 ? 0.1595 0.1712 0.1324 0.0137  0.0423  -0.0098 189 LEU A N   
1533 C  CA  . LEU A 188 ? 0.1743 0.1665 0.1161 0.0217  -0.0051 -0.0085 189 LEU A CA  
1534 C  C   . LEU A 188 ? 0.1640 0.1597 0.1150 0.0136  0.0174  0.0129  189 LEU A C   
1535 O  O   . LEU A 188 ? 0.1910 0.1795 0.1529 0.0206  0.0428  0.0017  189 LEU A O   
1536 C  CB  . LEU A 188 ? 0.1902 0.1741 0.1459 0.0175  0.0010  -0.0163 189 LEU A CB  
1537 C  CG  . LEU A 188 ? 0.2236 0.2236 0.1473 0.0032  0.0225  -0.0097 189 LEU A CG  
1538 C  CD1 . LEU A 188 ? 0.2203 0.2091 0.1990 -0.0250 0.0427  0.0038  189 LEU A CD1 
1539 C  CD2 . LEU A 188 ? 0.2391 0.2601 0.1159 -0.0295 0.0487  0.0035  189 LEU A CD2 
1540 N  N   . ASP A 189 ? 0.1576 0.1793 0.1080 -0.0137 0.0432  0.0313  190 ASP A N   
1541 C  CA  . ASP A 189 ? 0.1393 0.2086 0.0998 -0.0013 0.0071  -0.0421 190 ASP A CA  
1542 C  C   . ASP A 189 ? 0.1349 0.1215 0.0988 0.0155  0.0111  0.0163  190 ASP A C   
1543 O  O   . ASP A 189 ? 0.1243 0.1448 0.1141 0.0077  0.0163  0.0051  190 ASP A O   
1544 C  CB  . ASP A 189 ? 0.1904 0.2357 0.1493 -0.0157 0.0046  -0.0570 190 ASP A CB  
1545 C  CG  . ASP A 189 ? 0.2188 0.2820 0.1759 0.0417  0.0082  -0.0375 190 ASP A CG  
1546 O  OD1 . ASP A 189 ? 0.3905 0.4219 0.1714 0.0458  -0.0397 -0.0227 190 ASP A OD1 
1547 O  OD2 . ASP A 189 ? 0.3034 0.4309 0.2506 0.0348  0.0432  -0.1314 190 ASP A OD2 
1548 N  N   . TYR A 190 ? 0.1260 0.1425 0.0994 -0.0103 0.0063  0.0051  191 TYR A N   
1549 C  CA  . TYR A 190 ? 0.1089 0.1233 0.1021 0.0125  0.0148  -0.0190 191 TYR A CA  
1550 C  C   . TYR A 190 ? 0.1086 0.1138 0.1111 0.0107  -0.0060 -0.0051 191 TYR A C   
1551 O  O   . TYR A 190 ? 0.1136 0.1420 0.1009 -0.0030 -0.0097 0.0038  191 TYR A O   
1552 C  CB  . TYR A 190 ? 0.1230 0.1298 0.1213 -0.0091 -0.0114 -0.0092 191 TYR A CB  
1553 C  CG  . TYR A 190 ? 0.1116 0.1286 0.1208 -0.0203 -0.0104 -0.0078 191 TYR A CG  
1554 C  CD1 . TYR A 190 ? 0.1308 0.1587 0.1365 0.0000  -0.0041 -0.0132 191 TYR A CD1 
1555 C  CD2 . TYR A 190 ? 0.1222 0.1447 0.1091 -0.0115 -0.0207 0.0137  191 TYR A CD2 
1556 C  CE1 . TYR A 190 ? 0.1414 0.1465 0.1212 0.0003  0.0189  -0.0013 191 TYR A CE1 
1557 C  CE2 . TYR A 190 ? 0.1278 0.1495 0.1231 0.0076  -0.0178 0.0024  191 TYR A CE2 
1558 C  CZ  . TYR A 190 ? 0.1409 0.1366 0.1484 0.0063  -0.0013 0.0114  191 TYR A CZ  
1559 O  OH  . TYR A 190 ? 0.1651 0.1464 0.1624 0.0098  -0.0032 0.0086  191 TYR A OH  
1560 N  N   . TRP A 191 ? 0.1168 0.1114 0.0997 0.0092  0.0063  0.0044  192 TRP A N   
1561 C  CA  . TRP A 191 ? 0.1055 0.1188 0.0797 -0.0142 -0.0071 -0.0093 192 TRP A CA  
1562 C  C   . TRP A 191 ? 0.0992 0.1086 0.0912 0.0063  -0.0089 0.0024  192 TRP A C   
1563 O  O   . TRP A 191 ? 0.1037 0.1340 0.1156 0.0087  -0.0062 -0.0013 192 TRP A O   
1564 C  CB  . TRP A 191 ? 0.1269 0.1182 0.1086 0.0019  -0.0049 0.0006  192 TRP A CB  
1565 C  CG  . TRP A 191 ? 0.1116 0.1256 0.1270 -0.0093 0.0060  0.0173  192 TRP A CG  
1566 C  CD1 . TRP A 191 ? 0.1444 0.1267 0.1396 -0.0097 0.0066  -0.0063 192 TRP A CD1 
1567 C  CD2 . TRP A 191 ? 0.1136 0.1297 0.1222 -0.0230 -0.0054 0.0210  192 TRP A CD2 
1568 N  NE1 . TRP A 191 ? 0.1404 0.1188 0.1382 -0.0222 -0.0071 -0.0035 192 TRP A NE1 
1569 C  CE2 . TRP A 191 ? 0.1430 0.1294 0.1107 -0.0024 0.0142  0.0194  192 TRP A CE2 
1570 C  CE3 . TRP A 191 ? 0.1163 0.1261 0.1287 0.0105  0.0074  0.0152  192 TRP A CE3 
1571 C  CZ2 . TRP A 191 ? 0.1574 0.1317 0.1242 -0.0153 0.0098  -0.0043 192 TRP A CZ2 
1572 C  CZ3 . TRP A 191 ? 0.1421 0.1348 0.1009 0.0250  0.0089  0.0065  192 TRP A CZ3 
1573 C  CH2 . TRP A 191 ? 0.1486 0.1545 0.1360 -0.0057 0.0164  0.0185  192 TRP A CH2 
1574 N  N   . THR A 192 ? 0.0922 0.0994 0.0969 -0.0055 0.0043  -0.0068 193 THR A N   
1575 C  CA  . THR A 192 ? 0.1137 0.1071 0.0978 0.0091  0.0157  -0.0017 193 THR A CA  
1576 C  C   . THR A 192 ? 0.0900 0.1014 0.1037 0.0063  0.0035  -0.0173 193 THR A C   
1577 O  O   . THR A 192 ? 0.0906 0.1179 0.1094 -0.0010 -0.0024 -0.0024 193 THR A O   
1578 C  CB  . THR A 192 ? 0.1001 0.1100 0.1093 -0.0049 -0.0119 0.0080  193 THR A CB  
1579 O  OG1 . THR A 192 ? 0.1150 0.1096 0.1032 0.0034  0.0006  0.0114  193 THR A OG1 
1580 C  CG2 . THR A 192 ? 0.1152 0.1474 0.1280 0.0166  -0.0234 0.0017  193 THR A CG2 
1581 N  N   . TYR A 193 ? 0.1017 0.1211 0.0936 0.0132  0.0012  -0.0074 194 TYR A N   
1582 C  CA  . TYR A 193 ? 0.0897 0.1018 0.1037 -0.0020 0.0021  -0.0003 194 TYR A CA  
1583 C  C   . TYR A 193 ? 0.0886 0.0922 0.0848 0.0131  0.0038  0.0115  194 TYR A C   
1584 O  O   . TYR A 193 ? 0.1046 0.1097 0.0922 -0.0010 -0.0005 0.0010  194 TYR A O   
1585 C  CB  . TYR A 193 ? 0.1027 0.1313 0.1140 0.0060  -0.0015 0.0395  194 TYR A CB  
1586 C  CG  . TYR A 193 ? 0.0913 0.1146 0.1039 -0.0006 0.0131  0.0093  194 TYR A CG  
1587 C  CD1 . TYR A 193 ? 0.0913 0.0922 0.1134 -0.0043 -0.0017 0.0046  194 TYR A CD1 
1588 C  CD2 . TYR A 193 ? 0.1254 0.1159 0.0970 0.0087  0.0242  0.0173  194 TYR A CD2 
1589 C  CE1 . TYR A 193 ? 0.1188 0.0897 0.0777 -0.0137 0.0065  0.0219  194 TYR A CE1 
1590 C  CE2 . TYR A 193 ? 0.1128 0.1249 0.1396 0.0159  0.0164  0.0183  194 TYR A CE2 
1591 C  CZ  . TYR A 193 ? 0.0942 0.0987 0.0895 -0.0001 0.0147  0.0054  194 TYR A CZ  
1592 O  OH  . TYR A 193 ? 0.1172 0.1042 0.1071 0.0171  0.0032  0.0164  194 TYR A OH  
1593 N  N   . PRO A 194 ? 0.1097 0.1155 0.1015 0.0288  -0.0040 0.0057  195 PRO A N   
1594 C  CA  . PRO A 194 ? 0.1181 0.1091 0.0957 0.0267  -0.0015 0.0100  195 PRO A CA  
1595 C  C   . PRO A 194 ? 0.1115 0.1010 0.0900 0.0178  0.0068  0.0066  195 PRO A C   
1596 O  O   . PRO A 194 ? 0.1098 0.1287 0.1184 0.0113  0.0098  0.0184  195 PRO A O   
1597 C  CB  . PRO A 194 ? 0.1389 0.1453 0.1418 0.0399  0.0017  0.0096  195 PRO A CB  
1598 C  CG  . PRO A 194 ? 0.1351 0.1412 0.1509 0.0195  0.0197  0.0008  195 PRO A CG  
1599 C  CD  . PRO A 194 ? 0.1008 0.1626 0.1274 0.0209  -0.0142 -0.0116 195 PRO A CD  
1600 N  N   . GLY A 195 ? 0.1124 0.0949 0.0903 0.0216  -0.0003 -0.0052 196 GLY A N   
1601 C  CA  . GLY A 195 ? 0.1109 0.1142 0.1140 0.0060  -0.0076 0.0151  196 GLY A CA  
1602 C  C   . GLY A 195 ? 0.1150 0.1116 0.1075 0.0251  0.0006  -0.0044 196 GLY A C   
1603 O  O   . GLY A 195 ? 0.1287 0.1037 0.1003 0.0121  0.0125  -0.0040 196 GLY A O   
1604 N  N   . SER A 196 ? 0.1036 0.1059 0.1019 0.0147  -0.0027 0.0020  197 SER A N   
1605 C  CA  . SER A 196 ? 0.1111 0.1188 0.0754 0.0133  -0.0146 0.0113  197 SER A CA  
1606 C  C   . SER A 196 ? 0.1218 0.0985 0.1058 0.0107  0.0015  0.0063  197 SER A C   
1607 O  O   . SER A 196 ? 0.1216 0.1143 0.0824 0.0271  0.0085  0.0071  197 SER A O   
1608 C  CB  . SER A 196 ? 0.1525 0.1064 0.1137 0.0159  0.0159  0.0164  197 SER A CB  
1609 O  OG  . SER A 196 ? 0.1495 0.1114 0.1000 0.0282  0.0142  0.0093  197 SER A OG  
1610 N  N   . LEU A 197 ? 0.1039 0.0965 0.0906 0.0154  0.0003  0.0006  198 LEU A N   
1611 C  CA  . LEU A 197 ? 0.1053 0.1062 0.1204 0.0241  -0.0172 -0.0086 198 LEU A CA  
1612 C  C   . LEU A 197 ? 0.1111 0.1071 0.1010 0.0153  0.0148  -0.0122 198 LEU A C   
1613 O  O   . LEU A 197 ? 0.1272 0.1152 0.0974 0.0157  0.0098  0.0035  198 LEU A O   
1614 C  CB  . LEU A 197 ? 0.1507 0.1482 0.1107 0.0094  -0.0183 -0.0078 198 LEU A CB  
1615 C  CG  . LEU A 197 ? 0.1795 0.1331 0.1435 0.0182  0.0034  -0.0256 198 LEU A CG  
1616 C  CD1 . LEU A 197 ? 0.1947 0.1836 0.1858 -0.0357 -0.0143 -0.0399 198 LEU A CD1 
1617 C  CD2 . LEU A 197 ? 0.1696 0.1396 0.1294 -0.0073 -0.0170 0.0012  198 LEU A CD2 
1618 N  N   . THR A 198 ? 0.1314 0.1010 0.1127 0.0272  0.0285  0.0068  199 THR A N   
1619 C  CA  . THR A 198 ? 0.1233 0.1008 0.0948 0.0125  0.0096  -0.0048 199 THR A CA  
1620 C  C   . THR A 198 ? 0.1237 0.1208 0.1073 -0.0040 -0.0034 0.0000  199 THR A C   
1621 O  O   . THR A 198 ? 0.1511 0.1306 0.1049 0.0107  0.0157  -0.0001 199 THR A O   
1622 C  CB  . THR A 198 ? 0.1258 0.1112 0.0991 0.0082  0.0119  -0.0177 199 THR A CB  
1623 O  OG1 . THR A 198 ? 0.1195 0.1098 0.0994 0.0068  0.0087  -0.0104 199 THR A OG1 
1624 C  CG2 . THR A 198 ? 0.1285 0.1161 0.1225 0.0078  -0.0108 0.0031  199 THR A CG2 
1625 N  N   . THR A 199 ? 0.1788 0.1339 0.1102 0.0024  -0.0008 -0.0175 200 THR A N   
1626 C  CA  . THR A 199 ? 0.1843 0.1428 0.1133 0.0355  -0.0136 -0.0138 200 THR A CA  
1627 C  C   . THR A 199 ? 0.2145 0.1581 0.1326 0.0410  0.0231  -0.0113 200 THR A C   
1628 O  O   . THR A 199 ? 0.1825 0.1427 0.1285 0.0122  0.0052  -0.0120 200 THR A O   
1629 C  CB  . THR A 199 ? 0.1788 0.1937 0.1463 0.0377  -0.0003 -0.0102 200 THR A CB  
1630 O  OG1 . THR A 199 ? 0.2251 0.2005 0.2556 0.0007  0.0309  0.0030  200 THR A OG1 
1631 C  CG2 . THR A 199 ? 0.1772 0.1416 0.1820 0.0322  0.0010  -0.0107 200 THR A CG2 
1632 N  N   . PRO A 200 ? 0.2072 0.1491 0.1310 0.0555  -0.0096 -0.0272 201 PRO A N   
1633 C  CA  . PRO A 200 ? 0.2008 0.1572 0.1445 0.0324  -0.0091 -0.0489 201 PRO A CA  
1634 C  C   . PRO A 200 ? 0.2003 0.1665 0.1411 0.0278  -0.0188 -0.0359 201 PRO A C   
1635 O  O   . PRO A 200 ? 0.1960 0.1917 0.1705 0.0000  0.0052  -0.0132 201 PRO A O   
1636 C  CB  . PRO A 200 ? 0.2021 0.2131 0.1348 0.0051  -0.0115 -0.0190 201 PRO A CB  
1637 C  CG  . PRO A 200 ? 0.2244 0.2199 0.1380 0.0271  0.0031  -0.0353 201 PRO A CG  
1638 C  CD  . PRO A 200 ? 0.2116 0.1581 0.1340 0.0280  0.0015  -0.0118 201 PRO A CD  
1639 N  N   . PRO A 201 ? 0.1924 0.1924 0.1301 0.0241  0.0130  -0.0313 202 PRO A N   
1640 C  CA  . PRO A 201 ? 0.1745 0.1402 0.1932 0.0186  0.0034  -0.0390 202 PRO A CA  
1641 C  C   . PRO A 201 ? 0.1642 0.1619 0.1382 0.0074  0.0163  -0.0190 202 PRO A C   
1642 O  O   . PRO A 201 ? 0.1752 0.1692 0.1441 0.0174  -0.0085 -0.0423 202 PRO A O   
1643 C  CB  . PRO A 201 ? 0.2845 0.1483 0.1793 -0.0337 -0.0242 -0.0357 202 PRO A CB  
1644 C  CG  . PRO A 201 ? 0.2603 0.1820 0.2359 0.0467  0.0225  -0.0355 202 PRO A CG  
1645 C  CD  . PRO A 201 ? 0.1990 0.1790 0.2217 0.0057  -0.0037 -0.0280 202 PRO A CD  
1646 N  N   . LEU A 202 ? 0.1725 0.1457 0.1240 0.0097  0.0066  -0.0147 203 LEU A N   
1647 C  CA  . LEU A 202 ? 0.1477 0.1344 0.1481 0.0285  0.0054  -0.0092 203 LEU A CA  
1648 C  C   . LEU A 202 ? 0.1462 0.1270 0.1014 0.0153  0.0043  -0.0182 203 LEU A C   
1649 O  O   . LEU A 202 ? 0.1590 0.1465 0.1371 0.0234  0.0362  -0.0054 203 LEU A O   
1650 C  CB  . LEU A 202 ? 0.1619 0.1337 0.1191 0.0405  0.0274  -0.0189 203 LEU A CB  
1651 C  CG  . LEU A 202 ? 0.2023 0.1396 0.0936 0.0366  0.0127  -0.0068 203 LEU A CG  
1652 C  CD1 . LEU A 202 ? 0.2170 0.1781 0.1270 0.0271  0.0263  0.0178  203 LEU A CD1 
1653 C  CD2 . LEU A 202 ? 0.1896 0.1224 0.1200 0.0401  0.0020  0.0054  203 LEU A CD2 
1654 N  N   . LEU A 203 ? 0.1847 0.1383 0.1076 0.0157  0.0093  -0.0126 204 LEU A N   
1655 C  CA  . LEU A 203 ? 0.2011 0.1398 0.1258 0.0201  -0.0130 -0.0195 204 LEU A CA  
1656 C  C   . LEU A 203 ? 0.1515 0.1378 0.1265 0.0082  0.0086  -0.0100 204 LEU A C   
1657 O  O   . LEU A 203 ? 0.1536 0.1328 0.1154 0.0303  0.0292  0.0007  204 LEU A O   
1658 C  CB  . LEU A 203 ? 0.2160 0.1872 0.1711 -0.0052 -0.0340 -0.0115 204 LEU A CB  
1659 C  CG  . LEU A 203 ? 0.2549 0.1723 0.1664 -0.0059 0.0000  -0.0489 204 LEU A CG  
1660 C  CD1 . LEU A 203 ? 0.3145 0.2565 0.1870 -0.0344 -0.0164 -0.0634 204 LEU A CD1 
1661 C  CD2 . LEU A 203 ? 0.2937 0.2222 0.2344 0.0183  0.0303  -0.0621 204 LEU A CD2 
1662 N  N   . GLU A 204 ? 0.1628 0.1489 0.1551 0.0329  0.0109  -0.0015 205 GLU A N   
1663 C  CA  . GLU A 204 ? 0.1427 0.1185 0.1576 0.0318  0.0200  0.0078  205 GLU A CA  
1664 C  C   . GLU A 204 ? 0.1605 0.1445 0.1680 0.0189  0.0049  0.0098  205 GLU A C   
1665 O  O   . GLU A 204 ? 0.1835 0.1624 0.1886 0.0412  0.0318  0.0388  205 GLU A O   
1666 C  CB  . GLU A 204 ? 0.1739 0.1486 0.2107 0.0370  0.0505  0.0162  205 GLU A CB  
1667 C  CG  . GLU A 204 ? 0.1659 0.1604 0.1939 0.0403  0.0215  0.0362  205 GLU A CG  
1668 C  CD  . GLU A 204 ? 0.1653 0.1545 0.1753 0.0305  0.0375  -0.0137 205 GLU A CD  
1669 O  OE1 . GLU A 204 ? 0.2185 0.1851 0.2370 0.0764  0.0859  0.0164  205 GLU A OE1 
1670 O  OE2 . GLU A 204 ? 0.1745 0.1660 0.1342 0.0284  0.0408  -0.0083 205 GLU A OE2 
1671 N  N   . CYS A 205 ? 0.1477 0.1014 0.1360 0.0168  0.0206  0.0015  206 CYS A N   
1672 C  CA  . CYS A 205 ? 0.1407 0.1224 0.1158 -0.0138 0.0010  -0.0006 206 CYS A CA  
1673 C  C   . CYS A 205 ? 0.1059 0.1199 0.1202 0.0097  0.0164  0.0154  206 CYS A C   
1674 O  O   . CYS A 205 ? 0.1468 0.1006 0.1351 -0.0008 0.0340  0.0044  206 CYS A O   
1675 C  CB  . CYS A 205 ? 0.1319 0.1297 0.1339 0.0007  -0.0076 -0.0051 206 CYS A CB  
1676 S  SG  . CYS A 205 ? 0.1532 0.1373 0.1701 0.0217  -0.0017 0.0030  206 CYS A SG  
1677 N  N   . VAL A 206 ? 0.1262 0.1142 0.1048 0.0110  0.0087  -0.0041 207 VAL A N   
1678 C  CA  . VAL A 206 ? 0.1269 0.0935 0.0904 0.0159  0.0019  0.0052  207 VAL A CA  
1679 C  C   . VAL A 206 ? 0.1039 0.1005 0.1066 -0.0007 0.0076  0.0048  207 VAL A C   
1680 O  O   . VAL A 206 ? 0.1271 0.1220 0.1195 -0.0060 0.0096  0.0017  207 VAL A O   
1681 C  CB  . VAL A 206 ? 0.1430 0.0883 0.1075 0.0239  0.0110  -0.0031 207 VAL A CB  
1682 C  CG1 . VAL A 206 ? 0.1226 0.1093 0.1107 0.0297  0.0239  0.0164  207 VAL A CG1 
1683 C  CG2 . VAL A 206 ? 0.1412 0.1314 0.1258 0.0074  0.0115  0.0099  207 VAL A CG2 
1684 N  N   . THR A 207 ? 0.1125 0.0922 0.1030 0.0214  0.0052  0.0026  208 THR A N   
1685 C  CA  . THR A 207 ? 0.1224 0.1015 0.1077 0.0152  -0.0041 -0.0031 208 THR A CA  
1686 C  C   . THR A 207 ? 0.0960 0.0992 0.1000 -0.0003 0.0017  -0.0074 208 THR A C   
1687 O  O   . THR A 207 ? 0.1093 0.0881 0.1124 0.0038  0.0119  -0.0030 208 THR A O   
1688 C  CB  . THR A 207 ? 0.1332 0.0926 0.1058 0.0203  0.0111  -0.0074 208 THR A CB  
1689 O  OG1 . THR A 207 ? 0.1228 0.0970 0.1389 0.0240  -0.0066 0.0046  208 THR A OG1 
1690 C  CG2 . THR A 207 ? 0.1333 0.1346 0.1231 -0.0020 -0.0160 -0.0131 208 THR A CG2 
1691 N  N   . TRP A 208 ? 0.1085 0.0830 0.0997 0.0137  0.0020  0.0059  209 TRP A N   
1692 C  CA  . TRP A 208 ? 0.1114 0.0807 0.0882 0.0108  0.0155  0.0140  209 TRP A CA  
1693 C  C   . TRP A 208 ? 0.0897 0.0856 0.0979 0.0057  -0.0041 -0.0055 209 TRP A C   
1694 O  O   . TRP A 208 ? 0.0957 0.0988 0.0983 0.0000  -0.0068 -0.0006 209 TRP A O   
1695 C  CB  . TRP A 208 ? 0.1001 0.1021 0.0827 -0.0103 0.0043  0.0193  209 TRP A CB  
1696 C  CG  . TRP A 208 ? 0.0872 0.0751 0.0820 -0.0057 -0.0005 -0.0060 209 TRP A CG  
1697 C  CD1 . TRP A 208 ? 0.1305 0.0974 0.0859 0.0044  0.0120  -0.0126 209 TRP A CD1 
1698 C  CD2 . TRP A 208 ? 0.0922 0.0938 0.0958 -0.0065 0.0113  0.0098  209 TRP A CD2 
1699 N  NE1 . TRP A 208 ? 0.1086 0.1084 0.1176 0.0041  0.0217  0.0105  209 TRP A NE1 
1700 C  CE2 . TRP A 208 ? 0.1010 0.1073 0.1035 0.0065  -0.0015 0.0078  209 TRP A CE2 
1701 C  CE3 . TRP A 208 ? 0.0834 0.0852 0.1100 0.0076  0.0021  0.0110  209 TRP A CE3 
1702 C  CZ2 . TRP A 208 ? 0.0976 0.1027 0.1080 0.0105  0.0001  0.0239  209 TRP A CZ2 
1703 C  CZ3 . TRP A 208 ? 0.1055 0.1129 0.1105 0.0157  -0.0065 0.0118  209 TRP A CZ3 
1704 C  CH2 . TRP A 208 ? 0.1111 0.0979 0.1133 0.0126  -0.0046 0.0160  209 TRP A CH2 
1705 N  N   . ILE A 209 ? 0.1015 0.0841 0.0935 0.0148  0.0013  0.0006  210 ILE A N   
1706 C  CA  . ILE A 209 ? 0.0948 0.1044 0.0872 0.0027  0.0096  0.0008  210 ILE A CA  
1707 C  C   . ILE A 209 ? 0.0816 0.0985 0.0865 0.0024  -0.0118 -0.0082 210 ILE A C   
1708 O  O   . ILE A 209 ? 0.0915 0.0967 0.1096 -0.0013 -0.0156 0.0027  210 ILE A O   
1709 C  CB  . ILE A 209 ? 0.1295 0.1070 0.0811 0.0098  -0.0023 0.0032  210 ILE A CB  
1710 C  CG1 . ILE A 209 ? 0.1412 0.1061 0.1366 0.0044  0.0203  0.0186  210 ILE A CG1 
1711 C  CG2 . ILE A 209 ? 0.1371 0.1509 0.0903 0.0269  0.0320  -0.0105 210 ILE A CG2 
1712 C  CD1 . ILE A 209 ? 0.2078 0.1230 0.1461 -0.0222 0.0038  0.0401  210 ILE A CD1 
1713 N  N   . VAL A 210 ? 0.0961 0.0847 0.0768 0.0065  0.0017  0.0037  211 VAL A N   
1714 C  CA  . VAL A 210 ? 0.1040 0.0869 0.0773 0.0102  0.0104  0.0085  211 VAL A CA  
1715 C  C   . VAL A 210 ? 0.0857 0.0793 0.0811 -0.0065 0.0028  -0.0038 211 VAL A C   
1716 O  O   . VAL A 210 ? 0.1014 0.1174 0.1015 -0.0024 -0.0041 -0.0044 211 VAL A O   
1717 C  CB  . VAL A 210 ? 0.1062 0.0976 0.0939 0.0087  0.0166  0.0092  211 VAL A CB  
1718 C  CG1 . VAL A 210 ? 0.1067 0.0991 0.1082 0.0253  0.0143  -0.0098 211 VAL A CG1 
1719 C  CG2 . VAL A 210 ? 0.1188 0.1274 0.0945 0.0115  0.0052  -0.0041 211 VAL A CG2 
1720 N  N   . LEU A 211 ? 0.1059 0.0987 0.0843 0.0043  0.0135  -0.0043 212 LEU A N   
1721 C  CA  . LEU A 211 ? 0.1285 0.1145 0.0931 0.0040  0.0133  -0.0109 212 LEU A CA  
1722 C  C   . LEU A 211 ? 0.1428 0.1114 0.1118 0.0038  -0.0129 -0.0024 212 LEU A C   
1723 O  O   . LEU A 211 ? 0.1064 0.1308 0.1103 0.0147  0.0129  -0.0051 212 LEU A O   
1724 C  CB  . LEU A 211 ? 0.1143 0.1161 0.0895 0.0098  -0.0041 -0.0078 212 LEU A CB  
1725 C  CG  . LEU A 211 ? 0.1186 0.1237 0.1152 -0.0057 0.0153  -0.0054 212 LEU A CG  
1726 C  CD1 . LEU A 211 ? 0.1130 0.1559 0.1348 -0.0104 0.0237  -0.0085 212 LEU A CD1 
1727 C  CD2 . LEU A 211 ? 0.1371 0.1471 0.1204 -0.0008 -0.0073 0.0017  212 LEU A CD2 
1728 N  N   . LYS A 212 ? 0.1195 0.1296 0.1019 0.0043  0.0000  -0.0146 213 LYS A N   
1729 C  CA  . LYS A 212 ? 0.1360 0.1305 0.1234 0.0027  0.0080  -0.0110 213 LYS A CA  
1730 C  C   . LYS A 212 ? 0.1238 0.1163 0.1130 -0.0087 0.0049  -0.0133 213 LYS A C   
1731 O  O   . LYS A 212 ? 0.1642 0.1240 0.1472 -0.0081 0.0226  -0.0125 213 LYS A O   
1732 C  CB  . LYS A 212 ? 0.1689 0.1710 0.1766 0.0168  -0.0163 -0.0313 213 LYS A CB  
1733 C  CG  . LYS A 212 ? 0.2357 0.2069 0.2547 -0.0207 0.0656  -0.0252 213 LYS A CG  
1734 C  CD  . LYS A 212 ? 0.3828 0.3088 0.3928 0.0781  -0.0408 -0.1033 213 LYS A CD  
1735 C  CE  . LYS A 212 ? 0.3513 0.4196 0.6065 -0.1362 -0.1159 -0.0003 213 LYS A CE  
1736 N  NZ  . LYS A 212 ? 0.3370 0.3436 0.2574 0.0298  0.0240  -0.0100 213 LYS A NZ  
1737 N  N   . GLU A 213 ? 0.1050 0.1158 0.1150 -0.0148 -0.0027 -0.0073 214 GLU A N   
1738 C  CA  . GLU A 213 ? 0.1395 0.1164 0.1019 0.0032  -0.0037 -0.0019 214 GLU A CA  
1739 C  C   . GLU A 213 ? 0.1181 0.1252 0.1093 0.0038  0.0015  -0.0083 214 GLU A C   
1740 O  O   . GLU A 213 ? 0.1288 0.1292 0.1046 -0.0132 0.0173  -0.0091 214 GLU A O   
1741 C  CB  . GLU A 213 ? 0.1538 0.1475 0.1252 -0.0175 0.0320  -0.0041 214 GLU A CB  
1742 C  CG  . GLU A 213 ? 0.1886 0.2154 0.1773 0.0156  0.0498  -0.0351 214 GLU A CG  
1743 C  CD  . GLU A 213 ? 0.2075 0.2120 0.1879 0.0403  0.0353  -0.0375 214 GLU A CD  
1744 O  OE1 . GLU A 213 ? 0.2336 0.1897 0.1536 0.0076  0.0489  -0.0195 214 GLU A OE1 
1745 O  OE2 . GLU A 213 ? 0.2585 0.5128 0.3774 0.1035  0.1075  0.0003  214 GLU A OE2 
1746 N  N   . PRO A 214 ? 0.1218 0.1088 0.1215 -0.0043 0.0015  -0.0174 215 PRO A N   
1747 C  CA  . PRO A 214 ? 0.1127 0.1249 0.1484 0.0000  -0.0007 0.0107  215 PRO A CA  
1748 C  C   . PRO A 214 ? 0.1341 0.1407 0.1208 0.0063  0.0065  -0.0003 215 PRO A C   
1749 O  O   . PRO A 214 ? 0.1560 0.1659 0.1529 -0.0109 0.0208  -0.0329 215 PRO A O   
1750 C  CB  . PRO A 214 ? 0.1356 0.1137 0.1396 0.0012  0.0219  0.0003  215 PRO A CB  
1751 C  CG  . PRO A 214 ? 0.2951 0.1653 0.1884 -0.0186 -0.0474 0.0057  215 PRO A CG  
1752 C  CD  . PRO A 214 ? 0.1826 0.1062 0.1504 -0.0221 -0.0077 -0.0157 215 PRO A CD  
1753 N  N   . ILE A 215 ? 0.1158 0.1155 0.1197 0.0076  0.0000  0.0063  216 ILE A N   
1754 C  CA  . ILE A 215 ? 0.1222 0.1405 0.1401 0.0043  0.0159  0.0074  216 ILE A CA  
1755 C  C   . ILE A 215 ? 0.1268 0.1359 0.1328 0.0098  0.0174  -0.0059 216 ILE A C   
1756 O  O   . ILE A 215 ? 0.1648 0.1259 0.1430 0.0226  0.0284  0.0048  216 ILE A O   
1757 C  CB  . ILE A 215 ? 0.1544 0.1365 0.1380 -0.0093 0.0040  0.0163  216 ILE A CB  
1758 C  CG1 . ILE A 215 ? 0.1518 0.1244 0.1464 -0.0122 -0.0087 0.0096  216 ILE A CG1 
1759 C  CG2 . ILE A 215 ? 0.1495 0.1515 0.1897 0.0441  0.0085  0.0168  216 ILE A CG2 
1760 C  CD1 . ILE A 215 ? 0.1567 0.1156 0.1852 -0.0082 -0.0065 0.0017  216 ILE A CD1 
1761 N  N   . SER A 216 ? 0.1274 0.1377 0.1656 0.0093  0.0142  -0.0200 217 SER A N   
1762 C  CA  . SER A 216 ? 0.1349 0.1480 0.1635 -0.0037 -0.0046 -0.0015 217 SER A CA  
1763 C  C   . SER A 216 ? 0.1111 0.1143 0.1500 0.0252  0.0168  -0.0076 217 SER A C   
1764 O  O   . SER A 216 ? 0.1655 0.1617 0.1905 -0.0035 0.0353  0.0172  217 SER A O   
1765 C  CB  . SER A 216 ? 0.2587 0.1116 0.2930 -0.0027 -0.0362 -0.0671 217 SER A CB  
1766 O  OG  . SER A 216 ? 0.2431 0.2682 0.2721 0.0302  0.0065  -0.0423 217 SER A OG  
1767 N  N   . VAL A 217 ? 0.1375 0.1213 0.1499 0.0131  0.0060  -0.0116 218 VAL A N   
1768 C  CA  . VAL A 217 ? 0.1585 0.1165 0.1446 -0.0017 0.0031  -0.0046 218 VAL A CA  
1769 C  C   . VAL A 217 ? 0.1281 0.1281 0.1569 0.0076  -0.0172 0.0015  218 VAL A C   
1770 O  O   . VAL A 217 ? 0.1283 0.1253 0.1941 0.0193  0.0120  -0.0288 218 VAL A O   
1771 C  CB  . VAL A 217 ? 0.1623 0.1114 0.1773 0.0173  0.0281  -0.0159 218 VAL A CB  
1772 C  CG1 . VAL A 217 ? 0.1694 0.1220 0.1933 0.0239  -0.0149 -0.0006 218 VAL A CG1 
1773 C  CG2 . VAL A 217 ? 0.2072 0.1355 0.1847 0.0165  0.0467  0.0080  218 VAL A CG2 
1774 N  N   . SER A 218 ? 0.1290 0.1281 0.1603 0.0077  0.0005  -0.0093 219 SER A N   
1775 C  CA  . SER A 218 ? 0.1825 0.1141 0.1811 0.0167  0.0313  -0.0024 219 SER A CA  
1776 C  C   . SER A 218 ? 0.1637 0.1279 0.1558 0.0027  0.0019  -0.0194 219 SER A C   
1777 O  O   . SER A 218 ? 0.1511 0.1200 0.1793 0.0262  -0.0076 -0.0167 219 SER A O   
1778 C  CB  . SER A 218 ? 0.1378 0.1438 0.2278 0.0163  -0.0074 -0.0140 219 SER A CB  
1779 O  OG  . SER A 218 ? 0.1655 0.1744 0.2060 0.0412  -0.0142 -0.0206 219 SER A OG  
1780 N  N   A SER A 219 ? 0.1359 0.1344 0.2032 0.0055  0.0220  0.0274  220 SER A N   
1781 N  N   B SER A 219 ? 0.1359 0.1317 0.1913 0.0082  0.0204  0.0184  220 SER A N   
1782 C  CA  A SER A 219 ? 0.1708 0.1136 0.1782 0.0190  0.0198  -0.0259 220 SER A CA  
1783 C  CA  B SER A 219 ? 0.1608 0.1125 0.1800 0.0351  0.0190  -0.0172 220 SER A CA  
1784 C  C   A SER A 219 ? 0.1926 0.1150 0.2066 -0.0098 0.0220  -0.0100 220 SER A C   
1785 C  C   B SER A 219 ? 0.2016 0.1188 0.2000 -0.0114 0.0264  -0.0027 220 SER A C   
1786 O  O   A SER A 219 ? 0.2066 0.1358 0.1924 -0.0062 -0.0077 -0.0115 220 SER A O   
1787 O  O   B SER A 219 ? 0.2197 0.1328 0.2084 -0.0096 -0.0071 -0.0184 220 SER A O   
1788 C  CB  A SER A 219 ? 0.2370 0.1154 0.2991 0.0241  0.0344  0.0062  220 SER A CB  
1789 C  CB  B SER A 219 ? 0.2098 0.1121 0.2583 0.0601  0.0236  -0.0038 220 SER A CB  
1790 O  OG  A SER A 219 ? 0.2118 0.1064 0.2842 0.0091  -0.0144 -0.0222 220 SER A OG  
1791 O  OG  B SER A 219 ? 0.2069 0.1856 0.2581 -0.0115 0.0200  -0.0032 220 SER A OG  
1792 N  N   . GLU A 220 ? 0.1703 0.1244 0.2163 0.0153  0.0027  0.0187  221 GLU A N   
1793 C  CA  . GLU A 220 ? 0.2138 0.1639 0.2079 0.0012  0.0041  0.0057  221 GLU A CA  
1794 C  C   . GLU A 220 ? 0.1811 0.1666 0.2045 0.0308  -0.0178 0.0066  221 GLU A C   
1795 O  O   . GLU A 220 ? 0.1948 0.1771 0.2045 0.0194  -0.0164 -0.0035 221 GLU A O   
1796 C  CB  . GLU A 220 ? 0.2054 0.1682 0.2802 0.0362  0.0193  0.0043  221 GLU A CB  
1797 C  CG  . GLU A 220 ? 0.2294 0.2213 0.3521 0.0969  0.0171  0.0203  221 GLU A CG  
1798 C  CD  . GLU A 220 ? 0.3021 0.2258 0.3257 0.1019  0.0217  0.0027  221 GLU A CD  
1799 O  OE1 . GLU A 220 ? 0.2737 0.1940 0.3215 0.0925  0.0085  -0.0454 221 GLU A OE1 
1800 O  OE2 . GLU A 220 ? 0.5602 0.3291 0.5903 0.1801  -0.0820 -0.0803 221 GLU A OE2 
1801 N  N   . GLN A 221 ? 0.1483 0.1253 0.1930 0.0120  -0.0104 0.0020  222 GLN A N   
1802 C  CA  . GLN A 221 ? 0.1665 0.1164 0.1917 0.0152  0.0028  -0.0035 222 GLN A CA  
1803 C  C   . GLN A 221 ? 0.1477 0.1658 0.2079 -0.0118 0.0000  -0.0232 222 GLN A C   
1804 O  O   . GLN A 221 ? 0.1631 0.1488 0.1712 -0.0103 -0.0186 -0.0148 222 GLN A O   
1805 C  CB  . GLN A 221 ? 0.1570 0.1321 0.1659 -0.0001 0.0167  -0.0126 222 GLN A CB  
1806 C  CG  . GLN A 221 ? 0.1520 0.1491 0.1723 0.0073  0.0189  0.0164  222 GLN A CG  
1807 C  CD  . GLN A 221 ? 0.1416 0.1001 0.1766 0.0153  0.0006  -0.0115 222 GLN A CD  
1808 O  OE1 . GLN A 221 ? 0.1423 0.1400 0.1809 0.0077  -0.0168 -0.0124 222 GLN A OE1 
1809 N  NE2 . GLN A 221 ? 0.1444 0.1159 0.1859 0.0165  0.0153  -0.0006 222 GLN A NE2 
1810 N  N   . VAL A 222 ? 0.1506 0.1351 0.1967 -0.0241 0.0071  -0.0048 223 VAL A N   
1811 C  CA  . VAL A 222 ? 0.1251 0.1673 0.2039 -0.0236 -0.0001 -0.0020 223 VAL A CA  
1812 C  C   . VAL A 222 ? 0.1808 0.1592 0.1827 -0.0020 0.0245  -0.0076 223 VAL A C   
1813 O  O   . VAL A 222 ? 0.1823 0.1696 0.1863 -0.0146 0.0080  -0.0197 223 VAL A O   
1814 C  CB  . VAL A 222 ? 0.1640 0.1967 0.2506 -0.0478 0.0010  -0.0214 223 VAL A CB  
1815 C  CG1 . VAL A 222 ? 0.2748 0.2109 0.2289 -0.0091 -0.0043 -0.0206 223 VAL A CG1 
1816 C  CG2 . VAL A 222 ? 0.2460 0.2816 0.2721 0.0060  0.0502  -0.0062 223 VAL A CG2 
1817 N  N   . LEU A 223 ? 0.1919 0.1639 0.2109 -0.0012 -0.0207 -0.0238 224 LEU A N   
1818 C  CA  . LEU A 223 ? 0.2624 0.1534 0.2078 0.0040  -0.0059 -0.0066 224 LEU A CA  
1819 C  C   . LEU A 223 ? 0.2079 0.1827 0.1960 0.0307  0.0203  -0.0159 224 LEU A C   
1820 O  O   . LEU A 223 ? 0.2447 0.1972 0.1994 0.0401  -0.0192 0.0040  224 LEU A O   
1821 C  CB  . LEU A 223 ? 0.2763 0.1932 0.2912 0.0295  0.0223  -0.0091 224 LEU A CB  
1822 C  CG  . LEU A 223 ? 0.2556 0.2328 0.3005 -0.0006 -0.0089 -0.0006 224 LEU A CG  
1823 C  CD1 . LEU A 223 ? 0.3526 0.3359 0.4189 0.0737  0.0218  -0.0122 224 LEU A CD1 
1824 C  CD2 . LEU A 223 ? 0.4853 0.2129 0.3072 0.0383  0.0000  0.0353  224 LEU A CD2 
1825 N  N   . LYS A 224 ? 0.1876 0.1577 0.2199 -0.0013 -0.0057 -0.0105 225 LYS A N   
1826 C  CA  . LYS A 224 ? 0.1779 0.1984 0.1684 0.0168  -0.0038 -0.0372 225 LYS A CA  
1827 C  C   . LYS A 224 ? 0.1841 0.1659 0.1707 0.0362  -0.0348 -0.0113 225 LYS A C   
1828 O  O   . LYS A 224 ? 0.1707 0.1753 0.1626 0.0041  -0.0021 -0.0188 225 LYS A O   
1829 C  CB  . LYS A 224 ? 0.1653 0.1942 0.2449 -0.0175 0.0065  -0.0034 225 LYS A CB  
1830 C  CG  . LYS A 224 ? 0.1879 0.2795 0.2644 0.0353  0.0346  -0.0447 225 LYS A CG  
1831 C  CD  . LYS A 224 ? 0.3016 0.2908 0.2748 0.0447  0.0873  -0.0502 225 LYS A CD  
1832 C  CE  . LYS A 224 ? 0.2197 0.3898 0.4652 0.0478  0.0362  -0.0026 225 LYS A CE  
1833 N  NZ  . LYS A 224 ? 0.3986 0.3301 0.3136 0.0701  0.0003  0.0281  225 LYS A NZ  
1834 N  N   . PHE A 225 ? 0.1274 0.1364 0.1682 0.0020  -0.0054 -0.0005 226 PHE A N   
1835 C  CA  . PHE A 225 ? 0.1251 0.1435 0.1490 0.0015  -0.0065 -0.0081 226 PHE A CA  
1836 C  C   . PHE A 225 ? 0.1393 0.1592 0.1702 0.0005  -0.0258 -0.0125 226 PHE A C   
1837 O  O   . PHE A 225 ? 0.1601 0.1523 0.1689 0.0238  -0.0340 0.0055  226 PHE A O   
1838 C  CB  . PHE A 225 ? 0.1497 0.1453 0.1543 0.0097  -0.0274 0.0071  226 PHE A CB  
1839 C  CG  . PHE A 225 ? 0.1570 0.1360 0.1383 -0.0269 -0.0225 -0.0164 226 PHE A CG  
1840 C  CD1 . PHE A 225 ? 0.1978 0.1833 0.2481 -0.0175 -0.0104 0.0458  226 PHE A CD1 
1841 C  CD2 . PHE A 225 ? 0.1935 0.2872 0.1984 0.0564  0.0005  0.0379  226 PHE A CD2 
1842 C  CE1 . PHE A 225 ? 0.1888 0.1852 0.1818 -0.0581 -0.0326 -0.0170 226 PHE A CE1 
1843 C  CE2 . PHE A 225 ? 0.2540 0.2275 0.2337 0.0702  0.0147  0.0483  226 PHE A CE2 
1844 C  CZ  . PHE A 225 ? 0.2133 0.1999 0.2196 0.0441  0.0184  0.0020  226 PHE A CZ  
1845 N  N   . ARG A 226 ? 0.1520 0.1358 0.1649 0.0060  -0.0113 0.0012  227 ARG A N   
1846 C  CA  . ARG A 226 ? 0.1735 0.1660 0.1807 -0.0037 -0.0430 0.0076  227 ARG A CA  
1847 C  C   . ARG A 226 ? 0.1448 0.1393 0.1401 -0.0087 -0.0023 -0.0119 227 ARG A C   
1848 O  O   . ARG A 226 ? 0.1996 0.1878 0.1527 0.0049  -0.0252 0.0037  227 ARG A O   
1849 C  CB  . ARG A 226 ? 0.1666 0.1380 0.2107 -0.0076 -0.0427 0.0161  227 ARG A CB  
1850 C  CG  . ARG A 226 ? 0.1570 0.1554 0.1599 -0.0021 -0.0310 -0.0052 227 ARG A CG  
1851 C  CD  . ARG A 226 ? 0.1820 0.1545 0.1960 -0.0293 -0.0297 0.0021  227 ARG A CD  
1852 N  NE  . ARG A 226 ? 0.1631 0.1306 0.1885 0.0060  -0.0157 -0.0243 227 ARG A NE  
1853 C  CZ  . ARG A 226 ? 0.1558 0.1412 0.1782 0.0266  -0.0197 -0.0218 227 ARG A CZ  
1854 N  NH1 . ARG A 226 ? 0.2233 0.1793 0.2940 0.0861  0.0043  -0.0635 227 ARG A NH1 
1855 N  NH2 . ARG A 226 ? 0.1782 0.1459 0.2107 0.0172  -0.0553 -0.0355 227 ARG A NH2 
1856 N  N   . LYS A 227 ? 0.1367 0.1657 0.1811 0.0060  -0.0236 -0.0059 228 LYS A N   
1857 C  CA  . LYS A 227 ? 0.1680 0.1671 0.1896 0.0040  -0.0463 -0.0060 228 LYS A CA  
1858 C  C   . LYS A 227 ? 0.1868 0.1732 0.2080 0.0452  -0.0476 -0.0249 228 LYS A C   
1859 O  O   . LYS A 227 ? 0.1759 0.1833 0.1931 0.0107  -0.0568 -0.0071 228 LYS A O   
1860 C  CB  . LYS A 227 ? 0.1858 0.2045 0.2136 0.0120  -0.0103 0.0006  228 LYS A CB  
1861 C  CG  . LYS A 227 ? 0.2011 0.2490 0.2915 0.0599  -0.0255 -0.0548 228 LYS A CG  
1862 C  CD  . LYS A 227 ? 0.2495 0.3492 0.3152 0.1234  0.0337  -0.0023 228 LYS A CD  
1863 C  CE  . LYS A 227 ? 0.3235 0.5819 0.4787 0.0689  -0.0533 -0.0803 228 LYS A CE  
1864 N  NZ  . LYS A 227 ? 0.6241 0.9027 1.0889 0.0214  0.1216  0.1050  228 LYS A NZ  
1865 N  N   . LEU A 228 ? 0.1464 0.1565 0.1856 0.0386  -0.0262 -0.0252 229 LEU A N   
1866 C  CA  . LEU A 228 ? 0.1412 0.1466 0.1766 0.0201  -0.0518 -0.0103 229 LEU A CA  
1867 C  C   . LEU A 228 ? 0.1772 0.1498 0.1725 0.0051  -0.0557 0.0346  229 LEU A C   
1868 O  O   . LEU A 228 ? 0.1588 0.1551 0.1587 -0.0017 -0.0355 0.0071  229 LEU A O   
1869 C  CB  . LEU A 228 ? 0.1847 0.1374 0.1339 0.0148  -0.0324 0.0263  229 LEU A CB  
1870 C  CG  . LEU A 228 ? 0.1365 0.1321 0.1479 -0.0048 -0.0223 0.0088  229 LEU A CG  
1871 C  CD1 . LEU A 228 ? 0.1459 0.1610 0.1552 0.0114  -0.0293 0.0193  229 LEU A CD1 
1872 C  CD2 . LEU A 228 ? 0.1709 0.1833 0.1915 -0.0340 -0.0436 -0.0181 229 LEU A CD2 
1873 N  N   . ASN A 229 ? 0.1421 0.1552 0.1617 0.0132  -0.0275 0.0032  230 ASN A N   
1874 C  CA  . ASN A 229 ? 0.1738 0.2008 0.1626 0.0225  -0.0412 -0.0414 230 ASN A CA  
1875 C  C   . ASN A 229 ? 0.1809 0.1596 0.1513 -0.0114 -0.0293 -0.0348 230 ASN A C   
1876 O  O   . ASN A 229 ? 0.1732 0.1829 0.2063 -0.0091 -0.0439 0.0003  230 ASN A O   
1877 C  CB  . ASN A 229 ? 0.2073 0.2027 0.1766 0.0065  -0.0635 0.0051  230 ASN A CB  
1878 C  CG  . ASN A 229 ? 0.1802 0.2163 0.1987 0.0201  -0.0317 0.0043  230 ASN A CG  
1879 O  OD1 . ASN A 229 ? 0.2569 0.2433 0.2389 0.0331  -0.0929 -0.0146 230 ASN A OD1 
1880 N  ND2 . ASN A 229 ? 0.2073 0.2075 0.2100 0.0408  -0.0740 0.0183  230 ASN A ND2 
1881 N  N   . PHE A 230 ? 0.1691 0.1856 0.1565 0.0249  -0.0299 -0.0030 231 PHE A N   
1882 C  CA  . PHE A 230 ? 0.2016 0.1536 0.1441 0.0089  -0.0294 -0.0082 231 PHE A CA  
1883 C  C   . PHE A 230 ? 0.2511 0.2010 0.1473 0.0274  -0.0300 -0.0118 231 PHE A C   
1884 O  O   . PHE A 230 ? 0.2003 0.2075 0.1847 0.0273  -0.0518 -0.0439 231 PHE A O   
1885 C  CB  . PHE A 230 ? 0.2055 0.2050 0.1960 -0.0092 -0.0439 -0.0034 231 PHE A CB  
1886 C  CG  . PHE A 230 ? 0.1326 0.1902 0.1725 0.0085  -0.0163 -0.0026 231 PHE A CG  
1887 C  CD1 . PHE A 230 ? 0.1903 0.1878 0.1535 0.0351  -0.0208 -0.0317 231 PHE A CD1 
1888 C  CD2 . PHE A 230 ? 0.1994 0.2206 0.1903 0.0098  -0.0060 -0.0394 231 PHE A CD2 
1889 C  CE1 . PHE A 230 ? 0.2199 0.1958 0.1712 0.0283  -0.0344 -0.0588 231 PHE A CE1 
1890 C  CE2 . PHE A 230 ? 0.1994 0.2066 0.1714 0.0489  -0.0313 -0.0408 231 PHE A CE2 
1891 C  CZ  . PHE A 230 ? 0.1896 0.1905 0.1421 0.0366  -0.0135 -0.0304 231 PHE A CZ  
1892 N  N   . ASN A 231 ? 0.2154 0.2181 0.1649 -0.0104 -0.0808 -0.0296 232 ASN A N   
1893 C  CA  . ASN A 231 ? 0.2511 0.1698 0.1572 0.0231  -0.0544 -0.0412 232 ASN A CA  
1894 C  C   . ASN A 231 ? 0.1870 0.2490 0.2014 0.0361  -0.0167 -0.0195 232 ASN A C   
1895 O  O   . ASN A 231 ? 0.1884 0.1897 0.1703 0.0041  -0.0194 0.0049  232 ASN A O   
1896 C  CB  . ASN A 231 ? 0.2342 0.2078 0.1744 0.0577  -0.0520 0.0098  232 ASN A CB  
1897 C  CG  . ASN A 231 ? 0.2213 0.2236 0.2317 0.0256  -0.0199 -0.0193 232 ASN A CG  
1898 O  OD1 . ASN A 231 ? 0.2423 0.1929 0.2129 0.0450  -0.0295 -0.0008 232 ASN A OD1 
1899 N  ND2 . ASN A 231 ? 0.2424 0.2292 0.2921 0.0527  -0.0723 0.0027  232 ASN A ND2 
1900 N  N   . GLY A 232 ? 0.2319 0.1969 0.1981 0.0137  -0.0285 -0.0143 233 GLY A N   
1901 C  CA  . GLY A 232 ? 0.2415 0.2400 0.3046 0.0168  -0.0601 -0.0222 233 GLY A CA  
1902 C  C   . GLY A 232 ? 0.3012 0.2219 0.2337 0.0174  -0.0936 -0.0032 233 GLY A C   
1903 O  O   . GLY A 232 ? 0.2795 0.2655 0.2721 -0.0348 -0.1193 -0.0225 233 GLY A O   
1904 N  N   . GLU A 233 ? 0.2355 0.3095 0.3285 0.0865  -0.0737 -0.0303 234 GLU A N   
1905 C  CA  . GLU A 233 ? 0.1967 0.3781 0.3210 0.0421  -0.1168 -0.0485 234 GLU A CA  
1906 C  C   . GLU A 233 ? 0.6432 0.4126 0.4564 -0.0372 -0.0198 -0.0417 234 GLU A C   
1907 O  O   . GLU A 233 ? 0.3978 0.3831 0.4050 0.0474  -0.1859 -0.0310 234 GLU A O   
1908 C  CB  . GLU A 233 ? 0.2454 0.3691 0.3341 0.0057  -0.1437 -0.0599 234 GLU A CB  
1909 C  CG  . GLU A 233 ? 0.3355 0.4483 0.3998 0.0781  -0.1932 -0.0546 234 GLU A CG  
1910 C  CD  . GLU A 233 ? 0.4129 0.5418 0.4972 0.1333  -0.0537 0.0214  234 GLU A CD  
1911 O  OE1 . GLU A 233 ? 0.3955 0.7833 0.5328 0.1538  -0.0381 -0.0639 234 GLU A OE1 
1912 O  OE2 . GLU A 233 ? 0.3808 0.5461 0.4083 0.0439  -0.1875 -0.0342 234 GLU A OE2 
1913 N  N   A GLY A 234 ? 0.5939 0.1875 0.4041 0.1316  -0.3134 0.0921  235 GLY A N   
1914 N  N   B GLY A 234 ? 0.5673 0.2442 0.3161 0.1253  -0.3249 0.0597  235 GLY A N   
1915 C  CA  A GLY A 234 ? 0.4934 0.5034 0.5188 -0.1407 0.0007  0.0771  235 GLY A CA  
1916 C  CA  B GLY A 234 ? 0.3637 0.4237 0.3722 -0.0221 0.0126  0.0288  235 GLY A CA  
1917 C  C   A GLY A 234 ? 0.5633 0.7501 0.5332 -0.0450 -0.0922 0.0311  235 GLY A C   
1918 C  C   B GLY A 234 ? 0.3122 0.3346 0.4171 0.0445  -0.0162 0.1401  235 GLY A C   
1919 O  O   A GLY A 234 ? 0.8963 0.2500 0.3616 0.1541  -0.1325 -0.1870 235 GLY A O   
1920 O  O   B GLY A 234 ? 0.2118 0.3271 0.2590 0.0621  -0.1036 0.0340  235 GLY A O   
1921 N  N   . GLU A 235 ? 0.3215 0.4427 0.4160 0.0096  -0.2369 0.1010  236 GLU A N   
1922 C  CA  . GLU A 235 ? 0.3625 0.3876 0.3709 0.1040  -0.1319 0.0456  236 GLU A CA  
1923 C  C   . GLU A 235 ? 0.2824 0.3194 0.2829 -0.0165 -0.0496 0.0772  236 GLU A C   
1924 O  O   . GLU A 235 ? 0.2711 0.3012 0.2502 -0.0480 -0.0926 0.0121  236 GLU A O   
1925 C  CB  . GLU A 235 ? 0.3878 0.3873 0.4679 0.0744  -0.2003 -0.0060 236 GLU A CB  
1926 C  CG  . GLU A 235 ? 0.7171 0.1820 0.4138 0.0052  -0.4040 -0.0076 236 GLU A CG  
1927 C  CD  . GLU A 235 ? 0.7142 0.4120 0.8985 0.0643  -0.2098 0.1208  236 GLU A CD  
1928 O  OE1 . GLU A 235 ? 0.6421 0.4872 0.6000 -0.0838 0.0568  -0.2967 236 GLU A OE1 
1929 O  OE2 . GLU A 235 ? 0.6837 0.3959 0.4490 0.0303  -0.2456 -0.0384 236 GLU A OE2 
1930 N  N   . PRO A 236 ? 0.2649 0.3037 0.2551 -0.0087 -0.0868 0.0489  237 PRO A N   
1931 C  CA  . PRO A 236 ? 0.3296 0.3235 0.1856 -0.0188 -0.1027 0.0390  237 PRO A CA  
1932 C  C   . PRO A 236 ? 0.2217 0.2563 0.2001 0.0439  -0.0507 0.0234  237 PRO A C   
1933 O  O   . PRO A 236 ? 0.1969 0.2263 0.2242 0.0297  -0.0368 0.0339  237 PRO A O   
1934 C  CB  . PRO A 236 ? 0.2651 0.2621 0.2248 0.0280  -0.0551 0.0445  237 PRO A CB  
1935 C  CG  . PRO A 236 ? 0.5013 0.2576 0.2597 -0.0274 -0.0562 0.0310  237 PRO A CG  
1936 C  CD  . PRO A 236 ? 0.4732 0.2578 0.2892 -0.0286 -0.0272 0.1040  237 PRO A CD  
1937 N  N   . GLU A 237 ? 0.2350 0.2874 0.1770 0.0379  -0.0143 0.0397  238 GLU A N   
1938 C  CA  . GLU A 237 ? 0.2633 0.2373 0.1599 -0.0012 -0.0006 0.0068  238 GLU A CA  
1939 C  C   . GLU A 237 ? 0.2463 0.1750 0.1432 0.0212  -0.0175 0.0406  238 GLU A C   
1940 O  O   . GLU A 237 ? 0.2060 0.2271 0.2389 0.0254  -0.0200 0.0096  238 GLU A O   
1941 C  CB  . GLU A 237 ? 0.2664 0.2163 0.2964 0.0401  0.0054  0.0428  238 GLU A CB  
1942 C  CG  . GLU A 237 ? 0.2804 0.2278 0.3048 0.0346  0.0097  0.0031  238 GLU A CG  
1943 C  CD  . GLU A 237 ? 0.2149 0.3425 0.3296 0.0573  0.0204  0.0419  238 GLU A CD  
1944 O  OE1 . GLU A 237 ? 0.3626 0.3794 0.6075 0.1457  0.1363  0.1688  238 GLU A OE1 
1945 O  OE2 . GLU A 237 ? 0.2324 0.2540 0.3046 0.0621  -0.0348 0.0183  238 GLU A OE2 
1946 N  N   . GLU A 238 ? 0.1953 0.2117 0.1741 0.0631  -0.0449 -0.0159 239 GLU A N   
1947 C  CA  . GLU A 238 ? 0.2294 0.2486 0.1732 0.0272  -0.0318 -0.0157 239 GLU A CA  
1948 C  C   . GLU A 238 ? 0.1913 0.1730 0.1671 0.0234  -0.0186 0.0120  239 GLU A C   
1949 O  O   . GLU A 238 ? 0.2037 0.1962 0.1827 -0.0055 -0.0428 -0.0030 239 GLU A O   
1950 C  CB  . GLU A 238 ? 0.2391 0.2784 0.1597 0.0469  -0.0241 0.0124  239 GLU A CB  
1951 C  CG  . GLU A 238 ? 0.2994 0.3695 0.2012 0.0551  0.0233  0.0225  239 GLU A CG  
1952 C  CD  . GLU A 238 ? 0.3084 0.2201 0.2114 0.0432  -0.0035 0.0074  239 GLU A CD  
1953 O  OE1 . GLU A 238 ? 0.2581 0.3447 0.3050 0.0055  0.0307  0.0621  239 GLU A OE1 
1954 O  OE2 . GLU A 238 ? 0.3544 0.3088 0.2578 0.0763  -0.0584 -0.0881 239 GLU A OE2 
1955 N  N   . LEU A 239 ? 0.1798 0.2138 0.1653 0.0131  -0.0190 -0.0062 240 LEU A N   
1956 C  CA  . LEU A 239 ? 0.2027 0.2105 0.1536 0.0111  -0.0170 0.0355  240 LEU A CA  
1957 C  C   . LEU A 239 ? 0.1411 0.1766 0.1558 -0.0052 0.0166  -0.0035 240 LEU A C   
1958 O  O   . LEU A 239 ? 0.1518 0.2046 0.1587 0.0065  0.0028  0.0131  240 LEU A O   
1959 C  CB  . LEU A 239 ? 0.2168 0.2201 0.1937 -0.0105 -0.0147 0.0078  240 LEU A CB  
1960 C  CG  . LEU A 239 ? 0.2533 0.2036 0.2113 0.0138  -0.0094 0.0208  240 LEU A CG  
1961 C  CD1 . LEU A 239 ? 0.4632 0.2655 0.3643 -0.0184 0.0927  -0.0560 240 LEU A CD1 
1962 C  CD2 . LEU A 239 ? 0.2294 0.1859 0.2459 0.0182  -0.0715 0.0395  240 LEU A CD2 
1963 N  N   . MET A 240 ? 0.1457 0.1599 0.1374 -0.0082 -0.0201 0.0074  241 MET A N   
1964 C  CA  . MET A 240 ? 0.1662 0.1601 0.1813 -0.0119 -0.0478 -0.0076 241 MET A CA  
1965 C  C   . MET A 240 ? 0.1301 0.1457 0.1606 0.0118  -0.0082 -0.0153 241 MET A C   
1966 O  O   . MET A 240 ? 0.1373 0.1520 0.1348 0.0104  -0.0164 0.0040  241 MET A O   
1967 C  CB  . MET A 240 ? 0.2167 0.1676 0.1728 0.0231  -0.0381 0.0364  241 MET A CB  
1968 C  CG  . MET A 240 ? 0.1901 0.1513 0.1691 0.0357  -0.0377 -0.0107 241 MET A CG  
1969 S  SD  . MET A 240 ? 0.1978 0.1799 0.1806 0.0124  -0.0337 -0.0245 241 MET A SD  
1970 C  CE  . MET A 240 ? 0.1985 0.1608 0.1754 -0.0102 -0.0188 -0.0392 241 MET A CE  
1971 N  N   . VAL A 241 ? 0.1317 0.1238 0.1401 0.0003  -0.0285 0.0187  242 VAL A N   
1972 C  CA  . VAL A 241 ? 0.1231 0.1445 0.1520 0.0284  -0.0406 -0.0093 242 VAL A CA  
1973 C  C   . VAL A 241 ? 0.1333 0.1278 0.1224 0.0078  -0.0065 0.0161  242 VAL A C   
1974 O  O   . VAL A 241 ? 0.1581 0.1515 0.1312 0.0258  -0.0040 0.0137  242 VAL A O   
1975 C  CB  . VAL A 241 ? 0.1341 0.1414 0.1412 0.0294  -0.0152 -0.0094 242 VAL A CB  
1976 C  CG1 . VAL A 241 ? 0.1474 0.1592 0.1877 0.0175  0.0089  0.0041  242 VAL A CG1 
1977 C  CG2 . VAL A 241 ? 0.1845 0.1525 0.1466 0.0193  -0.0315 -0.0001 242 VAL A CG2 
1978 N  N   . ASP A 242 ? 0.1299 0.1215 0.1315 0.0102  -0.0266 0.0087  243 ASP A N   
1979 C  CA  . ASP A 242 ? 0.1489 0.1386 0.0949 0.0197  -0.0155 0.0120  243 ASP A CA  
1980 C  C   . ASP A 242 ? 0.1064 0.1319 0.1231 0.0054  -0.0065 -0.0043 243 ASP A C   
1981 O  O   . ASP A 242 ? 0.1536 0.1454 0.1456 0.0240  0.0161  0.0001  243 ASP A O   
1982 C  CB  . ASP A 242 ? 0.1497 0.1396 0.1216 -0.0076 0.0013  -0.0060 243 ASP A CB  
1983 C  CG  . ASP A 242 ? 0.1414 0.1347 0.1313 0.0137  -0.0392 0.0094  243 ASP A CG  
1984 O  OD1 . ASP A 242 ? 0.1477 0.1222 0.1202 0.0337  -0.0021 0.0049  243 ASP A OD1 
1985 O  OD2 . ASP A 242 ? 0.2152 0.1470 0.1702 0.0377  -0.0299 0.0244  243 ASP A OD2 
1986 N  N   . ASN A 243 ? 0.1350 0.1066 0.1057 0.0204  -0.0240 0.0094  244 ASN A N   
1987 C  CA  . ASN A 243 ? 0.1209 0.1134 0.1251 0.0194  -0.0181 0.0052  244 ASN A CA  
1988 C  C   . ASN A 243 ? 0.1012 0.0985 0.1075 0.0080  -0.0093 0.0078  244 ASN A C   
1989 O  O   . ASN A 243 ? 0.1348 0.1130 0.1326 -0.0063 -0.0207 0.0149  244 ASN A O   
1990 C  CB  . ASN A 243 ? 0.1335 0.1518 0.1039 0.0057  -0.0263 -0.0207 244 ASN A CB  
1991 C  CG  . ASN A 243 ? 0.1089 0.1351 0.1125 0.0183  -0.0286 -0.0057 244 ASN A CG  
1992 O  OD1 . ASN A 243 ? 0.1459 0.1308 0.1168 0.0017  -0.0082 -0.0103 244 ASN A OD1 
1993 N  ND2 . ASN A 243 ? 0.1563 0.1743 0.1705 -0.0381 -0.0030 -0.0286 244 ASN A ND2 
1994 N  N   . TRP A 244 ? 0.1168 0.1067 0.1127 0.0099  0.0015  0.0027  245 TRP A N   
1995 C  CA  . TRP A 244 ? 0.1211 0.1182 0.0953 0.0031  -0.0028 0.0135  245 TRP A CA  
1996 C  C   . TRP A 244 ? 0.1102 0.1006 0.1017 0.0000  -0.0055 -0.0054 245 TRP A C   
1997 O  O   . TRP A 244 ? 0.1313 0.1373 0.1249 0.0211  0.0001  0.0163  245 TRP A O   
1998 C  CB  . TRP A 244 ? 0.1181 0.1089 0.0976 0.0032  -0.0129 0.0085  245 TRP A CB  
1999 C  CG  . TRP A 244 ? 0.1215 0.1125 0.0845 0.0028  0.0040  -0.0113 245 TRP A CG  
2000 C  CD1 . TRP A 244 ? 0.1268 0.1098 0.1124 0.0001  -0.0086 0.0076  245 TRP A CD1 
2001 C  CD2 . TRP A 244 ? 0.1033 0.1058 0.1120 0.0083  -0.0031 0.0060  245 TRP A CD2 
2002 N  NE1 . TRP A 244 ? 0.1218 0.1103 0.1141 0.0006  -0.0177 0.0124  245 TRP A NE1 
2003 C  CE2 . TRP A 244 ? 0.1230 0.1075 0.0973 -0.0020 0.0006  0.0052  245 TRP A CE2 
2004 C  CE3 . TRP A 244 ? 0.1084 0.1387 0.1230 0.0093  -0.0161 0.0147  245 TRP A CE3 
2005 C  CZ2 . TRP A 244 ? 0.1371 0.1246 0.1256 -0.0041 0.0149  0.0019  245 TRP A CZ2 
2006 C  CZ3 . TRP A 244 ? 0.1720 0.1484 0.1378 -0.0049 -0.0237 0.0144  245 TRP A CZ3 
2007 C  CH2 . TRP A 244 ? 0.1500 0.1351 0.1331 -0.0076 -0.0161 0.0086  245 TRP A CH2 
2008 N  N   . ARG A 245 ? 0.1149 0.1136 0.1027 0.0137  0.0001  0.0059  246 ARG A N   
2009 C  CA  . ARG A 245 ? 0.1154 0.1089 0.1114 0.0188  0.0044  -0.0065 246 ARG A CA  
2010 C  C   . ARG A 245 ? 0.0954 0.1146 0.1003 0.0170  -0.0010 0.0057  246 ARG A C   
2011 O  O   . ARG A 245 ? 0.1383 0.1225 0.1080 0.0219  0.0104  0.0007  246 ARG A O   
2012 C  CB  . ARG A 245 ? 0.1170 0.1199 0.1010 0.0239  -0.0121 0.0098  246 ARG A CB  
2013 C  CG  . ARG A 245 ? 0.1279 0.1136 0.0784 0.0359  -0.0003 0.0030  246 ARG A CG  
2014 C  CD  . ARG A 245 ? 0.1511 0.1150 0.0987 0.0366  0.0216  0.0083  246 ARG A CD  
2015 N  NE  . ARG A 245 ? 0.1459 0.1340 0.0953 0.0366  0.0107  -0.0015 246 ARG A NE  
2016 C  CZ  . ARG A 245 ? 0.1395 0.1468 0.1009 0.0469  0.0127  0.0164  246 ARG A CZ  
2017 N  NH1 . ARG A 245 ? 0.1662 0.1202 0.1109 0.0252  0.0136  0.0027  246 ARG A NH1 
2018 N  NH2 . ARG A 245 ? 0.1719 0.1676 0.1195 0.0225  0.0416  -0.0217 246 ARG A NH2 
2019 N  N   . PRO A 246 ? 0.1508 0.1251 0.1197 0.0114  -0.0021 0.0041  247 PRO A N   
2020 C  CA  . PRO A 246 ? 0.1281 0.1188 0.1299 0.0215  0.0006  0.0107  247 PRO A CA  
2021 C  C   . PRO A 246 ? 0.1326 0.1077 0.0895 0.0068  -0.0055 0.0043  247 PRO A C   
2022 O  O   . PRO A 246 ? 0.1392 0.1190 0.1084 0.0190  0.0164  -0.0010 247 PRO A O   
2023 C  CB  . PRO A 246 ? 0.1490 0.1756 0.1766 -0.0237 -0.0109 0.0557  247 PRO A CB  
2024 C  CG  . PRO A 246 ? 0.3009 0.2671 0.1536 -0.0741 -0.0162 0.0375  247 PRO A CG  
2025 C  CD  . PRO A 246 ? 0.1858 0.1824 0.1209 -0.0230 -0.0013 0.0297  247 PRO A CD  
2026 N  N   . ALA A 247 ? 0.1246 0.1335 0.1075 0.0035  -0.0063 -0.0028 248 ALA A N   
2027 C  CA  . ALA A 247 ? 0.1208 0.1213 0.1288 0.0185  0.0017  0.0109  248 ALA A CA  
2028 C  C   . ALA A 247 ? 0.1565 0.1193 0.1254 0.0026  0.0229  0.0221  248 ALA A C   
2029 O  O   . ALA A 247 ? 0.1549 0.1588 0.1444 0.0115  0.0073  0.0361  248 ALA A O   
2030 C  CB  . ALA A 247 ? 0.1721 0.1572 0.1712 -0.0010 -0.0663 0.0251  248 ALA A CB  
2031 N  N   . GLN A 248 ? 0.1168 0.1272 0.1271 0.0153  0.0015  0.0046  249 GLN A N   
2032 C  CA  . GLN A 248 ? 0.1085 0.1489 0.1234 0.0097  0.0222  0.0149  249 GLN A CA  
2033 C  C   . GLN A 248 ? 0.1297 0.1319 0.1511 0.0253  0.0144  0.0043  249 GLN A C   
2034 O  O   . GLN A 248 ? 0.1466 0.1669 0.1556 -0.0013 0.0077  0.0181  249 GLN A O   
2035 C  CB  . GLN A 248 ? 0.1398 0.1558 0.1199 0.0118  0.0149  -0.0094 249 GLN A CB  
2036 C  CG  . GLN A 248 ? 0.1736 0.1412 0.1448 0.0013  -0.0243 -0.0057 249 GLN A CG  
2037 C  CD  . GLN A 248 ? 0.1337 0.1588 0.1416 0.0119  0.0098  -0.0063 249 GLN A CD  
2038 O  OE1 . GLN A 248 ? 0.1876 0.2260 0.1826 0.0370  0.0403  0.0131  249 GLN A OE1 
2039 N  NE2 . GLN A 248 ? 0.1780 0.1675 0.1626 0.0167  0.0392  0.0256  249 GLN A NE2 
2040 N  N   . PRO A 249 ? 0.1373 0.2213 0.1574 0.0333  0.0335  0.0355  250 PRO A N   
2041 C  CA  . PRO A 249 ? 0.1624 0.2407 0.1335 -0.0275 0.0165  0.0590  250 PRO A CA  
2042 C  C   . PRO A 249 ? 0.1271 0.1502 0.1586 0.0107  0.0315  0.0208  250 PRO A C   
2043 O  O   . PRO A 249 ? 0.1560 0.1710 0.1604 0.0046  0.0331  0.0287  250 PRO A O   
2044 C  CB  . PRO A 249 ? 0.1975 0.2967 0.2161 0.0344  0.0855  0.1064  250 PRO A CB  
2045 C  CG  . PRO A 249 ? 0.1639 0.3564 0.2433 0.0113  0.0232  0.0230  250 PRO A CG  
2046 C  CD  . PRO A 249 ? 0.1581 0.2328 0.1385 0.0174  0.0252  0.0206  250 PRO A CD  
2047 N  N   . LEU A 250 ? 0.1319 0.1671 0.1698 -0.0008 0.0216  0.0346  251 LEU A N   
2048 C  CA  . LEU A 250 ? 0.1610 0.1711 0.1490 0.0298  -0.0221 0.0228  251 LEU A CA  
2049 C  C   . LEU A 250 ? 0.1317 0.1800 0.1750 0.0093  0.0017  0.0295  251 LEU A C   
2050 O  O   . LEU A 250 ? 0.1572 0.1763 0.1757 0.0096  0.0381  0.0326  251 LEU A O   
2051 C  CB  . LEU A 250 ? 0.1482 0.1800 0.1978 0.0003  -0.0174 -0.0015 251 LEU A CB  
2052 C  CG  . LEU A 250 ? 0.1924 0.1847 0.1985 -0.0052 -0.0230 -0.0010 251 LEU A CG  
2053 C  CD1 . LEU A 250 ? 0.1515 0.1730 0.1687 0.0052  -0.0159 0.0055  251 LEU A CD1 
2054 C  CD2 . LEU A 250 ? 0.2222 0.2093 0.2291 0.0368  -0.0712 -0.0320 251 LEU A CD2 
2055 N  N   . LYS A 251 ? 0.1491 0.2143 0.2062 0.0015  0.0306  0.0308  252 LYS A N   
2056 C  CA  . LYS A 251 ? 0.1389 0.2436 0.2071 0.0220  0.0218  0.0804  252 LYS A CA  
2057 C  C   . LYS A 251 ? 0.1791 0.2230 0.2158 0.0617  0.0286  0.0383  252 LYS A C   
2058 O  O   . LYS A 251 ? 0.3111 0.3801 0.2375 0.0788  -0.0500 0.0020  252 LYS A O   
2059 C  CB  . LYS A 251 ? 0.2375 0.2364 0.2576 0.0628  0.0397  0.0309  252 LYS A CB  
2060 C  CG  . LYS A 251 ? 0.2662 0.3066 0.2786 0.0782  0.0024  0.0379  252 LYS A CG  
2061 C  CD  . LYS A 251 ? 0.3481 0.4200 0.3334 0.0103  0.0423  0.0041  252 LYS A CD  
2062 C  CE  . LYS A 251 ? 0.3932 0.3249 0.3616 0.0822  -0.0074 0.0125  252 LYS A CE  
2063 N  NZ  . LYS A 251 ? 0.4722 0.4302 0.3594 -0.0899 0.1242  0.0303  252 LYS A NZ  
2064 N  N   A ASN A 252 ? 0.1292 0.2492 0.2440 0.0597  0.0590  0.0478  253 ASN A N   
2065 N  N   B ASN A 252 ? 0.1976 0.2694 0.2404 0.1075  0.0670  0.0859  253 ASN A N   
2066 C  CA  A ASN A 252 ? 0.2694 0.2903 0.2560 0.1333  0.0432  0.0350  253 ASN A CA  
2067 C  CA  B ASN A 252 ? 0.2134 0.3233 0.2915 0.0447  0.0196  0.0293  253 ASN A CA  
2068 C  C   A ASN A 252 ? 0.2405 0.3802 0.2608 0.1172  0.0520  0.1133  253 ASN A C   
2069 C  C   B ASN A 252 ? 0.1545 0.2851 0.2398 -0.0445 -0.0381 0.0313  253 ASN A C   
2070 O  O   A ASN A 252 ? 0.1975 0.2675 0.2818 0.0032  -0.0233 0.0142  253 ASN A O   
2071 O  O   B ASN A 252 ? 0.1849 0.2712 0.2141 -0.0529 -0.0031 -0.0272 253 ASN A O   
2072 C  CB  A ASN A 252 ? 0.2402 0.3016 0.3291 0.1268  -0.0088 -0.0399 253 ASN A CB  
2073 C  CB  B ASN A 252 ? 0.1662 0.3224 0.3391 0.0176  0.0472  -0.0165 253 ASN A CB  
2074 C  CG  A ASN A 252 ? 0.2479 0.3050 0.3140 0.0443  -0.0187 0.0068  253 ASN A CG  
2075 C  CG  B ASN A 252 ? 0.2675 0.3562 0.2649 0.0104  0.0267  0.0140  253 ASN A CG  
2076 O  OD1 A ASN A 252 ? 0.3228 0.4311 0.3458 -0.0384 -0.1080 0.0518  253 ASN A OD1 
2077 O  OD1 B ASN A 252 ? 0.2276 0.3749 0.3628 -0.0260 0.1165  0.0160  253 ASN A OD1 
2078 N  ND2 A ASN A 252 ? 0.1958 0.3097 0.2563 0.0122  0.0035  -0.0091 253 ASN A ND2 
2079 N  ND2 B ASN A 252 ? 0.5094 0.5645 0.2822 0.0119  0.0034  -0.0785 253 ASN A ND2 
2080 N  N   . ARG A 253 ? 0.1360 0.2088 0.1692 -0.0108 -0.0017 0.0109  254 ARG A N   
2081 C  CA  . ARG A 253 ? 0.1303 0.1687 0.1508 0.0199  -0.0057 0.0274  254 ARG A CA  
2082 C  C   . ARG A 253 ? 0.1349 0.1569 0.1601 0.0340  -0.0253 0.0249  254 ARG A C   
2083 O  O   . ARG A 253 ? 0.3023 0.1905 0.1752 -0.0252 -0.0425 0.0206  254 ARG A O   
2084 C  CB  . ARG A 253 ? 0.1267 0.1249 0.1472 0.0244  -0.0116 0.0152  254 ARG A CB  
2085 C  CG  . ARG A 253 ? 0.1009 0.1529 0.1369 0.0219  -0.0070 -0.0057 254 ARG A CG  
2086 C  CD  . ARG A 253 ? 0.1193 0.1321 0.1432 0.0085  -0.0057 0.0220  254 ARG A CD  
2087 N  NE  . ARG A 253 ? 0.1322 0.1362 0.1290 0.0185  0.0159  0.0275  254 ARG A NE  
2088 C  CZ  . ARG A 253 ? 0.1263 0.1204 0.1242 0.0010  0.0003  0.0120  254 ARG A CZ  
2089 N  NH1 . ARG A 253 ? 0.1213 0.1368 0.1188 0.0006  0.0197  -0.0133 254 ARG A NH1 
2090 N  NH2 . ARG A 253 ? 0.1231 0.1155 0.1142 0.0295  0.0138  0.0017  254 ARG A NH2 
2091 N  N   A GLN A 254 ? 0.1197 0.1944 0.1377 0.0414  0.0030  0.0200  255 GLN A N   
2092 N  N   B GLN A 254 ? 0.1315 0.1899 0.1383 0.0412  0.0105  0.0159  255 GLN A N   
2093 C  CA  A GLN A 254 ? 0.1371 0.2407 0.1669 0.0307  0.0006  0.0038  255 GLN A CA  
2094 C  CA  B GLN A 254 ? 0.1277 0.2036 0.1836 0.0417  0.0116  0.0003  255 GLN A CA  
2095 C  C   A GLN A 254 ? 0.1344 0.1823 0.1261 0.0157  -0.0059 0.0043  255 GLN A C   
2096 C  C   B GLN A 254 ? 0.1233 0.1669 0.1854 -0.0068 -0.0060 -0.0104 255 GLN A C   
2097 O  O   A GLN A 254 ? 0.1666 0.1721 0.1708 0.0342  0.0339  0.0010  255 GLN A O   
2098 O  O   B GLN A 254 ? 0.1461 0.1432 0.1416 -0.0074 -0.0197 0.0173  255 GLN A O   
2099 C  CB  A GLN A 254 ? 0.1312 0.2265 0.2479 0.0996  -0.0078 0.0295  255 GLN A CB  
2100 C  CB  B GLN A 254 ? 0.1554 0.2542 0.1795 0.0478  0.0065  0.0204  255 GLN A CB  
2101 C  CG  A GLN A 254 ? 0.2160 0.3619 0.2405 0.0186  0.0326  -0.0125 255 GLN A CG  
2102 C  CG  B GLN A 254 ? 0.1620 0.2305 0.2536 0.0104  0.0401  0.0595  255 GLN A CG  
2103 C  CD  A GLN A 254 ? 0.2443 0.2718 0.3916 0.0078  -0.0388 -0.0098 255 GLN A CD  
2104 C  CD  B GLN A 254 ? 0.2712 0.4301 0.2910 0.0184  -0.0108 0.1050  255 GLN A CD  
2105 O  OE1 A GLN A 254 ? 0.2524 0.4338 0.4678 -0.1489 0.0359  0.0304  255 GLN A OE1 
2106 O  OE1 B GLN A 254 ? 0.2339 0.3016 0.2603 0.0003  0.0160  -0.0163 255 GLN A OE1 
2107 N  NE2 A GLN A 254 ? 0.2696 0.2728 0.2477 0.0397  -0.0355 -0.0159 255 GLN A NE2 
2108 N  NE2 B GLN A 254 ? 0.2594 0.2440 0.3161 0.0612  -0.0388 0.0432  255 GLN A NE2 
2109 N  N   . ILE A 255 ? 0.1481 0.1605 0.1410 -0.0034 -0.0006 0.0010  256 ILE A N   
2110 C  CA  . ILE A 255 ? 0.1305 0.1495 0.1355 0.0000  -0.0010 0.0226  256 ILE A CA  
2111 C  C   . ILE A 255 ? 0.1321 0.1380 0.1230 -0.0122 -0.0120 0.0078  256 ILE A C   
2112 O  O   . ILE A 255 ? 0.1279 0.1638 0.1565 -0.0142 -0.0165 0.0098  256 ILE A O   
2113 C  CB  . ILE A 255 ? 0.1203 0.1423 0.1382 -0.0031 0.0076  0.0027  256 ILE A CB  
2114 C  CG1 . ILE A 255 ? 0.1323 0.1357 0.1357 -0.0027 0.0038  0.0260  256 ILE A CG1 
2115 C  CG2 . ILE A 255 ? 0.1351 0.1849 0.1583 0.0109  0.0162  0.0020  256 ILE A CG2 
2116 C  CD1 . ILE A 255 ? 0.2269 0.1532 0.1811 0.0326  -0.0171 0.0222  256 ILE A CD1 
2117 N  N   . LYS A 256 ? 0.0979 0.1357 0.1238 -0.0019 0.0043  -0.0035 257 LYS A N   
2118 C  CA  . LYS A 256 ? 0.1263 0.1741 0.1335 -0.0175 0.0109  0.0068  257 LYS A CA  
2119 C  C   . LYS A 256 ? 0.1256 0.1322 0.1224 -0.0060 -0.0063 0.0130  257 LYS A C   
2120 O  O   . LYS A 256 ? 0.1177 0.1827 0.1601 0.0068  -0.0152 -0.0414 257 LYS A O   
2121 C  CB  . LYS A 256 ? 0.1580 0.1637 0.1568 0.0100  -0.0200 0.0006  257 LYS A CB  
2122 C  CG  . LYS A 256 ? 0.2327 0.2156 0.2255 0.0742  -0.0379 0.0184  257 LYS A CG  
2123 C  CD  . LYS A 256 ? 0.3361 0.2822 0.2897 0.0988  -0.0148 0.0280  257 LYS A CD  
2124 C  CE  . LYS A 256 ? 0.3950 0.4517 0.4887 0.0936  0.0483  -0.1112 257 LYS A CE  
2125 N  NZ  . LYS A 256 ? 0.4411 0.4410 0.5321 0.0667  0.0445  -0.1017 257 LYS A NZ  
2126 N  N   . ALA A 257 ? 0.1080 0.1644 0.1342 -0.0054 -0.0216 -0.0133 258 ALA A N   
2127 C  CA  . ALA A 257 ? 0.1308 0.1410 0.1389 -0.0065 -0.0028 -0.0104 258 ALA A CA  
2128 C  C   . ALA A 257 ? 0.1414 0.1430 0.1474 -0.0077 -0.0342 -0.0065 258 ALA A C   
2129 O  O   . ALA A 257 ? 0.1348 0.1721 0.1402 0.0250  -0.0219 0.0043  258 ALA A O   
2130 C  CB  . ALA A 257 ? 0.1865 0.1414 0.1297 -0.0119 -0.0021 -0.0043 258 ALA A CB  
2131 N  N   . SER A 258 ? 0.1405 0.1527 0.1330 -0.0148 -0.0030 0.0013  259 SER A N   
2132 C  CA  . SER A 258 ? 0.1520 0.1800 0.1396 -0.0127 -0.0088 0.0156  259 SER A CA  
2133 C  C   . SER A 258 ? 0.1678 0.1829 0.1263 -0.0038 -0.0293 0.0144  259 SER A C   
2134 O  O   . SER A 258 ? 0.2377 0.2490 0.1482 -0.0265 0.0143  0.0252  259 SER A O   
2135 C  CB  . SER A 258 ? 0.1551 0.1951 0.1305 -0.0077 0.0125  -0.0048 259 SER A CB  
2136 O  OG  . SER A 258 ? 0.1653 0.1836 0.1195 0.0015  -0.0222 -0.0006 259 SER A OG  
2137 N  N   . PHE A 259 ? 0.2134 0.1838 0.1446 0.0044  -0.0236 -0.0239 260 PHE A N   
2138 C  CA  . PHE A 259 ? 0.2228 0.1921 0.1741 -0.0041 -0.0164 -0.0562 260 PHE A CA  
2139 C  C   . PHE A 259 ? 0.2262 0.2206 0.1884 -0.0170 -0.0434 -0.0562 260 PHE A C   
2140 O  O   . PHE A 259 ? 0.2215 0.2199 0.2422 -0.0043 -0.0074 -0.0447 260 PHE A O   
2141 C  CB  . PHE A 259 ? 0.2002 0.2290 0.1247 0.0082  -0.0059 0.0111  260 PHE A CB  
2142 C  CG  . PHE A 259 ? 0.1872 0.1759 0.1445 -0.0071 0.0051  -0.0044 260 PHE A CG  
2143 C  CD1 . PHE A 259 ? 0.1565 0.1906 0.1556 0.0310  -0.0019 -0.0260 260 PHE A CD1 
2144 C  CD2 . PHE A 259 ? 0.2736 0.1948 0.1703 -0.0219 -0.0052 -0.0276 260 PHE A CD2 
2145 C  CE1 . PHE A 259 ? 0.1617 0.2075 0.2158 0.0364  0.0132  0.0017  260 PHE A CE1 
2146 C  CE2 . PHE A 259 ? 0.3251 0.1878 0.2364 -0.0154 -0.0241 0.0137  260 PHE A CE2 
2147 C  CZ  . PHE A 259 ? 0.2957 0.2108 0.2542 0.0225  0.0052  -0.0305 260 PHE A CZ  
2148 N  N   . LYS A 260 ? 0.3912 0.3842 0.2861 -0.0505 -0.0500 -0.1641 261 LYS A N   
2149 C  CA  . LYS A 260 ? 0.3612 0.4325 0.4634 -0.1339 -0.0608 -0.0790 261 LYS A CA  
2150 C  C   . LYS A 260 ? 0.5464 0.6876 0.6793 -0.0427 -0.0041 0.0857  261 LYS A C   
2151 O  O   . LYS A 260 ? 0.9174 1.0647 0.4663 -0.1881 -0.4020 -0.0285 261 LYS A O   
2152 C  CB  . LYS A 260 ? 0.4505 0.5623 0.3842 -0.0364 -0.2081 -0.0245 261 LYS A CB  
2153 C  CG  . LYS A 260 ? 0.5202 0.7232 0.6696 0.0784  -0.0929 -0.0714 261 LYS A CG  
2154 C  CD  . LYS A 260 ? 0.5153 0.2739 0.4851 -0.0657 -0.0515 -0.1903 261 LYS A CD  
2155 C  CE  . LYS A 260 ? 0.6032 0.5236 0.3614 0.0627  -0.2342 -0.0071 261 LYS A CE  
2156 N  NZ  . LYS A 260 ? 0.3971 0.4183 0.4805 -0.0810 -0.1159 0.0192  261 LYS A NZ  
2157 N  N   . HIS B 3   ? 0.3802 0.3986 0.3621 -0.0463 0.0653  0.1096  3   HIS B N   
2158 C  CA  . HIS B 3   ? 0.4095 0.4779 0.4707 -0.0261 0.0377  0.0491  3   HIS B CA  
2159 C  C   . HIS B 3   ? 0.5006 0.6407 0.3686 -0.0350 0.0445  0.0907  3   HIS B C   
2160 O  O   . HIS B 3   ? 0.4783 0.6215 0.6298 0.0209  0.0838  -0.0803 3   HIS B O   
2161 C  CB  . HIS B 3   ? 0.3326 0.4486 0.4821 -0.3305 0.1508  -0.3230 3   HIS B CB  
2162 C  CG  . HIS B 3   ? 0.7152 0.6768 1.0289 -0.3091 -0.3418 -0.1900 3   HIS B CG  
2163 N  ND1 . HIS B 3   ? 0.7027 0.7562 0.7675 -0.0732 0.6830  -0.1837 3   HIS B ND1 
2164 C  CD2 . HIS B 3   ? 0.3253 0.7174 0.6597 -0.2266 -0.0083 -0.5684 3   HIS B CD2 
2165 C  CE1 . HIS B 3   ? 1.0815 0.9117 1.0549 0.0306  0.1720  -0.1903 3   HIS B CE1 
2166 N  NE2 . HIS B 3   ? 0.6601 0.8604 1.0777 -0.0877 0.1732  -0.2010 3   HIS B NE2 
2167 N  N   . HIS B 4   ? 0.4790 0.4939 0.2529 -0.1208 -0.0159 -0.0904 4   HIS B N   
2168 C  CA  . HIS B 4   ? 0.6047 0.2939 0.2849 -0.0379 -0.0476 -0.1097 4   HIS B CA  
2169 C  C   . HIS B 4   ? 0.3596 0.2368 0.1885 0.0076  -0.0505 -0.0161 4   HIS B C   
2170 O  O   . HIS B 4   ? 0.2883 0.2741 0.2036 0.0197  -0.0232 -0.0068 4   HIS B O   
2171 C  CB  . HIS B 4   ? 0.5577 0.6057 0.2737 -0.1897 -0.0357 -0.1186 4   HIS B CB  
2172 C  CG  . HIS B 4   ? 0.5573 0.7861 0.6966 -0.0575 0.1679  -0.1036 4   HIS B CG  
2173 N  ND1 . HIS B 4   ? 0.7210 0.7116 0.4088 -0.1155 -0.0093 -0.0208 4   HIS B ND1 
2174 C  CD2 . HIS B 4   ? 0.7524 0.8070 0.9982 -0.0582 -0.0137 -0.3264 4   HIS B CD2 
2175 C  CE1 . HIS B 4   ? 0.7547 1.0874 1.3262 -0.3120 -0.2117 -0.1656 4   HIS B CE1 
2176 N  NE2 . HIS B 4   ? 0.5608 1.0893 1.2451 -0.1279 -0.2770 -0.0093 4   HIS B NE2 
2177 N  N   . TRP B 5   ? 0.3073 0.2266 0.1376 0.0032  -0.0282 -0.0229 5   TRP B N   
2178 C  CA  . TRP B 5   ? 0.1999 0.1668 0.1545 0.0065  -0.0159 -0.0263 5   TRP B CA  
2179 C  C   . TRP B 5   ? 0.1887 0.1962 0.1549 -0.0020 -0.0008 0.0037  5   TRP B C   
2180 O  O   . TRP B 5   ? 0.2254 0.1972 0.1572 0.0000  -0.0091 -0.0167 5   TRP B O   
2181 C  CB  . TRP B 5   ? 0.2429 0.1944 0.1470 0.0307  -0.0008 0.0017  5   TRP B CB  
2182 C  CG  . TRP B 5   ? 0.2179 0.1897 0.1560 0.0013  -0.0091 -0.0214 5   TRP B CG  
2183 C  CD1 . TRP B 5   ? 0.2402 0.2011 0.1701 -0.0296 -0.0267 0.0044  5   TRP B CD1 
2184 C  CD2 . TRP B 5   ? 0.1579 0.1748 0.1587 0.0132  -0.0149 -0.0070 5   TRP B CD2 
2185 N  NE1 . TRP B 5   ? 0.2009 0.1647 0.1781 -0.0085 -0.0425 0.0015  5   TRP B NE1 
2186 C  CE2 . TRP B 5   ? 0.1726 0.1879 0.1581 0.0355  -0.0165 -0.0083 5   TRP B CE2 
2187 C  CE3 . TRP B 5   ? 0.1508 0.1635 0.1216 0.0208  -0.0052 0.0063  5   TRP B CE3 
2188 C  CZ2 . TRP B 5   ? 0.1628 0.2070 0.1662 -0.0098 -0.0135 0.0238  5   TRP B CZ2 
2189 C  CZ3 . TRP B 5   ? 0.1419 0.1818 0.1258 -0.0046 -0.0037 0.0165  5   TRP B CZ3 
2190 C  CH2 . TRP B 5   ? 0.1541 0.2120 0.1423 -0.0109 -0.0219 0.0285  5   TRP B CH2 
2191 N  N   . GLY B 6   ? 0.2226 0.1592 0.1213 0.0253  0.0163  0.0137  6   GLY B N   
2192 C  CA  . GLY B 6   ? 0.1585 0.1759 0.1533 0.0096  0.0126  0.0032  6   GLY B CA  
2193 C  C   . GLY B 6   ? 0.1863 0.1962 0.1165 0.0097  -0.0017 0.0035  6   GLY B C   
2194 O  O   . GLY B 6   ? 0.1771 0.1705 0.1412 0.0071  -0.0073 0.0175  6   GLY B O   
2195 N  N   . TYR B 7   ? 0.1814 0.1777 0.1115 0.0006  0.0006  0.0100  7   TYR B N   
2196 C  CA  . TYR B 7   ? 0.2623 0.1419 0.1064 -0.0285 0.0262  0.0087  7   TYR B CA  
2197 C  C   . TYR B 7   ? 0.5015 0.2348 0.1547 -0.0974 -0.0173 0.0877  7   TYR B C   
2198 O  O   . TYR B 7   ? 0.5878 0.2684 0.1965 -0.0527 -0.0126 0.0097  7   TYR B O   
2199 C  CB  . TYR B 7   ? 0.2359 0.1705 0.1197 0.0384  -0.0110 -0.0006 7   TYR B CB  
2200 C  CG  . TYR B 7   ? 0.1445 0.1230 0.1179 0.0181  0.0010  -0.0127 7   TYR B CG  
2201 C  CD1 . TYR B 7   ? 0.1429 0.1495 0.1177 0.0049  0.0065  0.0057  7   TYR B CD1 
2202 C  CD2 . TYR B 7   ? 0.1960 0.1375 0.0987 -0.0076 0.0137  -0.0082 7   TYR B CD2 
2203 C  CE1 . TYR B 7   ? 0.1529 0.1152 0.1059 0.0217  0.0207  -0.0062 7   TYR B CE1 
2204 C  CE2 . TYR B 7   ? 0.1407 0.1398 0.1146 0.0077  -0.0076 -0.0038 7   TYR B CE2 
2205 C  CZ  . TYR B 7   ? 0.1480 0.1368 0.0960 0.0104  -0.0110 -0.0026 7   TYR B CZ  
2206 O  OH  . TYR B 7   ? 0.1738 0.1240 0.1281 0.0094  -0.0129 0.0154  7   TYR B OH  
2207 N  N   . GLY B 8   ? 0.3984 0.2312 0.1164 0.0671  0.0366  0.0322  8   GLY B N   
2208 C  CA  . GLY B 8   ? 0.4194 0.1436 0.2202 0.0582  -0.0148 0.0309  8   GLY B CA  
2209 C  C   . GLY B 8   ? 0.3323 0.2594 0.3000 0.0098  -0.0813 0.0615  8   GLY B C   
2210 O  O   . GLY B 8   ? 0.4023 0.3280 0.1719 -0.0052 -0.0653 0.0450  8   GLY B O   
2211 N  N   . LYS B 9   ? 0.7985 0.2222 0.2129 -0.0458 0.0329  0.0179  9   LYS B N   
2212 C  CA  . LYS B 9   ? 0.6873 0.2831 0.4101 -0.0329 0.0658  0.0467  9   LYS B CA  
2213 C  C   . LYS B 9   ? 0.3935 0.4088 0.1854 -0.0932 -0.0031 0.0118  9   LYS B C   
2214 O  O   . LYS B 9   ? 0.4406 0.2497 0.2840 -0.0219 0.0715  -0.0175 9   LYS B O   
2215 C  CB  . LYS B 9   ? 0.7326 0.4779 0.3273 -0.1368 0.0954  0.1061  9   LYS B CB  
2216 C  CG  . LYS B 9   ? 0.3617 0.3395 0.3048 0.0001  0.0151  -0.1076 9   LYS B CG  
2217 N  N   . HIS B 10  ? 0.4086 0.2157 0.1798 -0.0441 -0.0522 0.0746  10  HIS B N   
2218 C  CA  . HIS B 10  ? 0.3418 0.2558 0.1781 0.0436  -0.0627 0.0544  10  HIS B CA  
2219 C  C   . HIS B 10  ? 0.2603 0.2409 0.1833 -0.0294 -0.0086 0.0693  10  HIS B C   
2220 O  O   . HIS B 10  ? 0.3707 0.3109 0.1608 0.0317  0.0034  0.0623  10  HIS B O   
2221 C  CB  . HIS B 10  ? 0.3242 0.2623 0.1392 0.0417  -0.0441 0.0370  10  HIS B CB  
2222 C  CG  . HIS B 10  ? 0.3082 0.2292 0.2393 0.0240  -0.0366 -0.0041 10  HIS B CG  
2223 N  ND1 . HIS B 10  ? 0.2991 0.2592 0.2527 -0.0176 -0.0590 0.0516  10  HIS B ND1 
2224 C  CD2 . HIS B 10  ? 0.3472 0.2845 0.1696 0.0329  0.0010  0.0342  10  HIS B CD2 
2225 C  CE1 . HIS B 10  ? 0.2847 0.2536 0.1885 0.0273  0.0001  0.0586  10  HIS B CE1 
2226 N  NE2 . HIS B 10  ? 0.2793 0.2989 0.2260 -0.0185 -0.0157 0.0395  10  HIS B NE2 
2227 N  N   . ASN B 11  ? 0.2820 0.2064 0.1287 -0.0190 -0.0221 0.0148  11  ASN B N   
2228 C  CA  . ASN B 11  ? 0.2829 0.2258 0.1303 0.0275  -0.0461 0.0527  11  ASN B CA  
2229 C  C   . ASN B 11  ? 0.2377 0.1791 0.1298 -0.0043 -0.0239 -0.0105 11  ASN B C   
2230 O  O   . ASN B 11  ? 0.2150 0.1908 0.1577 -0.0135 -0.0131 0.0269  11  ASN B O   
2231 C  CB  . ASN B 11  ? 0.2673 0.2271 0.1260 0.0190  -0.0176 0.0478  11  ASN B CB  
2232 C  CG  . ASN B 11  ? 0.2576 0.1966 0.1619 0.0111  -0.0604 0.0557  11  ASN B CG  
2233 O  OD1 . ASN B 11  ? 0.2836 0.2193 0.1840 0.0027  -0.0244 0.0154  11  ASN B OD1 
2234 N  ND2 . ASN B 11  ? 0.2892 0.2560 0.1664 -0.0031 -0.0203 0.0074  11  ASN B ND2 
2235 N  N   . GLY B 12  ? 0.2330 0.1847 0.1115 -0.0068 0.0010  0.0368  12  GLY B N   
2236 C  CA  . GLY B 12  ? 0.1710 0.2108 0.1086 0.0000  0.0060  0.0208  12  GLY B CA  
2237 C  C   . GLY B 12  ? 0.1865 0.1407 0.1466 -0.0109 -0.0104 0.0148  12  GLY B C   
2238 O  O   . GLY B 12  ? 0.1917 0.1547 0.1340 -0.0107 0.0153  0.0230  12  GLY B O   
2239 N  N   . PRO B 13  ? 0.2012 0.1538 0.1107 0.0177  -0.0070 -0.0032 13  PRO B N   
2240 C  CA  . PRO B 13  ? 0.1738 0.1623 0.1204 0.0137  0.0070  -0.0164 13  PRO B CA  
2241 C  C   . PRO B 13  ? 0.1623 0.1540 0.1353 -0.0124 -0.0153 -0.0055 13  PRO B C   
2242 O  O   . PRO B 13  ? 0.2117 0.1845 0.1155 0.0228  0.0167  0.0156  13  PRO B O   
2243 C  CB  . PRO B 13  ? 0.1919 0.1446 0.1324 -0.0030 -0.0074 -0.0198 13  PRO B CB  
2244 C  CG  . PRO B 13  ? 0.1917 0.1935 0.1653 0.0119  -0.0544 0.0179  13  PRO B CG  
2245 C  CD  . PRO B 13  ? 0.1694 0.1911 0.1269 0.0300  -0.0057 0.0076  13  PRO B CD  
2246 N  N   A GLU B 14  ? 0.1567 0.1481 0.1601 0.0038  0.0124  0.0000  14  GLU B N   
2247 N  N   B GLU B 14  ? 0.1955 0.1601 0.1642 -0.0230 0.0195  0.0013  14  GLU B N   
2248 C  CA  A GLU B 14  ? 0.1554 0.1725 0.1958 -0.0154 0.0087  -0.0073 14  GLU B CA  
2249 C  CA  B GLU B 14  ? 0.2253 0.1646 0.2185 -0.0203 0.0439  -0.0148 14  GLU B CA  
2250 C  C   A GLU B 14  ? 0.1791 0.1700 0.1342 -0.0198 0.0186  0.0381  14  GLU B C   
2251 C  C   B GLU B 14  ? 0.1989 0.1788 0.1502 -0.0220 0.0062  0.0326  14  GLU B C   
2252 O  O   A GLU B 14  ? 0.1676 0.1727 0.1861 -0.0081 0.0215  0.0093  14  GLU B O   
2253 O  O   B GLU B 14  ? 0.2581 0.2280 0.2328 -0.0194 0.0900  0.0498  14  GLU B O   
2254 C  CB  A GLU B 14  ? 0.1344 0.1983 0.2088 -0.0192 0.0405  0.0366  14  GLU B CB  
2255 C  CB  B GLU B 14  ? 0.3307 0.1641 0.2294 -0.0219 0.0621  0.0096  14  GLU B CB  
2256 C  CG  A GLU B 14  ? 0.1958 0.1990 0.1826 -0.0211 0.0179  0.0024  14  GLU B CG  
2257 C  CG  B GLU B 14  ? 0.3571 0.1805 0.2046 -0.0979 -0.0342 -0.0289 14  GLU B CG  
2258 C  CD  A GLU B 14  ? 0.2217 0.2052 0.1465 -0.0136 0.0351  0.0263  14  GLU B CD  
2259 C  CD  B GLU B 14  ? 0.2493 0.3014 0.2890 -0.0820 -0.0339 -0.0166 14  GLU B CD  
2260 O  OE1 A GLU B 14  ? 0.1844 0.1498 0.1834 0.0487  0.0548  0.0822  14  GLU B OE1 
2261 O  OE1 B GLU B 14  ? 0.2876 0.3425 0.4237 -0.0104 0.0524  0.1318  14  GLU B OE1 
2262 O  OE2 A GLU B 14  ? 0.2321 0.1423 0.3431 0.0317  -0.0538 0.0017  14  GLU B OE2 
2263 O  OE2 B GLU B 14  ? 0.3219 0.2746 0.2529 -0.0173 -0.0592 0.0964  14  GLU B OE2 
2264 N  N   . HIS B 15  ? 0.1835 0.1392 0.1220 -0.0070 0.0153  0.0204  15  HIS B N   
2265 C  CA  . HIS B 15  ? 0.1660 0.1601 0.1114 -0.0037 0.0359  0.0000  15  HIS B CA  
2266 C  C   . HIS B 15  ? 0.1711 0.1520 0.1176 0.0129  0.0502  0.0259  15  HIS B C   
2267 O  O   . HIS B 15  ? 0.2125 0.1659 0.1109 -0.0198 0.0362  0.0136  15  HIS B O   
2268 C  CB  . HIS B 15  ? 0.1674 0.2070 0.1459 -0.0190 0.0167  0.0313  15  HIS B CB  
2269 C  CG  . HIS B 15  ? 0.2366 0.2028 0.1596 -0.0230 0.0309  0.0222  15  HIS B CG  
2270 N  ND1 . HIS B 15  ? 0.3018 0.2869 0.1699 0.0206  0.0463  0.0727  15  HIS B ND1 
2271 C  CD2 . HIS B 15  ? 0.2332 0.2400 0.1538 0.0331  -0.0137 0.0562  15  HIS B CD2 
2272 C  CE1 . HIS B 15  ? 0.2913 0.2402 0.2890 0.0109  0.0562  0.0957  15  HIS B CE1 
2273 N  NE2 . HIS B 15  ? 0.2840 0.2795 0.2245 0.0027  -0.0028 0.1052  15  HIS B NE2 
2274 N  N   . TRP B 16  ? 0.1516 0.1482 0.0983 -0.0108 0.0206  0.0185  16  TRP B N   
2275 C  CA  . TRP B 16  ? 0.1748 0.1429 0.0996 0.0156  0.0450  0.0126  16  TRP B CA  
2276 C  C   . TRP B 16  ? 0.1513 0.1536 0.0791 0.0031  0.0264  0.0115  16  TRP B C   
2277 O  O   . TRP B 16  ? 0.1811 0.1484 0.1220 -0.0135 0.0368  0.0060  16  TRP B O   
2278 C  CB  . TRP B 16  ? 0.1360 0.1675 0.0877 0.0186  0.0253  -0.0057 16  TRP B CB  
2279 C  CG  . TRP B 16  ? 0.1283 0.1326 0.1206 0.0020  0.0060  0.0091  16  TRP B CG  
2280 C  CD1 . TRP B 16  ? 0.1328 0.1453 0.1218 0.0178  -0.0019 0.0104  16  TRP B CD1 
2281 C  CD2 . TRP B 16  ? 0.1347 0.1348 0.1129 0.0081  0.0100  -0.0046 16  TRP B CD2 
2282 N  NE1 . TRP B 16  ? 0.1708 0.1418 0.1037 0.0165  0.0105  0.0131  16  TRP B NE1 
2283 C  CE2 . TRP B 16  ? 0.1301 0.1412 0.1057 -0.0116 -0.0099 0.0100  16  TRP B CE2 
2284 C  CE3 . TRP B 16  ? 0.1664 0.1308 0.0942 0.0131  0.0214  0.0057  16  TRP B CE3 
2285 C  CZ2 . TRP B 16  ? 0.1638 0.1194 0.1019 0.0137  -0.0034 0.0055  16  TRP B CZ2 
2286 C  CZ3 . TRP B 16  ? 0.1355 0.1375 0.1021 0.0066  0.0240  -0.0013 16  TRP B CZ3 
2287 C  CH2 . TRP B 16  ? 0.1444 0.1317 0.1059 0.0020  -0.0324 -0.0046 16  TRP B CH2 
2288 N  N   . HIS B 17  ? 0.1480 0.1630 0.1066 -0.0007 0.0318  0.0037  17  HIS B N   
2289 C  CA  . HIS B 17  ? 0.1445 0.1659 0.1159 -0.0038 0.0383  -0.0264 17  HIS B CA  
2290 C  C   . HIS B 17  ? 0.1646 0.1802 0.1098 0.0091  0.0017  -0.0137 17  HIS B C   
2291 O  O   . HIS B 17  ? 0.1897 0.1937 0.1295 0.0073  0.0522  -0.0003 17  HIS B O   
2292 C  CB  . HIS B 17  ? 0.1664 0.2131 0.1080 -0.0271 0.0292  0.0062  17  HIS B CB  
2293 C  CG  . HIS B 17  ? 0.2082 0.1856 0.1342 0.0043  0.0289  -0.0151 17  HIS B CG  
2294 N  ND1 . HIS B 17  ? 0.2271 0.2730 0.1632 -0.0210 0.0593  -0.0076 17  HIS B ND1 
2295 C  CD2 . HIS B 17  ? 0.1685 0.1944 0.1159 -0.0176 0.0225  0.0189  17  HIS B CD2 
2296 C  CE1 . HIS B 17  ? 0.2527 0.2547 0.2231 0.0057  0.0017  0.0538  17  HIS B CE1 
2297 N  NE2 . HIS B 17  ? 0.2256 0.2202 0.1303 -0.0452 0.0472  0.0104  17  HIS B NE2 
2298 N  N   . LYS B 18  ? 0.1714 0.1771 0.1118 0.0087  0.0315  -0.0003 18  LYS B N   
2299 C  CA  . LYS B 18  ? 0.2301 0.2055 0.1194 0.0144  0.0221  -0.0324 18  LYS B CA  
2300 C  C   . LYS B 18  ? 0.1717 0.2238 0.1827 0.0071  0.0493  -0.0214 18  LYS B C   
2301 O  O   . LYS B 18  ? 0.2904 0.2542 0.2378 -0.0282 0.1045  -0.0913 18  LYS B O   
2302 C  CB  . LYS B 18  ? 0.2389 0.1958 0.1145 -0.0201 0.0351  0.0167  18  LYS B CB  
2303 C  CG  . LYS B 18  ? 0.2057 0.2172 0.1610 -0.0175 0.0364  0.0489  18  LYS B CG  
2304 C  CD  . LYS B 18  ? 0.2310 0.2285 0.1412 -0.0219 0.0364  0.0463  18  LYS B CD  
2305 C  CE  . LYS B 18  ? 0.1727 0.2201 0.2007 -0.0141 -0.0362 -0.0065 18  LYS B CE  
2306 N  NZ  . LYS B 18  ? 0.1879 0.2883 0.1619 -0.0348 0.0048  0.0491  18  LYS B NZ  
2307 N  N   . ASP B 19  ? 0.1759 0.2229 0.1619 -0.0102 0.0467  0.0160  19  ASP B N   
2308 C  CA  . ASP B 19  ? 0.2166 0.2274 0.1651 -0.0063 0.0073  0.0020  19  ASP B CA  
2309 C  C   . ASP B 19  ? 0.2405 0.1980 0.1692 -0.0264 -0.0035 -0.0159 19  ASP B C   
2310 O  O   . ASP B 19  ? 0.2860 0.1764 0.1626 -0.0054 0.0120  -0.0463 19  ASP B O   
2311 C  CB  . ASP B 19  ? 0.2138 0.2518 0.1793 -0.0125 0.0562  0.0333  19  ASP B CB  
2312 C  CG  . ASP B 19  ? 0.3140 0.3838 0.2382 0.0333  0.0049  -0.0414 19  ASP B CG  
2313 O  OD1 . ASP B 19  ? 0.3569 0.3332 0.2809 -0.0197 0.0586  -0.0144 19  ASP B OD1 
2314 O  OD2 . ASP B 19  ? 0.4997 0.7888 0.3345 0.1953  0.0494  0.0582  19  ASP B OD2 
2315 N  N   . PHE B 20  ? 0.2079 0.1784 0.1306 -0.0375 0.0175  -0.0149 20  PHE B N   
2316 C  CA  . PHE B 20  ? 0.2120 0.1951 0.1286 0.0322  0.0384  -0.0054 20  PHE B CA  
2317 C  C   . PHE B 20  ? 0.1958 0.1739 0.1540 0.0013  0.0317  -0.0049 20  PHE B C   
2318 O  O   . PHE B 20  ? 0.1867 0.1563 0.1526 0.0060  0.0381  -0.0140 20  PHE B O   
2319 C  CB  . PHE B 20  ? 0.1897 0.1628 0.1152 -0.0034 0.0340  -0.0091 20  PHE B CB  
2320 C  CG  . PHE B 20  ? 0.1903 0.2021 0.0996 0.0092  0.0340  -0.0500 20  PHE B CG  
2321 C  CD1 . PHE B 20  ? 0.2258 0.2815 0.1307 -0.0342 0.0348  -0.0263 20  PHE B CD1 
2322 C  CD2 . PHE B 20  ? 0.2011 0.2355 0.1561 0.0187  0.0201  -0.0538 20  PHE B CD2 
2323 C  CE1 . PHE B 20  ? 0.1888 0.2133 0.1926 -0.0096 0.0425  -0.0124 20  PHE B CE1 
2324 C  CE2 . PHE B 20  ? 0.2635 0.2531 0.1938 -0.0410 0.0171  -0.0331 20  PHE B CE2 
2325 C  CZ  . PHE B 20  ? 0.2285 0.2440 0.1233 -0.0048 0.0359  -0.0482 20  PHE B CZ  
2326 N  N   . PRO B 21  ? 0.1768 0.1910 0.1486 -0.0044 0.0068  -0.0377 21  PRO B N   
2327 C  CA  . PRO B 21  ? 0.1414 0.2159 0.1281 0.0237  0.0024  -0.0505 21  PRO B CA  
2328 C  C   . PRO B 21  ? 0.1648 0.1438 0.1340 0.0364  0.0281  -0.0044 21  PRO B C   
2329 O  O   . PRO B 21  ? 0.1768 0.1809 0.1498 0.0034  0.0496  -0.0055 21  PRO B O   
2330 C  CB  . PRO B 21  ? 0.2131 0.3152 0.1678 0.0258  0.0689  -0.0976 21  PRO B CB  
2331 C  CG  . PRO B 21  ? 0.2639 0.3305 0.3199 -0.0057 0.0308  -0.1480 21  PRO B CG  
2332 C  CD  . PRO B 21  ? 0.2485 0.2370 0.1552 -0.0104 0.0243  -0.0688 21  PRO B CD  
2333 N  N   . ILE B 22  ? 0.1699 0.1307 0.1493 0.0244  0.0368  -0.0024 22  ILE B N   
2334 C  CA  . ILE B 22  ? 0.2070 0.1401 0.1558 -0.0024 0.0197  -0.0024 22  ILE B CA  
2335 C  C   . ILE B 22  ? 0.1569 0.1477 0.1441 0.0144  0.0227  0.0087  22  ILE B C   
2336 O  O   . ILE B 22  ? 0.1791 0.1701 0.1466 0.0060  0.0164  0.0074  22  ILE B O   
2337 C  CB  . ILE B 22  ? 0.1522 0.1577 0.1689 0.0103  0.0225  0.0140  22  ILE B CB  
2338 C  CG1 . ILE B 22  ? 0.1872 0.1556 0.1759 0.0240  0.0085  -0.0171 22  ILE B CG1 
2339 C  CG2 . ILE B 22  ? 0.1515 0.1899 0.1495 0.0390  0.0270  -0.0074 22  ILE B CG2 
2340 C  CD1 . ILE B 22  ? 0.2208 0.1914 0.2059 -0.0019 0.0237  -0.0104 22  ILE B CD1 
2341 N  N   . ALA B 23  ? 0.1425 0.1429 0.1438 0.0155  0.0209  -0.0005 23  ALA B N   
2342 C  CA  . ALA B 23  ? 0.1565 0.1377 0.1179 0.0190  0.0082  -0.0052 23  ALA B CA  
2343 C  C   . ALA B 23  ? 0.1507 0.1641 0.1267 0.0175  0.0111  -0.0140 23  ALA B C   
2344 O  O   . ALA B 23  ? 0.1867 0.1421 0.1534 0.0020  0.0283  -0.0115 23  ALA B O   
2345 C  CB  . ALA B 23  ? 0.1676 0.1409 0.1344 0.0397  0.0342  0.0178  23  ALA B CB  
2346 N  N   . LYS B 24  ? 0.1447 0.1538 0.1730 -0.0063 0.0362  0.0104  24  LYS B N   
2347 C  CA  . LYS B 24  ? 0.1324 0.2064 0.1208 0.0041  0.0390  0.0003  24  LYS B CA  
2348 C  C   . LYS B 24  ? 0.1965 0.2078 0.1477 0.0248  0.0210  -0.0020 24  LYS B C   
2349 O  O   . LYS B 24  ? 0.2021 0.2381 0.1770 0.0153  0.0395  0.0089  24  LYS B O   
2350 C  CB  . LYS B 24  ? 0.2066 0.2084 0.1569 -0.0076 0.0562  0.0277  24  LYS B CB  
2351 C  CG  . LYS B 24  ? 0.1905 0.2156 0.1924 0.0164  0.0452  0.0342  24  LYS B CG  
2352 C  CD  . LYS B 24  ? 0.2763 0.3298 0.1808 0.0052  0.0833  0.0403  24  LYS B CD  
2353 C  CE  . LYS B 24  ? 0.2928 0.2931 0.2023 -0.0098 0.0277  -0.0262 24  LYS B CE  
2354 N  NZ  . LYS B 24  ? 0.5327 0.2504 0.2339 -0.0412 0.0643  0.0149  24  LYS B NZ  
2355 N  N   . GLY B 25  ? 0.1549 0.1689 0.1730 0.0174  0.0149  0.0153  25  GLY B N   
2356 C  CA  . GLY B 25  ? 0.1659 0.2335 0.1296 0.0648  0.0098  -0.0129 25  GLY B CA  
2357 C  C   . GLY B 25  ? 0.1285 0.1876 0.1659 0.0012  0.0153  0.0052  25  GLY B C   
2358 O  O   . GLY B 25  ? 0.1366 0.2019 0.1843 -0.0013 0.0247  0.0351  25  GLY B O   
2359 N  N   . GLU B 26  ? 0.1190 0.2343 0.1613 0.0531  0.0460  0.0165  26  GLU B N   
2360 C  CA  . GLU B 26  ? 0.1481 0.2041 0.1838 0.0344  0.0171  -0.0044 26  GLU B CA  
2361 C  C   . GLU B 26  ? 0.1560 0.1614 0.1701 0.0000  0.0292  0.0108  26  GLU B C   
2362 O  O   . GLU B 26  ? 0.1206 0.2046 0.1845 0.0219  0.0094  0.0104  26  GLU B O   
2363 C  CB  . GLU B 26  ? 0.1416 0.2348 0.1994 0.0604  0.0305  -0.0046 26  GLU B CB  
2364 C  CG  . GLU B 26  ? 0.1603 0.2867 0.2091 0.0653  0.0401  0.0209  26  GLU B CG  
2365 C  CD  . GLU B 26  ? 0.2451 0.3916 0.3248 -0.0115 0.0995  0.0195  26  GLU B CD  
2366 O  OE1 . GLU B 26  ? 0.3276 0.4568 0.4542 -0.0209 0.0975  -0.0604 26  GLU B OE1 
2367 O  OE2 . GLU B 26  ? 0.3662 0.6401 0.4162 -0.0244 0.1510  0.0975  26  GLU B OE2 
2368 N  N   . ARG B 27  ? 0.1439 0.1410 0.1456 0.0143  0.0005  -0.0023 27  ARG B N   
2369 C  CA  . ARG B 27  ? 0.1161 0.1367 0.1224 0.0141  -0.0024 0.0093  27  ARG B CA  
2370 C  C   . ARG B 27  ? 0.1073 0.1317 0.1341 0.0081  0.0120  0.0060  27  ARG B C   
2371 O  O   . ARG B 27  ? 0.1324 0.1348 0.1423 0.0098  0.0163  0.0188  27  ARG B O   
2372 C  CB  . ARG B 27  ? 0.1455 0.1667 0.1784 0.0197  -0.0116 0.0223  27  ARG B CB  
2373 C  CG  . ARG B 27  ? 0.1637 0.2079 0.2129 0.0044  -0.0143 -0.0010 27  ARG B CG  
2374 C  CD  . ARG B 27  ? 0.1638 0.2470 0.2199 -0.0210 -0.0245 0.0017  27  ARG B CD  
2375 N  NE  . ARG B 27  ? 0.1779 0.2210 0.2039 -0.0010 -0.0337 0.0255  27  ARG B NE  
2376 C  CZ  . ARG B 27  ? 0.1599 0.1861 0.2168 0.0251  0.0043  0.0362  27  ARG B CZ  
2377 N  NH1 . ARG B 27  ? 0.2003 0.1965 0.2212 0.0575  -0.0305 0.0952  27  ARG B NH1 
2378 N  NH2 . ARG B 27  ? 0.1701 0.1924 0.1646 0.0189  -0.0136 0.0230  27  ARG B NH2 
2379 N  N   . GLN B 28  ? 0.1097 0.1401 0.1179 0.0220  -0.0017 0.0038  28  GLN B N   
2380 C  CA  . GLN B 28  ? 0.1176 0.1380 0.1163 0.0414  -0.0003 0.0043  28  GLN B CA  
2381 C  C   . GLN B 28  ? 0.0978 0.0917 0.1186 -0.0027 0.0065  -0.0017 28  GLN B C   
2382 O  O   . GLN B 28  ? 0.0922 0.1193 0.1186 0.0038  0.0015  0.0054  28  GLN B O   
2383 C  CB  . GLN B 28  ? 0.1342 0.1351 0.1005 0.0060  0.0155  0.0049  28  GLN B CB  
2384 C  CG  . GLN B 28  ? 0.1432 0.1195 0.1419 0.0192  0.0135  -0.0054 28  GLN B CG  
2385 C  CD  . GLN B 28  ? 0.1152 0.1276 0.1080 0.0164  0.0098  0.0189  28  GLN B CD  
2386 O  OE1 . GLN B 28  ? 0.1278 0.1204 0.1209 0.0234  0.0105  -0.0027 28  GLN B OE1 
2387 N  NE2 . GLN B 28  ? 0.1306 0.1298 0.1068 0.0023  0.0350  0.0057  28  GLN B NE2 
2388 N  N   . SER B 29  ? 0.1024 0.1055 0.0906 0.0176  0.0000  0.0192  29  SER B N   
2389 C  CA  . SER B 29  ? 0.0970 0.1084 0.0890 0.0103  0.0225  0.0114  29  SER B CA  
2390 C  C   . SER B 29  ? 0.1071 0.0904 0.0997 0.0100  0.0035  0.0098  29  SER B C   
2391 O  O   . SER B 29  ? 0.1184 0.1150 0.0991 0.0091  0.0080  0.0071  29  SER B O   
2392 C  CB  . SER B 29  ? 0.0958 0.0982 0.1249 0.0115  0.0205  0.0230  29  SER B CB  
2393 O  OG  . SER B 29  ? 0.1263 0.1015 0.1123 0.0151  0.0013  -0.0005 29  SER B OG  
2394 N  N   . PRO B 30  ? 0.1006 0.0964 0.0807 0.0013  0.0060  0.0081  30  PRO B N   
2395 C  CA  . PRO B 30  ? 0.1102 0.0921 0.0978 -0.0038 -0.0081 -0.0109 30  PRO B CA  
2396 C  C   . PRO B 30  ? 0.0820 0.1159 0.0967 0.0217  -0.0097 0.0013  30  PRO B C   
2397 O  O   . PRO B 30  ? 0.0957 0.1073 0.1071 0.0017  -0.0013 0.0038  30  PRO B O   
2398 C  CB  . PRO B 30  ? 0.1172 0.0897 0.0829 0.0111  0.0250  0.0248  30  PRO B CB  
2399 C  CG  . PRO B 30  ? 0.1147 0.1130 0.0676 0.0125  0.0092  0.0019  30  PRO B CG  
2400 C  CD  . PRO B 30  ? 0.1179 0.1105 0.0976 0.0207  -0.0109 0.0080  30  PRO B CD  
2401 N  N   . VAL B 31  ? 0.1008 0.1023 0.0961 -0.0163 -0.0057 0.0059  31  VAL B N   
2402 C  CA  . VAL B 31  ? 0.0935 0.1076 0.1367 -0.0082 -0.0135 -0.0146 31  VAL B CA  
2403 C  C   . VAL B 31  ? 0.1026 0.1190 0.0931 -0.0129 -0.0108 -0.0013 31  VAL B C   
2404 O  O   . VAL B 31  ? 0.1164 0.1247 0.1215 -0.0037 0.0098  -0.0096 31  VAL B O   
2405 C  CB  . VAL B 31  ? 0.1067 0.1280 0.1129 0.0098  -0.0132 0.0024  31  VAL B CB  
2406 C  CG1 . VAL B 31  ? 0.1569 0.1268 0.1588 0.0137  -0.0148 0.0000  31  VAL B CG1 
2407 C  CG2 . VAL B 31  ? 0.1328 0.1263 0.1242 -0.0020 -0.0153 0.0155  31  VAL B CG2 
2408 N  N   . ASP B 32  ? 0.1154 0.1032 0.1121 -0.0164 -0.0109 0.0104  32  ASP B N   
2409 C  CA  . ASP B 32  ? 0.1526 0.1121 0.1191 -0.0192 -0.0017 0.0107  32  ASP B CA  
2410 C  C   . ASP B 32  ? 0.0922 0.0944 0.1296 -0.0201 -0.0118 0.0048  32  ASP B C   
2411 O  O   . ASP B 32  ? 0.1228 0.1455 0.1360 0.0115  -0.0119 -0.0074 32  ASP B O   
2412 C  CB  . ASP B 32  ? 0.1386 0.1085 0.1365 -0.0142 -0.0111 0.0223  32  ASP B CB  
2413 C  CG  . ASP B 32  ? 0.1342 0.1583 0.1445 -0.0183 -0.0006 0.0035  32  ASP B CG  
2414 O  OD1 . ASP B 32  ? 0.1435 0.1136 0.1324 -0.0093 0.0065  -0.0099 32  ASP B OD1 
2415 O  OD2 . ASP B 32  ? 0.1486 0.1312 0.2260 -0.0156 -0.0265 -0.0044 32  ASP B OD2 
2416 N  N   . ILE B 33  ? 0.1218 0.0962 0.1091 -0.0137 -0.0085 0.0163  33  ILE B N   
2417 C  CA  . ILE B 33  ? 0.1317 0.1307 0.1032 -0.0099 -0.0120 0.0019  33  ILE B CA  
2418 C  C   . ILE B 33  ? 0.1378 0.1280 0.1448 0.0013  -0.0188 0.0001  33  ILE B C   
2419 O  O   . ILE B 33  ? 0.1404 0.1450 0.1459 -0.0131 -0.0093 -0.0135 33  ILE B O   
2420 C  CB  . ILE B 33  ? 0.1588 0.1296 0.1138 -0.0155 -0.0087 -0.0006 33  ILE B CB  
2421 C  CG1 . ILE B 33  ? 0.1299 0.1226 0.1197 -0.0164 -0.0184 0.0006  33  ILE B CG1 
2422 C  CG2 . ILE B 33  ? 0.1405 0.1651 0.1181 -0.0313 -0.0350 0.0152  33  ILE B CG2 
2423 C  CD1 . ILE B 33  ? 0.1721 0.1499 0.1696 -0.0259 0.0296  0.0081  33  ILE B CD1 
2424 N  N   . ASP B 34  ? 0.1385 0.1554 0.1784 -0.0197 -0.0366 0.0111  34  ASP B N   
2425 C  CA  . ASP B 34  ? 0.1942 0.1587 0.1912 -0.0328 -0.0105 -0.0077 34  ASP B CA  
2426 C  C   . ASP B 34  ? 0.1410 0.1592 0.1859 -0.0337 -0.0502 0.0097  34  ASP B C   
2427 O  O   . ASP B 34  ? 0.1691 0.1651 0.1967 -0.0132 -0.0397 0.0028  34  ASP B O   
2428 C  CB  . ASP B 34  ? 0.1624 0.1728 0.2029 -0.0186 -0.0136 0.0176  34  ASP B CB  
2429 C  CG  . ASP B 34  ? 0.2500 0.2278 0.2416 -0.0288 -0.0362 -0.0186 34  ASP B CG  
2430 O  OD1 . ASP B 34  ? 0.2397 0.2333 0.2441 -0.0452 -0.0297 0.0032  34  ASP B OD1 
2431 O  OD2 . ASP B 34  ? 0.3222 0.3738 0.2777 -0.1089 -0.0044 -0.0408 34  ASP B OD2 
2432 N  N   . THR B 35  ? 0.1762 0.1574 0.1698 -0.0436 -0.0313 0.0227  35  THR B N   
2433 C  CA  . THR B 35  ? 0.2043 0.1931 0.1696 -0.0454 -0.0151 0.0137  35  THR B CA  
2434 C  C   . THR B 35  ? 0.2328 0.1957 0.2282 -0.0346 -0.0706 0.0675  35  THR B C   
2435 O  O   . THR B 35  ? 0.2267 0.2172 0.2037 -0.0390 -0.0687 0.0218  35  THR B O   
2436 C  CB  . THR B 35  ? 0.2079 0.1881 0.1064 -0.0322 -0.0205 0.0320  35  THR B CB  
2437 O  OG1 . THR B 35  ? 0.2267 0.2111 0.1730 -0.0480 -0.0570 0.0126  35  THR B OG1 
2438 C  CG2 . THR B 35  ? 0.2011 0.2517 0.1933 -0.0571 -0.0357 0.0487  35  THR B CG2 
2439 N  N   . HIS B 36  ? 0.2194 0.2709 0.2197 -0.0335 -0.1079 0.0483  36  HIS B N   
2440 C  CA  . HIS B 36  ? 0.2073 0.2017 0.2339 -0.0727 -0.0988 0.0271  36  HIS B CA  
2441 C  C   . HIS B 36  ? 0.3273 0.2680 0.2305 -0.0019 -0.0794 0.0302  36  HIS B C   
2442 O  O   . HIS B 36  ? 0.3497 0.2705 0.4516 -0.0187 -0.1535 -0.0281 36  HIS B O   
2443 C  CB  . HIS B 36  ? 0.2020 0.2023 0.2915 -0.0364 -0.0957 0.0265  36  HIS B CB  
2444 C  CG  . HIS B 36  ? 0.2544 0.2337 0.3713 -0.0315 -0.0445 -0.0222 36  HIS B CG  
2445 N  ND1 . HIS B 36  ? 0.3984 0.3731 0.3513 -0.0082 -0.0816 0.0171  36  HIS B ND1 
2446 C  CD2 . HIS B 36  ? 0.1506 0.2188 0.3136 -0.0386 -0.0135 -0.0359 36  HIS B CD2 
2447 C  CE1 . HIS B 36  ? 0.2134 0.1842 0.3422 -0.0922 -0.0223 0.0458  36  HIS B CE1 
2448 N  NE2 . HIS B 36  ? 0.1887 0.2694 0.3364 -0.0212 -0.0456 0.0410  36  HIS B NE2 
2449 N  N   . THR B 37  ? 0.2561 0.2266 0.2443 -0.0059 -0.0417 0.0125  37  THR B N   
2450 C  CA  . THR B 37  ? 0.2255 0.2026 0.2499 -0.0342 -0.0401 0.0318  37  THR B CA  
2451 C  C   . THR B 37  ? 0.1926 0.2296 0.3152 -0.0467 -0.0264 0.0390  37  THR B C   
2452 O  O   . THR B 37  ? 0.2363 0.2319 0.3682 -0.0644 -0.0579 0.0427  37  THR B O   
2453 C  CB  . THR B 37  ? 0.2894 0.4743 0.3251 -0.0258 0.0226  0.1072  37  THR B CB  
2454 O  OG1 . THR B 37  ? 0.3777 0.5289 0.3688 -0.0041 -0.0102 -0.0060 37  THR B OG1 
2455 C  CG2 . THR B 37  ? 0.3826 0.2845 0.3055 -0.0049 -0.0164 0.1010  37  THR B CG2 
2456 N  N   . ALA B 38  ? 0.1795 0.2064 0.2127 -0.0304 -0.0822 0.0482  38  ALA B N   
2457 C  CA  . ALA B 38  ? 0.2008 0.2014 0.2334 -0.0498 -0.0958 0.0359  38  ALA B CA  
2458 C  C   . ALA B 38  ? 0.2308 0.1996 0.2260 -0.0166 -0.0423 0.0275  38  ALA B C   
2459 O  O   . ALA B 38  ? 0.3217 0.2282 0.2131 -0.0658 -0.0505 0.0143  38  ALA B O   
2460 C  CB  . ALA B 38  ? 0.2057 0.1764 0.2515 -0.0489 -0.0245 0.0625  38  ALA B CB  
2461 N  N   . LYS B 39  ? 0.1779 0.2275 0.1980 -0.0197 -0.0342 0.0432  39  LYS B N   
2462 C  CA  . LYS B 39  ? 0.1897 0.2380 0.2231 -0.0182 -0.0568 0.0608  39  LYS B CA  
2463 C  C   . LYS B 39  ? 0.2506 0.2387 0.2057 -0.0186 -0.0487 0.0472  39  LYS B C   
2464 O  O   . LYS B 39  ? 0.2023 0.2140 0.2064 -0.0344 -0.0553 0.0498  39  LYS B O   
2465 C  CB  . LYS B 39  ? 0.2348 0.2703 0.3086 0.0103  0.0252  0.0641  39  LYS B CB  
2466 C  CG  . LYS B 39  ? 0.3364 0.4290 0.3039 0.0498  -0.0592 0.0020  39  LYS B CG  
2467 C  CD  . LYS B 39  ? 0.2696 0.3237 0.3161 -0.0344 0.0172  0.1172  39  LYS B CD  
2468 C  CE  . LYS B 39  ? 0.3028 0.4539 0.2424 -0.1107 -0.0428 0.0895  39  LYS B CE  
2469 N  NZ  . LYS B 39  ? 0.2969 0.4966 0.2709 -0.1559 -0.0156 0.0581  39  LYS B NZ  
2470 N  N   . TYR B 40  ? 0.1911 0.2815 0.2179 -0.0478 -0.0436 0.0142  40  TYR B N   
2471 C  CA  . TYR B 40  ? 0.2301 0.2490 0.1861 0.0178  -0.0513 0.0120  40  TYR B CA  
2472 C  C   . TYR B 40  ? 0.1817 0.2256 0.1793 0.0076  -0.0298 -0.0008 40  TYR B C   
2473 O  O   . TYR B 40  ? 0.2045 0.3212 0.2123 0.0028  -0.0769 0.0533  40  TYR B O   
2474 C  CB  . TYR B 40  ? 0.2840 0.3664 0.2131 -0.0728 -0.0863 -0.0384 40  TYR B CB  
2475 C  CG  . TYR B 40  ? 0.2451 0.3440 0.2459 -0.0375 -0.0756 -0.0288 40  TYR B CG  
2476 C  CD1 . TYR B 40  ? 0.2763 0.2696 0.2700 -0.0472 -0.0186 -0.0808 40  TYR B CD1 
2477 C  CD2 . TYR B 40  ? 0.3300 0.5799 0.2705 -0.0939 -0.1571 -0.0152 40  TYR B CD2 
2478 C  CE1 . TYR B 40  ? 0.3152 0.4235 0.2750 -0.0212 -0.1014 0.0872  40  TYR B CE1 
2479 C  CE2 . TYR B 40  ? 0.4162 0.5397 0.3204 -0.0122 -0.1412 0.1097  40  TYR B CE2 
2480 C  CZ  . TYR B 40  ? 0.2874 0.5705 0.2400 0.0995  -0.0636 0.0617  40  TYR B CZ  
2481 O  OH  . TYR B 40  ? 0.4814 0.5885 0.2352 -0.0305 -0.0529 0.0474  40  TYR B OH  
2482 N  N   . ASP B 41  ? 0.2878 0.2445 0.1748 -0.0298 -0.0355 0.0680  41  ASP B N   
2483 C  CA  . ASP B 41  ? 0.1919 0.2328 0.2906 -0.0175 -0.0461 0.0300  41  ASP B CA  
2484 C  C   . ASP B 41  ? 0.2513 0.3768 0.2919 -0.0104 -0.0162 0.0425  41  ASP B C   
2485 O  O   . ASP B 41  ? 0.2425 0.2946 0.2488 -0.0324 -0.0098 -0.0017 41  ASP B O   
2486 C  CB  . ASP B 41  ? 0.4819 0.2851 0.2867 0.0310  0.0905  -0.0080 41  ASP B CB  
2487 C  CG  . ASP B 41  ? 0.4872 0.3215 0.4659 0.0553  -0.0326 -0.0082 41  ASP B CG  
2488 O  OD1 . ASP B 41  ? 0.3409 0.3811 0.4388 0.0769  0.0485  0.0465  41  ASP B OD1 
2489 O  OD2 . ASP B 41  ? 0.4305 0.4670 0.3907 -0.0758 0.1272  -0.0489 41  ASP B OD2 
2490 N  N   . PRO B 42  ? 0.2800 0.3679 0.2513 -0.0304 -0.0210 0.0307  42  PRO B N   
2491 C  CA  . PRO B 42  ? 0.2985 0.4566 0.2585 -0.0719 -0.0227 0.0684  42  PRO B CA  
2492 C  C   . PRO B 42  ? 0.3459 0.4506 0.3129 -0.0724 0.0049  0.0339  42  PRO B C   
2493 O  O   . PRO B 42  ? 0.4052 0.5031 0.3034 -0.0666 0.0388  0.1362  42  PRO B O   
2494 C  CB  . PRO B 42  ? 0.3226 0.4848 0.2755 -0.0697 -0.0186 0.0403  42  PRO B CB  
2495 C  CG  . PRO B 42  ? 0.2635 0.5117 0.2811 -0.0742 -0.0974 0.0984  42  PRO B CG  
2496 C  CD  . PRO B 42  ? 0.3041 0.4117 0.3239 -0.0526 -0.1720 0.1339  42  PRO B CD  
2497 N  N   . SER B 43  ? 0.2698 0.3377 0.3010 -0.0361 -0.1053 0.0505  43  SER B N   
2498 C  CA  . SER B 43  ? 0.3463 0.2890 0.5037 0.0307  -0.0798 0.0846  43  SER B CA  
2499 C  C   . SER B 43  ? 0.4445 0.3147 0.4614 -0.0518 -0.0819 0.0711  43  SER B C   
2500 O  O   . SER B 43  ? 0.5794 0.3619 0.6596 -0.0785 0.1321  0.0384  43  SER B O   
2501 C  CB  . SER B 43  ? 0.5443 0.4246 0.5011 0.0751  -0.0166 0.0516  43  SER B CB  
2502 O  OG  . SER B 43  ? 0.2163 0.4842 0.4715 0.0768  -0.0582 0.0093  43  SER B OG  
2503 N  N   . LEU B 44  ? 0.2642 0.3707 0.3671 -0.0606 0.0141  0.0619  44  LEU B N   
2504 C  CA  . LEU B 44  ? 0.2971 0.4036 0.4362 -0.0186 0.0239  -0.0127 44  LEU B CA  
2505 C  C   . LEU B 44  ? 0.4588 0.5295 0.3973 -0.1529 0.0939  -0.1591 44  LEU B C   
2506 O  O   . LEU B 44  ? 0.3926 0.5092 0.3204 -0.0822 -0.0006 -0.0964 44  LEU B O   
2507 C  CB  . LEU B 44  ? 0.2775 0.4546 0.3000 -0.0674 -0.0386 -0.0285 44  LEU B CB  
2508 C  CG  . LEU B 44  ? 0.2592 0.3282 0.2741 -0.0816 -0.0476 0.0260  44  LEU B CG  
2509 C  CD1 . LEU B 44  ? 0.3546 0.3616 0.1798 -0.0052 -0.0668 0.0120  44  LEU B CD1 
2510 C  CD2 . LEU B 44  ? 0.3228 0.2667 0.3923 -0.1143 -0.0732 0.0366  44  LEU B CD2 
2511 N  N   . LYS B 45  ? 0.3248 0.4284 0.5009 -0.0767 0.0943  -0.0888 45  LYS B N   
2512 C  CA  . LYS B 45  ? 0.4029 0.3350 0.4783 0.0351  0.1213  -0.0188 45  LYS B CA  
2513 C  C   . LYS B 45  ? 0.3113 0.3677 0.2858 -0.1059 0.0557  0.0262  45  LYS B C   
2514 O  O   . LYS B 45  ? 0.4514 0.5598 0.1922 0.0768  0.0021  -0.0062 45  LYS B O   
2515 C  CB  . LYS B 45  ? 0.2684 0.3314 0.2775 -0.0006 -0.1044 0.1875  45  LYS B CB  
2516 C  CG  . LYS B 45  ? 0.6194 0.7215 0.5995 0.0217  0.0384  -0.0966 45  LYS B CG  
2517 C  CD  . LYS B 45  ? 0.5310 0.6090 0.3935 0.1292  0.0542  -0.0197 45  LYS B CD  
2518 N  N   . PRO B 46  ? 0.2547 0.4198 0.2281 -0.0162 0.0292  -0.0192 46  PRO B N   
2519 C  CA  . PRO B 46  ? 0.3068 0.2854 0.2378 -0.0427 0.0195  -0.0581 46  PRO B CA  
2520 C  C   . PRO B 46  ? 0.3325 0.2687 0.1604 -0.0296 -0.0035 -0.0110 46  PRO B C   
2521 O  O   . PRO B 46  ? 0.2980 0.3050 0.1247 -0.0298 0.0397  -0.0377 46  PRO B O   
2522 C  CB  . PRO B 46  ? 0.3393 0.3325 0.2100 0.0097  0.0255  -0.0653 46  PRO B CB  
2523 C  CG  . PRO B 46  ? 0.4000 0.3874 0.2330 -0.0087 -0.0296 0.0910  46  PRO B CG  
2524 C  CD  . PRO B 46  ? 0.3404 0.4225 0.3055 0.0032  -0.0091 0.0740  46  PRO B CD  
2525 N  N   . LEU B 47  ? 0.3149 0.2637 0.1969 -0.0807 -0.0096 -0.0122 47  LEU B N   
2526 C  CA  . LEU B 47  ? 0.3517 0.3025 0.1401 -0.0778 0.0126  -0.0747 47  LEU B CA  
2527 C  C   . LEU B 47  ? 0.3542 0.2294 0.2301 -0.0414 0.0834  -0.0593 47  LEU B C   
2528 O  O   . LEU B 47  ? 0.4011 0.3321 0.2115 -0.1335 0.1008  -0.1137 47  LEU B O   
2529 C  CB  . LEU B 47  ? 0.4616 0.3328 0.2829 -0.0461 0.0266  -0.0328 47  LEU B CB  
2530 C  CG  . LEU B 47  ? 0.3664 0.3030 0.2389 0.0192  0.0815  0.0041  47  LEU B CG  
2531 C  CD1 . LEU B 47  ? 0.2955 0.3860 0.2563 0.0144  0.0775  -0.0732 47  LEU B CD1 
2532 C  CD2 . LEU B 47  ? 0.4329 0.2391 0.2425 0.0326  0.1356  0.0176  47  LEU B CD2 
2533 N  N   . SER B 48  ? 0.2240 0.1978 0.1419 -0.0454 0.0038  -0.0055 48  SER B N   
2534 C  CA  . SER B 48  ? 0.2330 0.2045 0.1402 -0.0271 0.0023  -0.0241 48  SER B CA  
2535 C  C   . SER B 48  ? 0.2364 0.1890 0.1594 0.0038  -0.0147 -0.0241 48  SER B C   
2536 O  O   . SER B 48  ? 0.2368 0.2018 0.1450 0.0034  -0.0041 -0.0234 48  SER B O   
2537 C  CB  . SER B 48  ? 0.2732 0.2375 0.1623 -0.0076 -0.0114 -0.0142 48  SER B CB  
2538 O  OG  . SER B 48  ? 0.2852 0.2743 0.1847 -0.0185 0.0057  0.0055  48  SER B OG  
2539 N  N   . VAL B 49  ? 0.2157 0.1775 0.1605 -0.0143 -0.0094 -0.0500 49  VAL B N   
2540 C  CA  . VAL B 49  ? 0.2037 0.2276 0.1894 0.0109  -0.0219 -0.0533 49  VAL B CA  
2541 C  C   . VAL B 49  ? 0.2639 0.2045 0.1541 0.0043  0.0203  -0.0456 49  VAL B C   
2542 O  O   . VAL B 49  ? 0.3253 0.3089 0.2123 0.0737  0.0417  -0.1023 49  VAL B O   
2543 C  CB  . VAL B 49  ? 0.2939 0.2536 0.2239 0.0485  -0.0403 -0.0527 49  VAL B CB  
2544 C  CG1 . VAL B 49  ? 0.3506 0.3370 0.3018 0.0186  -0.1155 -0.0225 49  VAL B CG1 
2545 C  CG2 . VAL B 49  ? 0.3583 0.2569 0.1773 -0.0379 -0.0628 -0.0471 49  VAL B CG2 
2546 N  N   . SER B 50  ? 0.2513 0.2102 0.1960 -0.0342 0.0087  -0.0320 50  SER B N   
2547 C  CA  . SER B 50  ? 0.2554 0.2239 0.1705 0.0170  0.0388  -0.0220 50  SER B CA  
2548 C  C   . SER B 50  ? 0.1985 0.2116 0.1834 -0.0028 0.0379  -0.0070 50  SER B C   
2549 O  O   . SER B 50  ? 0.2454 0.1971 0.2062 -0.0149 0.0100  -0.0263 50  SER B O   
2550 C  CB  . SER B 50  ? 0.3323 0.2454 0.1784 0.0318  -0.0189 -0.0639 50  SER B CB  
2551 O  OG  . SER B 50  ? 0.2944 0.3339 0.2346 0.0076  0.0093  0.0003  50  SER B OG  
2552 N  N   . TYR B 51  ? 0.2253 0.2276 0.1796 0.0214  0.0233  0.0159  51  TYR B N   
2553 C  CA  . TYR B 51  ? 0.1870 0.1908 0.2081 -0.0041 0.0124  -0.0293 51  TYR B CA  
2554 C  C   . TYR B 51  ? 0.2509 0.2030 0.1777 -0.0370 0.0127  0.0019  51  TYR B C   
2555 O  O   . TYR B 51  ? 0.2048 0.2380 0.2160 -0.0076 0.0392  0.0043  51  TYR B O   
2556 C  CB  . TYR B 51  ? 0.1938 0.2028 0.2023 0.0082  0.0606  -0.0126 51  TYR B CB  
2557 C  CG  . TYR B 51  ? 0.1565 0.1808 0.1948 0.0038  0.0229  -0.0241 51  TYR B CG  
2558 C  CD1 . TYR B 51  ? 0.1983 0.1630 0.1527 -0.0074 0.0359  -0.0190 51  TYR B CD1 
2559 C  CD2 . TYR B 51  ? 0.1807 0.1698 0.1635 0.0008  0.0209  -0.0054 51  TYR B CD2 
2560 C  CE1 . TYR B 51  ? 0.1703 0.1382 0.1389 -0.0135 0.0250  -0.0054 51  TYR B CE1 
2561 C  CE2 . TYR B 51  ? 0.1826 0.1461 0.1806 -0.0066 0.0256  -0.0408 51  TYR B CE2 
2562 C  CZ  . TYR B 51  ? 0.1515 0.1407 0.1220 -0.0080 0.0034  -0.0175 51  TYR B CZ  
2563 O  OH  . TYR B 51  ? 0.1495 0.1445 0.1464 0.0032  0.0286  -0.0082 51  TYR B OH  
2564 N  N   . ASP B 52  ? 0.3100 0.2436 0.1648 -0.0454 0.0657  -0.0046 52  ASP B N   
2565 C  CA  . ASP B 52  ? 0.3124 0.3145 0.1523 -0.0593 0.0745  0.0166  52  ASP B CA  
2566 C  C   . ASP B 52  ? 0.3151 0.2811 0.2469 -0.0114 0.0425  0.0445  52  ASP B C   
2567 O  O   . ASP B 52  ? 0.3023 0.3382 0.3720 -0.0296 0.0832  -0.0200 52  ASP B O   
2568 C  CB  . ASP B 52  ? 0.3129 0.3113 0.1843 -0.0546 0.0297  0.0646  52  ASP B CB  
2569 C  CG  . ASP B 52  ? 0.5092 0.4496 0.3102 0.0469  0.0049  0.1843  52  ASP B CG  
2570 O  OD1 . ASP B 52  ? 0.6597 0.7778 0.2847 0.1039  0.0873  0.0627  52  ASP B OD1 
2571 O  OD2 . ASP B 52  ? 1.0683 0.5153 0.6317 -0.2842 0.1525  0.1110  52  ASP B OD2 
2572 N  N   . GLN B 53  ? 0.3639 0.2608 0.1797 -0.0450 0.0359  0.0086  53  GLN B N   
2573 C  CA  . GLN B 53  ? 0.3986 0.2748 0.2148 -0.0355 0.0463  -0.0186 53  GLN B CA  
2574 C  C   . GLN B 53  ? 0.3537 0.2430 0.1987 -0.0658 0.0250  0.0121  53  GLN B C   
2575 O  O   . GLN B 53  ? 0.2845 0.2319 0.2169 -0.0588 0.0648  -0.0065 53  GLN B O   
2576 C  CB  . GLN B 53  ? 0.5285 0.2637 0.2702 0.0082  0.1553  0.0384  53  GLN B CB  
2577 C  CG  . GLN B 53  ? 0.6550 0.4338 0.2763 -0.0432 -0.0346 0.0714  53  GLN B CG  
2578 C  CD  . GLN B 53  ? 0.7663 0.7307 0.4650 -0.0617 0.1882  -0.1985 53  GLN B CD  
2579 O  OE1 . GLN B 53  ? 0.9392 0.8773 0.4944 -0.0562 0.0841  -0.0860 53  GLN B OE1 
2580 N  NE2 . GLN B 53  ? 1.2148 1.0825 0.6815 -0.2966 0.2211  -0.0551 53  GLN B NE2 
2581 N  N   . ALA B 54  ? 0.3188 0.2149 0.1845 0.0068  0.0549  -0.0122 54  ALA B N   
2582 C  CA  . ALA B 54  ? 0.2043 0.1775 0.1544 0.0017  -0.0013 0.0015  54  ALA B CA  
2583 C  C   . ALA B 54  ? 0.1887 0.2463 0.2237 0.0093  0.0153  -0.0089 54  ALA B C   
2584 O  O   . ALA B 54  ? 0.2985 0.3000 0.2615 0.0942  0.0509  -0.0147 54  ALA B O   
2585 C  CB  . ALA B 54  ? 0.2260 0.1820 0.2569 -0.0076 -0.0008 0.0024  54  ALA B CB  
2586 N  N   . THR B 55  ? 0.1938 0.1944 0.1759 -0.0447 0.0147  0.0070  55  THR B N   
2587 C  CA  . THR B 55  ? 0.1951 0.2210 0.2104 -0.0480 0.0296  0.0108  55  THR B CA  
2588 C  C   . THR B 55  ? 0.1550 0.1668 0.2050 -0.0160 0.0006  -0.0085 55  THR B C   
2589 O  O   . THR B 55  ? 0.1671 0.1568 0.1806 -0.0335 0.0172  0.0012  55  THR B O   
2590 C  CB  . THR B 55  ? 0.2782 0.2576 0.3361 -0.0727 -0.0463 0.0251  55  THR B CB  
2591 O  OG1 . THR B 55  ? 0.3657 0.3856 0.5392 -0.0821 0.1132  0.1071  55  THR B OG1 
2592 C  CG2 . THR B 55  ? 0.2702 0.2809 0.3016 -0.0872 -0.0851 0.0610  55  THR B CG2 
2593 N  N   . SER B 56  ? 0.1456 0.1480 0.1966 -0.0162 0.0454  0.0296  56  SER B N   
2594 C  CA  . SER B 56  ? 0.1481 0.1513 0.1527 -0.0006 0.0295  0.0051  56  SER B CA  
2595 C  C   . SER B 56  ? 0.1874 0.1701 0.1845 -0.0114 0.0103  0.0252  56  SER B C   
2596 O  O   . SER B 56  ? 0.1723 0.1845 0.2469 -0.0155 0.0146  0.0291  56  SER B O   
2597 C  CB  . SER B 56  ? 0.1472 0.1623 0.2420 0.0160  0.0203  -0.0283 56  SER B CB  
2598 O  OG  . SER B 56  ? 0.1447 0.1452 0.2096 -0.0098 0.0241  -0.0060 56  SER B OG  
2599 N  N   . LEU B 57  ? 0.1344 0.1474 0.1755 -0.0222 -0.0307 0.0296  57  LEU B N   
2600 C  CA  . LEU B 57  ? 0.2353 0.2016 0.2157 -0.0318 -0.0715 -0.0073 57  LEU B CA  
2601 C  C   . LEU B 57  ? 0.1366 0.2021 0.2034 -0.0223 -0.0276 0.0285  57  LEU B C   
2602 O  O   . LEU B 57  ? 0.1427 0.1790 0.2492 -0.0080 -0.0203 -0.0023 57  LEU B O   
2603 C  CB  . LEU B 57  ? 0.2402 0.2163 0.2917 -0.0392 -0.0303 0.0088  57  LEU B CB  
2604 C  CG  . LEU B 57  ? 0.2495 0.2518 0.3084 0.0052  -0.0767 0.0093  57  LEU B CG  
2605 C  CD1 . LEU B 57  ? 0.2944 0.1784 0.4074 -0.0017 -0.0522 -0.0471 57  LEU B CD1 
2606 C  CD2 . LEU B 57  ? 0.4851 0.2574 0.4984 0.0274  0.0043  0.1475  57  LEU B CD2 
2607 N  N   . ARG B 58  ? 0.1630 0.1633 0.1915 -0.0065 -0.0225 0.0198  58  ARG B N   
2608 C  CA  . ARG B 58  ? 0.1653 0.1436 0.1730 -0.0520 -0.0017 0.0175  58  ARG B CA  
2609 C  C   . ARG B 58  ? 0.1429 0.1384 0.1823 -0.0266 -0.0260 0.0076  58  ARG B C   
2610 O  O   . ARG B 58  ? 0.1437 0.1486 0.1975 -0.0223 -0.0412 0.0120  58  ARG B O   
2611 C  CB  . ARG B 58  ? 0.1960 0.2237 0.1899 -0.0410 -0.0238 -0.0076 58  ARG B CB  
2612 C  CG  . ARG B 58  ? 0.2940 0.3172 0.1335 -0.0346 0.0144  -0.0119 58  ARG B CG  
2613 C  CD  . ARG B 58  ? 0.3407 0.3655 0.3657 0.0829  0.1238  -0.0861 58  ARG B CD  
2614 N  NE  . ARG B 58  ? 0.2971 0.2899 0.1944 0.0008  -0.0041 -0.0577 58  ARG B NE  
2615 C  CZ  . ARG B 58  ? 0.2416 0.3046 0.1906 -0.0780 0.0255  -0.0626 58  ARG B CZ  
2616 N  NH1 . ARG B 58  ? 0.2518 0.2691 0.2617 -0.0070 -0.0359 -0.0781 58  ARG B NH1 
2617 N  NH2 . ARG B 58  ? 0.2820 0.2648 0.1784 -0.0381 -0.0260 -0.0264 58  ARG B NH2 
2618 N  N   . ILE B 59  ? 0.1405 0.1396 0.1574 -0.0068 -0.0252 0.0082  59  ILE B N   
2619 C  CA  . ILE B 59  ? 0.1444 0.1439 0.1517 -0.0027 0.0020  0.0006  59  ILE B CA  
2620 C  C   . ILE B 59  ? 0.1032 0.1371 0.1355 -0.0175 -0.0154 -0.0099 59  ILE B C   
2621 O  O   . ILE B 59  ? 0.1247 0.1556 0.1529 -0.0313 -0.0322 0.0153  59  ILE B O   
2622 C  CB  . ILE B 59  ? 0.1301 0.1615 0.1594 0.0038  -0.0024 -0.0120 59  ILE B CB  
2623 C  CG1 . ILE B 59  ? 0.1304 0.1750 0.1705 -0.0230 -0.0068 -0.0379 59  ILE B CG1 
2624 C  CG2 . ILE B 59  ? 0.1134 0.1693 0.1750 -0.0188 -0.0120 0.0419  59  ILE B CG2 
2625 C  CD1 . ILE B 59  ? 0.1411 0.1398 0.1829 -0.0103 -0.0153 -0.0197 59  ILE B CD1 
2626 N  N   . LEU B 60  ? 0.1299 0.1545 0.1685 -0.0024 0.0153  -0.0115 60  LEU B N   
2627 C  CA  . LEU B 60  ? 0.1114 0.1242 0.1517 -0.0078 0.0098  0.0000  60  LEU B CA  
2628 C  C   . LEU B 60  ? 0.1463 0.1272 0.1545 -0.0078 -0.0137 -0.0127 60  LEU B C   
2629 O  O   . LEU B 60  ? 0.1147 0.1577 0.1455 -0.0284 -0.0083 0.0057  60  LEU B O   
2630 C  CB  . LEU B 60  ? 0.1860 0.1168 0.1624 -0.0065 0.0194  -0.0066 60  LEU B CB  
2631 C  CG  . LEU B 60  ? 0.1448 0.1459 0.1621 0.0074  0.0049  -0.0044 60  LEU B CG  
2632 C  CD1 . LEU B 60  ? 0.2007 0.1637 0.1669 -0.0103 -0.0261 -0.0397 60  LEU B CD1 
2633 C  CD2 . LEU B 60  ? 0.1705 0.1692 0.2156 0.0370  -0.0159 -0.0187 60  LEU B CD2 
2634 N  N   . ASN B 61  ? 0.1220 0.1441 0.1398 0.0043  -0.0274 -0.0114 61  ASN B N   
2635 C  CA  . ASN B 61  ? 0.1377 0.1439 0.1353 0.0192  -0.0074 -0.0049 61  ASN B CA  
2636 C  C   . ASN B 61  ? 0.1475 0.1809 0.1517 0.0017  -0.0175 -0.0049 61  ASN B C   
2637 O  O   . ASN B 61  ? 0.1885 0.1613 0.1680 -0.0097 -0.0138 -0.0434 61  ASN B O   
2638 C  CB  . ASN B 61  ? 0.1568 0.1651 0.1874 0.0065  -0.0436 -0.0065 61  ASN B CB  
2639 C  CG  . ASN B 61  ? 0.1389 0.1404 0.1427 0.0126  -0.0234 -0.0141 61  ASN B CG  
2640 O  OD1 . ASN B 61  ? 0.1380 0.1723 0.1657 -0.0007 -0.0243 -0.0297 61  ASN B OD1 
2641 N  ND2 . ASN B 61  ? 0.1437 0.1317 0.1331 0.0059  -0.0401 -0.0157 61  ASN B ND2 
2642 N  N   . ASN B 62  ? 0.1466 0.1565 0.1746 0.0008  -0.0296 -0.0579 62  ASN B N   
2643 C  CA  . ASN B 62  ? 0.1868 0.1797 0.1875 -0.0063 -0.0159 -0.0568 62  ASN B CA  
2644 C  C   . ASN B 62  ? 0.2037 0.1856 0.1835 0.0204  -0.0222 -0.0494 62  ASN B C   
2645 O  O   . ASN B 62  ? 0.2547 0.2305 0.2355 0.0103  0.0383  -0.0839 62  ASN B O   
2646 C  CB  . ASN B 62  ? 0.1689 0.1683 0.2827 0.0233  -0.0173 -0.0218 62  ASN B CB  
2647 C  CG  . ASN B 62  ? 0.1394 0.1912 0.1926 -0.0024 -0.0054 0.0093  62  ASN B CG  
2648 O  OD1 . ASN B 62  ? 0.1744 0.1743 0.1960 0.0082  0.0264  -0.0062 62  ASN B OD1 
2649 N  ND2 . ASN B 62  ? 0.2217 0.2476 0.2486 -0.0062 -0.0296 0.0263  62  ASN B ND2 
2650 N  N   . GLY B 63  ? 0.1741 0.1666 0.1475 -0.0027 -0.0164 -0.0148 63  GLY B N   
2651 C  CA  . GLY B 63  ? 0.1583 0.1737 0.1280 -0.0275 -0.0094 -0.0250 63  GLY B CA  
2652 C  C   . GLY B 63  ? 0.1471 0.1753 0.1532 -0.0046 -0.0210 0.0010  63  GLY B C   
2653 O  O   . GLY B 63  ? 0.1691 0.1817 0.1520 0.0017  -0.0175 -0.0148 63  GLY B O   
2654 N  N   . HIS B 64  ? 0.1489 0.1504 0.1378 -0.0020 -0.0266 -0.0189 64  HIS B N   
2655 C  CA  . HIS B 64  ? 0.1405 0.1958 0.1423 0.0066  -0.0157 -0.0287 64  HIS B CA  
2656 C  C   . HIS B 64  ? 0.1316 0.1477 0.1324 -0.0051 0.0159  -0.0094 64  HIS B C   
2657 O  O   . HIS B 64  ? 0.1771 0.1784 0.1788 -0.0318 0.0062  -0.0249 64  HIS B O   
2658 C  CB  . HIS B 64  ? 0.1571 0.1847 0.1626 0.0161  0.0093  -0.0136 64  HIS B CB  
2659 C  CG  . HIS B 64  ? 0.1659 0.2077 0.2086 0.0324  -0.0126 -0.0294 64  HIS B CG  
2660 N  ND1 . HIS B 64  ? 0.1953 0.2621 0.2032 0.0511  -0.0267 -0.0077 64  HIS B ND1 
2661 C  CD2 . HIS B 64  ? 0.1747 0.2293 0.2050 0.0092  -0.0377 -0.0115 64  HIS B CD2 
2662 C  CE1 . HIS B 64  ? 0.2264 0.2549 0.2111 0.0581  -0.0461 -0.0324 64  HIS B CE1 
2663 N  NE2 . HIS B 64  ? 0.2565 0.2887 0.2055 0.0223  -0.0203 -0.0520 64  HIS B NE2 
2664 N  N   . ALA B 65  ? 0.1629 0.1394 0.1243 -0.0186 -0.0043 0.0000  65  ALA B N   
2665 C  CA  . ALA B 65  ? 0.1450 0.1698 0.1414 -0.0148 -0.0230 -0.0179 65  ALA B CA  
2666 C  C   . ALA B 65  ? 0.1158 0.1265 0.1339 -0.0070 -0.0266 -0.0197 65  ALA B C   
2667 O  O   . ALA B 65  ? 0.1561 0.1595 0.1435 -0.0149 -0.0152 -0.0344 65  ALA B O   
2668 C  CB  . ALA B 65  ? 0.1488 0.1989 0.1258 -0.0223 -0.0133 0.0013  65  ALA B CB  
2669 N  N   . PHE B 66  ? 0.1280 0.1475 0.1479 -0.0023 -0.0043 0.0177  66  PHE B N   
2670 C  CA  . PHE B 66  ? 0.1186 0.1527 0.1391 -0.0192 -0.0480 -0.0021 66  PHE B CA  
2671 C  C   . PHE B 66  ? 0.1313 0.1443 0.1292 0.0131  -0.0125 0.0031  66  PHE B C   
2672 O  O   . PHE B 66  ? 0.1445 0.1568 0.1755 0.0027  -0.0450 -0.0157 66  PHE B O   
2673 C  CB  . PHE B 66  ? 0.1547 0.1887 0.1493 0.0147  -0.0146 -0.0068 66  PHE B CB  
2674 C  CG  . PHE B 66  ? 0.1057 0.1380 0.1633 0.0172  -0.0322 0.0054  66  PHE B CG  
2675 C  CD1 . PHE B 66  ? 0.0935 0.1904 0.1752 0.0239  -0.0048 -0.0243 66  PHE B CD1 
2676 C  CD2 . PHE B 66  ? 0.1215 0.1571 0.1592 0.0165  -0.0077 0.0132  66  PHE B CD2 
2677 C  CE1 . PHE B 66  ? 0.1281 0.1570 0.1782 0.0166  -0.0096 -0.0021 66  PHE B CE1 
2678 C  CE2 . PHE B 66  ? 0.1380 0.1428 0.1635 0.0086  0.0170  0.0037  66  PHE B CE2 
2679 C  CZ  . PHE B 66  ? 0.1118 0.1438 0.1638 0.0240  0.0076  0.0038  66  PHE B CZ  
2680 N  N   A ASN B 67  ? 0.1226 0.1463 0.0996 -0.0054 -0.0142 0.0031  67  ASN B N   
2681 N  N   B ASN B 67  ? 0.1071 0.1595 0.1608 -0.0160 -0.0105 0.0142  67  ASN B N   
2682 C  CA  A ASN B 67  ? 0.1152 0.1750 0.1495 -0.0048 -0.0281 0.0353  67  ASN B CA  
2683 C  CA  B ASN B 67  ? 0.1335 0.1721 0.1773 -0.0086 -0.0239 0.0331  67  ASN B CA  
2684 C  C   A ASN B 67  ? 0.1326 0.1377 0.1231 -0.0142 -0.0174 0.0051  67  ASN B C   
2685 C  C   B ASN B 67  ? 0.1267 0.1268 0.1265 -0.0130 -0.0344 0.0013  67  ASN B C   
2686 O  O   A ASN B 67  ? 0.1222 0.1520 0.1716 -0.0114 -0.0322 -0.0074 67  ASN B O   
2687 O  O   B ASN B 67  ? 0.1114 0.1520 0.1786 -0.0102 -0.0509 0.0096  67  ASN B O   
2688 C  CB  A ASN B 67  ? 0.1010 0.2469 0.1344 0.0425  -0.0293 0.0361  67  ASN B CB  
2689 C  CB  B ASN B 67  ? 0.1527 0.2012 0.2107 0.0076  0.0287  0.0342  67  ASN B CB  
2690 C  CG  A ASN B 67  ? 0.2337 0.2524 0.1824 -0.0447 0.0366  -0.0286 67  ASN B CG  
2691 C  CG  B ASN B 67  ? 0.2073 0.1939 0.2585 0.0240  0.0020  0.0297  67  ASN B CG  
2692 O  OD1 A ASN B 67  ? 0.3456 0.3142 0.2048 0.0408  -0.0083 -0.0804 67  ASN B OD1 
2693 O  OD1 B ASN B 67  ? 0.2150 0.1732 0.2330 -0.0008 -0.0110 -0.0026 67  ASN B OD1 
2694 N  ND2 A ASN B 67  ? 0.1455 0.1992 0.1454 0.0049  0.0595  -0.0282 67  ASN B ND2 
2695 N  ND2 B ASN B 67  ? 0.2849 0.1826 0.2691 0.0825  0.0187  0.0034  67  ASN B ND2 
2696 N  N   . VAL B 68  ? 0.1215 0.1229 0.1344 -0.0138 -0.0225 0.0165  68  VAL B N   
2697 C  CA  . VAL B 68  ? 0.1197 0.1477 0.1639 -0.0153 -0.0244 0.0381  68  VAL B CA  
2698 C  C   . VAL B 68  ? 0.1254 0.1500 0.1423 -0.0098 -0.0010 0.0348  68  VAL B C   
2699 O  O   . VAL B 68  ? 0.1222 0.1432 0.1734 -0.0147 -0.0227 0.0342  68  VAL B O   
2700 C  CB  . VAL B 68  ? 0.1483 0.1477 0.1820 0.0028  0.0141  0.0256  68  VAL B CB  
2701 C  CG1 . VAL B 68  ? 0.1445 0.2152 0.1815 -0.0160 -0.0219 0.0520  68  VAL B CG1 
2702 C  CG2 . VAL B 68  ? 0.1601 0.1554 0.1541 0.0353  -0.0181 0.0071  68  VAL B CG2 
2703 N  N   . GLU B 69  ? 0.1533 0.1410 0.2102 -0.0161 -0.0272 0.0232  69  GLU B N   
2704 C  CA  . GLU B 69  ? 0.1304 0.1378 0.1639 -0.0034 -0.0141 -0.0131 69  GLU B CA  
2705 C  C   . GLU B 69  ? 0.1479 0.1357 0.2014 -0.0168 0.0120  0.0269  69  GLU B C   
2706 O  O   . GLU B 69  ? 0.1389 0.1719 0.2440 -0.0181 -0.0059 0.0361  69  GLU B O   
2707 C  CB  . GLU B 69  ? 0.1888 0.1726 0.1653 0.0024  -0.0046 -0.0200 69  GLU B CB  
2708 C  CG  . GLU B 69  ? 0.2533 0.2994 0.1849 0.0184  -0.0031 -0.0098 69  GLU B CG  
2709 C  CD  . GLU B 69  ? 0.2619 0.2434 0.1978 -0.0474 0.0238  -0.0244 69  GLU B CD  
2710 O  OE1 . GLU B 69  ? 0.2825 0.2924 0.2174 -0.0741 -0.0168 -0.0328 69  GLU B OE1 
2711 O  OE2 . GLU B 69  ? 0.3370 0.2475 0.1728 -0.0701 0.0252  -0.0211 69  GLU B OE2 
2712 N  N   . PHE B 70  ? 0.1543 0.1392 0.1435 -0.0157 -0.0212 0.0020  70  PHE B N   
2713 C  CA  . PHE B 70  ? 0.1416 0.1536 0.1538 -0.0148 0.0071  0.0099  70  PHE B CA  
2714 C  C   . PHE B 70  ? 0.1590 0.1653 0.1825 0.0143  0.0194  0.0188  70  PHE B C   
2715 O  O   . PHE B 70  ? 0.1705 0.1531 0.1844 -0.0218 -0.0034 0.0031  70  PHE B O   
2716 C  CB  . PHE B 70  ? 0.1486 0.1147 0.1800 -0.0239 -0.0091 0.0146  70  PHE B CB  
2717 C  CG  . PHE B 70  ? 0.1438 0.1374 0.1362 -0.0137 0.0077  0.0093  70  PHE B CG  
2718 C  CD1 . PHE B 70  ? 0.1376 0.1224 0.1532 -0.0038 -0.0062 0.0162  70  PHE B CD1 
2719 C  CD2 . PHE B 70  ? 0.1305 0.1536 0.1500 -0.0142 0.0041  -0.0051 70  PHE B CD2 
2720 C  CE1 . PHE B 70  ? 0.1714 0.1355 0.1518 -0.0291 -0.0140 -0.0077 70  PHE B CE1 
2721 C  CE2 . PHE B 70  ? 0.1294 0.1316 0.1692 -0.0154 -0.0032 0.0192  70  PHE B CE2 
2722 C  CZ  . PHE B 70  ? 0.1534 0.1356 0.1407 -0.0119 -0.0044 0.0197  70  PHE B CZ  
2723 N  N   . ASP B 71  ? 0.2032 0.1246 0.2337 -0.0313 0.0296  0.0034  71  ASP B N   
2724 C  CA  . ASP B 71  ? 0.1899 0.1421 0.2136 0.0017  0.0220  -0.0019 71  ASP B CA  
2725 C  C   . ASP B 71  ? 0.2188 0.1272 0.1975 -0.0214 -0.0114 -0.0120 71  ASP B C   
2726 O  O   . ASP B 71  ? 0.3251 0.2095 0.2151 -0.0282 0.0137  -0.0144 71  ASP B O   
2727 C  CB  . ASP B 71  ? 0.2544 0.1825 0.3562 -0.0634 0.0496  0.0104  71  ASP B CB  
2728 C  CG  . ASP B 71  ? 0.2946 0.1753 0.4783 -0.0401 0.0751  -0.0678 71  ASP B CG  
2729 O  OD1 . ASP B 71  ? 0.3300 0.1206 0.4016 -0.0496 0.0850  0.0205  71  ASP B OD1 
2730 O  OD2 . ASP B 71  ? 0.4210 0.3120 0.6374 -0.0599 0.1931  0.0153  71  ASP B OD2 
2731 N  N   . ASP B 72  ? 0.2105 0.1247 0.1750 -0.0109 0.0091  0.0126  72  ASP B N   
2732 C  CA  . ASP B 72  ? 0.2113 0.1430 0.1756 0.0181  0.0027  -0.0526 72  ASP B CA  
2733 C  C   . ASP B 72  ? 0.2244 0.1738 0.1980 0.0051  0.0074  -0.0184 72  ASP B C   
2734 O  O   . ASP B 72  ? 0.2615 0.1703 0.2658 0.0141  -0.0364 0.0074  72  ASP B O   
2735 C  CB  . ASP B 72  ? 0.2206 0.1728 0.1899 0.0078  -0.0322 -0.0458 72  ASP B CB  
2736 C  CG  . ASP B 72  ? 0.2118 0.2197 0.1554 -0.0289 -0.0248 0.0038  72  ASP B CG  
2737 O  OD1 . ASP B 72  ? 0.1872 0.2490 0.2195 -0.0432 0.0083  -0.0381 72  ASP B OD1 
2738 O  OD2 . ASP B 72  ? 0.1994 0.1802 0.2251 -0.0241 -0.0232 -0.0049 72  ASP B OD2 
2739 N  N   . SER B 73  ? 0.2883 0.1459 0.2194 -0.0024 -0.0078 -0.0171 73  SER B N   
2740 C  CA  . SER B 73  ? 0.3440 0.1326 0.2463 -0.0264 -0.0410 0.0132  73  SER B CA  
2741 C  C   . SER B 73  ? 0.3630 0.1833 0.2208 0.0230  0.0220  0.0299  73  SER B C   
2742 O  O   . SER B 73  ? 0.2813 0.1626 0.2476 0.0126  0.0408  0.0003  73  SER B O   
2743 C  CB  . SER B 73  ? 0.3851 0.1664 0.3465 -0.0740 -0.0375 -0.0293 73  SER B CB  
2744 O  OG  . SER B 73  ? 0.3212 0.1775 0.3309 -0.0670 -0.0960 0.0278  73  SER B OG  
2745 N  N   . GLN B 74  ? 0.3740 0.1608 0.2709 -0.0017 -0.0315 0.0284  74  GLN B N   
2746 C  CA  . GLN B 74  ? 0.3418 0.1793 0.2524 -0.0159 -0.0357 0.0296  74  GLN B CA  
2747 C  C   . GLN B 74  ? 0.3012 0.2152 0.2318 0.0296  -0.0127 0.0271  74  GLN B C   
2748 O  O   . GLN B 74  ? 0.2752 0.1982 0.2267 -0.0118 0.0597  -0.0153 74  GLN B O   
2749 C  CB  . GLN B 74  ? 0.3774 0.3048 0.1980 -0.0916 -0.0068 -0.0027 74  GLN B CB  
2750 C  CG  . GLN B 74  ? 0.2763 0.2897 0.3255 -0.0697 0.0518  -0.0221 74  GLN B CG  
2751 C  CD  . GLN B 74  ? 0.3240 0.3400 0.3055 -0.1286 0.0610  -0.0507 74  GLN B CD  
2752 O  OE1 . GLN B 74  ? 0.5253 0.5418 0.3919 -0.0952 0.1361  -0.0165 74  GLN B OE1 
2753 N  NE2 . GLN B 74  ? 0.3776 0.4690 0.5715 0.1123  -0.0209 -0.0092 74  GLN B NE2 
2754 N  N   . ASP B 75  ? 0.3350 0.3057 0.2242 0.0261  -0.0623 -0.0406 75  ASP B N   
2755 C  CA  . ASP B 75  ? 0.2707 0.2217 0.2651 0.0209  -0.0144 -0.0326 75  ASP B CA  
2756 C  C   . ASP B 75  ? 0.3341 0.2964 0.2378 0.0447  0.0619  -0.0082 75  ASP B C   
2757 O  O   . ASP B 75  ? 0.4589 0.4011 0.2346 0.0732  0.0038  -0.0553 75  ASP B O   
2758 C  CB  . ASP B 75  ? 0.4183 0.2903 0.3037 0.0769  -0.0205 -0.0251 75  ASP B CB  
2759 C  CG  . ASP B 75  ? 0.3569 0.3858 0.3792 0.0247  -0.0326 0.0397  75  ASP B CG  
2760 O  OD1 . ASP B 75  ? 0.4623 0.3871 0.3580 -0.0509 0.1894  0.0161  75  ASP B OD1 
2761 O  OD2 . ASP B 75  ? 0.5006 0.4720 0.4368 -0.0262 -0.1902 0.0450  75  ASP B OD2 
2762 N  N   . LYS B 76  ? 0.2879 0.2605 0.2876 -0.0684 0.0217  -0.0553 76  LYS B N   
2763 C  CA  . LYS B 76  ? 0.3682 0.2160 0.4040 -0.0035 -0.0463 -0.0136 76  LYS B CA  
2764 C  C   . LYS B 76  ? 0.6326 0.3664 0.5745 -0.2456 -0.0375 0.0535  76  LYS B C   
2765 O  O   . LYS B 76  ? 0.7605 0.7023 0.4666 -0.1362 0.1976  -0.0949 76  LYS B O   
2766 C  CB  . LYS B 76  ? 0.2472 0.2567 0.4725 0.0445  0.0864  -0.0546 76  LYS B CB  
2767 C  CG  . LYS B 76  ? 0.2344 0.3583 0.5561 -0.0370 0.0273  -0.0166 76  LYS B CG  
2768 C  CD  . LYS B 76  ? 0.2849 0.2230 0.5986 -0.0640 -0.1243 -0.0190 76  LYS B CD  
2769 N  N   . ALA B 77  ? 0.2662 0.3138 0.4023 -0.0546 0.1404  0.0131  77  ALA B N   
2770 C  CA  . ALA B 77  ? 0.2100 0.2865 0.2282 -0.0125 -0.0017 -0.0538 77  ALA B CA  
2771 C  C   . ALA B 77  ? 0.2328 0.2197 0.1958 0.0131  0.0329  -0.0196 77  ALA B C   
2772 O  O   . ALA B 77  ? 0.2827 0.3684 0.1893 0.0732  0.0732  0.0406  77  ALA B O   
2773 C  CB  . ALA B 77  ? 0.2151 0.2861 0.2899 0.0315  0.0006  -0.0066 77  ALA B CB  
2774 N  N   . VAL B 78  ? 0.1732 0.1705 0.2061 -0.0296 0.0496  0.0074  78  VAL B N   
2775 C  CA  . VAL B 78  ? 0.1583 0.2073 0.2184 -0.0292 0.0167  -0.0294 78  VAL B CA  
2776 C  C   . VAL B 78  ? 0.1545 0.1929 0.1640 0.0120  0.0107  -0.0520 78  VAL B C   
2777 O  O   . VAL B 78  ? 0.2202 0.1791 0.1717 -0.0125 0.0511  -0.0394 78  VAL B O   
2778 C  CB  . VAL B 78  ? 0.2867 0.2569 0.3176 -0.0176 -0.0028 -0.0074 78  VAL B CB  
2779 C  CG1 . VAL B 78  ? 0.3328 0.2039 0.3093 -0.0326 0.0428  -0.0104 78  VAL B CG1 
2780 C  CG2 . VAL B 78  ? 0.3792 0.2458 0.2565 -0.0666 -0.1037 0.0305  78  VAL B CG2 
2781 N  N   . LEU B 79  ? 0.1633 0.1258 0.1456 -0.0141 0.0063  0.0307  79  LEU B N   
2782 C  CA  . LEU B 79  ? 0.1665 0.1536 0.1391 -0.0003 0.0066  -0.0155 79  LEU B CA  
2783 C  C   . LEU B 79  ? 0.1942 0.1441 0.1280 0.0113  0.0035  -0.0013 79  LEU B C   
2784 O  O   . LEU B 79  ? 0.2318 0.1626 0.1734 0.0266  0.0026  -0.0251 79  LEU B O   
2785 C  CB  . LEU B 79  ? 0.2255 0.1906 0.1247 -0.0232 0.0370  -0.0320 79  LEU B CB  
2786 C  CG  . LEU B 79  ? 0.2314 0.1538 0.1572 0.0031  0.0176  0.0148  79  LEU B CG  
2787 C  CD1 . LEU B 79  ? 0.3048 0.1738 0.2111 -0.0259 0.0175  -0.0289 79  LEU B CD1 
2788 C  CD2 . LEU B 79  ? 0.2360 0.1804 0.1610 -0.0115 -0.0147 0.0361  79  LEU B CD2 
2789 N  N   . LYS B 80  ? 0.1890 0.1667 0.1513 -0.0103 -0.0289 -0.0015 80  LYS B N   
2790 C  CA  . LYS B 80  ? 0.1962 0.1650 0.1887 -0.0105 -0.0317 -0.0278 80  LYS B CA  
2791 C  C   . LYS B 80  ? 0.1838 0.2020 0.1411 -0.0017 -0.0121 -0.0265 80  LYS B C   
2792 O  O   . LYS B 80  ? 0.2369 0.1978 0.1365 -0.0052 -0.0303 -0.0344 80  LYS B O   
2793 C  CB  . LYS B 80  ? 0.2592 0.1976 0.1926 0.0120  -0.0264 0.0107  80  LYS B CB  
2794 C  CG  . LYS B 80  ? 0.2960 0.2220 0.1911 -0.0513 -0.0199 -0.0055 80  LYS B CG  
2795 C  CD  . LYS B 80  ? 0.3668 0.2574 0.1982 -0.0210 -0.0342 0.0344  80  LYS B CD  
2796 N  N   . GLY B 81  ? 0.2174 0.2010 0.1831 -0.0091 -0.0465 -0.0057 81  GLY B N   
2797 C  CA  . GLY B 81  ? 0.2579 0.1978 0.1666 -0.0474 -0.0436 0.0021  81  GLY B CA  
2798 C  C   . GLY B 81  ? 0.2696 0.2018 0.1996 -0.0527 -0.0566 0.0359  81  GLY B C   
2799 O  O   . GLY B 81  ? 0.2653 0.1818 0.1987 -0.0046 -0.0274 0.0146  81  GLY B O   
2800 N  N   . GLY B 82  ? 0.3729 0.2222 0.2359 -0.0746 -0.0653 0.0181  82  GLY B N   
2801 C  CA  . GLY B 82  ? 0.3411 0.2281 0.2165 -0.0617 -0.0379 -0.0041 82  GLY B CA  
2802 C  C   . GLY B 82  ? 0.3449 0.2154 0.2809 -0.0361 -0.1019 0.0401  82  GLY B C   
2803 O  O   . GLY B 82  ? 0.3497 0.2723 0.2459 -0.0361 -0.1090 0.0706  82  GLY B O   
2804 N  N   . PRO B 83  ? 0.2834 0.2281 0.2260 -0.0163 -0.0586 0.0383  83  PRO B N   
2805 C  CA  . PRO B 83  ? 0.3348 0.2034 0.2123 -0.0474 -0.0693 0.0423  83  PRO B CA  
2806 C  C   . PRO B 83  ? 0.1990 0.2021 0.2181 -0.0137 -0.0480 0.0298  83  PRO B C   
2807 O  O   . PRO B 83  ? 0.2301 0.2946 0.3000 -0.0417 -0.0185 0.0353  83  PRO B O   
2808 C  CB  . PRO B 83  ? 0.2971 0.2354 0.2328 -0.0734 -0.1090 0.0714  83  PRO B CB  
2809 C  CG  . PRO B 83  ? 0.2152 0.1969 0.2567 -0.0615 -0.0127 0.0549  83  PRO B CG  
2810 C  CD  . PRO B 83  ? 0.2836 0.1633 0.2567 -0.0121 -0.0573 -0.0065 83  PRO B CD  
2811 N  N   . LEU B 84  ? 0.1929 0.1917 0.1694 -0.0388 -0.0619 0.0331  84  LEU B N   
2812 C  CA  . LEU B 84  ? 0.2106 0.1326 0.2339 -0.0078 -0.0712 0.0370  84  LEU B CA  
2813 C  C   . LEU B 84  ? 0.2256 0.1895 0.1809 0.0087  -0.0175 0.0529  84  LEU B C   
2814 O  O   . LEU B 84  ? 0.2366 0.2050 0.1861 -0.0218 -0.0489 0.0601  84  LEU B O   
2815 C  CB  . LEU B 84  ? 0.1823 0.1367 0.1553 0.0189  -0.0328 0.0131  84  LEU B CB  
2816 C  CG  . LEU B 84  ? 0.1958 0.1428 0.1256 0.0017  -0.0241 0.0221  84  LEU B CG  
2817 C  CD1 . LEU B 84  ? 0.1852 0.1796 0.1439 -0.0031 0.0119  0.0308  84  LEU B CD1 
2818 C  CD2 . LEU B 84  ? 0.1802 0.1419 0.1235 0.0027  -0.0142 0.0137  84  LEU B CD2 
2819 N  N   . ASP B 85  ? 0.2669 0.1689 0.2037 -0.0109 -0.0449 0.0474  85  ASP B N   
2820 C  CA  . ASP B 85  ? 0.2752 0.1865 0.2438 0.0060  0.0037  0.0527  85  ASP B CA  
2821 C  C   . ASP B 85  ? 0.3440 0.2341 0.2249 -0.0244 -0.0502 0.0160  85  ASP B C   
2822 O  O   . ASP B 85  ? 0.3416 0.2811 0.2536 0.0298  -0.0419 0.0461  85  ASP B O   
2823 C  CB  . ASP B 85  ? 0.2378 0.2282 0.2542 -0.0076 -0.0465 0.0087  85  ASP B CB  
2824 C  CG  . ASP B 85  ? 0.2301 0.1365 0.2003 -0.0423 -0.0052 0.0296  85  ASP B CG  
2825 O  OD1 . ASP B 85  ? 0.2556 0.3149 0.2197 -0.0636 0.0138  -0.0432 85  ASP B OD1 
2826 O  OD2 . ASP B 85  ? 0.1766 0.2450 0.2696 -0.0176 -0.0315 0.0027  85  ASP B OD2 
2827 N  N   . GLY B 86  ? 0.3591 0.3068 0.2563 -0.0641 0.0425  -0.0741 86  GLY B N   
2828 C  CA  . GLY B 86  ? 0.2606 0.3041 0.3032 -0.0276 -0.0098 0.0154  86  GLY B CA  
2829 C  C   . GLY B 86  ? 0.2673 0.2073 0.2319 -0.0305 -0.0355 -0.0309 86  GLY B C   
2830 O  O   . GLY B 86  ? 0.3846 0.2872 0.3781 -0.0482 -0.0082 -0.1398 86  GLY B O   
2831 N  N   A THR B 87  ? 0.2197 0.2005 0.1592 -0.0218 -0.0240 0.0445  87  THR B N   
2832 N  N   B THR B 87  ? 0.2208 0.2032 0.1513 -0.0234 -0.0189 0.0535  87  THR B N   
2833 C  CA  A THR B 87  ? 0.2206 0.2019 0.1683 -0.0161 -0.0253 0.0231  87  THR B CA  
2834 C  CA  B THR B 87  ? 0.2148 0.1680 0.1561 -0.0205 -0.0384 0.0342  87  THR B CA  
2835 C  C   A THR B 87  ? 0.1718 0.1534 0.1509 0.0109  -0.0109 -0.0074 87  THR B C   
2836 C  C   B THR B 87  ? 0.1906 0.1457 0.1463 0.0175  -0.0320 -0.0034 87  THR B C   
2837 O  O   A THR B 87  ? 0.1208 0.1118 0.1419 -0.0104 -0.0074 0.0055  87  THR B O   
2838 O  O   B THR B 87  ? 0.1563 0.1037 0.1545 -0.0049 -0.0003 0.0043  87  THR B O   
2839 C  CB  A THR B 87  ? 0.2318 0.1935 0.1730 -0.0165 -0.0350 0.0500  87  THR B CB  
2840 C  CB  B THR B 87  ? 0.2431 0.1477 0.1380 -0.0271 -0.0207 0.0020  87  THR B CB  
2841 O  OG1 A THR B 87  ? 0.3014 0.2840 0.2019 -0.0088 -0.0612 0.0873  87  THR B OG1 
2842 O  OG1 B THR B 87  ? 0.2080 0.1256 0.1438 -0.0328 -0.0012 0.0132  87  THR B OG1 
2843 C  CG2 A THR B 87  ? 0.2499 0.1631 0.1447 0.0132  0.0200  0.0110  87  THR B CG2 
2844 C  CG2 B THR B 87  ? 0.2556 0.1841 0.1580 -0.0266 -0.0303 0.0498  87  THR B CG2 
2845 N  N   . TYR B 88  ? 0.2046 0.1244 0.1251 0.0107  -0.0013 0.0130  88  TYR B N   
2846 C  CA  . TYR B 88  ? 0.1504 0.1287 0.1130 -0.0035 -0.0049 0.0142  88  TYR B CA  
2847 C  C   . TYR B 88  ? 0.1416 0.1154 0.1234 -0.0078 0.0049  -0.0052 88  TYR B C   
2848 O  O   . TYR B 88  ? 0.1890 0.1908 0.1694 -0.0104 0.0214  -0.0421 88  TYR B O   
2849 C  CB  . TYR B 88  ? 0.1425 0.1172 0.1368 0.0054  0.0059  0.0083  88  TYR B CB  
2850 C  CG  . TYR B 88  ? 0.1434 0.0924 0.1398 0.0159  0.0108  0.0151  88  TYR B CG  
2851 C  CD1 . TYR B 88  ? 0.1687 0.1560 0.1377 -0.0131 -0.0043 0.0165  88  TYR B CD1 
2852 C  CD2 . TYR B 88  ? 0.1274 0.0748 0.1298 -0.0196 -0.0087 0.0091  88  TYR B CD2 
2853 C  CE1 . TYR B 88  ? 0.1446 0.1324 0.1301 -0.0062 -0.0175 -0.0089 88  TYR B CE1 
2854 C  CE2 . TYR B 88  ? 0.1290 0.1059 0.1297 -0.0031 -0.0049 0.0119  88  TYR B CE2 
2855 C  CZ  . TYR B 88  ? 0.1335 0.1137 0.1335 0.0080  -0.0107 -0.0046 88  TYR B CZ  
2856 O  OH  . TYR B 88  ? 0.1522 0.1221 0.1486 0.0096  -0.0156 0.0137  88  TYR B OH  
2857 N  N   . ARG B 89  ? 0.1378 0.1181 0.1071 -0.0122 -0.0105 0.0223  89  ARG B N   
2858 C  CA  . ARG B 89  ? 0.1504 0.1206 0.1430 -0.0171 0.0001  0.0081  89  ARG B CA  
2859 C  C   . ARG B 89  ? 0.1194 0.1170 0.1215 -0.0104 -0.0076 -0.0089 89  ARG B C   
2860 O  O   . ARG B 89  ? 0.1279 0.1010 0.1262 -0.0142 0.0007  0.0129  89  ARG B O   
2861 C  CB  . ARG B 89  ? 0.1597 0.1376 0.1809 -0.0263 0.0250  -0.0103 89  ARG B CB  
2862 C  CG  . ARG B 89  ? 0.1599 0.1614 0.2587 -0.0219 0.0130  -0.0024 89  ARG B CG  
2863 C  CD  . ARG B 89  ? 0.2199 0.1653 0.2328 -0.0346 -0.0197 -0.0003 89  ARG B CD  
2864 N  NE  . ARG B 89  ? 0.2111 0.1780 0.2461 -0.0266 -0.0219 -0.0027 89  ARG B NE  
2865 C  CZ  . ARG B 89  ? 0.2163 0.1559 0.2451 -0.0498 -0.0632 0.0227  89  ARG B CZ  
2866 N  NH1 . ARG B 89  ? 0.2696 0.1990 0.2427 -0.0443 -0.0241 0.0195  89  ARG B NH1 
2867 N  NH2 . ARG B 89  ? 0.2547 0.1825 0.2425 0.0110  -0.0228 0.0174  89  ARG B NH2 
2868 N  N   . LEU B 90  ? 0.1267 0.1127 0.1342 -0.0130 0.0071  0.0008  90  LEU B N   
2869 C  CA  . LEU B 90  ? 0.1136 0.1118 0.1186 -0.0076 -0.0010 -0.0085 90  LEU B CA  
2870 C  C   . LEU B 90  ? 0.1299 0.1085 0.1188 -0.0104 -0.0103 -0.0006 90  LEU B C   
2871 O  O   . LEU B 90  ? 0.1583 0.1513 0.1430 -0.0289 0.0218  -0.0015 90  LEU B O   
2872 C  CB  . LEU B 90  ? 0.1384 0.1068 0.1373 -0.0171 -0.0071 -0.0275 90  LEU B CB  
2873 C  CG  . LEU B 90  ? 0.1209 0.1332 0.1651 0.0065  -0.0006 -0.0044 90  LEU B CG  
2874 C  CD1 . LEU B 90  ? 0.1475 0.1471 0.2054 -0.0156 -0.0164 0.0043  90  LEU B CD1 
2875 C  CD2 . LEU B 90  ? 0.1655 0.1984 0.1949 0.0441  0.0372  -0.0161 90  LEU B CD2 
2876 N  N   . ILE B 91  ? 0.1262 0.0971 0.1125 -0.0017 -0.0109 0.0024  91  ILE B N   
2877 C  CA  . ILE B 91  ? 0.1261 0.1229 0.1167 0.0089  -0.0062 0.0012  91  ILE B CA  
2878 C  C   . ILE B 91  ? 0.1163 0.1055 0.1190 -0.0088 -0.0076 0.0059  91  ILE B C   
2879 O  O   . ILE B 91  ? 0.1098 0.0994 0.1493 -0.0105 -0.0057 -0.0102 91  ILE B O   
2880 C  CB  . ILE B 91  ? 0.1037 0.1240 0.1416 0.0030  -0.0082 -0.0094 91  ILE B CB  
2881 C  CG1 . ILE B 91  ? 0.1953 0.1605 0.1577 0.0105  -0.0286 -0.0432 91  ILE B CG1 
2882 C  CG2 . ILE B 91  ? 0.1283 0.1411 0.1687 -0.0051 -0.0013 -0.0031 91  ILE B CG2 
2883 C  CD1 . ILE B 91  ? 0.2524 0.1926 0.1827 0.0193  0.0168  -0.0285 91  ILE B CD1 
2884 N  N   . GLN B 92  ? 0.1326 0.0944 0.1344 0.0000  -0.0168 -0.0040 92  GLN B N   
2885 C  CA  . GLN B 92  ? 0.1005 0.0947 0.1228 -0.0226 -0.0034 0.0132  92  GLN B CA  
2886 C  C   . GLN B 92  ? 0.0909 0.1010 0.1315 -0.0094 -0.0156 -0.0115 92  GLN B C   
2887 O  O   . GLN B 92  ? 0.0922 0.1040 0.1306 -0.0113 -0.0028 -0.0019 92  GLN B O   
2888 C  CB  . GLN B 92  ? 0.1423 0.1355 0.1199 0.0012  0.0000  0.0209  92  GLN B CB  
2889 C  CG  . GLN B 92  ? 0.1689 0.1392 0.1497 -0.0208 0.0250  -0.0035 92  GLN B CG  
2890 C  CD  . GLN B 92  ? 0.1306 0.1559 0.1814 -0.0226 0.0108  -0.0008 92  GLN B CD  
2891 O  OE1 . GLN B 92  ? 0.1641 0.1362 0.2348 -0.0278 0.0181  -0.0156 92  GLN B OE1 
2892 N  NE2 . GLN B 92  ? 0.2479 0.2793 0.2066 0.0542  0.0164  0.0251  92  GLN B NE2 
2893 N  N   . PHE B 93  ? 0.1136 0.1015 0.1319 -0.0130 -0.0054 -0.0013 93  PHE B N   
2894 C  CA  . PHE B 93  ? 0.1080 0.0978 0.1165 -0.0038 -0.0043 0.0096  93  PHE B CA  
2895 C  C   . PHE B 93  ? 0.0865 0.1024 0.0906 -0.0057 -0.0063 -0.0108 93  PHE B C   
2896 O  O   . PHE B 93  ? 0.0949 0.1005 0.1425 0.0020  -0.0165 0.0019  93  PHE B O   
2897 C  CB  . PHE B 93  ? 0.1012 0.1143 0.1305 0.0010  0.0174  -0.0121 93  PHE B CB  
2898 C  CG  . PHE B 93  ? 0.1109 0.1102 0.1224 0.0006  0.0135  -0.0065 93  PHE B CG  
2899 C  CD1 . PHE B 93  ? 0.1030 0.1202 0.1829 0.0081  -0.0051 0.0085  93  PHE B CD1 
2900 C  CD2 . PHE B 93  ? 0.1230 0.1353 0.1383 -0.0130 0.0161  0.0037  93  PHE B CD2 
2901 C  CE1 . PHE B 93  ? 0.1161 0.1410 0.1407 0.0100  0.0297  0.0013  93  PHE B CE1 
2902 C  CE2 . PHE B 93  ? 0.1190 0.1276 0.1588 -0.0085 -0.0008 0.0122  93  PHE B CE2 
2903 C  CZ  . PHE B 93  ? 0.1290 0.1159 0.1622 0.0085  0.0138  0.0094  93  PHE B CZ  
2904 N  N   . HIS B 94  ? 0.1150 0.0890 0.1109 -0.0035 0.0024  0.0048  94  HIS B N   
2905 C  CA  . HIS B 94  ? 0.0967 0.0906 0.0952 -0.0076 -0.0098 0.0024  94  HIS B CA  
2906 C  C   . HIS B 94  ? 0.0804 0.0900 0.0906 0.0142  -0.0049 -0.0008 94  HIS B C   
2907 O  O   . HIS B 94  ? 0.0953 0.0922 0.0996 -0.0082 -0.0154 -0.0020 94  HIS B O   
2908 C  CB  . HIS B 94  ? 0.0781 0.1096 0.1186 -0.0041 -0.0140 -0.0120 94  HIS B CB  
2909 C  CG  . HIS B 94  ? 0.1003 0.0933 0.1055 0.0019  -0.0167 -0.0135 94  HIS B CG  
2910 N  ND1 . HIS B 94  ? 0.1057 0.1019 0.0985 0.0189  -0.0082 -0.0167 94  HIS B ND1 
2911 C  CD2 . HIS B 94  ? 0.0624 0.1114 0.0834 0.0049  -0.0102 0.0057  94  HIS B CD2 
2912 C  CE1 . HIS B 94  ? 0.1132 0.0965 0.0886 -0.0088 0.0000  0.0031  94  HIS B CE1 
2913 N  NE2 . HIS B 94  ? 0.0766 0.0878 0.0987 0.0008  -0.0038 0.0040  94  HIS B NE2 
2914 N  N   . PHE B 95  ? 0.1012 0.0739 0.1015 -0.0070 0.0055  0.0063  95  PHE B N   
2915 C  CA  . PHE B 95  ? 0.0940 0.0822 0.1035 -0.0060 0.0162  -0.0136 95  PHE B CA  
2916 C  C   . PHE B 95  ? 0.0965 0.0891 0.0897 0.0070  0.0035  -0.0068 95  PHE B C   
2917 O  O   . PHE B 95  ? 0.1267 0.1019 0.1133 -0.0125 -0.0065 -0.0154 95  PHE B O   
2918 C  CB  . PHE B 95  ? 0.1191 0.1001 0.1181 0.0207  0.0265  0.0073  95  PHE B CB  
2919 C  CG  . PHE B 95  ? 0.0782 0.1000 0.1039 0.0087  0.0148  -0.0121 95  PHE B CG  
2920 C  CD1 . PHE B 95  ? 0.1010 0.1071 0.0982 0.0063  0.0028  -0.0126 95  PHE B CD1 
2921 C  CD2 . PHE B 95  ? 0.1091 0.1134 0.1019 0.0159  0.0176  -0.0152 95  PHE B CD2 
2922 C  CE1 . PHE B 95  ? 0.1036 0.1391 0.1238 0.0163  0.0103  -0.0136 95  PHE B CE1 
2923 C  CE2 . PHE B 95  ? 0.1195 0.1071 0.1295 0.0063  0.0164  -0.0027 95  PHE B CE2 
2924 C  CZ  . PHE B 95  ? 0.1357 0.1052 0.1129 0.0015  0.0055  0.0068  95  PHE B CZ  
2925 N  N   . HIS B 96  ? 0.0931 0.1066 0.1085 0.0001  0.0078  0.0089  96  HIS B N   
2926 C  CA  . HIS B 96  ? 0.0789 0.0931 0.0834 0.0051  0.0129  0.0003  96  HIS B CA  
2927 C  C   . HIS B 96  ? 0.1082 0.1005 0.0829 0.0143  -0.0183 0.0024  96  HIS B C   
2928 O  O   . HIS B 96  ? 0.1138 0.0973 0.0904 0.0077  -0.0038 0.0049  96  HIS B O   
2929 C  CB  . HIS B 96  ? 0.0927 0.0825 0.1199 0.0204  -0.0021 0.0046  96  HIS B CB  
2930 C  CG  . HIS B 96  ? 0.0978 0.0832 0.0904 0.0024  0.0098  0.0000  96  HIS B CG  
2931 N  ND1 . HIS B 96  ? 0.0991 0.0861 0.0908 0.0113  -0.0006 -0.0097 96  HIS B ND1 
2932 C  CD2 . HIS B 96  ? 0.1134 0.0843 0.1121 0.0127  0.0099  0.0087  96  HIS B CD2 
2933 C  CE1 . HIS B 96  ? 0.1222 0.0861 0.1105 0.0116  -0.0003 -0.0013 96  HIS B CE1 
2934 N  NE2 . HIS B 96  ? 0.0813 0.0741 0.1040 0.0076  0.0147  0.0013  96  HIS B NE2 
2935 N  N   . TRP B 97  ? 0.0895 0.0760 0.0996 0.0105  -0.0054 0.0068  97  TRP B N   
2936 C  CA  . TRP B 97  ? 0.0915 0.0848 0.0949 0.0049  0.0013  0.0085  97  TRP B CA  
2937 C  C   . TRP B 97  ? 0.0736 0.0940 0.0821 0.0152  -0.0038 0.0049  97  TRP B C   
2938 O  O   . TRP B 97  ? 0.1123 0.0956 0.0865 0.0043  -0.0073 0.0015  97  TRP B O   
2939 C  CB  . TRP B 97  ? 0.0922 0.1156 0.1005 -0.0006 -0.0093 0.0035  97  TRP B CB  
2940 C  CG  . TRP B 97  ? 0.1071 0.0945 0.0917 0.0205  -0.0124 -0.0032 97  TRP B CG  
2941 C  CD1 . TRP B 97  ? 0.1015 0.1005 0.1064 0.0184  -0.0157 0.0110  97  TRP B CD1 
2942 C  CD2 . TRP B 97  ? 0.1218 0.1009 0.1005 0.0111  0.0007  0.0013  97  TRP B CD2 
2943 N  NE1 . TRP B 97  ? 0.1231 0.0918 0.1344 0.0068  -0.0212 -0.0015 97  TRP B NE1 
2944 C  CE2 . TRP B 97  ? 0.1170 0.0980 0.0983 0.0031  -0.0027 -0.0082 97  TRP B CE2 
2945 C  CE3 . TRP B 97  ? 0.1040 0.0938 0.1172 0.0071  0.0054  -0.0003 97  TRP B CE3 
2946 C  CZ2 . TRP B 97  ? 0.1337 0.1195 0.1075 -0.0173 -0.0054 -0.0048 97  TRP B CZ2 
2947 C  CZ3 . TRP B 97  ? 0.0976 0.1149 0.0980 -0.0093 -0.0049 -0.0060 97  TRP B CZ3 
2948 C  CH2 . TRP B 97  ? 0.1089 0.1392 0.1271 0.0236  -0.0254 -0.0007 97  TRP B CH2 
2949 N  N   . GLY B 98  ? 0.0888 0.0876 0.1012 0.0115  0.0037  0.0083  98  GLY B N   
2950 C  CA  . GLY B 98  ? 0.1057 0.1053 0.0985 0.0057  -0.0013 0.0197  98  GLY B CA  
2951 C  C   . GLY B 98  ? 0.1068 0.0940 0.1281 0.0010  -0.0094 -0.0046 98  GLY B C   
2952 O  O   . GLY B 98  ? 0.1262 0.1143 0.1409 0.0129  -0.0003 0.0060  98  GLY B O   
2953 N  N   . SER B 99  ? 0.1472 0.1159 0.1240 0.0263  -0.0074 0.0144  99  SER B N   
2954 C  CA  . SER B 99  ? 0.1493 0.1242 0.1259 0.0412  -0.0260 0.0049  99  SER B CA  
2955 C  C   . SER B 99  ? 0.1657 0.1376 0.1444 0.0274  -0.0086 0.0006  99  SER B C   
2956 O  O   . SER B 99  ? 0.1861 0.1674 0.1877 0.0406  0.0044  0.0026  99  SER B O   
2957 C  CB  . SER B 99  ? 0.1640 0.1194 0.1385 0.0370  -0.0082 0.0240  99  SER B CB  
2958 O  OG  . SER B 99  ? 0.1948 0.1463 0.1362 0.0218  0.0093  0.0315  99  SER B OG  
2959 N  N   . LEU B 100 ? 0.1606 0.1270 0.1362 0.0251  -0.0043 0.0000  100 LEU B N   
2960 C  CA  . LEU B 100 ? 0.2312 0.1369 0.1298 0.0096  -0.0099 -0.0097 100 LEU B CA  
2961 C  C   . LEU B 100 ? 0.1517 0.1281 0.1226 0.0275  -0.0055 -0.0032 100 LEU B C   
2962 O  O   . LEU B 100 ? 0.1723 0.1066 0.1425 0.0210  0.0003  0.0082  100 LEU B O   
2963 C  CB  . LEU B 100 ? 0.2212 0.1908 0.2181 -0.0211 -0.0447 -0.0015 100 LEU B CB  
2964 C  CG  . LEU B 100 ? 0.2581 0.1930 0.2066 0.0126  -0.0070 0.0019  100 LEU B CG  
2965 C  CD1 . LEU B 100 ? 0.3206 0.4007 0.2106 -0.0379 -0.0300 0.0562  100 LEU B CD1 
2966 C  CD2 . LEU B 100 ? 0.3395 0.2709 0.3019 0.0706  -0.0447 0.1326  100 LEU B CD2 
2967 N  N   . ASP B 101 ? 0.1579 0.1199 0.1226 0.0248  0.0306  0.0003  101 ASP B N   
2968 C  CA  . ASP B 101 ? 0.1676 0.1337 0.1362 -0.0166 0.0114  -0.0073 101 ASP B CA  
2969 C  C   . ASP B 101 ? 0.1797 0.1351 0.1538 0.0071  0.0005  -0.0132 101 ASP B C   
2970 O  O   . ASP B 101 ? 0.1726 0.1378 0.1799 -0.0120 -0.0206 -0.0076 101 ASP B O   
2971 C  CB  . ASP B 101 ? 0.1477 0.1321 0.1428 -0.0186 0.0140  -0.0322 101 ASP B CB  
2972 C  CG  . ASP B 101 ? 0.1738 0.1689 0.1913 0.0182  0.0131  -0.0198 101 ASP B CG  
2973 O  OD1 . ASP B 101 ? 0.1834 0.1595 0.1822 0.0131  0.0100  -0.0294 101 ASP B OD1 
2974 O  OD2 . ASP B 101 ? 0.2032 0.2005 0.2922 0.0292  0.0355  -0.0847 101 ASP B OD2 
2975 N  N   . GLY B 102 ? 0.1517 0.1260 0.1647 0.0035  0.0010  -0.0082 102 GLY B N   
2976 C  CA  . GLY B 102 ? 0.1641 0.1276 0.1773 0.0063  -0.0003 -0.0454 102 GLY B CA  
2977 C  C   . GLY B 102 ? 0.1590 0.1270 0.1513 0.0065  0.0028  -0.0115 102 GLY B C   
2978 O  O   . GLY B 102 ? 0.1746 0.1355 0.1732 -0.0131 -0.0109 -0.0197 102 GLY B O   
2979 N  N   . GLN B 103 ? 0.1378 0.1234 0.1319 0.0052  0.0065  -0.0230 103 GLN B N   
2980 C  CA  . GLN B 103 ? 0.1018 0.1027 0.1102 -0.0010 -0.0021 0.0000  103 GLN B CA  
2981 C  C   . GLN B 103 ? 0.0969 0.0924 0.0933 -0.0010 -0.0080 -0.0059 103 GLN B C   
2982 O  O   . GLN B 103 ? 0.1208 0.1059 0.1233 0.0125  -0.0023 -0.0027 103 GLN B O   
2983 C  CB  . GLN B 103 ? 0.1253 0.1145 0.1240 0.0063  0.0020  -0.0030 103 GLN B CB  
2984 C  CG  . GLN B 103 ? 0.1543 0.1292 0.1091 0.0222  -0.0129 0.0313  103 GLN B CG  
2985 C  CD  . GLN B 103 ? 0.1872 0.1500 0.1583 -0.0447 -0.0179 0.0357  103 GLN B CD  
2986 O  OE1 . GLN B 103 ? 0.2610 0.2495 0.2109 -0.1272 -0.0434 0.0692  103 GLN B OE1 
2987 N  NE2 . GLN B 103 ? 0.2045 0.1486 0.1369 -0.0020 -0.0003 0.0208  103 GLN B NE2 
2988 N  N   . GLY B 104 ? 0.1242 0.0985 0.0790 0.0031  -0.0048 0.0048  104 GLY B N   
2989 C  CA  . GLY B 104 ? 0.1023 0.0958 0.0940 0.0104  0.0000  -0.0017 104 GLY B CA  
2990 C  C   . GLY B 104 ? 0.0945 0.1005 0.1003 0.0057  -0.0015 -0.0131 104 GLY B C   
2991 O  O   . GLY B 104 ? 0.1141 0.1005 0.1089 -0.0097 0.0008  -0.0010 104 GLY B O   
2992 N  N   . SER B 105 ? 0.0961 0.1114 0.0757 0.0088  -0.0010 0.0098  105 SER B N   
2993 C  CA  . SER B 105 ? 0.0966 0.1088 0.0870 0.0256  -0.0093 -0.0156 105 SER B CA  
2994 C  C   . SER B 105 ? 0.0988 0.0906 0.0848 0.0102  -0.0027 -0.0030 105 SER B C   
2995 O  O   . SER B 105 ? 0.1220 0.0931 0.1158 0.0105  0.0143  0.0038  105 SER B O   
2996 C  CB  . SER B 105 ? 0.1240 0.1042 0.0962 -0.0116 -0.0173 0.0051  105 SER B CB  
2997 O  OG  . SER B 105 ? 0.1138 0.0822 0.1008 0.0000  -0.0041 -0.0003 105 SER B OG  
2998 N  N   . GLU B 106 ? 0.0897 0.0845 0.0920 0.0087  -0.0043 -0.0059 106 GLU B N   
2999 C  CA  . GLU B 106 ? 0.0983 0.0839 0.1100 -0.0038 0.0038  -0.0078 106 GLU B CA  
3000 C  C   . GLU B 106 ? 0.0961 0.0900 0.0974 0.0020  -0.0015 0.0035  106 GLU B C   
3001 O  O   . GLU B 106 ? 0.0945 0.0966 0.0935 -0.0010 0.0081  -0.0010 106 GLU B O   
3002 C  CB  . GLU B 106 ? 0.0957 0.0888 0.1133 0.0057  -0.0124 -0.0259 106 GLU B CB  
3003 C  CG  . GLU B 106 ? 0.1009 0.1118 0.1238 0.0141  -0.0182 -0.0142 106 GLU B CG  
3004 C  CD  . GLU B 106 ? 0.1316 0.1149 0.0892 0.0089  -0.0249 -0.0015 106 GLU B CD  
3005 O  OE1 . GLU B 106 ? 0.1195 0.1003 0.1046 0.0038  0.0130  -0.0024 106 GLU B OE1 
3006 O  OE2 . GLU B 106 ? 0.1438 0.1161 0.0985 0.0089  0.0017  0.0083  106 GLU B OE2 
3007 N  N   . HIS B 107 ? 0.0866 0.0874 0.0992 -0.0040 -0.0052 0.0120  107 HIS B N   
3008 C  CA  . HIS B 107 ? 0.0843 0.0769 0.0969 -0.0063 -0.0063 0.0038  107 HIS B CA  
3009 C  C   . HIS B 107 ? 0.0992 0.0881 0.1030 0.0019  0.0024  -0.0031 107 HIS B C   
3010 O  O   . HIS B 107 ? 0.0971 0.0985 0.0881 0.0031  -0.0006 -0.0012 107 HIS B O   
3011 C  CB  . HIS B 107 ? 0.1185 0.0915 0.0843 0.0015  0.0136  0.0071  107 HIS B CB  
3012 C  CG  . HIS B 107 ? 0.1064 0.0942 0.0966 -0.0085 -0.0219 0.0049  107 HIS B CG  
3013 N  ND1 . HIS B 107 ? 0.0962 0.0906 0.1046 -0.0088 0.0068  0.0093  107 HIS B ND1 
3014 C  CD2 . HIS B 107 ? 0.1312 0.0939 0.0881 -0.0005 -0.0094 0.0250  107 HIS B CD2 
3015 C  CE1 . HIS B 107 ? 0.0918 0.0872 0.0997 0.0023  -0.0030 0.0052  107 HIS B CE1 
3016 N  NE2 . HIS B 107 ? 0.0915 0.0877 0.0931 0.0109  -0.0044 0.0120  107 HIS B NE2 
3017 N  N   . THR B 108 ? 0.1159 0.0947 0.1023 -0.0151 -0.0132 -0.0057 108 THR B N   
3018 C  CA  . THR B 108 ? 0.1456 0.0800 0.1076 0.0080  -0.0174 0.0140  108 THR B CA  
3019 C  C   . THR B 108 ? 0.0918 0.0961 0.1006 0.0054  0.0110  0.0080  108 THR B C   
3020 O  O   . THR B 108 ? 0.1137 0.1068 0.1143 -0.0019 -0.0091 0.0142  108 THR B O   
3021 C  CB  . THR B 108 ? 0.0910 0.1258 0.1177 0.0026  -0.0013 0.0162  108 THR B CB  
3022 O  OG1 . THR B 108 ? 0.1053 0.1197 0.1416 0.0010  0.0027  0.0060  108 THR B OG1 
3023 C  CG2 . THR B 108 ? 0.1276 0.1423 0.1375 0.0076  -0.0324 0.0127  108 THR B CG2 
3024 N  N   . VAL B 109 ? 0.1181 0.1021 0.1167 -0.0104 -0.0176 -0.0068 109 VAL B N   
3025 C  CA  . VAL B 109 ? 0.1158 0.1091 0.1299 -0.0232 -0.0098 -0.0113 109 VAL B CA  
3026 C  C   . VAL B 109 ? 0.1191 0.1082 0.1209 -0.0098 -0.0082 -0.0107 109 VAL B C   
3027 O  O   . VAL B 109 ? 0.1333 0.1046 0.1389 -0.0071 -0.0062 -0.0041 109 VAL B O   
3028 C  CB  . VAL B 109 ? 0.1279 0.1231 0.1274 -0.0184 -0.0010 -0.0115 109 VAL B CB  
3029 C  CG1 . VAL B 109 ? 0.2029 0.1382 0.1246 -0.0105 -0.0065 0.0115  109 VAL B CG1 
3030 C  CG2 . VAL B 109 ? 0.1667 0.1208 0.1562 -0.0333 -0.0006 0.0065  109 VAL B CG2 
3031 N  N   . ASP B 110 ? 0.1161 0.1247 0.1378 -0.0209 -0.0329 0.0035  110 ASP B N   
3032 C  CA  . ASP B 110 ? 0.1671 0.1324 0.1362 -0.0292 -0.0298 0.0012  110 ASP B CA  
3033 C  C   . ASP B 110 ? 0.1376 0.1252 0.1378 -0.0155 -0.0098 0.0098  110 ASP B C   
3034 O  O   . ASP B 110 ? 0.1655 0.1272 0.1493 -0.0218 -0.0027 -0.0066 110 ASP B O   
3035 C  CB  . ASP B 110 ? 0.2123 0.1524 0.1741 -0.0535 -0.0750 -0.0209 110 ASP B CB  
3036 C  CG  . ASP B 110 ? 0.1684 0.1441 0.1764 -0.0386 -0.0206 -0.0010 110 ASP B CG  
3037 O  OD1 . ASP B 110 ? 0.2150 0.1662 0.1903 -0.0209 -0.0709 0.0040  110 ASP B OD1 
3038 O  OD2 . ASP B 110 ? 0.1994 0.2459 0.2029 -0.0597 -0.0190 0.0129  110 ASP B OD2 
3039 N  N   . LYS B 111 ? 0.1421 0.1199 0.1281 -0.0076 -0.0105 -0.0060 111 LYS B N   
3040 C  CA  . LYS B 111 ? 0.1308 0.1167 0.1547 -0.0068 -0.0017 0.0175  111 LYS B CA  
3041 C  C   . LYS B 111 ? 0.1389 0.1077 0.1517 -0.0031 -0.0155 -0.0006 111 LYS B C   
3042 O  O   . LYS B 111 ? 0.1658 0.1441 0.1358 -0.0124 -0.0131 0.0041  111 LYS B O   
3043 C  CB  . LYS B 111 ? 0.1689 0.1610 0.1669 -0.0137 0.0390  0.0266  111 LYS B CB  
3044 C  CG  . LYS B 111 ? 0.1441 0.1838 0.2393 -0.0329 0.0529  0.0344  111 LYS B CG  
3045 C  CD  . LYS B 111 ? 0.2025 0.2468 0.2522 0.0491  0.0340  0.0267  111 LYS B CD  
3046 C  CE  . LYS B 111 ? 0.2305 0.3267 0.2856 0.0263  0.0784  0.0949  111 LYS B CE  
3047 N  NZ  . LYS B 111 ? 0.2612 0.3375 0.2466 -0.0595 0.0701  0.0403  111 LYS B NZ  
3048 N  N   . LYS B 112 ? 0.1127 0.1032 0.1425 -0.0333 -0.0086 0.0032  112 LYS B N   
3049 C  CA  . LYS B 112 ? 0.1229 0.1215 0.1256 -0.0007 -0.0054 -0.0024 112 LYS B CA  
3050 C  C   . LYS B 112 ? 0.1150 0.1163 0.1190 -0.0005 0.0130  0.0120  112 LYS B C   
3051 O  O   . LYS B 112 ? 0.1238 0.1082 0.1299 0.0003  -0.0057 0.0130  112 LYS B O   
3052 C  CB  . LYS B 112 ? 0.1312 0.1356 0.1531 -0.0137 -0.0121 -0.0241 112 LYS B CB  
3053 C  CG  . LYS B 112 ? 0.1419 0.1676 0.1410 0.0320  0.0132  -0.0088 112 LYS B CG  
3054 C  CD  . LYS B 112 ? 0.1772 0.2469 0.1624 0.0339  0.0315  0.0205  112 LYS B CD  
3055 C  CE  . LYS B 112 ? 0.2154 0.2136 0.2091 0.0408  -0.0024 -0.0204 112 LYS B CE  
3056 N  NZ  . LYS B 112 ? 0.2095 0.1691 0.2511 0.0137  0.0131  0.0007  112 LYS B NZ  
3057 N  N   A LYS B 113 ? 0.1035 0.1018 0.1316 -0.0105 0.0026  0.0109  113 LYS B N   
3058 N  N   B LYS B 113 ? 0.1054 0.1067 0.1353 -0.0068 0.0021  0.0125  113 LYS B N   
3059 C  CA  A LYS B 113 ? 0.1064 0.1033 0.1184 -0.0070 -0.0080 0.0098  113 LYS B CA  
3060 C  CA  B LYS B 113 ? 0.1182 0.1033 0.1238 -0.0081 -0.0024 0.0086  113 LYS B CA  
3061 C  C   A LYS B 113 ? 0.1213 0.1003 0.1199 0.0038  -0.0035 -0.0027 113 LYS B C   
3062 C  C   B LYS B 113 ? 0.1172 0.1055 0.1473 0.0006  -0.0010 0.0041  113 LYS B C   
3063 O  O   A LYS B 113 ? 0.1140 0.0944 0.1150 0.0021  -0.0057 -0.0081 113 LYS B O   
3064 O  O   B LYS B 113 ? 0.1398 0.0882 0.1350 -0.0001 -0.0026 0.0057  113 LYS B O   
3065 C  CB  A LYS B 113 ? 0.1159 0.1161 0.1123 -0.0043 0.0005  0.0146  113 LYS B CB  
3066 C  CB  B LYS B 113 ? 0.1188 0.1186 0.1181 -0.0102 0.0070  0.0166  113 LYS B CB  
3067 C  CG  A LYS B 113 ? 0.1395 0.1005 0.1155 -0.0088 0.0124  0.0080  113 LYS B CG  
3068 C  CG  B LYS B 113 ? 0.1286 0.1351 0.1341 -0.0087 0.0190  0.0220  113 LYS B CG  
3069 C  CD  A LYS B 113 ? 0.1350 0.1333 0.1001 -0.0043 0.0274  0.0138  113 LYS B CD  
3070 C  CD  B LYS B 113 ? 0.1659 0.0985 0.1141 0.0251  0.0247  -0.0049 113 LYS B CD  
3071 C  CE  A LYS B 113 ? 0.1454 0.1220 0.1124 -0.0204 0.0114  -0.0085 113 LYS B CE  
3072 C  CE  B LYS B 113 ? 0.1220 0.1448 0.1486 0.0020  0.0170  -0.0015 113 LYS B CE  
3073 N  NZ  A LYS B 113 ? 0.1120 0.1811 0.1461 -0.0008 0.0140  0.0357  113 LYS B NZ  
3074 N  NZ  B LYS B 113 ? 0.1832 0.2249 0.1480 -0.0148 -0.0046 0.0239  113 LYS B NZ  
3075 N  N   . TYR B 114 ? 0.1114 0.1075 0.1154 -0.0026 0.0010  0.0060  114 TYR B N   
3076 C  CA  . TYR B 114 ? 0.1125 0.0978 0.1001 -0.0006 0.0096  0.0083  114 TYR B CA  
3077 C  C   . TYR B 114 ? 0.1067 0.0886 0.0961 0.0006  0.0098  -0.0062 114 TYR B C   
3078 O  O   . TYR B 114 ? 0.1109 0.1046 0.0915 0.0109  0.0031  -0.0003 114 TYR B O   
3079 C  CB  . TYR B 114 ? 0.1184 0.0894 0.0852 -0.0017 0.0006  0.0070  114 TYR B CB  
3080 C  CG  . TYR B 114 ? 0.1158 0.1030 0.1037 -0.0065 0.0031  -0.0006 114 TYR B CG  
3081 C  CD1 . TYR B 114 ? 0.1398 0.1213 0.1253 -0.0164 -0.0126 0.0189  114 TYR B CD1 
3082 C  CD2 . TYR B 114 ? 0.1529 0.1154 0.1204 -0.0013 -0.0034 -0.0210 114 TYR B CD2 
3083 C  CE1 . TYR B 114 ? 0.1373 0.1349 0.1583 -0.0027 -0.0302 0.0135  114 TYR B CE1 
3084 C  CE2 . TYR B 114 ? 0.2064 0.1653 0.1120 -0.0177 -0.0030 -0.0006 114 TYR B CE2 
3085 C  CZ  . TYR B 114 ? 0.1870 0.1405 0.1365 -0.0222 -0.0339 -0.0063 114 TYR B CZ  
3086 O  OH  . TYR B 114 ? 0.2461 0.2066 0.1790 -0.0125 -0.0588 0.0164  114 TYR B OH  
3087 N  N   . ALA B 115 ? 0.0924 0.0764 0.1001 -0.0115 0.0097  -0.0015 115 ALA B N   
3088 C  CA  . ALA B 115 ? 0.1142 0.0753 0.1127 0.0153  -0.0027 -0.0063 115 ALA B CA  
3089 C  C   . ALA B 115 ? 0.1163 0.0872 0.1102 -0.0223 -0.0121 0.0071  115 ALA B C   
3090 O  O   . ALA B 115 ? 0.1247 0.0818 0.1023 0.0149  -0.0087 0.0008  115 ALA B O   
3091 C  CB  . ALA B 115 ? 0.1068 0.1263 0.1186 0.0215  0.0083  -0.0060 115 ALA B CB  
3092 N  N   . ALA B 116 ? 0.1128 0.0886 0.1054 0.0034  0.0087  0.0027  116 ALA B N   
3093 C  CA  . ALA B 116 ? 0.1080 0.0962 0.1057 -0.0049 -0.0233 -0.0057 116 ALA B CA  
3094 C  C   . ALA B 116 ? 0.0939 0.0978 0.1067 0.0114  0.0031  -0.0186 116 ALA B C   
3095 O  O   . ALA B 116 ? 0.1048 0.0886 0.0903 -0.0066 0.0003  0.0054  116 ALA B O   
3096 C  CB  . ALA B 116 ? 0.1006 0.1010 0.0952 0.0038  -0.0034 -0.0032 116 ALA B CB  
3097 N  N   . GLU B 117 ? 0.1080 0.0848 0.1033 0.0104  0.0059  -0.0001 117 GLU B N   
3098 C  CA  . GLU B 117 ? 0.0978 0.0804 0.1199 0.0027  0.0024  0.0089  117 GLU B CA  
3099 C  C   . GLU B 117 ? 0.0927 0.1114 0.1003 -0.0100 0.0155  -0.0065 117 GLU B C   
3100 O  O   . GLU B 117 ? 0.1306 0.1000 0.0894 0.0000  0.0023  -0.0024 117 GLU B O   
3101 C  CB  . GLU B 117 ? 0.0982 0.0978 0.1048 0.0118  -0.0038 0.0102  117 GLU B CB  
3102 C  CG  . GLU B 117 ? 0.0881 0.1071 0.1203 0.0144  -0.0019 0.0057  117 GLU B CG  
3103 C  CD  . GLU B 117 ? 0.1111 0.1052 0.0974 -0.0049 0.0126  -0.0017 117 GLU B CD  
3104 O  OE1 . GLU B 117 ? 0.1106 0.1071 0.1073 -0.0041 0.0157  0.0054  117 GLU B OE1 
3105 O  OE2 . GLU B 117 ? 0.0936 0.1141 0.1163 0.0063  0.0019  0.0015  117 GLU B OE2 
3106 N  N   . LEU B 118 ? 0.0956 0.0906 0.0962 -0.0087 0.0060  0.0074  118 LEU B N   
3107 C  CA  . LEU B 118 ? 0.0868 0.0750 0.0917 -0.0001 -0.0017 -0.0024 118 LEU B CA  
3108 C  C   . LEU B 118 ? 0.0816 0.0824 0.0818 -0.0116 0.0076  0.0085  118 LEU B C   
3109 O  O   . LEU B 118 ? 0.0935 0.0958 0.0895 -0.0092 -0.0020 -0.0027 118 LEU B O   
3110 C  CB  . LEU B 118 ? 0.1375 0.0926 0.0870 -0.0038 0.0131  -0.0013 118 LEU B CB  
3111 C  CG  . LEU B 118 ? 0.1184 0.0861 0.0985 -0.0126 0.0143  -0.0083 118 LEU B CG  
3112 C  CD1 . LEU B 118 ? 0.1033 0.1215 0.1331 -0.0065 0.0035  -0.0063 118 LEU B CD1 
3113 C  CD2 . LEU B 118 ? 0.1190 0.1344 0.1001 -0.0131 0.0292  -0.0038 118 LEU B CD2 
3114 N  N   . HIS B 119 ? 0.0784 0.0775 0.0897 -0.0130 -0.0019 -0.0003 119 HIS B N   
3115 C  CA  . HIS B 119 ? 0.0971 0.0820 0.0918 0.0038  0.0178  -0.0006 119 HIS B CA  
3116 C  C   . HIS B 119 ? 0.0732 0.0864 0.0915 0.0043  0.0017  -0.0006 119 HIS B C   
3117 O  O   . HIS B 119 ? 0.0983 0.0949 0.0917 0.0093  -0.0200 0.0097  119 HIS B O   
3118 C  CB  . HIS B 119 ? 0.0854 0.0807 0.0696 -0.0105 0.0115  0.0015  119 HIS B CB  
3119 C  CG  . HIS B 119 ? 0.0881 0.0802 0.0882 -0.0063 0.0001  0.0129  119 HIS B CG  
3120 N  ND1 . HIS B 119 ? 0.0944 0.0929 0.0861 0.0044  -0.0017 -0.0038 119 HIS B ND1 
3121 C  CD2 . HIS B 119 ? 0.0913 0.0957 0.1206 0.0001  -0.0076 0.0012  119 HIS B CD2 
3122 C  CE1 . HIS B 119 ? 0.1030 0.0942 0.1082 0.0074  -0.0007 0.0055  119 HIS B CE1 
3123 N  NE2 . HIS B 119 ? 0.1066 0.1106 0.1107 -0.0046 0.0156  -0.0015 119 HIS B NE2 
3124 N  N   . LEU B 120 ? 0.1100 0.0904 0.0920 -0.0017 -0.0006 0.0035  120 LEU B N   
3125 C  CA  . LEU B 120 ? 0.1055 0.0967 0.1112 0.0041  0.0083  0.0052  120 LEU B CA  
3126 C  C   . LEU B 120 ? 0.0933 0.0818 0.0897 -0.0098 -0.0161 0.0049  120 LEU B C   
3127 O  O   . LEU B 120 ? 0.0926 0.0913 0.0987 -0.0078 -0.0044 -0.0028 120 LEU B O   
3128 C  CB  . LEU B 120 ? 0.1253 0.0860 0.1181 0.0130  0.0116  0.0000  120 LEU B CB  
3129 C  CG  . LEU B 120 ? 0.1125 0.1203 0.1167 0.0121  0.0091  -0.0049 120 LEU B CG  
3130 C  CD1 . LEU B 120 ? 0.1808 0.1263 0.1870 0.0125  -0.0040 -0.0456 120 LEU B CD1 
3131 C  CD2 . LEU B 120 ? 0.1328 0.1676 0.1721 -0.0032 0.0307  0.0353  120 LEU B CD2 
3132 N  N   . VAL B 121 ? 0.1001 0.0789 0.0904 0.0003  -0.0021 -0.0041 121 VAL B N   
3133 C  CA  . VAL B 121 ? 0.1109 0.0860 0.1084 0.0005  -0.0120 -0.0076 121 VAL B CA  
3134 C  C   . VAL B 121 ? 0.0922 0.0924 0.0947 -0.0115 -0.0073 -0.0087 121 VAL B C   
3135 O  O   . VAL B 121 ? 0.0913 0.0978 0.1246 -0.0060 -0.0028 -0.0059 121 VAL B O   
3136 C  CB  . VAL B 121 ? 0.1161 0.0949 0.1085 -0.0032 0.0000  -0.0043 121 VAL B CB  
3137 C  CG1 . VAL B 121 ? 0.1177 0.1133 0.1097 0.0059  -0.0038 -0.0137 121 VAL B CG1 
3138 C  CG2 . VAL B 121 ? 0.1259 0.1023 0.1001 -0.0397 -0.0142 0.0152  121 VAL B CG2 
3139 N  N   . HIS B 122 ? 0.0960 0.0834 0.0939 -0.0027 0.0020  0.0046  122 HIS B N   
3140 C  CA  . HIS B 122 ? 0.1247 0.0737 0.0974 -0.0008 -0.0060 -0.0065 122 HIS B CA  
3141 C  C   . HIS B 122 ? 0.1098 0.0927 0.1109 -0.0041 0.0052  0.0034  122 HIS B C   
3142 O  O   . HIS B 122 ? 0.1100 0.0861 0.1228 -0.0035 0.0065  -0.0023 122 HIS B O   
3143 C  CB  . HIS B 122 ? 0.1254 0.1066 0.0933 0.0006  -0.0182 -0.0017 122 HIS B CB  
3144 C  CG  . HIS B 122 ? 0.1233 0.0978 0.1143 -0.0037 -0.0183 -0.0099 122 HIS B CG  
3145 N  ND1 . HIS B 122 ? 0.1256 0.1008 0.1037 -0.0155 0.0097  0.0008  122 HIS B ND1 
3146 C  CD2 . HIS B 122 ? 0.1256 0.1197 0.1125 -0.0120 -0.0176 -0.0073 122 HIS B CD2 
3147 C  CE1 . HIS B 122 ? 0.1206 0.1283 0.1128 0.0044  0.0166  0.0010  122 HIS B CE1 
3148 N  NE2 . HIS B 122 ? 0.1384 0.1111 0.1071 -0.0035 0.0076  -0.0063 122 HIS B NE2 
3149 N  N   . TRP B 123 ? 0.1097 0.0936 0.0903 0.0010  -0.0081 -0.0044 123 TRP B N   
3150 C  CA  . TRP B 123 ? 0.1064 0.0933 0.1071 0.0074  -0.0138 0.0024  123 TRP B CA  
3151 C  C   . TRP B 123 ? 0.0958 0.0935 0.0920 -0.0092 -0.0054 -0.0049 123 TRP B C   
3152 O  O   . TRP B 123 ? 0.1147 0.1088 0.1084 -0.0013 0.0048  0.0049  123 TRP B O   
3153 C  CB  . TRP B 123 ? 0.1328 0.1289 0.1184 0.0006  -0.0115 -0.0152 123 TRP B CB  
3154 C  CG  . TRP B 123 ? 0.1453 0.1107 0.1465 0.0006  -0.0060 0.0046  123 TRP B CG  
3155 C  CD1 . TRP B 123 ? 0.1279 0.1330 0.1556 -0.0087 0.0057  -0.0205 123 TRP B CD1 
3156 C  CD2 . TRP B 123 ? 0.1448 0.1150 0.1369 0.0001  -0.0375 -0.0164 123 TRP B CD2 
3157 N  NE1 . TRP B 123 ? 0.1427 0.1225 0.1583 -0.0097 -0.0119 -0.0269 123 TRP B NE1 
3158 C  CE2 . TRP B 123 ? 0.1576 0.1138 0.1759 -0.0137 -0.0096 0.0000  123 TRP B CE2 
3159 C  CE3 . TRP B 123 ? 0.1687 0.0873 0.1500 -0.0030 -0.0017 -0.0141 123 TRP B CE3 
3160 C  CZ2 . TRP B 123 ? 0.1817 0.1049 0.1535 -0.0071 -0.0307 -0.0088 123 TRP B CZ2 
3161 C  CZ3 . TRP B 123 ? 0.1507 0.1127 0.1879 -0.0278 -0.0152 -0.0104 123 TRP B CZ3 
3162 C  CH2 . TRP B 123 ? 0.1471 0.1285 0.1631 0.0031  -0.0245 -0.0326 123 TRP B CH2 
3163 N  N   . ASN B 124 ? 0.1134 0.1080 0.1125 0.0041  -0.0087 0.0063  124 ASN B N   
3164 C  CA  . ASN B 124 ? 0.1254 0.1030 0.1308 0.0010  -0.0155 0.0232  124 ASN B CA  
3165 C  C   . ASN B 124 ? 0.1283 0.1021 0.1124 0.0122  -0.0035 0.0070  124 ASN B C   
3166 O  O   . ASN B 124 ? 0.1332 0.1012 0.1120 -0.0019 -0.0066 0.0044  124 ASN B O   
3167 C  CB  . ASN B 124 ? 0.1263 0.1224 0.1466 0.0048  -0.0308 -0.0024 124 ASN B CB  
3168 C  CG  . ASN B 124 ? 0.1509 0.1114 0.1359 0.0077  -0.0163 -0.0086 124 ASN B CG  
3169 O  OD1 . ASN B 124 ? 0.1540 0.1356 0.1606 0.0028  -0.0203 0.0133  124 ASN B OD1 
3170 N  ND2 . ASN B 124 ? 0.1495 0.1091 0.1923 -0.0043 -0.0368 0.0317  124 ASN B ND2 
3171 N  N   . THR B 125 ? 0.1233 0.1185 0.1387 -0.0131 -0.0062 0.0087  125 THR B N   
3172 C  CA  . THR B 125 ? 0.1389 0.0958 0.1708 -0.0066 0.0270  0.0203  125 THR B CA  
3173 C  C   . THR B 125 ? 0.1845 0.1271 0.1513 0.0013  -0.0204 0.0197  125 THR B C   
3174 O  O   . THR B 125 ? 0.2075 0.1378 0.1805 -0.0410 -0.0175 -0.0086 125 THR B O   
3175 C  CB  . THR B 125 ? 0.2226 0.1502 0.1883 -0.0379 0.0322  -0.0122 125 THR B CB  
3176 O  OG1 . THR B 125 ? 0.3111 0.1845 0.1796 -0.0313 0.0127  0.0333  125 THR B OG1 
3177 C  CG2 . THR B 125 ? 0.2386 0.1969 0.1843 0.0093  0.0680  -0.0087 125 THR B CG2 
3178 N  N   . LYS B 126 ? 0.1739 0.1123 0.1400 0.0154  -0.0269 0.0146  127 LYS B N   
3179 C  CA  . LYS B 126 ? 0.2125 0.1285 0.1603 0.0472  -0.0190 -0.0010 127 LYS B CA  
3180 C  C   . LYS B 126 ? 0.1623 0.1106 0.1520 0.0093  -0.0170 -0.0092 127 LYS B C   
3181 O  O   . LYS B 126 ? 0.2201 0.1310 0.1983 0.0230  -0.0068 -0.0142 127 LYS B O   
3182 C  CB  . LYS B 126 ? 0.2298 0.1495 0.2425 0.0289  -0.0103 0.0164  127 LYS B CB  
3183 C  CG  . LYS B 126 ? 0.2093 0.1786 0.1811 0.0253  -0.0320 0.0015  127 LYS B CG  
3184 C  CD  . LYS B 126 ? 0.2147 0.2127 0.3037 0.0450  -0.0802 -0.0557 127 LYS B CD  
3185 C  CE  . LYS B 126 ? 0.2226 0.2815 0.4072 0.0471  -0.0540 -0.0635 127 LYS B CE  
3186 N  NZ  . LYS B 126 ? 0.2687 0.3578 0.4113 -0.0668 -0.0460 -0.0509 127 LYS B NZ  
3187 N  N   . TYR B 127 ? 0.1407 0.1280 0.1416 0.0027  -0.0153 0.0019  128 TYR B N   
3188 C  CA  . TYR B 127 ? 0.1182 0.1222 0.1423 0.0071  0.0073  0.0135  128 TYR B CA  
3189 C  C   . TYR B 127 ? 0.1522 0.1017 0.1333 0.0231  -0.0076 0.0120  128 TYR B C   
3190 O  O   . TYR B 127 ? 0.1669 0.1154 0.1531 -0.0005 -0.0186 0.0001  128 TYR B O   
3191 C  CB  . TYR B 127 ? 0.1705 0.1172 0.1506 0.0000  -0.0093 0.0200  128 TYR B CB  
3192 C  CG  . TYR B 127 ? 0.1290 0.1023 0.1453 0.0118  0.0041  0.0049  128 TYR B CG  
3193 C  CD1 . TYR B 127 ? 0.1633 0.1188 0.1550 0.0337  -0.0030 0.0278  128 TYR B CD1 
3194 C  CD2 . TYR B 127 ? 0.1358 0.1202 0.1369 -0.0178 0.0082  0.0059  128 TYR B CD2 
3195 C  CE1 . TYR B 127 ? 0.1781 0.1238 0.1802 0.0247  -0.0222 0.0195  128 TYR B CE1 
3196 C  CE2 . TYR B 127 ? 0.1377 0.1301 0.1615 0.0214  -0.0186 0.0105  128 TYR B CE2 
3197 C  CZ  . TYR B 127 ? 0.1308 0.1335 0.1823 0.0126  -0.0098 0.0185  128 TYR B CZ  
3198 O  OH  . TYR B 127 ? 0.1583 0.1533 0.2046 0.0059  -0.0335 0.0282  128 TYR B OH  
3199 N  N   . GLY B 128 ? 0.1326 0.1039 0.1603 -0.0027 -0.0043 0.0094  129 GLY B N   
3200 C  CA  . GLY B 128 ? 0.1457 0.1001 0.1705 -0.0017 -0.0197 0.0015  129 GLY B CA  
3201 C  C   . GLY B 128 ? 0.1253 0.1216 0.1554 -0.0098 -0.0273 0.0062  129 GLY B C   
3202 O  O   . GLY B 128 ? 0.1592 0.1382 0.1872 -0.0165 -0.0121 -0.0005 129 GLY B O   
3203 N  N   . ASP B 129 ? 0.1531 0.1229 0.1533 0.0071  -0.0007 0.0007  130 ASP B N   
3204 C  CA  . ASP B 129 ? 0.1592 0.1366 0.1775 -0.0041 -0.0395 0.0012  130 ASP B CA  
3205 C  C   . ASP B 129 ? 0.1356 0.1629 0.1969 0.0135  -0.0218 0.0194  130 ASP B C   
3206 O  O   . ASP B 129 ? 0.1423 0.1299 0.2172 -0.0043 -0.0082 0.0183  130 ASP B O   
3207 C  CB  . ASP B 129 ? 0.2572 0.2078 0.1851 -0.0494 -0.0571 0.0238  130 ASP B CB  
3208 C  CG  . ASP B 129 ? 0.2174 0.1495 0.2447 -0.0200 -0.0299 0.0509  130 ASP B CG  
3209 O  OD1 . ASP B 129 ? 0.2143 0.2247 0.3316 0.0085  0.0619  -0.0209 130 ASP B OD1 
3210 O  OD2 . ASP B 129 ? 0.2989 0.2479 0.2490 -0.0331 -0.0728 -0.0172 130 ASP B OD2 
3211 N  N   . PHE B 130 ? 0.1195 0.1137 0.1996 -0.0041 -0.0472 0.0082  131 PHE B N   
3212 C  CA  . PHE B 130 ? 0.1832 0.1281 0.1903 -0.0133 0.0027  -0.0120 131 PHE B CA  
3213 C  C   . PHE B 130 ? 0.1436 0.1303 0.1571 -0.0131 -0.0218 -0.0074 131 PHE B C   
3214 O  O   . PHE B 130 ? 0.1326 0.1419 0.1561 -0.0070 -0.0085 0.0000  131 PHE B O   
3215 C  CB  . PHE B 130 ? 0.1795 0.1603 0.2157 0.0263  -0.0230 0.0035  131 PHE B CB  
3216 C  CG  . PHE B 130 ? 0.2039 0.2397 0.2447 -0.0399 -0.0183 -0.0116 131 PHE B CG  
3217 C  CD1 . PHE B 130 ? 0.1604 0.2642 0.3467 -0.0037 -0.0635 0.0737  131 PHE B CD1 
3218 C  CD2 . PHE B 130 ? 0.3140 0.2529 0.1878 0.0798  -0.0040 0.0013  131 PHE B CD2 
3219 C  CE1 . PHE B 130 ? 0.2179 0.3458 0.3228 -0.0157 -0.0771 0.0759  131 PHE B CE1 
3220 C  CE2 . PHE B 130 ? 0.3743 0.2509 0.3745 0.0013  -0.1313 0.0659  131 PHE B CE2 
3221 C  CZ  . PHE B 130 ? 0.4368 0.3535 0.3944 -0.0579 -0.1145 0.1649  131 PHE B CZ  
3222 N  N   . GLY B 131 ? 0.1753 0.1551 0.1466 -0.0157 -0.0296 -0.0087 132 GLY B N   
3223 C  CA  . GLY B 131 ? 0.1698 0.1904 0.1438 -0.0020 -0.0328 0.0143  132 GLY B CA  
3224 C  C   . GLY B 131 ? 0.1847 0.1708 0.1594 -0.0197 -0.0280 -0.0328 132 GLY B C   
3225 O  O   . GLY B 131 ? 0.2341 0.1766 0.1700 0.0109  -0.0049 -0.0261 132 GLY B O   
3226 N  N   . LYS B 132 ? 0.1675 0.1414 0.1766 0.0030  -0.0137 -0.0238 133 LYS B N   
3227 C  CA  . LYS B 132 ? 0.1554 0.1237 0.1896 -0.0161 -0.0055 -0.0203 133 LYS B CA  
3228 C  C   . LYS B 132 ? 0.1499 0.1448 0.1366 -0.0051 0.0141  -0.0140 133 LYS B C   
3229 O  O   . LYS B 132 ? 0.1470 0.1394 0.1775 0.0171  0.0183  -0.0245 133 LYS B O   
3230 C  CB  . LYS B 132 ? 0.2068 0.1447 0.1691 0.0156  -0.0046 -0.0102 133 LYS B CB  
3231 C  CG  . LYS B 132 ? 0.2707 0.1802 0.2509 -0.0709 0.0269  -0.0432 133 LYS B CG  
3232 C  CD  . LYS B 132 ? 0.5425 0.2951 0.3138 -0.0500 0.0890  -0.0816 133 LYS B CD  
3233 C  CE  . LYS B 132 ? 0.3303 0.3637 0.1561 -0.0092 0.0873  -0.0333 133 LYS B CE  
3234 N  NZ  . LYS B 132 ? 0.3269 0.5094 0.4801 -0.0895 -0.0181 0.0105  133 LYS B NZ  
3235 N  N   . ALA B 133 ? 0.1653 0.1150 0.1349 -0.0024 0.0173  -0.0093 134 ALA B N   
3236 C  CA  . ALA B 133 ? 0.1378 0.1233 0.1324 0.0024  -0.0066 0.0010  134 ALA B CA  
3237 C  C   . ALA B 133 ? 0.1276 0.1127 0.1172 0.0038  -0.0044 -0.0060 134 ALA B C   
3238 O  O   . ALA B 133 ? 0.1283 0.1367 0.1316 -0.0010 -0.0035 -0.0082 134 ALA B O   
3239 C  CB  . ALA B 133 ? 0.1423 0.1416 0.1213 0.0032  -0.0175 -0.0241 134 ALA B CB  
3240 N  N   . VAL B 134 ? 0.1407 0.1221 0.1407 0.0211  -0.0078 -0.0109 135 VAL B N   
3241 C  CA  . VAL B 134 ? 0.1321 0.1357 0.1396 0.0082  -0.0081 -0.0043 135 VAL B CA  
3242 C  C   . VAL B 134 ? 0.1570 0.1384 0.1182 -0.0038 -0.0172 -0.0266 135 VAL B C   
3243 O  O   . VAL B 134 ? 0.1504 0.1599 0.1436 0.0041  0.0052  0.0000  135 VAL B O   
3244 C  CB  . VAL B 134 ? 0.1351 0.1468 0.1197 -0.0010 -0.0166 -0.0074 135 VAL B CB  
3245 C  CG1 . VAL B 134 ? 0.1675 0.1610 0.2043 0.0351  -0.0155 -0.0300 135 VAL B CG1 
3246 C  CG2 . VAL B 134 ? 0.2019 0.1777 0.1292 0.0125  -0.0491 -0.0092 135 VAL B CG2 
3247 N  N   . GLN B 135 ? 0.1445 0.1294 0.1482 0.0131  -0.0098 -0.0065 136 GLN B N   
3248 C  CA  . GLN B 135 ? 0.1800 0.1508 0.1585 0.0137  0.0131  -0.0057 136 GLN B CA  
3249 C  C   . GLN B 135 ? 0.1631 0.1615 0.1734 0.0211  0.0083  0.0178  136 GLN B C   
3250 O  O   . GLN B 135 ? 0.1757 0.1854 0.2132 0.0125  0.0126  -0.0227 136 GLN B O   
3251 C  CB  . GLN B 135 ? 0.1901 0.1468 0.1854 0.0185  0.0051  -0.0190 136 GLN B CB  
3252 C  CG  . GLN B 135 ? 0.2282 0.1804 0.2400 -0.0070 -0.0295 -0.0199 136 GLN B CG  
3253 C  CD  . GLN B 135 ? 0.3483 0.2587 0.2834 -0.0137 -0.0049 -0.0740 136 GLN B CD  
3254 O  OE1 . GLN B 135 ? 0.4405 0.4440 0.4769 0.0307  0.0263  -0.1708 136 GLN B OE1 
3255 N  NE2 . GLN B 135 ? 0.3849 0.3594 0.3269 -0.0562 0.0074  -0.0861 136 GLN B NE2 
3256 N  N   . GLN B 136 ? 0.1647 0.1391 0.1421 -0.0046 -0.0307 0.0141  137 GLN B N   
3257 C  CA  . GLN B 136 ? 0.1283 0.1430 0.1554 0.0082  -0.0204 0.0006  137 GLN B CA  
3258 C  C   . GLN B 136 ? 0.1668 0.1480 0.1861 -0.0010 -0.0038 -0.0052 137 GLN B C   
3259 O  O   . GLN B 136 ? 0.1382 0.1328 0.1721 0.0093  -0.0062 0.0052  137 GLN B O   
3260 C  CB  . GLN B 136 ? 0.1432 0.1531 0.1492 0.0049  -0.0068 0.0000  137 GLN B CB  
3261 C  CG  . GLN B 136 ? 0.1782 0.1816 0.2242 -0.0057 -0.0461 0.0131  137 GLN B CG  
3262 C  CD  . GLN B 136 ? 0.2578 0.2134 0.2350 -0.0635 0.0111  0.0149  137 GLN B CD  
3263 O  OE1 . GLN B 136 ? 0.2253 0.1949 0.2296 0.0439  0.0080  0.0060  137 GLN B OE1 
3264 N  NE2 . GLN B 136 ? 0.4750 0.3253 0.3282 -0.0623 -0.0938 -0.0869 137 GLN B NE2 
3265 N  N   . PRO B 137 ? 0.1253 0.1414 0.1488 0.0220  0.0046  0.0035  138 PRO B N   
3266 C  CA  . PRO B 137 ? 0.1071 0.1585 0.1750 0.0093  -0.0104 0.0186  138 PRO B CA  
3267 C  C   . PRO B 137 ? 0.1077 0.1509 0.1674 0.0201  -0.0209 0.0100  138 PRO B C   
3268 O  O   . PRO B 137 ? 0.1784 0.1658 0.1854 -0.0144 0.0155  0.0208  138 PRO B O   
3269 C  CB  . PRO B 137 ? 0.1261 0.1990 0.2800 0.0068  -0.0500 0.0151  138 PRO B CB  
3270 C  CG  . PRO B 137 ? 0.1324 0.2626 0.3907 0.0306  0.0287  -0.0339 138 PRO B CG  
3271 C  CD  . PRO B 137 ? 0.1268 0.2118 0.1962 0.0599  0.0041  -0.0063 138 PRO B CD  
3272 N  N   . ASP B 138 ? 0.1149 0.1394 0.1550 0.0190  -0.0100 0.0157  139 ASP B N   
3273 C  CA  . ASP B 138 ? 0.1421 0.1553 0.1477 0.0108  -0.0346 -0.0049 139 ASP B CA  
3274 C  C   . ASP B 138 ? 0.1356 0.1226 0.1377 0.0104  0.0142  -0.0083 139 ASP B C   
3275 O  O   . ASP B 138 ? 0.1339 0.1299 0.1394 0.0121  -0.0082 0.0104  139 ASP B O   
3276 C  CB  . ASP B 138 ? 0.1324 0.1620 0.1748 -0.0154 -0.0261 0.0269  139 ASP B CB  
3277 C  CG  . ASP B 138 ? 0.1705 0.1768 0.1815 0.0155  -0.0298 0.0078  139 ASP B CG  
3278 O  OD1 . ASP B 138 ? 0.1790 0.1452 0.1861 0.0298  -0.0119 0.0265  139 ASP B OD1 
3279 O  OD2 . ASP B 138 ? 0.2100 0.2222 0.2235 0.0089  -0.0328 0.0515  139 ASP B OD2 
3280 N  N   . GLY B 139 ? 0.1202 0.1208 0.1470 0.0141  -0.0098 -0.0135 140 GLY B N   
3281 C  CA  . GLY B 139 ? 0.1093 0.1039 0.1649 0.0104  0.0010  -0.0066 140 GLY B CA  
3282 C  C   . GLY B 139 ? 0.0978 0.0947 0.1084 -0.0044 -0.0052 -0.0043 140 GLY B C   
3283 O  O   . GLY B 139 ? 0.1084 0.1001 0.1292 -0.0062 0.0023  0.0206  140 GLY B O   
3284 N  N   . LEU B 140 ? 0.1037 0.0886 0.1150 -0.0006 -0.0015 -0.0006 141 LEU B N   
3285 C  CA  . LEU B 140 ? 0.1129 0.1037 0.0838 0.0130  -0.0148 -0.0034 141 LEU B CA  
3286 C  C   . LEU B 140 ? 0.0960 0.1021 0.0888 0.0030  -0.0057 0.0111  141 LEU B C   
3287 O  O   . LEU B 140 ? 0.1019 0.0962 0.1173 -0.0035 -0.0010 -0.0065 141 LEU B O   
3288 C  CB  . LEU B 140 ? 0.1218 0.1079 0.1109 0.0055  -0.0263 0.0104  141 LEU B CB  
3289 C  CG  . LEU B 140 ? 0.1297 0.1378 0.1032 -0.0007 -0.0131 0.0151  141 LEU B CG  
3290 C  CD1 . LEU B 140 ? 0.1471 0.1319 0.1103 -0.0181 -0.0355 0.0165  141 LEU B CD1 
3291 C  CD2 . LEU B 140 ? 0.1599 0.1254 0.1376 -0.0109 -0.0329 0.0065  141 LEU B CD2 
3292 N  N   . ALA B 141 ? 0.1124 0.0762 0.0994 0.0059  0.0013  0.0001  142 ALA B N   
3293 C  CA  . ALA B 141 ? 0.1181 0.1006 0.0997 0.0048  -0.0132 -0.0146 142 ALA B CA  
3294 C  C   . ALA B 141 ? 0.0960 0.0891 0.0869 -0.0049 -0.0015 -0.0031 142 ALA B C   
3295 O  O   . ALA B 141 ? 0.0979 0.0897 0.1184 -0.0044 -0.0007 0.0030  142 ALA B O   
3296 C  CB  . ALA B 141 ? 0.1195 0.1168 0.1053 -0.0070 -0.0087 0.0006  142 ALA B CB  
3297 N  N   . VAL B 142 ? 0.1181 0.0798 0.1033 -0.0074 -0.0071 -0.0052 143 VAL B N   
3298 C  CA  . VAL B 142 ? 0.1055 0.1036 0.1001 0.0113  -0.0044 -0.0020 143 VAL B CA  
3299 C  C   . VAL B 142 ? 0.1046 0.0957 0.1014 0.0000  -0.0071 -0.0027 143 VAL B C   
3300 O  O   . VAL B 142 ? 0.0936 0.0969 0.1059 0.0017  -0.0046 -0.0003 143 VAL B O   
3301 C  CB  . VAL B 142 ? 0.0965 0.0904 0.0915 0.0003  0.0077  -0.0003 143 VAL B CB  
3302 C  CG1 . VAL B 142 ? 0.0901 0.1048 0.1066 0.0085  0.0040  0.0001  143 VAL B CG1 
3303 C  CG2 . VAL B 142 ? 0.1003 0.1224 0.1067 -0.0103 -0.0020 -0.0214 143 VAL B CG2 
3304 N  N   . LEU B 143 ? 0.1046 0.0827 0.0850 0.0003  -0.0010 -0.0006 144 LEU B N   
3305 C  CA  . LEU B 143 ? 0.1109 0.0789 0.1064 0.0078  0.0175  -0.0027 144 LEU B CA  
3306 C  C   . LEU B 143 ? 0.0841 0.0949 0.0900 0.0013  0.0017  -0.0052 144 LEU B C   
3307 O  O   . LEU B 143 ? 0.1055 0.0931 0.1149 0.0013  -0.0163 -0.0125 144 LEU B O   
3308 C  CB  . LEU B 143 ? 0.1398 0.1008 0.1179 -0.0119 0.0311  -0.0028 144 LEU B CB  
3309 C  CG  . LEU B 143 ? 0.1387 0.1430 0.1130 -0.0059 0.0196  -0.0087 144 LEU B CG  
3310 C  CD1 . LEU B 143 ? 0.1638 0.1606 0.1328 -0.0209 0.0010  -0.0278 144 LEU B CD1 
3311 C  CD2 . LEU B 143 ? 0.1464 0.1532 0.1164 -0.0051 0.0242  0.0138  144 LEU B CD2 
3312 N  N   . GLY B 144 ? 0.1019 0.0825 0.0967 -0.0044 -0.0060 -0.0023 145 GLY B N   
3313 C  CA  . GLY B 144 ? 0.1003 0.0683 0.1089 0.0001  -0.0140 -0.0107 145 GLY B CA  
3314 C  C   . GLY B 144 ? 0.0969 0.0798 0.0922 -0.0043 -0.0138 -0.0046 145 GLY B C   
3315 O  O   . GLY B 144 ? 0.1125 0.0948 0.1134 0.0057  -0.0115 -0.0054 145 GLY B O   
3316 N  N   . ILE B 145 ? 0.0983 0.0750 0.0933 0.0006  0.0186  0.0092  146 ILE B N   
3317 C  CA  . ILE B 145 ? 0.1111 0.0958 0.0973 0.0080  0.0311  -0.0085 146 ILE B CA  
3318 C  C   . ILE B 145 ? 0.0821 0.0983 0.0960 0.0052  0.0063  -0.0151 146 ILE B C   
3319 O  O   . ILE B 145 ? 0.1115 0.0952 0.1042 0.0000  0.0020  -0.0105 146 ILE B O   
3320 C  CB  . ILE B 145 ? 0.1177 0.1075 0.0829 -0.0043 0.0274  0.0027  146 ILE B CB  
3321 C  CG1 . ILE B 145 ? 0.1459 0.1208 0.1362 -0.0046 0.0015  0.0262  146 ILE B CG1 
3322 C  CG2 . ILE B 145 ? 0.1508 0.1216 0.1170 0.0000  0.0242  -0.0194 146 ILE B CG2 
3323 C  CD1 . ILE B 145 ? 0.1353 0.1529 0.1620 -0.0153 0.0218  -0.0019 146 ILE B CD1 
3324 N  N   . PHE B 146 ? 0.0899 0.0861 0.1009 0.0024  0.0132  0.0000  147 PHE B N   
3325 C  CA  . PHE B 146 ? 0.0964 0.0910 0.1026 -0.0052 0.0078  0.0068  147 PHE B CA  
3326 C  C   . PHE B 146 ? 0.1059 0.0834 0.1032 -0.0010 0.0125  0.0010  147 PHE B C   
3327 O  O   . PHE B 146 ? 0.1186 0.1197 0.1019 0.0043  0.0113  -0.0024 147 PHE B O   
3328 C  CB  . PHE B 146 ? 0.0970 0.1023 0.0985 -0.0074 0.0066  -0.0073 147 PHE B CB  
3329 C  CG  . PHE B 146 ? 0.0915 0.0800 0.0961 -0.0005 0.0086  0.0082  147 PHE B CG  
3330 C  CD1 . PHE B 146 ? 0.1115 0.0807 0.1008 -0.0005 0.0100  0.0086  147 PHE B CD1 
3331 C  CD2 . PHE B 146 ? 0.0982 0.0820 0.1125 -0.0154 -0.0041 -0.0060 147 PHE B CD2 
3332 C  CE1 . PHE B 146 ? 0.0951 0.0924 0.1100 0.0000  0.0043  0.0027  147 PHE B CE1 
3333 C  CE2 . PHE B 146 ? 0.1211 0.1077 0.0933 -0.0020 0.0118  -0.0103 147 PHE B CE2 
3334 C  CZ  . PHE B 146 ? 0.1145 0.0847 0.0976 -0.0142 0.0046  -0.0143 147 PHE B CZ  
3335 N  N   . LEU B 147 ? 0.0936 0.1045 0.1012 0.0049  0.0012  -0.0020 148 LEU B N   
3336 C  CA  . LEU B 147 ? 0.1026 0.0863 0.1159 0.0059  0.0087  0.0087  148 LEU B CA  
3337 C  C   . LEU B 147 ? 0.1149 0.0951 0.0970 -0.0137 -0.0087 -0.0245 148 LEU B C   
3338 O  O   . LEU B 147 ? 0.1238 0.0979 0.1112 -0.0065 0.0094  -0.0089 148 LEU B O   
3339 C  CB  . LEU B 147 ? 0.1286 0.1071 0.0948 -0.0120 -0.0003 -0.0054 148 LEU B CB  
3340 C  CG  . LEU B 147 ? 0.1269 0.0913 0.1242 -0.0015 0.0154  -0.0094 148 LEU B CG  
3341 C  CD1 . LEU B 147 ? 0.1213 0.1195 0.1463 0.0183  -0.0127 -0.0037 148 LEU B CD1 
3342 C  CD2 . LEU B 147 ? 0.1123 0.1244 0.1308 0.0048  0.0044  0.0026  148 LEU B CD2 
3343 N  N   . LYS B 148 ? 0.1150 0.0969 0.1091 0.0073  0.0125  -0.0118 149 LYS B N   
3344 C  CA  . LYS B 148 ? 0.1283 0.0956 0.1427 -0.0241 0.0149  0.0078  149 LYS B CA  
3345 C  C   . LYS B 148 ? 0.1380 0.1271 0.1272 -0.0146 0.0203  -0.0031 149 LYS B C   
3346 O  O   . LYS B 148 ? 0.1254 0.1350 0.1554 0.0035  0.0353  0.0065  149 LYS B O   
3347 C  CB  . LYS B 148 ? 0.1305 0.1279 0.1554 -0.0109 -0.0041 -0.0259 149 LYS B CB  
3348 C  CG  . LYS B 148 ? 0.1565 0.1337 0.1887 0.0098  -0.0070 -0.0107 149 LYS B CG  
3349 C  CD  . LYS B 148 ? 0.2046 0.2336 0.2179 -0.0489 0.0198  -0.0538 149 LYS B CD  
3350 C  CE  . LYS B 148 ? 0.3271 0.3481 0.2240 -0.0485 0.0152  -0.1084 149 LYS B CE  
3351 N  NZ  . LYS B 148 ? 0.5443 0.5364 0.3353 -0.1137 -0.1298 -0.1852 149 LYS B NZ  
3352 N  N   . VAL B 149 ? 0.1296 0.1091 0.1606 0.0059  0.0076  -0.0038 150 VAL B N   
3353 C  CA  . VAL B 149 ? 0.1378 0.1272 0.1355 0.0137  0.0192  0.0142  150 VAL B CA  
3354 C  C   . VAL B 149 ? 0.1450 0.1353 0.1662 -0.0012 0.0088  -0.0082 150 VAL B C   
3355 O  O   . VAL B 149 ? 0.1445 0.1509 0.1678 -0.0088 0.0204  -0.0116 150 VAL B O   
3356 C  CB  . VAL B 149 ? 0.1590 0.1170 0.1374 0.0273  -0.0003 0.0104  150 VAL B CB  
3357 C  CG1 . VAL B 149 ? 0.1457 0.1581 0.1705 0.0255  -0.0078 0.0049  150 VAL B CG1 
3358 C  CG2 . VAL B 149 ? 0.2034 0.1556 0.1913 0.0377  0.0208  -0.0269 150 VAL B CG2 
3359 N  N   . GLY B 150 ? 0.1532 0.1107 0.1409 -0.0013 0.0230  -0.0232 151 GLY B N   
3360 C  CA  . GLY B 150 ? 0.1596 0.1308 0.1543 0.0010  0.0199  -0.0544 151 GLY B CA  
3361 C  C   . GLY B 150 ? 0.1495 0.1308 0.1592 0.0194  0.0207  -0.0417 151 GLY B C   
3362 O  O   . GLY B 150 ? 0.1615 0.1459 0.1631 0.0309  0.0093  -0.0230 151 GLY B O   
3363 N  N   A SER B 151 ? 0.1755 0.1495 0.1604 0.0151  0.0296  -0.0370 152 SER B N   
3364 N  N   B SER B 151 ? 0.1728 0.1531 0.1626 0.0157  0.0266  -0.0313 152 SER B N   
3365 C  CA  A SER B 151 ? 0.1775 0.1283 0.1784 -0.0003 0.0205  -0.0222 152 SER B CA  
3366 C  CA  B SER B 151 ? 0.1571 0.1167 0.1718 0.0168  0.0038  -0.0060 152 SER B CA  
3367 C  C   A SER B 151 ? 0.1462 0.1385 0.1841 0.0060  0.0226  -0.0337 152 SER B C   
3368 C  C   B SER B 151 ? 0.1464 0.1301 0.1870 -0.0034 0.0280  -0.0195 152 SER B C   
3369 O  O   A SER B 151 ? 0.1365 0.1605 0.1150 0.0189  0.0109  -0.0175 152 SER B O   
3370 O  O   B SER B 151 ? 0.1251 0.1448 0.1419 0.0035  0.0194  -0.0003 152 SER B O   
3371 C  CB  A SER B 151 ? 0.2409 0.2326 0.1714 0.0204  0.0219  -0.0493 152 SER B CB  
3372 C  CB  B SER B 151 ? 0.2064 0.1942 0.1504 0.0364  0.0138  -0.0412 152 SER B CB  
3373 O  OG  A SER B 151 ? 0.2298 0.2451 0.2019 0.0065  0.0483  0.0032  152 SER B OG  
3374 O  OG  B SER B 151 ? 0.2811 0.2118 0.1775 -0.0410 0.0026  -0.0351 152 SER B OG  
3375 N  N   . ALA B 152 ? 0.1410 0.1290 0.1820 0.0006  0.0237  0.0046  153 ALA B N   
3376 C  CA  . ALA B 152 ? 0.1378 0.1364 0.1453 0.0136  0.0055  -0.0006 153 ALA B CA  
3377 C  C   . ALA B 152 ? 0.1226 0.1369 0.1333 -0.0015 0.0063  0.0020  153 ALA B C   
3378 O  O   . ALA B 152 ? 0.1913 0.1565 0.1459 0.0104  0.0259  0.0038  153 ALA B O   
3379 C  CB  . ALA B 152 ? 0.1348 0.1404 0.2373 0.0118  0.0049  0.0219  153 ALA B CB  
3380 N  N   . LYS B 153 ? 0.1377 0.1079 0.1615 0.0046  0.0205  -0.0038 154 LYS B N   
3381 C  CA  . LYS B 153 ? 0.1387 0.1509 0.1344 0.0070  0.0184  -0.0044 154 LYS B CA  
3382 C  C   . LYS B 153 ? 0.1726 0.1398 0.1520 0.0087  0.0276  0.0108  154 LYS B C   
3383 O  O   . LYS B 153 ? 0.1204 0.1423 0.1368 0.0092  0.0157  0.0010  154 LYS B O   
3384 C  CB  . LYS B 153 ? 0.1286 0.1576 0.1527 0.0008  0.0243  -0.0178 154 LYS B CB  
3385 C  CG  . LYS B 153 ? 0.1529 0.1533 0.1562 0.0205  0.0024  -0.0062 154 LYS B CG  
3386 C  CD  . LYS B 153 ? 0.1534 0.1492 0.1944 0.0170  -0.0401 0.0020  154 LYS B CD  
3387 C  CE  . LYS B 153 ? 0.2122 0.1570 0.1944 0.0026  -0.0156 0.0373  154 LYS B CE  
3388 N  NZ  . LYS B 153 ? 0.3075 0.2427 0.1926 0.0000  -0.0087 -0.0281 154 LYS B NZ  
3389 N  N   . PRO B 154 ? 0.1489 0.1572 0.1513 0.0099  0.0230  -0.0071 155 PRO B N   
3390 C  CA  . PRO B 154 ? 0.1929 0.1795 0.1563 -0.0249 0.0384  -0.0120 155 PRO B CA  
3391 C  C   . PRO B 154 ? 0.1292 0.1809 0.1252 0.0000  0.0458  0.0254  155 PRO B C   
3392 O  O   . PRO B 154 ? 0.1782 0.1976 0.1969 -0.0242 0.0250  -0.0040 155 PRO B O   
3393 C  CB  . PRO B 154 ? 0.2072 0.1838 0.1450 -0.0021 0.0381  -0.0350 155 PRO B CB  
3394 C  CG  . PRO B 154 ? 0.1902 0.2370 0.2001 -0.0461 0.0542  -0.0357 155 PRO B CG  
3395 C  CD  . PRO B 154 ? 0.1763 0.2061 0.1404 -0.0001 0.0237  -0.0392 155 PRO B CD  
3396 N  N   . GLY B 155 ? 0.1448 0.1253 0.1453 0.0076  0.0252  0.0126  156 GLY B N   
3397 C  CA  . GLY B 155 ? 0.2174 0.1466 0.1547 0.0136  0.0142  -0.0197 156 GLY B CA  
3398 C  C   . GLY B 155 ? 0.1631 0.1502 0.1495 -0.0205 0.0143  -0.0043 156 GLY B C   
3399 O  O   . GLY B 155 ? 0.2849 0.1626 0.1895 -0.0322 0.0244  -0.0037 156 GLY B O   
3400 N  N   . LEU B 156 ? 0.1465 0.1583 0.1150 0.0211  0.0249  -0.0020 157 LEU B N   
3401 C  CA  . LEU B 156 ? 0.1288 0.1134 0.1182 0.0010  0.0203  -0.0159 157 LEU B CA  
3402 C  C   . LEU B 156 ? 0.1456 0.1064 0.1387 0.0092  0.0137  -0.0026 157 LEU B C   
3403 O  O   . LEU B 156 ? 0.1086 0.1243 0.1265 0.0040  0.0116  -0.0043 157 LEU B O   
3404 C  CB  . LEU B 156 ? 0.1551 0.1322 0.1554 -0.0164 0.0233  -0.0155 157 LEU B CB  
3405 C  CG  . LEU B 156 ? 0.1199 0.1351 0.1403 0.0055  0.0052  -0.0154 157 LEU B CG  
3406 C  CD1 . LEU B 156 ? 0.1400 0.1473 0.1944 0.0296  0.0193  -0.0136 157 LEU B CD1 
3407 C  CD2 . LEU B 156 ? 0.1075 0.1619 0.1599 0.0019  0.0133  0.0052  157 LEU B CD2 
3408 N  N   . GLN B 157 ? 0.1281 0.1288 0.1323 0.0054  0.0217  0.0005  158 GLN B N   
3409 C  CA  . GLN B 157 ? 0.1319 0.1721 0.1535 0.0141  0.0013  -0.0337 158 GLN B CA  
3410 C  C   . GLN B 157 ? 0.1308 0.1457 0.1766 0.0285  -0.0003 -0.0065 158 GLN B C   
3411 O  O   . GLN B 157 ? 0.1452 0.1608 0.1444 -0.0008 0.0271  -0.0085 158 GLN B O   
3412 C  CB  . GLN B 157 ? 0.1824 0.1642 0.1730 0.0288  0.0285  -0.0220 158 GLN B CB  
3413 C  CG  . GLN B 157 ? 0.1913 0.2088 0.1773 0.0138  0.0057  -0.0126 158 GLN B CG  
3414 C  CD  . GLN B 157 ? 0.1474 0.1574 0.1849 0.0351  0.0034  -0.0021 158 GLN B CD  
3415 O  OE1 . GLN B 157 ? 0.1703 0.1520 0.2097 0.0110  -0.0119 0.0006  158 GLN B OE1 
3416 N  NE2 . GLN B 157 ? 0.1642 0.1741 0.2030 0.0472  -0.0044 -0.0254 158 GLN B NE2 
3417 N  N   . LYS B 158 ? 0.1656 0.1633 0.1669 -0.0028 0.0353  -0.0129 159 LYS B N   
3418 C  CA  . LYS B 158 ? 0.1168 0.1717 0.1842 0.0076  0.0168  -0.0070 159 LYS B CA  
3419 C  C   . LYS B 158 ? 0.1400 0.1486 0.1757 0.0015  0.0085  0.0049  159 LYS B C   
3420 O  O   . LYS B 158 ? 0.1335 0.1633 0.1969 0.0138  -0.0020 -0.0357 159 LYS B O   
3421 C  CB  . LYS B 158 ? 0.2062 0.2152 0.2107 -0.0684 0.0476  0.0264  159 LYS B CB  
3422 C  CG  . LYS B 158 ? 0.3084 0.3582 0.2984 -0.0568 0.1324  -0.0469 159 LYS B CG  
3423 C  CD  . LYS B 158 ? 0.4973 0.3630 0.3741 -0.0864 0.0914  -0.0032 159 LYS B CD  
3424 C  CE  . LYS B 158 ? 0.4862 0.4065 0.4589 -0.2213 0.1557  -0.0264 159 LYS B CE  
3425 N  NZ  . LYS B 158 ? 0.5432 0.4246 0.4866 -0.2254 -0.0219 0.0065  159 LYS B NZ  
3426 N  N   . VAL B 159 ? 0.1335 0.1563 0.1710 0.0160  0.0132  -0.0020 160 VAL B N   
3427 C  CA  . VAL B 159 ? 0.1096 0.1286 0.1276 0.0076  0.0073  -0.0082 160 VAL B CA  
3428 C  C   . VAL B 159 ? 0.1216 0.1504 0.1687 -0.0078 -0.0178 -0.0104 160 VAL B C   
3429 O  O   . VAL B 159 ? 0.1580 0.1472 0.1676 0.0118  0.0049  -0.0107 160 VAL B O   
3430 C  CB  . VAL B 159 ? 0.1143 0.1481 0.1565 0.0052  0.0120  0.0155  160 VAL B CB  
3431 C  CG1 . VAL B 159 ? 0.1344 0.1741 0.1550 0.0041  0.0038  0.0032  160 VAL B CG1 
3432 C  CG2 . VAL B 159 ? 0.1818 0.1702 0.2337 0.0441  0.0277  0.0278  160 VAL B CG2 
3433 N  N   . VAL B 160 ? 0.1367 0.1295 0.1565 0.0085  0.0163  0.0017  161 VAL B N   
3434 C  CA  . VAL B 160 ? 0.1852 0.1474 0.1884 0.0196  -0.0157 0.0059  161 VAL B CA  
3435 C  C   . VAL B 160 ? 0.1737 0.1376 0.1574 0.0172  0.0015  0.0052  161 VAL B C   
3436 O  O   . VAL B 160 ? 0.1721 0.1597 0.1620 0.0155  -0.0165 -0.0168 161 VAL B O   
3437 C  CB  . VAL B 160 ? 0.1872 0.1466 0.2188 0.0010  -0.0383 0.0015  161 VAL B CB  
3438 C  CG1 . VAL B 160 ? 0.2351 0.1835 0.2260 0.0366  0.0015  -0.0195 161 VAL B CG1 
3439 C  CG2 . VAL B 160 ? 0.2075 0.1547 0.2847 -0.0063 -0.0478 -0.0098 161 VAL B CG2 
3440 N  N   . ASP B 161 ? 0.1421 0.1569 0.1850 0.0372  0.0023  -0.0174 162 ASP B N   
3441 C  CA  . ASP B 161 ? 0.1439 0.1919 0.2418 0.0005  -0.0001 -0.0379 162 ASP B CA  
3442 C  C   . ASP B 161 ? 0.1560 0.2114 0.2393 0.0318  -0.0329 -0.0474 162 ASP B C   
3443 O  O   . ASP B 161 ? 0.1998 0.2666 0.2958 0.0697  -0.0690 -0.0542 162 ASP B O   
3444 C  CB  . ASP B 161 ? 0.1787 0.2642 0.2626 0.0060  0.0221  -0.0549 162 ASP B CB  
3445 C  CG  . ASP B 161 ? 0.1844 0.2452 0.2436 0.0416  0.0126  -0.0092 162 ASP B CG  
3446 O  OD1 . ASP B 161 ? 0.2626 0.2937 0.2949 0.0281  0.0454  -0.0141 162 ASP B OD1 
3447 O  OD2 . ASP B 161 ? 0.2194 0.2653 0.2517 0.0395  -0.0109 -0.0131 162 ASP B OD2 
3448 N  N   . VAL B 162 ? 0.1517 0.1542 0.2206 -0.0006 -0.0017 -0.0328 163 VAL B N   
3449 C  CA  . VAL B 162 ? 0.1689 0.1875 0.1743 0.0074  -0.0100 -0.0337 163 VAL B CA  
3450 C  C   . VAL B 162 ? 0.1383 0.1764 0.1964 -0.0082 -0.0089 -0.0104 163 VAL B C   
3451 O  O   . VAL B 162 ? 0.1474 0.1831 0.2063 0.0142  -0.0133 -0.0305 163 VAL B O   
3452 C  CB  . VAL B 162 ? 0.1702 0.1762 0.2364 -0.0377 -0.0379 0.0054  163 VAL B CB  
3453 C  CG1 . VAL B 162 ? 0.2052 0.1452 0.2572 0.0231  -0.0115 0.0143  163 VAL B CG1 
3454 C  CG2 . VAL B 162 ? 0.1868 0.2037 0.1886 -0.0186 -0.0173 -0.0285 163 VAL B CG2 
3455 N  N   . LEU B 163 ? 0.1222 0.1811 0.1554 -0.0074 0.0305  -0.0225 164 LEU B N   
3456 C  CA  . LEU B 163 ? 0.1741 0.1477 0.1030 0.0005  0.0003  -0.0243 164 LEU B CA  
3457 C  C   . LEU B 163 ? 0.1678 0.1641 0.1935 -0.0116 -0.0308 -0.0159 164 LEU B C   
3458 O  O   . LEU B 163 ? 0.1676 0.1836 0.1885 -0.0017 -0.0289 -0.0172 164 LEU B O   
3459 C  CB  . LEU B 163 ? 0.1556 0.1684 0.1784 -0.0006 -0.0350 0.0103  164 LEU B CB  
3460 C  CG  . LEU B 163 ? 0.1242 0.1425 0.1676 -0.0003 -0.0215 -0.0046 164 LEU B CG  
3461 C  CD1 . LEU B 163 ? 0.1869 0.1777 0.1928 -0.0410 0.0148  -0.0303 164 LEU B CD1 
3462 C  CD2 . LEU B 163 ? 0.1382 0.1558 0.1843 0.0297  -0.0262 -0.0044 164 LEU B CD2 
3463 N  N   . ASP B 164 ? 0.1818 0.1590 0.2111 0.0152  -0.0480 -0.0174 165 ASP B N   
3464 C  CA  . ASP B 164 ? 0.2014 0.1906 0.2323 0.0639  -0.0505 -0.0111 165 ASP B CA  
3465 C  C   . ASP B 164 ? 0.1577 0.2263 0.2233 -0.0010 -0.0480 0.0142  165 ASP B C   
3466 O  O   . ASP B 164 ? 0.2610 0.3009 0.2831 0.0313  -0.1274 0.0044  165 ASP B O   
3467 C  CB  . ASP B 164 ? 0.1960 0.2856 0.3776 0.0865  -0.0359 -0.0460 165 ASP B CB  
3468 C  CG  . ASP B 164 ? 0.3253 0.3882 0.4381 0.0452  -0.0392 -0.0276 165 ASP B CG  
3469 O  OD1 . ASP B 164 ? 0.3668 0.3481 0.4556 0.0625  -0.0489 -0.0925 165 ASP B OD1 
3470 O  OD2 . ASP B 164 ? 0.6417 0.7597 0.7699 0.1933  -0.3278 -0.1650 165 ASP B OD2 
3471 N  N   . SER B 165 ? 0.1387 0.1914 0.2009 -0.0114 -0.0269 -0.0131 166 SER B N   
3472 C  CA  . SER B 165 ? 0.1698 0.2106 0.2017 -0.0010 -0.0175 -0.0318 166 SER B CA  
3473 C  C   . SER B 165 ? 0.1551 0.1750 0.2172 -0.0254 -0.0208 -0.0250 166 SER B C   
3474 O  O   . SER B 165 ? 0.1929 0.1955 0.2299 -0.0083 -0.0274 -0.0463 166 SER B O   
3475 C  CB  . SER B 165 ? 0.2824 0.2115 0.2485 -0.0564 -0.0776 0.0078  166 SER B CB  
3476 O  OG  . SER B 165 ? 0.2303 0.2278 0.2752 -0.0160 -0.0020 0.0043  166 SER B OG  
3477 N  N   . ILE B 166 ? 0.1127 0.1653 0.1998 0.0013  -0.0189 -0.0300 167 ILE B N   
3478 C  CA  . ILE B 166 ? 0.1741 0.1360 0.1475 0.0078  -0.0237 -0.0230 167 ILE B CA  
3479 C  C   . ILE B 166 ? 0.1748 0.1409 0.1596 0.0142  -0.0026 -0.0218 167 ILE B C   
3480 O  O   . ILE B 166 ? 0.1502 0.1673 0.1541 -0.0037 -0.0238 -0.0068 167 ILE B O   
3481 C  CB  . ILE B 166 ? 0.1525 0.1583 0.1613 0.0035  -0.0305 -0.0082 167 ILE B CB  
3482 C  CG1 . ILE B 166 ? 0.0985 0.1635 0.1635 -0.0048 -0.0188 -0.0142 167 ILE B CG1 
3483 C  CG2 . ILE B 166 ? 0.1527 0.1644 0.2127 -0.0214 0.0124  -0.0120 167 ILE B CG2 
3484 C  CD1 . ILE B 166 ? 0.1518 0.1529 0.1734 0.0141  -0.0331 0.0147  167 ILE B CD1 
3485 N  N   . LYS B 167 ? 0.1563 0.1577 0.1623 0.0043  -0.0307 -0.0096 168 LYS B N   
3486 C  CA  . LYS B 167 ? 0.1493 0.1529 0.1604 0.0142  -0.0120 0.0076  168 LYS B CA  
3487 C  C   . LYS B 167 ? 0.1710 0.1791 0.1319 -0.0068 -0.0125 0.0091  168 LYS B C   
3488 O  O   . LYS B 167 ? 0.1549 0.1660 0.1757 0.0024  -0.0177 -0.0315 168 LYS B O   
3489 C  CB  . LYS B 167 ? 0.1466 0.1495 0.2111 0.0416  -0.0162 0.0091  168 LYS B CB  
3490 C  CG  . LYS B 167 ? 0.2312 0.1881 0.1893 0.0434  -0.0137 0.0232  168 LYS B CG  
3491 C  CD  . LYS B 167 ? 0.2590 0.3219 0.2499 0.0816  -0.0228 0.1023  168 LYS B CD  
3492 C  CE  . LYS B 167 ? 0.3070 0.4027 0.3865 0.0118  -0.0173 0.1656  168 LYS B CE  
3493 N  NZ  . LYS B 167 ? 0.6387 0.5310 0.5117 0.1570  -0.2401 0.1231  168 LYS B NZ  
3494 N  N   . THR B 168 ? 0.1738 0.1615 0.1657 0.0007  -0.0027 -0.0109 169 THR B N   
3495 C  CA  . THR B 168 ? 0.1465 0.1908 0.1563 -0.0034 -0.0308 -0.0258 169 THR B CA  
3496 C  C   . THR B 168 ? 0.1371 0.1818 0.1533 -0.0206 -0.0270 0.0059  169 THR B C   
3497 O  O   . THR B 168 ? 0.1630 0.1563 0.1576 -0.0076 -0.0209 -0.0193 169 THR B O   
3498 C  CB  . THR B 168 ? 0.1666 0.1955 0.1642 -0.0006 -0.0302 -0.0140 169 THR B CB  
3499 O  OG1 . THR B 168 ? 0.1888 0.2413 0.1698 -0.0113 -0.0688 -0.0148 169 THR B OG1 
3500 C  CG2 . THR B 168 ? 0.1773 0.1985 0.1971 -0.0007 -0.0806 0.0096  169 THR B CG2 
3501 N  N   . LYS B 169 ? 0.1500 0.1910 0.1434 -0.0012 -0.0286 -0.0324 170 LYS B N   
3502 C  CA  . LYS B 169 ? 0.2161 0.1728 0.1492 0.0003  -0.0024 -0.0071 170 LYS B CA  
3503 C  C   . LYS B 169 ? 0.1847 0.1998 0.1509 -0.0240 -0.0062 -0.0049 170 LYS B C   
3504 O  O   . LYS B 169 ? 0.2409 0.2614 0.1844 0.0167  -0.0441 -0.0441 170 LYS B O   
3505 C  CB  . LYS B 169 ? 0.2224 0.1888 0.1150 -0.0065 -0.0115 -0.0368 170 LYS B CB  
3506 C  CG  . LYS B 169 ? 0.2016 0.2221 0.2037 -0.0282 -0.0092 -0.0375 170 LYS B CG  
3507 C  CD  . LYS B 169 ? 0.2396 0.2099 0.2019 -0.0091 -0.0008 -0.0306 170 LYS B CD  
3508 C  CE  . LYS B 169 ? 0.3905 0.4074 0.1642 0.0190  -0.0015 -0.0276 170 LYS B CE  
3509 N  NZ  . LYS B 169 ? 0.5231 0.6723 0.3129 0.0161  0.1067  -0.1715 170 LYS B NZ  
3510 N  N   . GLY B 170 ? 0.1852 0.1691 0.1780 -0.0138 -0.0230 -0.0520 171 GLY B N   
3511 C  CA  . GLY B 170 ? 0.2116 0.1829 0.1502 -0.0340 0.0156  -0.0531 171 GLY B CA  
3512 C  C   . GLY B 170 ? 0.1868 0.2005 0.2558 -0.0189 -0.0030 -0.0113 171 GLY B C   
3513 O  O   . GLY B 170 ? 0.2578 0.1806 0.2488 -0.0592 0.0251  -0.0610 171 GLY B O   
3514 N  N   . LYS B 171 ? 0.1844 0.1766 0.1267 -0.0133 -0.0060 -0.0342 172 LYS B N   
3515 C  CA  . LYS B 171 ? 0.1793 0.2168 0.1229 -0.0083 -0.0164 -0.0460 172 LYS B CA  
3516 C  C   . LYS B 171 ? 0.1574 0.1820 0.1784 0.0035  -0.0259 0.0193  172 LYS B C   
3517 O  O   . LYS B 171 ? 0.1637 0.1829 0.1669 -0.0210 -0.0214 -0.0135 172 LYS B O   
3518 C  CB  . LYS B 171 ? 0.2393 0.2061 0.1544 -0.0159 -0.0126 -0.0193 172 LYS B CB  
3519 C  CG  . LYS B 171 ? 0.2278 0.2603 0.1820 0.0346  -0.0255 0.0133  172 LYS B CG  
3520 C  CD  . LYS B 171 ? 0.2716 0.2612 0.3420 0.0522  -0.0953 -0.0167 172 LYS B CD  
3521 C  CE  . LYS B 171 ? 0.3282 0.5898 0.4059 0.0781  -0.1709 0.1414  172 LYS B CE  
3522 N  NZ  . LYS B 171 ? 0.6381 0.4519 0.6352 -0.0109 0.0159  0.0209  172 LYS B NZ  
3523 N  N   . SER B 172 ? 0.1641 0.1834 0.1642 -0.0485 -0.0315 -0.0155 173 SER B N   
3524 C  CA  . SER B 172 ? 0.1937 0.2027 0.1656 0.0077  -0.0346 -0.0266 173 SER B CA  
3525 C  C   . SER B 172 ? 0.1474 0.2037 0.1831 -0.0121 -0.0185 -0.0005 173 SER B C   
3526 O  O   . SER B 172 ? 0.1500 0.2470 0.2583 -0.0377 -0.0693 0.0219  173 SER B O   
3527 C  CB  . SER B 172 ? 0.1667 0.1711 0.1981 -0.0320 -0.0219 -0.0052 173 SER B CB  
3528 O  OG  . SER B 172 ? 0.2456 0.1987 0.2897 -0.0485 -0.0504 -0.0121 173 SER B OG  
3529 N  N   . ALA B 173 ? 0.1277 0.2289 0.2037 -0.0129 -0.0337 0.0408  174 ALA B N   
3530 C  CA  . ALA B 173 ? 0.1152 0.2393 0.2136 -0.0175 -0.0326 0.0270  174 ALA B CA  
3531 C  C   . ALA B 173 ? 0.1534 0.2328 0.1791 0.0013  -0.0068 0.0115  174 ALA B C   
3532 O  O   . ALA B 173 ? 0.1199 0.2062 0.1796 -0.0116 -0.0093 0.0190  174 ALA B O   
3533 C  CB  . ALA B 173 ? 0.1498 0.2190 0.2888 -0.0068 -0.0149 0.0408  174 ALA B CB  
3534 N  N   . ASP B 174 ? 0.1919 0.2229 0.1906 -0.0362 0.0119  -0.0001 175 ASP B N   
3535 C  CA  . ASP B 174 ? 0.1887 0.2336 0.2167 -0.0755 -0.0251 0.0379  175 ASP B CA  
3536 C  C   . ASP B 174 ? 0.2199 0.2282 0.2648 -0.0419 -0.0419 0.0031  175 ASP B C   
3537 O  O   . ASP B 174 ? 0.2355 0.2328 0.2815 -0.0044 -0.0161 -0.0162 175 ASP B O   
3538 C  CB  . ASP B 174 ? 0.2228 0.2996 0.3129 -0.1106 0.0366  0.0044  175 ASP B CB  
3539 C  CG  . ASP B 174 ? 0.3142 0.2957 0.3871 0.0110  -0.0068 -0.0348 175 ASP B CG  
3540 O  OD1 . ASP B 174 ? 0.2215 0.4189 0.6123 0.0267  0.0098  -0.1115 175 ASP B OD1 
3541 O  OD2 . ASP B 174 ? 0.2852 0.4492 0.3725 0.0204  -0.0080 -0.0010 175 ASP B OD2 
3542 N  N   . PHE B 175 ? 0.1673 0.1791 0.1901 -0.0119 -0.0100 -0.0215 176 PHE B N   
3543 C  CA  . PHE B 175 ? 0.1650 0.1741 0.1993 -0.0551 -0.0417 0.0138  176 PHE B CA  
3544 C  C   . PHE B 175 ? 0.1887 0.1490 0.1689 -0.0057 0.0230  0.0122  176 PHE B C   
3545 O  O   . PHE B 175 ? 0.1964 0.2206 0.2249 -0.0012 -0.0109 0.0195  176 PHE B O   
3546 C  CB  . PHE B 175 ? 0.1378 0.1811 0.1983 -0.0480 -0.0043 -0.0140 176 PHE B CB  
3547 C  CG  . PHE B 175 ? 0.1574 0.1644 0.1759 -0.0027 0.0035  0.0173  176 PHE B CG  
3548 C  CD1 . PHE B 175 ? 0.2061 0.1574 0.2416 0.0104  -0.0570 0.0046  176 PHE B CD1 
3549 C  CD2 . PHE B 175 ? 0.1601 0.2027 0.2050 -0.0254 0.0074  -0.0013 176 PHE B CD2 
3550 C  CE1 . PHE B 175 ? 0.2310 0.1974 0.2395 0.0231  -0.0544 -0.0148 176 PHE B CE1 
3551 C  CE2 . PHE B 175 ? 0.1730 0.1632 0.2107 -0.0052 0.0156  0.0175  176 PHE B CE2 
3552 C  CZ  . PHE B 175 ? 0.1748 0.1624 0.2387 -0.0021 0.0041  -0.0083 176 PHE B CZ  
3553 N  N   . THR B 176 ? 0.1441 0.1750 0.2087 -0.0218 0.0076  0.0131  177 THR B N   
3554 C  CA  . THR B 176 ? 0.1773 0.1604 0.2063 -0.0416 -0.0109 0.0102  177 THR B CA  
3555 C  C   . THR B 176 ? 0.0892 0.1360 0.1617 -0.0313 0.0184  0.0160  177 THR B C   
3556 O  O   . THR B 176 ? 0.1362 0.1538 0.2188 -0.0258 -0.0245 -0.0074 177 THR B O   
3557 C  CB  . THR B 176 ? 0.1561 0.2116 0.2484 -0.0432 0.0286  -0.0097 177 THR B CB  
3558 O  OG1 . THR B 176 ? 0.1696 0.2217 0.4000 -0.0357 -0.0186 0.0520  177 THR B OG1 
3559 C  CG2 . THR B 176 ? 0.2763 0.2696 0.2581 -0.1439 0.0163  -0.0274 177 THR B CG2 
3560 N  N   . ASN B 177 ? 0.1468 0.1924 0.1721 -0.0147 -0.0104 0.0126  178 ASN B N   
3561 C  CA  . ASN B 177 ? 0.1766 0.1969 0.2036 -0.0120 0.0089  -0.0076 178 ASN B CA  
3562 C  C   . ASN B 177 ? 0.1441 0.2095 0.2596 -0.0103 0.0289  -0.0282 178 ASN B C   
3563 O  O   . ASN B 177 ? 0.2148 0.2140 0.3235 -0.0852 0.0722  -0.0373 178 ASN B O   
3564 C  CB  . ASN B 177 ? 0.1888 0.1583 0.2648 -0.0516 0.0247  -0.0206 178 ASN B CB  
3565 C  CG  . ASN B 177 ? 0.1756 0.1773 0.2339 -0.0326 0.0185  -0.0003 178 ASN B CG  
3566 O  OD1 . ASN B 177 ? 0.2375 0.2360 0.2973 -0.0487 -0.0231 0.0119  178 ASN B OD1 
3567 N  ND2 . ASN B 177 ? 0.1669 0.2147 0.2224 -0.0351 0.0153  -0.0111 178 ASN B ND2 
3568 N  N   . PHE B 178 ? 0.1443 0.1301 0.2177 -0.0324 -0.0073 0.0020  179 PHE B N   
3569 C  CA  . PHE B 178 ? 0.1362 0.1287 0.1847 -0.0189 0.0119  -0.0184 179 PHE B CA  
3570 C  C   . PHE B 178 ? 0.1279 0.1552 0.1689 -0.0049 0.0353  -0.0091 179 PHE B C   
3571 O  O   . PHE B 178 ? 0.1308 0.1536 0.2255 -0.0168 0.0032  -0.0153 179 PHE B O   
3572 C  CB  . PHE B 178 ? 0.1653 0.1326 0.1626 -0.0326 -0.0010 -0.0198 179 PHE B CB  
3573 C  CG  . PHE B 178 ? 0.1233 0.1313 0.1683 -0.0209 0.0035  -0.0097 179 PHE B CG  
3574 C  CD1 . PHE B 178 ? 0.1694 0.1445 0.1817 -0.0252 0.0003  0.0065  179 PHE B CD1 
3575 C  CD2 . PHE B 178 ? 0.1289 0.1536 0.1680 -0.0201 -0.0041 0.0005  179 PHE B CD2 
3576 C  CE1 . PHE B 178 ? 0.1446 0.1504 0.2134 -0.0232 -0.0242 -0.0026 179 PHE B CE1 
3577 C  CE2 . PHE B 178 ? 0.1313 0.1495 0.1366 -0.0062 0.0220  -0.0217 179 PHE B CE2 
3578 C  CZ  . PHE B 178 ? 0.1326 0.1364 0.1502 -0.0152 0.0051  0.0161  179 PHE B CZ  
3579 N  N   . ASP B 179 ? 0.1319 0.1833 0.1680 -0.0234 -0.0013 -0.0015 180 ASP B N   
3580 C  CA  . ASP B 179 ? 0.1386 0.1647 0.1542 -0.0233 0.0115  0.0020  180 ASP B CA  
3581 C  C   . ASP B 179 ? 0.1491 0.1373 0.1597 -0.0126 0.0108  0.0093  180 ASP B C   
3582 O  O   . ASP B 179 ? 0.1500 0.1435 0.1635 -0.0103 0.0104  -0.0038 180 ASP B O   
3583 C  CB  . ASP B 179 ? 0.1532 0.1856 0.1592 -0.0187 0.0339  0.0307  180 ASP B CB  
3584 C  CG  . ASP B 179 ? 0.2194 0.2334 0.1829 -0.0109 0.0156  0.0483  180 ASP B CG  
3585 O  OD1 . ASP B 179 ? 0.1942 0.1905 0.1793 -0.0357 0.0068  0.0256  180 ASP B OD1 
3586 O  OD2 . ASP B 179 ? 0.2921 0.3433 0.2150 -0.0289 0.0958  0.0253  180 ASP B OD2 
3587 N  N   . PRO B 180 ? 0.1389 0.1495 0.1493 -0.0017 0.0091  0.0055  181 PRO B N   
3588 C  CA  . PRO B 180 ? 0.1475 0.1685 0.1586 -0.0119 0.0076  -0.0238 181 PRO B CA  
3589 C  C   . PRO B 180 ? 0.1428 0.1563 0.1269 0.0024  0.0100  0.0006  181 PRO B C   
3590 O  O   . PRO B 180 ? 0.1389 0.1366 0.1407 -0.0087 0.0211  0.0027  181 PRO B O   
3591 C  CB  . PRO B 180 ? 0.1611 0.1710 0.1721 -0.0020 0.0273  0.0000  181 PRO B CB  
3592 C  CG  . PRO B 180 ? 0.1624 0.1550 0.1948 0.0000  -0.0166 -0.0103 181 PRO B CG  
3593 C  CD  . PRO B 180 ? 0.1613 0.1590 0.1921 -0.0098 0.0397  -0.0102 181 PRO B CD  
3594 N  N   . ARG B 181 ? 0.1660 0.1601 0.1290 -0.0096 0.0130  -0.0125 182 ARG B N   
3595 C  CA  . ARG B 181 ? 0.1572 0.1632 0.1079 -0.0017 0.0190  0.0166  182 ARG B CA  
3596 C  C   . ARG B 181 ? 0.1516 0.1705 0.1513 -0.0175 0.0166  0.0066  182 ARG B C   
3597 O  O   . ARG B 181 ? 0.1698 0.1649 0.1335 -0.0194 0.0239  0.0049  182 ARG B O   
3598 C  CB  . ARG B 181 ? 0.1755 0.1599 0.1133 -0.0289 0.0232  0.0281  182 ARG B CB  
3599 C  CG  . ARG B 181 ? 0.2151 0.1518 0.1319 -0.0120 0.0324  -0.0031 182 ARG B CG  
3600 C  CD  . ARG B 181 ? 0.2258 0.2011 0.1479 -0.0057 0.0052  0.0377  182 ARG B CD  
3601 N  NE  . ARG B 181 ? 0.2174 0.1802 0.1633 -0.0220 0.0244  -0.0192 182 ARG B NE  
3602 C  CZ  . ARG B 181 ? 0.2664 0.2547 0.2305 -0.0668 -0.0027 0.0340  182 ARG B CZ  
3603 N  NH1 . ARG B 181 ? 0.4077 0.2836 0.2071 -0.0606 -0.0399 0.0109  182 ARG B NH1 
3604 N  NH2 . ARG B 181 ? 0.2933 0.2797 0.1982 -0.1159 0.0007  0.0115  182 ARG B NH2 
3605 N  N   . GLY B 182 ? 0.1405 0.1418 0.1410 -0.0098 0.0258  0.0322  183 GLY B N   
3606 C  CA  . GLY B 182 ? 0.1664 0.1342 0.1709 -0.0003 0.0131  0.0138  183 GLY B CA  
3607 C  C   . GLY B 182 ? 0.1615 0.1710 0.1660 0.0252  0.0216  0.0205  183 GLY B C   
3608 O  O   . GLY B 182 ? 0.1851 0.1588 0.1680 0.0186  0.0527  -0.0046 183 GLY B O   
3609 N  N   . LEU B 183 ? 0.1251 0.1572 0.1344 -0.0171 0.0198  0.0037  184 LEU B N   
3610 C  CA  . LEU B 183 ? 0.1565 0.1353 0.1371 -0.0054 0.0238  0.0142  184 LEU B CA  
3611 C  C   . LEU B 183 ? 0.1335 0.1586 0.1457 0.0129  0.0209  0.0038  184 LEU B C   
3612 O  O   . LEU B 183 ? 0.1615 0.1619 0.1432 -0.0329 0.0093  -0.0031 184 LEU B O   
3613 C  CB  . LEU B 183 ? 0.1529 0.1854 0.1224 -0.0575 0.0348  0.0130  184 LEU B CB  
3614 C  CG  . LEU B 183 ? 0.1527 0.1667 0.1274 -0.0125 0.0054  0.0092  184 LEU B CG  
3615 C  CD1 . LEU B 183 ? 0.1847 0.2106 0.1410 -0.0632 0.0186  -0.0120 184 LEU B CD1 
3616 C  CD2 . LEU B 183 ? 0.2468 0.1933 0.2418 0.0315  -0.0175 0.0160  184 LEU B CD2 
3617 N  N   . LEU B 184 ? 0.1568 0.1272 0.1453 -0.0148 0.0007  0.0020  185 LEU B N   
3618 C  CA  . LEU B 184 ? 0.1466 0.1412 0.1286 -0.0226 0.0071  -0.0076 185 LEU B CA  
3619 C  C   . LEU B 184 ? 0.1301 0.1638 0.1380 -0.0010 -0.0091 -0.0143 185 LEU B C   
3620 O  O   . LEU B 184 ? 0.1585 0.2025 0.1782 -0.0065 0.0286  -0.0522 185 LEU B O   
3621 C  CB  . LEU B 184 ? 0.1556 0.1547 0.1061 0.0027  0.0190  -0.0060 185 LEU B CB  
3622 C  CG  . LEU B 184 ? 0.1680 0.1333 0.1479 -0.0070 0.0274  0.0140  185 LEU B CG  
3623 C  CD1 . LEU B 184 ? 0.1967 0.1585 0.1518 -0.0020 0.0131  0.0219  185 LEU B CD1 
3624 C  CD2 . LEU B 184 ? 0.1800 0.1795 0.1441 -0.0256 0.0339  0.0197  185 LEU B CD2 
3625 N  N   . PRO B 185 ? 0.1444 0.1517 0.1186 -0.0241 0.0230  -0.0163 186 PRO B N   
3626 C  CA  . PRO B 185 ? 0.1310 0.1567 0.1082 -0.0278 0.0087  -0.0074 186 PRO B CA  
3627 C  C   . PRO B 185 ? 0.1920 0.1387 0.1217 0.0105  0.0348  -0.0170 186 PRO B C   
3628 O  O   . PRO B 185 ? 0.2032 0.1619 0.1226 -0.0238 0.0324  -0.0031 186 PRO B O   
3629 C  CB  . PRO B 185 ? 0.1678 0.1477 0.1132 -0.0357 0.0082  0.0110  186 PRO B CB  
3630 C  CG  . PRO B 185 ? 0.1556 0.1263 0.1425 -0.0236 0.0216  0.0222  186 PRO B CG  
3631 C  CD  . PRO B 185 ? 0.1319 0.1640 0.1394 0.0007  0.0226  0.0098  186 PRO B CD  
3632 N  N   . GLU B 186 ? 0.1948 0.1465 0.1252 -0.0098 0.0233  -0.0244 187 GLU B N   
3633 C  CA  . GLU B 186 ? 0.2025 0.2008 0.0961 -0.0313 0.0114  -0.0148 187 GLU B CA  
3634 C  C   . GLU B 186 ? 0.2323 0.1865 0.1179 -0.0231 0.0262  -0.0294 187 GLU B C   
3635 O  O   . GLU B 186 ? 0.3050 0.2206 0.1659 -0.0200 0.0456  0.0055  187 GLU B O   
3636 C  CB  . GLU B 186 ? 0.2563 0.1667 0.1933 -0.0038 0.0454  -0.0280 187 GLU B CB  
3637 C  CG  . GLU B 186 ? 0.2822 0.2224 0.2782 -0.0071 0.0295  -0.0509 187 GLU B CG  
3638 C  CD  . GLU B 186 ? 0.2714 0.2456 0.2084 -0.0307 0.0102  -0.0372 187 GLU B CD  
3639 O  OE1 . GLU B 186 ? 0.2831 0.2527 0.2330 0.0086  0.0109  -0.0826 187 GLU B OE1 
3640 O  OE2 . GLU B 186 ? 0.3767 0.2840 0.2703 0.0531  0.0258  -0.0147 187 GLU B OE2 
3641 N  N   . SER B 187 ? 0.1932 0.1903 0.1172 -0.0171 0.0309  -0.0082 188 SER B N   
3642 C  CA  . SER B 187 ? 0.2118 0.1712 0.1651 -0.0239 0.0471  0.0030  188 SER B CA  
3643 C  C   . SER B 187 ? 0.2283 0.1544 0.1445 -0.0137 0.0034  -0.0071 188 SER B C   
3644 O  O   . SER B 187 ? 0.2124 0.1957 0.1520 -0.0121 0.0219  0.0188  188 SER B O   
3645 C  CB  . SER B 187 ? 0.1903 0.2141 0.1213 -0.0386 -0.0020 -0.0190 188 SER B CB  
3646 O  OG  . SER B 187 ? 0.2148 0.1987 0.1660 -0.0271 0.0085  -0.0226 188 SER B OG  
3647 N  N   . LEU B 188 ? 0.1931 0.1671 0.1075 -0.0249 0.0189  -0.0005 189 LEU B N   
3648 C  CA  . LEU B 188 ? 0.2172 0.1601 0.1588 0.0020  0.0063  -0.0104 189 LEU B CA  
3649 C  C   . LEU B 188 ? 0.1881 0.1571 0.1028 0.0187  0.0020  0.0032  189 LEU B C   
3650 O  O   . LEU B 188 ? 0.2333 0.1998 0.1650 0.0329  0.0155  -0.0219 189 LEU B O   
3651 C  CB  . LEU B 188 ? 0.3025 0.2113 0.1432 -0.0099 0.0193  -0.0030 189 LEU B CB  
3652 C  CG  . LEU B 188 ? 0.3136 0.2098 0.1538 -0.0157 0.0126  0.0329  189 LEU B CG  
3653 C  CD1 . LEU B 188 ? 0.3542 0.1904 0.1949 -0.0120 0.1124  0.0081  189 LEU B CD1 
3654 C  CD2 . LEU B 188 ? 0.1850 0.2379 0.1459 -0.0104 0.0051  -0.0082 189 LEU B CD2 
3655 N  N   . ASP B 189 ? 0.1953 0.1831 0.1050 -0.0368 0.0093  -0.0082 190 ASP B N   
3656 C  CA  . ASP B 189 ? 0.2120 0.1956 0.1150 -0.0012 -0.0132 -0.0340 190 ASP B CA  
3657 C  C   . ASP B 189 ? 0.1522 0.1331 0.1252 0.0177  0.0083  0.0070  190 ASP B C   
3658 O  O   . ASP B 189 ? 0.1601 0.1371 0.1337 0.0082  -0.0104 0.0104  190 ASP B O   
3659 C  CB  . ASP B 189 ? 0.2806 0.2158 0.2134 -0.0171 -0.0571 -0.0639 190 ASP B CB  
3660 C  CG  . ASP B 189 ? 0.2912 0.3389 0.2633 0.0364  -0.0449 -0.0221 190 ASP B CG  
3661 O  OD1 . ASP B 189 ? 0.4368 0.4009 0.1263 0.0236  -0.0474 -0.0428 190 ASP B OD1 
3662 O  OD2 . ASP B 189 ? 0.3894 0.4733 0.2391 -0.0270 -0.0355 -0.1456 190 ASP B OD2 
3663 N  N   . TYR B 190 ? 0.1439 0.1445 0.0931 0.0054  -0.0127 0.0015  191 TYR B N   
3664 C  CA  . TYR B 190 ? 0.1509 0.1409 0.1023 -0.0062 0.0059  -0.0261 191 TYR B CA  
3665 C  C   . TYR B 190 ? 0.1341 0.1335 0.1230 -0.0046 -0.0201 -0.0140 191 TYR B C   
3666 O  O   . TYR B 190 ? 0.1380 0.1493 0.1172 -0.0086 -0.0274 -0.0092 191 TYR B O   
3667 C  CB  . TYR B 190 ? 0.1563 0.1221 0.1535 0.0126  -0.0247 -0.0260 191 TYR B CB  
3668 C  CG  . TYR B 190 ? 0.1357 0.1195 0.1466 -0.0149 -0.0113 -0.0153 191 TYR B CG  
3669 C  CD1 . TYR B 190 ? 0.1396 0.1702 0.1414 0.0037  -0.0249 -0.0256 191 TYR B CD1 
3670 C  CD2 . TYR B 190 ? 0.1483 0.1387 0.1382 -0.0168 -0.0500 0.0010  191 TYR B CD2 
3671 C  CE1 . TYR B 190 ? 0.1808 0.1425 0.1513 -0.0037 -0.0228 -0.0153 191 TYR B CE1 
3672 C  CE2 . TYR B 190 ? 0.1923 0.1439 0.1693 0.0065  -0.0324 -0.0007 191 TYR B CE2 
3673 C  CZ  . TYR B 190 ? 0.1832 0.1482 0.1931 -0.0078 -0.0414 -0.0119 191 TYR B CZ  
3674 O  OH  . TYR B 190 ? 0.2266 0.1475 0.2186 0.0186  -0.0450 0.0024  191 TYR B OH  
3675 N  N   . TRP B 191 ? 0.1369 0.1008 0.1172 -0.0032 -0.0068 -0.0109 192 TRP B N   
3676 C  CA  . TRP B 191 ? 0.1303 0.1240 0.1006 -0.0071 -0.0146 -0.0024 192 TRP B CA  
3677 C  C   . TRP B 191 ? 0.0841 0.1120 0.1208 -0.0006 -0.0177 -0.0041 192 TRP B C   
3678 O  O   . TRP B 191 ? 0.1130 0.1369 0.1450 -0.0092 -0.0331 -0.0092 192 TRP B O   
3679 C  CB  . TRP B 191 ? 0.1595 0.1270 0.1202 -0.0006 -0.0184 0.0003  192 TRP B CB  
3680 C  CG  . TRP B 191 ? 0.1194 0.1116 0.1308 -0.0133 -0.0201 0.0293  192 TRP B CG  
3681 C  CD1 . TRP B 191 ? 0.1377 0.1277 0.1301 -0.0048 -0.0214 -0.0020 192 TRP B CD1 
3682 C  CD2 . TRP B 191 ? 0.1262 0.1233 0.1337 -0.0086 -0.0115 0.0074  192 TRP B CD2 
3683 N  NE1 . TRP B 191 ? 0.1847 0.1272 0.1439 -0.0206 -0.0051 -0.0006 192 TRP B NE1 
3684 C  CE2 . TRP B 191 ? 0.1615 0.1168 0.1567 -0.0131 -0.0035 0.0127  192 TRP B CE2 
3685 C  CE3 . TRP B 191 ? 0.1353 0.1398 0.1206 -0.0040 -0.0131 0.0164  192 TRP B CE3 
3686 C  CZ2 . TRP B 191 ? 0.1680 0.1208 0.1465 -0.0178 -0.0065 -0.0005 192 TRP B CZ2 
3687 C  CZ3 . TRP B 191 ? 0.1743 0.1498 0.0929 0.0099  0.0055  0.0206  192 TRP B CZ3 
3688 C  CH2 . TRP B 191 ? 0.1574 0.1427 0.1461 -0.0076 0.0287  0.0230  192 TRP B CH2 
3689 N  N   . THR B 192 ? 0.1084 0.1030 0.0998 0.0035  -0.0142 0.0001  193 THR B N   
3690 C  CA  . THR B 192 ? 0.1138 0.1237 0.0969 -0.0276 -0.0010 -0.0006 193 THR B CA  
3691 C  C   . THR B 192 ? 0.1021 0.1127 0.1080 -0.0003 -0.0210 0.0038  193 THR B C   
3692 O  O   . THR B 192 ? 0.1042 0.1349 0.1389 -0.0109 -0.0237 0.0068  193 THR B O   
3693 C  CB  . THR B 192 ? 0.0956 0.1186 0.1111 -0.0043 -0.0286 0.0171  193 THR B CB  
3694 O  OG1 . THR B 192 ? 0.1358 0.1066 0.1299 -0.0127 -0.0254 0.0135  193 THR B OG1 
3695 C  CG2 . THR B 192 ? 0.1211 0.1655 0.1308 -0.0060 -0.0524 0.0236  193 THR B CG2 
3696 N  N   . TYR B 193 ? 0.1199 0.1035 0.1177 0.0141  -0.0074 -0.0085 194 TYR B N   
3697 C  CA  . TYR B 193 ? 0.1195 0.1107 0.1215 -0.0140 0.0141  -0.0129 194 TYR B CA  
3698 C  C   . TYR B 193 ? 0.0913 0.1048 0.1188 0.0000  0.0063  0.0131  194 TYR B C   
3699 O  O   . TYR B 193 ? 0.0931 0.1212 0.1215 -0.0049 -0.0199 0.0097  194 TYR B O   
3700 C  CB  . TYR B 193 ? 0.1231 0.1203 0.1149 -0.0040 -0.0250 0.0168  194 TYR B CB  
3701 C  CG  . TYR B 193 ? 0.1103 0.1018 0.1224 -0.0063 -0.0118 0.0031  194 TYR B CG  
3702 C  CD1 . TYR B 193 ? 0.1086 0.1082 0.1238 -0.0220 0.0055  0.0183  194 TYR B CD1 
3703 C  CD2 . TYR B 193 ? 0.1221 0.0926 0.1163 0.0097  0.0010  0.0273  194 TYR B CD2 
3704 C  CE1 . TYR B 193 ? 0.1313 0.0987 0.1042 -0.0230 -0.0141 0.0144  194 TYR B CE1 
3705 C  CE2 . TYR B 193 ? 0.1195 0.1124 0.1217 -0.0031 -0.0038 -0.0076 194 TYR B CE2 
3706 C  CZ  . TYR B 193 ? 0.1075 0.0913 0.1156 0.0007  0.0066  0.0135  194 TYR B CZ  
3707 O  OH  . TYR B 193 ? 0.1015 0.1012 0.1046 0.0038  0.0046  0.0063  194 TYR B OH  
3708 N  N   . PRO B 194 ? 0.1150 0.1279 0.0998 0.0118  -0.0003 0.0000  195 PRO B N   
3709 C  CA  . PRO B 194 ? 0.1278 0.1032 0.1140 0.0261  -0.0065 0.0130  195 PRO B CA  
3710 C  C   . PRO B 194 ? 0.1154 0.0985 0.0939 0.0060  0.0054  0.0013  195 PRO B C   
3711 O  O   . PRO B 194 ? 0.1240 0.1182 0.1411 -0.0043 -0.0024 0.0249  195 PRO B O   
3712 C  CB  . PRO B 194 ? 0.1246 0.1272 0.1680 0.0289  -0.0118 0.0052  195 PRO B CB  
3713 C  CG  . PRO B 194 ? 0.1120 0.1520 0.1605 0.0284  -0.0201 -0.0242 195 PRO B CG  
3714 C  CD  . PRO B 194 ? 0.1179 0.1651 0.1299 0.0127  -0.0184 -0.0148 195 PRO B CD  
3715 N  N   . GLY B 195 ? 0.1109 0.0952 0.1014 0.0049  -0.0017 0.0024  196 GLY B N   
3716 C  CA  . GLY B 195 ? 0.1021 0.1024 0.1017 0.0001  -0.0116 0.0035  196 GLY B CA  
3717 C  C   . GLY B 195 ? 0.1073 0.1012 0.0976 0.0174  -0.0108 -0.0048 196 GLY B C   
3718 O  O   . GLY B 195 ? 0.1066 0.1014 0.1186 0.0082  0.0006  0.0031  196 GLY B O   
3719 N  N   . SER B 196 ? 0.0958 0.0973 0.1017 0.0087  -0.0098 0.0109  197 SER B N   
3720 C  CA  . SER B 196 ? 0.0958 0.0987 0.0856 0.0087  -0.0080 0.0087  197 SER B CA  
3721 C  C   . SER B 196 ? 0.1039 0.0839 0.0985 -0.0024 0.0031  0.0098  197 SER B C   
3722 O  O   . SER B 196 ? 0.1030 0.1053 0.0922 0.0122  0.0065  -0.0049 197 SER B O   
3723 C  CB  . SER B 196 ? 0.1143 0.1067 0.1089 0.0049  0.0086  0.0228  197 SER B CB  
3724 O  OG  . SER B 196 ? 0.1037 0.1136 0.1000 0.0185  0.0046  0.0141  197 SER B OG  
3725 N  N   . LEU B 197 ? 0.1003 0.1009 0.0802 0.0089  0.0021  0.0027  198 LEU B N   
3726 C  CA  . LEU B 197 ? 0.1039 0.0883 0.1120 0.0131  -0.0003 -0.0082 198 LEU B CA  
3727 C  C   . LEU B 197 ? 0.1228 0.0996 0.0745 0.0109  0.0159  -0.0104 198 LEU B C   
3728 O  O   . LEU B 197 ? 0.1035 0.1044 0.0953 0.0098  0.0082  -0.0008 198 LEU B O   
3729 C  CB  . LEU B 197 ? 0.1511 0.1287 0.1058 0.0019  -0.0220 0.0049  198 LEU B CB  
3730 C  CG  . LEU B 197 ? 0.1220 0.1150 0.1200 0.0099  -0.0065 -0.0126 198 LEU B CG  
3731 C  CD1 . LEU B 197 ? 0.1590 0.1401 0.1473 -0.0059 -0.0125 -0.0331 198 LEU B CD1 
3732 C  CD2 . LEU B 197 ? 0.1560 0.1518 0.1145 -0.0103 -0.0059 0.0103  198 LEU B CD2 
3733 N  N   . THR B 198 ? 0.1046 0.1015 0.0899 0.0024  0.0085  -0.0099 199 THR B N   
3734 C  CA  . THR B 198 ? 0.1109 0.1018 0.1079 -0.0034 0.0068  0.0034  199 THR B CA  
3735 C  C   . THR B 198 ? 0.1292 0.0983 0.0978 -0.0020 0.0252  -0.0008 199 THR B C   
3736 O  O   . THR B 198 ? 0.1290 0.1161 0.0908 0.0010  0.0174  0.0031  199 THR B O   
3737 C  CB  . THR B 198 ? 0.0936 0.1059 0.1075 0.0122  0.0074  0.0030  199 THR B CB  
3738 O  OG1 . THR B 198 ? 0.0939 0.0951 0.0878 -0.0062 0.0087  0.0038  199 THR B OG1 
3739 C  CG2 . THR B 198 ? 0.1062 0.1044 0.1181 0.0007  -0.0153 0.0078  199 THR B CG2 
3740 N  N   . THR B 199 ? 0.1270 0.1182 0.1019 0.0006  -0.0125 -0.0093 200 THR B N   
3741 C  CA  . THR B 199 ? 0.1472 0.1076 0.1212 0.0197  -0.0307 -0.0089 200 THR B CA  
3742 C  C   . THR B 199 ? 0.1274 0.1292 0.1040 0.0088  0.0043  -0.0167 200 THR B C   
3743 O  O   . THR B 199 ? 0.1520 0.1362 0.1082 0.0208  0.0035  -0.0102 200 THR B O   
3744 C  CB  . THR B 199 ? 0.1516 0.1899 0.1271 0.0452  -0.0167 -0.0094 200 THR B CB  
3745 O  OG1 . THR B 199 ? 0.1746 0.1969 0.2339 -0.0041 0.0078  0.0015  200 THR B OG1 
3746 C  CG2 . THR B 199 ? 0.1482 0.1423 0.1811 0.0269  0.0071  -0.0122 200 THR B CG2 
3747 N  N   . PRO B 200 ? 0.1497 0.1310 0.1066 0.0219  -0.0017 -0.0121 201 PRO B N   
3748 C  CA  . PRO B 200 ? 0.1739 0.1348 0.1335 0.0109  -0.0035 -0.0226 201 PRO B CA  
3749 C  C   . PRO B 200 ? 0.1373 0.1466 0.1459 0.0148  -0.0091 -0.0110 201 PRO B C   
3750 O  O   . PRO B 200 ? 0.1551 0.1798 0.1545 0.0099  -0.0020 0.0181  201 PRO B O   
3751 C  CB  . PRO B 200 ? 0.1387 0.1646 0.1190 0.0173  0.0109  0.0076  201 PRO B CB  
3752 C  CG  . PRO B 200 ? 0.1705 0.1725 0.1220 0.0114  -0.0012 -0.0198 201 PRO B CG  
3753 C  CD  . PRO B 200 ? 0.1538 0.1371 0.1127 0.0195  -0.0157 0.0013  201 PRO B CD  
3754 N  N   . PRO B 201 ? 0.1418 0.1488 0.1286 0.0046  -0.0005 -0.0219 202 PRO B N   
3755 C  CA  . PRO B 201 ? 0.1360 0.1369 0.1705 0.0023  0.0065  -0.0115 202 PRO B CA  
3756 C  C   . PRO B 201 ? 0.1412 0.1705 0.1319 0.0142  0.0070  -0.0065 202 PRO B C   
3757 O  O   . PRO B 201 ? 0.1483 0.1420 0.1536 0.0119  0.0131  -0.0219 202 PRO B O   
3758 C  CB  . PRO B 201 ? 0.1847 0.1360 0.1911 -0.0065 -0.0138 -0.0340 202 PRO B CB  
3759 C  CG  . PRO B 201 ? 0.1874 0.1653 0.2303 0.0176  0.0227  -0.0372 202 PRO B CG  
3760 C  CD  . PRO B 201 ? 0.1635 0.1522 0.2127 -0.0023 -0.0153 -0.0074 202 PRO B CD  
3761 N  N   . LEU B 202 ? 0.1270 0.1136 0.1028 -0.0070 -0.0040 0.0062  203 LEU B N   
3762 C  CA  . LEU B 202 ? 0.1030 0.1032 0.1165 -0.0017 0.0065  0.0013  203 LEU B CA  
3763 C  C   . LEU B 202 ? 0.1305 0.1181 0.1229 0.0104  0.0035  -0.0031 203 LEU B C   
3764 O  O   . LEU B 202 ? 0.1256 0.1150 0.1418 0.0110  0.0196  0.0074  203 LEU B O   
3765 C  CB  . LEU B 202 ? 0.1185 0.1359 0.0906 0.0211  0.0313  0.0062  203 LEU B CB  
3766 C  CG  . LEU B 202 ? 0.1464 0.1272 0.0842 0.0342  0.0278  0.0074  203 LEU B CG  
3767 C  CD1 . LEU B 202 ? 0.1847 0.1754 0.0985 0.0044  0.0414  0.0118  203 LEU B CD1 
3768 C  CD2 . LEU B 202 ? 0.1511 0.1077 0.1202 0.0215  0.0248  0.0086  203 LEU B CD2 
3769 N  N   . LEU B 203 ? 0.1375 0.1156 0.1168 0.0156  0.0146  0.0076  204 LEU B N   
3770 C  CA  . LEU B 203 ? 0.1483 0.1106 0.1188 0.0142  -0.0136 -0.0111 204 LEU B CA  
3771 C  C   . LEU B 203 ? 0.1292 0.1306 0.1141 0.0132  -0.0098 0.0076  204 LEU B C   
3772 O  O   . LEU B 203 ? 0.1145 0.1204 0.1212 0.0092  0.0038  0.0023  204 LEU B O   
3773 C  CB  . LEU B 203 ? 0.1827 0.1471 0.1587 -0.0138 -0.0113 -0.0133 204 LEU B CB  
3774 C  CG  . LEU B 203 ? 0.1739 0.1592 0.1626 -0.0217 -0.0057 -0.0364 204 LEU B CG  
3775 C  CD1 . LEU B 203 ? 0.2700 0.2070 0.1574 -0.0671 -0.0458 -0.0394 204 LEU B CD1 
3776 C  CD2 . LEU B 203 ? 0.2815 0.2136 0.2019 0.0059  0.0355  -0.0425 204 LEU B CD2 
3777 N  N   . GLU B 204 ? 0.1229 0.1283 0.1231 0.0302  0.0000  0.0019  205 GLU B N   
3778 C  CA  . GLU B 204 ? 0.0985 0.1106 0.1337 0.0244  0.0000  -0.0007 205 GLU B CA  
3779 C  C   . GLU B 204 ? 0.1125 0.1046 0.1655 0.0052  -0.0008 0.0060  205 GLU B C   
3780 O  O   . GLU B 204 ? 0.1182 0.1576 0.1653 0.0322  0.0165  0.0229  205 GLU B O   
3781 C  CB  . GLU B 204 ? 0.1146 0.1360 0.1708 0.0373  0.0162  0.0142  205 GLU B CB  
3782 C  CG  . GLU B 204 ? 0.1639 0.1173 0.1818 0.0287  0.0456  0.0098  205 GLU B CG  
3783 C  CD  . GLU B 204 ? 0.1662 0.1594 0.1973 0.0163  0.0251  -0.0089 205 GLU B CD  
3784 O  OE1 . GLU B 204 ? 0.1561 0.2053 0.2330 0.0432  0.0438  0.0337  205 GLU B OE1 
3785 O  OE2 . GLU B 204 ? 0.1461 0.1633 0.1723 0.0255  0.0419  0.0020  205 GLU B OE2 
3786 N  N   . CYS B 205 ? 0.1409 0.1125 0.1124 0.0068  0.0289  0.0131  206 CYS B N   
3787 C  CA  . CYS B 205 ? 0.0992 0.1200 0.1086 -0.0052 0.0037  0.0038  206 CYS B CA  
3788 C  C   . CYS B 205 ? 0.1064 0.1046 0.1023 0.0111  0.0114  0.0100  206 CYS B C   
3789 O  O   . CYS B 205 ? 0.1294 0.1030 0.1367 -0.0049 0.0193  0.0093  206 CYS B O   
3790 C  CB  . CYS B 205 ? 0.1279 0.1215 0.1349 0.0027  -0.0046 -0.0120 206 CYS B CB  
3791 S  SG  . CYS B 205 ? 0.1310 0.1225 0.1544 0.0052  -0.0031 0.0024  206 CYS B SG  
3792 N  N   . VAL B 206 ? 0.1233 0.1009 0.1132 -0.0012 0.0119  -0.0048 207 VAL B N   
3793 C  CA  . VAL B 206 ? 0.1071 0.0820 0.1084 -0.0031 -0.0030 -0.0007 207 VAL B CA  
3794 C  C   . VAL B 206 ? 0.1068 0.0920 0.1188 0.0046  -0.0017 0.0007  207 VAL B C   
3795 O  O   . VAL B 206 ? 0.1197 0.1265 0.1383 -0.0087 -0.0034 -0.0046 207 VAL B O   
3796 C  CB  . VAL B 206 ? 0.0997 0.0962 0.0969 0.0077  -0.0005 0.0085  207 VAL B CB  
3797 C  CG1 . VAL B 206 ? 0.1179 0.1228 0.1120 0.0100  0.0255  0.0043  207 VAL B CG1 
3798 C  CG2 . VAL B 206 ? 0.1251 0.1116 0.1215 -0.0131 -0.0154 0.0110  207 VAL B CG2 
3799 N  N   . THR B 207 ? 0.1269 0.0870 0.0994 0.0135  -0.0023 -0.0017 208 THR B N   
3800 C  CA  . THR B 207 ? 0.1062 0.1032 0.1066 0.0133  -0.0076 0.0034  208 THR B CA  
3801 C  C   . THR B 207 ? 0.1001 0.0900 0.1281 -0.0019 0.0003  -0.0024 208 THR B C   
3802 O  O   . THR B 207 ? 0.0996 0.0953 0.1268 0.0005  0.0052  -0.0116 208 THR B O   
3803 C  CB  . THR B 207 ? 0.1259 0.1017 0.1030 0.0173  -0.0104 -0.0003 208 THR B CB  
3804 O  OG1 . THR B 207 ? 0.1341 0.1000 0.1330 0.0165  -0.0187 0.0115  208 THR B OG1 
3805 C  CG2 . THR B 207 ? 0.1529 0.1340 0.1116 -0.0100 -0.0133 -0.0212 208 THR B CG2 
3806 N  N   . TRP B 208 ? 0.1116 0.0854 0.1068 -0.0030 -0.0057 0.0038  209 TRP B N   
3807 C  CA  . TRP B 208 ? 0.1001 0.0883 0.0951 0.0017  0.0082  -0.0043 209 TRP B CA  
3808 C  C   . TRP B 208 ? 0.0912 0.0915 0.0866 0.0024  -0.0055 0.0109  209 TRP B C   
3809 O  O   . TRP B 208 ? 0.1037 0.0991 0.1052 0.0012  -0.0104 0.0040  209 TRP B O   
3810 C  CB  . TRP B 208 ? 0.1023 0.1098 0.0954 -0.0155 -0.0210 0.0143  209 TRP B CB  
3811 C  CG  . TRP B 208 ? 0.1033 0.1042 0.0895 -0.0034 -0.0030 0.0012  209 TRP B CG  
3812 C  CD1 . TRP B 208 ? 0.0951 0.1077 0.0812 -0.0110 0.0049  0.0059  209 TRP B CD1 
3813 C  CD2 . TRP B 208 ? 0.0987 0.0847 0.0901 0.0005  0.0024  0.0066  209 TRP B CD2 
3814 N  NE1 . TRP B 208 ? 0.1103 0.1145 0.1124 0.0181  -0.0041 0.0077  209 TRP B NE1 
3815 C  CE2 . TRP B 208 ? 0.0978 0.0836 0.0994 -0.0088 -0.0003 0.0066  209 TRP B CE2 
3816 C  CE3 . TRP B 208 ? 0.0906 0.0803 0.0951 -0.0003 0.0082  0.0189  209 TRP B CE3 
3817 C  CZ2 . TRP B 208 ? 0.0806 0.1147 0.1256 -0.0085 0.0000  0.0129  209 TRP B CZ2 
3818 C  CZ3 . TRP B 208 ? 0.1109 0.1224 0.1027 0.0121  -0.0057 0.0208  209 TRP B CZ3 
3819 C  CH2 . TRP B 208 ? 0.1134 0.0940 0.1084 0.0057  -0.0003 0.0339  209 TRP B CH2 
3820 N  N   . ILE B 209 ? 0.1075 0.0870 0.0860 0.0006  0.0017  -0.0013 210 ILE B N   
3821 C  CA  . ILE B 209 ? 0.1080 0.1159 0.0721 0.0088  0.0160  0.0020  210 ILE B CA  
3822 C  C   . ILE B 209 ? 0.1019 0.1028 0.0754 -0.0006 -0.0135 -0.0028 210 ILE B C   
3823 O  O   . ILE B 209 ? 0.1024 0.1067 0.1158 -0.0111 -0.0108 0.0013  210 ILE B O   
3824 C  CB  . ILE B 209 ? 0.1260 0.1115 0.0945 -0.0055 0.0230  0.0049  210 ILE B CB  
3825 C  CG1 . ILE B 209 ? 0.1490 0.1062 0.1448 0.0052  -0.0054 0.0308  210 ILE B CG1 
3826 C  CG2 . ILE B 209 ? 0.1606 0.1351 0.1044 -0.0220 0.0196  -0.0031 210 ILE B CG2 
3827 C  CD1 . ILE B 209 ? 0.1896 0.1324 0.1665 -0.0194 0.0172  0.0252  210 ILE B CD1 
3828 N  N   . VAL B 210 ? 0.1058 0.0951 0.0856 -0.0116 0.0017  0.0006  211 VAL B N   
3829 C  CA  . VAL B 210 ? 0.1199 0.1055 0.0979 -0.0098 0.0048  0.0040  211 VAL B CA  
3830 C  C   . VAL B 210 ? 0.0994 0.0847 0.0845 -0.0068 -0.0094 0.0148  211 VAL B C   
3831 O  O   . VAL B 210 ? 0.1158 0.1062 0.1141 -0.0006 -0.0320 0.0021  211 VAL B O   
3832 C  CB  . VAL B 210 ? 0.1272 0.1003 0.0838 -0.0118 0.0081  -0.0024 211 VAL B CB  
3833 C  CG1 . VAL B 210 ? 0.1317 0.1030 0.0917 0.0111  0.0046  -0.0063 211 VAL B CG1 
3834 C  CG2 . VAL B 210 ? 0.1261 0.1127 0.1014 0.0017  0.0232  -0.0250 211 VAL B CG2 
3835 N  N   . LEU B 211 ? 0.1240 0.1149 0.0882 0.0006  0.0060  -0.0041 212 LEU B N   
3836 C  CA  . LEU B 211 ? 0.1213 0.1118 0.0888 0.0120  -0.0013 -0.0093 212 LEU B CA  
3837 C  C   . LEU B 211 ? 0.1247 0.1054 0.1005 -0.0046 -0.0121 -0.0046 212 LEU B C   
3838 O  O   . LEU B 211 ? 0.1411 0.1277 0.0998 0.0103  0.0043  -0.0027 212 LEU B O   
3839 C  CB  . LEU B 211 ? 0.1317 0.1233 0.1021 -0.0026 0.0041  -0.0110 212 LEU B CB  
3840 C  CG  . LEU B 211 ? 0.1402 0.1147 0.1195 -0.0074 0.0189  -0.0168 212 LEU B CG  
3841 C  CD1 . LEU B 211 ? 0.1477 0.1967 0.1614 -0.0163 0.0353  -0.0086 212 LEU B CD1 
3842 C  CD2 . LEU B 211 ? 0.1597 0.1689 0.1235 -0.0019 0.0013  0.0063  212 LEU B CD2 
3843 N  N   A LYS B 212 ? 0.1249 0.1292 0.1052 -0.0181 -0.0055 -0.0262 213 LYS B N   
3844 N  N   B LYS B 212 ? 0.1217 0.1204 0.0974 -0.0132 -0.0082 -0.0120 213 LYS B N   
3845 C  CA  A LYS B 212 ? 0.1304 0.1170 0.1265 -0.0073 0.0091  -0.0054 213 LYS B CA  
3846 C  CA  B LYS B 212 ? 0.1258 0.1146 0.1003 -0.0063 -0.0078 0.0012  213 LYS B CA  
3847 C  C   A LYS B 212 ? 0.1124 0.1093 0.1308 -0.0197 -0.0211 -0.0151 213 LYS B C   
3848 C  C   B LYS B 212 ? 0.1152 0.1127 0.1211 -0.0198 -0.0104 -0.0137 213 LYS B C   
3849 O  O   A LYS B 212 ? 0.1574 0.1179 0.1199 -0.0214 -0.0137 0.0003  213 LYS B O   
3850 O  O   B LYS B 212 ? 0.1425 0.1199 0.1317 -0.0003 0.0119  -0.0008 213 LYS B O   
3851 C  CB  A LYS B 212 ? 0.1466 0.1617 0.1504 0.0203  -0.0250 -0.0131 213 LYS B CB  
3852 C  CB  B LYS B 212 ? 0.1439 0.1317 0.1017 -0.0089 -0.0223 0.0270  213 LYS B CB  
3853 C  CG  A LYS B 212 ? 0.1969 0.2000 0.2484 -0.0671 -0.0182 -0.0010 213 LYS B CG  
3854 C  CG  B LYS B 212 ? 0.1586 0.1482 0.1313 -0.0412 -0.0013 0.0284  213 LYS B CG  
3855 C  CD  A LYS B 212 ? 0.2354 0.3736 0.2278 0.0509  0.0006  -0.0351 213 LYS B CD  
3856 C  CD  B LYS B 212 ? 0.1639 0.1703 0.1931 -0.0245 -0.0197 -0.0198 213 LYS B CD  
3857 C  CE  A LYS B 212 ? 0.2463 0.3009 0.2116 -0.0280 -0.0659 0.0351  213 LYS B CE  
3858 C  CE  B LYS B 212 ? 0.2574 0.1791 0.3456 -0.0762 -0.0001 -0.0263 213 LYS B CE  
3859 N  NZ  A LYS B 212 ? 0.1852 0.1940 0.0709 0.0024  0.0003  0.0031  213 LYS B NZ  
3860 N  NZ  B LYS B 212 ? 0.4363 0.3188 0.3391 0.1071  -0.0008 -0.1097 213 LYS B NZ  
3861 N  N   . GLU B 213 ? 0.1308 0.1163 0.0958 -0.0099 0.0000  -0.0078 214 GLU B N   
3862 C  CA  . GLU B 213 ? 0.1421 0.1221 0.1155 0.0001  0.0054  0.0073  214 GLU B CA  
3863 C  C   . GLU B 213 ? 0.1120 0.1149 0.1215 0.0020  0.0054  -0.0013 214 GLU B C   
3864 O  O   . GLU B 213 ? 0.1411 0.1285 0.0965 -0.0175 0.0148  -0.0015 214 GLU B O   
3865 C  CB  . GLU B 213 ? 0.1689 0.1477 0.1064 -0.0131 0.0131  0.0007  214 GLU B CB  
3866 C  CG  . GLU B 213 ? 0.1984 0.1617 0.1611 0.0089  0.0463  -0.0077 214 GLU B CG  
3867 C  CD  . GLU B 213 ? 0.1865 0.1827 0.1278 0.0351  0.0201  -0.0379 214 GLU B CD  
3868 O  OE1 . GLU B 213 ? 0.2605 0.2048 0.1534 0.0032  0.0115  -0.0113 214 GLU B OE1 
3869 O  OE2 . GLU B 213 ? 0.2727 0.4050 0.2764 0.0597  0.0562  -0.0275 214 GLU B OE2 
3870 N  N   . PRO B 214 ? 0.1251 0.0996 0.1009 -0.0077 0.0063  -0.0049 215 PRO B N   
3871 C  CA  . PRO B 214 ? 0.1235 0.0996 0.1098 0.0006  -0.0020 0.0086  215 PRO B CA  
3872 C  C   . PRO B 214 ? 0.1265 0.1332 0.1118 0.0006  0.0076  -0.0049 215 PRO B C   
3873 O  O   . PRO B 214 ? 0.1509 0.1611 0.1267 -0.0176 0.0259  -0.0240 215 PRO B O   
3874 C  CB  . PRO B 214 ? 0.1754 0.1059 0.1484 0.0038  0.0274  0.0074  215 PRO B CB  
3875 C  CG  . PRO B 214 ? 0.2549 0.1558 0.1504 -0.0132 -0.0322 0.0211  215 PRO B CG  
3876 C  CD  . PRO B 214 ? 0.1762 0.1088 0.1283 -0.0318 -0.0194 -0.0068 215 PRO B CD  
3877 N  N   . ILE B 215 ? 0.0976 0.1179 0.1249 0.0070  0.0023  -0.0013 216 ILE B N   
3878 C  CA  . ILE B 215 ? 0.1010 0.1200 0.1307 0.0107  0.0060  -0.0074 216 ILE B CA  
3879 C  C   . ILE B 215 ? 0.1464 0.1218 0.1298 0.0076  0.0351  0.0113  216 ILE B C   
3880 O  O   . ILE B 215 ? 0.1516 0.1179 0.1195 0.0141  0.0221  0.0104  216 ILE B O   
3881 C  CB  . ILE B 215 ? 0.1427 0.1310 0.1212 -0.0131 0.0054  0.0100  216 ILE B CB  
3882 C  CG1 . ILE B 215 ? 0.1533 0.1158 0.1321 0.0077  0.0125  -0.0049 216 ILE B CG1 
3883 C  CG2 . ILE B 215 ? 0.1565 0.1221 0.1513 0.0118  0.0172  0.0098  216 ILE B CG2 
3884 C  CD1 . ILE B 215 ? 0.1391 0.1368 0.1660 -0.0015 0.0182  0.0142  216 ILE B CD1 
3885 N  N   . SER B 216 ? 0.0642 0.0562 0.0669 -0.0091 0.0052  0.0060  217 SER B N   
3886 C  CA  . SER B 216 ? 0.0705 0.0672 0.0424 -0.0052 0.0094  0.0065  217 SER B CA  
3887 C  C   . SER B 216 ? 0.0571 0.0340 0.0815 0.0114  0.0098  -0.0120 217 SER B C   
3888 O  O   . SER B 216 ? 0.0582 0.0522 0.0718 0.0124  0.0137  -0.0041 217 SER B O   
3889 C  CB  . SER B 216 ? 0.1049 0.0415 0.1075 0.0135  -0.0147 -0.0132 217 SER B CB  
3890 O  OG  . SER B 216 ? 0.1123 0.1659 0.1457 -0.0104 -0.0038 -0.0189 217 SER B OG  
3891 N  N   . VAL B 217 ? 0.1161 0.1150 0.1218 0.0126  0.0010  -0.0082 218 VAL B N   
3892 C  CA  . VAL B 217 ? 0.1419 0.0983 0.1278 -0.0041 -0.0120 -0.0206 218 VAL B CA  
3893 C  C   . VAL B 217 ? 0.1177 0.1203 0.1243 0.0078  0.0012  0.0015  218 VAL B C   
3894 O  O   . VAL B 217 ? 0.1220 0.1121 0.1322 0.0153  0.0207  -0.0126 218 VAL B O   
3895 C  CB  . VAL B 217 ? 0.1513 0.1105 0.1190 0.0166  0.0197  -0.0093 218 VAL B CB  
3896 C  CG1 . VAL B 217 ? 0.1856 0.1076 0.1421 0.0107  0.0115  0.0054  218 VAL B CG1 
3897 C  CG2 . VAL B 217 ? 0.1791 0.1146 0.1416 0.0144  0.0366  0.0141  218 VAL B CG2 
3898 N  N   . SER B 218 ? 0.1158 0.1226 0.1312 0.0143  0.0177  -0.0044 219 SER B N   
3899 C  CA  . SER B 218 ? 0.1613 0.1059 0.1500 0.0203  0.0178  -0.0020 219 SER B CA  
3900 C  C   . SER B 218 ? 0.1403 0.1075 0.1360 -0.0074 0.0104  -0.0083 219 SER B C   
3901 O  O   . SER B 218 ? 0.1252 0.1136 0.1427 0.0054  0.0086  -0.0153 219 SER B O   
3902 C  CB  . SER B 218 ? 0.1306 0.1316 0.1457 0.0065  0.0074  -0.0054 219 SER B CB  
3903 O  OG  . SER B 218 ? 0.1533 0.1608 0.1642 0.0208  0.0049  -0.0197 219 SER B OG  
3904 N  N   A SER B 219 ? 0.1416 0.1172 0.1594 0.0124  0.0266  0.0262  220 SER B N   
3905 N  N   B SER B 219 ? 0.1337 0.1154 0.1498 0.0088  0.0197  0.0143  220 SER B N   
3906 C  CA  A SER B 219 ? 0.1723 0.1093 0.1427 -0.0010 0.0133  -0.0121 220 SER B CA  
3907 C  CA  B SER B 219 ? 0.1705 0.1133 0.1468 0.0038  0.0078  -0.0052 220 SER B CA  
3908 C  C   A SER B 219 ? 0.1554 0.1111 0.1289 0.0093  0.0082  0.0078  220 SER B C   
3909 C  C   B SER B 219 ? 0.1619 0.1089 0.1482 0.0026  0.0153  0.0071  220 SER B C   
3910 O  O   A SER B 219 ? 0.1838 0.1538 0.1066 -0.0003 0.0092  -0.0080 220 SER B O   
3911 O  O   B SER B 219 ? 0.1536 0.1279 0.1283 0.0006  -0.0198 -0.0066 220 SER B O   
3912 C  CB  A SER B 219 ? 0.1981 0.1136 0.1655 0.0185  0.0162  0.0311  220 SER B CB  
3913 C  CB  B SER B 219 ? 0.2086 0.1152 0.1971 0.0196  0.0219  0.0063  220 SER B CB  
3914 O  OG  A SER B 219 ? 0.1481 0.1033 0.2036 0.0181  -0.0465 0.0054  220 SER B OG  
3915 O  OG  B SER B 219 ? 0.2179 0.1987 0.1940 0.0225  -0.0024 0.0046  220 SER B OG  
3916 N  N   . GLU B 220 ? 0.1569 0.1283 0.1226 0.0153  0.0017  0.0173  221 GLU B N   
3917 C  CA  . GLU B 220 ? 0.1782 0.1532 0.1676 0.0043  0.0082  0.0103  221 GLU B CA  
3918 C  C   . GLU B 220 ? 0.1517 0.1306 0.1358 0.0028  0.0043  -0.0044 221 GLU B C   
3919 O  O   . GLU B 220 ? 0.1781 0.1499 0.1527 0.0313  -0.0344 0.0000  221 GLU B O   
3920 C  CB  . GLU B 220 ? 0.1779 0.1691 0.2178 0.0408  0.0124  0.0135  221 GLU B CB  
3921 C  CG  . GLU B 220 ? 0.2382 0.1784 0.2851 0.0729  -0.0024 -0.0126 221 GLU B CG  
3922 C  CD  . GLU B 220 ? 0.2840 0.2400 0.2409 0.1085  0.0162  -0.0274 221 GLU B CD  
3923 O  OE1 . GLU B 220 ? 0.2978 0.1942 0.2251 0.0983  0.0221  -0.0152 221 GLU B OE1 
3924 O  OE2 . GLU B 220 ? 0.5080 0.2628 0.4844 0.1767  -0.0663 -0.0485 221 GLU B OE2 
3925 N  N   . GLN B 221 ? 0.1328 0.1225 0.1331 0.0059  0.0299  0.0060  222 GLN B N   
3926 C  CA  . GLN B 221 ? 0.1565 0.1097 0.1199 -0.0038 0.0326  -0.0103 222 GLN B CA  
3927 C  C   . GLN B 221 ? 0.1331 0.1254 0.1097 -0.0133 0.0087  -0.0034 222 GLN B C   
3928 O  O   . GLN B 221 ? 0.1590 0.1332 0.1335 -0.0041 0.0000  -0.0252 222 GLN B O   
3929 C  CB  . GLN B 221 ? 0.1495 0.1349 0.1100 0.0194  0.0149  -0.0094 222 GLN B CB  
3930 C  CG  . GLN B 221 ? 0.1231 0.1669 0.1252 0.0082  0.0156  -0.0104 222 GLN B CG  
3931 C  CD  . GLN B 221 ? 0.1159 0.1094 0.1615 0.0219  -0.0063 -0.0102 222 GLN B CD  
3932 O  OE1 . GLN B 221 ? 0.1167 0.1342 0.1344 -0.0017 0.0098  0.0066  222 GLN B OE1 
3933 N  NE2 . GLN B 221 ? 0.1149 0.1134 0.1437 0.0076  0.0049  -0.0070 222 GLN B NE2 
3934 N  N   . VAL B 222 ? 0.1244 0.1368 0.1507 -0.0137 0.0226  -0.0190 223 VAL B N   
3935 C  CA  . VAL B 222 ? 0.1463 0.1409 0.1364 -0.0099 0.0252  -0.0163 223 VAL B CA  
3936 C  C   . VAL B 222 ? 0.1669 0.1231 0.1529 -0.0087 0.0093  -0.0024 223 VAL B C   
3937 O  O   . VAL B 222 ? 0.1477 0.1506 0.1369 -0.0097 0.0000  -0.0219 223 VAL B O   
3938 C  CB  . VAL B 222 ? 0.1500 0.1971 0.2041 -0.0138 0.0275  -0.0196 223 VAL B CB  
3939 C  CG1 . VAL B 222 ? 0.2442 0.1928 0.1748 0.0087  0.0283  -0.0383 223 VAL B CG1 
3940 C  CG2 . VAL B 222 ? 0.2222 0.2111 0.1538 0.0046  0.0760  0.0265  223 VAL B CG2 
3941 N  N   . LEU B 223 ? 0.1708 0.1389 0.1597 -0.0046 0.0000  0.0194  224 LEU B N   
3942 C  CA  . LEU B 223 ? 0.2053 0.1680 0.1387 0.0007  0.0086  0.0198  224 LEU B CA  
3943 C  C   . LEU B 223 ? 0.1802 0.1890 0.1594 0.0232  0.0031  0.0010  224 LEU B C   
3944 O  O   . LEU B 223 ? 0.1868 0.1831 0.1443 0.0195  0.0054  0.0049  224 LEU B O   
3945 C  CB  . LEU B 223 ? 0.2881 0.1750 0.2041 0.0381  0.0081  0.0070  224 LEU B CB  
3946 C  CG  . LEU B 223 ? 0.2691 0.2373 0.2192 -0.0017 0.0388  -0.0153 224 LEU B CG  
3947 C  CD1 . LEU B 223 ? 0.2815 0.2822 0.3050 0.0745  0.0194  -0.0131 224 LEU B CD1 
3948 C  CD2 . LEU B 223 ? 0.3348 0.2220 0.2809 0.0337  -0.0015 0.0640  224 LEU B CD2 
3949 N  N   . LYS B 224 ? 0.1405 0.1493 0.1683 0.0065  0.0076  -0.0142 225 LYS B N   
3950 C  CA  . LYS B 224 ? 0.2050 0.1739 0.1459 -0.0027 -0.0088 0.0146  225 LYS B CA  
3951 C  C   . LYS B 224 ? 0.1438 0.1541 0.1526 -0.0157 -0.0171 0.0105  225 LYS B C   
3952 O  O   . LYS B 224 ? 0.1489 0.1730 0.1621 0.0035  -0.0283 -0.0248 225 LYS B O   
3953 C  CB  . LYS B 224 ? 0.1883 0.2393 0.1888 -0.0233 0.0144  -0.0178 225 LYS B CB  
3954 C  CG  . LYS B 224 ? 0.2231 0.2682 0.2549 0.0366  0.0518  -0.0562 225 LYS B CG  
3955 C  CD  . LYS B 224 ? 0.2754 0.2784 0.3939 -0.0115 0.0847  -0.0551 225 LYS B CD  
3956 C  CE  . LYS B 224 ? 0.2608 0.3747 0.3673 0.0630  0.0410  0.0094  225 LYS B CE  
3957 N  NZ  . LYS B 224 ? 0.3926 0.3594 0.3538 0.1085  0.0744  -0.0013 225 LYS B NZ  
3958 N  N   . PHE B 225 ? 0.1360 0.1269 0.1483 0.0024  0.0060  0.0087  226 PHE B N   
3959 C  CA  . PHE B 225 ? 0.1161 0.1595 0.1398 0.0013  -0.0073 -0.0083 226 PHE B CA  
3960 C  C   . PHE B 225 ? 0.1204 0.1331 0.1411 -0.0076 -0.0071 -0.0175 226 PHE B C   
3961 O  O   . PHE B 225 ? 0.1492 0.1393 0.1306 0.0335  -0.0267 -0.0030 226 PHE B O   
3962 C  CB  . PHE B 225 ? 0.1272 0.1298 0.1242 0.0006  -0.0188 -0.0060 226 PHE B CB  
3963 C  CG  . PHE B 225 ? 0.1498 0.1331 0.1278 0.0119  0.0159  -0.0080 226 PHE B CG  
3964 C  CD1 . PHE B 225 ? 0.1692 0.2125 0.1480 -0.0308 0.0015  0.0289  226 PHE B CD1 
3965 C  CD2 . PHE B 225 ? 0.1702 0.2231 0.1818 0.0357  0.0037  0.0121  226 PHE B CD2 
3966 C  CE1 . PHE B 225 ? 0.2136 0.1969 0.1292 0.0266  -0.0026 0.0057  226 PHE B CE1 
3967 C  CE2 . PHE B 225 ? 0.2150 0.2157 0.1605 0.0590  0.0322  0.0329  226 PHE B CE2 
3968 C  CZ  . PHE B 225 ? 0.1890 0.1806 0.2287 0.0142  0.0340  -0.0269 226 PHE B CZ  
3969 N  N   . ARG B 226 ? 0.1328 0.1407 0.1263 -0.0131 -0.0105 0.0052  227 ARG B N   
3970 C  CA  . ARG B 226 ? 0.1224 0.1502 0.1242 0.0017  0.0048  0.0008  227 ARG B CA  
3971 C  C   . ARG B 226 ? 0.1391 0.1703 0.1516 0.0099  -0.0020 -0.0179 227 ARG B C   
3972 O  O   . ARG B 226 ? 0.1885 0.1750 0.1411 -0.0162 -0.0098 -0.0081 227 ARG B O   
3973 C  CB  . ARG B 226 ? 0.1369 0.1344 0.1784 -0.0088 -0.0052 0.0000  227 ARG B CB  
3974 C  CG  . ARG B 226 ? 0.1222 0.1477 0.1538 0.0006  -0.0077 -0.0118 227 ARG B CG  
3975 C  CD  . ARG B 226 ? 0.1493 0.1601 0.2148 -0.0073 -0.0403 -0.0198 227 ARG B CD  
3976 N  NE  . ARG B 226 ? 0.1531 0.1614 0.1703 -0.0013 -0.0019 -0.0285 227 ARG B NE  
3977 C  CZ  . ARG B 226 ? 0.1416 0.1249 0.1887 0.0208  -0.0248 -0.0121 227 ARG B CZ  
3978 N  NH1 . ARG B 226 ? 0.1854 0.1832 0.2194 0.0830  0.0003  -0.0188 227 ARG B NH1 
3979 N  NH2 . ARG B 226 ? 0.1533 0.1612 0.1808 0.0057  -0.0269 -0.0531 227 ARG B NH2 
3980 N  N   . LYS B 227 ? 0.1340 0.1676 0.1560 0.0024  -0.0188 0.0060  228 LYS B N   
3981 C  CA  . LYS B 227 ? 0.1578 0.1793 0.1727 0.0353  -0.0423 -0.0188 228 LYS B CA  
3982 C  C   . LYS B 227 ? 0.1425 0.1380 0.1709 0.0052  -0.0476 0.0162  228 LYS B C   
3983 O  O   . LYS B 227 ? 0.1544 0.1870 0.1687 0.0153  -0.0582 -0.0171 228 LYS B O   
3984 C  CB  . LYS B 227 ? 0.1348 0.2073 0.2206 0.0270  -0.0242 -0.0103 228 LYS B CB  
3985 C  CG  . LYS B 227 ? 0.2086 0.2129 0.2750 0.0423  -0.0142 -0.0297 228 LYS B CG  
3986 C  CD  . LYS B 227 ? 0.3203 0.4240 0.3474 0.1739  0.0511  -0.0355 228 LYS B CD  
3987 C  CE  . LYS B 227 ? 0.4291 0.6491 0.4095 0.1120  -0.0537 -0.1548 228 LYS B CE  
3988 N  NZ  . LYS B 227 ? 0.4485 0.6245 0.7455 0.1676  0.0678  -0.1264 228 LYS B NZ  
3989 N  N   . LEU B 228 ? 0.1423 0.1375 0.1495 0.0209  -0.0245 -0.0006 229 LEU B N   
3990 C  CA  . LEU B 228 ? 0.1263 0.1464 0.1391 0.0276  -0.0107 0.0020  229 LEU B CA  
3991 C  C   . LEU B 228 ? 0.1222 0.1301 0.1377 0.0162  -0.0300 0.0013  229 LEU B C   
3992 O  O   . LEU B 228 ? 0.1391 0.1489 0.1638 0.0126  -0.0242 0.0148  229 LEU B O   
3993 C  CB  . LEU B 228 ? 0.1195 0.1527 0.1317 0.0197  -0.0197 -0.0003 229 LEU B CB  
3994 C  CG  . LEU B 228 ? 0.1495 0.1723 0.1296 -0.0089 -0.0254 0.0027  229 LEU B CG  
3995 C  CD1 . LEU B 228 ? 0.1610 0.1586 0.1455 0.0498  -0.0238 -0.0063 229 LEU B CD1 
3996 C  CD2 . LEU B 228 ? 0.1829 0.1619 0.2230 -0.0272 -0.0520 0.0066  229 LEU B CD2 
3997 N  N   . ASN B 229 ? 0.1565 0.1678 0.1213 0.0298  -0.0326 -0.0272 230 ASN B N   
3998 C  CA  . ASN B 229 ? 0.1356 0.1606 0.1249 0.0231  -0.0241 -0.0124 230 ASN B CA  
3999 C  C   . ASN B 229 ? 0.1640 0.1518 0.1369 -0.0030 -0.0065 -0.0118 230 ASN B C   
4000 O  O   . ASN B 229 ? 0.1699 0.1689 0.1498 -0.0070 -0.0182 -0.0038 230 ASN B O   
4001 C  CB  . ASN B 229 ? 0.1502 0.1845 0.1279 0.0017  -0.0438 -0.0046 230 ASN B CB  
4002 C  CG  . ASN B 229 ? 0.1796 0.1899 0.2360 0.0035  -0.0658 -0.0052 230 ASN B CG  
4003 O  OD1 . ASN B 229 ? 0.2138 0.2653 0.2617 -0.0138 -0.0811 0.0085  230 ASN B OD1 
4004 N  ND2 . ASN B 229 ? 0.1693 0.1969 0.1851 0.0414  -0.0626 0.0060  230 ASN B ND2 
4005 N  N   . PHE B 230 ? 0.1380 0.1799 0.1172 0.0309  -0.0221 -0.0248 231 PHE B N   
4006 C  CA  . PHE B 230 ? 0.1538 0.1741 0.1382 0.0046  -0.0133 -0.0511 231 PHE B CA  
4007 C  C   . PHE B 230 ? 0.1732 0.2204 0.1551 0.0082  -0.0465 -0.0211 231 PHE B C   
4008 O  O   . PHE B 230 ? 0.1815 0.2059 0.1502 -0.0013 -0.0348 -0.0491 231 PHE B O   
4009 C  CB  . PHE B 230 ? 0.1526 0.1902 0.1805 -0.0059 -0.0065 -0.0231 231 PHE B CB  
4010 C  CG  . PHE B 230 ? 0.1732 0.1748 0.1330 0.0208  -0.0159 -0.0153 231 PHE B CG  
4011 C  CD1 . PHE B 230 ? 0.1581 0.1705 0.1698 0.0227  -0.0315 -0.0206 231 PHE B CD1 
4012 C  CD2 . PHE B 230 ? 0.1507 0.1926 0.2000 -0.0043 -0.0471 0.0195  231 PHE B CD2 
4013 C  CE1 . PHE B 230 ? 0.1518 0.1569 0.1461 -0.0201 -0.0041 -0.0178 231 PHE B CE1 
4014 C  CE2 . PHE B 230 ? 0.1568 0.1522 0.1730 -0.0096 -0.0236 0.0057  231 PHE B CE2 
4015 C  CZ  . PHE B 230 ? 0.1349 0.1527 0.1579 0.0031  0.0071  -0.0010 231 PHE B CZ  
4016 N  N   . ASN B 231 ? 0.1743 0.2019 0.1263 0.0186  -0.0286 -0.0181 232 ASN B N   
4017 C  CA  . ASN B 231 ? 0.1879 0.2069 0.1660 0.0113  -0.0381 -0.0467 232 ASN B CA  
4018 C  C   . ASN B 231 ? 0.1791 0.2242 0.1621 0.0183  -0.0277 -0.0012 232 ASN B C   
4019 O  O   . ASN B 231 ? 0.1854 0.2255 0.1547 0.0153  -0.0428 -0.0137 232 ASN B O   
4020 C  CB  . ASN B 231 ? 0.2506 0.2657 0.1701 0.0355  -0.0663 -0.0254 232 ASN B CB  
4021 C  CG  . ASN B 231 ? 0.2125 0.2098 0.1612 -0.0281 -0.0113 0.0000  232 ASN B CG  
4022 O  OD1 . ASN B 231 ? 0.2371 0.1750 0.1632 0.0173  -0.0553 -0.0068 232 ASN B OD1 
4023 N  ND2 . ASN B 231 ? 0.2159 0.2786 0.1818 0.0066  -0.0456 0.0401  232 ASN B ND2 
4024 N  N   . GLY B 232 ? 0.2549 0.2064 0.2278 -0.0003 -0.0640 -0.0320 233 GLY B N   
4025 C  CA  . GLY B 232 ? 0.2470 0.2944 0.1628 0.0252  -0.0551 0.0109  233 GLY B CA  
4026 C  C   . GLY B 232 ? 0.2060 0.2084 0.2362 -0.0087 -0.0214 -0.0068 233 GLY B C   
4027 O  O   . GLY B 232 ? 0.2461 0.2393 0.1621 -0.0148 -0.0751 0.0031  233 GLY B O   
4028 N  N   . GLU B 233 ? 0.1998 0.2569 0.1870 -0.0003 -0.0445 -0.0277 234 GLU B N   
4029 C  CA  . GLU B 233 ? 0.2026 0.2454 0.1842 0.0126  -0.0344 0.0326  234 GLU B CA  
4030 C  C   . GLU B 233 ? 0.1980 0.2235 0.1931 -0.0272 -0.0176 -0.0057 234 GLU B C   
4031 O  O   . GLU B 233 ? 0.2188 0.2764 0.2352 -0.0082 -0.0392 -0.0340 234 GLU B O   
4032 C  CB  . GLU B 233 ? 0.1852 0.2596 0.2248 0.0003  0.0007  -0.0364 234 GLU B CB  
4033 C  CG  . GLU B 233 ? 0.2136 0.2754 0.2341 0.0120  0.0071  -0.0612 234 GLU B CG  
4034 C  CD  . GLU B 233 ? 0.2425 0.3461 0.3479 -0.0130 0.0012  0.0417  234 GLU B CD  
4035 O  OE1 . GLU B 233 ? 0.3418 0.3851 0.3222 0.0094  -0.0131 -0.0066 234 GLU B OE1 
4036 O  OE2 . GLU B 233 ? 0.2642 0.4415 0.4110 0.0511  0.0006  0.0175  234 GLU B OE2 
4037 N  N   . GLY B 234 ? 0.2418 0.2919 0.2021 0.0015  -0.0869 0.0068  235 GLY B N   
4038 C  CA  . GLY B 234 ? 0.3215 0.2775 0.2148 -0.0162 -0.0474 0.0469  235 GLY B CA  
4039 C  C   . GLY B 234 ? 0.2644 0.4474 0.2536 -0.0617 -0.0432 -0.0027 235 GLY B C   
4040 O  O   . GLY B 234 ? 0.2542 0.4613 0.2231 0.0244  -0.0810 0.0544  235 GLY B O   
4041 N  N   . GLU B 235 ? 0.3867 0.3634 0.1488 -0.0423 -0.0923 0.0037  236 GLU B N   
4042 C  CA  . GLU B 235 ? 0.3043 0.3138 0.2179 0.0041  -0.0416 0.0238  236 GLU B CA  
4043 C  C   . GLU B 235 ? 0.2896 0.3971 0.2791 -0.0764 -0.1010 -0.0300 236 GLU B C   
4044 O  O   . GLU B 235 ? 0.3560 0.2691 0.2592 -0.0228 -0.0653 0.0403  236 GLU B O   
4045 C  CB  . GLU B 235 ? 0.3016 0.3289 0.2104 -0.0194 -0.0406 0.0129  236 GLU B CB  
4046 C  CG  . GLU B 235 ? 0.3005 0.3483 0.2888 0.0092  -0.0954 -0.0237 236 GLU B CG  
4047 C  CD  . GLU B 235 ? 0.3373 0.3923 0.4248 0.0115  -0.1851 -0.1027 236 GLU B CD  
4048 O  OE1 . GLU B 235 ? 0.4569 0.4469 0.2190 -0.0401 -0.0909 -0.0850 236 GLU B OE1 
4049 O  OE2 . GLU B 235 ? 0.4474 0.3970 0.4833 -0.0186 -0.0917 -0.1167 236 GLU B OE2 
4050 N  N   . PRO B 236 ? 0.2971 0.2881 0.1775 -0.0298 -0.0502 -0.0141 237 PRO B N   
4051 C  CA  . PRO B 236 ? 0.4192 0.3134 0.0976 -0.0386 -0.0386 -0.0156 237 PRO B CA  
4052 C  C   . PRO B 236 ? 0.2078 0.3052 0.1644 0.0114  -0.1143 -0.0137 237 PRO B C   
4053 O  O   . PRO B 236 ? 0.2626 0.3246 0.1843 0.0395  -0.0903 -0.0127 237 PRO B O   
4054 C  CB  . PRO B 236 ? 0.3589 0.5167 0.1240 0.0304  -0.0439 -0.0359 237 PRO B CB  
4055 C  CG  . PRO B 236 ? 0.4657 0.4257 0.3436 -0.1465 -0.1677 -0.0258 237 PRO B CG  
4056 C  CD  . PRO B 236 ? 0.3267 0.4144 0.2494 -0.0392 0.0126  -0.0425 237 PRO B CD  
4057 N  N   . GLU B 237 ? 0.3249 0.2689 0.1689 -0.0024 -0.0612 0.0789  238 GLU B N   
4058 C  CA  . GLU B 237 ? 0.2597 0.2714 0.1739 -0.0100 -0.0593 0.0000  238 GLU B CA  
4059 C  C   . GLU B 237 ? 0.2346 0.2020 0.1755 0.0126  -0.0368 -0.0034 238 GLU B C   
4060 O  O   . GLU B 237 ? 0.2178 0.2294 0.1784 -0.0109 -0.0236 0.0203  238 GLU B O   
4061 C  CB  . GLU B 237 ? 0.2741 0.2389 0.2500 0.0302  -0.0261 0.0109  238 GLU B CB  
4062 C  CG  . GLU B 237 ? 0.3808 0.3524 0.2386 0.0531  0.0035  -0.0129 238 GLU B CG  
4063 C  CD  . GLU B 237 ? 0.3366 0.3398 0.3709 0.0575  0.0236  0.0089  238 GLU B CD  
4064 O  OE1 . GLU B 237 ? 0.4531 0.3840 0.4925 0.0636  0.0908  0.1312  238 GLU B OE1 
4065 O  OE2 . GLU B 237 ? 0.3361 0.2493 0.3276 0.0480  -0.0460 0.0293  238 GLU B OE2 
4066 N  N   . GLU B 238 ? 0.2192 0.2192 0.1441 0.0351  -0.0320 0.0006  239 GLU B N   
4067 C  CA  . GLU B 238 ? 0.2060 0.2522 0.1532 0.0000  0.0081  -0.0060 239 GLU B CA  
4068 C  C   . GLU B 238 ? 0.1941 0.1978 0.1513 0.0219  -0.0533 0.0164  239 GLU B C   
4069 O  O   . GLU B 238 ? 0.2314 0.2048 0.1980 -0.0041 -0.0384 -0.0080 239 GLU B O   
4070 C  CB  . GLU B 238 ? 0.2558 0.2757 0.2372 0.0701  -0.0337 -0.0410 239 GLU B CB  
4071 C  CG  . GLU B 238 ? 0.4625 0.6229 0.2517 0.1893  -0.1169 0.0277  239 GLU B CG  
4072 C  CD  . GLU B 238 ? 0.6794 0.8217 0.6838 0.2662  0.1309  -0.0487 239 GLU B CD  
4073 O  OE1 . GLU B 238 ? 0.6689 0.5708 0.7302 0.4122  0.2994  -0.2069 239 GLU B OE1 
4074 O  OE2 . GLU B 238 ? 0.5425 1.0364 1.1172 0.0824  0.3353  -0.2301 239 GLU B OE2 
4075 N  N   . LEU B 239 ? 0.1727 0.2179 0.1270 0.0161  -0.0307 0.0031  240 LEU B N   
4076 C  CA  . LEU B 239 ? 0.2082 0.1908 0.1125 0.0131  -0.0281 0.0076  240 LEU B CA  
4077 C  C   . LEU B 239 ? 0.1272 0.1520 0.1070 -0.0160 -0.0103 0.0052  240 LEU B C   
4078 O  O   . LEU B 239 ? 0.1383 0.1924 0.1246 0.0082  -0.0265 -0.0054 240 LEU B O   
4079 C  CB  . LEU B 239 ? 0.2005 0.1784 0.1262 0.0211  -0.0303 0.0132  240 LEU B CB  
4080 C  CG  . LEU B 239 ? 0.1809 0.1832 0.1775 0.0299  -0.0071 -0.0008 240 LEU B CG  
4081 C  CD1 . LEU B 239 ? 0.2687 0.1793 0.2894 0.0104  0.0291  -0.0313 240 LEU B CD1 
4082 C  CD2 . LEU B 239 ? 0.1771 0.1815 0.2440 0.0019  -0.0513 0.0077  240 LEU B CD2 
4083 N  N   . MET B 240 ? 0.1297 0.1391 0.1335 -0.0093 -0.0324 0.0103  241 MET B N   
4084 C  CA  . MET B 240 ? 0.1436 0.1665 0.1471 0.0038  -0.0579 -0.0102 241 MET B CA  
4085 C  C   . MET B 240 ? 0.1150 0.1319 0.1015 0.0170  -0.0038 -0.0044 241 MET B C   
4086 O  O   . MET B 240 ? 0.1252 0.1604 0.1188 0.0140  -0.0043 -0.0190 241 MET B O   
4087 C  CB  . MET B 240 ? 0.1782 0.1829 0.1552 0.0093  -0.0419 -0.0006 241 MET B CB  
4088 C  CG  . MET B 240 ? 0.1351 0.1841 0.1197 0.0174  -0.0073 0.0055  241 MET B CG  
4089 S  SD  . MET B 240 ? 0.1572 0.1526 0.1498 0.0015  -0.0215 -0.0074 241 MET B SD  
4090 C  CE  . MET B 240 ? 0.1638 0.1849 0.1565 0.0140  -0.0432 -0.0452 241 MET B CE  
4091 N  N   . VAL B 241 ? 0.1070 0.1274 0.1364 0.0006  -0.0281 0.0066  242 VAL B N   
4092 C  CA  . VAL B 241 ? 0.1145 0.1247 0.1281 0.0122  -0.0230 -0.0035 242 VAL B CA  
4093 C  C   . VAL B 241 ? 0.1191 0.1292 0.1221 0.0052  -0.0131 -0.0125 242 VAL B C   
4094 O  O   . VAL B 241 ? 0.1283 0.1425 0.1240 0.0259  -0.0071 0.0028  242 VAL B O   
4095 C  CB  . VAL B 241 ? 0.1071 0.1269 0.1096 0.0259  -0.0010 0.0049  242 VAL B CB  
4096 C  CG1 . VAL B 241 ? 0.1021 0.1450 0.1457 0.0215  -0.0065 -0.0171 242 VAL B CG1 
4097 C  CG2 . VAL B 241 ? 0.1585 0.1477 0.1136 0.0031  -0.0024 0.0006  242 VAL B CG2 
4098 N  N   . ASP B 242 ? 0.0958 0.1067 0.1042 0.0065  -0.0140 0.0087  243 ASP B N   
4099 C  CA  . ASP B 242 ? 0.1023 0.1222 0.0956 0.0122  0.0013  0.0151  243 ASP B CA  
4100 C  C   . ASP B 242 ? 0.1114 0.1084 0.1042 0.0133  -0.0105 0.0000  243 ASP B C   
4101 O  O   . ASP B 242 ? 0.1389 0.1358 0.1296 0.0137  0.0068  -0.0028 243 ASP B O   
4102 C  CB  . ASP B 242 ? 0.1258 0.1186 0.1076 -0.0060 0.0057  0.0021  243 ASP B CB  
4103 C  CG  . ASP B 242 ? 0.1351 0.1186 0.1165 0.0108  -0.0054 0.0046  243 ASP B CG  
4104 O  OD1 . ASP B 242 ? 0.1281 0.1125 0.1111 0.0157  -0.0065 0.0041  243 ASP B OD1 
4105 O  OD2 . ASP B 242 ? 0.1739 0.1289 0.1425 0.0277  -0.0049 0.0221  243 ASP B OD2 
4106 N  N   . ASN B 243 ? 0.1142 0.0997 0.0811 0.0192  -0.0115 0.0086  244 ASN B N   
4107 C  CA  . ASN B 243 ? 0.1039 0.1055 0.1224 0.0071  -0.0062 0.0107  244 ASN B CA  
4108 C  C   . ASN B 243 ? 0.0997 0.0994 0.1014 0.0024  0.0037  0.0000  244 ASN B C   
4109 O  O   . ASN B 243 ? 0.1118 0.1058 0.1206 -0.0107 -0.0121 0.0015  244 ASN B O   
4110 C  CB  . ASN B 243 ? 0.1014 0.1389 0.0824 -0.0068 -0.0037 0.0035  244 ASN B CB  
4111 C  CG  . ASN B 243 ? 0.1280 0.1246 0.0900 0.0093  -0.0043 -0.0121 244 ASN B CG  
4112 O  OD1 . ASN B 243 ? 0.1457 0.1039 0.1032 -0.0040 0.0012  -0.0059 244 ASN B OD1 
4113 N  ND2 . ASN B 243 ? 0.1680 0.1536 0.1454 -0.0285 -0.0076 -0.0326 244 ASN B ND2 
4114 N  N   . TRP B 244 ? 0.0841 0.1086 0.0973 0.0114  -0.0085 0.0059  245 TRP B N   
4115 C  CA  . TRP B 244 ? 0.0786 0.0957 0.0936 0.0077  -0.0176 0.0051  245 TRP B CA  
4116 C  C   . TRP B 244 ? 0.1194 0.0998 0.1050 0.0051  0.0071  -0.0020 245 TRP B C   
4117 O  O   . TRP B 244 ? 0.1185 0.1278 0.1134 0.0063  0.0132  0.0141  245 TRP B O   
4118 C  CB  . TRP B 244 ? 0.1186 0.0949 0.0987 0.0110  -0.0129 -0.0003 245 TRP B CB  
4119 C  CG  . TRP B 244 ? 0.1067 0.1010 0.0859 -0.0098 -0.0071 -0.0030 245 TRP B CG  
4120 C  CD1 . TRP B 244 ? 0.1202 0.0973 0.1093 0.0006  -0.0178 -0.0059 245 TRP B CD1 
4121 C  CD2 . TRP B 244 ? 0.1066 0.1032 0.0890 0.0046  0.0015  -0.0046 245 TRP B CD2 
4122 N  NE1 . TRP B 244 ? 0.1222 0.1091 0.1037 -0.0031 -0.0007 0.0170  245 TRP B NE1 
4123 C  CE2 . TRP B 244 ? 0.1188 0.1010 0.0847 0.0073  0.0073  0.0003  245 TRP B CE2 
4124 C  CE3 . TRP B 244 ? 0.0985 0.1301 0.1121 -0.0015 0.0051  0.0024  245 TRP B CE3 
4125 C  CZ2 . TRP B 244 ? 0.1242 0.1229 0.1186 -0.0111 0.0066  0.0068  245 TRP B CZ2 
4126 C  CZ3 . TRP B 244 ? 0.1419 0.1484 0.1529 -0.0162 -0.0148 0.0082  245 TRP B CZ3 
4127 C  CH2 . TRP B 244 ? 0.1163 0.1344 0.1292 -0.0342 -0.0083 0.0035  245 TRP B CH2 
4128 N  N   . ARG B 245 ? 0.0903 0.1102 0.0964 0.0063  -0.0040 -0.0010 246 ARG B N   
4129 C  CA  . ARG B 245 ? 0.1052 0.1023 0.0966 0.0173  0.0071  0.0000  246 ARG B CA  
4130 C  C   . ARG B 245 ? 0.0816 0.1181 0.1014 0.0144  -0.0007 0.0031  246 ARG B C   
4131 O  O   . ARG B 245 ? 0.1001 0.1199 0.0964 0.0020  -0.0030 -0.0068 246 ARG B O   
4132 C  CB  . ARG B 245 ? 0.1164 0.1238 0.1100 0.0270  0.0052  0.0000  246 ARG B CB  
4133 C  CG  . ARG B 245 ? 0.0940 0.1039 0.0994 0.0135  0.0092  0.0065  246 ARG B CG  
4134 C  CD  . ARG B 245 ? 0.1369 0.1058 0.1039 0.0302  0.0153  -0.0109 246 ARG B CD  
4135 N  NE  . ARG B 245 ? 0.1366 0.1211 0.0865 0.0193  0.0100  -0.0126 246 ARG B NE  
4136 C  CZ  . ARG B 245 ? 0.1403 0.1259 0.1159 0.0248  0.0206  -0.0006 246 ARG B CZ  
4137 N  NH1 . ARG B 245 ? 0.1411 0.1356 0.1129 0.0368  -0.0070 -0.0006 246 ARG B NH1 
4138 N  NH2 . ARG B 245 ? 0.1348 0.1601 0.1168 0.0165  0.0214  -0.0121 246 ARG B NH2 
4139 N  N   . PRO B 246 ? 0.1179 0.1105 0.1181 0.0041  -0.0164 0.0062  247 PRO B N   
4140 C  CA  . PRO B 246 ? 0.0945 0.1116 0.1307 0.0000  -0.0111 0.0040  247 PRO B CA  
4141 C  C   . PRO B 246 ? 0.1096 0.1070 0.1188 0.0094  -0.0006 0.0104  247 PRO B C   
4142 O  O   . PRO B 246 ? 0.1176 0.1158 0.1100 0.0074  0.0059  -0.0013 247 PRO B O   
4143 C  CB  . PRO B 246 ? 0.1506 0.1610 0.1578 -0.0065 -0.0073 0.0443  247 PRO B CB  
4144 C  CG  . PRO B 246 ? 0.2748 0.2418 0.1489 -0.1005 -0.0001 0.0335  247 PRO B CG  
4145 C  CD  . PRO B 246 ? 0.1310 0.1775 0.1225 -0.0395 0.0105  0.0166  247 PRO B CD  
4146 N  N   . ALA B 247 ? 0.1077 0.1128 0.1179 -0.0110 -0.0126 0.0103  248 ALA B N   
4147 C  CA  . ALA B 247 ? 0.1252 0.1134 0.1351 0.0063  -0.0066 0.0078  248 ALA B CA  
4148 C  C   . ALA B 247 ? 0.1149 0.1222 0.1185 -0.0129 -0.0126 0.0116  248 ALA B C   
4149 O  O   . ALA B 247 ? 0.1235 0.1574 0.1484 0.0043  -0.0015 0.0361  248 ALA B O   
4150 C  CB  . ALA B 247 ? 0.1563 0.1669 0.1450 -0.0088 -0.0373 0.0092  248 ALA B CB  
4151 N  N   . GLN B 248 ? 0.1159 0.1211 0.1333 0.0209  0.0068  0.0051  249 GLN B N   
4152 C  CA  . GLN B 248 ? 0.1107 0.1522 0.1030 0.0027  0.0015  0.0038  249 GLN B CA  
4153 C  C   . GLN B 248 ? 0.1179 0.1191 0.1184 0.0076  0.0049  0.0149  249 GLN B C   
4154 O  O   . GLN B 248 ? 0.1453 0.1353 0.1322 0.0000  -0.0060 0.0093  249 GLN B O   
4155 C  CB  . GLN B 248 ? 0.1202 0.1246 0.1204 0.0187  0.0000  0.0141  249 GLN B CB  
4156 C  CG  . GLN B 248 ? 0.1395 0.1330 0.1262 0.0077  -0.0199 -0.0006 249 GLN B CG  
4157 C  CD  . GLN B 248 ? 0.1504 0.1720 0.1185 0.0137  0.0185  0.0000  249 GLN B CD  
4158 O  OE1 . GLN B 248 ? 0.1743 0.2055 0.1653 0.0379  0.0250  0.0017  249 GLN B OE1 
4159 N  NE2 . GLN B 248 ? 0.1536 0.1570 0.1560 -0.0020 0.0162  0.0236  249 GLN B NE2 
4160 N  N   . PRO B 249 ? 0.1140 0.1782 0.1615 0.0048  0.0052  0.0066  250 PRO B N   
4161 C  CA  . PRO B 249 ? 0.1265 0.2082 0.1529 -0.0098 0.0049  0.0430  250 PRO B CA  
4162 C  C   . PRO B 249 ? 0.1247 0.1405 0.1538 0.0207  0.0132  0.0146  250 PRO B C   
4163 O  O   . PRO B 249 ? 0.1457 0.1687 0.1604 -0.0041 0.0068  0.0153  250 PRO B O   
4164 C  CB  . PRO B 249 ? 0.1881 0.2926 0.1784 0.0291  0.0738  0.1045  250 PRO B CB  
4165 C  CG  . PRO B 249 ? 0.1396 0.2949 0.2579 0.0049  0.0322  0.0608  250 PRO B CG  
4166 C  CD  . PRO B 249 ? 0.1243 0.2307 0.1692 0.0313  0.0271  0.0148  250 PRO B CD  
4167 N  N   . LEU B 250 ? 0.1344 0.1702 0.1617 -0.0074 0.0214  0.0267  251 LEU B N   
4168 C  CA  . LEU B 250 ? 0.1597 0.1615 0.1540 0.0129  -0.0342 0.0186  251 LEU B CA  
4169 C  C   . LEU B 250 ? 0.1533 0.1673 0.1967 0.0020  0.0051  0.0260  251 LEU B C   
4170 O  O   . LEU B 250 ? 0.1452 0.1644 0.1863 -0.0015 0.0124  0.0337  251 LEU B O   
4171 C  CB  . LEU B 250 ? 0.1738 0.1791 0.1960 -0.0331 -0.0129 0.0008  251 LEU B CB  
4172 C  CG  . LEU B 250 ? 0.1669 0.1845 0.1836 0.0046  -0.0204 -0.0100 251 LEU B CG  
4173 C  CD1 . LEU B 250 ? 0.1630 0.1869 0.2258 0.0131  0.0000  0.0161  251 LEU B CD1 
4174 C  CD2 . LEU B 250 ? 0.2030 0.2427 0.2258 0.0447  -0.0593 -0.0469 251 LEU B CD2 
4175 N  N   . LYS B 251 ? 0.1489 0.1863 0.2145 0.0115  0.0230  0.0109  252 LYS B N   
4176 C  CA  . LYS B 251 ? 0.1124 0.1994 0.2152 -0.0130 0.0148  0.0170  252 LYS B CA  
4177 C  C   . LYS B 251 ? 0.1879 0.1971 0.2134 0.0215  0.0226  0.0196  252 LYS B C   
4178 O  O   . LYS B 251 ? 0.2179 0.2851 0.2432 -0.0136 -0.0511 0.0241  252 LYS B O   
4179 C  CB  . LYS B 251 ? 0.1947 0.2123 0.2416 0.0502  0.0236  0.0126  252 LYS B CB  
4180 C  CG  . LYS B 251 ? 0.2486 0.1611 0.3118 0.0544  -0.0295 0.0460  252 LYS B CG  
4181 C  CD  . LYS B 251 ? 0.2702 0.3075 0.2910 0.0690  -0.0196 0.0093  252 LYS B CD  
4182 C  CE  . LYS B 251 ? 0.4007 0.3095 0.2908 0.0285  0.0027  0.0450  252 LYS B CE  
4183 N  NZ  . LYS B 251 ? 0.4388 0.3786 0.3309 -0.0644 0.0988  -0.0149 252 LYS B NZ  
4184 N  N   . ASN B 252 ? 0.1279 0.2258 0.1942 0.0194  0.0121  0.0293  253 ASN B N   
4185 C  CA  . ASN B 252 ? 0.2384 0.3890 0.2565 0.1169  -0.0652 0.0247  253 ASN B CA  
4186 C  C   . ASN B 252 ? 0.2985 0.5752 0.3693 0.1023  0.0452  0.1553  253 ASN B C   
4187 O  O   . ASN B 252 ? 0.1951 0.6254 0.4589 -0.0549 -0.0855 0.0903  253 ASN B O   
4188 C  CB  . ASN B 252 ? 0.3957 0.3813 0.3684 0.1516  0.0087  0.0684  253 ASN B CB  
4189 C  CG  . ASN B 252 ? 0.3707 0.3433 0.4947 0.0930  -0.0524 0.1111  253 ASN B CG  
4190 O  OD1 . ASN B 252 ? 0.4907 0.6647 0.6744 -0.1322 -0.0386 -0.0315 253 ASN B OD1 
4191 N  ND2 . ASN B 252 ? 0.3129 0.3287 0.3269 0.0452  -0.0031 0.0094  253 ASN B ND2 
4192 N  N   . ARG B 253 ? 0.1640 0.2700 0.2217 -0.0315 -0.0162 0.0236  254 ARG B N   
4193 C  CA  . ARG B 253 ? 0.1299 0.1996 0.1708 0.0109  -0.0329 0.0172  254 ARG B CA  
4194 C  C   . ARG B 253 ? 0.1492 0.1763 0.1838 0.0174  -0.0157 0.0041  254 ARG B C   
4195 O  O   . ARG B 253 ? 0.2597 0.1967 0.2095 -0.0275 -0.0474 0.0326  254 ARG B O   
4196 C  CB  . ARG B 253 ? 0.1123 0.1642 0.1881 0.0074  -0.0296 0.0152  254 ARG B CB  
4197 C  CG  . ARG B 253 ? 0.0863 0.1574 0.1985 0.0277  -0.0315 0.0093  254 ARG B CG  
4198 C  CD  . ARG B 253 ? 0.1001 0.1377 0.1935 0.0071  -0.0381 0.0458  254 ARG B CD  
4199 N  NE  . ARG B 253 ? 0.1353 0.1326 0.1772 0.0126  -0.0222 0.0355  254 ARG B NE  
4200 C  CZ  . ARG B 253 ? 0.1067 0.1283 0.1378 0.0034  -0.0105 0.0192  254 ARG B CZ  
4201 N  NH1 . ARG B 253 ? 0.1143 0.1225 0.1202 -0.0010 0.0184  0.0216  254 ARG B NH1 
4202 N  NH2 . ARG B 253 ? 0.1299 0.1165 0.1344 0.0124  -0.0040 0.0186  254 ARG B NH2 
4203 N  N   . GLN B 254 ? 0.1393 0.1766 0.1894 0.0229  -0.0099 0.0239  255 GLN B N   
4204 C  CA  . GLN B 254 ? 0.1594 0.2366 0.2070 0.0010  -0.0419 0.0267  255 GLN B CA  
4205 C  C   . GLN B 254 ? 0.1504 0.2348 0.2958 -0.0379 0.0035  -0.0659 255 GLN B C   
4206 O  O   . GLN B 254 ? 0.2363 0.1876 0.3194 -0.0315 0.0153  -0.0017 255 GLN B O   
4207 C  CB  . GLN B 254 ? 0.2583 0.3172 0.2592 0.0538  -0.0617 0.0860  255 GLN B CB  
4208 C  CG  . GLN B 254 ? 0.5256 0.6474 0.4200 0.0399  -0.0193 -0.0522 255 GLN B CG  
4209 C  CD  . GLN B 254 ? 0.3826 0.7598 0.7698 0.0373  -0.3650 0.1520  255 GLN B CD  
4210 O  OE1 . GLN B 254 ? 0.8668 1.6332 0.7573 -0.0571 -0.1855 0.0419  255 GLN B OE1 
4211 N  NE2 . GLN B 254 ? 0.8151 1.0324 0.8914 0.1080  -0.1456 0.1435  255 GLN B NE2 
4212 N  N   . ILE B 255 ? 0.1515 0.1721 0.1525 -0.0070 -0.0280 -0.0001 256 ILE B N   
4213 C  CA  . ILE B 255 ? 0.1288 0.1712 0.1459 0.0046  -0.0362 0.0392  256 ILE B CA  
4214 C  C   . ILE B 255 ? 0.1430 0.1608 0.1465 -0.0364 -0.0165 0.0187  256 ILE B C   
4215 O  O   . ILE B 255 ? 0.1648 0.1847 0.1798 -0.0421 -0.0250 -0.0012 256 ILE B O   
4216 C  CB  . ILE B 255 ? 0.1608 0.1299 0.1407 -0.0130 -0.0121 0.0197  256 ILE B CB  
4217 C  CG1 . ILE B 255 ? 0.1727 0.1470 0.1340 -0.0243 -0.0198 0.0592  256 ILE B CG1 
4218 C  CG2 . ILE B 255 ? 0.1516 0.1841 0.2353 0.0126  -0.0274 0.0006  256 ILE B CG2 
4219 C  CD1 . ILE B 255 ? 0.2012 0.1912 0.1870 0.0368  -0.0555 0.0194  256 ILE B CD1 
4220 N  N   . LYS B 256 ? 0.1360 0.1930 0.1280 -0.0403 -0.0093 0.0143  257 LYS B N   
4221 C  CA  . LYS B 256 ? 0.1509 0.1881 0.1315 -0.0248 -0.0130 0.0046  257 LYS B CA  
4222 C  C   . LYS B 256 ? 0.1331 0.1525 0.1617 -0.0046 -0.0417 -0.0046 257 LYS B C   
4223 O  O   . LYS B 256 ? 0.1368 0.2037 0.1642 -0.0048 -0.0649 -0.0311 257 LYS B O   
4224 C  CB  . LYS B 256 ? 0.1856 0.1924 0.2087 -0.0007 -0.0277 0.0318  257 LYS B CB  
4225 C  CG  . LYS B 256 ? 0.2321 0.2648 0.2443 0.0160  -0.0152 0.0179  257 LYS B CG  
4226 C  CD  . LYS B 256 ? 0.3418 0.3253 0.3808 0.0877  -0.0370 0.0502  257 LYS B CD  
4227 C  CE  . LYS B 256 ? 0.4442 0.4776 0.6825 0.1763  0.0388  0.0463  257 LYS B CE  
4228 N  NZ  . LYS B 256 ? 0.8014 0.5389 0.4029 0.0324  0.1273  -0.0362 257 LYS B NZ  
4229 N  N   . ALA B 257 ? 0.1807 0.1890 0.1315 -0.0242 -0.0381 0.0020  258 ALA B N   
4230 C  CA  . ALA B 257 ? 0.1671 0.1867 0.1585 -0.0441 -0.0223 -0.0005 258 ALA B CA  
4231 C  C   . ALA B 257 ? 0.1588 0.1910 0.1421 -0.0108 -0.0509 0.0149  258 ALA B C   
4232 O  O   . ALA B 257 ? 0.1621 0.2328 0.1870 -0.0153 -0.0662 0.0302  258 ALA B O   
4233 C  CB  . ALA B 257 ? 0.2298 0.1820 0.1375 -0.0671 -0.0324 -0.0024 258 ALA B CB  
4234 N  N   . SER B 258 ? 0.1781 0.1680 0.1462 -0.0351 -0.0307 0.0013  259 SER B N   
4235 C  CA  . SER B 258 ? 0.2134 0.2025 0.1559 -0.0593 -0.0218 0.0081  259 SER B CA  
4236 C  C   . SER B 258 ? 0.2386 0.2080 0.1475 -0.0282 -0.0494 -0.0054 259 SER B C   
4237 O  O   . SER B 258 ? 0.2653 0.3170 0.1662 -0.0271 -0.0395 0.0313  259 SER B O   
4238 C  CB  . SER B 258 ? 0.1775 0.2133 0.2284 -0.0071 -0.0266 0.0085  259 SER B CB  
4239 O  OG  . SER B 258 ? 0.1912 0.1884 0.1215 -0.0031 -0.0372 0.0060  259 SER B OG  
4240 N  N   . PHE B 259 ? 0.2429 0.2264 0.1254 -0.0239 -0.0357 -0.0326 260 PHE B N   
4241 C  CA  . PHE B 259 ? 0.2890 0.2788 0.1495 -0.0211 -0.0155 -0.0640 260 PHE B CA  
4242 C  C   . PHE B 259 ? 0.3319 0.3089 0.1850 -0.0274 -0.0375 -0.0417 260 PHE B C   
4243 O  O   . PHE B 259 ? 0.2811 0.2836 0.2935 -0.0860 -0.0375 -0.0786 260 PHE B O   
4244 C  CB  . PHE B 259 ? 0.2924 0.2594 0.1875 -0.0194 -0.0395 -0.0119 260 PHE B CB  
4245 C  CG  . PHE B 259 ? 0.3574 0.2312 0.1833 -0.0653 -0.0142 -0.0093 260 PHE B CG  
4246 C  CD1 . PHE B 259 ? 0.2640 0.2319 0.1748 -0.0133 0.0203  -0.0452 260 PHE B CD1 
4247 C  CD2 . PHE B 259 ? 0.3729 0.2269 0.2037 -0.0802 -0.0342 -0.0307 260 PHE B CD2 
4248 C  CE1 . PHE B 259 ? 0.2847 0.1863 0.2221 0.0015  0.0219  0.0109  260 PHE B CE1 
4249 C  CE2 . PHE B 259 ? 0.3894 0.2089 0.2308 -0.0688 0.0019  -0.0416 260 PHE B CE2 
4250 C  CZ  . PHE B 259 ? 0.3088 0.2196 0.2134 0.0200  0.0142  -0.0296 260 PHE B CZ  
4251 N  N   . LYS B 260 ? 0.4587 0.4689 0.3088 -0.0542 -0.1031 -0.1880 261 LYS B N   
4252 C  CA  . LYS B 260 ? 0.4387 0.4679 0.5016 -0.0860 -0.1455 -0.0798 261 LYS B CA  
4253 C  C   . LYS B 260 ? 0.4431 0.7444 0.6322 -0.0412 -0.0606 -0.0864 261 LYS B C   
4254 O  O   . LYS B 260 ? 0.7181 0.9616 0.5479 -0.2757 -0.1880 -0.1347 261 LYS B O   
4255 C  CB  . LYS B 260 ? 0.3932 0.6304 0.3923 -0.0073 -0.1759 -0.0228 261 LYS B CB  
4256 C  CG  . LYS B 260 ? 0.7333 0.7174 0.7006 0.0986  0.0469  -0.1334 261 LYS B CG  
4257 C  CD  . LYS B 260 ? 0.6639 0.3754 0.5885 0.1081  -0.1770 -0.0775 261 LYS B CD  
4258 C  CE  . LYS B 260 ? 0.6448 0.5899 0.4683 0.1439  -0.0196 0.0096  261 LYS B CE  
4259 N  NZ  . LYS B 260 ? 0.6080 0.4684 0.4693 -0.0013 -0.0038 -0.0344 261 LYS B NZ  
4260 N  N   . HIS C 3   ? 0.3646 0.4002 0.3535 -0.0630 0.1719  -0.1011 3   HIS C N   
4261 C  CA  . HIS C 3   ? 0.4090 0.4847 0.3919 0.0395  0.0886  -0.1287 3   HIS C CA  
4262 C  C   . HIS C 3   ? 0.4234 0.4610 0.4768 0.0778  -0.0485 -0.0606 3   HIS C C   
4263 O  O   . HIS C 3   ? 0.4077 0.5662 0.6980 -0.1722 0.0469  0.0882  3   HIS C O   
4264 C  CB  . HIS C 3   ? 0.2822 0.4968 0.5005 0.1479  0.1162  0.1396  3   HIS C CB  
4265 C  CG  . HIS C 3   ? 0.6021 0.3862 0.6322 0.1020  0.0236  0.1473  3   HIS C CG  
4266 N  ND1 . HIS C 3   ? 0.4124 0.5616 0.4794 -0.1203 0.1168  0.0309  3   HIS C ND1 
4267 C  CD2 . HIS C 3   ? 0.5570 0.4822 0.4031 0.1576  0.0284  0.0511  3   HIS C CD2 
4268 C  CE1 . HIS C 3   ? 0.7670 0.4262 0.7023 -0.0680 0.0549  0.1895  3   HIS C CE1 
4269 N  NE2 . HIS C 3   ? 0.4745 0.4815 0.6184 0.0015  0.0681  0.1722  3   HIS C NE2 
4270 N  N   . HIS C 4   ? 0.6450 0.4307 0.2369 0.1067  -0.0346 0.0610  4   HIS C N   
4271 C  CA  . HIS C 4   ? 0.5922 0.3063 0.2354 0.0357  -0.0500 0.0918  4   HIS C CA  
4272 C  C   . HIS C 4   ? 0.3341 0.2597 0.2258 0.0277  -0.0675 0.0122  4   HIS C C   
4273 O  O   . HIS C 4   ? 0.3201 0.2711 0.2077 -0.0241 -0.0035 0.0265  4   HIS C O   
4274 C  CB  . HIS C 4   ? 0.7825 0.4884 0.1567 0.2709  -0.1367 0.1486  4   HIS C CB  
4275 C  CG  . HIS C 4   ? 1.1001 0.6977 0.7292 -0.0006 0.0249  0.0100  4   HIS C CG  
4276 N  ND1 . HIS C 4   ? 0.8733 0.8489 0.6385 -0.0142 0.1895  0.1687  4   HIS C ND1 
4277 C  CD2 . HIS C 4   ? 1.1038 0.6998 0.5049 0.1561  0.5101  -0.1080 4   HIS C CD2 
4278 C  CE1 . HIS C 4   ? 0.6825 0.5766 1.0776 0.0445  0.1633  0.1729  4   HIS C CE1 
4279 N  NE2 . HIS C 4   ? 0.9631 0.7556 0.8842 0.2032  0.3454  -0.1023 4   HIS C NE2 
4280 N  N   . TRP C 5   ? 0.3215 0.2442 0.1525 -0.0137 -0.0192 0.0214  5   TRP C N   
4281 C  CA  . TRP C 5   ? 0.2339 0.1800 0.1450 -0.0063 -0.0147 0.0307  5   TRP C CA  
4282 C  C   . TRP C 5   ? 0.1867 0.1781 0.1360 0.0103  0.0006  -0.0230 5   TRP C C   
4283 O  O   . TRP C 5   ? 0.2228 0.1976 0.1538 0.0130  0.0120  0.0315  5   TRP C O   
4284 C  CB  . TRP C 5   ? 0.2366 0.1629 0.1583 -0.0125 0.0092  0.0272  5   TRP C CB  
4285 C  CG  . TRP C 5   ? 0.2154 0.1694 0.1721 -0.0241 -0.0177 0.0097  5   TRP C CG  
4286 C  CD1 . TRP C 5   ? 0.2509 0.2239 0.1709 0.0355  -0.0405 0.0373  5   TRP C CD1 
4287 C  CD2 . TRP C 5   ? 0.1689 0.1825 0.1858 -0.0115 0.0078  0.0044  5   TRP C CD2 
4288 N  NE1 . TRP C 5   ? 0.2154 0.1797 0.2129 -0.0038 -0.0247 0.0186  5   TRP C NE1 
4289 C  CE2 . TRP C 5   ? 0.1831 0.1793 0.1674 -0.0271 -0.0209 0.0043  5   TRP C CE2 
4290 C  CE3 . TRP C 5   ? 0.1604 0.1759 0.1197 -0.0260 -0.0034 -0.0043 5   TRP C CE3 
4291 C  CZ2 . TRP C 5   ? 0.1371 0.1966 0.1628 0.0087  -0.0190 -0.0258 5   TRP C CZ2 
4292 C  CZ3 . TRP C 5   ? 0.1653 0.1924 0.1298 -0.0113 0.0187  -0.0267 5   TRP C CZ3 
4293 C  CH2 . TRP C 5   ? 0.1727 0.1993 0.1579 -0.0111 0.0153  -0.0266 5   TRP C CH2 
4294 N  N   . GLY C 6   ? 0.1964 0.1711 0.1128 -0.0129 0.0077  -0.0109 6   GLY C N   
4295 C  CA  . GLY C 6   ? 0.1773 0.1876 0.1427 -0.0217 -0.0122 0.0091  6   GLY C CA  
4296 C  C   . GLY C 6   ? 0.1939 0.1996 0.1368 0.0124  -0.0085 -0.0038 6   GLY C C   
4297 O  O   . GLY C 6   ? 0.1822 0.1798 0.1516 -0.0207 -0.0120 -0.0136 6   GLY C O   
4298 N  N   . TYR C 7   ? 0.2124 0.1811 0.1272 0.0135  -0.0428 -0.0104 7   TYR C N   
4299 C  CA  . TYR C 7   ? 0.2592 0.1479 0.1068 0.0087  0.0080  -0.0068 7   TYR C CA  
4300 C  C   . TYR C 7   ? 0.4890 0.2117 0.1520 0.0535  -0.0680 -0.0564 7   TYR C C   
4301 O  O   . TYR C 7   ? 0.5562 0.2508 0.2086 0.0392  -0.0186 -0.0092 7   TYR C O   
4302 C  CB  . TYR C 7   ? 0.2400 0.1924 0.1385 -0.0353 0.0038  -0.0105 7   TYR C CB  
4303 C  CG  . TYR C 7   ? 0.1615 0.1565 0.1425 -0.0137 0.0131  0.0043  7   TYR C CG  
4304 C  CD1 . TYR C 7   ? 0.1642 0.1814 0.1233 -0.0093 0.0320  0.0044  7   TYR C CD1 
4305 C  CD2 . TYR C 7   ? 0.1938 0.1526 0.1075 0.0013  -0.0143 0.0010  7   TYR C CD2 
4306 C  CE1 . TYR C 7   ? 0.1159 0.1297 0.1057 -0.0088 0.0156  0.0121  7   TYR C CE1 
4307 C  CE2 . TYR C 7   ? 0.1489 0.1472 0.1403 -0.0094 -0.0142 -0.0031 7   TYR C CE2 
4308 C  CZ  . TYR C 7   ? 0.1376 0.1356 0.1014 -0.0109 0.0007  0.0173  7   TYR C CZ  
4309 O  OH  . TYR C 7   ? 0.1721 0.1373 0.1341 -0.0024 -0.0198 0.0023  7   TYR C OH  
4310 N  N   . GLY C 8   ? 0.3824 0.2154 0.1168 -0.0649 0.0357  -0.0146 8   GLY C N   
4311 C  CA  . GLY C 8   ? 0.4311 0.1725 0.2001 -0.0767 -0.0653 -0.0237 8   GLY C CA  
4312 C  C   . GLY C 8   ? 0.3846 0.2027 0.2633 -0.0001 -0.0914 -0.0147 8   GLY C C   
4313 O  O   . GLY C 8   ? 0.4785 0.4034 0.1872 -0.0070 -0.0696 -0.0785 8   GLY C O   
4314 N  N   . LYS C 9   ? 0.8314 0.2025 0.1941 0.1032  0.0729  -0.0452 9   LYS C N   
4315 C  CA  . LYS C 9   ? 0.7652 0.2560 0.4207 -0.0031 0.1659  -0.0571 9   LYS C CA  
4316 C  C   . LYS C 9   ? 0.4305 0.3855 0.2382 0.1000  0.0012  0.0086  9   LYS C C   
4317 O  O   . LYS C 9   ? 0.4219 0.3165 0.2305 -0.0126 0.0401  -0.0063 9   LYS C O   
4318 C  CB  . LYS C 9   ? 1.2085 0.6004 0.4786 0.0277  -0.1562 0.0689  9   LYS C CB  
4319 C  CG  . LYS C 9   ? 0.6780 0.6883 0.0698 0.0560  0.0105  -0.1700 9   LYS C CG  
4320 N  N   . HIS C 10  ? 0.3939 0.2228 0.1472 0.0291  -0.0491 -0.0575 10  HIS C N   
4321 C  CA  . HIS C 10  ? 0.3134 0.2476 0.1545 -0.0031 -0.0392 -0.0252 10  HIS C CA  
4322 C  C   . HIS C 10  ? 0.2402 0.2181 0.1768 0.0286  0.0199  -0.0304 10  HIS C C   
4323 O  O   . HIS C 10  ? 0.3296 0.2667 0.1628 -0.0383 -0.0037 -0.0639 10  HIS C O   
4324 C  CB  . HIS C 10  ? 0.3856 0.2786 0.1513 -0.0031 -0.0592 -0.0258 10  HIS C CB  
4325 C  CG  . HIS C 10  ? 0.2931 0.2655 0.2283 -0.0909 -0.0298 0.0210  10  HIS C CG  
4326 N  ND1 . HIS C 10  ? 0.3131 0.2899 0.2148 0.0031  -0.0631 -0.0137 10  HIS C ND1 
4327 C  CD2 . HIS C 10  ? 0.3560 0.2978 0.1811 -0.0680 -0.0182 -0.0233 10  HIS C CD2 
4328 C  CE1 . HIS C 10  ? 0.3068 0.2802 0.1780 -0.0120 0.0239  -0.0608 10  HIS C CE1 
4329 N  NE2 . HIS C 10  ? 0.3538 0.3686 0.2384 0.0126  -0.0043 -0.0573 10  HIS C NE2 
4330 N  N   . ASN C 11  ? 0.2806 0.2095 0.1197 0.0105  -0.0216 -0.0318 11  ASN C N   
4331 C  CA  . ASN C 11  ? 0.2472 0.1913 0.1204 -0.0038 -0.0408 -0.0149 11  ASN C CA  
4332 C  C   . ASN C 11  ? 0.2148 0.1705 0.1337 -0.0104 -0.0227 -0.0080 11  ASN C C   
4333 O  O   . ASN C 11  ? 0.2098 0.2014 0.1497 0.0276  0.0082  -0.0480 11  ASN C O   
4334 C  CB  . ASN C 11  ? 0.2443 0.2188 0.1127 -0.0245 -0.0200 -0.0122 11  ASN C CB  
4335 C  CG  . ASN C 11  ? 0.2220 0.1861 0.1788 0.0031  -0.0427 -0.0527 11  ASN C CG  
4336 O  OD1 . ASN C 11  ? 0.2743 0.2197 0.1962 -0.0024 -0.0037 0.0057  11  ASN C OD1 
4337 N  ND2 . ASN C 11  ? 0.2293 0.2786 0.1635 0.0137  -0.0379 -0.0035 11  ASN C ND2 
4338 N  N   . GLY C 12  ? 0.2418 0.1796 0.1120 -0.0035 0.0003  -0.0201 12  GLY C N   
4339 C  CA  . GLY C 12  ? 0.1741 0.2233 0.0961 -0.0118 -0.0024 -0.0595 12  GLY C CA  
4340 C  C   . GLY C 12  ? 0.1587 0.1511 0.1365 0.0194  -0.0020 -0.0020 12  GLY C C   
4341 O  O   . GLY C 12  ? 0.1784 0.1576 0.1351 0.0049  0.0195  -0.0236 12  GLY C O   
4342 N  N   . PRO C 13  ? 0.1919 0.1563 0.1057 -0.0109 -0.0027 -0.0076 13  PRO C N   
4343 C  CA  . PRO C 13  ? 0.1730 0.1613 0.1465 -0.0230 0.0027  0.0190  13  PRO C CA  
4344 C  C   . PRO C 13  ? 0.1820 0.1396 0.1215 0.0082  0.0015  0.0105  13  PRO C C   
4345 O  O   . PRO C 13  ? 0.1981 0.1888 0.0933 -0.0274 0.0186  -0.0052 13  PRO C O   
4346 C  CB  . PRO C 13  ? 0.1905 0.1723 0.1260 0.0040  -0.0194 0.0215  13  PRO C CB  
4347 C  CG  . PRO C 13  ? 0.2141 0.1875 0.1298 -0.0172 -0.0381 -0.0089 13  PRO C CG  
4348 C  CD  . PRO C 13  ? 0.1752 0.1975 0.1176 -0.0348 -0.0065 -0.0156 13  PRO C CD  
4349 N  N   A GLU C 14  ? 0.1423 0.1538 0.1676 0.0122  0.0098  -0.0142 14  GLU C N   
4350 N  N   B GLU C 14  ? 0.1874 0.1592 0.1777 0.0320  0.0129  -0.0148 14  GLU C N   
4351 C  CA  A GLU C 14  ? 0.1586 0.1673 0.2161 0.0082  0.0408  0.0027  14  GLU C CA  
4352 C  CA  B GLU C 14  ? 0.2196 0.1472 0.2346 0.0368  0.0447  -0.0031 14  GLU C CA  
4353 C  C   A GLU C 14  ? 0.1958 0.1775 0.1295 0.0173  0.0125  -0.0476 14  GLU C C   
4354 C  C   B GLU C 14  ? 0.2039 0.1876 0.1569 0.0086  -0.0030 -0.0472 14  GLU C C   
4355 O  O   A GLU C 14  ? 0.1913 0.1568 0.1459 0.0120  0.0162  -0.0153 14  GLU C O   
4356 O  O   B GLU C 14  ? 0.2777 0.2032 0.2025 0.0115  0.0707  -0.0297 14  GLU C O   
4357 C  CB  A GLU C 14  ? 0.1777 0.2257 0.2691 0.0324  0.0216  -0.0653 14  GLU C CB  
4358 C  CB  B GLU C 14  ? 0.3100 0.1569 0.2264 0.0538  0.0643  0.0080  14  GLU C CB  
4359 C  CG  A GLU C 14  ? 0.1956 0.1710 0.1669 0.0329  0.0463  -0.0318 14  GLU C CG  
4360 C  CG  B GLU C 14  ? 0.3037 0.1453 0.2531 -0.0251 -0.0131 0.0361  14  GLU C CG  
4361 C  CD  A GLU C 14  ? 0.2091 0.2398 0.1854 0.0353  0.0653  -0.0706 14  GLU C CD  
4362 C  CD  B GLU C 14  ? 0.2802 0.2951 0.2626 0.0436  -0.0184 0.0184  14  GLU C CD  
4363 O  OE1 A GLU C 14  ? 0.2118 0.1860 0.1720 -0.0555 0.0648  -0.1088 14  GLU C OE1 
4364 O  OE1 B GLU C 14  ? 0.2590 0.2766 0.2813 0.0308  0.0063  -0.0668 14  GLU C OE1 
4365 O  OE2 A GLU C 14  ? 0.2906 0.1186 0.4169 0.0028  -0.0368 -0.0436 14  GLU C OE2 
4366 O  OE2 B GLU C 14  ? 0.3384 0.3819 0.3009 -0.0313 0.0762  -0.0454 14  GLU C OE2 
4367 N  N   . HIS C 15  ? 0.1935 0.1488 0.1401 0.0038  0.0197  -0.0219 15  HIS C N   
4368 C  CA  . HIS C 15  ? 0.1701 0.1592 0.1168 0.0097  0.0232  -0.0149 15  HIS C CA  
4369 C  C   . HIS C 15  ? 0.1617 0.1536 0.1209 0.0000  0.0317  -0.0230 15  HIS C C   
4370 O  O   . HIS C 15  ? 0.2160 0.1831 0.1115 -0.0003 0.0410  -0.0052 15  HIS C O   
4371 C  CB  . HIS C 15  ? 0.1662 0.1709 0.1394 0.0118  0.0007  -0.0219 15  HIS C CB  
4372 C  CG  . HIS C 15  ? 0.1816 0.2075 0.1545 0.0141  0.0333  -0.0315 15  HIS C CG  
4373 N  ND1 . HIS C 15  ? 0.3106 0.2572 0.1614 -0.0289 0.0604  -0.0785 15  HIS C ND1 
4374 C  CD2 . HIS C 15  ? 0.2226 0.2027 0.1881 0.0175  0.0242  -0.0544 15  HIS C CD2 
4375 C  CE1 . HIS C 15  ? 0.3355 0.2734 0.3070 -0.0557 0.0929  -0.1349 15  HIS C CE1 
4376 N  NE2 . HIS C 15  ? 0.3273 0.2452 0.2111 -0.0100 0.0063  -0.0975 15  HIS C NE2 
4377 N  N   . TRP C 16  ? 0.1621 0.1401 0.1062 0.0144  0.0252  -0.0214 16  TRP C N   
4378 C  CA  . TRP C 16  ? 0.1793 0.1371 0.0976 -0.0057 0.0220  -0.0142 16  TRP C CA  
4379 C  C   . TRP C 16  ? 0.1488 0.1559 0.0970 0.0017  0.0311  -0.0179 16  TRP C C   
4380 O  O   . TRP C 16  ? 0.1741 0.1543 0.1179 0.0136  0.0460  -0.0037 16  TRP C O   
4381 C  CB  . TRP C 16  ? 0.1321 0.1502 0.0824 -0.0200 0.0141  -0.0070 16  TRP C CB  
4382 C  CG  . TRP C 16  ? 0.1385 0.1356 0.1258 -0.0102 0.0027  -0.0063 16  TRP C CG  
4383 C  CD1 . TRP C 16  ? 0.1246 0.1439 0.1274 -0.0166 0.0057  0.0057  16  TRP C CD1 
4384 C  CD2 . TRP C 16  ? 0.1684 0.1430 0.1256 -0.0245 0.0052  -0.0038 16  TRP C CD2 
4385 N  NE1 . TRP C 16  ? 0.1578 0.1556 0.1100 -0.0200 0.0214  -0.0174 16  TRP C NE1 
4386 C  CE2 . TRP C 16  ? 0.1378 0.1326 0.0964 0.0057  0.0073  -0.0120 16  TRP C CE2 
4387 C  CE3 . TRP C 16  ? 0.1513 0.1154 0.1084 -0.0193 0.0120  0.0066  16  TRP C CE3 
4388 C  CZ2 . TRP C 16  ? 0.1653 0.1155 0.1012 -0.0114 0.0104  0.0020  16  TRP C CZ2 
4389 C  CZ3 . TRP C 16  ? 0.1289 0.1292 0.1145 -0.0109 0.0242  0.0111  16  TRP C CZ3 
4390 C  CH2 . TRP C 16  ? 0.1312 0.1456 0.1181 0.0059  -0.0331 -0.0076 16  TRP C CH2 
4391 N  N   . HIS C 17  ? 0.1520 0.1659 0.1215 0.0032  0.0218  -0.0032 17  HIS C N   
4392 C  CA  . HIS C 17  ? 0.1561 0.1586 0.1333 0.0060  0.0176  0.0049  17  HIS C CA  
4393 C  C   . HIS C 17  ? 0.1556 0.1854 0.1289 -0.0156 0.0024  0.0105  17  HIS C C   
4394 O  O   . HIS C 17  ? 0.2036 0.1899 0.1319 -0.0059 0.0392  0.0000  17  HIS C O   
4395 C  CB  . HIS C 17  ? 0.1917 0.2050 0.1134 0.0256  0.0137  0.0044  17  HIS C CB  
4396 C  CG  . HIS C 17  ? 0.2172 0.1852 0.1330 -0.0005 0.0307  0.0209  17  HIS C CG  
4397 N  ND1 . HIS C 17  ? 0.2289 0.2384 0.1687 0.0381  0.0450  0.0032  17  HIS C ND1 
4398 C  CD2 . HIS C 17  ? 0.2055 0.1856 0.1326 0.0208  0.0395  -0.0337 17  HIS C CD2 
4399 C  CE1 . HIS C 17  ? 0.2048 0.2312 0.2088 0.0037  0.0201  -0.0575 17  HIS C CE1 
4400 N  NE2 . HIS C 17  ? 0.2375 0.2073 0.1181 0.0403  0.0328  -0.0082 17  HIS C NE2 
4401 N  N   . LYS C 18  ? 0.1412 0.1756 0.1181 -0.0137 0.0401  0.0115  18  LYS C N   
4402 C  CA  . LYS C 18  ? 0.2285 0.2043 0.1037 0.0057  0.0362  0.0211  18  LYS C CA  
4403 C  C   . LYS C 18  ? 0.1834 0.2199 0.2285 0.0023  0.0599  0.0211  18  LYS C C   
4404 O  O   . LYS C 18  ? 0.2944 0.2492 0.2262 0.0386  0.1150  0.0727  18  LYS C O   
4405 C  CB  . LYS C 18  ? 0.2294 0.1797 0.1186 0.0049  0.0399  0.0082  18  LYS C CB  
4406 C  CG  . LYS C 18  ? 0.2628 0.2278 0.1190 0.0505  0.0142  -0.0131 18  LYS C CG  
4407 C  CD  . LYS C 18  ? 0.2619 0.2199 0.1378 0.0159  0.0538  -0.0434 18  LYS C CD  
4408 C  CE  . LYS C 18  ? 0.1481 0.2339 0.1644 0.0179  -0.0452 0.0080  18  LYS C CE  
4409 N  NZ  . LYS C 18  ? 0.1827 0.2472 0.1565 0.0192  0.0198  -0.0494 18  LYS C NZ  
4410 N  N   . ASP C 19  ? 0.1987 0.2303 0.1445 0.0282  0.0401  -0.0132 19  ASP C N   
4411 C  CA  . ASP C 19  ? 0.2283 0.2205 0.1811 0.0337  -0.0247 0.0017  19  ASP C CA  
4412 C  C   . ASP C 19  ? 0.2926 0.1826 0.1644 0.0054  0.0242  0.0381  19  ASP C C   
4413 O  O   . ASP C 19  ? 0.2865 0.1904 0.1342 0.0310  0.0172  0.0237  19  ASP C O   
4414 C  CB  . ASP C 19  ? 0.2389 0.2569 0.1870 0.0217  0.0081  -0.0285 19  ASP C CB  
4415 C  CG  . ASP C 19  ? 0.2653 0.4129 0.2903 0.0131  -0.0357 0.1086  19  ASP C CG  
4416 O  OD1 . ASP C 19  ? 0.4442 0.4569 0.2994 -0.0692 0.0939  0.0700  19  ASP C OD1 
4417 O  OD2 . ASP C 19  ? 0.5202 0.6570 0.3228 -0.1691 0.1209  0.0041  19  ASP C OD2 
4418 N  N   . PHE C 20  ? 0.2123 0.1856 0.1289 0.0461  0.0265  0.0085  20  PHE C N   
4419 C  CA  . PHE C 20  ? 0.1805 0.1897 0.1270 -0.0362 0.0200  0.0127  20  PHE C CA  
4420 C  C   . PHE C 20  ? 0.1789 0.1581 0.1613 -0.0013 0.0208  0.0252  20  PHE C C   
4421 O  O   . PHE C 20  ? 0.1976 0.1489 0.1259 -0.0031 0.0269  0.0109  20  PHE C O   
4422 C  CB  . PHE C 20  ? 0.1734 0.1678 0.1140 -0.0137 0.0253  0.0142  20  PHE C CB  
4423 C  CG  . PHE C 20  ? 0.1944 0.2140 0.1052 0.0034  0.0351  0.0526  20  PHE C CG  
4424 C  CD1 . PHE C 20  ? 0.2682 0.2612 0.1710 0.0399  0.0335  0.0292  20  PHE C CD1 
4425 C  CD2 . PHE C 20  ? 0.1805 0.2369 0.1341 -0.0049 0.0329  0.0520  20  PHE C CD2 
4426 C  CE1 . PHE C 20  ? 0.2449 0.2673 0.1754 0.0247  0.0463  0.0192  20  PHE C CE1 
4427 C  CE2 . PHE C 20  ? 0.2199 0.2535 0.1789 0.0344  0.0142  0.0432  20  PHE C CE2 
4428 C  CZ  . PHE C 20  ? 0.2640 0.2563 0.1301 0.0054  0.0643  0.0533  20  PHE C CZ  
4429 N  N   . PRO C 21  ? 0.1741 0.1732 0.1292 0.0062  0.0260  0.0137  21  PRO C N   
4430 C  CA  . PRO C 21  ? 0.1527 0.1800 0.1362 -0.0086 0.0137  0.0472  21  PRO C CA  
4431 C  C   . PRO C 21  ? 0.1782 0.1475 0.1385 -0.0205 0.0271  -0.0074 21  PRO C C   
4432 O  O   . PRO C 21  ? 0.1714 0.1993 0.1508 -0.0015 0.0439  0.0097  21  PRO C O   
4433 C  CB  . PRO C 21  ? 0.1766 0.2763 0.1542 0.0054  0.0634  0.0718  21  PRO C CB  
4434 C  CG  . PRO C 21  ? 0.2314 0.2597 0.2908 0.0229  0.0678  0.0982  21  PRO C CG  
4435 C  CD  . PRO C 21  ? 0.2500 0.1990 0.1827 0.0133  0.0507  0.0564  21  PRO C CD  
4436 N  N   A ILE C 22  ? 0.1960 0.1614 0.1286 -0.0010 0.0423  0.0000  22  ILE C N   
4437 N  N   B ILE C 22  ? 0.1568 0.1500 0.1156 -0.0100 0.0262  0.0034  22  ILE C N   
4438 C  CA  A ILE C 22  ? 0.2095 0.1465 0.1340 -0.0177 0.0548  0.0062  22  ILE C CA  
4439 C  CA  B ILE C 22  ? 0.1867 0.1240 0.1213 -0.0138 0.0159  -0.0027 22  ILE C CA  
4440 C  C   A ILE C 22  ? 0.1703 0.1366 0.1468 -0.0137 0.0253  -0.0131 22  ILE C C   
4441 C  C   B ILE C 22  ? 0.1567 0.1215 0.1344 -0.0008 0.0287  -0.0096 22  ILE C C   
4442 O  O   A ILE C 22  ? 0.1800 0.1701 0.1366 0.0020  0.0401  -0.0111 22  ILE C O   
4443 O  O   B ILE C 22  ? 0.1689 0.1671 0.1276 -0.0024 0.0364  -0.0019 22  ILE C O   
4444 C  CB  A ILE C 22  ? 0.2050 0.1542 0.1920 0.0122  0.0463  -0.0015 22  ILE C CB  
4445 C  CB  B ILE C 22  ? 0.1240 0.1784 0.1500 -0.0041 0.0164  -0.0206 22  ILE C CB  
4446 C  CG1 A ILE C 22  ? 0.2175 0.1712 0.2434 -0.0288 0.0153  0.0041  22  ILE C CG1 
4447 C  CG1 B ILE C 22  ? 0.1414 0.0970 0.1392 -0.0055 0.0054  0.0463  22  ILE C CG1 
4448 C  CG2 A ILE C 22  ? 0.2023 0.2037 0.1856 -0.0074 0.0408  -0.0222 22  ILE C CG2 
4449 C  CG2 B ILE C 22  ? 0.1172 0.1420 0.0879 -0.0126 -0.0229 0.0140  22  ILE C CG2 
4450 C  CD1 A ILE C 22  ? 0.1804 0.2071 0.2293 -0.0227 0.0938  0.0315  22  ILE C CD1 
4451 C  CD1 B ILE C 22  ? 0.1447 0.1253 0.1520 0.0068  0.0282  0.0219  22  ILE C CD1 
4452 N  N   . ALA C 23  ? 0.1453 0.1473 0.1328 -0.0043 0.0263  -0.0073 23  ALA C N   
4453 C  CA  . ALA C 23  ? 0.1635 0.1479 0.1138 0.0129  0.0160  -0.0091 23  ALA C CA  
4454 C  C   . ALA C 23  ? 0.1416 0.1687 0.1283 -0.0003 0.0236  -0.0003 23  ALA C C   
4455 O  O   . ALA C 23  ? 0.1680 0.1412 0.1464 0.0038  0.0218  0.0021  23  ALA C O   
4456 C  CB  . ALA C 23  ? 0.1955 0.1486 0.1244 -0.0251 0.0480  -0.0269 23  ALA C CB  
4457 N  N   . LYS C 24  ? 0.1515 0.1498 0.1671 -0.0054 0.0313  -0.0071 24  LYS C N   
4458 C  CA  . LYS C 24  ? 0.1301 0.1791 0.1445 -0.0032 0.0625  -0.0043 24  LYS C CA  
4459 C  C   . LYS C 24  ? 0.1798 0.2251 0.1568 0.0027  0.0100  -0.0035 24  LYS C C   
4460 O  O   . LYS C 24  ? 0.1754 0.2440 0.1827 -0.0161 0.0456  0.0046  24  LYS C O   
4461 C  CB  . LYS C 24  ? 0.1852 0.2090 0.1588 0.0264  0.0485  -0.0110 24  LYS C CB  
4462 C  CG  . LYS C 24  ? 0.2325 0.2583 0.1639 -0.0120 0.0362  -0.0263 24  LYS C CG  
4463 C  CD  . LYS C 24  ? 0.3005 0.2874 0.1489 0.0362  0.0461  -0.0151 24  LYS C CD  
4464 C  CE  . LYS C 24  ? 0.2980 0.2860 0.1890 0.0024  0.0768  -0.0248 24  LYS C CE  
4465 N  NZ  . LYS C 24  ? 0.5763 0.2899 0.2901 0.0335  0.0062  -0.0136 24  LYS C NZ  
4466 N  N   . GLY C 25  ? 0.1932 0.1763 0.1750 -0.0120 0.0206  -0.0230 25  GLY C N   
4467 C  CA  . GLY C 25  ? 0.1888 0.2226 0.1507 -0.0419 0.0010  0.0046  25  GLY C CA  
4468 C  C   . GLY C 25  ? 0.1326 0.1799 0.1563 0.0020  0.0091  -0.0140 25  GLY C C   
4469 O  O   . GLY C 25  ? 0.1452 0.2030 0.1787 -0.0104 0.0348  -0.0103 25  GLY C O   
4470 N  N   . GLU C 26  ? 0.1347 0.2064 0.1601 -0.0307 0.0509  -0.0218 26  GLU C N   
4471 C  CA  . GLU C 26  ? 0.1298 0.2011 0.1755 -0.0203 0.0152  0.0006  26  GLU C CA  
4472 C  C   . GLU C 26  ? 0.1597 0.1840 0.1603 -0.0028 0.0153  -0.0215 26  GLU C C   
4473 O  O   . GLU C 26  ? 0.1438 0.2091 0.1876 0.0026  -0.0111 -0.0143 26  GLU C O   
4474 C  CB  . GLU C 26  ? 0.1613 0.2529 0.1705 -0.0775 0.0131  0.0164  26  GLU C CB  
4475 C  CG  . GLU C 26  ? 0.1721 0.2858 0.2081 -0.0305 0.0386  0.0152  26  GLU C CG  
4476 C  CD  . GLU C 26  ? 0.2782 0.3515 0.3287 0.0043  0.1155  -0.0311 26  GLU C CD  
4477 O  OE1 . GLU C 26  ? 0.2942 0.4354 0.4151 0.0337  0.0469  -0.0137 26  GLU C OE1 
4478 O  OE2 . GLU C 26  ? 0.4496 0.6524 0.3488 0.0903  0.1243  -0.0529 26  GLU C OE2 
4479 N  N   . ARG C 27  ? 0.1488 0.1517 0.1448 -0.0161 -0.0062 -0.0129 27  ARG C N   
4480 C  CA  . ARG C 27  ? 0.1240 0.1368 0.1098 -0.0138 -0.0071 0.0081  27  ARG C CA  
4481 C  C   . ARG C 27  ? 0.1150 0.1281 0.1443 0.0006  0.0193  -0.0054 27  ARG C C   
4482 O  O   . ARG C 27  ? 0.1159 0.1357 0.1358 -0.0057 0.0152  -0.0138 27  ARG C O   
4483 C  CB  . ARG C 27  ? 0.1635 0.1558 0.2166 -0.0087 -0.0203 -0.0233 27  ARG C CB  
4484 C  CG  . ARG C 27  ? 0.1879 0.1793 0.1949 -0.0397 -0.0003 0.0124  27  ARG C CG  
4485 C  CD  . ARG C 27  ? 0.2104 0.2459 0.2406 0.0485  0.0087  -0.0032 27  ARG C CD  
4486 N  NE  . ARG C 27  ? 0.1962 0.2114 0.2009 0.0217  -0.0267 -0.0414 27  ARG C NE  
4487 C  CZ  . ARG C 27  ? 0.1412 0.1423 0.2134 0.0078  -0.0186 -0.0472 27  ARG C CZ  
4488 N  NH1 . ARG C 27  ? 0.1646 0.2483 0.2488 -0.0908 0.0005  -0.0944 27  ARG C NH1 
4489 N  NH2 . ARG C 27  ? 0.2052 0.1931 0.1802 -0.0284 0.0135  -0.0178 27  ARG C NH2 
4490 N  N   . GLN C 28  ? 0.1224 0.1447 0.1186 -0.0143 0.0165  -0.0109 28  GLN C N   
4491 C  CA  . GLN C 28  ? 0.1360 0.1414 0.1167 -0.0271 0.0057  -0.0027 28  GLN C CA  
4492 C  C   . GLN C 28  ? 0.1142 0.1084 0.1089 0.0012  0.0055  -0.0068 28  GLN C C   
4493 O  O   . GLN C 28  ? 0.1032 0.1237 0.1269 -0.0057 -0.0063 -0.0076 28  GLN C O   
4494 C  CB  . GLN C 28  ? 0.1315 0.1511 0.1086 -0.0192 0.0118  -0.0083 28  GLN C CB  
4495 C  CG  . GLN C 28  ? 0.1298 0.1305 0.1407 -0.0124 0.0060  -0.0020 28  GLN C CG  
4496 C  CD  . GLN C 28  ? 0.1019 0.1254 0.1237 -0.0195 0.0127  -0.0149 28  GLN C CD  
4497 O  OE1 . GLN C 28  ? 0.1165 0.1156 0.1252 -0.0200 0.0076  -0.0015 28  GLN C OE1 
4498 N  NE2 . GLN C 28  ? 0.1396 0.1233 0.0949 -0.0151 0.0308  -0.0049 28  GLN C NE2 
4499 N  N   . SER C 29  ? 0.0994 0.1033 0.0912 -0.0166 0.0000  -0.0035 29  SER C N   
4500 C  CA  . SER C 29  ? 0.0957 0.1064 0.0994 -0.0099 0.0200  -0.0124 29  SER C CA  
4501 C  C   . SER C 29  ? 0.1116 0.1067 0.0913 -0.0159 0.0003  -0.0098 29  SER C C   
4502 O  O   . SER C 29  ? 0.1174 0.1102 0.0985 -0.0124 0.0048  0.0026  29  SER C O   
4503 C  CB  . SER C 29  ? 0.1023 0.0924 0.1199 0.0017  0.0113  -0.0237 29  SER C CB  
4504 O  OG  . SER C 29  ? 0.1114 0.1035 0.1143 -0.0130 0.0000  0.0031  29  SER C OG  
4505 N  N   . PRO C 30  ? 0.0956 0.1014 0.0922 0.0059  0.0013  -0.0080 30  PRO C N   
4506 C  CA  . PRO C 30  ? 0.0847 0.0960 0.0966 0.0051  0.0006  0.0048  30  PRO C CA  
4507 C  C   . PRO C 30  ? 0.0811 0.1066 0.0836 -0.0111 -0.0120 -0.0104 30  PRO C C   
4508 O  O   . PRO C 30  ? 0.0989 0.1024 0.0908 0.0023  0.0052  -0.0057 30  PRO C O   
4509 C  CB  . PRO C 30  ? 0.1082 0.0933 0.0917 -0.0137 0.0098  -0.0199 30  PRO C CB  
4510 C  CG  . PRO C 30  ? 0.0976 0.1254 0.0850 -0.0043 0.0010  -0.0038 30  PRO C CG  
4511 C  CD  . PRO C 30  ? 0.0931 0.1177 0.1048 -0.0212 -0.0048 -0.0035 30  PRO C CD  
4512 N  N   . VAL C 31  ? 0.0962 0.1037 0.0915 0.0094  -0.0115 0.0027  31  VAL C N   
4513 C  CA  . VAL C 31  ? 0.0900 0.0857 0.1308 0.0052  -0.0148 0.0115  31  VAL C CA  
4514 C  C   . VAL C 31  ? 0.1019 0.1014 0.1109 0.0027  -0.0003 0.0062  31  VAL C C   
4515 O  O   . VAL C 31  ? 0.1091 0.1164 0.1222 0.0196  0.0078  -0.0003 31  VAL C O   
4516 C  CB  . VAL C 31  ? 0.1299 0.1055 0.1195 -0.0098 -0.0218 -0.0140 31  VAL C CB  
4517 C  CG1 . VAL C 31  ? 0.1358 0.1204 0.1536 -0.0170 -0.0179 -0.0060 31  VAL C CG1 
4518 C  CG2 . VAL C 31  ? 0.1299 0.1243 0.1287 -0.0027 -0.0080 -0.0175 31  VAL C CG2 
4519 N  N   . ASP C 32  ? 0.1142 0.1107 0.1146 0.0220  -0.0059 -0.0006 32  ASP C N   
4520 C  CA  . ASP C 32  ? 0.1185 0.1086 0.1165 0.0138  -0.0006 -0.0017 32  ASP C CA  
4521 C  C   . ASP C 32  ? 0.1134 0.0992 0.1242 0.0148  -0.0062 -0.0006 32  ASP C C   
4522 O  O   . ASP C 32  ? 0.1407 0.1605 0.1556 -0.0125 0.0024  -0.0087 32  ASP C O   
4523 C  CB  . ASP C 32  ? 0.1271 0.1228 0.1482 0.0156  0.0051  -0.0148 32  ASP C CB  
4524 C  CG  . ASP C 32  ? 0.1242 0.1425 0.1418 0.0155  -0.0054 -0.0118 32  ASP C CG  
4525 O  OD1 . ASP C 32  ? 0.1346 0.1080 0.1532 0.0087  -0.0021 0.0040  32  ASP C OD1 
4526 O  OD2 . ASP C 32  ? 0.1423 0.1373 0.2037 0.0138  -0.0152 0.0208  32  ASP C OD2 
4527 N  N   . ILE C 33  ? 0.1240 0.1039 0.1107 0.0175  -0.0015 -0.0144 33  ILE C N   
4528 C  CA  . ILE C 33  ? 0.1332 0.1240 0.1197 0.0251  0.0000  -0.0274 33  ILE C CA  
4529 C  C   . ILE C 33  ? 0.1356 0.1174 0.1298 -0.0071 -0.0197 -0.0164 33  ILE C C   
4530 O  O   . ILE C 33  ? 0.1427 0.1358 0.1423 0.0110  -0.0109 -0.0006 33  ILE C O   
4531 C  CB  . ILE C 33  ? 0.1353 0.1206 0.1138 0.0275  -0.0038 -0.0057 33  ILE C CB  
4532 C  CG1 . ILE C 33  ? 0.1301 0.1088 0.1493 0.0259  -0.0154 0.0126  33  ILE C CG1 
4533 C  CG2 . ILE C 33  ? 0.1378 0.1714 0.1188 0.0211  -0.0326 -0.0229 33  ILE C CG2 
4534 C  CD1 . ILE C 33  ? 0.1691 0.1310 0.1748 0.0350  0.0195  -0.0077 33  ILE C CD1 
4535 N  N   . ASP C 34  ? 0.1402 0.1410 0.1723 0.0291  -0.0271 -0.0176 34  ASP C N   
4536 C  CA  . ASP C 34  ? 0.2034 0.1396 0.1662 0.0368  -0.0052 0.0108  34  ASP C CA  
4537 C  C   . ASP C 34  ? 0.1455 0.1750 0.1924 0.0467  -0.0309 0.0027  34  ASP C C   
4538 O  O   . ASP C 34  ? 0.1802 0.1716 0.2293 0.0275  -0.0410 -0.0052 34  ASP C O   
4539 C  CB  . ASP C 34  ? 0.1633 0.1561 0.2019 0.0256  -0.0201 -0.0436 34  ASP C CB  
4540 C  CG  . ASP C 34  ? 0.2824 0.1725 0.2224 0.0529  -0.0038 -0.0082 34  ASP C CG  
4541 O  OD1 . ASP C 34  ? 0.2242 0.2212 0.2339 0.0644  -0.0399 -0.0078 34  ASP C OD1 
4542 O  OD2 . ASP C 34  ? 0.3131 0.3269 0.2748 0.0922  0.0124  0.0339  34  ASP C OD2 
4543 N  N   . THR C 35  ? 0.1495 0.1513 0.1700 0.0373  -0.0318 0.0000  35  THR C N   
4544 C  CA  . THR C 35  ? 0.1651 0.1824 0.1748 0.0410  -0.0203 -0.0250 35  THR C CA  
4545 C  C   . THR C 35  ? 0.2002 0.2348 0.2125 0.0573  -0.0640 -0.0412 35  THR C C   
4546 O  O   . THR C 35  ? 0.2513 0.2152 0.2206 0.0359  -0.0961 -0.0328 35  THR C O   
4547 C  CB  . THR C 35  ? 0.2169 0.1840 0.1492 0.0416  -0.0149 -0.0129 35  THR C CB  
4548 O  OG1 . THR C 35  ? 0.2294 0.2066 0.1956 0.0522  -0.0627 -0.0137 35  THR C OG1 
4549 C  CG2 . THR C 35  ? 0.2072 0.2509 0.2012 0.0626  -0.0480 -0.0709 35  THR C CG2 
4550 N  N   . HIS C 36  ? 0.2116 0.2381 0.2090 0.0410  -0.0974 -0.0324 36  HIS C N   
4551 C  CA  . HIS C 36  ? 0.1974 0.1980 0.2642 0.0719  -0.1196 -0.0328 36  HIS C CA  
4552 C  C   . HIS C 36  ? 0.3251 0.2572 0.2488 0.0140  -0.0825 0.0081  36  HIS C C   
4553 O  O   . HIS C 36  ? 0.3495 0.2468 0.4050 0.0188  -0.1090 0.0630  36  HIS C O   
4554 C  CB  . HIS C 36  ? 0.2494 0.2016 0.3711 0.0729  -0.1277 -0.0560 36  HIS C CB  
4555 C  CG  . HIS C 36  ? 0.1822 0.2594 0.3337 0.0957  -0.0401 -0.0668 36  HIS C CG  
4556 N  ND1 . HIS C 36  ? 0.2163 0.2199 0.4753 0.0355  0.0329  0.1293  36  HIS C ND1 
4557 C  CD2 . HIS C 36  ? 0.2097 0.2597 0.4588 0.1323  -0.0496 -0.0456 36  HIS C CD2 
4558 C  CE1 . HIS C 36  ? 0.2660 0.1917 0.4801 0.0632  -0.0878 -0.0500 36  HIS C CE1 
4559 N  NE2 . HIS C 36  ? 0.2506 0.2879 0.4279 0.0780  0.0103  0.0098  36  HIS C NE2 
4560 N  N   . THR C 37  ? 0.2321 0.1763 0.2434 0.0120  -0.0719 -0.0211 37  THR C N   
4561 C  CA  . THR C 37  ? 0.1994 0.1747 0.2671 0.0322  -0.0460 -0.0241 37  THR C CA  
4562 C  C   . THR C 37  ? 0.1924 0.1966 0.3485 0.0548  0.0003  -0.0366 37  THR C C   
4563 O  O   . THR C 37  ? 0.2231 0.2475 0.3273 0.0285  -0.0474 -0.0350 37  THR C O   
4564 C  CB  . THR C 37  ? 0.3468 0.4190 0.3102 0.1269  -0.0083 -0.0969 37  THR C CB  
4565 O  OG1 . THR C 37  ? 0.2978 0.3655 0.3680 0.0258  -0.0182 -0.0454 37  THR C OG1 
4566 C  CG2 . THR C 37  ? 0.3831 0.2450 0.2529 0.0326  -0.0197 -0.0848 37  THR C CG2 
4567 N  N   . ALA C 38  ? 0.1877 0.2023 0.1756 0.0318  -0.0654 -0.0368 38  ALA C N   
4568 C  CA  . ALA C 38  ? 0.1896 0.1799 0.2293 0.0555  -0.0965 -0.0456 38  ALA C CA  
4569 C  C   . ALA C 38  ? 0.2592 0.2249 0.2021 0.0225  -0.0533 -0.0132 38  ALA C C   
4570 O  O   . ALA C 38  ? 0.2906 0.2208 0.2179 0.0344  -0.0619 -0.0192 38  ALA C O   
4571 C  CB  . ALA C 38  ? 0.2048 0.1818 0.2269 0.0370  -0.0535 -0.0434 38  ALA C CB  
4572 N  N   . LYS C 39  ? 0.1730 0.2062 0.1790 0.0175  -0.0305 -0.0450 39  LYS C N   
4573 C  CA  . LYS C 39  ? 0.1976 0.2477 0.2005 0.0675  -0.0337 -0.0709 39  LYS C CA  
4574 C  C   . LYS C 39  ? 0.2554 0.1994 0.1748 0.0553  -0.0208 -0.0441 39  LYS C C   
4575 O  O   . LYS C 39  ? 0.1791 0.2163 0.1991 0.0428  -0.0705 -0.0498 39  LYS C O   
4576 C  CB  . LYS C 39  ? 0.2157 0.2863 0.3109 0.0035  -0.0137 -0.0597 39  LYS C CB  
4577 C  CG  . LYS C 39  ? 0.2795 0.4167 0.2793 -0.0483 -0.0676 0.0031  39  LYS C CG  
4578 C  CD  . LYS C 39  ? 0.2691 0.3580 0.2445 0.0815  0.0438  -0.0697 39  LYS C CD  
4579 C  CE  . LYS C 39  ? 0.2930 0.4704 0.2436 0.0834  -0.0575 -0.0219 39  LYS C CE  
4580 N  NZ  . LYS C 39  ? 0.2790 0.4470 0.2646 0.1015  -0.0379 -0.0511 39  LYS C NZ  
4581 N  N   . TYR C 40  ? 0.1906 0.2389 0.1915 0.0419  -0.0320 -0.0052 40  TYR C N   
4582 C  CA  . TYR C 40  ? 0.2285 0.2797 0.1739 -0.0057 -0.0474 -0.0017 40  TYR C CA  
4583 C  C   . TYR C 40  ? 0.1664 0.2520 0.2396 0.0175  -0.0339 -0.0248 40  TYR C C   
4584 O  O   . TYR C 40  ? 0.1926 0.3095 0.2238 -0.0071 -0.0465 -0.0178 40  TYR C O   
4585 C  CB  . TYR C 40  ? 0.3023 0.3488 0.1904 0.0350  -0.1199 0.0445  40  TYR C CB  
4586 C  CG  . TYR C 40  ? 0.2671 0.3591 0.2402 0.0038  -0.0690 -0.0024 40  TYR C CG  
4587 C  CD1 . TYR C 40  ? 0.2757 0.2470 0.3233 -0.0249 -0.0918 0.0044  40  TYR C CD1 
4588 C  CD2 . TYR C 40  ? 0.3458 0.5677 0.3055 0.0573  -0.1747 -0.0068 40  TYR C CD2 
4589 C  CE1 . TYR C 40  ? 0.2635 0.3923 0.3163 -0.0096 -0.0684 -0.0225 40  TYR C CE1 
4590 C  CE2 . TYR C 40  ? 0.4167 0.5486 0.4248 0.0089  -0.1281 -0.0163 40  TYR C CE2 
4591 C  CZ  . TYR C 40  ? 0.4011 0.4875 0.2748 -0.0111 -0.0734 -0.0480 40  TYR C CZ  
4592 O  OH  . TYR C 40  ? 0.4645 0.5817 0.2233 -0.0168 -0.0763 -0.0320 40  TYR C OH  
4593 N  N   . ASP C 41  ? 0.2709 0.2063 0.1405 0.0258  -0.0282 -0.0410 41  ASP C N   
4594 C  CA  . ASP C 41  ? 0.1389 0.2414 0.3156 -0.0126 0.0015  -0.0342 41  ASP C CA  
4595 C  C   . ASP C 41  ? 0.2962 0.4004 0.2289 0.0103  -0.0181 -0.0463 41  ASP C C   
4596 O  O   . ASP C 41  ? 0.2958 0.3434 0.2063 0.0239  0.0013  0.0080  41  ASP C O   
4597 C  CB  . ASP C 41  ? 0.4244 0.2818 0.2953 -0.0701 0.0230  -0.0141 41  ASP C CB  
4598 C  CG  . ASP C 41  ? 0.4494 0.3246 0.4688 -0.0782 0.0546  -0.0153 41  ASP C CG  
4599 O  OD1 . ASP C 41  ? 0.2896 0.3804 0.4998 -0.0174 0.0522  -0.0886 41  ASP C OD1 
4600 O  OD2 . ASP C 41  ? 0.4334 0.3729 0.4329 0.0205  0.1101  0.0650  41  ASP C OD2 
4601 N  N   . PRO C 42  ? 0.2393 0.4865 0.2601 -0.0193 -0.0417 -0.0932 42  PRO C N   
4602 C  CA  . PRO C 42  ? 0.3445 0.4790 0.2052 0.0241  -0.0742 -0.1345 42  PRO C CA  
4603 C  C   . PRO C 42  ? 0.3316 0.4616 0.2003 0.0513  -0.0421 -0.0340 42  PRO C C   
4604 O  O   . PRO C 42  ? 0.4423 0.4654 0.2612 0.0359  0.0375  -0.0881 42  PRO C O   
4605 C  CB  . PRO C 42  ? 0.3883 0.5720 0.2263 0.0698  -0.0775 -0.0826 42  PRO C CB  
4606 C  CG  . PRO C 42  ? 0.3555 0.6065 0.2524 0.0249  -0.1000 -0.1340 42  PRO C CG  
4607 C  CD  . PRO C 42  ? 0.3203 0.4040 0.2239 0.0599  -0.1451 -0.0772 42  PRO C CD  
4608 N  N   . SER C 43  ? 0.2746 0.2899 0.2734 0.0289  -0.0794 -0.0586 43  SER C N   
4609 C  CA  . SER C 43  ? 0.3400 0.2433 0.4602 -0.0403 -0.1115 -0.0614 43  SER C CA  
4610 C  C   . SER C 43  ? 0.3156 0.3251 0.4178 0.0111  -0.0540 -0.0621 43  SER C C   
4611 O  O   . SER C 43  ? 0.4995 0.3616 0.6001 0.0688  0.1879  -0.0428 43  SER C O   
4612 C  CB  . SER C 43  ? 0.5453 0.4117 0.4650 -0.0648 0.0262  -0.0644 43  SER C CB  
4613 O  OG  . SER C 43  ? 0.3547 0.4295 0.4269 -0.1905 -0.0198 0.0122  43  SER C OG  
4614 N  N   . LEU C 44  ? 0.2518 0.3368 0.3064 0.0500  -0.0168 -0.0577 44  LEU C N   
4615 C  CA  . LEU C 44  ? 0.2463 0.3880 0.4875 0.1030  -0.0190 -0.0024 44  LEU C CA  
4616 C  C   . LEU C 44  ? 0.4423 0.5253 0.3662 0.1462  0.0397  0.0899  44  LEU C C   
4617 O  O   . LEU C 44  ? 0.3046 0.4828 0.3935 0.0513  0.0579  0.1209  44  LEU C O   
4618 C  CB  . LEU C 44  ? 0.2694 0.3962 0.2752 0.0562  -0.0102 0.0564  44  LEU C CB  
4619 C  CG  . LEU C 44  ? 0.2594 0.3210 0.2407 0.0636  -0.0272 -0.0089 44  LEU C CG  
4620 C  CD1 . LEU C 44  ? 0.3041 0.3623 0.1524 -0.0476 0.0027  0.0251  44  LEU C CD1 
4621 C  CD2 . LEU C 44  ? 0.2838 0.2777 0.2915 0.0837  -0.0500 -0.0524 44  LEU C CD2 
4622 N  N   . LYS C 45  ? 0.3826 0.3973 0.4205 0.0692  0.0913  0.0800  45  LYS C N   
4623 C  CA  . LYS C 45  ? 0.4484 0.3982 0.4394 0.0483  0.1046  -0.0432 45  LYS C CA  
4624 C  C   . LYS C 45  ? 0.3912 0.4693 0.2829 0.0762  0.0383  -0.0082 45  LYS C C   
4625 O  O   . LYS C 45  ? 0.4240 0.4686 0.2063 -0.0467 -0.0070 0.0441  45  LYS C O   
4626 C  CB  . LYS C 45  ? 0.3170 0.3070 0.3422 0.0003  -0.0601 -0.2011 45  LYS C CB  
4627 C  CG  . LYS C 45  ? 0.6226 0.8406 0.8183 -0.1098 -0.0597 0.0073  45  LYS C CG  
4628 C  CD  . LYS C 45  ? 0.7749 0.7087 0.6018 0.1657  -0.0944 -0.2186 45  LYS C CD  
4629 C  CE  . LYS C 45  ? 0.7200 0.6366 0.9556 -0.0256 -0.1001 0.2381  45  LYS C CE  
4630 N  NZ  . LYS C 45  ? 0.6295 0.6547 0.7925 0.0023  -0.0220 0.2824  45  LYS C NZ  
4631 N  N   . PRO C 46  ? 0.2615 0.3790 0.2264 0.0199  -0.0245 0.0657  46  PRO C N   
4632 C  CA  . PRO C 46  ? 0.3334 0.2791 0.2199 0.0634  0.0097  0.0260  46  PRO C CA  
4633 C  C   . PRO C 46  ? 0.2369 0.2711 0.2048 0.0297  -0.0304 0.0044  46  PRO C C   
4634 O  O   . PRO C 46  ? 0.3077 0.3034 0.1382 0.0489  0.0130  0.0328  46  PRO C O   
4635 C  CB  . PRO C 46  ? 0.2953 0.3594 0.2452 -0.0038 0.0131  0.0742  46  PRO C CB  
4636 C  CG  . PRO C 46  ? 0.3970 0.3914 0.1926 -0.0384 -0.0237 -0.0562 46  PRO C CG  
4637 C  CD  . PRO C 46  ? 0.3192 0.3350 0.2590 0.0035  -0.0329 -0.0155 46  PRO C CD  
4638 N  N   . LEU C 47  ? 0.3472 0.3379 0.1933 0.0926  0.0220  -0.0147 47  LEU C N   
4639 C  CA  . LEU C 47  ? 0.3208 0.2955 0.1559 0.0680  0.0294  0.0351  47  LEU C CA  
4640 C  C   . LEU C 47  ? 0.3438 0.2267 0.2382 0.0903  0.1045  0.0657  47  LEU C C   
4641 O  O   . LEU C 47  ? 0.3564 0.2978 0.2353 0.1176  0.1190  0.1001  47  LEU C O   
4642 C  CB  . LEU C 47  ? 0.4740 0.2865 0.2800 0.0747  -0.0163 0.0120  47  LEU C CB  
4643 C  CG  . LEU C 47  ? 0.4140 0.3587 0.2275 -0.0549 0.0803  0.0318  47  LEU C CG  
4644 C  CD1 . LEU C 47  ? 0.4535 0.3668 0.1685 -0.0368 0.1296  0.0445  47  LEU C CD1 
4645 C  CD2 . LEU C 47  ? 0.3743 0.2287 0.2357 -0.0161 0.0791  0.0329  47  LEU C CD2 
4646 N  N   . SER C 48  ? 0.2296 0.2233 0.1261 0.0560  0.0303  0.0167  48  SER C N   
4647 C  CA  . SER C 48  ? 0.2255 0.2230 0.1310 0.0192  0.0041  -0.0049 48  SER C CA  
4648 C  C   . SER C 48  ? 0.2317 0.1793 0.1611 0.0228  -0.0153 0.0226  48  SER C C   
4649 O  O   . SER C 48  ? 0.2569 0.1949 0.1572 -0.0178 0.0055  0.0226  48  SER C O   
4650 C  CB  . SER C 48  ? 0.2524 0.2342 0.1825 -0.0115 -0.0066 0.0007  48  SER C CB  
4651 O  OG  . SER C 48  ? 0.3027 0.2459 0.1721 0.0364  0.0076  0.0020  48  SER C OG  
4652 N  N   . VAL C 49  ? 0.2500 0.2105 0.1872 0.0076  -0.0182 0.0309  49  VAL C N   
4653 C  CA  . VAL C 49  ? 0.2255 0.1886 0.1691 -0.0187 -0.0197 0.0293  49  VAL C CA  
4654 C  C   . VAL C 49  ? 0.2795 0.2303 0.1698 -0.0110 0.0379  0.0381  49  VAL C C   
4655 O  O   . VAL C 49  ? 0.3526 0.3190 0.2321 -0.0859 0.0383  0.1042  49  VAL C O   
4656 C  CB  . VAL C 49  ? 0.2606 0.1910 0.2170 -0.0562 -0.0231 0.0494  49  VAL C CB  
4657 C  CG1 . VAL C 49  ? 0.2786 0.3134 0.2852 -0.0461 -0.0738 0.0109  49  VAL C CG1 
4658 C  CG2 . VAL C 49  ? 0.2888 0.2330 0.2199 0.0153  -0.0170 0.0790  49  VAL C CG2 
4659 N  N   . SER C 50  ? 0.2269 0.2174 0.2193 -0.0008 0.0051  0.0294  50  SER C N   
4660 C  CA  . SER C 50  ? 0.2572 0.2276 0.1987 -0.0340 0.0412  0.0178  50  SER C CA  
4661 C  C   . SER C 50  ? 0.2152 0.2036 0.1511 0.0006  0.0394  -0.0027 50  SER C C   
4662 O  O   . SER C 50  ? 0.2246 0.2068 0.2064 -0.0057 0.0403  0.0399  50  SER C O   
4663 C  CB  . SER C 50  ? 0.3201 0.2854 0.1750 -0.0688 -0.0111 0.0167  50  SER C CB  
4664 O  OG  . SER C 50  ? 0.3054 0.3594 0.2387 -0.0187 0.0087  0.0010  50  SER C OG  
4665 N  N   . TYR C 51  ? 0.2039 0.1981 0.1617 -0.0167 0.0228  -0.0071 51  TYR C N   
4666 C  CA  . TYR C 51  ? 0.1771 0.1883 0.1675 0.0297  0.0153  0.0160  51  TYR C CA  
4667 C  C   . TYR C 51  ? 0.2148 0.1951 0.2011 0.0425  0.0109  0.0046  51  TYR C C   
4668 O  O   . TYR C 51  ? 0.1840 0.2454 0.2233 0.0209  0.0346  -0.0003 51  TYR C O   
4669 C  CB  . TYR C 51  ? 0.1838 0.1820 0.1922 -0.0165 0.0379  -0.0030 51  TYR C CB  
4670 C  CG  . TYR C 51  ? 0.1748 0.1870 0.1689 0.0135  0.0214  0.0317  51  TYR C CG  
4671 C  CD1 . TYR C 51  ? 0.1964 0.1511 0.1772 0.0240  0.0339  0.0124  51  TYR C CD1 
4672 C  CD2 . TYR C 51  ? 0.1734 0.1764 0.1718 0.0390  0.0198  0.0221  51  TYR C CD2 
4673 C  CE1 . TYR C 51  ? 0.1935 0.1353 0.1299 0.0171  0.0258  0.0024  51  TYR C CE1 
4674 C  CE2 . TYR C 51  ? 0.1732 0.1678 0.1286 -0.0028 0.0130  0.0195  51  TYR C CE2 
4675 C  CZ  . TYR C 51  ? 0.1420 0.1344 0.1301 0.0172  -0.0041 0.0038  51  TYR C CZ  
4676 O  OH  . TYR C 51  ? 0.1680 0.1577 0.1509 0.0031  0.0229  0.0012  51  TYR C OH  
4677 N  N   . ASP C 52  ? 0.3014 0.2411 0.2023 0.0516  0.0764  0.0000  52  ASP C N   
4678 C  CA  . ASP C 52  ? 0.2908 0.3253 0.1896 0.0829  0.0430  0.0063  52  ASP C CA  
4679 C  C   . ASP C 52  ? 0.3282 0.2430 0.2472 0.0359  0.0370  -0.0137 52  ASP C C   
4680 O  O   . ASP C 52  ? 0.3210 0.3684 0.3916 0.0872  0.0879  0.0000  52  ASP C O   
4681 C  CB  . ASP C 52  ? 0.3086 0.3578 0.1856 0.0773  -0.0091 -0.0211 52  ASP C CB  
4682 C  CG  . ASP C 52  ? 0.4862 0.4650 0.2967 -0.0062 0.0544  -0.0991 52  ASP C CG  
4683 O  OD1 . ASP C 52  ? 0.6832 0.6838 0.4183 0.0193  0.1858  0.0104  52  ASP C OD1 
4684 O  OD2 . ASP C 52  ? 1.0182 0.5659 0.4333 0.3876  0.0251  -0.0636 52  ASP C OD2 
4685 N  N   . GLN C 53  ? 0.3061 0.2504 0.1939 0.0381  0.0450  -0.0564 53  GLN C N   
4686 C  CA  . GLN C 53  ? 0.4187 0.2754 0.2357 0.0731  0.0243  0.0034  53  GLN C CA  
4687 C  C   . GLN C 53  ? 0.3427 0.2125 0.2188 0.0386  0.0211  -0.0177 53  GLN C C   
4688 O  O   . GLN C 53  ? 0.3161 0.2305 0.2460 0.0428  0.0318  0.0092  53  GLN C O   
4689 C  CB  . GLN C 53  ? 0.3666 0.2793 0.2429 -0.0221 0.0725  0.0085  53  GLN C CB  
4690 C  CG  . GLN C 53  ? 0.5730 0.4923 0.2955 0.0298  0.0296  -0.0648 53  GLN C CG  
4691 C  CD  . GLN C 53  ? 0.5899 0.6568 0.3607 0.1233  0.1260  0.0082  53  GLN C CD  
4692 O  OE1 . GLN C 53  ? 0.4489 0.6912 0.4692 0.2310  0.1638  0.0842  53  GLN C OE1 
4693 N  NE2 . GLN C 53  ? 0.8780 0.5848 0.3986 0.2400  -0.0324 0.0617  53  GLN C NE2 
4694 N  N   . ALA C 54  ? 0.2691 0.1920 0.1971 0.0244  0.0491  0.0307  54  ALA C N   
4695 C  CA  . ALA C 54  ? 0.2120 0.2077 0.1693 0.0176  0.0368  0.0085  54  ALA C CA  
4696 C  C   . ALA C 54  ? 0.2195 0.2266 0.2281 0.0005  0.0368  -0.0081 54  ALA C C   
4697 O  O   . ALA C 54  ? 0.3149 0.3039 0.2237 -0.0825 0.0674  -0.0023 54  ALA C O   
4698 C  CB  . ALA C 54  ? 0.2429 0.2123 0.2619 0.0020  0.0287  -0.0032 54  ALA C CB  
4699 N  N   A THR C 55  ? 0.2020 0.1932 0.1788 0.0357  0.0255  -0.0181 55  THR C N   
4700 N  N   B THR C 55  ? 0.1926 0.1914 0.1791 0.0434  0.0291  -0.0249 55  THR C N   
4701 C  CA  A THR C 55  ? 0.2436 0.2003 0.2452 0.0308  -0.0063 -0.0237 55  THR C CA  
4702 C  CA  B THR C 55  ? 0.2086 0.2093 0.2398 0.0671  0.0222  -0.0381 55  THR C CA  
4703 C  C   A THR C 55  ? 0.1316 0.1581 0.2195 0.0333  -0.0178 0.0275  55  THR C C   
4704 C  C   B THR C 55  ? 0.1617 0.1622 0.2016 0.0236  0.0057  0.0199  55  THR C C   
4705 O  O   A THR C 55  ? 0.1233 0.1371 0.1884 0.0505  0.0063  -0.0043 55  THR C O   
4706 O  O   B THR C 55  ? 0.1720 0.1342 0.1511 0.0249  0.0063  0.0012  55  THR C O   
4707 C  CB  A THR C 55  ? 0.2879 0.2346 0.3689 0.0511  0.0141  -0.0137 55  THR C CB  
4708 C  CB  B THR C 55  ? 0.2411 0.1915 0.2951 -0.0157 0.0046  -0.0405 55  THR C CB  
4709 O  OG1 A THR C 55  ? 0.3427 0.2269 0.4546 0.1482  -0.0537 -0.0909 55  THR C OG1 
4710 O  OG1 B THR C 55  ? 0.3522 0.2802 0.2504 0.0031  0.0328  0.0259  55  THR C OG1 
4711 C  CG2 A THR C 55  ? 0.2567 0.2070 0.1960 0.0560  0.0197  0.0794  55  THR C CG2 
4712 C  CG2 B THR C 55  ? 0.2569 0.1301 0.2791 0.0292  0.0997  -0.0306 55  THR C CG2 
4713 N  N   . SER C 56  ? 0.1637 0.1446 0.2102 0.0390  0.0220  -0.0023 56  SER C N   
4714 C  CA  . SER C 56  ? 0.1513 0.1360 0.1495 0.0203  0.0096  0.0206  56  SER C CA  
4715 C  C   . SER C 56  ? 0.1355 0.1667 0.1901 0.0177  0.0060  -0.0164 56  SER C C   
4716 O  O   . SER C 56  ? 0.1567 0.1624 0.2472 0.0266  0.0273  -0.0244 56  SER C O   
4717 C  CB  . SER C 56  ? 0.1313 0.1447 0.2416 0.0153  0.0099  0.0434  56  SER C CB  
4718 O  OG  . SER C 56  ? 0.1380 0.1457 0.2052 0.0137  0.0119  0.0040  56  SER C OG  
4719 N  N   . LEU C 57  ? 0.1730 0.1544 0.1814 0.0306  -0.0274 -0.0167 57  LEU C N   
4720 C  CA  . LEU C 57  ? 0.2350 0.1606 0.2197 0.0460  -0.0671 -0.0220 57  LEU C CA  
4721 C  C   . LEU C 57  ? 0.1398 0.1699 0.1689 0.0277  -0.0353 -0.0225 57  LEU C C   
4722 O  O   . LEU C 57  ? 0.1378 0.1831 0.2136 0.0364  -0.0222 -0.0041 57  LEU C O   
4723 C  CB  . LEU C 57  ? 0.2237 0.1904 0.2779 0.0259  -0.0357 0.0026  57  LEU C CB  
4724 C  CG  . LEU C 57  ? 0.2447 0.2284 0.3059 0.0157  -0.0776 -0.0252 57  LEU C CG  
4725 C  CD1 . LEU C 57  ? 0.3558 0.2953 0.3671 -0.0120 -0.1004 0.0847  57  LEU C CD1 
4726 C  CD2 . LEU C 57  ? 0.3704 0.2231 0.5971 0.0346  -0.0634 -0.1835 57  LEU C CD2 
4727 N  N   . ARG C 58  ? 0.1635 0.1646 0.2072 0.0351  -0.0161 -0.0272 58  ARG C N   
4728 C  CA  . ARG C 58  ? 0.1825 0.1328 0.1893 0.0597  -0.0038 -0.0049 58  ARG C CA  
4729 C  C   . ARG C 58  ? 0.1100 0.1365 0.1714 0.0335  -0.0445 0.0046  58  ARG C C   
4730 O  O   . ARG C 58  ? 0.1152 0.1490 0.1727 0.0148  -0.0383 -0.0080 58  ARG C O   
4731 C  CB  . ARG C 58  ? 0.2102 0.1775 0.2082 0.0339  -0.0195 0.0159  58  ARG C CB  
4732 C  CG  . ARG C 58  ? 0.3447 0.2619 0.1748 0.0410  -0.0081 0.0432  58  ARG C CG  
4733 C  CD  . ARG C 58  ? 0.2660 0.2860 0.2608 -0.0617 0.0511  0.0515  58  ARG C CD  
4734 N  NE  . ARG C 58  ? 0.2675 0.2576 0.1863 0.0136  0.0259  0.0715  58  ARG C NE  
4735 C  CZ  . ARG C 58  ? 0.1993 0.2888 0.1793 0.0592  0.0262  0.0507  58  ARG C CZ  
4736 N  NH1 . ARG C 58  ? 0.2565 0.3190 0.2361 0.0199  -0.0291 0.1428  58  ARG C NH1 
4737 N  NH2 . ARG C 58  ? 0.2483 0.2572 0.2036 0.0388  0.0124  0.0052  58  ARG C NH2 
4738 N  N   . ILE C 59  ? 0.1308 0.1371 0.1615 0.0089  -0.0170 -0.0063 59  ILE C N   
4739 C  CA  . ILE C 59  ? 0.1003 0.1380 0.1459 -0.0063 -0.0087 0.0096  59  ILE C CA  
4740 C  C   . ILE C 59  ? 0.1247 0.1447 0.1348 0.0219  -0.0219 0.0299  59  ILE C C   
4741 O  O   . ILE C 59  ? 0.1194 0.1754 0.1518 0.0230  -0.0315 0.0024  59  ILE C O   
4742 C  CB  . ILE C 59  ? 0.1265 0.1296 0.1517 0.0215  0.0192  0.0032  59  ILE C CB  
4743 C  CG1 . ILE C 59  ? 0.1150 0.1402 0.1748 0.0430  0.0003  0.0124  59  ILE C CG1 
4744 C  CG2 . ILE C 59  ? 0.1134 0.1644 0.1761 0.0291  -0.0007 -0.0148 59  ILE C CG2 
4745 C  CD1 . ILE C 59  ? 0.1798 0.1306 0.1922 0.0010  -0.0098 0.0251  59  ILE C CD1 
4746 N  N   . LEU C 60  ? 0.1685 0.1910 0.1484 0.0007  0.0054  0.0108  60  LEU C N   
4747 C  CA  . LEU C 60  ? 0.1197 0.1213 0.1389 0.0041  -0.0037 -0.0003 60  LEU C CA  
4748 C  C   . LEU C 60  ? 0.1344 0.1463 0.1723 0.0113  -0.0003 0.0091  60  LEU C C   
4749 O  O   . LEU C 60  ? 0.1272 0.1687 0.1491 0.0245  -0.0068 0.0104  60  LEU C O   
4750 C  CB  . LEU C 60  ? 0.1779 0.1441 0.1676 -0.0097 0.0237  0.0364  60  LEU C CB  
4751 C  CG  . LEU C 60  ? 0.1393 0.1633 0.1684 -0.0070 0.0104  0.0288  60  LEU C CG  
4752 C  CD1 . LEU C 60  ? 0.2269 0.1666 0.1766 0.0242  -0.0383 0.0505  60  LEU C CD1 
4753 C  CD2 . LEU C 60  ? 0.1827 0.1932 0.2269 -0.0456 -0.0230 0.0087  60  LEU C CD2 
4754 N  N   . ASN C 61  ? 0.1331 0.1268 0.1556 0.0041  -0.0159 0.0118  61  ASN C N   
4755 C  CA  . ASN C 61  ? 0.1222 0.1606 0.1486 -0.0144 -0.0175 0.0046  61  ASN C CA  
4756 C  C   . ASN C 61  ? 0.1357 0.2075 0.1744 -0.0080 -0.0121 0.0197  61  ASN C C   
4757 O  O   . ASN C 61  ? 0.1847 0.1644 0.1657 0.0068  -0.0032 0.0516  61  ASN C O   
4758 C  CB  . ASN C 61  ? 0.1523 0.1621 0.1714 -0.0043 -0.0386 -0.0003 61  ASN C CB  
4759 C  CG  . ASN C 61  ? 0.1342 0.1500 0.1193 -0.0115 -0.0221 0.0126  61  ASN C CG  
4760 O  OD1 . ASN C 61  ? 0.1342 0.1736 0.1554 0.0046  -0.0147 0.0388  61  ASN C OD1 
4761 N  ND2 . ASN C 61  ? 0.1567 0.1535 0.1396 0.0015  -0.0425 0.0026  61  ASN C ND2 
4762 N  N   . ASN C 62  ? 0.1411 0.1483 0.2005 -0.0027 -0.0142 0.0635  62  ASN C N   
4763 C  CA  . ASN C 62  ? 0.1818 0.1675 0.1982 0.0021  -0.0070 0.0568  62  ASN C CA  
4764 C  C   . ASN C 62  ? 0.2193 0.1896 0.1650 -0.0258 -0.0417 0.0187  62  ASN C C   
4765 O  O   . ASN C 62  ? 0.1957 0.2630 0.2576 -0.0109 0.0054  0.0908  62  ASN C O   
4766 C  CB  . ASN C 62  ? 0.1772 0.1666 0.2976 -0.0035 -0.0208 0.0395  62  ASN C CB  
4767 C  CG  . ASN C 62  ? 0.1511 0.1836 0.1999 -0.0179 -0.0205 0.0065  62  ASN C CG  
4768 O  OD1 . ASN C 62  ? 0.1842 0.1983 0.1935 0.0068  -0.0089 0.0199  62  ASN C OD1 
4769 N  ND2 . ASN C 62  ? 0.2545 0.2777 0.3021 0.0066  -0.1116 -0.0663 62  ASN C ND2 
4770 N  N   . GLY C 63  ? 0.1737 0.1603 0.1513 0.0111  -0.0249 0.0324  63  GLY C N   
4771 C  CA  . GLY C 63  ? 0.1588 0.1748 0.1587 0.0234  -0.0046 0.0320  63  GLY C CA  
4772 C  C   . GLY C 63  ? 0.1567 0.1595 0.1644 0.0083  -0.0209 0.0120  63  GLY C C   
4773 O  O   . GLY C 63  ? 0.1981 0.1852 0.1658 -0.0057 -0.0119 0.0291  63  GLY C O   
4774 N  N   . HIS C 64  ? 0.1481 0.1571 0.1526 0.0181  -0.0157 0.0214  64  HIS C N   
4775 C  CA  . HIS C 64  ? 0.1279 0.1721 0.1393 0.0035  0.0000  0.0203  64  HIS C CA  
4776 C  C   . HIS C 64  ? 0.1495 0.1527 0.1351 0.0063  0.0021  0.0199  64  HIS C C   
4777 O  O   . HIS C 64  ? 0.1874 0.1818 0.1708 0.0463  0.0041  0.0342  64  HIS C O   
4778 C  CB  . HIS C 64  ? 0.1703 0.1815 0.1368 -0.0214 -0.0063 0.0082  64  HIS C CB  
4779 C  CG  . HIS C 64  ? 0.1571 0.1967 0.1905 -0.0320 -0.0277 0.0317  64  HIS C CG  
4780 N  ND1 . HIS C 64  ? 0.1947 0.2549 0.2053 -0.0447 -0.0392 0.0147  64  HIS C ND1 
4781 C  CD2 . HIS C 64  ? 0.1876 0.2151 0.2170 0.0083  -0.0125 0.0089  64  HIS C CD2 
4782 C  CE1 . HIS C 64  ? 0.2621 0.2425 0.1923 -0.0483 -0.0211 0.0412  64  HIS C CE1 
4783 N  NE2 . HIS C 64  ? 0.2123 0.2522 0.1826 -0.0297 -0.0284 0.0665  64  HIS C NE2 
4784 N  N   . ALA C 65  ? 0.1676 0.1479 0.1430 0.0055  0.0027  0.0129  65  ALA C N   
4785 C  CA  . ALA C 65  ? 0.1386 0.1597 0.1377 0.0060  -0.0326 0.0221  65  ALA C CA  
4786 C  C   . ALA C 65  ? 0.1455 0.1466 0.1525 0.0286  -0.0073 0.0221  65  ALA C C   
4787 O  O   . ALA C 65  ? 0.1475 0.1732 0.1574 0.0020  -0.0255 0.0322  65  ALA C O   
4788 C  CB  . ALA C 65  ? 0.1267 0.2066 0.1536 0.0264  -0.0298 0.0000  65  ALA C CB  
4789 N  N   . PHE C 66  ? 0.1313 0.1358 0.1459 0.0098  -0.0046 0.0131  66  PHE C N   
4790 C  CA  . PHE C 66  ? 0.1261 0.1540 0.1412 0.0146  -0.0491 0.0068  66  PHE C CA  
4791 C  C   . PHE C 66  ? 0.1437 0.1182 0.1489 0.0060  -0.0285 -0.0093 66  PHE C C   
4792 O  O   . PHE C 66  ? 0.1366 0.1675 0.1642 0.0063  -0.0261 0.0104  66  PHE C O   
4793 C  CB  . PHE C 66  ? 0.1349 0.1829 0.1536 -0.0073 -0.0200 0.0144  66  PHE C CB  
4794 C  CG  . PHE C 66  ? 0.1033 0.1341 0.1492 -0.0189 -0.0111 -0.0028 66  PHE C CG  
4795 C  CD1 . PHE C 66  ? 0.1012 0.1647 0.1585 -0.0160 -0.0060 0.0077  66  PHE C CD1 
4796 C  CD2 . PHE C 66  ? 0.1161 0.1569 0.1738 0.0024  -0.0049 0.0000  66  PHE C CD2 
4797 C  CE1 . PHE C 66  ? 0.1425 0.1489 0.1755 -0.0001 0.0087  0.0148  66  PHE C CE1 
4798 C  CE2 . PHE C 66  ? 0.1324 0.1502 0.1594 0.0046  -0.0222 0.0063  66  PHE C CE2 
4799 C  CZ  . PHE C 66  ? 0.1262 0.1400 0.1597 -0.0057 0.0076  0.0124  66  PHE C CZ  
4800 N  N   . ASN C 67  ? 0.1303 0.1412 0.1414 0.0265  -0.0110 -0.0038 67  ASN C N   
4801 C  CA  . ASN C 67  ? 0.1393 0.1592 0.1639 0.0040  -0.0171 -0.0219 67  ASN C CA  
4802 C  C   . ASN C 67  ? 0.1203 0.1297 0.1256 0.0350  -0.0302 -0.0006 67  ASN C C   
4803 O  O   . ASN C 67  ? 0.1134 0.1902 0.1856 0.0242  -0.0364 0.0219  67  ASN C O   
4804 C  CB  . ASN C 67  ? 0.2312 0.2357 0.1932 -0.0663 0.0096  -0.0421 67  ASN C CB  
4805 C  CG  . ASN C 67  ? 0.3389 0.3765 0.2655 0.0419  0.0035  0.0355  67  ASN C CG  
4806 O  OD1 . ASN C 67  ? 0.7961 0.1966 0.2944 0.1843  0.0887  0.1744  67  ASN C OD1 
4807 N  ND2 . ASN C 67  ? 0.3129 0.3093 0.2527 0.0627  0.0998  0.0303  67  ASN C ND2 
4808 N  N   . VAL C 68  ? 0.1254 0.1254 0.1364 0.0127  -0.0062 -0.0055 68  VAL C N   
4809 C  CA  . VAL C 68  ? 0.1137 0.1437 0.1610 0.0017  0.0113  -0.0221 68  VAL C CA  
4810 C  C   . VAL C 68  ? 0.1443 0.1332 0.1601 0.0217  -0.0197 -0.0346 68  VAL C C   
4811 O  O   . VAL C 68  ? 0.1303 0.1387 0.1685 0.0200  -0.0245 -0.0324 68  VAL C O   
4812 C  CB  . VAL C 68  ? 0.1278 0.1668 0.1680 0.0065  0.0120  -0.0164 68  VAL C CB  
4813 C  CG1 . VAL C 68  ? 0.1285 0.2129 0.1941 0.0259  -0.0048 -0.0657 68  VAL C CG1 
4814 C  CG2 . VAL C 68  ? 0.1822 0.1799 0.1721 -0.0493 -0.0040 -0.0228 68  VAL C CG2 
4815 N  N   . GLU C 69  ? 0.1337 0.1335 0.2035 0.0179  -0.0269 -0.0219 69  GLU C N   
4816 C  CA  . GLU C 69  ? 0.1280 0.1416 0.1958 0.0182  -0.0153 0.0089  69  GLU C CA  
4817 C  C   . GLU C 69  ? 0.1511 0.1305 0.1957 0.0302  0.0149  -0.0076 69  GLU C C   
4818 O  O   . GLU C 69  ? 0.1466 0.1509 0.2187 0.0207  -0.0017 -0.0298 69  GLU C O   
4819 C  CB  . GLU C 69  ? 0.1998 0.1626 0.1743 0.0258  -0.0263 -0.0133 69  GLU C CB  
4820 C  CG  . GLU C 69  ? 0.2806 0.2547 0.1615 0.0230  0.0241  0.0288  69  GLU C CG  
4821 C  CD  . GLU C 69  ? 0.3122 0.3287 0.2280 0.1371  0.0174  0.0395  69  GLU C CD  
4822 O  OE1 . GLU C 69  ? 0.2824 0.3571 0.2384 0.0798  0.0051  0.0392  69  GLU C OE1 
4823 O  OE2 . GLU C 69  ? 0.4557 0.2955 0.1969 0.1457  0.0274  0.0226  69  GLU C OE2 
4824 N  N   . PHE C 70  ? 0.1365 0.1456 0.1454 0.0294  -0.0194 0.0006  70  PHE C N   
4825 C  CA  . PHE C 70  ? 0.1567 0.1342 0.1484 0.0109  0.0003  0.0076  70  PHE C CA  
4826 C  C   . PHE C 70  ? 0.1558 0.1504 0.1640 0.0034  0.0174  -0.0233 70  PHE C C   
4827 O  O   . PHE C 70  ? 0.1816 0.1545 0.1764 0.0249  0.0092  0.0103  70  PHE C O   
4828 C  CB  . PHE C 70  ? 0.1586 0.1254 0.1685 0.0152  -0.0110 0.0041  70  PHE C CB  
4829 C  CG  . PHE C 70  ? 0.1439 0.1188 0.1378 0.0230  0.0113  0.0000  70  PHE C CG  
4830 C  CD1 . PHE C 70  ? 0.1396 0.1308 0.1556 0.0276  0.0120  -0.0115 70  PHE C CD1 
4831 C  CD2 . PHE C 70  ? 0.1100 0.1615 0.1477 0.0159  0.0092  0.0173  70  PHE C CD2 
4832 C  CE1 . PHE C 70  ? 0.1827 0.1490 0.1472 0.0251  -0.0037 0.0113  70  PHE C CE1 
4833 C  CE2 . PHE C 70  ? 0.1705 0.1364 0.1694 0.0154  -0.0065 -0.0138 70  PHE C CE2 
4834 C  CZ  . PHE C 70  ? 0.1599 0.1389 0.1491 0.0034  -0.0060 0.0142  70  PHE C CZ  
4835 N  N   . ASP C 71  ? 0.1798 0.1298 0.2278 0.0507  0.0262  -0.0107 71  ASP C N   
4836 C  CA  . ASP C 71  ? 0.1863 0.1462 0.2301 0.0181  0.0208  -0.0114 71  ASP C CA  
4837 C  C   . ASP C 71  ? 0.2339 0.1383 0.2355 0.0344  0.0098  -0.0357 71  ASP C C   
4838 O  O   . ASP C 71  ? 0.3571 0.2107 0.2412 0.0207  0.0170  0.0225  71  ASP C O   
4839 C  CB  . ASP C 71  ? 0.2412 0.1875 0.3623 0.0494  0.0439  -0.0412 71  ASP C CB  
4840 C  CG  . ASP C 71  ? 0.3203 0.1874 0.5343 0.0621  0.0873  0.0357  71  ASP C CG  
4841 O  OD1 . ASP C 71  ? 0.2908 0.1673 0.3858 0.0571  0.0425  -0.0351 71  ASP C OD1 
4842 O  OD2 . ASP C 71  ? 0.4726 0.2296 0.6480 0.0586  0.2881  -0.0672 71  ASP C OD2 
4843 N  N   . ASP C 72  ? 0.2114 0.1271 0.2071 0.0342  0.0171  0.0088  72  ASP C N   
4844 C  CA  . ASP C 72  ? 0.2231 0.1446 0.1757 0.0003  0.0024  0.0443  72  ASP C CA  
4845 C  C   . ASP C 72  ? 0.2196 0.1650 0.2281 0.0098  0.0017  0.0142  72  ASP C C   
4846 O  O   . ASP C 72  ? 0.2736 0.1728 0.2633 0.0010  -0.0388 0.0175  72  ASP C O   
4847 C  CB  . ASP C 72  ? 0.2409 0.1718 0.1928 0.0103  -0.0113 0.0439  72  ASP C CB  
4848 C  CG  . ASP C 72  ? 0.2084 0.2230 0.1474 0.0241  -0.0152 -0.0023 72  ASP C CG  
4849 O  OD1 . ASP C 72  ? 0.2098 0.2587 0.2208 0.0621  -0.0015 0.0198  72  ASP C OD1 
4850 O  OD2 . ASP C 72  ? 0.1894 0.1915 0.2213 0.0317  -0.0241 0.0032  72  ASP C OD2 
4851 N  N   . SER C 73  ? 0.2721 0.1391 0.1967 0.0076  0.0041  0.0357  73  SER C N   
4852 C  CA  . SER C 73  ? 0.3641 0.1262 0.2379 0.0445  -0.0214 -0.0182 73  SER C CA  
4853 C  C   . SER C 73  ? 0.3402 0.1820 0.2132 -0.0286 0.0364  -0.0293 73  SER C C   
4854 O  O   . SER C 73  ? 0.2608 0.1762 0.2407 0.0054  0.0251  0.0142  73  SER C O   
4855 C  CB  . SER C 73  ? 0.3693 0.1941 0.3104 0.0551  -0.0302 0.0251  73  SER C CB  
4856 O  OG  . SER C 73  ? 0.3271 0.1346 0.3285 0.0285  -0.0738 -0.0357 73  SER C OG  
4857 N  N   . GLN C 74  ? 0.3436 0.1915 0.2606 -0.0328 -0.0206 -0.0159 74  GLN C N   
4858 C  CA  . GLN C 74  ? 0.3702 0.1793 0.2685 0.0342  -0.0166 -0.0154 74  GLN C CA  
4859 C  C   . GLN C 74  ? 0.2587 0.2587 0.2088 -0.0094 -0.0219 -0.0430 74  GLN C C   
4860 O  O   . GLN C 74  ? 0.2511 0.1903 0.2105 -0.0114 0.0339  0.0148  74  GLN C O   
4861 C  CB  . GLN C 74  ? 0.4291 0.2628 0.2166 0.0961  -0.0142 -0.0065 74  GLN C CB  
4862 C  CG  . GLN C 74  ? 0.3668 0.2415 0.3783 0.0564  0.0716  0.0979  74  GLN C CG  
4863 C  CD  . GLN C 74  ? 0.4187 0.4544 0.4131 0.1172  0.0798  0.0834  74  GLN C CD  
4864 O  OE1 . GLN C 74  ? 0.8428 0.6711 0.4301 0.2055  -0.0706 0.1527  74  GLN C OE1 
4865 N  NE2 . GLN C 74  ? 0.4754 0.3860 0.5748 -0.0725 0.0838  -0.1422 74  GLN C NE2 
4866 N  N   . ASP C 75  ? 0.2493 0.3007 0.2276 -0.0306 -0.0676 0.0086  75  ASP C N   
4867 C  CA  . ASP C 75  ? 0.2509 0.2655 0.2797 -0.0261 -0.0092 0.0467  75  ASP C CA  
4868 C  C   . ASP C 75  ? 0.3346 0.2874 0.2215 -0.0733 0.0447  -0.0113 75  ASP C C   
4869 O  O   . ASP C 75  ? 0.3777 0.3623 0.2292 0.0167  0.0041  0.0242  75  ASP C O   
4870 C  CB  . ASP C 75  ? 0.5325 0.3479 0.3172 -0.1119 -0.1028 0.0689  75  ASP C CB  
4871 C  CG  . ASP C 75  ? 0.4968 0.3192 0.5174 0.1462  -0.1045 -0.0461 75  ASP C CG  
4872 O  OD1 . ASP C 75  ? 0.4593 0.2763 0.5327 0.1154  0.0675  -0.0203 75  ASP C OD1 
4873 O  OD2 . ASP C 75  ? 0.5690 0.5070 0.4435 0.0625  -0.1106 -0.0034 75  ASP C OD2 
4874 N  N   . LYS C 76  ? 0.2345 0.2644 0.3129 0.0729  0.0244  0.0461  76  LYS C N   
4875 C  CA  . LYS C 76  ? 0.3684 0.2395 0.3312 -0.0078 -0.0197 0.0155  76  LYS C CA  
4876 C  C   . LYS C 76  ? 0.5360 0.3125 0.4663 0.0909  -0.0278 0.0091  76  LYS C C   
4877 O  O   . LYS C 76  ? 0.5214 0.6529 0.4661 0.0628  0.0295  0.0017  76  LYS C O   
4878 C  CB  . LYS C 76  ? 0.2951 0.2303 0.5264 0.0263  0.0656  -0.0447 76  LYS C CB  
4879 C  CG  . LYS C 76  ? 0.4667 0.3452 0.6219 0.1474  0.0582  -0.0104 76  LYS C CG  
4880 C  CD  . LYS C 76  ? 0.4990 0.1906 0.5996 0.0698  0.0035  0.0821  76  LYS C CD  
4881 C  CE  . LYS C 76  ? 0.5036 0.4113 0.5485 0.0728  -0.1040 0.0599  76  LYS C CE  
4882 N  NZ  . LYS C 76  ? 0.4889 0.4101 0.3838 0.1886  -0.0070 -0.0357 76  LYS C NZ  
4883 N  N   . ALA C 77  ? 0.2667 0.2980 0.3400 0.0386  0.1133  -0.0172 77  ALA C N   
4884 C  CA  . ALA C 77  ? 0.2007 0.3208 0.2409 0.0019  0.0263  0.0307  77  ALA C CA  
4885 C  C   . ALA C 77  ? 0.1958 0.2090 0.1693 -0.0220 0.0255  -0.0043 77  ALA C C   
4886 O  O   . ALA C 77  ? 0.2597 0.3716 0.2012 -0.0636 0.0857  -0.0384 77  ALA C O   
4887 C  CB  . ALA C 77  ? 0.2009 0.2439 0.3280 -0.0196 0.0175  0.0182  77  ALA C CB  
4888 N  N   . VAL C 78  ? 0.1572 0.1757 0.1923 0.0263  0.0551  -0.0054 78  VAL C N   
4889 C  CA  . VAL C 78  ? 0.1563 0.2104 0.2350 0.0384  0.0458  0.0141  78  VAL C CA  
4890 C  C   . VAL C 78  ? 0.1664 0.1836 0.1691 -0.0049 0.0217  0.0527  78  VAL C C   
4891 O  O   . VAL C 78  ? 0.2421 0.1820 0.1847 -0.0105 0.0430  0.0337  78  VAL C O   
4892 C  CB  . VAL C 78  ? 0.3230 0.2513 0.3422 0.0401  -0.0208 -0.0236 78  VAL C CB  
4893 C  CG1 . VAL C 78  ? 0.3197 0.2012 0.3052 0.0260  0.0659  0.0286  78  VAL C CG1 
4894 C  CG2 . VAL C 78  ? 0.3300 0.2336 0.3046 0.0412  -0.0210 0.0085  78  VAL C CG2 
4895 N  N   . LEU C 79  ? 0.1599 0.1486 0.1560 0.0161  -0.0102 -0.0080 79  LEU C N   
4896 C  CA  . LEU C 79  ? 0.1719 0.1626 0.1337 0.0140  0.0049  0.0168  79  LEU C CA  
4897 C  C   . LEU C 79  ? 0.2072 0.1439 0.1468 -0.0080 -0.0230 0.0206  79  LEU C C   
4898 O  O   . LEU C 79  ? 0.2054 0.1709 0.1683 -0.0203 -0.0133 0.0243  79  LEU C O   
4899 C  CB  . LEU C 79  ? 0.1877 0.1771 0.1466 0.0195  0.0370  0.0115  79  LEU C CB  
4900 C  CG  . LEU C 79  ? 0.2287 0.1456 0.1556 0.0293  0.0144  -0.0186 79  LEU C CG  
4901 C  CD1 . LEU C 79  ? 0.2870 0.1421 0.2026 0.0375  0.0168  0.0066  79  LEU C CD1 
4902 C  CD2 . LEU C 79  ? 0.1937 0.1756 0.1486 0.0192  0.0285  -0.0212 79  LEU C CD2 
4903 N  N   . LYS C 80  ? 0.1867 0.1904 0.1436 0.0041  -0.0184 0.0138  80  LYS C N   
4904 C  CA  . LYS C 80  ? 0.2068 0.1583 0.1502 0.0230  -0.0057 -0.0055 80  LYS C CA  
4905 C  C   . LYS C 80  ? 0.2109 0.1881 0.1235 -0.0089 -0.0077 0.0108  80  LYS C C   
4906 O  O   . LYS C 80  ? 0.2152 0.1897 0.1599 -0.0032 -0.0220 0.0212  80  LYS C O   
4907 C  CB  . LYS C 80  ? 0.2705 0.1622 0.2217 0.0222  -0.0076 -0.0403 80  LYS C CB  
4908 C  CG  . LYS C 80  ? 0.2962 0.2203 0.2289 0.0511  -0.0222 -0.0230 80  LYS C CG  
4909 C  CD  . LYS C 80  ? 0.3986 0.2685 0.2037 0.1289  0.0450  -0.0204 80  LYS C CD  
4910 N  N   . GLY C 81  ? 0.2213 0.1987 0.1622 0.0108  -0.0491 -0.0062 81  GLY C N   
4911 C  CA  . GLY C 81  ? 0.2407 0.1994 0.1587 0.0346  -0.0364 -0.0041 81  GLY C CA  
4912 C  C   . GLY C 81  ? 0.2903 0.2159 0.2300 0.0804  -0.0381 -0.0113 81  GLY C C   
4913 O  O   . GLY C 81  ? 0.2940 0.1847 0.2262 -0.0010 -0.0474 -0.0156 81  GLY C O   
4914 N  N   . GLY C 82  ? 0.4192 0.1662 0.2527 0.0851  -0.0012 0.0063  82  GLY C N   
4915 C  CA  . GLY C 82  ? 0.3447 0.1692 0.2561 0.0641  -0.0218 0.0102  82  GLY C CA  
4916 C  C   . GLY C 82  ? 0.3201 0.2026 0.2637 0.0250  -0.0681 -0.0348 82  GLY C C   
4917 O  O   . GLY C 82  ? 0.3242 0.2894 0.2481 0.0586  -0.1177 -0.0759 82  GLY C O   
4918 N  N   . PRO C 83  ? 0.2994 0.2048 0.2129 0.0551  -0.0408 -0.0238 83  PRO C N   
4919 C  CA  . PRO C 83  ? 0.2955 0.2095 0.2148 0.0447  -0.0843 -0.0114 83  PRO C CA  
4920 C  C   . PRO C 83  ? 0.2032 0.2179 0.2359 0.0062  -0.0331 -0.0379 83  PRO C C   
4921 O  O   . PRO C 83  ? 0.2448 0.2842 0.2691 0.0252  -0.0142 -0.0282 83  PRO C O   
4922 C  CB  . PRO C 83  ? 0.2700 0.2508 0.2445 0.0474  -0.0535 -0.0649 83  PRO C CB  
4923 C  CG  . PRO C 83  ? 0.2196 0.2138 0.2337 0.0680  -0.0289 -0.0631 83  PRO C CG  
4924 C  CD  . PRO C 83  ? 0.2574 0.2091 0.2470 0.0286  -0.0522 0.0027  83  PRO C CD  
4925 N  N   . LEU C 84  ? 0.1967 0.1845 0.1709 0.0270  -0.0445 -0.0342 84  LEU C N   
4926 C  CA  . LEU C 84  ? 0.2333 0.1401 0.2179 0.0181  -0.0230 -0.0469 84  LEU C CA  
4927 C  C   . LEU C 84  ? 0.2215 0.1962 0.2080 -0.0100 0.0013  -0.0636 84  LEU C C   
4928 O  O   . LEU C 84  ? 0.3154 0.2159 0.2084 -0.0006 -0.0741 -0.0816 84  LEU C O   
4929 C  CB  . LEU C 84  ? 0.2107 0.1375 0.1414 -0.0070 -0.0125 -0.0236 84  LEU C CB  
4930 C  CG  . LEU C 84  ? 0.2134 0.1317 0.1369 0.0206  -0.0373 -0.0273 84  LEU C CG  
4931 C  CD1 . LEU C 84  ? 0.1987 0.1849 0.1392 0.0126  0.0017  -0.0174 84  LEU C CD1 
4932 C  CD2 . LEU C 84  ? 0.1736 0.1308 0.1364 0.0085  -0.0099 -0.0093 84  LEU C CD2 
4933 N  N   . ASP C 85  ? 0.2626 0.1770 0.2190 -0.0104 -0.0377 -0.0335 85  ASP C N   
4934 C  CA  . ASP C 85  ? 0.3077 0.1553 0.2754 0.0241  0.0027  -0.0188 85  ASP C CA  
4935 C  C   . ASP C 85  ? 0.3080 0.1800 0.2150 0.0388  -0.0238 -0.0160 85  ASP C C   
4936 O  O   . ASP C 85  ? 0.3386 0.2594 0.2632 -0.0142 -0.0432 -0.0584 85  ASP C O   
4937 C  CB  . ASP C 85  ? 0.2879 0.1761 0.3249 -0.0060 -0.0436 -0.0768 85  ASP C CB  
4938 C  CG  . ASP C 85  ? 0.3492 0.3677 0.3806 0.0882  -0.0113 -0.0703 85  ASP C CG  
4939 O  OD1 . ASP C 85  ? 0.5199 0.5178 0.3537 0.1826  0.0364  0.0428  85  ASP C OD1 
4940 O  OD2 . ASP C 85  ? 0.3355 0.4222 0.3987 0.0060  -0.0346 -0.0309 85  ASP C OD2 
4941 N  N   . GLY C 86  ? 0.3167 0.2897 0.2382 0.0693  0.0386  -0.0020 86  GLY C N   
4942 C  CA  . GLY C 86  ? 0.2416 0.2856 0.2585 0.0183  0.0085  -0.0209 86  GLY C CA  
4943 C  C   . GLY C 86  ? 0.2579 0.2418 0.2132 0.0082  -0.0155 0.0185  86  GLY C C   
4944 O  O   . GLY C 86  ? 0.2933 0.2752 0.3337 0.0520  0.0010  0.0715  86  GLY C O   
4945 N  N   A THR C 87  ? 0.2215 0.2199 0.1685 0.0173  -0.0160 -0.0627 87  THR C N   
4946 N  N   B THR C 87  ? 0.2090 0.2186 0.1692 0.0007  -0.0175 -0.0553 87  THR C N   
4947 C  CA  A THR C 87  ? 0.2269 0.1908 0.1498 0.0261  -0.0111 -0.0310 87  THR C CA  
4948 C  CA  B THR C 87  ? 0.2215 0.1608 0.1447 0.0015  -0.0249 -0.0368 87  THR C CA  
4949 C  C   A THR C 87  ? 0.2152 0.1411 0.1497 -0.0368 -0.0093 -0.0098 87  THR C C   
4950 C  C   B THR C 87  ? 0.1377 0.1286 0.1103 0.0038  0.0344  -0.0216 87  THR C C   
4951 O  O   A THR C 87  ? 0.1757 0.1339 0.1425 0.0217  -0.0198 -0.0107 87  THR C O   
4952 O  O   B THR C 87  ? 0.1057 0.1145 0.1191 0.0136  0.0027  -0.0071 87  THR C O   
4953 C  CB  A THR C 87  ? 0.2635 0.1750 0.1554 0.0222  0.0274  -0.0271 87  THR C CB  
4954 C  CB  B THR C 87  ? 0.2337 0.1649 0.1529 0.0013  -0.0048 -0.0165 87  THR C CB  
4955 O  OG1 A THR C 87  ? 0.3524 0.2522 0.2406 0.0215  -0.0381 -0.1168 87  THR C OG1 
4956 O  OG1 B THR C 87  ? 0.1827 0.1626 0.1617 0.0383  -0.0038 -0.0119 87  THR C OG1 
4957 C  CG2 A THR C 87  ? 0.3059 0.1928 0.2442 -0.0335 0.0183  -0.0395 87  THR C CG2 
4958 C  CG2 B THR C 87  ? 0.2569 0.1682 0.1447 0.0274  -0.0008 -0.0154 87  THR C CG2 
4959 N  N   . TYR C 88  ? 0.2021 0.1269 0.1263 -0.0131 -0.0082 -0.0077 88  TYR C N   
4960 C  CA  . TYR C 88  ? 0.1518 0.1285 0.1182 0.0111  -0.0055 -0.0184 88  TYR C CA  
4961 C  C   . TYR C 88  ? 0.1398 0.1181 0.1199 0.0230  0.0225  0.0190  88  TYR C C   
4962 O  O   . TYR C 88  ? 0.1932 0.1854 0.1635 0.0342  0.0170  0.0518  88  TYR C O   
4963 C  CB  . TYR C 88  ? 0.1568 0.1097 0.1551 -0.0034 0.0017  -0.0297 88  TYR C CB  
4964 C  CG  . TYR C 88  ? 0.1535 0.1199 0.1238 -0.0059 0.0040  -0.0081 88  TYR C CG  
4965 C  CD1 . TYR C 88  ? 0.1644 0.1163 0.1322 0.0137  -0.0051 -0.0135 88  TYR C CD1 
4966 C  CD2 . TYR C 88  ? 0.1407 0.0854 0.1401 0.0126  0.0068  -0.0121 88  TYR C CD2 
4967 C  CE1 . TYR C 88  ? 0.1490 0.1438 0.1150 0.0012  -0.0147 -0.0118 88  TYR C CE1 
4968 C  CE2 . TYR C 88  ? 0.1263 0.1082 0.1172 0.0093  -0.0068 -0.0083 88  TYR C CE2 
4969 C  CZ  . TYR C 88  ? 0.1259 0.0976 0.1216 -0.0001 -0.0109 -0.0082 88  TYR C CZ  
4970 O  OH  . TYR C 88  ? 0.1383 0.1150 0.1583 -0.0166 -0.0130 -0.0057 88  TYR C OH  
4971 N  N   . ARG C 89  ? 0.1389 0.1075 0.1121 0.0114  -0.0142 -0.0185 89  ARG C N   
4972 C  CA  . ARG C 89  ? 0.1437 0.0912 0.1261 0.0122  -0.0059 -0.0103 89  ARG C CA  
4973 C  C   . ARG C 89  ? 0.1071 0.1105 0.1220 0.0126  -0.0159 0.0066  89  ARG C C   
4974 O  O   . ARG C 89  ? 0.1407 0.1030 0.1152 0.0175  0.0023  -0.0051 89  ARG C O   
4975 C  CB  . ARG C 89  ? 0.1590 0.1314 0.2120 0.0353  -0.0114 -0.0040 89  ARG C CB  
4976 C  CG  . ARG C 89  ? 0.1513 0.1635 0.2337 0.0443  -0.0113 0.0205  89  ARG C CG  
4977 C  CD  . ARG C 89  ? 0.2100 0.1477 0.2407 0.0269  -0.0062 -0.0174 89  ARG C CD  
4978 N  NE  . ARG C 89  ? 0.2118 0.1511 0.2766 0.0511  -0.0172 -0.0280 89  ARG C NE  
4979 C  CZ  . ARG C 89  ? 0.2345 0.1580 0.2468 0.0324  -0.0551 -0.0077 89  ARG C CZ  
4980 N  NH1 . ARG C 89  ? 0.2827 0.1858 0.1883 0.0551  0.0096  -0.0293 89  ARG C NH1 
4981 N  NH2 . ARG C 89  ? 0.2569 0.1894 0.2066 0.0006  0.0051  -0.0102 89  ARG C NH2 
4982 N  N   . LEU C 90  ? 0.1240 0.0957 0.1263 0.0114  -0.0046 0.0066  90  LEU C N   
4983 C  CA  . LEU C 90  ? 0.1308 0.1064 0.1173 0.0027  -0.0098 0.0142  90  LEU C CA  
4984 C  C   . LEU C 90  ? 0.1271 0.0954 0.1283 0.0305  -0.0074 0.0085  90  LEU C C   
4985 O  O   . LEU C 90  ? 0.1457 0.1463 0.1488 0.0423  0.0104  0.0148  90  LEU C O   
4986 C  CB  . LEU C 90  ? 0.1252 0.1240 0.1244 0.0267  0.0148  0.0241  90  LEU C CB  
4987 C  CG  . LEU C 90  ? 0.1181 0.1409 0.1398 0.0183  -0.0118 0.0179  90  LEU C CG  
4988 C  CD1 . LEU C 90  ? 0.1504 0.1355 0.2002 0.0160  -0.0093 0.0234  90  LEU C CD1 
4989 C  CD2 . LEU C 90  ? 0.1780 0.1791 0.1629 0.0010  0.0311  0.0100  90  LEU C CD2 
4990 N  N   . ILE C 91  ? 0.1380 0.0976 0.1100 0.0012  -0.0081 0.0110  91  ILE C N   
4991 C  CA  . ILE C 91  ? 0.1292 0.1283 0.1226 -0.0013 -0.0081 -0.0024 91  ILE C CA  
4992 C  C   . ILE C 91  ? 0.1204 0.1023 0.1215 0.0155  -0.0132 0.0046  91  ILE C C   
4993 O  O   . ILE C 91  ? 0.0930 0.1116 0.1419 0.0015  -0.0091 0.0013  91  ILE C O   
4994 C  CB  . ILE C 91  ? 0.1199 0.1292 0.1303 0.0143  -0.0049 0.0178  91  ILE C CB  
4995 C  CG1 . ILE C 91  ? 0.1570 0.1416 0.1674 0.0060  -0.0425 0.0357  91  ILE C CG1 
4996 C  CG2 . ILE C 91  ? 0.1328 0.1423 0.1461 0.0138  0.0087  -0.0124 91  ILE C CG2 
4997 C  CD1 . ILE C 91  ? 0.2581 0.1987 0.1899 -0.0221 0.0220  0.0241  91  ILE C CD1 
4998 N  N   . GLN C 92  ? 0.1138 0.0965 0.1491 0.0142  -0.0066 0.0092  92  GLN C N   
4999 C  CA  . GLN C 92  ? 0.1211 0.1105 0.1283 0.0270  -0.0164 0.0031  92  GLN C CA  
5000 C  C   . GLN C 92  ? 0.1059 0.1073 0.1444 0.0124  -0.0176 0.0111  92  GLN C C   
5001 O  O   . GLN C 92  ? 0.0983 0.1019 0.1340 0.0094  -0.0060 -0.0059 92  GLN C O   
5002 C  CB  . GLN C 92  ? 0.1515 0.1515 0.1276 0.0152  -0.0034 0.0000  92  GLN C CB  
5003 C  CG  . GLN C 92  ? 0.1685 0.1368 0.1550 0.0299  0.0063  -0.0076 92  GLN C CG  
5004 C  CD  . GLN C 92  ? 0.1708 0.1511 0.1834 0.0177  0.0265  0.0076  92  GLN C CD  
5005 O  OE1 . GLN C 92  ? 0.1544 0.1373 0.2163 0.0375  0.0074  0.0073  92  GLN C OE1 
5006 N  NE2 . GLN C 92  ? 0.2845 0.2581 0.1852 -0.0544 0.0057  -0.0210 92  GLN C NE2 
5007 N  N   . PHE C 93  ? 0.1168 0.0881 0.1308 0.0179  -0.0035 -0.0020 93  PHE C N   
5008 C  CA  . PHE C 93  ? 0.1071 0.0906 0.1093 0.0142  -0.0188 -0.0013 93  PHE C CA  
5009 C  C   . PHE C 93  ? 0.1133 0.1027 0.0883 0.0054  -0.0074 0.0137  93  PHE C C   
5010 O  O   . PHE C 93  ? 0.0991 0.1037 0.1429 0.0043  -0.0141 -0.0081 93  PHE C O   
5011 C  CB  . PHE C 93  ? 0.0827 0.0940 0.1197 0.0057  0.0100  0.0070  93  PHE C CB  
5012 C  CG  . PHE C 93  ? 0.0962 0.1128 0.1184 -0.0055 0.0043  -0.0071 93  PHE C CG  
5013 C  CD1 . PHE C 93  ? 0.1071 0.1088 0.1852 -0.0250 -0.0055 -0.0001 93  PHE C CD1 
5014 C  CD2 . PHE C 93  ? 0.1089 0.1366 0.1441 0.0302  0.0055  -0.0038 93  PHE C CD2 
5015 C  CE1 . PHE C 93  ? 0.1155 0.1369 0.1303 -0.0071 0.0265  -0.0178 93  PHE C CE1 
5016 C  CE2 . PHE C 93  ? 0.1323 0.1265 0.1587 0.0142  -0.0031 -0.0091 93  PHE C CE2 
5017 C  CZ  . PHE C 93  ? 0.0931 0.1242 0.1511 -0.0023 0.0205  -0.0082 93  PHE C CZ  
5018 N  N   . HIS C 94  ? 0.1118 0.0886 0.1138 -0.0037 0.0027  0.0013  94  HIS C N   
5019 C  CA  . HIS C 94  ? 0.0974 0.0878 0.0971 0.0216  0.0054  -0.0044 94  HIS C CA  
5020 C  C   . HIS C 94  ? 0.0913 0.0843 0.0926 -0.0054 -0.0060 0.0049  94  HIS C C   
5021 O  O   . HIS C 94  ? 0.1024 0.0901 0.1111 0.0098  -0.0229 0.0020  94  HIS C O   
5022 C  CB  . HIS C 94  ? 0.0838 0.1064 0.1186 0.0162  0.0019  0.0153  94  HIS C CB  
5023 C  CG  . HIS C 94  ? 0.0922 0.0790 0.0868 -0.0052 -0.0051 0.0222  94  HIS C CG  
5024 N  ND1 . HIS C 94  ? 0.1039 0.0918 0.0877 -0.0052 -0.0093 0.0074  94  HIS C ND1 
5025 C  CD2 . HIS C 94  ? 0.0710 0.1111 0.0847 -0.0017 0.0007  -0.0059 94  HIS C CD2 
5026 C  CE1 . HIS C 94  ? 0.1116 0.0958 0.1048 0.0100  0.0148  0.0065  94  HIS C CE1 
5027 N  NE2 . HIS C 94  ? 0.0987 0.0843 0.0951 -0.0013 -0.0208 0.0163  94  HIS C NE2 
5028 N  N   . PHE C 95  ? 0.1075 0.0881 0.1001 0.0060  0.0038  -0.0060 95  PHE C N   
5029 C  CA  . PHE C 95  ? 0.0856 0.0906 0.1102 0.0096  0.0140  0.0041  95  PHE C CA  
5030 C  C   . PHE C 95  ? 0.1008 0.0929 0.0820 0.0041  -0.0076 -0.0013 95  PHE C C   
5031 O  O   . PHE C 95  ? 0.1256 0.0913 0.1059 0.0167  -0.0063 0.0098  95  PHE C O   
5032 C  CB  . PHE C 95  ? 0.1254 0.0985 0.1093 -0.0077 0.0076  0.0135  95  PHE C CB  
5033 C  CG  . PHE C 95  ? 0.1058 0.0974 0.1164 -0.0060 0.0130  0.0168  95  PHE C CG  
5034 C  CD1 . PHE C 95  ? 0.1080 0.0897 0.1170 -0.0120 -0.0153 -0.0027 95  PHE C CD1 
5035 C  CD2 . PHE C 95  ? 0.1194 0.1098 0.1070 -0.0178 0.0121  0.0077  95  PHE C CD2 
5036 C  CE1 . PHE C 95  ? 0.1052 0.1272 0.1307 -0.0192 -0.0001 0.0155  95  PHE C CE1 
5037 C  CE2 . PHE C 95  ? 0.1182 0.1202 0.1301 -0.0093 0.0103  -0.0070 95  PHE C CE2 
5038 C  CZ  . PHE C 95  ? 0.1436 0.1184 0.1230 0.0052  -0.0034 -0.0031 95  PHE C CZ  
5039 N  N   . HIS C 96  ? 0.0903 0.0979 0.1048 0.0082  0.0006  0.0000  96  HIS C N   
5040 C  CA  . HIS C 96  ? 0.0759 0.0890 0.0873 0.0083  -0.0109 -0.0031 96  HIS C CA  
5041 C  C   . HIS C 96  ? 0.0881 0.1054 0.0891 -0.0035 -0.0049 0.0000  96  HIS C C   
5042 O  O   . HIS C 96  ? 0.1023 0.1015 0.0897 -0.0037 -0.0027 -0.0020 96  HIS C O   
5043 C  CB  . HIS C 96  ? 0.0960 0.0883 0.1221 0.0005  -0.0001 0.0015  96  HIS C CB  
5044 C  CG  . HIS C 96  ? 0.0988 0.0929 0.0983 0.0078  0.0020  0.0015  96  HIS C CG  
5045 N  ND1 . HIS C 96  ? 0.1035 0.1052 0.1032 -0.0066 0.0012  0.0082  96  HIS C ND1 
5046 C  CD2 . HIS C 96  ? 0.1037 0.0769 0.1098 -0.0028 0.0148  -0.0012 96  HIS C CD2 
5047 C  CE1 . HIS C 96  ? 0.1045 0.1000 0.1084 0.0230  0.0000  -0.0115 96  HIS C CE1 
5048 N  NE2 . HIS C 96  ? 0.1080 0.0710 0.0960 0.0006  0.0063  -0.0017 96  HIS C NE2 
5049 N  N   . TRP C 97  ? 0.0874 0.0701 0.0994 0.0021  -0.0068 -0.0003 97  TRP C N   
5050 C  CA  . TRP C 97  ? 0.1067 0.0690 0.0957 0.0003  0.0076  -0.0040 97  TRP C CA  
5051 C  C   . TRP C 97  ? 0.0798 0.0967 0.0838 -0.0127 -0.0008 -0.0041 97  TRP C C   
5052 O  O   . TRP C 97  ? 0.1237 0.0913 0.0883 -0.0026 -0.0077 -0.0013 97  TRP C O   
5053 C  CB  . TRP C 97  ? 0.0991 0.1120 0.1077 -0.0046 -0.0124 0.0055  97  TRP C CB  
5054 C  CG  . TRP C 97  ? 0.1014 0.0879 0.1009 -0.0074 -0.0063 0.0035  97  TRP C CG  
5055 C  CD1 . TRP C 97  ? 0.1094 0.1146 0.1109 -0.0212 -0.0146 -0.0030 97  TRP C CD1 
5056 C  CD2 . TRP C 97  ? 0.1112 0.1053 0.1132 -0.0078 -0.0077 -0.0008 97  TRP C CD2 
5057 N  NE1 . TRP C 97  ? 0.1269 0.0996 0.1421 -0.0007 -0.0136 -0.0076 97  TRP C NE1 
5058 C  CE2 . TRP C 97  ? 0.1224 0.0985 0.0933 0.0054  -0.0068 0.0107  97  TRP C CE2 
5059 C  CE3 . TRP C 97  ? 0.0931 0.0954 0.1103 0.0001  0.0026  0.0049  97  TRP C CE3 
5060 C  CZ2 . TRP C 97  ? 0.1287 0.1268 0.1109 0.0156  -0.0189 0.0131  97  TRP C CZ2 
5061 C  CZ3 . TRP C 97  ? 0.0996 0.1167 0.1023 0.0172  0.0124  0.0142  97  TRP C CZ3 
5062 C  CH2 . TRP C 97  ? 0.1091 0.1213 0.1211 -0.0023 -0.0176 0.0068  97  TRP C CH2 
5063 N  N   . GLY C 98  ? 0.1036 0.0890 0.0992 0.0060  -0.0108 0.0015  98  GLY C N   
5064 C  CA  . GLY C 98  ? 0.1121 0.1080 0.1042 0.0005  -0.0082 -0.0177 98  GLY C CA  
5065 C  C   . GLY C 98  ? 0.1132 0.0983 0.1369 -0.0082 0.0046  0.0054  98  GLY C C   
5066 O  O   . GLY C 98  ? 0.1208 0.1097 0.1290 -0.0054 0.0024  -0.0003 98  GLY C O   
5067 N  N   . SER C 99  ? 0.1571 0.1204 0.1259 -0.0153 -0.0142 -0.0110 99  SER C N   
5068 C  CA  . SER C 99  ? 0.1601 0.1206 0.1308 -0.0256 -0.0030 -0.0249 99  SER C CA  
5069 C  C   . SER C 99  ? 0.1369 0.1285 0.1601 -0.0148 -0.0046 -0.0198 99  SER C C   
5070 O  O   . SER C 99  ? 0.1816 0.1788 0.2127 -0.0502 -0.0252 -0.0205 99  SER C O   
5071 C  CB  . SER C 99  ? 0.1605 0.1360 0.1353 -0.0294 0.0026  -0.0269 99  SER C CB  
5072 O  OG  . SER C 99  ? 0.2008 0.1457 0.1333 -0.0043 0.0024  -0.0412 99  SER C OG  
5073 N  N   . LEU C 100 ? 0.1660 0.1253 0.1098 -0.0241 0.0110  0.0003  100 LEU C N   
5074 C  CA  . LEU C 100 ? 0.2404 0.1167 0.1568 0.0073  -0.0225 0.0068  100 LEU C CA  
5075 C  C   . LEU C 100 ? 0.1581 0.1570 0.1434 -0.0478 0.0098  0.0019  100 LEU C C   
5076 O  O   . LEU C 100 ? 0.1699 0.1053 0.1386 -0.0233 -0.0066 0.0035  100 LEU C O   
5077 C  CB  . LEU C 100 ? 0.2698 0.1829 0.2089 0.0208  -0.0170 -0.0088 100 LEU C CB  
5078 C  CG  . LEU C 100 ? 0.2700 0.1901 0.2267 -0.0212 0.0027  -0.0403 100 LEU C CG  
5079 C  CD1 . LEU C 100 ? 0.3352 0.4539 0.3109 -0.0287 0.0533  -0.0820 100 LEU C CD1 
5080 C  CD2 . LEU C 100 ? 0.2603 0.2603 0.3420 -0.0529 -0.0718 -0.1077 100 LEU C CD2 
5081 N  N   . ASP C 101 ? 0.1854 0.1308 0.1324 -0.0024 0.0282  -0.0086 101 ASP C N   
5082 C  CA  . ASP C 101 ? 0.1685 0.1347 0.1317 0.0148  0.0000  0.0083  101 ASP C CA  
5083 C  C   . ASP C 101 ? 0.1723 0.1243 0.1421 -0.0015 -0.0032 -0.0115 101 ASP C C   
5084 O  O   . ASP C 101 ? 0.1755 0.1305 0.1730 0.0060  -0.0263 0.0000  101 ASP C O   
5085 C  CB  . ASP C 101 ? 0.1595 0.1410 0.1863 0.0306  0.0247  0.0342  101 ASP C CB  
5086 C  CG  . ASP C 101 ? 0.1664 0.1450 0.1974 -0.0007 0.0012  0.0239  101 ASP C CG  
5087 O  OD1 . ASP C 101 ? 0.1895 0.1699 0.2030 0.0125  -0.0063 0.0344  101 ASP C OD1 
5088 O  OD2 . ASP C 101 ? 0.2020 0.2309 0.3057 -0.0142 0.0209  0.1062  101 ASP C OD2 
5089 N  N   . GLY C 102 ? 0.1382 0.1202 0.1802 0.0131  0.0129  0.0028  102 GLY C N   
5090 C  CA  . GLY C 102 ? 0.1378 0.1168 0.2066 0.0030  0.0353  0.0218  102 GLY C CA  
5091 C  C   . GLY C 102 ? 0.1671 0.1206 0.1459 -0.0087 0.0083  0.0081  102 GLY C C   
5092 O  O   . GLY C 102 ? 0.1699 0.1441 0.1622 0.0196  -0.0068 0.0188  102 GLY C O   
5093 N  N   . GLN C 103 ? 0.1412 0.1357 0.1229 -0.0041 0.0057  0.0116  103 GLN C N   
5094 C  CA  . GLN C 103 ? 0.1100 0.1096 0.1216 0.0071  -0.0127 0.0017  103 GLN C CA  
5095 C  C   . GLN C 103 ? 0.1177 0.0952 0.0904 -0.0021 0.0038  0.0027  103 GLN C C   
5096 O  O   . GLN C 103 ? 0.1200 0.1107 0.1215 0.0054  -0.0141 -0.0057 103 GLN C O   
5097 C  CB  . GLN C 103 ? 0.1251 0.1064 0.1258 0.0165  -0.0120 0.0007  103 GLN C CB  
5098 C  CG  . GLN C 103 ? 0.1333 0.1240 0.1091 -0.0183 -0.0193 -0.0223 103 GLN C CG  
5099 C  CD  . GLN C 103 ? 0.2029 0.1353 0.1727 0.0302  -0.0038 -0.0423 103 GLN C CD  
5100 O  OE1 . GLN C 103 ? 0.2782 0.2596 0.2023 0.1133  -0.0465 -0.0662 103 GLN C OE1 
5101 N  NE2 . GLN C 103 ? 0.2354 0.1718 0.1499 0.0077  0.0089  -0.0177 103 GLN C NE2 
5102 N  N   . GLY C 104 ? 0.1071 0.0915 0.0825 -0.0049 0.0028  -0.0015 104 GLY C N   
5103 C  CA  . GLY C 104 ? 0.1150 0.0908 0.1040 -0.0049 -0.0051 0.0044  104 GLY C CA  
5104 C  C   . GLY C 104 ? 0.0878 0.0942 0.0944 0.0010  -0.0097 0.0054  104 GLY C C   
5105 O  O   . GLY C 104 ? 0.1195 0.1059 0.1152 0.0091  -0.0066 0.0108  104 GLY C O   
5106 N  N   . SER C 105 ? 0.0821 0.0998 0.0764 -0.0108 0.0027  -0.0060 105 SER C N   
5107 C  CA  . SER C 105 ? 0.1039 0.0997 0.0945 -0.0178 -0.0013 -0.0063 105 SER C CA  
5108 C  C   . SER C 105 ? 0.1050 0.0915 0.0854 -0.0048 -0.0086 -0.0001 105 SER C C   
5109 O  O   . SER C 105 ? 0.0997 0.1024 0.1091 -0.0118 0.0110  -0.0071 105 SER C O   
5110 C  CB  . SER C 105 ? 0.1093 0.0960 0.1093 0.0215  -0.0001 0.0044  105 SER C CB  
5111 O  OG  . SER C 105 ? 0.1103 0.0703 0.1091 0.0051  0.0013  -0.0020 105 SER C OG  
5112 N  N   . GLU C 106 ? 0.0952 0.0821 0.0879 -0.0027 0.0006  0.0096  106 GLU C N   
5113 C  CA  . GLU C 106 ? 0.0829 0.0719 0.1112 0.0060  0.0063  -0.0049 106 GLU C CA  
5114 C  C   . GLU C 106 ? 0.0829 0.0827 0.1093 0.0035  0.0035  0.0028  106 GLU C C   
5115 O  O   . GLU C 106 ? 0.0957 0.1039 0.0942 0.0044  0.0131  -0.0071 106 GLU C O   
5116 C  CB  . GLU C 106 ? 0.0870 0.0816 0.1036 0.0103  -0.0115 0.0175  106 GLU C CB  
5117 C  CG  . GLU C 106 ? 0.1019 0.1163 0.1308 -0.0126 -0.0219 0.0181  106 GLU C CG  
5118 C  CD  . GLU C 106 ? 0.1419 0.1142 0.0927 -0.0104 -0.0222 0.0078  106 GLU C CD  
5119 O  OE1 . GLU C 106 ? 0.1377 0.1035 0.1121 -0.0003 0.0137  0.0027  106 GLU C OE1 
5120 O  OE2 . GLU C 106 ? 0.1383 0.1224 0.0985 -0.0052 0.0062  -0.0089 106 GLU C OE2 
5121 N  N   . HIS C 107 ? 0.0807 0.0951 0.1005 0.0089  0.0006  -0.0003 107 HIS C N   
5122 C  CA  . HIS C 107 ? 0.0949 0.0815 0.0842 -0.0037 -0.0133 -0.0102 107 HIS C CA  
5123 C  C   . HIS C 107 ? 0.1008 0.0931 0.0952 0.0021  -0.0052 -0.0021 107 HIS C C   
5124 O  O   . HIS C 107 ? 0.1114 0.1006 0.1064 0.0037  0.0023  0.0000  107 HIS C O   
5125 C  CB  . HIS C 107 ? 0.1080 0.0888 0.0669 -0.0031 0.0131  -0.0052 107 HIS C CB  
5126 C  CG  . HIS C 107 ? 0.1015 0.0927 0.0913 0.0065  -0.0142 -0.0012 107 HIS C CG  
5127 N  ND1 . HIS C 107 ? 0.0931 0.0899 0.0930 0.0080  0.0019  0.0049  107 HIS C ND1 
5128 C  CD2 . HIS C 107 ? 0.1170 0.0890 0.0870 -0.0065 -0.0100 0.0015  107 HIS C CD2 
5129 C  CE1 . HIS C 107 ? 0.0948 0.0949 0.0868 -0.0043 0.0051  -0.0003 107 HIS C CE1 
5130 N  NE2 . HIS C 107 ? 0.0996 0.0872 0.0960 0.0010  -0.0038 -0.0099 107 HIS C NE2 
5131 N  N   . THR C 108 ? 0.1076 0.0927 0.1035 0.0087  -0.0267 0.0074  108 THR C N   
5132 C  CA  . THR C 108 ? 0.1206 0.0694 0.1215 0.0052  -0.0153 -0.0074 108 THR C CA  
5133 C  C   . THR C 108 ? 0.0996 0.0970 0.1082 -0.0003 0.0001  0.0012  108 THR C C   
5134 O  O   . THR C 108 ? 0.1191 0.1036 0.1234 0.0017  0.0031  -0.0082 108 THR C O   
5135 C  CB  . THR C 108 ? 0.0969 0.1149 0.1086 0.0051  0.0000  -0.0038 108 THR C CB  
5136 O  OG1 . THR C 108 ? 0.1010 0.1105 0.1346 0.0151  0.0166  -0.0063 108 THR C OG1 
5137 C  CG2 . THR C 108 ? 0.1041 0.1076 0.1271 -0.0052 -0.0288 -0.0109 108 THR C CG2 
5138 N  N   . VAL C 109 ? 0.1077 0.1019 0.1089 0.0156  -0.0034 0.0063  109 VAL C N   
5139 C  CA  . VAL C 109 ? 0.1098 0.1143 0.1066 0.0276  -0.0127 -0.0012 109 VAL C CA  
5140 C  C   . VAL C 109 ? 0.1235 0.1156 0.1244 0.0105  -0.0102 0.0089  109 VAL C C   
5141 O  O   . VAL C 109 ? 0.1362 0.1076 0.1289 0.0176  -0.0144 -0.0005 109 VAL C O   
5142 C  CB  . VAL C 109 ? 0.1414 0.1075 0.1202 0.0250  0.0124  -0.0060 109 VAL C CB  
5143 C  CG1 . VAL C 109 ? 0.2019 0.1362 0.1299 0.0153  -0.0063 -0.0028 109 VAL C CG1 
5144 C  CG2 . VAL C 109 ? 0.1592 0.1344 0.1676 0.0493  0.0000  -0.0203 109 VAL C CG2 
5145 N  N   . ASP C 110 ? 0.1190 0.1134 0.1389 0.0200  -0.0170 -0.0115 110 ASP C N   
5146 C  CA  . ASP C 110 ? 0.1965 0.1199 0.1592 0.0531  -0.0348 -0.0194 110 ASP C CA  
5147 C  C   . ASP C 110 ? 0.1491 0.1168 0.1292 0.0098  -0.0289 -0.0017 110 ASP C C   
5148 O  O   . ASP C 110 ? 0.1653 0.1231 0.1574 0.0324  -0.0062 0.0071  110 ASP C O   
5149 C  CB  . ASP C 110 ? 0.1919 0.1362 0.1562 0.0544  -0.0467 0.0055  110 ASP C CB  
5150 C  CG  . ASP C 110 ? 0.1396 0.1480 0.1721 0.0509  -0.0225 0.0037  110 ASP C CG  
5151 O  OD1 . ASP C 110 ? 0.2087 0.1551 0.1784 0.0256  -0.0522 -0.0060 110 ASP C OD1 
5152 O  OD2 . ASP C 110 ? 0.2127 0.2448 0.2019 0.0509  -0.0366 -0.0028 110 ASP C OD2 
5153 N  N   . LYS C 111 ? 0.1206 0.1124 0.1416 0.0194  -0.0085 0.0152  111 LYS C N   
5154 C  CA  . LYS C 111 ? 0.1281 0.1118 0.1511 0.0199  0.0080  -0.0082 111 LYS C CA  
5155 C  C   . LYS C 111 ? 0.1279 0.1150 0.1443 0.0269  -0.0126 -0.0085 111 LYS C C   
5156 O  O   . LYS C 111 ? 0.1574 0.1306 0.1386 0.0140  -0.0203 -0.0068 111 LYS C O   
5157 C  CB  . LYS C 111 ? 0.1425 0.1407 0.1737 0.0187  0.0229  -0.0225 111 LYS C CB  
5158 C  CG  . LYS C 111 ? 0.1278 0.1784 0.2556 0.0337  0.0394  -0.0089 111 LYS C CG  
5159 C  CD  . LYS C 111 ? 0.2558 0.2829 0.2474 -0.0640 0.0763  0.0027  111 LYS C CD  
5160 C  CE  . LYS C 111 ? 0.1894 0.2919 0.2976 -0.0284 0.0242  -0.0857 111 LYS C CE  
5161 N  NZ  . LYS C 111 ? 0.2912 0.3253 0.2894 0.0595  0.0970  -0.0243 111 LYS C NZ  
5162 N  N   . LYS C 112 ? 0.1238 0.0873 0.1349 0.0236  0.0052  -0.0059 112 LYS C N   
5163 C  CA  . LYS C 112 ? 0.1165 0.1217 0.1365 0.0074  -0.0078 0.0148  112 LYS C CA  
5164 C  C   . LYS C 112 ? 0.1057 0.1167 0.1130 0.0017  0.0151  -0.0041 112 LYS C C   
5165 O  O   . LYS C 112 ? 0.1200 0.1006 0.1285 -0.0023 0.0052  -0.0127 112 LYS C O   
5166 C  CB  . LYS C 112 ? 0.1235 0.1212 0.1667 0.0154  -0.0070 0.0126  112 LYS C CB  
5167 C  CG  . LYS C 112 ? 0.1540 0.1567 0.1565 -0.0313 0.0038  0.0317  112 LYS C CG  
5168 C  CD  . LYS C 112 ? 0.1781 0.2416 0.1748 -0.0046 0.0538  -0.0098 112 LYS C CD  
5169 C  CE  . LYS C 112 ? 0.2140 0.1996 0.2104 -0.0274 0.0388  0.0208  112 LYS C CE  
5170 N  NZ  . LYS C 112 ? 0.2111 0.1754 0.2529 -0.0043 0.0388  -0.0035 112 LYS C NZ  
5171 N  N   A LYS C 113 ? 0.1014 0.1059 0.1172 0.0133  0.0020  -0.0153 113 LYS C N   
5172 N  N   B LYS C 113 ? 0.1014 0.1068 0.1145 0.0094  0.0035  -0.0164 113 LYS C N   
5173 C  CA  A LYS C 113 ? 0.1127 0.0872 0.1359 0.0220  0.0096  -0.0071 113 LYS C CA  
5174 C  CA  B LYS C 113 ? 0.1141 0.0996 0.1305 0.0243  0.0122  -0.0097 113 LYS C CA  
5175 C  C   A LYS C 113 ? 0.1269 0.0870 0.1145 0.0017  0.0073  -0.0070 113 LYS C C   
5176 C  C   B LYS C 113 ? 0.1138 0.0909 0.1362 -0.0024 0.0049  -0.0096 113 LYS C C   
5177 O  O   A LYS C 113 ? 0.1237 0.0906 0.1124 -0.0052 0.0063  -0.0027 113 LYS C O   
5178 O  O   B LYS C 113 ? 0.1331 0.0843 0.1146 0.0000  -0.0156 0.0105  113 LYS C O   
5179 C  CB  A LYS C 113 ? 0.1001 0.1283 0.1176 0.0164  0.0122  0.0005  113 LYS C CB  
5180 C  CB  B LYS C 113 ? 0.1326 0.0864 0.1208 0.0062  0.0126  -0.0141 113 LYS C CB  
5181 C  CG  A LYS C 113 ? 0.1096 0.1057 0.1168 0.0038  0.0037  -0.0104 113 LYS C CG  
5182 C  CG  B LYS C 113 ? 0.1337 0.1407 0.1256 -0.0159 0.0063  -0.0248 113 LYS C CG  
5183 C  CD  A LYS C 113 ? 0.1102 0.1678 0.0927 -0.0098 0.0081  -0.0109 113 LYS C CD  
5184 C  CD  B LYS C 113 ? 0.1470 0.0879 0.1120 -0.0211 0.0173  -0.0037 113 LYS C CD  
5185 C  CE  A LYS C 113 ? 0.1398 0.1215 0.1102 0.0005  0.0034  0.0089  113 LYS C CE  
5186 C  CE  B LYS C 113 ? 0.1235 0.1601 0.1167 -0.0187 -0.0015 0.0130  113 LYS C CE  
5187 N  NZ  A LYS C 113 ? 0.1324 0.1516 0.1578 0.0103  -0.0003 -0.0028 113 LYS C NZ  
5188 N  NZ  B LYS C 113 ? 0.1687 0.2055 0.1304 0.0125  0.0175  0.0015  113 LYS C NZ  
5189 N  N   . TYR C 114 ? 0.0948 0.1010 0.1062 0.0077  -0.0007 -0.0038 114 TYR C N   
5190 C  CA  . TYR C 114 ? 0.0935 0.0992 0.0971 0.0113  0.0059  -0.0031 114 TYR C CA  
5191 C  C   . TYR C 114 ? 0.1045 0.0795 0.1001 0.0120  0.0023  0.0109  114 TYR C C   
5192 O  O   . TYR C 114 ? 0.1188 0.0994 0.0899 -0.0024 0.0049  0.0017  114 TYR C O   
5193 C  CB  . TYR C 114 ? 0.1195 0.1127 0.0894 0.0080  -0.0071 -0.0135 114 TYR C CB  
5194 C  CG  . TYR C 114 ? 0.1109 0.0969 0.1100 0.0156  0.0001  -0.0005 114 TYR C CG  
5195 C  CD1 . TYR C 114 ? 0.1193 0.1005 0.1319 0.0261  -0.0144 0.0008  114 TYR C CD1 
5196 C  CD2 . TYR C 114 ? 0.1301 0.0991 0.1249 0.0120  0.0007  -0.0007 114 TYR C CD2 
5197 C  CE1 . TYR C 114 ? 0.1335 0.1364 0.1475 0.0274  -0.0243 -0.0087 114 TYR C CE1 
5198 C  CE2 . TYR C 114 ? 0.1800 0.1441 0.1251 0.0310  0.0085  -0.0068 114 TYR C CE2 
5199 C  CZ  . TYR C 114 ? 0.1685 0.1536 0.1461 0.0244  -0.0276 0.0127  114 TYR C CZ  
5200 O  OH  . TYR C 114 ? 0.2309 0.1994 0.1953 0.0178  -0.0756 -0.0043 114 TYR C OH  
5201 N  N   . ALA C 115 ? 0.0969 0.0879 0.1055 0.0115  -0.0017 0.0006  115 ALA C N   
5202 C  CA  . ALA C 115 ? 0.1215 0.0723 0.1105 -0.0052 -0.0099 -0.0049 115 ALA C CA  
5203 C  C   . ALA C 115 ? 0.1071 0.0809 0.1084 0.0102  -0.0054 -0.0060 115 ALA C C   
5204 O  O   . ALA C 115 ? 0.1316 0.0829 0.1053 -0.0019 -0.0071 -0.0062 115 ALA C O   
5205 C  CB  . ALA C 115 ? 0.1534 0.1194 0.1066 -0.0015 0.0243  -0.0097 115 ALA C CB  
5206 N  N   . ALA C 116 ? 0.1121 0.0845 0.1093 -0.0017 0.0057  -0.0077 116 ALA C N   
5207 C  CA  . ALA C 116 ? 0.0951 0.1012 0.1096 0.0115  -0.0086 0.0032  116 ALA C CA  
5208 C  C   . ALA C 116 ? 0.0892 0.0912 0.1091 0.0068  0.0023  0.0082  116 ALA C C   
5209 O  O   . ALA C 116 ? 0.0992 0.0915 0.0978 0.0035  0.0000  0.0017  116 ALA C O   
5210 C  CB  . ALA C 116 ? 0.0888 0.1115 0.1052 0.0087  -0.0013 0.0048  116 ALA C CB  
5211 N  N   . GLU C 117 ? 0.1021 0.0824 0.0969 0.0012  0.0006  0.0000  117 GLU C N   
5212 C  CA  . GLU C 117 ? 0.0949 0.0732 0.1141 0.0149  0.0082  -0.0035 117 GLU C CA  
5213 C  C   . GLU C 117 ? 0.0807 0.0912 0.0881 0.0104  -0.0030 -0.0086 117 GLU C C   
5214 O  O   . GLU C 117 ? 0.1261 0.1053 0.1026 0.0175  -0.0006 0.0083  117 GLU C O   
5215 C  CB  . GLU C 117 ? 0.0895 0.1177 0.1066 0.0013  0.0024  -0.0094 117 GLU C CB  
5216 C  CG  . GLU C 117 ? 0.0966 0.1000 0.1217 0.0013  0.0013  -0.0137 117 GLU C CG  
5217 C  CD  . GLU C 117 ? 0.1159 0.0992 0.0942 0.0000  -0.0105 0.0003  117 GLU C CD  
5218 O  OE1 . GLU C 117 ? 0.1107 0.1040 0.1071 0.0003  0.0186  -0.0017 117 GLU C OE1 
5219 O  OE2 . GLU C 117 ? 0.0861 0.1006 0.1102 -0.0060 0.0027  0.0052  117 GLU C OE2 
5220 N  N   . LEU C 118 ? 0.0976 0.0820 0.1015 0.0160  0.0005  -0.0109 118 LEU C N   
5221 C  CA  . LEU C 118 ? 0.0929 0.0703 0.0930 0.0114  0.0065  0.0035  118 LEU C CA  
5222 C  C   . LEU C 118 ? 0.0834 0.0854 0.0839 0.0108  -0.0015 0.0038  118 LEU C C   
5223 O  O   . LEU C 118 ? 0.0966 0.0822 0.0886 0.0165  -0.0071 -0.0001 118 LEU C O   
5224 C  CB  . LEU C 118 ? 0.1161 0.0974 0.0859 0.0126  0.0151  -0.0032 118 LEU C CB  
5225 C  CG  . LEU C 118 ? 0.0998 0.0908 0.1150 0.0259  0.0093  0.0034  118 LEU C CG  
5226 C  CD1 . LEU C 118 ? 0.0910 0.1211 0.1384 0.0113  0.0074  0.0057  118 LEU C CD1 
5227 C  CD2 . LEU C 118 ? 0.1351 0.1409 0.1059 0.0331  0.0362  0.0001  118 LEU C CD2 
5228 N  N   . HIS C 119 ? 0.0931 0.0626 0.0890 0.0154  -0.0013 0.0000  119 HIS C N   
5229 C  CA  . HIS C 119 ? 0.0960 0.0794 0.0866 0.0024  0.0147  0.0000  119 HIS C CA  
5230 C  C   . HIS C 119 ? 0.0857 0.0885 0.0821 0.0093  0.0074  0.0023  119 HIS C C   
5231 O  O   . HIS C 119 ? 0.0958 0.0912 0.0922 0.0049  -0.0173 -0.0070 119 HIS C O   
5232 C  CB  . HIS C 119 ? 0.0976 0.0861 0.0877 0.0179  0.0193  -0.0008 119 HIS C CB  
5233 C  CG  . HIS C 119 ? 0.0755 0.0888 0.0815 0.0024  -0.0044 -0.0091 119 HIS C CG  
5234 N  ND1 . HIS C 119 ? 0.1035 0.0931 0.0852 0.0066  0.0043  0.0140  119 HIS C ND1 
5235 C  CD2 . HIS C 119 ? 0.0987 0.0802 0.1109 0.0078  0.0035  -0.0027 119 HIS C CD2 
5236 C  CE1 . HIS C 119 ? 0.0685 0.1019 0.1037 -0.0032 -0.0181 0.0125  119 HIS C CE1 
5237 N  NE2 . HIS C 119 ? 0.0988 0.1010 0.1023 0.0102  0.0146  0.0019  119 HIS C NE2 
5238 N  N   . LEU C 120 ? 0.0996 0.0901 0.0952 0.0142  -0.0031 0.0013  120 LEU C N   
5239 C  CA  . LEU C 120 ? 0.1084 0.0845 0.1042 0.0065  0.0119  -0.0138 120 LEU C CA  
5240 C  C   . LEU C 120 ? 0.0931 0.0873 0.0938 0.0153  -0.0093 0.0000  120 LEU C C   
5241 O  O   . LEU C 120 ? 0.0906 0.0971 0.0942 0.0062  -0.0021 0.0035  120 LEU C O   
5242 C  CB  . LEU C 120 ? 0.1332 0.0940 0.1107 0.0030  0.0258  -0.0133 120 LEU C CB  
5243 C  CG  . LEU C 120 ? 0.1057 0.1152 0.1299 0.0185  -0.0034 -0.0027 120 LEU C CG  
5244 C  CD1 . LEU C 120 ? 0.1737 0.1335 0.1865 0.0077  -0.0205 0.0542  120 LEU C CD1 
5245 C  CD2 . LEU C 120 ? 0.1382 0.1642 0.1809 0.0216  0.0406  -0.0406 120 LEU C CD2 
5246 N  N   . VAL C 121 ? 0.1057 0.0873 0.1012 0.0065  -0.0092 0.0063  121 VAL C N   
5247 C  CA  . VAL C 121 ? 0.1150 0.0958 0.1008 0.0000  -0.0019 0.0003  121 VAL C CA  
5248 C  C   . VAL C 121 ? 0.0949 0.0922 0.0960 0.0049  0.0076  0.0055  121 VAL C C   
5249 O  O   . VAL C 121 ? 0.0939 0.1019 0.1281 0.0010  0.0015  0.0003  121 VAL C O   
5250 C  CB  . VAL C 121 ? 0.1355 0.0967 0.1057 0.0020  -0.0087 0.0032  121 VAL C CB  
5251 C  CG1 . VAL C 121 ? 0.1459 0.1368 0.0755 0.0024  0.0054  0.0149  121 VAL C CG1 
5252 C  CG2 . VAL C 121 ? 0.1312 0.1075 0.1142 0.0115  -0.0203 -0.0275 121 VAL C CG2 
5253 N  N   . HIS C 122 ? 0.1044 0.0839 0.0940 0.0027  0.0021  0.0099  122 HIS C N   
5254 C  CA  . HIS C 122 ? 0.1224 0.0913 0.1079 -0.0020 -0.0108 -0.0010 122 HIS C CA  
5255 C  C   . HIS C 122 ? 0.1073 0.1055 0.1107 0.0111  0.0001  0.0086  122 HIS C C   
5256 O  O   . HIS C 122 ? 0.1082 0.0833 0.1308 0.0037  0.0063  0.0006  122 HIS C O   
5257 C  CB  . HIS C 122 ? 0.1262 0.1077 0.0926 0.0030  -0.0109 0.0006  122 HIS C CB  
5258 C  CG  . HIS C 122 ? 0.1222 0.0890 0.1018 0.0179  -0.0186 0.0124  122 HIS C CG  
5259 N  ND1 . HIS C 122 ? 0.1317 0.0877 0.1001 0.0215  0.0105  -0.0059 122 HIS C ND1 
5260 C  CD2 . HIS C 122 ? 0.1263 0.1143 0.1048 0.0151  -0.0063 -0.0027 122 HIS C CD2 
5261 C  CE1 . HIS C 122 ? 0.1280 0.1229 0.0956 -0.0068 0.0046  -0.0122 122 HIS C CE1 
5262 N  NE2 . HIS C 122 ? 0.1226 0.1164 0.0983 0.0099  0.0021  0.0037  122 HIS C NE2 
5263 N  N   . TRP C 123 ? 0.1061 0.1000 0.1037 0.0006  0.0000  0.0119  123 TRP C N   
5264 C  CA  . TRP C 123 ? 0.1127 0.0874 0.1039 -0.0021 -0.0083 -0.0035 123 TRP C CA  
5265 C  C   . TRP C 123 ? 0.0966 0.0906 0.0908 0.0040  -0.0049 0.0077  123 TRP C C   
5266 O  O   . TRP C 123 ? 0.1280 0.1053 0.1127 -0.0052 0.0115  0.0008  123 TRP C O   
5267 C  CB  . TRP C 123 ? 0.1457 0.1152 0.1324 0.0104  0.0031  0.0318  123 TRP C CB  
5268 C  CG  . TRP C 123 ? 0.1502 0.1082 0.1109 0.0086  -0.0149 0.0027  123 TRP C CG  
5269 C  CD1 . TRP C 123 ? 0.1310 0.1254 0.1699 0.0208  0.0118  0.0188  123 TRP C CD1 
5270 C  CD2 . TRP C 123 ? 0.1518 0.1128 0.1492 -0.0024 -0.0165 0.0059  123 TRP C CD2 
5271 N  NE1 . TRP C 123 ? 0.1254 0.1206 0.1622 0.0142  -0.0238 0.0102  123 TRP C NE1 
5272 C  CE2 . TRP C 123 ? 0.1534 0.1229 0.1744 -0.0017 -0.0087 -0.0122 123 TRP C CE2 
5273 C  CE3 . TRP C 123 ? 0.1710 0.0985 0.1393 0.0099  -0.0260 0.0006  123 TRP C CE3 
5274 C  CZ2 . TRP C 123 ? 0.1737 0.1269 0.1953 0.0225  -0.0346 0.0156  123 TRP C CZ2 
5275 C  CZ3 . TRP C 123 ? 0.1594 0.1106 0.1678 0.0272  -0.0077 0.0253  123 TRP C CZ3 
5276 C  CH2 . TRP C 123 ? 0.1489 0.1464 0.2011 0.0089  -0.0423 0.0237  123 TRP C CH2 
5277 N  N   . ASN C 124 ? 0.1073 0.0994 0.1121 -0.0115 -0.0082 -0.0104 124 ASN C N   
5278 C  CA  . ASN C 124 ? 0.1190 0.0938 0.1267 0.0040  -0.0166 -0.0186 124 ASN C CA  
5279 C  C   . ASN C 124 ? 0.1386 0.0985 0.1143 -0.0091 0.0035  -0.0087 124 ASN C C   
5280 O  O   . ASN C 124 ? 0.1504 0.0974 0.1147 -0.0077 -0.0100 0.0000  124 ASN C O   
5281 C  CB  . ASN C 124 ? 0.1161 0.1085 0.1495 0.0052  -0.0198 -0.0080 124 ASN C CB  
5282 C  CG  . ASN C 124 ? 0.1292 0.1062 0.1197 -0.0057 -0.0034 0.0048  124 ASN C CG  
5283 O  OD1 . ASN C 124 ? 0.1597 0.1238 0.1588 0.0007  -0.0149 -0.0241 124 ASN C OD1 
5284 N  ND2 . ASN C 124 ? 0.1444 0.1012 0.1763 0.0078  -0.0229 -0.0201 124 ASN C ND2 
5285 N  N   . THR C 125 ? 0.1353 0.1209 0.1389 0.0137  -0.0010 -0.0245 125 THR C N   
5286 C  CA  . THR C 125 ? 0.1507 0.1064 0.1682 0.0144  0.0211  -0.0126 125 THR C CA  
5287 C  C   . THR C 125 ? 0.1781 0.1290 0.1331 0.0110  0.0008  -0.0217 125 THR C C   
5288 O  O   . THR C 125 ? 0.2002 0.1313 0.1745 0.0282  -0.0105 0.0086  125 THR C O   
5289 C  CB  . THR C 125 ? 0.2301 0.1457 0.1937 0.0171  0.0197  -0.0307 125 THR C CB  
5290 O  OG1 . THR C 125 ? 0.3163 0.1793 0.1826 0.0238  -0.0052 -0.0507 125 THR C OG1 
5291 C  CG2 . THR C 125 ? 0.2450 0.1780 0.2436 -0.0119 0.0712  0.0115  125 THR C CG2 
5292 N  N   . LYS C 126 ? 0.1854 0.1071 0.1410 -0.0313 -0.0331 -0.0164 127 LYS C N   
5293 C  CA  . LYS C 126 ? 0.1840 0.1411 0.1816 -0.0485 -0.0309 -0.0030 127 LYS C CA  
5294 C  C   . LYS C 126 ? 0.1635 0.0974 0.1762 0.0048  -0.0093 0.0015  127 LYS C C   
5295 O  O   . LYS C 126 ? 0.2025 0.1185 0.1908 -0.0185 -0.0028 0.0197  127 LYS C O   
5296 C  CB  . LYS C 126 ? 0.1807 0.1588 0.2050 -0.0201 0.0109  -0.0140 127 LYS C CB  
5297 C  CG  . LYS C 126 ? 0.1532 0.1852 0.2337 -0.0219 -0.0226 -0.0205 127 LYS C CG  
5298 C  CD  . LYS C 126 ? 0.2039 0.2703 0.3077 -0.0588 -0.0873 0.0696  127 LYS C CD  
5299 C  CE  . LYS C 126 ? 0.3102 0.3813 0.2872 -0.0044 -0.0544 0.0538  127 LYS C CE  
5300 N  NZ  . LYS C 126 ? 0.3901 0.5004 0.5740 -0.1044 0.0553  0.1268  127 LYS C NZ  
5301 N  N   . TYR C 127 ? 0.1393 0.1322 0.1595 0.0035  -0.0114 -0.0143 128 TYR C N   
5302 C  CA  . TYR C 127 ? 0.1212 0.1270 0.1508 -0.0034 0.0263  -0.0147 128 TYR C CA  
5303 C  C   . TYR C 127 ? 0.1648 0.1046 0.1410 0.0010  0.0135  -0.0076 128 TYR C C   
5304 O  O   . TYR C 127 ? 0.1673 0.0994 0.1556 0.0113  -0.0167 0.0066  128 TYR C O   
5305 C  CB  . TYR C 127 ? 0.1809 0.1037 0.1341 -0.0010 -0.0021 -0.0252 128 TYR C CB  
5306 C  CG  . TYR C 127 ? 0.1439 0.1067 0.1359 -0.0144 0.0077  -0.0020 128 TYR C CG  
5307 C  CD1 . TYR C 127 ? 0.1323 0.1233 0.1723 -0.0041 0.0082  -0.0118 128 TYR C CD1 
5308 C  CD2 . TYR C 127 ? 0.1267 0.1224 0.1554 0.0076  -0.0031 -0.0046 128 TYR C CD2 
5309 C  CE1 . TYR C 127 ? 0.1500 0.1357 0.2090 -0.0073 -0.0318 -0.0125 128 TYR C CE1 
5310 C  CE2 . TYR C 127 ? 0.1240 0.1256 0.1586 -0.0038 -0.0211 -0.0138 128 TYR C CE2 
5311 C  CZ  . TYR C 127 ? 0.1493 0.1222 0.1624 -0.0076 -0.0177 -0.0315 128 TYR C CZ  
5312 O  OH  . TYR C 127 ? 0.1606 0.1466 0.2142 -0.0032 -0.0227 -0.0434 128 TYR C OH  
5313 N  N   . GLY C 128 ? 0.1378 0.1150 0.1471 0.0068  0.0068  0.0100  129 GLY C N   
5314 C  CA  . GLY C 128 ? 0.1509 0.1120 0.1709 0.0057  -0.0247 -0.0003 129 GLY C CA  
5315 C  C   . GLY C 128 ? 0.1269 0.1143 0.1396 0.0176  -0.0156 0.0031  129 GLY C C   
5316 O  O   . GLY C 128 ? 0.1630 0.1212 0.1958 0.0119  -0.0043 -0.0035 129 GLY C O   
5317 N  N   . ASP C 129 ? 0.1263 0.1333 0.1623 0.0105  -0.0162 -0.0089 130 ASP C N   
5318 C  CA  . ASP C 129 ? 0.1729 0.1268 0.1797 0.0124  -0.0337 -0.0315 130 ASP C CA  
5319 C  C   . ASP C 129 ? 0.1500 0.1520 0.1809 -0.0059 0.0144  -0.0132 130 ASP C C   
5320 O  O   . ASP C 129 ? 0.1529 0.1267 0.2003 0.0055  -0.0115 -0.0122 130 ASP C O   
5321 C  CB  . ASP C 129 ? 0.2205 0.1741 0.1777 0.0403  -0.0226 -0.0346 130 ASP C CB  
5322 C  CG  . ASP C 129 ? 0.2441 0.1608 0.1935 0.0308  -0.0260 -0.0812 130 ASP C CG  
5323 O  OD1 . ASP C 129 ? 0.2327 0.2246 0.3122 -0.0197 0.0553  0.0315  130 ASP C OD1 
5324 O  OD2 . ASP C 129 ? 0.2870 0.2721 0.2802 0.0320  -0.0722 0.0344  130 ASP C OD2 
5325 N  N   . PHE C 130 ? 0.1322 0.1190 0.1938 0.0137  -0.0463 -0.0046 131 PHE C N   
5326 C  CA  . PHE C 130 ? 0.1597 0.1310 0.1676 0.0252  -0.0215 0.0164  131 PHE C CA  
5327 C  C   . PHE C 130 ? 0.1470 0.1405 0.1462 0.0245  -0.0274 -0.0057 131 PHE C C   
5328 O  O   . PHE C 130 ? 0.1425 0.1272 0.1541 0.0073  -0.0118 0.0027  131 PHE C O   
5329 C  CB  . PHE C 130 ? 0.1956 0.1730 0.2125 -0.0361 -0.0233 0.0390  131 PHE C CB  
5330 C  CG  . PHE C 130 ? 0.2363 0.1929 0.2861 -0.0020 -0.0383 -0.0096 131 PHE C CG  
5331 C  CD1 . PHE C 130 ? 0.2494 0.3156 0.4229 0.0263  -0.0846 -0.0498 131 PHE C CD1 
5332 C  CD2 . PHE C 130 ? 0.3679 0.2233 0.2267 -0.0401 -0.0339 0.0109  131 PHE C CD2 
5333 C  CE1 . PHE C 130 ? 0.2427 0.3923 0.2773 0.0052  -0.0178 0.0038  131 PHE C CE1 
5334 C  CE2 . PHE C 130 ? 0.3892 0.2293 0.3731 0.0487  -0.1335 -0.0167 131 PHE C CE2 
5335 C  CZ  . PHE C 130 ? 0.3447 0.3111 0.3468 0.0344  -0.1125 -0.1115 131 PHE C CZ  
5336 N  N   . GLY C 131 ? 0.1588 0.1578 0.1527 0.0115  -0.0340 0.0080  132 GLY C N   
5337 C  CA  . GLY C 131 ? 0.1711 0.1520 0.1500 0.0226  -0.0474 0.0023  132 GLY C CA  
5338 C  C   . GLY C 131 ? 0.1850 0.1781 0.1554 0.0283  -0.0362 0.0278  132 GLY C C   
5339 O  O   . GLY C 131 ? 0.2229 0.1762 0.1764 -0.0059 0.0010  -0.0006 132 GLY C O   
5340 N  N   . LYS C 132 ? 0.1999 0.1471 0.1389 0.0108  -0.0364 0.0368  133 LYS C N   
5341 C  CA  . LYS C 132 ? 0.1937 0.1240 0.1699 0.0141  -0.0017 0.0233  133 LYS C CA  
5342 C  C   . LYS C 132 ? 0.1461 0.1332 0.1550 0.0041  -0.0167 0.0172  133 LYS C C   
5343 O  O   . LYS C 132 ? 0.1419 0.1337 0.1865 -0.0148 0.0122  0.0203  133 LYS C O   
5344 C  CB  . LYS C 132 ? 0.2025 0.1396 0.1393 0.0207  -0.0012 0.0001  133 LYS C CB  
5345 C  CG  . LYS C 132 ? 0.2567 0.2027 0.2222 0.0830  0.0361  0.0496  133 LYS C CG  
5346 C  CD  . LYS C 132 ? 0.3016 0.3310 0.2838 0.0794  0.0619  0.0617  133 LYS C CD  
5347 C  CE  . LYS C 132 ? 0.2951 0.3183 0.3603 -0.0063 0.0732  0.0408  133 LYS C CE  
5348 N  NZ  . LYS C 132 ? 0.5766 0.3292 0.6808 -0.2043 -0.0269 -0.0108 133 LYS C NZ  
5349 N  N   . ALA C 133 ? 0.1644 0.1188 0.1477 -0.0020 0.0152  0.0152  134 ALA C N   
5350 C  CA  . ALA C 133 ? 0.1222 0.1572 0.1586 0.0138  -0.0060 -0.0019 134 ALA C CA  
5351 C  C   . ALA C 133 ? 0.1301 0.1141 0.1290 -0.0100 -0.0077 0.0020  134 ALA C C   
5352 O  O   . ALA C 133 ? 0.1297 0.1322 0.1328 0.0020  -0.0001 0.0019  134 ALA C O   
5353 C  CB  . ALA C 133 ? 0.1545 0.1310 0.1333 -0.0142 -0.0024 0.0186  134 ALA C CB  
5354 N  N   . VAL C 134 ? 0.1308 0.1041 0.1301 -0.0142 -0.0074 0.0107  135 VAL C N   
5355 C  CA  . VAL C 134 ? 0.1216 0.1234 0.1298 0.0107  0.0003  0.0140  135 VAL C CA  
5356 C  C   . VAL C 134 ? 0.1684 0.1401 0.1218 0.0006  0.0000  0.0154  135 VAL C C   
5357 O  O   . VAL C 134 ? 0.1527 0.1626 0.1465 0.0082  -0.0041 -0.0104 135 VAL C O   
5358 C  CB  . VAL C 134 ? 0.1359 0.1508 0.1588 0.0105  -0.0109 -0.0007 135 VAL C CB  
5359 C  CG1 . VAL C 134 ? 0.1649 0.1923 0.1926 -0.0320 -0.0233 0.0267  135 VAL C CG1 
5360 C  CG2 . VAL C 134 ? 0.1798 0.1565 0.1389 -0.0183 -0.0160 0.0062  135 VAL C CG2 
5361 N  N   . GLN C 135 ? 0.1635 0.1230 0.1395 -0.0250 -0.0013 -0.0021 136 GLN C N   
5362 C  CA  . GLN C 135 ? 0.1597 0.1434 0.1667 -0.0043 0.0048  -0.0093 136 GLN C CA  
5363 C  C   . GLN C 135 ? 0.1540 0.1770 0.1490 -0.0159 -0.0006 -0.0192 136 GLN C C   
5364 O  O   . GLN C 135 ? 0.1798 0.1944 0.1896 -0.0197 0.0217  0.0076  136 GLN C O   
5365 C  CB  . GLN C 135 ? 0.1753 0.1628 0.1906 -0.0193 0.0073  0.0274  136 GLN C CB  
5366 C  CG  . GLN C 135 ? 0.2186 0.2027 0.2046 0.0116  -0.0017 0.0226  136 GLN C CG  
5367 C  CD  . GLN C 135 ? 0.3041 0.2644 0.2811 -0.0010 -0.0675 0.0566  136 GLN C CD  
5368 O  OE1 . GLN C 135 ? 0.3792 0.4466 0.3628 0.0675  0.0421  0.0820  136 GLN C OE1 
5369 N  NE2 . GLN C 135 ? 0.3977 0.3458 0.3813 -0.0131 0.0348  0.1722  136 GLN C NE2 
5370 N  N   . GLN C 136 ? 0.1524 0.1328 0.1472 0.0104  -0.0100 -0.0028 137 GLN C N   
5371 C  CA  . GLN C 136 ? 0.1351 0.1391 0.1571 -0.0121 -0.0088 -0.0153 137 GLN C CA  
5372 C  C   . GLN C 136 ? 0.1703 0.1486 0.1796 -0.0010 -0.0055 0.0032  137 GLN C C   
5373 O  O   . GLN C 136 ? 0.1226 0.1504 0.1666 -0.0138 -0.0094 -0.0142 137 GLN C O   
5374 C  CB  . GLN C 136 ? 0.1240 0.1624 0.1545 0.0046  0.0087  -0.0065 137 GLN C CB  
5375 C  CG  . GLN C 136 ? 0.2199 0.1748 0.2231 0.0188  -0.0228 -0.0263 137 GLN C CG  
5376 C  CD  . GLN C 136 ? 0.2087 0.2039 0.2348 0.0916  0.0000  -0.0113 137 GLN C CD  
5377 O  OE1 . GLN C 136 ? 0.2034 0.1919 0.2303 -0.0612 0.0223  -0.0006 137 GLN C OE1 
5378 N  NE2 . GLN C 136 ? 0.2842 0.2660 0.2287 0.0219  -0.0663 0.0681  137 GLN C NE2 
5379 N  N   . PRO C 137 ? 0.1342 0.1382 0.1572 -0.0005 0.0174  -0.0166 138 PRO C N   
5380 C  CA  . PRO C 137 ? 0.1116 0.1606 0.1972 0.0017  -0.0098 -0.0259 138 PRO C CA  
5381 C  C   . PRO C 137 ? 0.1615 0.1775 0.1926 -0.0252 -0.0243 -0.0163 138 PRO C C   
5382 O  O   . PRO C 137 ? 0.1914 0.1631 0.1844 0.0140  0.0035  -0.0231 138 PRO C O   
5383 C  CB  . PRO C 137 ? 0.1168 0.2488 0.2827 -0.0137 -0.0248 -0.0203 138 PRO C CB  
5384 C  CG  . PRO C 137 ? 0.2053 0.2745 0.3228 -0.0469 0.0023  0.0608  138 PRO C CG  
5385 C  CD  . PRO C 137 ? 0.1464 0.2129 0.2293 -0.0496 0.0062  -0.0024 138 PRO C CD  
5386 N  N   . ASP C 138 ? 0.1037 0.1447 0.1545 -0.0081 -0.0165 0.0024  139 ASP C N   
5387 C  CA  . ASP C 138 ? 0.1209 0.1721 0.1497 -0.0096 -0.0322 -0.0013 139 ASP C CA  
5388 C  C   . ASP C 138 ? 0.1298 0.1375 0.1443 0.0035  -0.0076 -0.0017 139 ASP C C   
5389 O  O   . ASP C 138 ? 0.1407 0.1427 0.1412 -0.0046 -0.0068 -0.0078 139 ASP C O   
5390 C  CB  . ASP C 138 ? 0.1689 0.1459 0.2048 0.0078  -0.0434 -0.0252 139 ASP C CB  
5391 C  CG  . ASP C 138 ? 0.1678 0.1685 0.1928 -0.0049 -0.0282 -0.0091 139 ASP C CG  
5392 O  OD1 . ASP C 138 ? 0.1824 0.1632 0.1888 -0.0135 -0.0216 -0.0320 139 ASP C OD1 
5393 O  OD2 . ASP C 138 ? 0.2166 0.2500 0.2436 -0.0375 -0.0322 -0.0606 139 ASP C OD2 
5394 N  N   . GLY C 139 ? 0.1197 0.1331 0.1459 0.0026  -0.0164 0.0205  140 GLY C N   
5395 C  CA  . GLY C 139 ? 0.1019 0.1023 0.1788 0.0037  -0.0222 0.0142  140 GLY C CA  
5396 C  C   . GLY C 139 ? 0.1015 0.1067 0.1109 0.0108  -0.0135 -0.0035 140 GLY C C   
5397 O  O   . GLY C 139 ? 0.1100 0.1005 0.1340 0.0005  0.0089  -0.0119 140 GLY C O   
5398 N  N   . LEU C 140 ? 0.1120 0.0938 0.1120 -0.0003 -0.0003 0.0089  141 LEU C N   
5399 C  CA  . LEU C 140 ? 0.0966 0.1048 0.0821 -0.0054 -0.0113 -0.0049 141 LEU C CA  
5400 C  C   . LEU C 140 ? 0.0944 0.0960 0.1005 0.0076  -0.0003 -0.0175 141 LEU C C   
5401 O  O   . LEU C 140 ? 0.0970 0.0886 0.1249 0.0044  -0.0110 0.0013  141 LEU C O   
5402 C  CB  . LEU C 140 ? 0.1062 0.1030 0.1003 -0.0001 -0.0143 -0.0076 141 LEU C CB  
5403 C  CG  . LEU C 140 ? 0.1224 0.1100 0.1186 0.0105  -0.0214 -0.0094 141 LEU C CG  
5404 C  CD1 . LEU C 140 ? 0.1577 0.1152 0.1323 0.0113  -0.0223 -0.0320 141 LEU C CD1 
5405 C  CD2 . LEU C 140 ? 0.1418 0.1313 0.1376 0.0102  -0.0225 -0.0141 141 LEU C CD2 
5406 N  N   . ALA C 141 ? 0.1010 0.0864 0.0974 -0.0068 0.0027  -0.0043 142 ALA C N   
5407 C  CA  . ALA C 141 ? 0.1152 0.0904 0.1067 -0.0136 -0.0097 0.0119  142 ALA C CA  
5408 C  C   . ALA C 141 ? 0.0903 0.1003 0.0926 0.0040  0.0044  -0.0041 142 ALA C C   
5409 O  O   . ALA C 141 ? 0.0992 0.0910 0.1243 0.0087  -0.0013 -0.0054 142 ALA C O   
5410 C  CB  . ALA C 141 ? 0.1221 0.1066 0.1102 0.0032  -0.0043 0.0120  142 ALA C CB  
5411 N  N   . VAL C 142 ? 0.1125 0.0829 0.0918 0.0043  -0.0032 0.0077  143 VAL C N   
5412 C  CA  . VAL C 142 ? 0.1174 0.0910 0.0920 -0.0120 0.0020  0.0063  143 VAL C CA  
5413 C  C   . VAL C 142 ? 0.0879 0.0850 0.0966 0.0000  -0.0166 0.0096  143 VAL C C   
5414 O  O   . VAL C 142 ? 0.1049 0.1005 0.1070 0.0074  -0.0174 0.0015  143 VAL C O   
5415 C  CB  . VAL C 142 ? 0.0944 0.0908 0.0895 0.0063  -0.0099 0.0086  143 VAL C CB  
5416 C  CG1 . VAL C 142 ? 0.0929 0.1003 0.1084 -0.0041 -0.0093 -0.0054 143 VAL C CG1 
5417 C  CG2 . VAL C 142 ? 0.1306 0.1059 0.0924 0.0105  -0.0068 0.0177  143 VAL C CG2 
5418 N  N   . LEU C 143 ? 0.1024 0.0878 0.0890 0.0059  -0.0020 0.0054  144 LEU C N   
5419 C  CA  . LEU C 143 ? 0.0988 0.0797 0.1204 0.0010  0.0137  0.0076  144 LEU C CA  
5420 C  C   . LEU C 143 ? 0.0746 0.0956 0.0886 0.0174  0.0034  0.0093  144 LEU C C   
5421 O  O   . LEU C 143 ? 0.1091 0.1032 0.1107 0.0031  -0.0153 0.0141  144 LEU C O   
5422 C  CB  . LEU C 143 ? 0.1452 0.1077 0.1267 -0.0026 0.0434  0.0031  144 LEU C CB  
5423 C  CG  . LEU C 143 ? 0.1428 0.1385 0.1111 -0.0043 0.0103  0.0065  144 LEU C CG  
5424 C  CD1 . LEU C 143 ? 0.1446 0.1438 0.1124 0.0234  0.0115  0.0147  144 LEU C CD1 
5425 C  CD2 . LEU C 143 ? 0.1511 0.1563 0.1269 0.0185  0.0281  0.0085  144 LEU C CD2 
5426 N  N   . GLY C 144 ? 0.1021 0.0719 0.0989 0.0146  0.0041  -0.0041 145 GLY C N   
5427 C  CA  . GLY C 144 ? 0.1141 0.0604 0.0987 0.0028  -0.0148 0.0140  145 GLY C CA  
5428 C  C   . GLY C 144 ? 0.0818 0.0839 0.0825 0.0193  -0.0024 0.0041  145 GLY C C   
5429 O  O   . GLY C 144 ? 0.1243 0.0895 0.1049 0.0046  -0.0179 0.0087  145 GLY C O   
5430 N  N   . ILE C 145 ? 0.0942 0.0790 0.1027 0.0007  0.0054  -0.0010 146 ILE C N   
5431 C  CA  . ILE C 145 ? 0.0978 0.0962 0.0997 -0.0115 0.0181  0.0020  146 ILE C CA  
5432 C  C   . ILE C 145 ? 0.0885 0.0966 0.0988 0.0054  -0.0071 0.0125  146 ILE C C   
5433 O  O   . ILE C 145 ? 0.1118 0.0888 0.0989 0.0035  -0.0057 0.0153  146 ILE C O   
5434 C  CB  . ILE C 145 ? 0.1136 0.1019 0.1023 0.0153  -0.0017 0.0019  146 ILE C CB  
5435 C  CG1 . ILE C 145 ? 0.1459 0.1111 0.1387 0.0081  0.0163  -0.0188 146 ILE C CG1 
5436 C  CG2 . ILE C 145 ? 0.1326 0.1371 0.1102 -0.0096 0.0344  -0.0008 146 ILE C CG2 
5437 C  CD1 . ILE C 145 ? 0.1414 0.1380 0.1475 0.0355  0.0156  0.0161  146 ILE C CD1 
5438 N  N   . PHE C 146 ? 0.0951 0.0899 0.0930 -0.0006 0.0087  0.0052  147 PHE C N   
5439 C  CA  . PHE C 146 ? 0.1021 0.0854 0.1077 0.0059  0.0052  0.0040  147 PHE C CA  
5440 C  C   . PHE C 146 ? 0.1100 0.0790 0.1005 0.0013  0.0183  0.0040  147 PHE C C   
5441 O  O   . PHE C 146 ? 0.1268 0.1093 0.0956 0.0052  0.0157  0.0030  147 PHE C O   
5442 C  CB  . PHE C 146 ? 0.0974 0.0913 0.1116 0.0092  0.0001  0.0043  147 PHE C CB  
5443 C  CG  . PHE C 146 ? 0.0866 0.0856 0.0967 0.0184  0.0163  -0.0035 147 PHE C CG  
5444 C  CD1 . PHE C 146 ? 0.0976 0.0903 0.0903 0.0109  0.0076  -0.0188 147 PHE C CD1 
5445 C  CD2 . PHE C 146 ? 0.1091 0.0807 0.1278 0.0263  0.0000  0.0100  147 PHE C CD2 
5446 C  CE1 . PHE C 146 ? 0.1066 0.0890 0.1164 0.0085  0.0060  0.0046  147 PHE C CE1 
5447 C  CE2 . PHE C 146 ? 0.1322 0.0899 0.1143 -0.0023 0.0020  0.0171  147 PHE C CE2 
5448 C  CZ  . PHE C 146 ? 0.1154 0.0843 0.1010 0.0193  0.0017  0.0153  147 PHE C CZ  
5449 N  N   . LEU C 147 ? 0.1026 0.1070 0.1037 -0.0020 -0.0068 0.0015  148 LEU C N   
5450 C  CA  . LEU C 147 ? 0.0886 0.0866 0.1080 0.0027  -0.0035 -0.0122 148 LEU C CA  
5451 C  C   . LEU C 147 ? 0.1154 0.1010 0.1206 0.0052  0.0130  0.0120  148 LEU C C   
5452 O  O   . LEU C 147 ? 0.1242 0.1036 0.1073 0.0159  0.0038  0.0043  148 LEU C O   
5453 C  CB  . LEU C 147 ? 0.1107 0.0988 0.1054 0.0148  -0.0083 -0.0041 148 LEU C CB  
5454 C  CG  . LEU C 147 ? 0.1387 0.0885 0.1215 0.0087  0.0096  0.0054  148 LEU C CG  
5455 C  CD1 . LEU C 147 ? 0.1270 0.1149 0.1572 -0.0126 -0.0020 0.0100  148 LEU C CD1 
5456 C  CD2 . LEU C 147 ? 0.1256 0.1335 0.1287 0.0065  0.0138  0.0081  148 LEU C CD2 
5457 N  N   . LYS C 148 ? 0.1233 0.0886 0.1130 -0.0143 0.0164  0.0017  149 LYS C N   
5458 C  CA  . LYS C 148 ? 0.1310 0.0809 0.1752 0.0043  0.0057  0.0098  149 LYS C CA  
5459 C  C   . LYS C 148 ? 0.1276 0.1240 0.1188 0.0131  0.0096  0.0006  149 LYS C C   
5460 O  O   . LYS C 148 ? 0.1186 0.1333 0.1588 0.0017  0.0159  -0.0212 149 LYS C O   
5461 C  CB  . LYS C 148 ? 0.1565 0.1347 0.1580 0.0219  0.0008  0.0175  149 LYS C CB  
5462 C  CG  . LYS C 148 ? 0.1633 0.1480 0.1594 0.0127  -0.0109 0.0060  149 LYS C CG  
5463 C  CD  . LYS C 148 ? 0.2515 0.2294 0.2253 0.0628  -0.0275 0.0320  149 LYS C CD  
5464 C  CE  . LYS C 148 ? 0.3537 0.3964 0.3120 0.0878  -0.0291 0.1412  149 LYS C CE  
5465 N  NZ  . LYS C 148 ? 0.5371 0.5853 0.4718 0.1172  -0.0337 0.1762  149 LYS C NZ  
5466 N  N   . VAL C 149 ? 0.1385 0.1028 0.1632 0.0044  0.0049  0.0041  150 VAL C N   
5467 C  CA  . VAL C 149 ? 0.1491 0.1307 0.1244 -0.0119 0.0193  -0.0122 150 VAL C CA  
5468 C  C   . VAL C 149 ? 0.1404 0.1344 0.1274 0.0192  0.0116  0.0138  150 VAL C C   
5469 O  O   . VAL C 149 ? 0.1466 0.1486 0.1761 0.0225  0.0108  0.0054  150 VAL C O   
5470 C  CB  . VAL C 149 ? 0.1391 0.1335 0.1347 -0.0089 0.0028  -0.0120 150 VAL C CB  
5471 C  CG1 . VAL C 149 ? 0.1427 0.1632 0.1718 -0.0186 -0.0114 -0.0217 150 VAL C CG1 
5472 C  CG2 . VAL C 149 ? 0.1824 0.1763 0.1709 -0.0417 0.0127  0.0140  150 VAL C CG2 
5473 N  N   . GLY C 150 ? 0.1288 0.1186 0.1279 -0.0040 0.0219  0.0091  151 GLY C N   
5474 C  CA  . GLY C 150 ? 0.1527 0.1405 0.1619 0.0239  0.0351  0.0590  151 GLY C CA  
5475 C  C   . GLY C 150 ? 0.1359 0.1267 0.1508 -0.0170 0.0233  0.0406  151 GLY C C   
5476 O  O   . GLY C 150 ? 0.1511 0.1342 0.1630 -0.0232 0.0142  0.0253  151 GLY C O   
5477 N  N   A SER C 151 ? 0.1599 0.1410 0.1590 -0.0043 0.0226  0.0288  152 SER C N   
5478 N  N   B SER C 151 ? 0.1565 0.1410 0.1603 -0.0131 0.0234  0.0266  152 SER C N   
5479 C  CA  A SER C 151 ? 0.1823 0.1321 0.1685 0.0214  0.0311  0.0100  152 SER C CA  
5480 C  CA  B SER C 151 ? 0.1914 0.1398 0.1684 0.0183  0.0303  -0.0024 152 SER C CA  
5481 C  C   A SER C 151 ? 0.1459 0.1251 0.1642 -0.0048 -0.0149 0.0006  152 SER C C   
5482 C  C   B SER C 151 ? 0.1450 0.1326 0.1998 -0.0065 0.0065  0.0015  152 SER C C   
5483 O  O   A SER C 151 ? 0.1504 0.1642 0.1240 0.0000  0.0250  0.0065  152 SER C O   
5484 O  O   B SER C 151 ? 0.1382 0.1590 0.1428 0.0040  0.0256  0.0027  152 SER C O   
5485 C  CB  A SER C 151 ? 0.2296 0.1975 0.1543 0.0160  0.0148  0.0226  152 SER C CB  
5486 C  CB  B SER C 151 ? 0.2157 0.1894 0.1480 -0.0219 0.0294  0.0013  152 SER C CB  
5487 O  OG  A SER C 151 ? 0.2165 0.2876 0.1796 -0.0006 0.0280  0.0372  152 SER C OG  
5488 O  OG  B SER C 151 ? 0.2813 0.2709 0.1569 0.0443  0.0253  0.0271  152 SER C OG  
5489 N  N   . ALA C 152 ? 0.1346 0.1404 0.1734 0.0089  0.0188  -0.0252 153 ALA C N   
5490 C  CA  . ALA C 152 ? 0.1350 0.1547 0.1578 -0.0062 0.0238  -0.0068 153 ALA C CA  
5491 C  C   . ALA C 152 ? 0.1299 0.1402 0.1303 0.0077  0.0043  -0.0023 153 ALA C C   
5492 O  O   . ALA C 152 ? 0.1976 0.1472 0.1504 -0.0057 0.0251  0.0085  153 ALA C O   
5493 C  CB  . ALA C 152 ? 0.1208 0.1739 0.2263 0.0055  0.0111  -0.0020 153 ALA C CB  
5494 N  N   . LYS C 153 ? 0.1492 0.1191 0.1685 0.0115  0.0234  -0.0013 154 LYS C N   
5495 C  CA  . LYS C 153 ? 0.1391 0.1369 0.1368 -0.0031 0.0220  0.0122  154 LYS C CA  
5496 C  C   . LYS C 153 ? 0.1515 0.1335 0.1383 -0.0159 0.0104  -0.0147 154 LYS C C   
5497 O  O   . LYS C 153 ? 0.1333 0.1331 0.1377 0.0098  0.0177  0.0054  154 LYS C O   
5498 C  CB  . LYS C 153 ? 0.1304 0.1412 0.1405 0.0115  0.0366  0.0080  154 LYS C CB  
5499 C  CG  . LYS C 153 ? 0.1729 0.1544 0.1711 0.0038  0.0114  -0.0130 154 LYS C CG  
5500 C  CD  . LYS C 153 ? 0.1581 0.1535 0.2003 -0.0215 -0.0295 0.0063  154 LYS C CD  
5501 C  CE  . LYS C 153 ? 0.2254 0.1441 0.2018 -0.0041 -0.0113 -0.0274 154 LYS C CE  
5502 N  NZ  . LYS C 153 ? 0.3504 0.3079 0.2353 -0.0274 -0.0421 0.0282  154 LYS C NZ  
5503 N  N   . PRO C 154 ? 0.1583 0.1719 0.1534 0.0065  0.0251  0.0236  155 PRO C N   
5504 C  CA  . PRO C 154 ? 0.1732 0.1762 0.1662 0.0080  0.0465  0.0017  155 PRO C CA  
5505 C  C   . PRO C 154 ? 0.1483 0.1725 0.1220 0.0218  0.0441  -0.0361 155 PRO C C   
5506 O  O   . PRO C 154 ? 0.1816 0.2030 0.1703 0.0317  0.0196  -0.0065 155 PRO C O   
5507 C  CB  . PRO C 154 ? 0.2199 0.1905 0.1701 -0.0024 0.0662  0.0216  155 PRO C CB  
5508 C  CG  . PRO C 154 ? 0.1829 0.2476 0.1969 0.0326  0.0619  0.0242  155 PRO C CG  
5509 C  CD  . PRO C 154 ? 0.1761 0.1644 0.1466 0.0381  0.0427  0.0348  155 PRO C CD  
5510 N  N   . GLY C 155 ? 0.1585 0.1395 0.1614 0.0073  0.0328  -0.0082 156 GLY C N   
5511 C  CA  . GLY C 155 ? 0.2131 0.1508 0.1490 -0.0041 0.0309  0.0060  156 GLY C CA  
5512 C  C   . GLY C 155 ? 0.1586 0.1375 0.1362 0.0013  0.0052  -0.0071 156 GLY C C   
5513 O  O   . GLY C 155 ? 0.2664 0.1526 0.2007 0.0324  0.0080  0.0066  156 GLY C O   
5514 N  N   . LEU C 156 ? 0.1269 0.1482 0.1197 0.0017  0.0168  -0.0010 157 LEU C N   
5515 C  CA  . LEU C 156 ? 0.1410 0.1179 0.1277 0.0273  0.0217  0.0193  157 LEU C CA  
5516 C  C   . LEU C 156 ? 0.1463 0.1225 0.1587 -0.0108 0.0236  0.0005  157 LEU C C   
5517 O  O   . LEU C 156 ? 0.1173 0.1333 0.1472 0.0057  0.0017  -0.0013 157 LEU C O   
5518 C  CB  . LEU C 156 ? 0.1231 0.1443 0.1565 0.0324  0.0219  0.0274  157 LEU C CB  
5519 C  CG  . LEU C 156 ? 0.1168 0.1419 0.1526 0.0107  0.0070  0.0137  157 LEU C CG  
5520 C  CD1 . LEU C 156 ? 0.1446 0.1683 0.1727 -0.0161 0.0163  0.0146  157 LEU C CD1 
5521 C  CD2 . LEU C 156 ? 0.1281 0.1886 0.1495 0.0165  0.0230  -0.0098 157 LEU C CD2 
5522 N  N   . GLN C 157 ? 0.1396 0.1412 0.1414 0.0003  0.0346  -0.0092 158 GLN C N   
5523 C  CA  . GLN C 157 ? 0.1439 0.1809 0.1700 -0.0070 0.0149  0.0368  158 GLN C CA  
5524 C  C   . GLN C 157 ? 0.1085 0.1468 0.1608 -0.0200 0.0131  0.0006  158 GLN C C   
5525 O  O   . GLN C 157 ? 0.1504 0.1423 0.1452 0.0031  0.0133  0.0051  158 GLN C O   
5526 C  CB  . GLN C 157 ? 0.1658 0.1737 0.1789 -0.0164 0.0612  0.0046  158 GLN C CB  
5527 C  CG  . GLN C 157 ? 0.1820 0.1852 0.2106 0.0146  0.0099  -0.0114 158 GLN C CG  
5528 C  CD  . GLN C 157 ? 0.1612 0.1856 0.1897 -0.0003 0.0187  -0.0105 158 GLN C CD  
5529 O  OE1 . GLN C 157 ? 0.1657 0.1542 0.2060 -0.0324 -0.0085 0.0132  158 GLN C OE1 
5530 N  NE2 . GLN C 157 ? 0.1623 0.1808 0.2109 -0.0275 -0.0031 0.0403  158 GLN C NE2 
5531 N  N   . LYS C 158 ? 0.1471 0.1729 0.1923 0.0126  0.0280  -0.0092 159 LYS C N   
5532 C  CA  . LYS C 158 ? 0.1443 0.1836 0.1868 0.0081  0.0215  0.0030  159 LYS C CA  
5533 C  C   . LYS C 158 ? 0.1450 0.1902 0.1879 0.0071  0.0035  -0.0013 159 LYS C C   
5534 O  O   . LYS C 158 ? 0.1349 0.1838 0.2088 0.0120  0.0119  0.0375  159 LYS C O   
5535 C  CB  . LYS C 158 ? 0.2257 0.1811 0.1917 0.0564  0.0232  0.0244  159 LYS C CB  
5536 C  CG  . LYS C 158 ? 0.3603 0.3330 0.2944 0.0505  0.1462  -0.0185 159 LYS C CG  
5537 C  CD  . LYS C 158 ? 0.4894 0.2797 0.5131 0.0956  0.1107  -0.0137 159 LYS C CD  
5538 C  CE  . LYS C 158 ? 0.4970 0.5141 0.5809 0.1834  0.1888  -0.0414 159 LYS C CE  
5539 N  NZ  . LYS C 158 ? 0.4878 0.3923 0.5108 0.1675  -0.0895 -0.0013 159 LYS C NZ  
5540 N  N   . VAL C 159 ? 0.1403 0.1560 0.1642 -0.0093 0.0125  -0.0046 160 VAL C N   
5541 C  CA  . VAL C 159 ? 0.1331 0.1456 0.1226 -0.0114 -0.0001 0.0086  160 VAL C CA  
5542 C  C   . VAL C 159 ? 0.1066 0.1550 0.1635 0.0100  -0.0027 0.0006  160 VAL C C   
5543 O  O   . VAL C 159 ? 0.1651 0.1585 0.1709 -0.0141 -0.0019 0.0265  160 VAL C O   
5544 C  CB  . VAL C 159 ? 0.1242 0.1393 0.1545 0.0060  -0.0003 0.0017  160 VAL C CB  
5545 C  CG1 . VAL C 159 ? 0.1394 0.1766 0.1550 -0.0285 0.0071  0.0133  160 VAL C CG1 
5546 C  CG2 . VAL C 159 ? 0.1678 0.1517 0.2337 -0.0248 0.0317  -0.0296 160 VAL C CG2 
5547 N  N   . VAL C 160 ? 0.1376 0.1249 0.1425 -0.0054 0.0138  0.0041  161 VAL C N   
5548 C  CA  . VAL C 160 ? 0.1868 0.1524 0.1845 0.0070  -0.0113 -0.0030 161 VAL C CA  
5549 C  C   . VAL C 160 ? 0.1762 0.1333 0.1601 -0.0165 -0.0041 0.0024  161 VAL C C   
5550 O  O   . VAL C 160 ? 0.1676 0.1705 0.1623 -0.0001 -0.0063 0.0175  161 VAL C O   
5551 C  CB  . VAL C 160 ? 0.2105 0.1378 0.2242 0.0153  -0.0337 -0.0194 161 VAL C CB  
5552 C  CG1 . VAL C 160 ? 0.2407 0.1641 0.2290 -0.0350 -0.0152 0.0063  161 VAL C CG1 
5553 C  CG2 . VAL C 160 ? 0.2176 0.1565 0.2904 0.0302  -0.0135 0.0007  161 VAL C CG2 
5554 N  N   . ASP C 161 ? 0.1328 0.1529 0.1644 -0.0383 -0.0102 0.0340  162 ASP C N   
5555 C  CA  . ASP C 161 ? 0.1429 0.1911 0.2339 -0.0160 -0.0043 0.0445  162 ASP C CA  
5556 C  C   . ASP C 161 ? 0.1515 0.2055 0.2391 -0.0216 -0.0443 0.0511  162 ASP C C   
5557 O  O   . ASP C 161 ? 0.2003 0.2856 0.2917 -0.0315 -0.0666 0.0432  162 ASP C O   
5558 C  CB  . ASP C 161 ? 0.1818 0.2829 0.2885 0.0211  -0.0015 0.0568  162 ASP C CB  
5559 C  CG  . ASP C 161 ? 0.1610 0.2671 0.2513 -0.0684 0.0000  -0.0017 162 ASP C CG  
5560 O  OD1 . ASP C 161 ? 0.2689 0.2872 0.3045 -0.0151 -0.0013 0.0241  162 ASP C OD1 
5561 O  OD2 . ASP C 161 ? 0.2296 0.2969 0.2481 -0.0065 0.0381  0.0076  162 ASP C OD2 
5562 N  N   . VAL C 162 ? 0.1613 0.1534 0.2253 0.0086  0.0127  0.0377  163 VAL C N   
5563 C  CA  . VAL C 162 ? 0.1813 0.1926 0.1613 -0.0172 -0.0046 0.0295  163 VAL C CA  
5564 C  C   . VAL C 162 ? 0.1295 0.1565 0.1702 0.0077  -0.0032 0.0148  163 VAL C C   
5565 O  O   . VAL C 162 ? 0.1527 0.1784 0.1953 -0.0027 -0.0324 0.0249  163 VAL C O   
5566 C  CB  . VAL C 162 ? 0.1698 0.1777 0.2060 0.0337  -0.0284 0.0066  163 VAL C CB  
5567 C  CG1 . VAL C 162 ? 0.1771 0.1462 0.2373 0.0116  -0.0104 0.0076  163 VAL C CG1 
5568 C  CG2 . VAL C 162 ? 0.1881 0.1917 0.2391 0.0403  -0.0637 0.0068  163 VAL C CG2 
5569 N  N   . LEU C 163 ? 0.1559 0.1867 0.1948 0.0199  0.0425  0.0160  164 LEU C N   
5570 C  CA  . LEU C 163 ? 0.1746 0.1605 0.1310 0.0007  -0.0043 0.0285  164 LEU C CA  
5571 C  C   . LEU C 163 ? 0.1856 0.1638 0.1840 -0.0005 -0.0256 -0.0048 164 LEU C C   
5572 O  O   . LEU C 163 ? 0.1637 0.2030 0.1762 0.0176  -0.0276 0.0071  164 LEU C O   
5573 C  CB  . LEU C 163 ? 0.1705 0.1465 0.1630 -0.0012 -0.0219 -0.0289 164 LEU C CB  
5574 C  CG  . LEU C 163 ? 0.1199 0.1597 0.1741 0.0055  -0.0252 0.0160  164 LEU C CG  
5575 C  CD1 . LEU C 163 ? 0.1788 0.1797 0.1808 0.0432  -0.0027 0.0151  164 LEU C CD1 
5576 C  CD2 . LEU C 163 ? 0.1323 0.1736 0.1833 -0.0383 -0.0315 -0.0006 164 LEU C CD2 
5577 N  N   . ASP C 164 ? 0.2009 0.1854 0.2026 -0.0078 -0.0430 0.0109  165 ASP C N   
5578 C  CA  . ASP C 164 ? 0.2023 0.2346 0.2316 -0.0417 -0.0460 0.0230  165 ASP C CA  
5579 C  C   . ASP C 164 ? 0.2012 0.2646 0.2477 0.0059  -0.0671 -0.0209 165 ASP C C   
5580 O  O   . ASP C 164 ? 0.2870 0.2984 0.2696 -0.0020 -0.1132 -0.0060 165 ASP C O   
5581 C  CB  . ASP C 164 ? 0.2314 0.2707 0.3454 -0.0798 -0.0599 0.0666  165 ASP C CB  
5582 C  CG  . ASP C 164 ? 0.1899 0.5066 0.3675 -0.0153 -0.1198 0.0825  165 ASP C CG  
5583 O  OD1 . ASP C 164 ? 0.4731 0.5274 0.4861 -0.0362 -0.0073 0.0239  165 ASP C OD1 
5584 O  OD2 . ASP C 164 ? 0.6302 1.2659 0.6482 -0.4731 -0.0901 0.1286  165 ASP C OD2 
5585 N  N   . SER C 165 ? 0.1438 0.1972 0.2136 0.0186  -0.0099 0.0232  166 SER C N   
5586 C  CA  . SER C 165 ? 0.1737 0.2039 0.2149 0.0098  -0.0104 0.0395  166 SER C CA  
5587 C  C   . SER C 165 ? 0.1432 0.1921 0.2206 0.0211  -0.0222 0.0305  166 SER C C   
5588 O  O   . SER C 165 ? 0.1612 0.2169 0.2093 0.0003  -0.0281 0.0416  166 SER C O   
5589 C  CB  . SER C 165 ? 0.3012 0.2343 0.2361 0.0781  -0.1058 0.0063  166 SER C CB  
5590 O  OG  . SER C 165 ? 0.2493 0.2436 0.2637 0.0315  -0.0337 0.0065  166 SER C OG  
5591 N  N   . ILE C 166 ? 0.1075 0.1753 0.2099 -0.0006 -0.0108 0.0164  167 ILE C N   
5592 C  CA  . ILE C 166 ? 0.1757 0.1400 0.1592 0.0104  -0.0152 0.0179  167 ILE C CA  
5593 C  C   . ILE C 166 ? 0.1466 0.1525 0.1263 -0.0181 0.0012  0.0003  167 ILE C C   
5594 O  O   . ILE C 166 ? 0.1475 0.1829 0.1466 -0.0020 -0.0278 0.0179  167 ILE C O   
5595 C  CB  . ILE C 166 ? 0.1784 0.1450 0.1737 0.0099  -0.0368 0.0060  167 ILE C CB  
5596 C  CG1 . ILE C 166 ? 0.1032 0.1630 0.1678 -0.0019 -0.0206 0.0362  167 ILE C CG1 
5597 C  CG2 . ILE C 166 ? 0.1559 0.1624 0.2032 0.0186  0.0194  0.0078  167 ILE C CG2 
5598 C  CD1 . ILE C 166 ? 0.1622 0.1368 0.1905 -0.0184 -0.0482 0.0092  167 ILE C CD1 
5599 N  N   . LYS C 167 ? 0.1572 0.1647 0.1705 -0.0115 -0.0201 0.0055  168 LYS C N   
5600 C  CA  . LYS C 167 ? 0.1432 0.1599 0.1506 -0.0137 -0.0196 0.0015  168 LYS C CA  
5601 C  C   . LYS C 167 ? 0.1825 0.1811 0.1518 -0.0037 -0.0098 0.0074  168 LYS C C   
5602 O  O   . LYS C 167 ? 0.1438 0.1641 0.1787 0.0000  -0.0132 0.0198  168 LYS C O   
5603 C  CB  . LYS C 167 ? 0.1805 0.1748 0.2203 -0.0577 -0.0401 0.0017  168 LYS C CB  
5604 C  CG  . LYS C 167 ? 0.2228 0.2048 0.2197 -0.0348 -0.0281 -0.0417 168 LYS C CG  
5605 C  CD  . LYS C 167 ? 0.2561 0.2721 0.3215 -0.0527 -0.0137 -0.0895 168 LYS C CD  
5606 C  CE  . LYS C 167 ? 0.2971 0.3553 0.4513 -0.0239 -0.0065 -0.1436 168 LYS C CE  
5607 N  NZ  . LYS C 167 ? 0.4605 0.3889 0.4250 -0.0986 -0.1585 -0.0803 168 LYS C NZ  
5608 N  N   . THR C 168 ? 0.1835 0.1762 0.1603 0.0098  -0.0164 0.0133  169 THR C N   
5609 C  CA  . THR C 168 ? 0.1881 0.1791 0.1429 -0.0077 -0.0403 0.0216  169 THR C CA  
5610 C  C   . THR C 168 ? 0.1630 0.1709 0.1540 0.0071  -0.0228 -0.0086 169 THR C C   
5611 O  O   . THR C 168 ? 0.1619 0.1723 0.1648 0.0178  -0.0423 0.0250  169 THR C O   
5612 C  CB  . THR C 168 ? 0.1601 0.1745 0.1937 0.0148  -0.0597 0.0003  169 THR C CB  
5613 O  OG1 . THR C 168 ? 0.1649 0.2274 0.1878 0.0232  -0.0584 0.0143  169 THR C OG1 
5614 C  CG2 . THR C 168 ? 0.1994 0.1850 0.1773 -0.0104 -0.0628 -0.0250 169 THR C CG2 
5615 N  N   . LYS C 169 ? 0.1353 0.2152 0.1509 -0.0109 -0.0535 0.0291  170 LYS C N   
5616 C  CA  . LYS C 169 ? 0.2055 0.1762 0.1337 0.0103  -0.0147 0.0013  170 LYS C CA  
5617 C  C   . LYS C 169 ? 0.1931 0.1845 0.1687 0.0166  -0.0456 0.0218  170 LYS C C   
5618 O  O   . LYS C 169 ? 0.2188 0.2703 0.1944 -0.0229 -0.0631 0.0679  170 LYS C O   
5619 C  CB  . LYS C 169 ? 0.1964 0.2059 0.1292 0.0006  -0.0087 0.0038  170 LYS C CB  
5620 C  CG  . LYS C 169 ? 0.2220 0.2210 0.1843 -0.0048 -0.0059 0.0425  170 LYS C CG  
5621 C  CD  . LYS C 169 ? 0.2502 0.2278 0.2028 -0.0197 -0.0212 0.0346  170 LYS C CD  
5622 C  CE  . LYS C 169 ? 0.3434 0.3021 0.2291 0.0198  0.0109  0.0219  170 LYS C CE  
5623 N  NZ  . LYS C 169 ? 0.4697 0.7052 0.3910 -0.0170 0.1010  0.1266  170 LYS C NZ  
5624 N  N   . GLY C 170 ? 0.1960 0.1601 0.2041 0.0201  -0.0278 0.0632  171 GLY C N   
5625 C  CA  . GLY C 170 ? 0.2269 0.1691 0.1466 0.0513  0.0052  0.0548  171 GLY C CA  
5626 C  C   . GLY C 170 ? 0.1964 0.1976 0.2563 0.0267  -0.0151 0.0048  171 GLY C C   
5627 O  O   . GLY C 170 ? 0.2714 0.1940 0.2588 0.0617  0.0186  0.0505  171 GLY C O   
5628 N  N   . LYS C 171 ? 0.1888 0.1493 0.1427 0.0333  -0.0024 0.0261  172 LYS C N   
5629 C  CA  . LYS C 171 ? 0.1606 0.2025 0.1608 0.0010  -0.0318 0.0573  172 LYS C CA  
5630 C  C   . LYS C 171 ? 0.1321 0.1753 0.1996 -0.0013 -0.0185 0.0040  172 LYS C C   
5631 O  O   . LYS C 171 ? 0.1425 0.1612 0.1538 0.0186  -0.0186 0.0168  172 LYS C O   
5632 C  CB  . LYS C 171 ? 0.1924 0.2059 0.1852 -0.0059 -0.0212 0.0337  172 LYS C CB  
5633 C  CG  . LYS C 171 ? 0.2822 0.1984 0.2023 -0.0309 -0.0035 -0.0041 172 LYS C CG  
5634 C  CD  . LYS C 171 ? 0.2813 0.2565 0.3980 -0.0375 0.0254  0.0147  172 LYS C CD  
5635 C  CE  . LYS C 171 ? 0.3653 0.4714 0.3592 -0.0148 0.0610  0.0728  172 LYS C CE  
5636 N  NZ  . LYS C 171 ? 0.3680 0.3510 0.4593 -0.0136 -0.1310 0.0114  172 LYS C NZ  
5637 N  N   . SER C 172 ? 0.1748 0.1732 0.1527 0.0491  -0.0168 0.0423  173 SER C N   
5638 C  CA  . SER C 172 ? 0.1854 0.2145 0.1635 0.0007  -0.0190 0.0399  173 SER C CA  
5639 C  C   . SER C 172 ? 0.1353 0.1784 0.1608 0.0194  -0.0414 0.0206  173 SER C C   
5640 O  O   . SER C 172 ? 0.1310 0.2405 0.2123 0.0317  -0.0631 -0.0086 173 SER C O   
5641 C  CB  . SER C 172 ? 0.1606 0.1748 0.2125 0.0324  -0.0116 0.0249  173 SER C CB  
5642 O  OG  . SER C 172 ? 0.2172 0.2278 0.3231 0.0636  -0.0452 0.0337  173 SER C OG  
5643 N  N   . ALA C 173 ? 0.1620 0.2181 0.1887 0.0013  -0.0260 -0.0273 174 ALA C N   
5644 C  CA  . ALA C 173 ? 0.1427 0.2260 0.1759 0.0149  -0.0165 -0.0063 174 ALA C CA  
5645 C  C   . ALA C 173 ? 0.1588 0.2314 0.2002 0.0199  0.0003  -0.0408 174 ALA C C   
5646 O  O   . ALA C 173 ? 0.1280 0.2102 0.2052 0.0386  -0.0013 -0.0130 174 ALA C O   
5647 C  CB  . ALA C 173 ? 0.1976 0.1962 0.3079 -0.0115 -0.0041 -0.0401 174 ALA C CB  
5648 N  N   . ASP C 174 ? 0.1642 0.2124 0.1717 0.0491  0.0031  0.0037  175 ASP C N   
5649 C  CA  . ASP C 174 ? 0.1653 0.2418 0.2147 0.0610  -0.0049 -0.0329 175 ASP C CA  
5650 C  C   . ASP C 174 ? 0.2215 0.2238 0.2592 0.0185  -0.0285 -0.0081 175 ASP C C   
5651 O  O   . ASP C 174 ? 0.2069 0.2477 0.2518 0.0034  -0.0373 -0.0078 175 ASP C O   
5652 C  CB  . ASP C 174 ? 0.2197 0.2637 0.2684 0.1136  0.0296  -0.0392 175 ASP C CB  
5653 C  CG  . ASP C 174 ? 0.3007 0.3718 0.4668 0.0772  -0.0127 0.0653  175 ASP C CG  
5654 O  OD1 . ASP C 174 ? 0.2694 0.4305 0.5537 -0.0137 -0.0078 0.0566  175 ASP C OD1 
5655 O  OD2 . ASP C 174 ? 0.2921 0.4779 0.3501 0.0516  -0.0076 0.0102  175 ASP C OD2 
5656 N  N   . PHE C 175 ? 0.1630 0.1739 0.1716 0.0162  -0.0060 0.0073  176 PHE C N   
5657 C  CA  . PHE C 175 ? 0.1687 0.1948 0.2068 0.0812  -0.0322 -0.0092 176 PHE C CA  
5658 C  C   . PHE C 175 ? 0.2091 0.1782 0.2075 0.0027  0.0206  -0.0003 176 PHE C C   
5659 O  O   . PHE C 175 ? 0.1735 0.2361 0.2157 0.0207  0.0068  -0.0167 176 PHE C O   
5660 C  CB  . PHE C 175 ? 0.1647 0.1509 0.2210 0.0452  -0.0006 0.0099  176 PHE C CB  
5661 C  CG  . PHE C 175 ? 0.1734 0.1502 0.1841 0.0082  0.0138  -0.0173 176 PHE C CG  
5662 C  CD1 . PHE C 175 ? 0.1814 0.1642 0.1906 -0.0066 -0.0286 0.0164  176 PHE C CD1 
5663 C  CD2 . PHE C 175 ? 0.2039 0.1971 0.1707 0.0507  0.0049  0.0170  176 PHE C CD2 
5664 C  CE1 . PHE C 175 ? 0.2053 0.1570 0.2366 0.0003  -0.0260 0.0175  176 PHE C CE1 
5665 C  CE2 . PHE C 175 ? 0.1973 0.1396 0.2330 0.0234  -0.0080 0.0035  176 PHE C CE2 
5666 C  CZ  . PHE C 175 ? 0.2005 0.1653 0.1824 0.0148  -0.0027 -0.0097 176 PHE C CZ  
5667 N  N   . THR C 176 ? 0.1750 0.2011 0.2204 0.0225  -0.0194 -0.0216 177 THR C N   
5668 C  CA  . THR C 176 ? 0.1793 0.1675 0.2009 0.0511  -0.0104 -0.0043 177 THR C CA  
5669 C  C   . THR C 176 ? 0.1093 0.1498 0.1570 0.0252  0.0111  -0.0115 177 THR C C   
5670 O  O   . THR C 176 ? 0.1261 0.1547 0.2168 0.0297  -0.0124 0.0091  177 THR C O   
5671 C  CB  . THR C 176 ? 0.1599 0.2120 0.2219 0.0494  0.0412  0.0063  177 THR C CB  
5672 O  OG1 . THR C 176 ? 0.1777 0.2176 0.3655 0.0493  -0.0040 -0.0214 177 THR C OG1 
5673 C  CG2 . THR C 176 ? 0.2594 0.2327 0.2488 0.1189  0.0172  0.0285  177 THR C CG2 
5674 N  N   . ASN C 177 ? 0.1247 0.1588 0.1782 0.0296  -0.0085 -0.0085 178 ASN C N   
5675 C  CA  . ASN C 177 ? 0.1563 0.1692 0.1965 0.0271  0.0263  0.0060  178 ASN C CA  
5676 C  C   . ASN C 177 ? 0.1563 0.2057 0.2084 0.0403  0.0140  0.0300  178 ASN C C   
5677 O  O   . ASN C 177 ? 0.2082 0.2177 0.2653 0.0657  0.0658  0.0324  178 ASN C O   
5678 C  CB  . ASN C 177 ? 0.1815 0.1735 0.2434 0.0427  0.0608  0.0226  178 ASN C CB  
5679 C  CG  . ASN C 177 ? 0.1985 0.1926 0.2558 0.0494  0.0127  -0.0130 178 ASN C CG  
5680 O  OD1 . ASN C 177 ? 0.2363 0.2177 0.2603 0.0491  0.0154  -0.0074 178 ASN C OD1 
5681 N  ND2 . ASN C 177 ? 0.1588 0.2258 0.2384 0.0524  0.0205  -0.0143 178 ASN C ND2 
5682 N  N   . PHE C 178 ? 0.1326 0.1414 0.1971 0.0346  -0.0017 0.0114  179 PHE C N   
5683 C  CA  . PHE C 178 ? 0.1251 0.1313 0.1678 0.0285  -0.0076 0.0182  179 PHE C CA  
5684 C  C   . PHE C 178 ? 0.1152 0.1588 0.1588 0.0209  0.0289  0.0065  179 PHE C C   
5685 O  O   . PHE C 178 ? 0.1405 0.1435 0.2226 0.0214  0.0065  0.0230  179 PHE C O   
5686 C  CB  . PHE C 178 ? 0.1630 0.1434 0.1718 0.0526  -0.0100 0.0171  179 PHE C CB  
5687 C  CG  . PHE C 178 ? 0.1346 0.1365 0.1737 0.0294  0.0093  0.0181  179 PHE C CG  
5688 C  CD1 . PHE C 178 ? 0.1763 0.1396 0.1856 0.0329  0.0166  -0.0186 179 PHE C CD1 
5689 C  CD2 . PHE C 178 ? 0.1346 0.1429 0.1444 0.0260  0.0244  0.0229  179 PHE C CD2 
5690 C  CE1 . PHE C 178 ? 0.1563 0.1402 0.2384 0.0197  -0.0204 0.0207  179 PHE C CE1 
5691 C  CE2 . PHE C 178 ? 0.1592 0.1599 0.1567 0.0274  -0.0010 0.0310  179 PHE C CE2 
5692 C  CZ  . PHE C 178 ? 0.1337 0.1529 0.1795 0.0283  -0.0114 0.0074  179 PHE C CZ  
5693 N  N   . ASP C 179 ? 0.1177 0.1620 0.1745 0.0263  0.0066  0.0017  180 ASP C N   
5694 C  CA  . ASP C 179 ? 0.1307 0.1533 0.1484 0.0217  0.0081  -0.0137 180 ASP C CA  
5695 C  C   . ASP C 179 ? 0.1425 0.1328 0.1541 0.0126  -0.0001 -0.0130 180 ASP C C   
5696 O  O   . ASP C 179 ? 0.1567 0.1385 0.1547 0.0136  0.0153  0.0074  180 ASP C O   
5697 C  CB  . ASP C 179 ? 0.1796 0.1904 0.1523 0.0425  0.0240  -0.0142 180 ASP C CB  
5698 C  CG  . ASP C 179 ? 0.1908 0.2142 0.1879 0.0226  0.0335  -0.0445 180 ASP C CG  
5699 O  OD1 . ASP C 179 ? 0.2107 0.1835 0.1759 0.0373  0.0241  -0.0210 180 ASP C OD1 
5700 O  OD2 . ASP C 179 ? 0.2829 0.3813 0.2048 0.0211  0.0700  -0.0291 180 ASP C OD2 
5701 N  N   . PRO C 180 ? 0.1497 0.1342 0.1448 0.0082  0.0138  -0.0092 181 PRO C N   
5702 C  CA  . PRO C 180 ? 0.1462 0.1908 0.1350 0.0237  0.0144  0.0160  181 PRO C CA  
5703 C  C   . PRO C 180 ? 0.1280 0.1489 0.1145 -0.0020 0.0187  0.0071  181 PRO C C   
5704 O  O   . PRO C 180 ? 0.1425 0.1398 0.1430 0.0164  0.0233  0.0076  181 PRO C O   
5705 C  CB  . PRO C 180 ? 0.1480 0.1796 0.1617 0.0052  0.0154  -0.0071 181 PRO C CB  
5706 C  CG  . PRO C 180 ? 0.1538 0.1572 0.2098 0.0186  -0.0113 0.0189  181 PRO C CG  
5707 C  CD  . PRO C 180 ? 0.1500 0.1386 0.1976 0.0182  0.0443  0.0136  181 PRO C CD  
5708 N  N   . ARG C 181 ? 0.1527 0.1538 0.1159 0.0077  0.0234  0.0066  182 ARG C N   
5709 C  CA  . ARG C 181 ? 0.1755 0.1412 0.1193 0.0189  0.0093  -0.0212 182 ARG C CA  
5710 C  C   . ARG C 181 ? 0.1421 0.1682 0.1418 0.0107  0.0364  0.0076  182 ARG C C   
5711 O  O   . ARG C 181 ? 0.1829 0.1526 0.1348 0.0193  0.0255  0.0007  182 ARG C O   
5712 C  CB  . ARG C 181 ? 0.1815 0.1547 0.1289 0.0237  0.0274  -0.0307 182 ARG C CB  
5713 C  CG  . ARG C 181 ? 0.2300 0.1498 0.1511 0.0035  0.0032  -0.0080 182 ARG C CG  
5714 C  CD  . ARG C 181 ? 0.2427 0.1872 0.1836 0.0086  0.0218  -0.0114 182 ARG C CD  
5715 N  NE  . ARG C 181 ? 0.2260 0.2064 0.1748 0.0379  0.0258  0.0065  182 ARG C NE  
5716 C  CZ  . ARG C 181 ? 0.2545 0.2529 0.2231 0.0220  0.0110  -0.0491 182 ARG C CZ  
5717 N  NH1 . ARG C 181 ? 0.3876 0.2500 0.2050 0.0340  -0.0399 -0.0233 182 ARG C NH1 
5718 N  NH2 . ARG C 181 ? 0.3073 0.2750 0.2360 0.0909  0.0000  -0.0167 182 ARG C NH2 
5719 N  N   . GLY C 182 ? 0.1596 0.1347 0.1669 0.0057  0.0219  -0.0227 183 GLY C N   
5720 C  CA  . GLY C 182 ? 0.1642 0.1356 0.2149 0.0176  0.0212  -0.0355 183 GLY C CA  
5721 C  C   . GLY C 182 ? 0.1527 0.1653 0.1396 -0.0073 0.0154  -0.0284 183 GLY C C   
5722 O  O   . GLY C 182 ? 0.1665 0.1529 0.2073 0.0118  0.0342  -0.0038 183 GLY C O   
5723 N  N   . LEU C 183 ? 0.1177 0.1412 0.1488 0.0244  0.0304  -0.0017 184 LEU C N   
5724 C  CA  . LEU C 183 ? 0.1484 0.1409 0.1594 0.0377  0.0284  0.0010  184 LEU C CA  
5725 C  C   . LEU C 183 ? 0.1369 0.1500 0.1437 0.0003  0.0227  -0.0109 184 LEU C C   
5726 O  O   . LEU C 183 ? 0.1648 0.1682 0.1351 0.0342  0.0152  0.0017  184 LEU C O   
5727 C  CB  . LEU C 183 ? 0.1347 0.1716 0.1094 0.0394  0.0113  -0.0157 184 LEU C CB  
5728 C  CG  . LEU C 183 ? 0.1154 0.1587 0.1337 0.0190  0.0184  -0.0083 184 LEU C CG  
5729 C  CD1 . LEU C 183 ? 0.1328 0.1879 0.1522 0.0535  0.0212  0.0126  184 LEU C CD1 
5730 C  CD2 . LEU C 183 ? 0.2005 0.1646 0.2017 0.0065  -0.0080 -0.0228 184 LEU C CD2 
5731 N  N   . LEU C 184 ? 0.1730 0.1470 0.1384 0.0175  0.0080  0.0013  185 LEU C N   
5732 C  CA  . LEU C 184 ? 0.1515 0.1450 0.1289 -0.0010 0.0237  0.0164  185 LEU C CA  
5733 C  C   . LEU C 184 ? 0.1199 0.1578 0.1660 0.0130  -0.0032 0.0326  185 LEU C C   
5734 O  O   . LEU C 184 ? 0.1683 0.2012 0.1714 0.0359  0.0342  0.0375  185 LEU C O   
5735 C  CB  . LEU C 184 ? 0.1423 0.1471 0.1344 0.0013  0.0027  0.0048  185 LEU C CB  
5736 C  CG  . LEU C 184 ? 0.1624 0.1342 0.1427 0.0271  0.0242  -0.0097 185 LEU C CG  
5737 C  CD1 . LEU C 184 ? 0.2039 0.1906 0.1371 0.0351  0.0015  -0.0275 185 LEU C CD1 
5738 C  CD2 . LEU C 184 ? 0.1708 0.1721 0.1445 0.0034  0.0261  -0.0006 185 LEU C CD2 
5739 N  N   . PRO C 185 ? 0.1527 0.1480 0.1356 0.0271  0.0212  0.0077  186 PRO C N   
5740 C  CA  . PRO C 185 ? 0.1613 0.1438 0.1106 0.0346  0.0219  -0.0130 186 PRO C CA  
5741 C  C   . PRO C 185 ? 0.1849 0.1344 0.1159 0.0310  0.0359  0.0100  186 PRO C C   
5742 O  O   . PRO C 185 ? 0.2060 0.1472 0.1191 0.0272  0.0458  0.0017  186 PRO C O   
5743 C  CB  . PRO C 185 ? 0.1506 0.1447 0.1070 0.0270  0.0233  -0.0051 186 PRO C CB  
5744 C  CG  . PRO C 185 ? 0.1489 0.1281 0.1534 0.0270  0.0197  -0.0186 186 PRO C CG  
5745 C  CD  . PRO C 185 ? 0.1283 0.1558 0.1238 0.0055  0.0065  -0.0041 186 PRO C CD  
5746 N  N   . GLU C 186 ? 0.1635 0.1348 0.1307 0.0171  0.0219  0.0204  187 GLU C N   
5747 C  CA  . GLU C 186 ? 0.1861 0.1802 0.0930 0.0329  0.0131  0.0102  187 GLU C CA  
5748 C  C   . GLU C 186 ? 0.2138 0.1580 0.1204 0.0228  0.0130  0.0259  187 GLU C C   
5749 O  O   . GLU C 186 ? 0.2863 0.2109 0.1647 0.0155  0.0571  -0.0262 187 GLU C O   
5750 C  CB  . GLU C 186 ? 0.2635 0.1739 0.2185 -0.0184 0.0728  0.0601  187 GLU C CB  
5751 C  CG  . GLU C 186 ? 0.3195 0.2341 0.2723 -0.0439 0.0432  0.0513  187 GLU C CG  
5752 C  CD  . GLU C 186 ? 0.2251 0.2563 0.1933 0.0044  0.0153  0.0318  187 GLU C CD  
5753 O  OE1 . GLU C 186 ? 0.2811 0.2980 0.2418 0.0381  0.0141  0.1004  187 GLU C OE1 
5754 O  OE2 . GLU C 186 ? 0.3165 0.3111 0.3068 -0.0593 0.0309  -0.0010 187 GLU C OE2 
5755 N  N   . SER C 187 ? 0.1923 0.2039 0.1326 0.0230  0.0286  0.0188  188 SER C N   
5756 C  CA  . SER C 187 ? 0.2402 0.1665 0.1543 0.0397  0.0197  0.0175  188 SER C CA  
5757 C  C   . SER C 187 ? 0.2249 0.1817 0.1301 -0.0017 0.0337  0.0126  188 SER C C   
5758 O  O   . SER C 187 ? 0.2292 0.1754 0.1592 0.0103  -0.0041 -0.0178 188 SER C O   
5759 C  CB  . SER C 187 ? 0.1815 0.2023 0.1396 0.0397  -0.0114 0.0008  188 SER C CB  
5760 O  OG  . SER C 187 ? 0.2190 0.2125 0.1693 0.0083  0.0066  0.0307  188 SER C OG  
5761 N  N   . LEU C 188 ? 0.2023 0.1696 0.1097 -0.0010 0.0296  0.0010  189 LEU C N   
5762 C  CA  . LEU C 188 ? 0.2059 0.1492 0.1419 -0.0102 0.0275  -0.0020 189 LEU C CA  
5763 C  C   . LEU C 188 ? 0.1993 0.1682 0.0964 -0.0032 -0.0103 -0.0250 189 LEU C C   
5764 O  O   . LEU C 188 ? 0.2248 0.2064 0.1678 -0.0175 0.0081  0.0147  189 LEU C O   
5765 C  CB  . LEU C 188 ? 0.2964 0.1644 0.2142 -0.0063 0.0185  -0.0120 189 LEU C CB  
5766 C  CG  . LEU C 188 ? 0.3055 0.1890 0.1502 0.0247  0.0381  -0.0001 189 LEU C CG  
5767 C  CD1 . LEU C 188 ? 0.3919 0.1793 0.2561 0.0430  0.1231  -0.0038 189 LEU C CD1 
5768 C  CD2 . LEU C 188 ? 0.2867 0.2449 0.1789 0.0137  0.0249  0.0001  189 LEU C CD2 
5769 N  N   . ASP C 189 ? 0.2116 0.1834 0.1032 0.0337  -0.0119 -0.0082 190 ASP C N   
5770 C  CA  . ASP C 189 ? 0.2308 0.1953 0.0983 0.0068  0.0280  0.0186  190 ASP C CA  
5771 C  C   . ASP C 189 ? 0.1448 0.1285 0.1097 0.0010  0.0207  0.0003  190 ASP C C   
5772 O  O   . ASP C 189 ? 0.1800 0.1457 0.1105 -0.0073 0.0086  -0.0012 190 ASP C O   
5773 C  CB  . ASP C 189 ? 0.1896 0.2199 0.1710 0.0146  -0.0264 0.0560  190 ASP C CB  
5774 C  CG  . ASP C 189 ? 0.3152 0.2770 0.1973 -0.0103 -0.0263 0.0241  190 ASP C CG  
5775 O  OD1 . ASP C 189 ? 0.3682 0.4277 0.1523 -0.0119 -0.0428 -0.0049 190 ASP C OD1 
5776 O  OD2 . ASP C 189 ? 0.3337 0.4492 0.2878 0.0162  -0.0236 0.1704  190 ASP C OD2 
5777 N  N   . TYR C 190 ? 0.1409 0.1438 0.1057 0.0012  -0.0168 0.0217  191 TYR C N   
5778 C  CA  . TYR C 190 ? 0.1500 0.1289 0.1012 0.0099  -0.0006 0.0351  191 TYR C CA  
5779 C  C   . TYR C 190 ? 0.1313 0.1446 0.1288 0.0013  -0.0293 0.0146  191 TYR C C   
5780 O  O   . TYR C 190 ? 0.1411 0.1470 0.1142 0.0044  -0.0299 0.0142  191 TYR C O   
5781 C  CB  . TYR C 190 ? 0.1653 0.1193 0.1450 0.0000  -0.0245 0.0263  191 TYR C CB  
5782 C  CG  . TYR C 190 ? 0.1513 0.1242 0.1360 0.0175  -0.0129 0.0277  191 TYR C CG  
5783 C  CD1 . TYR C 190 ? 0.1346 0.1611 0.1423 0.0099  -0.0177 0.0120  191 TYR C CD1 
5784 C  CD2 . TYR C 190 ? 0.1518 0.1402 0.1495 0.0210  -0.0458 0.0038  191 TYR C CD2 
5785 C  CE1 . TYR C 190 ? 0.1723 0.1358 0.1601 -0.0179 0.0026  0.0148  191 TYR C CE1 
5786 C  CE2 . TYR C 190 ? 0.1878 0.1450 0.1728 0.0017  -0.0274 0.0111  191 TYR C CE2 
5787 C  CZ  . TYR C 190 ? 0.1563 0.1766 0.1649 0.0074  -0.0480 0.0054  191 TYR C CZ  
5788 O  OH  . TYR C 190 ? 0.2113 0.1541 0.2125 0.0020  -0.0529 -0.0038 191 TYR C OH  
5789 N  N   . TRP C 191 ? 0.1150 0.0942 0.1161 0.0081  -0.0122 0.0093  192 TRP C N   
5790 C  CA  . TRP C 191 ? 0.1274 0.1138 0.1066 0.0262  -0.0030 0.0094  192 TRP C CA  
5791 C  C   . TRP C 191 ? 0.1067 0.1042 0.1170 0.0063  -0.0185 -0.0027 192 TRP C C   
5792 O  O   . TRP C 191 ? 0.1036 0.1261 0.1454 0.0000  -0.0241 0.0113  192 TRP C O   
5793 C  CB  . TRP C 191 ? 0.1324 0.1220 0.1355 0.0074  -0.0138 0.0063  192 TRP C CB  
5794 C  CG  . TRP C 191 ? 0.1172 0.1145 0.1204 0.0144  -0.0196 -0.0060 192 TRP C CG  
5795 C  CD1 . TRP C 191 ? 0.1164 0.1247 0.1286 0.0059  -0.0172 0.0008  192 TRP C CD1 
5796 C  CD2 . TRP C 191 ? 0.1348 0.1278 0.1163 0.0076  0.0028  -0.0119 192 TRP C CD2 
5797 N  NE1 . TRP C 191 ? 0.1802 0.1238 0.1552 0.0284  -0.0148 0.0052  192 TRP C NE1 
5798 C  CE2 . TRP C 191 ? 0.1601 0.1176 0.1560 0.0057  0.0130  -0.0010 192 TRP C CE2 
5799 C  CE3 . TRP C 191 ? 0.1362 0.1405 0.1359 0.0040  0.0154  -0.0200 192 TRP C CE3 
5800 C  CZ2 . TRP C 191 ? 0.1436 0.1215 0.1459 0.0148  0.0207  -0.0006 192 TRP C CZ2 
5801 C  CZ3 . TRP C 191 ? 0.1865 0.1552 0.1114 -0.0131 -0.0052 -0.0071 192 TRP C CZ3 
5802 C  CH2 . TRP C 191 ? 0.1626 0.1520 0.1571 -0.0007 0.0175  -0.0309 192 TRP C CH2 
5803 N  N   . THR C 192 ? 0.1305 0.0994 0.1123 0.0001  -0.0057 0.0105  193 THR C N   
5804 C  CA  . THR C 192 ? 0.1030 0.1132 0.1102 0.0080  -0.0078 0.0052  193 THR C CA  
5805 C  C   . THR C 192 ? 0.0917 0.1142 0.1132 0.0054  -0.0099 -0.0017 193 THR C C   
5806 O  O   . THR C 192 ? 0.1093 0.1353 0.1222 0.0208  -0.0272 -0.0092 193 THR C O   
5807 C  CB  . THR C 192 ? 0.1127 0.1120 0.1179 0.0171  -0.0441 -0.0032 193 THR C CB  
5808 O  OG1 . THR C 192 ? 0.1358 0.1055 0.1356 0.0208  -0.0200 0.0015  193 THR C OG1 
5809 C  CG2 . THR C 192 ? 0.1226 0.1520 0.1262 0.0063  -0.0461 -0.0228 193 THR C CG2 
5810 N  N   . TYR C 193 ? 0.1176 0.1147 0.1134 -0.0137 -0.0051 0.0021  194 TYR C N   
5811 C  CA  . TYR C 193 ? 0.1159 0.1213 0.1143 0.0080  -0.0026 0.0119  194 TYR C CA  
5812 C  C   . TYR C 193 ? 0.1082 0.1080 0.1188 0.0001  -0.0019 -0.0121 194 TYR C C   
5813 O  O   . TYR C 193 ? 0.1023 0.1086 0.1263 0.0012  -0.0147 -0.0153 194 TYR C O   
5814 C  CB  . TYR C 193 ? 0.1075 0.1246 0.1360 0.0038  -0.0281 -0.0178 194 TYR C CB  
5815 C  CG  . TYR C 193 ? 0.1127 0.1014 0.1164 0.0082  -0.0076 -0.0080 194 TYR C CG  
5816 C  CD1 . TYR C 193 ? 0.1177 0.0847 0.1204 0.0197  0.0005  -0.0220 194 TYR C CD1 
5817 C  CD2 . TYR C 193 ? 0.1190 0.1052 0.1179 0.0081  0.0034  -0.0243 194 TYR C CD2 
5818 C  CE1 . TYR C 193 ? 0.1140 0.0833 0.0994 0.0109  -0.0017 -0.0054 194 TYR C CE1 
5819 C  CE2 . TYR C 193 ? 0.1062 0.1028 0.1244 0.0200  0.0000  0.0041  194 TYR C CE2 
5820 C  CZ  . TYR C 193 ? 0.0951 0.0793 0.0971 0.0059  0.0003  -0.0044 194 TYR C CZ  
5821 O  OH  . TYR C 193 ? 0.1001 0.1021 0.1035 0.0080  0.0035  -0.0049 194 TYR C OH  
5822 N  N   . PRO C 194 ? 0.1120 0.1094 0.0980 -0.0171 -0.0100 -0.0093 195 PRO C N   
5823 C  CA  . PRO C 194 ? 0.1507 0.0969 0.1253 -0.0297 -0.0176 -0.0184 195 PRO C CA  
5824 C  C   . PRO C 194 ? 0.1114 0.0971 0.0915 -0.0082 -0.0070 0.0026  195 PRO C C   
5825 O  O   . PRO C 194 ? 0.1215 0.1149 0.1375 0.0115  -0.0063 -0.0121 195 PRO C O   
5826 C  CB  . PRO C 194 ? 0.1286 0.1380 0.1611 -0.0174 -0.0331 -0.0127 195 PRO C CB  
5827 C  CG  . PRO C 194 ? 0.0839 0.1689 0.1533 -0.0186 -0.0232 0.0093  195 PRO C CG  
5828 C  CD  . PRO C 194 ? 0.1193 0.1727 0.1437 -0.0164 -0.0163 0.0137  195 PRO C CD  
5829 N  N   . GLY C 195 ? 0.1023 0.1036 0.0992 -0.0108 -0.0035 0.0031  196 GLY C N   
5830 C  CA  . GLY C 195 ? 0.1170 0.1102 0.0912 0.0040  -0.0098 -0.0082 196 GLY C CA  
5831 C  C   . GLY C 195 ? 0.0904 0.1023 0.1197 -0.0043 -0.0078 -0.0115 196 GLY C C   
5832 O  O   . GLY C 195 ? 0.1120 0.1064 0.1145 -0.0122 0.0043  -0.0071 196 GLY C O   
5833 N  N   . SER C 196 ? 0.0763 0.0868 0.1062 0.0021  -0.0076 -0.0003 197 SER C N   
5834 C  CA  . SER C 196 ? 0.1005 0.1154 0.0843 -0.0010 -0.0153 -0.0034 197 SER C CA  
5835 C  C   . SER C 196 ? 0.1062 0.0892 0.1204 0.0006  0.0020  0.0034  197 SER C C   
5836 O  O   . SER C 196 ? 0.0982 0.1032 0.0960 -0.0098 0.0052  0.0000  197 SER C O   
5837 C  CB  . SER C 196 ? 0.1313 0.1001 0.0948 -0.0102 0.0167  -0.0068 197 SER C CB  
5838 O  OG  . SER C 196 ? 0.1021 0.1021 0.1116 -0.0146 0.0055  -0.0012 197 SER C OG  
5839 N  N   . LEU C 197 ? 0.0900 0.1052 0.0820 -0.0111 0.0024  -0.0003 198 LEU C N   
5840 C  CA  . LEU C 197 ? 0.0924 0.0929 0.0913 -0.0149 0.0041  0.0087  198 LEU C CA  
5841 C  C   . LEU C 197 ? 0.1093 0.1064 0.0917 -0.0054 0.0085  -0.0030 198 LEU C C   
5842 O  O   . LEU C 197 ? 0.1071 0.1107 0.0942 -0.0063 0.0071  0.0010  198 LEU C O   
5843 C  CB  . LEU C 197 ? 0.1493 0.1306 0.1228 0.0203  -0.0115 0.0015  198 LEU C CB  
5844 C  CG  . LEU C 197 ? 0.1386 0.1080 0.1037 0.0003  -0.0055 0.0071  198 LEU C CG  
5845 C  CD1 . LEU C 197 ? 0.1668 0.1497 0.1518 0.0300  0.0177  0.0461  198 LEU C CD1 
5846 C  CD2 . LEU C 197 ? 0.2012 0.1483 0.1362 0.0350  0.0152  -0.0043 198 LEU C CD2 
5847 N  N   . THR C 198 ? 0.1073 0.1045 0.1057 -0.0032 0.0038  -0.0100 199 THR C N   
5848 C  CA  . THR C 198 ? 0.1312 0.0989 0.1028 -0.0098 0.0038  -0.0015 199 THR C CA  
5849 C  C   . THR C 198 ? 0.1389 0.1184 0.0854 -0.0020 0.0248  0.0076  199 THR C C   
5850 O  O   . THR C 198 ? 0.1377 0.1150 0.0888 -0.0126 0.0109  0.0057  199 THR C O   
5851 C  CB  . THR C 198 ? 0.0953 0.0988 0.0938 -0.0093 0.0015  0.0049  199 THR C CB  
5852 O  OG1 . THR C 198 ? 0.1023 0.1118 0.1028 0.0142  0.0040  0.0034  199 THR C OG1 
5853 C  CG2 . THR C 198 ? 0.1118 0.1134 0.1067 0.0043  -0.0272 0.0038  199 THR C CG2 
5854 N  N   . THR C 199 ? 0.1231 0.1247 0.1076 -0.0035 -0.0038 0.0192  200 THR C N   
5855 C  CA  . THR C 199 ? 0.1355 0.1310 0.1137 -0.0348 -0.0210 0.0194  200 THR C CA  
5856 C  C   . THR C 199 ? 0.1382 0.1290 0.1132 -0.0087 0.0205  0.0054  200 THR C C   
5857 O  O   . THR C 199 ? 0.1660 0.1297 0.1109 -0.0126 0.0032  0.0126  200 THR C O   
5858 C  CB  . THR C 199 ? 0.1425 0.2021 0.1396 -0.0315 -0.0091 0.0241  200 THR C CB  
5859 O  OG1 . THR C 199 ? 0.1912 0.1960 0.2518 0.0340  0.0219  0.0116  200 THR C OG1 
5860 C  CG2 . THR C 199 ? 0.1495 0.1596 0.1659 -0.0430 -0.0006 -0.0062 200 THR C CG2 
5861 N  N   . PRO C 200 ? 0.1565 0.1308 0.1084 -0.0269 -0.0239 0.0142  201 PRO C N   
5862 C  CA  . PRO C 200 ? 0.1930 0.1374 0.1161 -0.0192 -0.0003 0.0250  201 PRO C CA  
5863 C  C   . PRO C 200 ? 0.1437 0.1587 0.1380 -0.0229 -0.0052 0.0074  201 PRO C C   
5864 O  O   . PRO C 200 ? 0.1596 0.1768 0.1694 -0.0034 0.0020  -0.0012 201 PRO C O   
5865 C  CB  . PRO C 200 ? 0.1721 0.1920 0.1032 -0.0201 0.0133  0.0083  201 PRO C CB  
5866 C  CG  . PRO C 200 ? 0.1978 0.1757 0.1263 -0.0164 0.0342  0.0326  201 PRO C CG  
5867 C  CD  . PRO C 200 ? 0.1653 0.1565 0.0974 -0.0251 -0.0103 -0.0043 201 PRO C CD  
5868 N  N   . PRO C 201 ? 0.1599 0.1646 0.1057 -0.0057 0.0046  0.0043  202 PRO C N   
5869 C  CA  . PRO C 201 ? 0.1457 0.1545 0.1655 0.0071  0.0052  0.0482  202 PRO C CA  
5870 C  C   . PRO C 201 ? 0.1488 0.1596 0.1342 -0.0140 0.0087  -0.0012 202 PRO C C   
5871 O  O   . PRO C 201 ? 0.1552 0.1389 0.1444 -0.0027 0.0141  0.0210  202 PRO C O   
5872 C  CB  . PRO C 201 ? 0.1941 0.1536 0.1651 0.0019  -0.0098 0.0372  202 PRO C CB  
5873 C  CG  . PRO C 201 ? 0.1759 0.1779 0.2041 -0.0035 0.0267  0.0329  202 PRO C CG  
5874 C  CD  . PRO C 201 ? 0.1700 0.1552 0.1895 -0.0005 -0.0070 -0.0028 202 PRO C CD  
5875 N  N   . LEU C 202 ? 0.1247 0.1093 0.1073 0.0006  0.0071  -0.0006 203 LEU C N   
5876 C  CA  . LEU C 202 ? 0.1276 0.1231 0.1184 -0.0046 0.0221  -0.0038 203 LEU C CA  
5877 C  C   . LEU C 202 ? 0.1234 0.1314 0.1168 0.0051  0.0098  0.0013  203 LEU C C   
5878 O  O   . LEU C 202 ? 0.1163 0.1179 0.1164 -0.0131 0.0115  -0.0062 203 LEU C O   
5879 C  CB  . LEU C 202 ? 0.1191 0.1360 0.0921 -0.0164 0.0272  -0.0015 203 LEU C CB  
5880 C  CG  . LEU C 202 ? 0.1465 0.1213 0.1054 -0.0229 0.0322  -0.0119 203 LEU C CG  
5881 C  CD1 . LEU C 202 ? 0.1983 0.1479 0.1186 0.0062  0.0370  -0.0199 203 LEU C CD1 
5882 C  CD2 . LEU C 202 ? 0.1820 0.1362 0.1009 -0.0256 0.0296  -0.0074 203 LEU C CD2 
5883 N  N   . LEU C 203 ? 0.1365 0.1156 0.1197 -0.0087 0.0183  -0.0023 204 LEU C N   
5884 C  CA  . LEU C 203 ? 0.1394 0.1127 0.1337 -0.0177 -0.0041 0.0103  204 LEU C CA  
5885 C  C   . LEU C 203 ? 0.1438 0.1259 0.1234 -0.0148 -0.0043 -0.0062 204 LEU C C   
5886 O  O   . LEU C 203 ? 0.1190 0.1102 0.1313 -0.0088 0.0140  -0.0062 204 LEU C O   
5887 C  CB  . LEU C 203 ? 0.1552 0.1156 0.1650 0.0071  -0.0165 -0.0054 204 LEU C CB  
5888 C  CG  . LEU C 203 ? 0.1987 0.1365 0.1899 0.0162  -0.0082 0.0126  204 LEU C CG  
5889 C  CD1 . LEU C 203 ? 0.2134 0.1638 0.1630 0.0482  -0.0447 0.0147  204 LEU C CD1 
5890 C  CD2 . LEU C 203 ? 0.2865 0.1716 0.1868 0.0040  0.0240  0.0485  204 LEU C CD2 
5891 N  N   . GLU C 204 ? 0.1316 0.1308 0.1260 -0.0192 -0.0105 -0.0057 205 GLU C N   
5892 C  CA  . GLU C 204 ? 0.1003 0.1313 0.1271 -0.0146 0.0000  -0.0013 205 GLU C CA  
5893 C  C   . GLU C 204 ? 0.1103 0.1288 0.1547 -0.0024 0.0027  -0.0147 205 GLU C C   
5894 O  O   . GLU C 204 ? 0.1319 0.1639 0.1676 -0.0260 0.0082  -0.0232 205 GLU C O   
5895 C  CB  . GLU C 204 ? 0.1215 0.1356 0.1798 -0.0254 0.0399  -0.0149 205 GLU C CB  
5896 C  CG  . GLU C 204 ? 0.1351 0.1412 0.1328 -0.0189 0.0185  0.0096  205 GLU C CG  
5897 C  CD  . GLU C 204 ? 0.1432 0.1592 0.1700 -0.0026 0.0057  -0.0010 205 GLU C CD  
5898 O  OE1 . GLU C 204 ? 0.1498 0.2005 0.2373 -0.0315 0.0644  -0.0414 205 GLU C OE1 
5899 O  OE2 . GLU C 204 ? 0.1369 0.1553 0.1714 -0.0183 0.0406  -0.0010 205 GLU C OE2 
5900 N  N   . CYS C 205 ? 0.1128 0.1058 0.1149 0.0010  0.0166  -0.0013 206 CYS C N   
5901 C  CA  . CYS C 205 ? 0.1120 0.1221 0.1213 0.0147  -0.0028 -0.0087 206 CYS C CA  
5902 C  C   . CYS C 205 ? 0.1204 0.0922 0.1301 -0.0162 0.0188  -0.0192 206 CYS C C   
5903 O  O   . CYS C 205 ? 0.1351 0.1138 0.1416 0.0087  0.0239  -0.0104 206 CYS C O   
5904 C  CB  . CYS C 205 ? 0.1297 0.1450 0.1374 0.0012  -0.0260 0.0020  206 CYS C CB  
5905 S  SG  . CYS C 205 ? 0.1294 0.1283 0.1516 0.0000  -0.0043 -0.0059 206 CYS C SG  
5906 N  N   . VAL C 206 ? 0.1024 0.0989 0.1269 0.0082  0.0024  0.0098  207 VAL C N   
5907 C  CA  . VAL C 206 ? 0.1217 0.0863 0.1089 0.0041  -0.0054 -0.0044 207 VAL C CA  
5908 C  C   . VAL C 206 ? 0.0936 0.0800 0.1082 -0.0136 0.0085  -0.0068 207 VAL C C   
5909 O  O   . VAL C 206 ? 0.1143 0.1246 0.1340 0.0189  0.0046  -0.0012 207 VAL C O   
5910 C  CB  . VAL C 206 ? 0.1071 0.0996 0.0958 -0.0017 0.0179  -0.0124 207 VAL C CB  
5911 C  CG1 . VAL C 206 ? 0.1026 0.1155 0.1064 -0.0137 0.0267  -0.0126 207 VAL C CG1 
5912 C  CG2 . VAL C 206 ? 0.1374 0.1244 0.0997 0.0077  -0.0068 -0.0087 207 VAL C CG2 
5913 N  N   . THR C 207 ? 0.1188 0.0952 0.0913 -0.0031 0.0038  0.0003  208 THR C N   
5914 C  CA  . THR C 207 ? 0.1089 0.1150 0.0965 -0.0113 -0.0076 0.0017  208 THR C CA  
5915 C  C   . THR C 207 ? 0.0978 0.1018 0.1120 0.0066  -0.0087 0.0035  208 THR C C   
5916 O  O   . THR C 207 ? 0.0940 0.0915 0.1297 -0.0017 0.0010  0.0082  208 THR C O   
5917 C  CB  . THR C 207 ? 0.1295 0.1093 0.1103 -0.0197 -0.0044 -0.0077 208 THR C CB  
5918 O  OG1 . THR C 207 ? 0.1407 0.1012 0.1202 -0.0164 -0.0164 -0.0099 208 THR C OG1 
5919 C  CG2 . THR C 207 ? 0.1897 0.1136 0.1181 0.0194  -0.0187 -0.0008 208 THR C CG2 
5920 N  N   . TRP C 208 ? 0.1005 0.0954 0.1073 0.0057  -0.0048 -0.0026 209 TRP C N   
5921 C  CA  . TRP C 208 ? 0.1080 0.0976 0.0847 -0.0073 -0.0121 -0.0113 209 TRP C CA  
5922 C  C   . TRP C 208 ? 0.0940 0.1012 0.0824 0.0074  -0.0057 -0.0087 209 TRP C C   
5923 O  O   . TRP C 208 ? 0.1046 0.0967 0.1010 0.0023  -0.0110 0.0021  209 TRP C O   
5924 C  CB  . TRP C 208 ? 0.1062 0.1098 0.0945 0.0217  -0.0151 -0.0110 209 TRP C CB  
5925 C  CG  . TRP C 208 ? 0.0951 0.0872 0.0886 0.0094  0.0013  -0.0098 209 TRP C CG  
5926 C  CD1 . TRP C 208 ? 0.1132 0.0775 0.0897 0.0093  0.0024  0.0017  209 TRP C CD1 
5927 C  CD2 . TRP C 208 ? 0.1010 0.0700 0.1167 0.0024  0.0052  -0.0020 209 TRP C CD2 
5928 N  NE1 . TRP C 208 ? 0.1150 0.0945 0.0978 -0.0027 0.0078  -0.0154 209 TRP C NE1 
5929 C  CE2 . TRP C 208 ? 0.0921 0.0913 0.1109 0.0131  -0.0006 -0.0098 209 TRP C CE2 
5930 C  CE3 . TRP C 208 ? 0.0897 0.0707 0.1039 0.0049  0.0098  -0.0159 209 TRP C CE3 
5931 C  CZ2 . TRP C 208 ? 0.0908 0.1037 0.1114 0.0044  -0.0041 -0.0181 209 TRP C CZ2 
5932 C  CZ3 . TRP C 208 ? 0.1073 0.0970 0.1174 0.0001  0.0054  -0.0263 209 TRP C CZ3 
5933 C  CH2 . TRP C 208 ? 0.1082 0.0939 0.1222 -0.0017 0.0071  -0.0333 209 TRP C CH2 
5934 N  N   . ILE C 209 ? 0.1102 0.0966 0.0830 0.0089  -0.0010 0.0010  210 ILE C N   
5935 C  CA  . ILE C 209 ? 0.1268 0.0870 0.0926 0.0000  0.0057  0.0003  210 ILE C CA  
5936 C  C   . ILE C 209 ? 0.0888 0.1067 0.0917 -0.0024 -0.0071 0.0055  210 ILE C C   
5937 O  O   . ILE C 209 ? 0.0935 0.1008 0.1277 0.0083  -0.0198 0.0023  210 ILE C O   
5938 C  CB  . ILE C 209 ? 0.1317 0.1050 0.0992 0.0065  0.0270  -0.0073 210 ILE C CB  
5939 C  CG1 . ILE C 209 ? 0.1711 0.1033 0.1278 0.0070  0.0008  -0.0071 210 ILE C CG1 
5940 C  CG2 . ILE C 209 ? 0.1500 0.1353 0.0895 0.0046  0.0344  -0.0023 210 ILE C CG2 
5941 C  CD1 . ILE C 209 ? 0.2125 0.1265 0.1312 0.0240  0.0054  -0.0206 210 ILE C CD1 
5942 N  N   . VAL C 210 ? 0.1209 0.0944 0.0854 0.0000  0.0074  -0.0010 211 VAL C N   
5943 C  CA  . VAL C 210 ? 0.1062 0.0991 0.0851 0.0066  0.0080  0.0028  211 VAL C CA  
5944 C  C   . VAL C 210 ? 0.0971 0.0762 0.0803 0.0010  -0.0078 -0.0046 211 VAL C C   
5945 O  O   . VAL C 210 ? 0.1167 0.1082 0.1121 0.0096  -0.0190 -0.0040 211 VAL C O   
5946 C  CB  . VAL C 210 ? 0.1234 0.1068 0.0811 -0.0048 0.0273  0.0020  211 VAL C CB  
5947 C  CG1 . VAL C 210 ? 0.1328 0.0961 0.0996 -0.0153 -0.0028 -0.0071 211 VAL C CG1 
5948 C  CG2 . VAL C 210 ? 0.1353 0.1289 0.0927 -0.0021 0.0038  0.0199  211 VAL C CG2 
5949 N  N   . LEU C 211 ? 0.1127 0.1096 0.0931 -0.0003 0.0043  0.0010  212 LEU C N   
5950 C  CA  . LEU C 211 ? 0.1193 0.1071 0.0940 -0.0121 0.0010  0.0035  212 LEU C CA  
5951 C  C   . LEU C 211 ? 0.1274 0.1120 0.1075 0.0065  -0.0060 0.0076  212 LEU C C   
5952 O  O   . LEU C 211 ? 0.1333 0.1221 0.1147 -0.0060 0.0040  0.0040  212 LEU C O   
5953 C  CB  . LEU C 211 ? 0.1173 0.1071 0.1082 -0.0105 -0.0197 0.0164  212 LEU C CB  
5954 C  CG  . LEU C 211 ? 0.1398 0.1362 0.1107 0.0228  0.0285  0.0120  212 LEU C CG  
5955 C  CD1 . LEU C 211 ? 0.1256 0.1852 0.1644 0.0274  0.0322  -0.0077 212 LEU C CD1 
5956 C  CD2 . LEU C 211 ? 0.1601 0.1547 0.1332 0.0135  0.0094  -0.0057 212 LEU C CD2 
5957 N  N   . LYS C 212 ? 0.1274 0.1256 0.1014 0.0129  0.0026  0.0201  213 LYS C N   
5958 C  CA  . LYS C 212 ? 0.1272 0.1154 0.1409 0.0035  0.0034  0.0168  213 LYS C CA  
5959 C  C   . LYS C 212 ? 0.1127 0.1270 0.1294 0.0124  -0.0226 0.0093  213 LYS C C   
5960 O  O   . LYS C 212 ? 0.1685 0.1333 0.1477 0.0240  0.0208  0.0082  213 LYS C O   
5961 C  CB  . LYS C 212 ? 0.1748 0.1502 0.1387 -0.0093 -0.0195 -0.0013 213 LYS C CB  
5962 C  CG  . LYS C 212 ? 0.1856 0.1829 0.2192 -0.0167 0.0052  0.0183  213 LYS C CG  
5963 C  CD  . LYS C 212 ? 0.5979 0.3964 0.2919 -0.0461 -0.0392 0.0649  213 LYS C CD  
5964 C  CE  . LYS C 212 ? 0.4126 0.4135 0.4189 0.0062  -0.1303 -0.1026 213 LYS C CE  
5965 N  NZ  . LYS C 212 ? 0.3235 0.3190 0.1890 0.0146  -0.0201 0.0076  213 LYS C NZ  
5966 N  N   . GLU C 213 ? 0.1290 0.1150 0.1000 0.0179  0.0083  0.0154  214 GLU C N   
5967 C  CA  . GLU C 213 ? 0.1504 0.1342 0.1091 0.0060  0.0126  -0.0207 214 GLU C CA  
5968 C  C   . GLU C 213 ? 0.1303 0.1211 0.1100 -0.0037 -0.0043 0.0120  214 GLU C C   
5969 O  O   . GLU C 213 ? 0.1396 0.1115 0.1045 0.0172  0.0225  0.0089  214 GLU C O   
5970 C  CB  . GLU C 213 ? 0.1464 0.1668 0.0985 0.0030  0.0137  -0.0204 214 GLU C CB  
5971 C  CG  . GLU C 213 ? 0.1967 0.1646 0.1629 -0.0132 0.0386  -0.0082 214 GLU C CG  
5972 C  CD  . GLU C 213 ? 0.2314 0.2276 0.1242 -0.0472 0.0170  0.0461  214 GLU C CD  
5973 O  OE1 . GLU C 213 ? 0.2601 0.1915 0.1508 0.0076  0.0643  0.0286  214 GLU C OE1 
5974 O  OE2 . GLU C 213 ? 0.3531 0.5864 0.2885 -0.1687 0.1376  0.0122  214 GLU C OE2 
5975 N  N   . PRO C 214 ? 0.1254 0.1032 0.1152 0.0098  0.0105  0.0081  215 PRO C N   
5976 C  CA  . PRO C 214 ? 0.1280 0.1085 0.1217 0.0023  0.0044  -0.0114 215 PRO C CA  
5977 C  C   . PRO C 214 ? 0.1298 0.1448 0.1033 0.0119  0.0055  0.0071  215 PRO C C   
5978 O  O   . PRO C 214 ? 0.1631 0.1527 0.1231 0.0154  0.0288  0.0200  215 PRO C O   
5979 C  CB  . PRO C 214 ? 0.1459 0.0998 0.1260 0.0127  0.0186  -0.0088 215 PRO C CB  
5980 C  CG  . PRO C 214 ? 0.2777 0.1678 0.1856 0.0225  -0.0648 -0.0019 215 PRO C CG  
5981 C  CD  . PRO C 214 ? 0.1669 0.1080 0.1096 0.0373  -0.0071 0.0082  215 PRO C CD  
5982 N  N   . ILE C 215 ? 0.0982 0.1071 0.1359 0.0032  0.0015  -0.0087 216 ILE C N   
5983 C  CA  . ILE C 215 ? 0.0991 0.1301 0.1342 -0.0010 0.0008  -0.0065 216 ILE C CA  
5984 C  C   . ILE C 215 ? 0.1224 0.1145 0.1326 -0.0091 0.0253  -0.0081 216 ILE C C   
5985 O  O   . ILE C 215 ? 0.1389 0.1172 0.1308 -0.0027 0.0229  -0.0006 216 ILE C O   
5986 C  CB  . ILE C 215 ? 0.1541 0.1177 0.1314 0.0146  0.0126  -0.0055 216 ILE C CB  
5987 C  CG1 . ILE C 215 ? 0.1339 0.1377 0.1357 0.0109  0.0057  0.0052  216 ILE C CG1 
5988 C  CG2 . ILE C 215 ? 0.1684 0.1392 0.1481 0.0027  0.0221  -0.0310 216 ILE C CG2 
5989 C  CD1 . ILE C 215 ? 0.1425 0.1231 0.1708 0.0153  0.0241  0.0024  216 ILE C CD1 
5990 N  N   . SER C 216 ? 0.0866 0.0693 0.0551 -0.0043 0.0074  -0.0060 217 SER C N   
5991 C  CA  . SER C 216 ? 0.0584 0.0642 0.0496 -0.0043 0.0200  -0.0037 217 SER C CA  
5992 C  C   . SER C 216 ? 0.0569 0.0336 0.0818 -0.0048 0.0214  0.0143  217 SER C C   
5993 O  O   . SER C 216 ? 0.0663 0.0642 0.0480 0.0132  0.0051  0.0104  217 SER C O   
5994 C  CB  . SER C 216 ? 0.0901 0.0680 0.1242 -0.0108 0.0121  0.0357  217 SER C CB  
5995 O  OG  . SER C 216 ? 0.1276 0.1506 0.1626 -0.0026 0.0080  0.0350  217 SER C OG  
5996 N  N   . VAL C 217 ? 0.1224 0.1270 0.1170 -0.0182 0.0071  0.0068  218 VAL C N   
5997 C  CA  . VAL C 217 ? 0.1333 0.1103 0.1204 -0.0085 0.0013  0.0107  218 VAL C CA  
5998 C  C   . VAL C 217 ? 0.1292 0.1125 0.1308 0.0006  0.0163  -0.0044 218 VAL C C   
5999 O  O   . VAL C 217 ? 0.1295 0.1046 0.1423 -0.0054 0.0153  0.0049  218 VAL C O   
6000 C  CB  . VAL C 217 ? 0.1499 0.1138 0.1303 0.0010  0.0265  0.0098  218 VAL C CB  
6001 C  CG1 . VAL C 217 ? 0.1432 0.1120 0.1438 -0.0001 0.0172  -0.0032 218 VAL C CG1 
6002 C  CG2 . VAL C 217 ? 0.1563 0.1292 0.1592 -0.0119 0.0513  0.0093  218 VAL C CG2 
6003 N  N   . SER C 218 ? 0.1254 0.1263 0.1371 -0.0100 0.0195  0.0005  219 SER C N   
6004 C  CA  . SER C 218 ? 0.1353 0.1263 0.1299 -0.0012 0.0107  -0.0162 219 SER C CA  
6005 C  C   . SER C 218 ? 0.1430 0.1100 0.1212 -0.0015 0.0116  -0.0027 219 SER C C   
6006 O  O   . SER C 218 ? 0.1439 0.1258 0.1513 0.0074  0.0099  0.0120  219 SER C O   
6007 C  CB  . SER C 218 ? 0.1164 0.1337 0.1581 -0.0080 -0.0027 0.0142  219 SER C CB  
6008 O  OG  . SER C 218 ? 0.1396 0.1466 0.1398 -0.0142 0.0096  0.0200  219 SER C OG  
6009 N  N   A SER C 219 ? 0.1572 0.1035 0.1466 -0.0010 0.0255  -0.0148 220 SER C N   
6010 N  N   B SER C 219 ? 0.1580 0.1032 0.1499 -0.0010 0.0219  -0.0131 220 SER C N   
6011 C  CA  A SER C 219 ? 0.1685 0.1247 0.1520 -0.0041 0.0174  -0.0136 220 SER C CA  
6012 C  CA  B SER C 219 ? 0.1628 0.1272 0.1563 -0.0231 0.0211  -0.0120 220 SER C CA  
6013 C  C   A SER C 219 ? 0.1793 0.1307 0.1252 0.0120  0.0329  -0.0027 220 SER C C   
6014 C  C   B SER C 219 ? 0.1849 0.1222 0.1412 0.0162  0.0368  -0.0147 220 SER C C   
6015 O  O   A SER C 219 ? 0.1818 0.1448 0.1253 -0.0051 0.0221  0.0120  220 SER C O   
6016 O  O   B SER C 219 ? 0.2060 0.1445 0.1292 -0.0154 0.0031  -0.0088 220 SER C O   
6017 C  CB  A SER C 219 ? 0.2344 0.1258 0.2348 -0.0020 0.0173  -0.0304 220 SER C CB  
6018 C  CB  B SER C 219 ? 0.1965 0.1362 0.2220 -0.0322 -0.0240 -0.0083 220 SER C CB  
6019 O  OG  A SER C 219 ? 0.2161 0.1045 0.2082 0.0051  -0.0239 -0.0068 220 SER C OG  
6020 O  OG  B SER C 219 ? 0.2030 0.1741 0.2166 -0.0024 -0.0386 0.0038  220 SER C OG  
6021 N  N   . GLU C 220 ? 0.1558 0.1287 0.1489 -0.0012 0.0060  -0.0140 221 GLU C N   
6022 C  CA  . GLU C 220 ? 0.1710 0.1544 0.1761 0.0028  0.0099  -0.0006 221 GLU C CA  
6023 C  C   . GLU C 220 ? 0.1483 0.1377 0.1427 0.0126  -0.0052 0.0010  221 GLU C C   
6024 O  O   . GLU C 220 ? 0.1809 0.1563 0.1448 -0.0085 -0.0392 -0.0107 221 GLU C O   
6025 C  CB  . GLU C 220 ? 0.1750 0.1838 0.2330 0.0120  0.0335  -0.0060 221 GLU C CB  
6026 C  CG  . GLU C 220 ? 0.2621 0.2082 0.3003 -0.0350 0.0043  0.0088  221 GLU C CG  
6027 C  CD  . GLU C 220 ? 0.3310 0.2330 0.3301 -0.0474 -0.0307 0.0135  221 GLU C CD  
6028 O  OE1 . GLU C 220 ? 0.2816 0.1800 0.2872 -0.0381 0.0156  0.0065  221 GLU C OE1 
6029 O  OE2 . GLU C 220 ? 0.5097 0.2989 0.5435 -0.1418 -0.1083 0.1404  221 GLU C OE2 
6030 N  N   . GLN C 221 ? 0.1347 0.1249 0.1432 0.0017  0.0132  -0.0006 222 GLN C N   
6031 C  CA  . GLN C 221 ? 0.1446 0.1188 0.1430 -0.0038 0.0149  0.0188  222 GLN C CA  
6032 C  C   . GLN C 221 ? 0.1378 0.1168 0.1283 0.0063  0.0052  0.0141  222 GLN C C   
6033 O  O   . GLN C 221 ? 0.1477 0.1464 0.1404 0.0038  -0.0122 0.0266  222 GLN C O   
6034 C  CB  . GLN C 221 ? 0.1308 0.1475 0.1319 0.0020  0.0111  -0.0043 222 GLN C CB  
6035 C  CG  . GLN C 221 ? 0.1154 0.1662 0.1347 -0.0003 -0.0044 0.0242  222 GLN C CG  
6036 C  CD  . GLN C 221 ? 0.1076 0.1242 0.1571 -0.0251 0.0001  0.0184  222 GLN C CD  
6037 O  OE1 . GLN C 221 ? 0.1246 0.1349 0.1285 0.0081  0.0108  -0.0001 222 GLN C OE1 
6038 N  NE2 . GLN C 221 ? 0.1380 0.1170 0.1597 -0.0137 0.0015  0.0105  222 GLN C NE2 
6039 N  N   . VAL C 222 ? 0.1378 0.1321 0.1474 0.0020  0.0223  0.0082  223 VAL C N   
6040 C  CA  . VAL C 222 ? 0.1529 0.1389 0.1326 0.0225  0.0207  0.0218  223 VAL C CA  
6041 C  C   . VAL C 222 ? 0.1691 0.1475 0.1662 0.0230  -0.0017 0.0153  223 VAL C C   
6042 O  O   . VAL C 222 ? 0.1500 0.1538 0.1533 0.0197  -0.0013 0.0261  223 VAL C O   
6043 C  CB  . VAL C 222 ? 0.1701 0.1791 0.2039 0.0472  0.0293  0.0377  223 VAL C CB  
6044 C  CG1 . VAL C 222 ? 0.2500 0.1847 0.1590 -0.0015 0.0153  0.0657  223 VAL C CG1 
6045 C  CG2 . VAL C 222 ? 0.2156 0.2124 0.1908 0.0124  0.0659  0.0087  223 VAL C CG2 
6046 N  N   . LEU C 223 ? 0.1678 0.1540 0.1290 0.0071  0.0040  -0.0218 224 LEU C N   
6047 C  CA  . LEU C 223 ? 0.2096 0.1757 0.1229 0.0065  0.0015  -0.0244 224 LEU C CA  
6048 C  C   . LEU C 223 ? 0.1768 0.1764 0.1474 -0.0282 0.0074  0.0165  224 LEU C C   
6049 O  O   . LEU C 223 ? 0.2023 0.1951 0.1299 -0.0184 0.0065  0.0099  224 LEU C O   
6050 C  CB  . LEU C 223 ? 0.2361 0.2093 0.2105 -0.0074 0.0364  0.0445  224 LEU C CB  
6051 C  CG  . LEU C 223 ? 0.2485 0.2386 0.1748 0.0219  0.0136  0.0092  224 LEU C CG  
6052 C  CD1 . LEU C 223 ? 0.2953 0.2876 0.2831 -0.0645 0.0124  0.0182  224 LEU C CD1 
6053 C  CD2 . LEU C 223 ? 0.2667 0.2633 0.1969 -0.0192 0.0186  -0.0370 224 LEU C CD2 
6054 N  N   . LYS C 224 ? 0.1502 0.1673 0.1520 0.0083  -0.0082 0.0142  225 LYS C N   
6055 C  CA  . LYS C 224 ? 0.1888 0.1753 0.1583 0.0010  0.0035  0.0065  225 LYS C CA  
6056 C  C   . LYS C 224 ? 0.1495 0.1556 0.1619 0.0063  -0.0143 0.0070  225 LYS C C   
6057 O  O   . LYS C 224 ? 0.1418 0.1614 0.1615 0.0007  -0.0296 0.0269  225 LYS C O   
6058 C  CB  . LYS C 224 ? 0.2123 0.2109 0.1870 -0.0043 0.0216  0.0017  225 LYS C CB  
6059 C  CG  . LYS C 224 ? 0.2551 0.2265 0.2125 -0.0505 0.0498  -0.0063 225 LYS C CG  
6060 C  CD  . LYS C 224 ? 0.2451 0.3172 0.4625 -0.0384 0.0979  -0.0248 225 LYS C CD  
6061 C  CE  . LYS C 224 ? 0.2388 0.3677 0.3506 -0.0956 0.0736  -0.0140 225 LYS C CE  
6062 N  NZ  . LYS C 224 ? 0.3111 0.4695 0.3115 -0.0781 0.0408  -0.0103 225 LYS C NZ  
6063 N  N   . PHE C 225 ? 0.1382 0.1215 0.1450 -0.0081 0.0043  0.0051  226 PHE C N   
6064 C  CA  . PHE C 225 ? 0.1097 0.1398 0.1310 0.0051  -0.0027 0.0230  226 PHE C CA  
6065 C  C   . PHE C 225 ? 0.1281 0.1421 0.1457 0.0076  -0.0199 0.0131  226 PHE C C   
6066 O  O   . PHE C 225 ? 0.1439 0.1500 0.1430 -0.0081 -0.0157 0.0068  226 PHE C O   
6067 C  CB  . PHE C 225 ? 0.1292 0.1506 0.1308 0.0074  -0.0255 -0.0082 226 PHE C CB  
6068 C  CG  . PHE C 225 ? 0.1565 0.1350 0.1423 -0.0254 0.0207  -0.0030 226 PHE C CG  
6069 C  CD1 . PHE C 225 ? 0.1919 0.2267 0.1371 0.0355  0.0001  -0.0443 226 PHE C CD1 
6070 C  CD2 . PHE C 225 ? 0.1703 0.1741 0.1532 -0.0324 0.0181  -0.0165 226 PHE C CD2 
6071 C  CE1 . PHE C 225 ? 0.2197 0.2178 0.1603 -0.0051 -0.0086 -0.0346 226 PHE C CE1 
6072 C  CE2 . PHE C 225 ? 0.2028 0.2366 0.1709 -0.0522 0.0143  -0.0601 226 PHE C CE2 
6073 C  CZ  . PHE C 225 ? 0.2057 0.1617 0.1644 -0.0126 0.0152  0.0170  226 PHE C CZ  
6074 N  N   . ARG C 226 ? 0.1213 0.1326 0.1179 0.0055  -0.0087 0.0019  227 ARG C N   
6075 C  CA  . ARG C 226 ? 0.1513 0.1559 0.1335 0.0100  -0.0131 -0.0035 227 ARG C CA  
6076 C  C   . ARG C 226 ? 0.1480 0.1452 0.1541 -0.0218 -0.0003 0.0148  227 ARG C C   
6077 O  O   . ARG C 226 ? 0.1580 0.1737 0.1434 -0.0038 -0.0049 -0.0020 227 ARG C O   
6078 C  CB  . ARG C 226 ? 0.1383 0.1421 0.1675 0.0130  -0.0027 -0.0057 227 ARG C CB  
6079 C  CG  . ARG C 226 ? 0.1330 0.1580 0.1574 -0.0031 -0.0153 0.0164  227 ARG C CG  
6080 C  CD  . ARG C 226 ? 0.1554 0.1545 0.2303 0.0057  -0.0220 0.0071  227 ARG C CD  
6081 N  NE  . ARG C 226 ? 0.1619 0.1538 0.1843 -0.0020 0.0060  0.0362  227 ARG C NE  
6082 C  CZ  . ARG C 226 ? 0.1543 0.1306 0.1836 -0.0229 -0.0147 0.0256  227 ARG C CZ  
6083 N  NH1 . ARG C 226 ? 0.1536 0.1922 0.2413 -0.0653 -0.0125 0.0216  227 ARG C NH1 
6084 N  NH2 . ARG C 226 ? 0.1787 0.1640 0.1939 -0.0073 -0.0273 0.0577  227 ARG C NH2 
6085 N  N   . LYS C 227 ? 0.1340 0.1532 0.1508 -0.0008 -0.0181 0.0135  228 LYS C N   
6086 C  CA  . LYS C 227 ? 0.1728 0.1578 0.1459 -0.0080 -0.0329 0.0222  228 LYS C CA  
6087 C  C   . LYS C 227 ? 0.1378 0.1346 0.1516 0.0046  -0.0412 0.0119  228 LYS C C   
6088 O  O   . LYS C 227 ? 0.1834 0.1709 0.1642 -0.0253 -0.0681 0.0322  228 LYS C O   
6089 C  CB  . LYS C 227 ? 0.1580 0.2192 0.2066 -0.0306 -0.0204 0.0283  228 LYS C CB  
6090 C  CG  . LYS C 227 ? 0.1495 0.2240 0.3151 -0.0494 -0.0114 0.0264  228 LYS C CG  
6091 C  CD  . LYS C 227 ? 0.2930 0.4153 0.3318 -0.1477 0.0456  0.0231  228 LYS C CD  
6092 C  CE  . LYS C 227 ? 0.4700 0.5339 0.4149 -0.0843 -0.0245 0.1351  228 LYS C CE  
6093 N  NZ  . LYS C 227 ? 0.6423 0.3953 0.5016 -0.0582 -0.0410 0.0806  228 LYS C NZ  
6094 N  N   . LEU C 228 ? 0.1355 0.1463 0.1777 -0.0020 -0.0410 0.0136  229 LEU C N   
6095 C  CA  . LEU C 228 ? 0.1360 0.1395 0.1350 -0.0263 -0.0091 -0.0052 229 LEU C CA  
6096 C  C   . LEU C 228 ? 0.1186 0.1371 0.1407 -0.0221 -0.0339 0.0015  229 LEU C C   
6097 O  O   . LEU C 228 ? 0.1376 0.1626 0.1326 0.0023  -0.0370 -0.0041 229 LEU C O   
6098 C  CB  . LEU C 228 ? 0.1386 0.1547 0.1326 -0.0337 -0.0368 0.0153  229 LEU C CB  
6099 C  CG  . LEU C 228 ? 0.1376 0.1601 0.1396 0.0008  -0.0288 0.0031  229 LEU C CG  
6100 C  CD1 . LEU C 228 ? 0.1344 0.1851 0.1543 -0.0313 -0.0333 0.0232  229 LEU C CD1 
6101 C  CD2 . LEU C 228 ? 0.1678 0.1660 0.1969 0.0151  -0.0502 -0.0076 229 LEU C CD2 
6102 N  N   . ASN C 229 ? 0.1558 0.1771 0.1328 -0.0074 -0.0182 0.0171  230 ASN C N   
6103 C  CA  . ASN C 229 ? 0.1448 0.1694 0.1188 -0.0048 -0.0315 -0.0027 230 ASN C CA  
6104 C  C   . ASN C 229 ? 0.1666 0.1633 0.1583 0.0253  -0.0153 -0.0027 230 ASN C C   
6105 O  O   . ASN C 229 ? 0.1644 0.1833 0.1466 -0.0046 -0.0187 0.0008  230 ASN C O   
6106 C  CB  . ASN C 229 ? 0.1605 0.1975 0.1301 0.0015  -0.0472 0.0065  230 ASN C CB  
6107 C  CG  . ASN C 229 ? 0.1671 0.2151 0.1973 -0.0015 -0.0412 0.0250  230 ASN C CG  
6108 O  OD1 . ASN C 229 ? 0.2240 0.2673 0.2287 -0.0052 -0.0803 -0.0046 230 ASN C OD1 
6109 N  ND2 . ASN C 229 ? 0.2143 0.1958 0.1791 -0.0405 -0.0544 -0.0116 230 ASN C ND2 
6110 N  N   . PHE C 230 ? 0.1360 0.1966 0.1186 -0.0355 -0.0172 0.0077  231 PHE C N   
6111 C  CA  . PHE C 230 ? 0.1700 0.1623 0.1360 0.0043  -0.0122 0.0450  231 PHE C CA  
6112 C  C   . PHE C 230 ? 0.1694 0.2186 0.1683 -0.0043 -0.0573 0.0240  231 PHE C C   
6113 O  O   . PHE C 230 ? 0.1870 0.2091 0.1714 0.0104  -0.0194 0.0417  231 PHE C O   
6114 C  CB  . PHE C 230 ? 0.1324 0.2215 0.1717 0.0113  -0.0204 0.0266  231 PHE C CB  
6115 C  CG  . PHE C 230 ? 0.1586 0.1696 0.1346 -0.0103 -0.0226 0.0244  231 PHE C CG  
6116 C  CD1 . PHE C 230 ? 0.1694 0.1585 0.1545 -0.0159 -0.0258 0.0184  231 PHE C CD1 
6117 C  CD2 . PHE C 230 ? 0.1793 0.1721 0.1817 -0.0131 -0.0386 0.0130  231 PHE C CD2 
6118 C  CE1 . PHE C 230 ? 0.1326 0.1506 0.1714 -0.0144 0.0006  0.0168  231 PHE C CE1 
6119 C  CE2 . PHE C 230 ? 0.1500 0.1473 0.1702 -0.0230 -0.0313 -0.0003 231 PHE C CE2 
6120 C  CZ  . PHE C 230 ? 0.1324 0.1538 0.1332 0.0003  0.0012  0.0003  231 PHE C CZ  
6121 N  N   . ASN C 231 ? 0.1423 0.2113 0.1443 -0.0149 -0.0454 0.0154  232 ASN C N   
6122 C  CA  . ASN C 231 ? 0.1793 0.1951 0.1764 0.0189  -0.0597 0.0310  232 ASN C CA  
6123 C  C   . ASN C 231 ? 0.1647 0.2398 0.1513 0.0098  -0.0178 0.0063  232 ASN C C   
6124 O  O   . ASN C 231 ? 0.1806 0.2165 0.1540 -0.0020 -0.0313 0.0137  232 ASN C O   
6125 C  CB  . ASN C 231 ? 0.2226 0.2319 0.1547 -0.0054 -0.0511 0.0220  232 ASN C CB  
6126 C  CG  . ASN C 231 ? 0.2129 0.2009 0.1833 0.0199  -0.0142 -0.0286 232 ASN C CG  
6127 O  OD1 . ASN C 231 ? 0.2168 0.1893 0.1929 -0.0370 -0.0619 0.0131  232 ASN C OD1 
6128 N  ND2 . ASN C 231 ? 0.2205 0.2538 0.1802 -0.0161 -0.0205 -0.0097 232 ASN C ND2 
6129 N  N   . GLY C 232 ? 0.2248 0.1902 0.1906 -0.0236 -0.0513 0.0230  233 GLY C N   
6130 C  CA  . GLY C 232 ? 0.2184 0.2682 0.2596 -0.0059 -0.0353 -0.0031 233 GLY C CA  
6131 C  C   . GLY C 232 ? 0.2021 0.1694 0.2240 0.0278  -0.0068 0.0306  233 GLY C C   
6132 O  O   . GLY C 232 ? 0.2430 0.2495 0.1723 0.0432  -0.0670 -0.0068 233 GLY C O   
6133 N  N   . GLU C 233 ? 0.2129 0.2324 0.1809 0.0063  -0.0196 0.0324  234 GLU C N   
6134 C  CA  . GLU C 233 ? 0.2393 0.2431 0.2104 0.0049  -0.0263 -0.0403 234 GLU C CA  
6135 C  C   . GLU C 233 ? 0.2014 0.2206 0.1985 0.0181  0.0020  -0.0078 234 GLU C C   
6136 O  O   . GLU C 233 ? 0.2204 0.2806 0.2743 -0.0210 -0.0527 0.0320  234 GLU C O   
6137 C  CB  . GLU C 233 ? 0.1782 0.2256 0.1993 -0.0194 -0.0463 -0.0054 234 GLU C CB  
6138 C  CG  . GLU C 233 ? 0.1865 0.2951 0.1814 -0.0171 -0.0684 0.0284  234 GLU C CG  
6139 C  CD  . GLU C 233 ? 0.2549 0.3600 0.3222 -0.0164 0.0419  -0.0030 234 GLU C CD  
6140 O  OE1 . GLU C 233 ? 0.3903 0.3661 0.3274 -0.0082 -0.0231 -0.0165 234 GLU C OE1 
6141 O  OE2 . GLU C 233 ? 0.2881 0.3723 0.3689 -0.0443 -0.0062 0.0463  234 GLU C OE2 
6142 N  N   . GLY C 234 ? 0.2412 0.2626 0.1985 0.0116  -0.0993 -0.0041 235 GLY C N   
6143 C  CA  . GLY C 234 ? 0.2937 0.3619 0.2079 -0.0498 -0.0074 -0.0851 235 GLY C CA  
6144 C  C   . GLY C 234 ? 0.2136 0.3919 0.2325 0.0335  -0.0361 0.0242  235 GLY C C   
6145 O  O   . GLY C 234 ? 0.3217 0.4585 0.2023 -0.0359 -0.1180 -0.0186 235 GLY C O   
6146 N  N   . GLU C 235 ? 0.2766 0.3458 0.1964 0.0116  -0.0762 0.0221  236 GLU C N   
6147 C  CA  . GLU C 235 ? 0.2476 0.2958 0.1553 -0.0110 -0.0288 0.0086  236 GLU C CA  
6148 C  C   . GLU C 235 ? 0.2465 0.3607 0.2894 0.0317  -0.1027 0.0294  236 GLU C C   
6149 O  O   . GLU C 235 ? 0.3407 0.3538 0.2017 0.0351  -0.0485 -0.0214 236 GLU C O   
6150 C  CB  . GLU C 235 ? 0.2759 0.2903 0.1951 0.0197  0.0051  -0.0566 236 GLU C CB  
6151 C  CG  . GLU C 235 ? 0.2515 0.3406 0.3488 -0.1147 -0.0939 0.0263  236 GLU C CG  
6152 C  CD  . GLU C 235 ? 0.3188 0.3312 0.3810 -0.0991 -0.1360 0.0640  236 GLU C CD  
6153 O  OE1 . GLU C 235 ? 0.3896 0.4325 0.2215 -0.0164 -0.0852 0.0311  236 GLU C OE1 
6154 O  OE2 . GLU C 235 ? 0.4241 0.4516 0.4280 0.0615  -0.1449 0.0992  236 GLU C OE2 
6155 N  N   . PRO C 236 ? 0.3161 0.2854 0.1691 0.0186  -0.0656 0.0276  237 PRO C N   
6156 C  CA  . PRO C 236 ? 0.3512 0.3325 0.1570 0.0474  -0.0546 0.0394  237 PRO C CA  
6157 C  C   . PRO C 236 ? 0.2669 0.3289 0.2118 -0.0288 -0.1151 0.0129  237 PRO C C   
6158 O  O   . PRO C 236 ? 0.2939 0.3000 0.1915 -0.0163 -0.0892 0.0007  237 PRO C O   
6159 C  CB  . PRO C 236 ? 0.2815 0.4388 0.1879 0.0015  -0.0690 0.0357  237 PRO C CB  
6160 C  CG  . PRO C 236 ? 0.3991 0.3801 0.2842 0.1439  -0.0493 0.0472  237 PRO C CG  
6161 C  CD  . PRO C 236 ? 0.3459 0.3975 0.2061 0.0573  0.0254  -0.0250 237 PRO C CD  
6162 N  N   . GLU C 237 ? 0.3558 0.2888 0.1622 0.0126  -0.0788 -0.0449 238 GLU C N   
6163 C  CA  . GLU C 237 ? 0.2363 0.2442 0.1604 -0.0137 -0.0450 0.0243  238 GLU C CA  
6164 C  C   . GLU C 237 ? 0.2669 0.1974 0.1685 0.0140  -0.0438 0.0207  238 GLU C C   
6165 O  O   . GLU C 237 ? 0.2096 0.2124 0.1920 -0.0103 -0.0133 -0.0148 238 GLU C O   
6166 C  CB  . GLU C 237 ? 0.2612 0.2556 0.2312 -0.0612 -0.0149 0.0093  238 GLU C CB  
6167 C  CG  . GLU C 237 ? 0.3323 0.4320 0.2084 -0.1035 0.0130  0.0165  238 GLU C CG  
6168 C  CD  . GLU C 237 ? 0.3768 0.3133 0.4104 -0.1014 0.0298  0.0088  238 GLU C CD  
6169 O  OE1 . GLU C 237 ? 0.4516 0.4138 0.5857 -0.1118 0.0780  -0.1481 238 GLU C OE1 
6170 O  OE2 . GLU C 237 ? 0.3172 0.3003 0.3424 -0.0984 -0.0878 -0.0434 238 GLU C OE2 
6171 N  N   . GLU C 238 ? 0.1967 0.2405 0.1583 -0.0174 -0.0310 -0.0057 239 GLU C N   
6172 C  CA  . GLU C 238 ? 0.1976 0.2766 0.1615 0.0229  -0.0210 0.0315  239 GLU C CA  
6173 C  C   . GLU C 238 ? 0.2025 0.1818 0.1554 -0.0035 -0.0544 -0.0114 239 GLU C C   
6174 O  O   . GLU C 238 ? 0.2393 0.1976 0.1805 -0.0013 -0.0551 0.0287  239 GLU C O   
6175 C  CB  . GLU C 238 ? 0.2951 0.2485 0.2152 -0.0329 -0.0284 0.0286  239 GLU C CB  
6176 C  CG  . GLU C 238 ? 0.3508 0.4458 0.2511 -0.0310 0.0156  0.0458  239 GLU C CG  
6177 C  CD  . GLU C 238 ? 0.3337 0.4391 0.3810 -0.0162 0.0997  0.1423  239 GLU C CD  
6178 O  OE1 . GLU C 238 ? 1.2310 0.8517 0.7386 -0.1762 0.0157  0.1411  239 GLU C OE1 
6179 O  OE2 . GLU C 238 ? 0.5770 0.8528 0.5105 -0.2617 -0.0423 0.1509  239 GLU C OE2 
6180 N  N   . LEU C 239 ? 0.1814 0.1998 0.1335 -0.0124 -0.0456 0.0068  240 LEU C N   
6181 C  CA  . LEU C 239 ? 0.1983 0.1840 0.1111 -0.0219 -0.0375 0.0092  240 LEU C CA  
6182 C  C   . LEU C 239 ? 0.1506 0.1836 0.1052 0.0086  -0.0186 0.0131  240 LEU C C   
6183 O  O   . LEU C 239 ? 0.1588 0.1944 0.1350 -0.0200 -0.0272 0.0089  240 LEU C O   
6184 C  CB  . LEU C 239 ? 0.1858 0.1545 0.1492 -0.0034 -0.0110 -0.0104 240 LEU C CB  
6185 C  CG  . LEU C 239 ? 0.1926 0.2084 0.1499 -0.0204 -0.0021 -0.0258 240 LEU C CG  
6186 C  CD1 . LEU C 239 ? 0.2560 0.1577 0.2646 -0.0156 0.0544  -0.0412 240 LEU C CD1 
6187 C  CD2 . LEU C 239 ? 0.1847 0.1899 0.1759 -0.0159 -0.0251 -0.0094 240 LEU C CD2 
6188 N  N   . MET C 240 ? 0.1296 0.1590 0.1220 0.0054  -0.0359 -0.0041 241 MET C N   
6189 C  CA  . MET C 240 ? 0.1441 0.1650 0.1368 0.0055  -0.0487 0.0000  241 MET C CA  
6190 C  C   . MET C 240 ? 0.1097 0.1384 0.0982 -0.0194 -0.0173 0.0035  241 MET C C   
6191 O  O   . MET C 240 ? 0.1269 0.1674 0.1195 -0.0010 -0.0115 0.0192  241 MET C O   
6192 C  CB  . MET C 240 ? 0.1597 0.1827 0.1238 0.0010  -0.0231 -0.0073 241 MET C CB  
6193 C  CG  . MET C 240 ? 0.1220 0.1827 0.1296 -0.0120 -0.0096 -0.0093 241 MET C CG  
6194 S  SD  . MET C 240 ? 0.1596 0.1547 0.1529 0.0006  -0.0204 0.0113  241 MET C SD  
6195 C  CE  . MET C 240 ? 0.1438 0.1768 0.1479 -0.0066 -0.0644 0.0405  241 MET C CE  
6196 N  N   . VAL C 241 ? 0.1129 0.1319 0.1292 -0.0105 -0.0272 0.0020  242 VAL C N   
6197 C  CA  . VAL C 241 ? 0.1152 0.1208 0.1229 0.0017  -0.0092 0.0006  242 VAL C CA  
6198 C  C   . VAL C 241 ? 0.1231 0.1217 0.1176 0.0005  -0.0163 0.0021  242 VAL C C   
6199 O  O   . VAL C 241 ? 0.1308 0.1448 0.1216 -0.0245 -0.0093 0.0133  242 VAL C O   
6200 C  CB  . VAL C 241 ? 0.1143 0.1358 0.1220 -0.0265 -0.0091 -0.0070 242 VAL C CB  
6201 C  CG1 . VAL C 241 ? 0.1188 0.1597 0.1691 -0.0138 -0.0105 0.0021  242 VAL C CG1 
6202 C  CG2 . VAL C 241 ? 0.1611 0.1430 0.1145 -0.0070 -0.0221 0.0015  242 VAL C CG2 
6203 N  N   . ASP C 242 ? 0.1027 0.1100 0.1080 -0.0155 -0.0284 -0.0083 243 ASP C N   
6204 C  CA  . ASP C 242 ? 0.1185 0.1159 0.0978 -0.0133 0.0111  -0.0164 243 ASP C CA  
6205 C  C   . ASP C 242 ? 0.1164 0.1124 0.0987 -0.0105 -0.0143 0.0027  243 ASP C C   
6206 O  O   . ASP C 242 ? 0.1448 0.1208 0.1145 -0.0087 0.0129  -0.0062 243 ASP C O   
6207 C  CB  . ASP C 242 ? 0.1118 0.1094 0.1179 0.0093  0.0102  -0.0010 243 ASP C CB  
6208 C  CG  . ASP C 242 ? 0.1362 0.1091 0.1199 -0.0114 -0.0122 0.0001  243 ASP C CG  
6209 O  OD1 . ASP C 242 ? 0.1281 0.1089 0.1229 -0.0040 -0.0111 -0.0163 243 ASP C OD1 
6210 O  OD2 . ASP C 242 ? 0.1768 0.1288 0.1351 -0.0161 -0.0038 -0.0173 243 ASP C OD2 
6211 N  N   . ASN C 243 ? 0.1237 0.0947 0.0900 -0.0230 -0.0127 -0.0102 244 ASN C N   
6212 C  CA  . ASN C 243 ? 0.1024 0.1143 0.1269 -0.0132 -0.0085 -0.0068 244 ASN C CA  
6213 C  C   . ASN C 243 ? 0.1005 0.1076 0.0956 0.0006  -0.0049 -0.0098 244 ASN C C   
6214 O  O   . ASN C 243 ? 0.1127 0.1080 0.1091 0.0131  -0.0177 -0.0080 244 ASN C O   
6215 C  CB  . ASN C 243 ? 0.1130 0.1190 0.1048 0.0088  -0.0020 -0.0015 244 ASN C CB  
6216 C  CG  . ASN C 243 ? 0.1283 0.1231 0.1124 -0.0178 -0.0060 0.0164  244 ASN C CG  
6217 O  OD1 . ASN C 243 ? 0.1475 0.1222 0.1107 0.0077  0.0003  0.0059  244 ASN C OD1 
6218 N  ND2 . ASN C 243 ? 0.1703 0.1730 0.1554 0.0221  0.0038  0.0362  244 ASN C ND2 
6219 N  N   . TRP C 244 ? 0.0957 0.0994 0.0954 -0.0093 -0.0107 0.0010  245 TRP C N   
6220 C  CA  . TRP C 244 ? 0.0859 0.0947 0.0913 -0.0204 -0.0087 0.0010  245 TRP C CA  
6221 C  C   . TRP C 244 ? 0.1142 0.1186 0.0970 -0.0071 0.0049  -0.0054 245 TRP C C   
6222 O  O   . TRP C 244 ? 0.1212 0.1170 0.1071 -0.0038 0.0035  -0.0131 245 TRP C O   
6223 C  CB  . TRP C 244 ? 0.0994 0.0870 0.1040 -0.0104 -0.0229 0.0003  245 TRP C CB  
6224 C  CG  . TRP C 244 ? 0.0920 0.0957 0.0827 0.0065  0.0027  0.0040  245 TRP C CG  
6225 C  CD1 . TRP C 244 ? 0.1137 0.0994 0.0788 -0.0031 -0.0086 -0.0076 245 TRP C CD1 
6226 C  CD2 . TRP C 244 ? 0.1028 0.0992 0.0956 0.0057  0.0063  0.0017  245 TRP C CD2 
6227 N  NE1 . TRP C 244 ? 0.1174 0.1032 0.1073 0.0046  -0.0074 -0.0155 245 TRP C NE1 
6228 C  CE2 . TRP C 244 ? 0.1170 0.0970 0.0994 0.0048  0.0138  0.0003  245 TRP C CE2 
6229 C  CE3 . TRP C 244 ? 0.1114 0.1243 0.1173 -0.0020 0.0065  0.0057  245 TRP C CE3 
6230 C  CZ2 . TRP C 244 ? 0.1199 0.1150 0.1364 0.0216  0.0077  0.0000  245 TRP C CZ2 
6231 C  CZ3 . TRP C 244 ? 0.1272 0.1405 0.1281 0.0038  0.0076  0.0000  245 TRP C CZ3 
6232 C  CH2 . TRP C 244 ? 0.1278 0.1342 0.1346 0.0168  0.0049  -0.0063 245 TRP C CH2 
6233 N  N   . ARG C 245 ? 0.0949 0.1089 0.0825 -0.0151 -0.0077 0.0121  246 ARG C N   
6234 C  CA  . ARG C 245 ? 0.1138 0.1039 0.1023 -0.0083 0.0100  0.0028  246 ARG C CA  
6235 C  C   . ARG C 245 ? 0.0881 0.1287 0.1133 -0.0102 0.0118  -0.0013 246 ARG C C   
6236 O  O   . ARG C 245 ? 0.1181 0.1217 0.1132 -0.0110 -0.0065 -0.0031 246 ARG C O   
6237 C  CB  . ARG C 245 ? 0.1098 0.1204 0.0962 -0.0264 0.0132  -0.0086 246 ARG C CB  
6238 C  CG  . ARG C 245 ? 0.1152 0.1015 0.1152 -0.0197 0.0326  -0.0115 246 ARG C CG  
6239 C  CD  . ARG C 245 ? 0.1425 0.0952 0.1125 -0.0155 0.0099  0.0131  246 ARG C CD  
6240 N  NE  . ARG C 245 ? 0.1373 0.1243 0.0991 -0.0197 0.0065  0.0054  246 ARG C NE  
6241 C  CZ  . ARG C 245 ? 0.1384 0.1238 0.1109 -0.0161 0.0092  -0.0063 246 ARG C CZ  
6242 N  NH1 . ARG C 245 ? 0.1430 0.1280 0.0949 -0.0277 0.0078  0.0065  246 ARG C NH1 
6243 N  NH2 . ARG C 245 ? 0.1428 0.1635 0.1347 -0.0297 0.0240  0.0076  246 ARG C NH2 
6244 N  N   . PRO C 246 ? 0.1062 0.1193 0.1190 -0.0012 -0.0133 -0.0070 247 PRO C N   
6245 C  CA  . PRO C 246 ? 0.0976 0.1145 0.1398 0.0133  -0.0154 -0.0087 247 PRO C CA  
6246 C  C   . PRO C 246 ? 0.1181 0.1128 0.1109 -0.0006 0.0071  -0.0020 247 PRO C C   
6247 O  O   . PRO C 246 ? 0.1220 0.1116 0.1140 -0.0104 0.0010  -0.0021 247 PRO C O   
6248 C  CB  . PRO C 246 ? 0.1427 0.1649 0.1585 0.0250  0.0005  -0.0386 247 PRO C CB  
6249 C  CG  . PRO C 246 ? 0.2574 0.2287 0.1838 0.0989  -0.0015 -0.0491 247 PRO C CG  
6250 C  CD  . PRO C 246 ? 0.1374 0.1628 0.1188 0.0197  0.0186  -0.0057 247 PRO C CD  
6251 N  N   . ALA C 247 ? 0.1179 0.1168 0.1156 0.0135  -0.0107 -0.0055 248 ALA C N   
6252 C  CA  . ALA C 247 ? 0.1211 0.1170 0.1358 -0.0087 -0.0078 0.0059  248 ALA C CA  
6253 C  C   . ALA C 247 ? 0.1127 0.1145 0.1283 0.0109  0.0003  -0.0118 248 ALA C C   
6254 O  O   . ALA C 247 ? 0.1261 0.1525 0.1571 0.0030  0.0057  -0.0359 248 ALA C O   
6255 C  CB  . ALA C 247 ? 0.1572 0.1541 0.1349 -0.0098 -0.0280 0.0160  248 ALA C CB  
6256 N  N   . GLN C 248 ? 0.1049 0.1134 0.1439 -0.0024 0.0127  -0.0054 249 GLN C N   
6257 C  CA  . GLN C 248 ? 0.1193 0.1254 0.1021 0.0063  0.0048  -0.0001 249 GLN C CA  
6258 C  C   . GLN C 248 ? 0.1256 0.1116 0.1233 0.0096  0.0085  -0.0024 249 GLN C C   
6259 O  O   . GLN C 248 ? 0.1349 0.1432 0.1348 0.0043  -0.0037 -0.0229 249 GLN C O   
6260 C  CB  . GLN C 248 ? 0.1129 0.1185 0.1272 0.0020  -0.0027 -0.0164 249 GLN C CB  
6261 C  CG  . GLN C 248 ? 0.1317 0.1412 0.1202 -0.0080 -0.0298 0.0054  249 GLN C CG  
6262 C  CD  . GLN C 248 ? 0.1448 0.1640 0.1202 -0.0144 0.0049  0.0197  249 GLN C CD  
6263 O  OE1 . GLN C 248 ? 0.1639 0.1951 0.1580 -0.0308 0.0205  0.0086  249 GLN C OE1 
6264 N  NE2 . GLN C 248 ? 0.1365 0.1536 0.1231 -0.0096 -0.0017 -0.0051 249 GLN C NE2 
6265 N  N   . PRO C 249 ? 0.1323 0.1782 0.1680 -0.0023 0.0063  0.0054  250 PRO C N   
6266 C  CA  . PRO C 249 ? 0.1421 0.1976 0.1708 0.0165  0.0057  -0.0489 250 PRO C CA  
6267 C  C   . PRO C 249 ? 0.1233 0.1362 0.1734 -0.0100 0.0208  -0.0109 250 PRO C C   
6268 O  O   . PRO C 249 ? 0.1409 0.1633 0.1624 0.0115  0.0209  -0.0216 250 PRO C O   
6269 C  CB  . PRO C 249 ? 0.1967 0.3203 0.1957 -0.0214 0.0608  -0.1159 250 PRO C CB  
6270 C  CG  . PRO C 249 ? 0.1635 0.3248 0.2606 -0.0076 0.0342  -0.0727 250 PRO C CG  
6271 C  CD  . PRO C 249 ? 0.1395 0.2460 0.1531 -0.0013 0.0245  -0.0240 250 PRO C CD  
6272 N  N   . LEU C 250 ? 0.1342 0.1608 0.1782 0.0122  -0.0007 -0.0344 251 LEU C N   
6273 C  CA  . LEU C 250 ? 0.1437 0.1870 0.1280 -0.0065 -0.0436 -0.0034 251 LEU C CA  
6274 C  C   . LEU C 250 ? 0.1486 0.1793 0.2009 0.0099  0.0127  -0.0192 251 LEU C C   
6275 O  O   . LEU C 250 ? 0.1244 0.1671 0.2021 0.0098  0.0012  -0.0297 251 LEU C O   
6276 C  CB  . LEU C 250 ? 0.1339 0.1786 0.1725 0.0258  -0.0195 0.0085  251 LEU C CB  
6277 C  CG  . LEU C 250 ? 0.1814 0.1920 0.1620 -0.0197 -0.0229 0.0063  251 LEU C CG  
6278 C  CD1 . LEU C 250 ? 0.1578 0.2020 0.2064 -0.0164 -0.0318 -0.0102 251 LEU C CD1 
6279 C  CD2 . LEU C 250 ? 0.1824 0.2373 0.2222 0.0133  -0.0276 0.0339  251 LEU C CD2 
6280 N  N   . LYS C 251 ? 0.1421 0.1955 0.2108 -0.0110 0.0275  -0.0076 252 LYS C N   
6281 C  CA  . LYS C 251 ? 0.1058 0.1965 0.2192 0.0098  0.0066  -0.0164 252 LYS C CA  
6282 C  C   . LYS C 251 ? 0.1834 0.2048 0.2342 0.0186  0.0282  -0.0373 252 LYS C C   
6283 O  O   . LYS C 251 ? 0.2267 0.2949 0.2447 0.0181  -0.0271 -0.0099 252 LYS C O   
6284 C  CB  . LYS C 251 ? 0.1935 0.2029 0.2275 -0.0034 0.0317  -0.0001 252 LYS C CB  
6285 C  CG  . LYS C 251 ? 0.2488 0.2271 0.2890 -0.0397 -0.0007 -0.0240 252 LYS C CG  
6286 C  CD  . LYS C 251 ? 0.3136 0.3411 0.2662 -0.0177 0.0148  -0.0452 252 LYS C CD  
6287 C  CE  . LYS C 251 ? 0.3413 0.2989 0.2524 0.0083  0.0205  -0.0645 252 LYS C CE  
6288 N  NZ  . LYS C 251 ? 0.3298 0.3474 0.3919 0.0368  0.0649  -0.0208 252 LYS C NZ  
6289 N  N   . ASN C 252 ? 0.1298 0.2169 0.2030 0.0013  0.0222  -0.0375 253 ASN C N   
6290 C  CA  . ASN C 252 ? 0.2151 0.4451 0.2619 -0.0719 -0.0189 -0.0364 253 ASN C CA  
6291 C  C   . ASN C 252 ? 0.2890 0.5256 0.3406 -0.1469 0.0346  -0.1532 253 ASN C C   
6292 O  O   . ASN C 252 ? 0.2861 0.6112 0.4020 0.0964  -0.0621 -0.1028 253 ASN C O   
6293 C  CB  . ASN C 252 ? 0.3549 0.4040 0.3711 -0.0798 0.0978  0.0020  253 ASN C CB  
6294 C  CG  . ASN C 252 ? 0.2736 0.5906 0.9951 -0.1181 0.1106  0.1230  253 ASN C CG  
6295 O  OD1 . ASN C 252 ? 0.3086 0.6608 0.8264 -0.1316 0.0267  0.1597  253 ASN C OD1 
6296 N  ND2 . ASN C 252 ? 0.9812 0.7354 1.1835 -0.2662 -0.3226 -0.0291 253 ASN C ND2 
6297 N  N   . ARG C 253 ? 0.1493 0.2980 0.1825 0.0373  -0.0153 0.0035  254 ARG C N   
6298 C  CA  . ARG C 253 ? 0.1290 0.1911 0.1730 -0.0164 -0.0186 -0.0263 254 ARG C CA  
6299 C  C   . ARG C 253 ? 0.1743 0.1793 0.1984 -0.0065 -0.0296 -0.0140 254 ARG C C   
6300 O  O   . ARG C 253 ? 0.2619 0.1951 0.2183 0.0339  -0.0741 -0.0124 254 ARG C O   
6301 C  CB  . ARG C 253 ? 0.1221 0.1759 0.1790 -0.0068 -0.0203 -0.0005 254 ARG C CB  
6302 C  CG  . ARG C 253 ? 0.1094 0.1392 0.2009 -0.0125 -0.0157 -0.0252 254 ARG C CG  
6303 C  CD  . ARG C 253 ? 0.1059 0.1474 0.1747 0.0005  -0.0170 -0.0236 254 ARG C CD  
6304 N  NE  . ARG C 253 ? 0.1174 0.1342 0.1754 0.0043  -0.0219 -0.0230 254 ARG C NE  
6305 C  CZ  . ARG C 253 ? 0.0985 0.1184 0.1274 0.0005  -0.0109 -0.0096 254 ARG C CZ  
6306 N  NH1 . ARG C 253 ? 0.1057 0.1152 0.1253 0.0179  0.0181  -0.0030 254 ARG C NH1 
6307 N  NH2 . ARG C 253 ? 0.1152 0.1221 0.1362 -0.0126 -0.0049 -0.0177 254 ARG C NH2 
6308 N  N   . GLN C 254 ? 0.1429 0.1831 0.1949 -0.0337 -0.0216 -0.0276 255 GLN C N   
6309 C  CA  . GLN C 254 ? 0.1802 0.2499 0.2159 -0.0206 -0.0189 -0.0152 255 GLN C CA  
6310 C  C   . GLN C 254 ? 0.1538 0.1975 0.2442 0.0201  0.0135  0.0057  255 GLN C C   
6311 O  O   . GLN C 254 ? 0.2060 0.1917 0.2987 0.0031  0.0125  -0.0063 255 GLN C O   
6312 C  CB  . GLN C 254 ? 0.2745 0.3244 0.2398 -0.0251 -0.0680 -0.0339 255 GLN C CB  
6313 C  CG  . GLN C 254 ? 0.3754 0.5332 0.3258 -0.0597 -0.0582 0.0074  255 GLN C CG  
6314 C  CD  . GLN C 254 ? 0.4456 0.7803 0.7146 -0.0851 -0.4984 -0.1679 255 GLN C CD  
6315 O  OE1 . GLN C 254 ? 0.6219 1.2684 1.2067 -0.0992 -0.5562 0.2802  255 GLN C OE1 
6316 N  NE2 . GLN C 254 ? 0.6459 1.0959 1.0556 0.0842  -0.1553 0.0107  255 GLN C NE2 
6317 N  N   . ILE C 255 ? 0.1362 0.1649 0.1472 0.0140  -0.0116 0.0046  256 ILE C N   
6318 C  CA  . ILE C 255 ? 0.1335 0.1725 0.1592 0.0000  -0.0149 -0.0438 256 ILE C CA  
6319 C  C   . ILE C 255 ? 0.1714 0.1666 0.1463 0.0405  -0.0318 -0.0284 256 ILE C C   
6320 O  O   . ILE C 255 ? 0.1511 0.1574 0.1671 0.0238  -0.0273 -0.0164 256 ILE C O   
6321 C  CB  . ILE C 255 ? 0.1420 0.1580 0.1396 -0.0164 -0.0120 -0.0207 256 ILE C CB  
6322 C  CG1 . ILE C 255 ? 0.1775 0.1500 0.1218 0.0120  0.0037  -0.0509 256 ILE C CG1 
6323 C  CG2 . ILE C 255 ? 0.1423 0.1793 0.2097 -0.0027 -0.0241 -0.0194 256 ILE C CG2 
6324 C  CD1 . ILE C 255 ? 0.1843 0.1755 0.1728 -0.0463 -0.0140 -0.0048 256 ILE C CD1 
6325 N  N   . LYS C 256 ? 0.1446 0.1676 0.1337 0.0309  -0.0223 -0.0137 257 LYS C N   
6326 C  CA  . LYS C 256 ? 0.1362 0.1490 0.1351 0.0375  -0.0092 -0.0125 257 LYS C CA  
6327 C  C   . LYS C 256 ? 0.1517 0.1644 0.1396 0.0131  -0.0157 0.0102  257 LYS C C   
6328 O  O   . LYS C 256 ? 0.1581 0.1958 0.1613 0.0027  -0.0560 0.0401  257 LYS C O   
6329 C  CB  . LYS C 256 ? 0.1877 0.1844 0.2134 -0.0038 -0.0621 -0.0485 257 LYS C CB  
6330 C  CG  . LYS C 256 ? 0.2682 0.2680 0.2402 -0.0923 -0.0423 -0.0631 257 LYS C CG  
6331 C  CD  . LYS C 256 ? 0.3465 0.2867 0.4340 -0.1435 -0.0003 -0.0671 257 LYS C CD  
6332 C  CE  . LYS C 256 ? 0.4061 0.4410 0.7335 -0.2122 0.0577  -0.0548 257 LYS C CE  
6333 N  NZ  . LYS C 256 ? 0.6065 0.5346 0.3614 0.0110  0.0205  0.0274  257 LYS C NZ  
6334 N  N   . ALA C 257 ? 0.1667 0.1824 0.1206 0.0370  -0.0328 0.0110  258 ALA C N   
6335 C  CA  . ALA C 257 ? 0.1428 0.2003 0.1279 0.0436  -0.0239 -0.0032 258 ALA C CA  
6336 C  C   . ALA C 257 ? 0.1549 0.1847 0.1619 0.0087  -0.0419 -0.0311 258 ALA C C   
6337 O  O   . ALA C 257 ? 0.1718 0.2350 0.1606 0.0078  -0.0763 -0.0220 258 ALA C O   
6338 C  CB  . ALA C 257 ? 0.2120 0.1881 0.1439 0.0579  -0.0313 -0.0130 258 ALA C CB  
6339 N  N   . SER C 258 ? 0.1619 0.1659 0.1499 0.0281  -0.0203 -0.0038 259 SER C N   
6340 C  CA  . SER C 258 ? 0.2251 0.2120 0.1547 0.0491  -0.0361 -0.0093 259 SER C CA  
6341 C  C   . SER C 258 ? 0.2001 0.2077 0.1492 0.0070  -0.0318 0.0081  259 SER C C   
6342 O  O   . SER C 258 ? 0.2511 0.2980 0.1879 0.0291  -0.0187 -0.0351 259 SER C O   
6343 C  CB  . SER C 258 ? 0.1777 0.1736 0.1974 -0.0038 -0.0361 -0.0028 259 SER C CB  
6344 O  OG  . SER C 258 ? 0.1777 0.1648 0.1251 0.0023  -0.0230 0.0020  259 SER C OG  
6345 N  N   . PHE C 259 ? 0.2183 0.2308 0.1547 -0.0024 -0.0401 0.0199  260 PHE C N   
6346 C  CA  . PHE C 259 ? 0.3176 0.2669 0.1796 0.0108  -0.0168 0.0564  260 PHE C CA  
6347 C  C   . PHE C 259 ? 0.2842 0.2781 0.1913 0.0041  -0.0370 0.0461  260 PHE C C   
6348 O  O   . PHE C 259 ? 0.2761 0.2552 0.2709 0.0763  -0.0190 0.0675  260 PHE C O   
6349 C  CB  . PHE C 259 ? 0.2926 0.2700 0.1662 -0.0077 -0.0066 0.0085  260 PHE C CB  
6350 C  CG  . PHE C 259 ? 0.3152 0.2246 0.1836 0.0661  -0.0214 -0.0051 260 PHE C CG  
6351 C  CD1 . PHE C 259 ? 0.2175 0.2357 0.1782 0.0251  -0.0207 0.0126  260 PHE C CD1 
6352 C  CD2 . PHE C 259 ? 0.4007 0.2109 0.2342 0.0485  -0.0299 0.0320  260 PHE C CD2 
6353 C  CE1 . PHE C 259 ? 0.2490 0.2080 0.1845 0.0179  0.0044  -0.0046 260 PHE C CE1 
6354 C  CE2 . PHE C 259 ? 0.3504 0.2411 0.2057 0.0142  0.0289  0.0384  260 PHE C CE2 
6355 C  CZ  . PHE C 259 ? 0.3000 0.1971 0.2129 0.0000  -0.0425 0.0030  260 PHE C CZ  
6356 N  N   . LYS C 260 ? 0.4700 0.4445 0.2926 -0.0241 -0.1425 0.1953  261 LYS C N   
6357 C  CA  . LYS C 260 ? 0.4337 0.4618 0.4196 0.0401  -0.1730 0.0683  261 LYS C CA  
6358 C  C   . LYS C 260 ? 0.4226 0.5181 0.5770 0.2006  0.1149  -0.0608 261 LYS C C   
6359 O  O   . LYS C 260 ? 0.9255 0.8633 0.5115 -0.0151 0.0027  0.2249  261 LYS C O   
6360 C  CB  . LYS C 260 ? 0.7487 0.5067 0.4837 -0.1700 -0.0267 0.1351  261 LYS C CB  
6361 N  N   . HIS D 3   ? 0.3375 0.3341 0.3010 0.0000  0.0758  -0.0623 3   HIS D N   
6362 C  CA  . HIS D 3   ? 0.4841 0.5383 0.3328 0.1721  0.0555  -0.0821 3   HIS D CA  
6363 C  C   . HIS D 3   ? 0.5248 0.5217 0.4555 0.0562  -0.0776 0.0184  3   HIS D C   
6364 O  O   . HIS D 3   ? 0.4973 0.5992 0.6291 -0.1146 0.0597  0.1544  3   HIS D O   
6365 C  CB  . HIS D 3   ? 0.3571 0.4506 0.4362 0.0962  0.1665  0.1327  3   HIS D CB  
6366 C  CG  . HIS D 3   ? 0.3917 0.4167 0.4763 0.0608  0.0015  0.0778  3   HIS D CG  
6367 N  ND1 . HIS D 3   ? 0.3961 0.4666 0.4880 -0.0196 -0.0031 -0.0103 3   HIS D ND1 
6368 C  CD2 . HIS D 3   ? 0.3064 0.3729 0.2976 0.0751  0.0825  0.0408  3   HIS D CD2 
6369 C  CE1 . HIS D 3   ? 0.5138 0.5113 0.2651 -0.0421 0.0335  0.1107  3   HIS D CE1 
6370 N  NE2 . HIS D 3   ? 0.3908 0.4332 0.3176 0.0364  -0.1121 0.1371  3   HIS D NE2 
6371 N  N   . HIS D 4   ? 0.9759 0.5643 0.2413 0.0808  0.0174  0.0625  4   HIS D N   
6372 C  CA  . HIS D 4   ? 0.5393 0.3571 0.3510 0.1569  -0.0527 0.0586  4   HIS D CA  
6373 C  C   . HIS D 4   ? 0.2978 0.2847 0.2305 -0.0366 -0.0562 0.0089  4   HIS D C   
6374 O  O   . HIS D 4   ? 0.3145 0.2743 0.1492 0.0094  -0.0408 0.0269  4   HIS D O   
6375 C  CB  . HIS D 4   ? 0.7437 0.4365 0.2736 0.2440  -0.0017 0.0187  4   HIS D CB  
6376 C  CG  . HIS D 4   ? 0.8794 0.6700 0.6122 -0.0812 0.1579  0.0698  4   HIS D CG  
6377 N  ND1 . HIS D 4   ? 1.1098 0.8962 0.7506 0.0667  -0.0057 -0.0524 4   HIS D ND1 
6378 C  CD2 . HIS D 4   ? 0.6141 0.6348 0.4991 0.1651  0.1915  0.0152  4   HIS D CD2 
6379 C  CE1 . HIS D 4   ? 0.9744 0.8869 0.9593 0.2056  -0.1474 -0.4747 4   HIS D CE1 
6380 N  NE2 . HIS D 4   ? 1.0224 0.6432 1.1708 0.0489  -0.1572 0.0057  4   HIS D NE2 
6381 N  N   . TRP D 5   ? 0.3257 0.2551 0.1493 0.0359  -0.0093 -0.0085 5   TRP D N   
6382 C  CA  . TRP D 5   ? 0.2425 0.1639 0.1800 -0.0006 0.0006  0.0148  5   TRP D CA  
6383 C  C   . TRP D 5   ? 0.1993 0.2184 0.1444 -0.0054 -0.0270 -0.0192 5   TRP D C   
6384 O  O   . TRP D 5   ? 0.2389 0.2035 0.1377 0.0149  -0.0015 0.0200  5   TRP D O   
6385 C  CB  . TRP D 5   ? 0.2976 0.1944 0.1576 -0.0091 0.0186  -0.0102 5   TRP D CB  
6386 C  CG  . TRP D 5   ? 0.2513 0.1978 0.1678 0.0240  0.0266  0.0137  5   TRP D CG  
6387 C  CD1 . TRP D 5   ? 0.3346 0.2122 0.1648 0.0395  0.0073  0.0315  5   TRP D CD1 
6388 C  CD2 . TRP D 5   ? 0.2240 0.1852 0.1646 -0.0230 -0.0164 -0.0003 5   TRP D CD2 
6389 N  NE1 . TRP D 5   ? 0.2260 0.1976 0.1885 0.0320  -0.0199 0.0049  5   TRP D NE1 
6390 C  CE2 . TRP D 5   ? 0.2815 0.1914 0.1536 0.0104  -0.0156 -0.0031 5   TRP D CE2 
6391 C  CE3 . TRP D 5   ? 0.1825 0.1818 0.1114 -0.0168 -0.0351 -0.0088 5   TRP D CE3 
6392 C  CZ2 . TRP D 5   ? 0.2208 0.2073 0.2066 -0.0013 0.0167  0.0003  5   TRP D CZ2 
6393 C  CZ3 . TRP D 5   ? 0.1508 0.1975 0.1495 -0.0331 -0.0037 -0.0362 5   TRP D CZ3 
6394 C  CH2 . TRP D 5   ? 0.1905 0.2073 0.1578 0.0038  -0.0241 -0.0295 5   TRP D CH2 
6395 N  N   . GLY D 6   ? 0.2370 0.1805 0.1533 0.0024  0.0049  -0.0211 6   GLY D N   
6396 C  CA  . GLY D 6   ? 0.2149 0.2248 0.1597 -0.0222 -0.0250 -0.0207 6   GLY D CA  
6397 C  C   . GLY D 6   ? 0.1834 0.1908 0.1383 -0.0140 0.0104  -0.0390 6   GLY D C   
6398 O  O   . GLY D 6   ? 0.1806 0.2044 0.1394 -0.0044 0.0126  0.0081  6   GLY D O   
6399 N  N   . TYR D 7   ? 0.2466 0.1759 0.1112 -0.0283 -0.0046 -0.0071 7   TYR D N   
6400 C  CA  . TYR D 7   ? 0.2321 0.1635 0.1395 -0.0157 0.0129  0.0027  7   TYR D CA  
6401 C  C   . TYR D 7   ? 0.2865 0.2066 0.1822 0.0068  0.0052  -0.0346 7   TYR D C   
6402 O  O   . TYR D 7   ? 0.3350 0.2418 0.1626 -0.0038 0.0007  -0.0164 7   TYR D O   
6403 C  CB  . TYR D 7   ? 0.2123 0.1886 0.1295 -0.0212 0.0085  -0.0080 7   TYR D CB  
6404 C  CG  . TYR D 7   ? 0.1813 0.1684 0.1152 -0.0359 -0.0034 0.0161  7   TYR D CG  
6405 C  CD1 . TYR D 7   ? 0.1285 0.1750 0.1177 -0.0096 0.0346  -0.0129 7   TYR D CD1 
6406 C  CD2 . TYR D 7   ? 0.2323 0.1657 0.1680 -0.0184 -0.0187 0.0003  7   TYR D CD2 
6407 C  CE1 . TYR D 7   ? 0.1551 0.1364 0.1181 -0.0141 0.0416  0.0023  7   TYR D CE1 
6408 C  CE2 . TYR D 7   ? 0.1838 0.1867 0.1366 -0.0375 -0.0153 0.0211  7   TYR D CE2 
6409 C  CZ  . TYR D 7   ? 0.1289 0.1527 0.1186 -0.0156 0.0229  0.0027  7   TYR D CZ  
6410 O  OH  . TYR D 7   ? 0.2020 0.1455 0.1404 -0.0129 -0.0137 -0.0121 7   TYR D OH  
6411 N  N   . GLY D 8   ? 0.3176 0.2427 0.1820 -0.0373 -0.0097 -0.0518 8   GLY D N   
6412 C  CA  . GLY D 8   ? 0.2763 0.2072 0.1685 -0.0511 0.0265  -0.0294 8   GLY D CA  
6413 C  C   . GLY D 8   ? 0.2646 0.2547 0.1771 -0.0216 -0.0017 -0.0114 8   GLY D C   
6414 O  O   . GLY D 8   ? 0.3077 0.2524 0.1247 -0.0172 -0.0207 -0.0159 8   GLY D O   
6415 N  N   . LYS D 9   ? 0.3039 0.2305 0.2028 -0.0505 0.0509  -0.0173 9   LYS D N   
6416 C  CA  . LYS D 9   ? 0.3449 0.2389 0.2615 -0.0491 0.0671  -0.0010 9   LYS D CA  
6417 C  C   . LYS D 9   ? 0.2282 0.2066 0.1511 -0.0430 0.0001  -0.0357 9   LYS D C   
6418 O  O   . LYS D 9   ? 0.2601 0.2324 0.1538 0.0234  0.0062  0.0097  9   LYS D O   
6419 C  CB  . LYS D 9   ? 0.3402 0.2651 0.2389 -0.0104 0.0373  -0.0361 9   LYS D CB  
6420 C  CG  . LYS D 9   ? 0.3404 0.2872 0.3671 -0.0383 0.0059  -0.0634 9   LYS D CG  
6421 C  CD  . LYS D 9   ? 0.6344 0.4618 0.4790 0.0662  -0.0153 -0.1948 9   LYS D CD  
6422 C  CE  . LYS D 9   ? 0.7475 0.6500 0.4912 0.1559  0.1349  -0.0749 9   LYS D CE  
6423 N  NZ  . LYS D 9   ? 0.6902 0.6154 0.6478 0.1415  0.0388  -0.2140 9   LYS D NZ  
6424 N  N   . HIS D 10  ? 0.3021 0.1908 0.1734 -0.0164 -0.0103 -0.0331 10  HIS D N   
6425 C  CA  . HIS D 10  ? 0.2422 0.2168 0.1520 -0.0226 -0.0258 -0.0023 10  HIS D CA  
6426 C  C   . HIS D 10  ? 0.2649 0.2158 0.1558 -0.0208 0.0037  -0.0153 10  HIS D C   
6427 O  O   . HIS D 10  ? 0.2509 0.2258 0.1567 0.0176  0.0146  -0.0286 10  HIS D O   
6428 C  CB  . HIS D 10  ? 0.2242 0.2057 0.1518 0.0263  -0.0282 -0.0331 10  HIS D CB  
6429 C  CG  . HIS D 10  ? 0.2237 0.2141 0.1626 0.0168  0.0205  0.0082  10  HIS D CG  
6430 N  ND1 . HIS D 10  ? 0.2739 0.2330 0.1667 0.0133  0.0366  -0.0032 10  HIS D ND1 
6431 C  CD2 . HIS D 10  ? 0.2443 0.2131 0.1481 -0.0148 -0.0193 -0.0038 10  HIS D CD2 
6432 C  CE1 . HIS D 10  ? 0.2590 0.2396 0.2445 0.0187  -0.0003 -0.0711 10  HIS D CE1 
6433 N  NE2 . HIS D 10  ? 0.2443 0.2440 0.1795 0.0107  0.0153  -0.0003 10  HIS D NE2 
6434 N  N   . ASN D 11  ? 0.2215 0.1863 0.1611 0.0294  0.0012  -0.0108 11  ASN D N   
6435 C  CA  . ASN D 11  ? 0.2353 0.1683 0.1421 0.0087  -0.0263 0.0074  11  ASN D CA  
6436 C  C   . ASN D 11  ? 0.2632 0.1798 0.1339 0.0252  0.0137  0.0142  11  ASN D C   
6437 O  O   . ASN D 11  ? 0.2696 0.2017 0.1272 0.0421  0.0127  0.0003  11  ASN D O   
6438 C  CB  . ASN D 11  ? 0.2064 0.1939 0.1114 -0.0044 -0.0178 -0.0040 11  ASN D CB  
6439 C  CG  . ASN D 11  ? 0.2285 0.2041 0.1587 0.0119  0.0154  -0.0337 11  ASN D CG  
6440 O  OD1 . ASN D 11  ? 0.2737 0.2465 0.1928 0.0043  0.0251  0.0196  11  ASN D OD1 
6441 N  ND2 . ASN D 11  ? 0.1996 0.2685 0.2102 0.0142  -0.0093 0.0059  11  ASN D ND2 
6442 N  N   . GLY D 12  ? 0.2230 0.1816 0.0978 -0.0005 0.0028  0.0031  12  GLY D N   
6443 C  CA  . GLY D 12  ? 0.2174 0.2239 0.0953 0.0152  -0.0006 -0.0020 12  GLY D CA  
6444 C  C   . GLY D 12  ? 0.2154 0.1637 0.1213 -0.0121 -0.0041 -0.0071 12  GLY D C   
6445 O  O   . GLY D 12  ? 0.2091 0.1642 0.1316 0.0133  0.0066  0.0001  12  GLY D O   
6446 N  N   . PRO D 13  ? 0.1762 0.1777 0.1037 0.0043  0.0087  0.0054  13  PRO D N   
6447 C  CA  . PRO D 13  ? 0.1984 0.1538 0.1231 -0.0041 0.0052  0.0142  13  PRO D CA  
6448 C  C   . PRO D 13  ? 0.2088 0.2143 0.1103 -0.0283 -0.0024 0.0078  13  PRO D C   
6449 O  O   . PRO D 13  ? 0.2398 0.1883 0.0957 -0.0237 0.0206  -0.0028 13  PRO D O   
6450 C  CB  . PRO D 13  ? 0.2355 0.1942 0.1129 -0.0560 -0.0038 0.0259  13  PRO D CB  
6451 C  CG  . PRO D 13  ? 0.1953 0.2111 0.1204 0.0000  -0.0049 -0.0147 13  PRO D CG  
6452 C  CD  . PRO D 13  ? 0.2262 0.1933 0.1308 -0.0412 0.0120  -0.0263 13  PRO D CD  
6453 N  N   . GLU D 14  ? 0.2181 0.1567 0.1486 0.0177  -0.0074 0.0174  14  GLU D N   
6454 C  CA  . GLU D 14  ? 0.2436 0.1793 0.1702 0.0419  0.0065  0.0171  14  GLU D CA  
6455 C  C   . GLU D 14  ? 0.1680 0.1590 0.1500 0.0015  0.0071  -0.0098 14  GLU D C   
6456 O  O   . GLU D 14  ? 0.2251 0.2063 0.1588 0.0211  0.0231  -0.0049 14  GLU D O   
6457 C  CB  . GLU D 14  ? 0.2748 0.1933 0.2483 0.0690  0.0571  0.0368  14  GLU D CB  
6458 C  CG  . GLU D 14  ? 0.3991 0.1563 0.3420 0.0007  0.0087  0.0676  14  GLU D CG  
6459 C  CD  . GLU D 14  ? 0.4485 0.6355 0.4440 -0.0489 -0.0493 0.0670  14  GLU D CD  
6460 O  OE1 . GLU D 14  ? 0.4326 0.4413 0.4088 0.0017  0.0313  0.0632  14  GLU D OE1 
6461 O  OE2 . GLU D 14  ? 0.5177 0.5274 0.4987 0.1319  0.0300  -0.0136 14  GLU D OE2 
6462 N  N   . HIS D 15  ? 0.1985 0.1518 0.1172 0.0081  0.0040  -0.0196 15  HIS D N   
6463 C  CA  . HIS D 15  ? 0.2450 0.1653 0.1378 0.0015  0.0017  0.0121  15  HIS D CA  
6464 C  C   . HIS D 15  ? 0.2887 0.1683 0.1009 -0.0065 0.0326  -0.0311 15  HIS D C   
6465 O  O   . HIS D 15  ? 0.2245 0.1658 0.1216 -0.0003 0.0285  -0.0066 15  HIS D O   
6466 C  CB  . HIS D 15  ? 0.2481 0.1777 0.1570 0.0104  -0.0097 -0.0130 15  HIS D CB  
6467 C  CG  . HIS D 15  ? 0.2445 0.1991 0.1107 0.0111  0.0041  -0.0010 15  HIS D CG  
6468 N  ND1 . HIS D 15  ? 0.2865 0.2120 0.1259 0.0248  0.0059  -0.0038 15  HIS D ND1 
6469 C  CD2 . HIS D 15  ? 0.2504 0.2093 0.1673 0.0155  -0.0250 -0.0375 15  HIS D CD2 
6470 C  CE1 . HIS D 15  ? 0.1935 0.2000 0.2240 0.0125  0.0126  -0.0254 15  HIS D CE1 
6471 N  NE2 . HIS D 15  ? 0.2585 0.2136 0.1614 0.0073  0.0173  -0.0299 15  HIS D NE2 
6472 N  N   . TRP D 16  ? 0.2188 0.1533 0.0992 0.0115  0.0320  -0.0291 16  TRP D N   
6473 C  CA  . TRP D 16  ? 0.2072 0.1504 0.0864 -0.0076 0.0236  -0.0302 16  TRP D CA  
6474 C  C   . TRP D 16  ? 0.1656 0.1466 0.0825 0.0078  0.0276  -0.0041 16  TRP D C   
6475 O  O   . TRP D 16  ? 0.2118 0.1504 0.1032 0.0094  0.0337  -0.0051 16  TRP D O   
6476 C  CB  . TRP D 16  ? 0.1863 0.1738 0.0852 -0.0159 0.0228  0.0010  16  TRP D CB  
6477 C  CG  . TRP D 16  ? 0.1533 0.1635 0.1213 -0.0113 0.0031  0.0126  16  TRP D CG  
6478 C  CD1 . TRP D 16  ? 0.1540 0.1475 0.1583 -0.0129 -0.0252 -0.0115 16  TRP D CD1 
6479 C  CD2 . TRP D 16  ? 0.1816 0.1587 0.1084 -0.0089 0.0221  -0.0046 16  TRP D CD2 
6480 N  NE1 . TRP D 16  ? 0.1816 0.1558 0.0992 -0.0197 -0.0082 0.0005  16  TRP D NE1 
6481 C  CE2 . TRP D 16  ? 0.1606 0.1791 0.0989 0.0155  -0.0073 0.0027  16  TRP D CE2 
6482 C  CE3 . TRP D 16  ? 0.1946 0.1373 0.1137 -0.0361 0.0080  0.0013  16  TRP D CE3 
6483 C  CZ2 . TRP D 16  ? 0.2318 0.1466 0.1220 -0.0421 0.0258  0.0098  16  TRP D CZ2 
6484 C  CZ3 . TRP D 16  ? 0.1915 0.1696 0.1173 -0.0028 0.0348  -0.0041 16  TRP D CZ3 
6485 C  CH2 . TRP D 16  ? 0.1960 0.1764 0.1495 0.0003  -0.0188 -0.0241 16  TRP D CH2 
6486 N  N   . HIS D 17  ? 0.1720 0.1763 0.1089 -0.0024 0.0304  -0.0034 17  HIS D N   
6487 C  CA  . HIS D 17  ? 0.1642 0.1932 0.1425 0.0032  0.0168  0.0141  17  HIS D CA  
6488 C  C   . HIS D 17  ? 0.2125 0.2197 0.1355 -0.0362 0.0298  0.0017  17  HIS D C   
6489 O  O   . HIS D 17  ? 0.2217 0.1974 0.0980 0.0063  0.0142  0.0034  17  HIS D O   
6490 C  CB  . HIS D 17  ? 0.1941 0.1899 0.1283 0.0186  0.0099  -0.0093 17  HIS D CB  
6491 C  CG  . HIS D 17  ? 0.2014 0.1806 0.1520 0.0129  0.0559  0.0103  17  HIS D CG  
6492 N  ND1 . HIS D 17  ? 0.2666 0.2161 0.1996 -0.0091 0.0640  -0.0274 17  HIS D ND1 
6493 C  CD2 . HIS D 17  ? 0.2312 0.2023 0.1204 0.0212  0.0135  -0.0115 17  HIS D CD2 
6494 C  CE1 . HIS D 17  ? 0.2935 0.2357 0.1720 0.0206  0.0322  -0.0625 17  HIS D CE1 
6495 N  NE2 . HIS D 17  ? 0.2485 0.2404 0.1332 0.0357  0.0344  -0.0060 17  HIS D NE2 
6496 N  N   . LYS D 18  ? 0.2194 0.1969 0.1172 0.0126  0.0445  0.0221  18  LYS D N   
6497 C  CA  . LYS D 18  ? 0.2352 0.1852 0.1050 -0.0151 0.0251  0.0176  18  LYS D CA  
6498 C  C   . LYS D 18  ? 0.2439 0.2073 0.2115 0.0082  0.0842  -0.0119 18  LYS D C   
6499 O  O   . LYS D 18  ? 0.3388 0.2328 0.1818 0.0038  0.0671  0.0231  18  LYS D O   
6500 C  CB  . LYS D 18  ? 0.2246 0.1759 0.1274 -0.0035 0.0217  -0.0051 18  LYS D CB  
6501 C  CG  . LYS D 18  ? 0.2693 0.2100 0.1340 0.0263  -0.0132 -0.0147 18  LYS D CG  
6502 C  CD  . LYS D 18  ? 0.2184 0.2169 0.1395 -0.0046 0.0297  -0.0432 18  LYS D CD  
6503 C  CE  . LYS D 18  ? 0.2364 0.1604 0.1809 0.0208  0.0175  -0.0275 18  LYS D CE  
6504 N  NZ  . LYS D 18  ? 0.2156 0.2055 0.1389 0.0640  0.0127  -0.0210 18  LYS D NZ  
6505 N  N   . ASP D 19  ? 0.2542 0.2411 0.1416 0.0207  0.0648  0.0149  19  ASP D N   
6506 C  CA  . ASP D 19  ? 0.3738 0.2518 0.1341 0.0452  0.0401  -0.0078 19  ASP D CA  
6507 C  C   . ASP D 19  ? 0.2617 0.1978 0.1854 0.0551  -0.0054 -0.0020 19  ASP D C   
6508 O  O   . ASP D 19  ? 0.3526 0.1817 0.1511 0.0265  0.0003  0.0212  19  ASP D O   
6509 C  CB  . ASP D 19  ? 0.3190 0.2982 0.1856 0.1074  0.0406  -0.0007 19  ASP D CB  
6510 C  CG  . ASP D 19  ? 0.4872 0.5004 0.1906 -0.0690 -0.0270 0.0057  19  ASP D CG  
6511 O  OD1 . ASP D 19  ? 0.4453 0.4677 0.1996 -0.0131 -0.0239 0.0255  19  ASP D OD1 
6512 O  OD2 . ASP D 19  ? 0.6460 0.6793 0.2915 -0.0489 -0.0173 0.0114  19  ASP D OD2 
6513 N  N   . PHE D 20  ? 0.2230 0.1987 0.1190 0.0043  0.0511  0.0076  20  PHE D N   
6514 C  CA  . PHE D 20  ? 0.1847 0.2084 0.0944 -0.0162 0.0603  0.0077  20  PHE D CA  
6515 C  C   . PHE D 20  ? 0.2075 0.1870 0.1429 0.0076  0.0439  -0.0068 20  PHE D C   
6516 O  O   . PHE D 20  ? 0.2657 0.1770 0.1260 -0.0074 0.0192  0.0015  20  PHE D O   
6517 C  CB  . PHE D 20  ? 0.2027 0.2265 0.1218 0.0062  0.0641  0.0344  20  PHE D CB  
6518 C  CG  . PHE D 20  ? 0.2090 0.2341 0.1315 0.0034  0.0482  0.0410  20  PHE D CG  
6519 C  CD1 . PHE D 20  ? 0.2633 0.2833 0.1369 0.0478  0.0428  0.0562  20  PHE D CD1 
6520 C  CD2 . PHE D 20  ? 0.2314 0.3028 0.1443 -0.0474 0.0318  0.0568  20  PHE D CD2 
6521 C  CE1 . PHE D 20  ? 0.2336 0.2741 0.1786 0.0253  0.0302  0.0231  20  PHE D CE1 
6522 C  CE2 . PHE D 20  ? 0.2628 0.2633 0.1362 0.0248  0.0375  0.0487  20  PHE D CE2 
6523 C  CZ  . PHE D 20  ? 0.2806 0.2696 0.1145 0.0388  0.0483  0.0531  20  PHE D CZ  
6524 N  N   . PRO D 21  ? 0.2262 0.1865 0.1281 -0.0157 0.0337  0.0206  21  PRO D N   
6525 C  CA  . PRO D 21  ? 0.2197 0.2178 0.1544 -0.0188 0.0689  0.0630  21  PRO D CA  
6526 C  C   . PRO D 21  ? 0.2073 0.2116 0.1734 -0.0035 0.0467  0.0043  21  PRO D C   
6527 O  O   . PRO D 21  ? 0.2245 0.1983 0.1404 -0.0262 0.0720  0.0073  21  PRO D O   
6528 C  CB  . PRO D 21  ? 0.3034 0.2587 0.0994 -0.0423 0.0900  0.0529  21  PRO D CB  
6529 C  CG  . PRO D 21  ? 0.3001 0.3190 0.3161 -0.0074 0.0978  0.1124  21  PRO D CG  
6530 C  CD  . PRO D 21  ? 0.2833 0.2388 0.1535 0.0116  0.0203  0.0603  21  PRO D CD  
6531 N  N   . ILE D 22  ? 0.2063 0.1844 0.1287 -0.0148 0.0307  0.0165  22  ILE D N   
6532 C  CA  . ILE D 22  ? 0.2370 0.1619 0.1367 -0.0467 0.0584  0.0165  22  ILE D CA  
6533 C  C   . ILE D 22  ? 0.1563 0.1529 0.1482 -0.0040 0.0255  0.0293  22  ILE D C   
6534 O  O   . ILE D 22  ? 0.2364 0.1763 0.1203 -0.0027 0.0329  0.0041  22  ILE D O   
6535 C  CB  . ILE D 22  ? 0.2037 0.1606 0.1705 -0.0125 0.0177  -0.0031 22  ILE D CB  
6536 C  CG1 . ILE D 22  ? 0.2215 0.2086 0.1490 -0.0504 -0.0076 0.0222  22  ILE D CG1 
6537 C  CG2 . ILE D 22  ? 0.2039 0.1971 0.1556 -0.0129 0.0452  0.0133  22  ILE D CG2 
6538 C  CD1 . ILE D 22  ? 0.2700 0.2606 0.3515 -0.0575 0.0001  -0.0283 22  ILE D CD1 
6539 N  N   . ALA D 23  ? 0.1877 0.1676 0.1313 -0.0281 0.0487  0.0052  23  ALA D N   
6540 C  CA  . ALA D 23  ? 0.1859 0.1711 0.1152 -0.0130 0.0168  0.0120  23  ALA D CA  
6541 C  C   . ALA D 23  ? 0.1827 0.1628 0.1261 -0.0161 0.0176  -0.0054 23  ALA D C   
6542 O  O   . ALA D 23  ? 0.2138 0.1524 0.1373 -0.0087 0.0176  0.0108  23  ALA D O   
6543 C  CB  . ALA D 23  ? 0.2055 0.1680 0.1079 -0.0143 0.0300  -0.0170 23  ALA D CB  
6544 N  N   . LYS D 24  ? 0.2133 0.1692 0.1520 -0.0146 0.0443  -0.0210 24  LYS D N   
6545 C  CA  . LYS D 24  ? 0.1876 0.2197 0.1392 -0.0230 0.0524  -0.0109 24  LYS D CA  
6546 C  C   . LYS D 24  ? 0.2275 0.2072 0.1966 -0.0227 0.0252  0.0149  24  LYS D C   
6547 O  O   . LYS D 24  ? 0.2287 0.2861 0.1960 -0.0217 0.0549  0.0153  24  LYS D O   
6548 C  CB  . LYS D 24  ? 0.2206 0.2434 0.1720 -0.0203 0.0617  -0.0148 24  LYS D CB  
6549 C  CG  . LYS D 24  ? 0.2657 0.2825 0.1658 0.0137  0.0152  -0.0339 24  LYS D CG  
6550 C  CD  . LYS D 24  ? 0.3885 0.3804 0.1996 0.0003  0.0706  -0.0640 24  LYS D CD  
6551 C  CE  . LYS D 24  ? 0.4056 0.3495 0.2439 0.0043  0.0220  -0.0137 24  LYS D CE  
6552 N  NZ  . LYS D 24  ? 0.4034 0.3129 0.3142 0.0176  -0.0229 -0.1019 24  LYS D NZ  
6553 N  N   . GLY D 25  ? 0.2028 0.2052 0.1872 -0.0491 0.0278  -0.0188 25  GLY D N   
6554 C  CA  . GLY D 25  ? 0.2373 0.2179 0.1865 -0.0760 0.0487  0.0278  25  GLY D CA  
6555 C  C   . GLY D 25  ? 0.2030 0.2158 0.1836 -0.0159 0.0573  -0.0116 25  GLY D C   
6556 O  O   . GLY D 25  ? 0.1962 0.2330 0.1484 -0.0137 0.0529  -0.0161 25  GLY D O   
6557 N  N   . GLU D 26  ? 0.1746 0.2535 0.1659 -0.0690 0.0571  -0.0217 26  GLU D N   
6558 C  CA  . GLU D 26  ? 0.1906 0.2064 0.1781 -0.0500 0.0421  -0.0147 26  GLU D CA  
6559 C  C   . GLU D 26  ? 0.1723 0.1914 0.1412 -0.0046 0.0307  -0.0124 26  GLU D C   
6560 O  O   . GLU D 26  ? 0.1186 0.2360 0.1935 -0.0205 0.0125  -0.0077 26  GLU D O   
6561 C  CB  . GLU D 26  ? 0.2073 0.3109 0.2264 -0.1259 0.0590  -0.0088 26  GLU D CB  
6562 C  CG  . GLU D 26  ? 0.2842 0.3759 0.2793 -0.1379 0.1066  -0.0215 26  GLU D CG  
6563 C  CD  . GLU D 26  ? 0.2583 0.4124 0.3975 -0.0428 0.0579  0.0223  26  GLU D CD  
6564 O  OE1 . GLU D 26  ? 0.2815 0.4156 0.3860 -0.0474 0.0843  0.0214  26  GLU D OE1 
6565 O  OE2 . GLU D 26  ? 0.3786 0.5673 0.4632 0.0185  0.1286  -0.0581 26  GLU D OE2 
6566 N  N   . ARG D 27  ? 0.1536 0.1353 0.1296 -0.0342 0.0228  -0.0208 27  ARG D N   
6567 C  CA  . ARG D 27  ? 0.1468 0.1659 0.0920 -0.0212 0.0066  0.0073  27  ARG D CA  
6568 C  C   . ARG D 27  ? 0.1324 0.1269 0.1323 -0.0043 -0.0005 0.0164  27  ARG D C   
6569 O  O   . ARG D 27  ? 0.1438 0.1430 0.1271 -0.0238 0.0141  -0.0133 27  ARG D O   
6570 C  CB  . ARG D 27  ? 0.1306 0.1631 0.2084 -0.0048 0.0055  -0.0307 27  ARG D CB  
6571 C  CG  . ARG D 27  ? 0.2141 0.2172 0.2009 -0.0436 0.0357  0.0051  27  ARG D CG  
6572 C  CD  . ARG D 27  ? 0.2540 0.3046 0.3100 0.0474  0.0351  -0.0899 27  ARG D CD  
6573 N  NE  . ARG D 27  ? 0.2529 0.2531 0.2271 0.0008  -0.0070 -0.0037 27  ARG D NE  
6574 C  CZ  . ARG D 27  ? 0.2163 0.1635 0.2457 -0.0141 0.0032  -0.0222 27  ARG D CZ  
6575 N  NH1 . ARG D 27  ? 0.2264 0.2298 0.1824 -0.1248 0.0218  -0.0571 27  ARG D NH1 
6576 N  NH2 . ARG D 27  ? 0.2490 0.1872 0.1867 -0.0549 0.0044  0.0120  27  ARG D NH2 
6577 N  N   . GLN D 28  ? 0.1281 0.1371 0.1001 -0.0326 0.0195  0.0012  28  GLN D N   
6578 C  CA  . GLN D 28  ? 0.1323 0.1377 0.1037 -0.0210 0.0200  0.0000  28  GLN D CA  
6579 C  C   . GLN D 28  ? 0.1202 0.0982 0.1123 -0.0086 0.0063  0.0027  28  GLN D C   
6580 O  O   . GLN D 28  ? 0.1230 0.1240 0.1107 -0.0152 0.0110  0.0001  28  GLN D O   
6581 C  CB  . GLN D 28  ? 0.1599 0.1396 0.0965 -0.0439 0.0111  -0.0085 28  GLN D CB  
6582 C  CG  . GLN D 28  ? 0.1601 0.1400 0.1224 -0.0348 0.0342  0.0124  28  GLN D CG  
6583 C  CD  . GLN D 28  ? 0.1434 0.1412 0.1076 -0.0494 0.0439  0.0184  28  GLN D CD  
6584 O  OE1 . GLN D 28  ? 0.1599 0.1545 0.1231 -0.0370 0.0162  -0.0020 28  GLN D OE1 
6585 N  NE2 . GLN D 28  ? 0.1592 0.1305 0.0879 -0.0124 0.0324  0.0148  28  GLN D NE2 
6586 N  N   . SER D 29  ? 0.1140 0.1145 0.0836 -0.0245 0.0030  -0.0013 29  SER D N   
6587 C  CA  . SER D 29  ? 0.1040 0.1035 0.1082 -0.0194 0.0261  0.0031  29  SER D CA  
6588 C  C   . SER D 29  ? 0.1252 0.1124 0.1048 -0.0074 0.0114  -0.0051 29  SER D C   
6589 O  O   . SER D 29  ? 0.1339 0.1170 0.0996 -0.0178 0.0031  -0.0081 29  SER D O   
6590 C  CB  . SER D 29  ? 0.1316 0.1121 0.0983 -0.0089 0.0035  -0.0133 29  SER D CB  
6591 O  OG  . SER D 29  ? 0.1310 0.1041 0.1010 -0.0260 0.0015  0.0062  29  SER D OG  
6592 N  N   . PRO D 30  ? 0.0852 0.1100 0.0860 -0.0003 -0.0046 -0.0046 30  PRO D N   
6593 C  CA  . PRO D 30  ? 0.1084 0.1269 0.1006 -0.0060 -0.0055 0.0295  30  PRO D CA  
6594 C  C   . PRO D 30  ? 0.1116 0.1005 0.0757 -0.0088 0.0120  -0.0153 30  PRO D C   
6595 O  O   . PRO D 30  ? 0.1033 0.1084 0.0886 -0.0136 0.0173  -0.0052 30  PRO D O   
6596 C  CB  . PRO D 30  ? 0.1064 0.1152 0.0920 -0.0168 0.0037  -0.0221 30  PRO D CB  
6597 C  CG  . PRO D 30  ? 0.1444 0.1369 0.0897 -0.0038 0.0108  -0.0100 30  PRO D CG  
6598 C  CD  . PRO D 30  ? 0.1098 0.1200 0.0788 -0.0205 0.0027  -0.0083 30  PRO D CD  
6599 N  N   . VAL D 31  ? 0.1014 0.0929 0.0922 0.0012  -0.0006 -0.0070 31  VAL D N   
6600 C  CA  . VAL D 31  ? 0.0874 0.1109 0.1197 -0.0104 -0.0024 0.0097  31  VAL D CA  
6601 C  C   . VAL D 31  ? 0.1150 0.0891 0.1141 0.0028  0.0132  -0.0096 31  VAL D C   
6602 O  O   . VAL D 31  ? 0.1036 0.1165 0.1199 0.0024  0.0098  -0.0078 31  VAL D O   
6603 C  CB  . VAL D 31  ? 0.1055 0.1015 0.0847 -0.0142 0.0107  -0.0049 31  VAL D CB  
6604 C  CG1 . VAL D 31  ? 0.1246 0.1237 0.1209 -0.0342 0.0228  0.0102  31  VAL D CG1 
6605 C  CG2 . VAL D 31  ? 0.1221 0.1215 0.0915 -0.0027 0.0110  -0.0108 31  VAL D CG2 
6606 N  N   . ASP D 32  ? 0.1249 0.1096 0.1164 0.0104  0.0109  -0.0065 32  ASP D N   
6607 C  CA  . ASP D 32  ? 0.1146 0.1133 0.1082 0.0154  -0.0071 -0.0019 32  ASP D CA  
6608 C  C   . ASP D 32  ? 0.1061 0.1018 0.1269 0.0031  0.0077  -0.0126 32  ASP D C   
6609 O  O   . ASP D 32  ? 0.1168 0.1425 0.1362 -0.0182 0.0048  -0.0085 32  ASP D O   
6610 C  CB  . ASP D 32  ? 0.1491 0.1265 0.1477 0.0076  0.0133  -0.0099 32  ASP D CB  
6611 C  CG  . ASP D 32  ? 0.1443 0.1312 0.1565 -0.0035 0.0163  0.0024  32  ASP D CG  
6612 O  OD1 . ASP D 32  ? 0.1181 0.1190 0.1317 0.0041  -0.0038 -0.0038 32  ASP D OD1 
6613 O  OD2 . ASP D 32  ? 0.1565 0.1650 0.2339 -0.0038 -0.0087 0.0146  32  ASP D OD2 
6614 N  N   . ILE D 33  ? 0.1140 0.1093 0.1024 0.0068  0.0038  -0.0054 33  ILE D N   
6615 C  CA  . ILE D 33  ? 0.1276 0.1393 0.1127 0.0019  0.0000  -0.0182 33  ILE D CA  
6616 C  C   . ILE D 33  ? 0.1247 0.1353 0.1466 -0.0034 -0.0190 -0.0143 33  ILE D C   
6617 O  O   . ILE D 33  ? 0.1538 0.1437 0.1382 0.0131  -0.0081 -0.0041 33  ILE D O   
6618 C  CB  . ILE D 33  ? 0.1314 0.1448 0.1071 0.0199  -0.0153 -0.0076 33  ILE D CB  
6619 C  CG1 . ILE D 33  ? 0.1246 0.1235 0.1254 0.0105  -0.0044 0.0003  33  ILE D CG1 
6620 C  CG2 . ILE D 33  ? 0.1429 0.1592 0.1156 0.0188  -0.0388 -0.0083 33  ILE D CG2 
6621 C  CD1 . ILE D 33  ? 0.1565 0.1502 0.1518 0.0285  0.0226  -0.0074 33  ILE D CD1 
6622 N  N   . ASP D 34  ? 0.1172 0.1477 0.1389 0.0143  -0.0251 -0.0147 34  ASP D N   
6623 C  CA  . ASP D 34  ? 0.1728 0.1630 0.1531 0.0137  -0.0187 0.0074  34  ASP D CA  
6624 C  C   . ASP D 34  ? 0.1333 0.1312 0.1577 0.0248  -0.0192 0.0094  34  ASP D C   
6625 O  O   . ASP D 34  ? 0.1633 0.1592 0.2021 0.0046  -0.0432 -0.0242 34  ASP D O   
6626 C  CB  . ASP D 34  ? 0.1887 0.1574 0.2217 0.0006  -0.0013 -0.0299 34  ASP D CB  
6627 C  CG  . ASP D 34  ? 0.2960 0.2008 0.2465 0.0568  0.0110  -0.0299 34  ASP D CG  
6628 O  OD1 . ASP D 34  ? 0.2321 0.2576 0.2847 0.0788  -0.0132 0.0066  34  ASP D OD1 
6629 O  OD2 . ASP D 34  ? 0.3666 0.4018 0.4379 0.1368  0.0645  0.0007  34  ASP D OD2 
6630 N  N   . THR D 35  ? 0.1313 0.1486 0.1547 0.0296  -0.0218 -0.0063 35  THR D N   
6631 C  CA  . THR D 35  ? 0.1580 0.1732 0.1477 0.0370  -0.0265 -0.0031 35  THR D CA  
6632 C  C   . THR D 35  ? 0.1529 0.1700 0.1714 0.0504  -0.0318 -0.0196 35  THR D C   
6633 O  O   . THR D 35  ? 0.1951 0.2109 0.2091 0.0310  -0.0436 -0.0432 35  THR D O   
6634 C  CB  . THR D 35  ? 0.1736 0.1622 0.1547 0.0414  -0.0263 -0.0076 35  THR D CB  
6635 O  OG1 . THR D 35  ? 0.2160 0.1845 0.2060 0.0546  -0.0474 -0.0027 35  THR D OG1 
6636 C  CG2 . THR D 35  ? 0.1580 0.2398 0.1924 0.0856  -0.0344 -0.0362 35  THR D CG2 
6637 N  N   . HIS D 36  ? 0.1532 0.2021 0.1991 0.0401  -0.0614 -0.0357 36  HIS D N   
6638 C  CA  . HIS D 36  ? 0.1665 0.1671 0.2292 0.0496  -0.0685 0.0005  36  HIS D CA  
6639 C  C   . HIS D 36  ? 0.1310 0.2628 0.2274 -0.0077 -0.0498 -0.0171 36  HIS D C   
6640 O  O   . HIS D 36  ? 0.1725 0.2587 0.2280 -0.0052 -0.0623 -0.0129 36  HIS D O   
6641 C  CB  . HIS D 36  ? 0.2199 0.2073 0.2518 0.1233  -0.0226 0.0421  36  HIS D CB  
6642 C  CG  . HIS D 36  ? 0.1745 0.1860 0.2971 0.0688  -0.0615 0.0008  36  HIS D CG  
6643 N  ND1 . HIS D 36  ? 0.2069 0.2565 0.3483 0.0684  0.0172  0.0293  36  HIS D ND1 
6644 C  CD2 . HIS D 36  ? 0.1389 0.1811 0.3093 0.0749  -0.0164 0.0038  36  HIS D CD2 
6645 C  CE1 . HIS D 36  ? 0.2723 0.3140 0.4340 0.0068  0.0238  -0.0377 36  HIS D CE1 
6646 N  NE2 . HIS D 36  ? 0.2601 0.2741 0.3503 0.0137  -0.0538 -0.0062 36  HIS D NE2 
6647 N  N   A THR D 37  ? 0.2551 0.1726 0.2160 0.0263  -0.0604 -0.0511 37  THR D N   
6648 N  N   B THR D 37  ? 0.2642 0.1660 0.2273 0.0423  -0.0443 -0.0405 37  THR D N   
6649 C  CA  A THR D 37  ? 0.2465 0.1869 0.2615 0.0346  -0.0505 -0.0109 37  THR D CA  
6650 C  CA  B THR D 37  ? 0.2003 0.2020 0.2395 0.0498  -0.0498 0.0001  37  THR D CA  
6651 C  C   A THR D 37  ? 0.1297 0.1944 0.2522 0.0183  -0.0476 -0.0173 37  THR D C   
6652 C  C   B THR D 37  ? 0.1362 0.1982 0.1937 -0.0054 0.0020  -0.0129 37  THR D C   
6653 O  O   A THR D 37  ? 0.2134 0.2249 0.2646 0.0250  -0.0540 0.0234  37  THR D O   
6654 O  O   B THR D 37  ? 0.1342 0.1890 0.1463 0.0110  -0.0127 -0.0168 37  THR D O   
6655 C  CB  A THR D 37  ? 0.1750 0.2597 0.2610 -0.0005 -0.0763 -0.0093 37  THR D CB  
6656 C  CB  B THR D 37  ? 0.1836 0.2019 0.2754 0.0939  0.0148  -0.0060 37  THR D CB  
6657 O  OG1 A THR D 37  ? 0.2152 0.2779 0.2108 0.0436  -0.0737 -0.0980 37  THR D OG1 
6658 O  OG1 B THR D 37  ? 0.3111 0.1802 0.2707 0.0807  -0.0185 -0.0439 37  THR D OG1 
6659 C  CG2 A THR D 37  ? 0.1861 0.2746 0.3028 0.0093  -0.1711 -0.0820 37  THR D CG2 
6660 C  CG2 B THR D 37  ? 0.1134 0.2391 0.2779 0.0653  0.0135  -0.0133 37  THR D CG2 
6661 N  N   . ALA D 38  ? 0.1613 0.1631 0.1807 0.0221  -0.0428 -0.0322 38  ALA D N   
6662 C  CA  . ALA D 38  ? 0.1504 0.1511 0.1852 0.0307  -0.0394 -0.0353 38  ALA D CA  
6663 C  C   . ALA D 38  ? 0.2380 0.1834 0.1693 0.0046  -0.0505 0.0096  38  ALA D C   
6664 O  O   . ALA D 38  ? 0.3560 0.2222 0.2134 0.0307  -0.0544 0.0087  38  ALA D O   
6665 C  CB  . ALA D 38  ? 0.1542 0.1854 0.2007 -0.0041 -0.0375 -0.0041 38  ALA D CB  
6666 N  N   . LYS D 39  ? 0.1820 0.2001 0.2072 0.0178  -0.0276 -0.0364 39  LYS D N   
6667 C  CA  . LYS D 39  ? 0.2070 0.2583 0.2091 0.0154  -0.0043 -0.0480 39  LYS D CA  
6668 C  C   . LYS D 39  ? 0.1994 0.1741 0.1606 0.0203  -0.0215 -0.0390 39  LYS D C   
6669 O  O   . LYS D 39  ? 0.1425 0.2098 0.1809 0.0185  -0.0261 -0.0048 39  LYS D O   
6670 C  CB  . LYS D 39  ? 0.1374 0.2336 0.3145 -0.0026 0.0133  -0.0342 39  LYS D CB  
6671 C  CG  . LYS D 39  ? 0.2267 0.3833 0.2601 -0.0439 -0.0351 -0.0081 39  LYS D CG  
6672 C  CD  . LYS D 39  ? 0.2707 0.2739 0.2506 0.0593  0.0310  -0.0768 39  LYS D CD  
6673 C  CE  . LYS D 39  ? 0.3540 0.4491 0.3429 0.0606  -0.1110 -0.0666 39  LYS D CE  
6674 N  NZ  . LYS D 39  ? 0.3736 0.4431 0.2836 0.1888  0.0010  -0.0557 39  LYS D NZ  
6675 N  N   . TYR D 40  ? 0.1698 0.2028 0.2098 0.0344  -0.0507 -0.0147 40  TYR D N   
6676 C  CA  . TYR D 40  ? 0.1852 0.1999 0.1886 0.0104  -0.0480 0.0071  40  TYR D CA  
6677 C  C   . TYR D 40  ? 0.1154 0.2026 0.2071 -0.0086 0.0080  -0.0096 40  TYR D C   
6678 O  O   . TYR D 40  ? 0.1326 0.2651 0.1926 0.0000  -0.0372 -0.0249 40  TYR D O   
6679 C  CB  . TYR D 40  ? 0.1953 0.2948 0.2041 0.0020  -0.0028 0.0625  40  TYR D CB  
6680 C  CG  . TYR D 40  ? 0.2409 0.3388 0.1906 0.0226  -0.0643 0.0159  40  TYR D CG  
6681 C  CD1 . TYR D 40  ? 0.2111 0.2732 0.2100 -0.0177 -0.0288 0.0362  40  TYR D CD1 
6682 C  CD2 . TYR D 40  ? 0.2962 0.4560 0.1739 -0.0057 -0.0395 0.0146  40  TYR D CD2 
6683 C  CE1 . TYR D 40  ? 0.3226 0.3684 0.2294 -0.0211 -0.0295 0.0093  40  TYR D CE1 
6684 C  CE2 . TYR D 40  ? 0.2678 0.4327 0.2861 0.0474  -0.0152 -0.0417 40  TYR D CE2 
6685 C  CZ  . TYR D 40  ? 0.2431 0.4203 0.2556 0.0226  0.0057  -0.0416 40  TYR D CZ  
6686 O  OH  . TYR D 40  ? 0.2969 0.4905 0.2238 -0.0023 -0.0185 -0.1044 40  TYR D OH  
6687 N  N   . ASP D 41  ? 0.1992 0.1931 0.1472 0.0120  -0.0035 -0.0291 41  ASP D N   
6688 C  CA  . ASP D 41  ? 0.1260 0.2027 0.2117 0.0046  -0.0063 -0.0252 41  ASP D CA  
6689 C  C   . ASP D 41  ? 0.2132 0.3161 0.1859 0.0234  -0.0057 -0.0007 41  ASP D C   
6690 O  O   . ASP D 41  ? 0.2377 0.3091 0.2127 0.0143  0.0238  -0.0228 41  ASP D O   
6691 C  CB  . ASP D 41  ? 0.1696 0.2238 0.2451 0.0015  -0.0130 -0.0251 41  ASP D CB  
6692 C  CG  . ASP D 41  ? 0.3000 0.2890 0.3657 -0.0540 -0.0138 0.0320  41  ASP D CG  
6693 O  OD1 . ASP D 41  ? 0.2707 0.2698 0.3309 -0.0218 0.0265  -0.0289 41  ASP D OD1 
6694 O  OD2 . ASP D 41  ? 0.3366 0.3149 0.3750 0.0041  -0.0031 0.0467  41  ASP D OD2 
6695 N  N   . PRO D 42  ? 0.1982 0.3447 0.2282 0.0375  -0.0381 -0.0461 42  PRO D N   
6696 C  CA  . PRO D 42  ? 0.2845 0.3702 0.1775 -0.0168 -0.0439 -0.0353 42  PRO D CA  
6697 C  C   . PRO D 42  ? 0.2795 0.3318 0.2170 0.0166  -0.0403 -0.0586 42  PRO D C   
6698 O  O   . PRO D 42  ? 0.3312 0.4456 0.2407 0.0944  -0.0388 -0.0693 42  PRO D O   
6699 C  CB  . PRO D 42  ? 0.3871 0.5332 0.2666 0.0430  -0.1203 -0.0557 42  PRO D CB  
6700 C  CG  . PRO D 42  ? 0.3804 0.5354 0.2664 0.0324  -0.1097 -0.1356 42  PRO D CG  
6701 C  CD  . PRO D 42  ? 0.2574 0.3605 0.2160 0.0907  -0.0993 -0.0560 42  PRO D CD  
6702 N  N   . SER D 43  ? 0.2572 0.2971 0.2578 0.0164  -0.0141 -0.0662 43  SER D N   
6703 C  CA  . SER D 43  ? 0.3021 0.2431 0.4045 -0.0089 -0.0368 -0.0531 43  SER D CA  
6704 C  C   . SER D 43  ? 0.3235 0.3158 0.3131 0.0151  -0.0711 -0.0958 43  SER D C   
6705 O  O   . SER D 43  ? 0.3452 0.3140 0.4445 0.0171  -0.0329 -0.1221 43  SER D O   
6706 C  CB  . SER D 43  ? 0.3664 0.3605 0.3623 0.0100  0.0680  -0.0226 43  SER D CB  
6707 O  OG  . SER D 43  ? 0.2626 0.3745 0.4618 -0.0667 0.0850  0.0309  43  SER D OG  
6708 N  N   . LEU D 44  ? 0.1736 0.2992 0.2436 -0.0063 0.0209  -0.0560 44  LEU D N   
6709 C  CA  . LEU D 44  ? 0.1802 0.2818 0.2696 0.0368  0.0167  -0.0566 44  LEU D CA  
6710 C  C   . LEU D 44  ? 0.2240 0.3898 0.2391 0.0333  0.0140  0.0085  44  LEU D C   
6711 O  O   . LEU D 44  ? 0.3122 0.4546 0.3034 0.0443  0.0502  0.1096  44  LEU D O   
6712 C  CB  . LEU D 44  ? 0.2018 0.2716 0.1998 0.0425  0.0010  -0.0163 44  LEU D CB  
6713 C  CG  . LEU D 44  ? 0.2012 0.2178 0.1787 0.0256  -0.0104 0.0003  44  LEU D CG  
6714 C  CD1 . LEU D 44  ? 0.2554 0.2878 0.2657 -0.0685 -0.0271 -0.0241 44  LEU D CD1 
6715 C  CD2 . LEU D 44  ? 0.2014 0.2587 0.2351 0.0164  0.0041  0.0284  44  LEU D CD2 
6716 N  N   . LYS D 45  ? 0.2707 0.2777 0.2793 0.0461  0.1014  -0.0027 45  LYS D N   
6717 C  CA  . LYS D 45  ? 0.2328 0.3165 0.2265 -0.0121 0.0714  -0.0231 45  LYS D CA  
6718 C  C   . LYS D 45  ? 0.2375 0.2639 0.2202 0.0229  0.0340  -0.0298 45  LYS D C   
6719 O  O   . LYS D 45  ? 0.2732 0.2834 0.1838 -0.0170 0.0132  0.0087  45  LYS D O   
6720 C  CB  . LYS D 45  ? 0.3544 0.2619 0.2666 -0.0137 0.0167  -0.1353 45  LYS D CB  
6721 C  CG  . LYS D 45  ? 0.2680 0.4108 0.3925 -0.0577 0.0776  -0.0610 45  LYS D CG  
6722 C  CD  . LYS D 45  ? 0.6432 0.4859 0.5451 -0.0903 0.0252  0.0408  45  LYS D CD  
6723 N  N   . PRO D 46  ? 0.2445 0.2570 0.1747 -0.0054 0.0070  0.0206  46  PRO D N   
6724 C  CA  . PRO D 46  ? 0.2497 0.2100 0.1996 0.0229  0.0166  0.0302  46  PRO D CA  
6725 C  C   . PRO D 46  ? 0.2118 0.2016 0.1504 0.0012  0.0003  -0.0003 46  PRO D C   
6726 O  O   . PRO D 46  ? 0.2196 0.2204 0.1770 -0.0193 0.0377  0.0007  46  PRO D O   
6727 C  CB  . PRO D 46  ? 0.2596 0.2867 0.1935 0.0388  0.0129  0.0568  46  PRO D CB  
6728 C  CG  . PRO D 46  ? 0.2682 0.3785 0.2087 -0.0807 0.0274  -0.0261 46  PRO D CG  
6729 C  CD  . PRO D 46  ? 0.2452 0.2754 0.2011 -0.0187 0.0419  -0.0513 46  PRO D CD  
6730 N  N   . LEU D 47  ? 0.2166 0.2552 0.1847 0.0450  0.0384  -0.0137 47  LEU D N   
6731 C  CA  . LEU D 47  ? 0.2082 0.2440 0.1829 0.0062  0.0046  0.0581  47  LEU D CA  
6732 C  C   . LEU D 47  ? 0.2757 0.2149 0.1875 0.0346  0.0416  0.0322  47  LEU D C   
6733 O  O   . LEU D 47  ? 0.2736 0.2948 0.2404 0.0496  0.1071  0.0662  47  LEU D O   
6734 C  CB  . LEU D 47  ? 0.3118 0.2926 0.2477 0.0357  -0.0270 0.0351  47  LEU D CB  
6735 C  CG  . LEU D 47  ? 0.2890 0.2472 0.2412 -0.0491 -0.0065 0.0640  47  LEU D CG  
6736 C  CD1 . LEU D 47  ? 0.3303 0.3248 0.1987 -0.0447 0.0973  0.0417  47  LEU D CD1 
6737 C  CD2 . LEU D 47  ? 0.3357 0.2811 0.2619 -0.0701 0.1080  -0.0458 47  LEU D CD2 
6738 N  N   . SER D 48  ? 0.1957 0.2152 0.1543 0.0298  0.0051  0.0216  48  SER D N   
6739 C  CA  . SER D 48  ? 0.1905 0.2023 0.1802 -0.0054 -0.0144 -0.0044 48  SER D CA  
6740 C  C   . SER D 48  ? 0.1876 0.1817 0.1574 0.0167  0.0068  0.0258  48  SER D C   
6741 O  O   . SER D 48  ? 0.2011 0.2109 0.1502 -0.0262 0.0087  0.0276  48  SER D O   
6742 C  CB  . SER D 48  ? 0.2700 0.1946 0.2360 0.0329  0.0032  0.0093  48  SER D CB  
6743 O  OG  . SER D 48  ? 0.2795 0.2671 0.2165 0.0405  0.0445  -0.0229 48  SER D OG  
6744 N  N   . VAL D 49  ? 0.2115 0.2084 0.1571 -0.0121 -0.0017 0.0286  49  VAL D N   
6745 C  CA  . VAL D 49  ? 0.2134 0.2242 0.1930 0.0032  -0.0120 0.0417  49  VAL D CA  
6746 C  C   . VAL D 49  ? 0.2698 0.2423 0.1744 0.0184  0.0549  0.0218  49  VAL D C   
6747 O  O   . VAL D 49  ? 0.2813 0.3102 0.2431 -0.0278 0.0142  0.1273  49  VAL D O   
6748 C  CB  . VAL D 49  ? 0.2736 0.2479 0.2002 -0.0478 -0.0201 0.0126  49  VAL D CB  
6749 C  CG1 . VAL D 49  ? 0.2637 0.3307 0.3461 -0.0333 -0.1067 0.0434  49  VAL D CG1 
6750 C  CG2 . VAL D 49  ? 0.3400 0.2404 0.2477 -0.0267 0.0255  0.0141  49  VAL D CG2 
6751 N  N   . SER D 50  ? 0.2185 0.2105 0.2319 -0.0182 0.0401  0.0292  50  SER D N   
6752 C  CA  . SER D 50  ? 0.2443 0.2669 0.1914 -0.0124 0.0715  0.0410  50  SER D CA  
6753 C  C   . SER D 50  ? 0.2224 0.2639 0.2211 -0.0152 0.0839  -0.0005 50  SER D C   
6754 O  O   . SER D 50  ? 0.2294 0.2305 0.3226 0.0211  0.0399  0.0211  50  SER D O   
6755 C  CB  . SER D 50  ? 0.3296 0.2887 0.3048 0.0467  0.0621  -0.0164 50  SER D CB  
6756 O  OG  . SER D 50  ? 0.4058 0.4000 0.3179 -0.0533 0.0861  -0.0219 50  SER D OG  
6757 N  N   . TYR D 51  ? 0.2161 0.2161 0.1964 -0.0035 0.0562  0.0087  51  TYR D N   
6758 C  CA  . TYR D 51  ? 0.1656 0.2287 0.2603 0.0098  0.0461  -0.0065 51  TYR D CA  
6759 C  C   . TYR D 51  ? 0.2052 0.1969 0.2271 0.0684  0.0300  -0.0034 51  TYR D C   
6760 O  O   . TYR D 51  ? 0.2159 0.3267 0.2585 0.0467  0.0476  -0.0085 51  TYR D O   
6761 C  CB  . TYR D 51  ? 0.1938 0.2502 0.2440 -0.0157 0.0544  -0.0199 51  TYR D CB  
6762 C  CG  . TYR D 51  ? 0.1414 0.1990 0.2001 0.0137  0.0008  0.0197  51  TYR D CG  
6763 C  CD1 . TYR D 51  ? 0.1978 0.1675 0.1868 0.0041  0.0273  0.0046  51  TYR D CD1 
6764 C  CD2 . TYR D 51  ? 0.1838 0.1775 0.2163 0.0088  0.0251  0.0275  51  TYR D CD2 
6765 C  CE1 . TYR D 51  ? 0.1831 0.1435 0.1604 0.0210  0.0271  0.0271  51  TYR D CE1 
6766 C  CE2 . TYR D 51  ? 0.1669 0.1615 0.2057 -0.0239 0.0107  0.0190  51  TYR D CE2 
6767 C  CZ  . TYR D 51  ? 0.1626 0.1466 0.1382 0.0007  0.0186  0.0162  51  TYR D CZ  
6768 O  OH  . TYR D 51  ? 0.1687 0.1726 0.1773 -0.0028 0.0372  -0.0020 51  TYR D OH  
6769 N  N   . ASP D 52  ? 0.2231 0.2452 0.2249 0.0524  0.0661  0.0271  52  ASP D N   
6770 C  CA  . ASP D 52  ? 0.2608 0.4408 0.2219 0.1273  0.0628  -0.0041 52  ASP D CA  
6771 C  C   . ASP D 52  ? 0.2973 0.2870 0.3574 0.0966  0.0974  0.0226  52  ASP D C   
6772 O  O   . ASP D 52  ? 0.2958 0.4530 0.3562 0.0806  0.1049  0.0438  52  ASP D O   
6773 C  CB  . ASP D 52  ? 0.3043 0.4172 0.1804 0.1080  0.0636  0.0285  52  ASP D CB  
6774 C  CG  . ASP D 52  ? 0.6040 0.5590 0.3856 -0.0222 0.0032  -0.0507 52  ASP D CG  
6775 O  OD1 . ASP D 52  ? 0.7096 0.8869 0.4909 0.0443  0.0944  0.1709  52  ASP D OD1 
6776 O  OD2 . ASP D 52  ? 0.9537 0.7142 0.5928 0.4140  -0.0851 0.0874  52  ASP D OD2 
6777 N  N   . GLN D 53  ? 0.3125 0.2689 0.2129 0.1004  0.0798  0.0089  53  GLN D N   
6778 C  CA  . GLN D 53  ? 0.3477 0.2664 0.1858 0.0595  -0.0065 -0.0051 53  GLN D CA  
6779 C  C   . GLN D 53  ? 0.2536 0.2116 0.1784 0.0221  -0.0103 -0.0298 53  GLN D C   
6780 O  O   . GLN D 53  ? 0.2917 0.2091 0.2899 0.0515  0.0364  -0.0078 53  GLN D O   
6781 C  CB  . GLN D 53  ? 0.3770 0.2592 0.2931 0.0248  0.0646  -0.0131 53  GLN D CB  
6782 C  CG  . GLN D 53  ? 0.4395 0.3689 0.3404 -0.0055 -0.0487 -0.0979 53  GLN D CG  
6783 C  CD  . GLN D 53  ? 0.6359 0.6600 0.3454 0.2669  0.2587  -0.0540 53  GLN D CD  
6784 O  OE1 . GLN D 53  ? 0.7415 0.8320 0.4368 0.2931  0.2148  0.1328  53  GLN D OE1 
6785 N  NE2 . GLN D 53  ? 0.9221 0.7283 0.6646 0.3389  0.0262  0.0489  53  GLN D NE2 
6786 N  N   . ALA D 54  ? 0.2181 0.1705 0.2043 0.0218  0.0126  0.0098  54  ALA D N   
6787 C  CA  . ALA D 54  ? 0.1709 0.2123 0.1842 0.0310  0.0052  -0.0063 54  ALA D CA  
6788 C  C   . ALA D 54  ? 0.1728 0.2275 0.1833 0.0071  0.0194  -0.0026 54  ALA D C   
6789 O  O   . ALA D 54  ? 0.2493 0.2795 0.2533 -0.0408 0.0434  0.0108  54  ALA D O   
6790 C  CB  . ALA D 54  ? 0.2271 0.1800 0.1989 0.0000  0.0038  0.0280  54  ALA D CB  
6791 N  N   . THR D 55  ? 0.1475 0.1726 0.1721 0.0320  0.0081  -0.0093 55  THR D N   
6792 C  CA  . THR D 55  ? 0.1410 0.2142 0.1976 0.0582  -0.0088 -0.0421 55  THR D CA  
6793 C  C   . THR D 55  ? 0.1342 0.1646 0.1626 0.0315  0.0087  0.0227  55  THR D C   
6794 O  O   . THR D 55  ? 0.1736 0.1387 0.2131 0.0295  0.0063  0.0098  55  THR D O   
6795 C  CB  . THR D 55  ? 0.3027 0.2544 0.2757 0.1384  -0.0366 -0.0108 55  THR D CB  
6796 O  OG1 . THR D 55  ? 0.3614 0.3165 0.3546 0.0537  -0.0599 -0.0701 55  THR D OG1 
6797 C  CG2 . THR D 55  ? 0.2671 0.2361 0.3984 0.0908  -0.0772 -0.1517 55  THR D CG2 
6798 N  N   . SER D 56  ? 0.1490 0.1653 0.1747 0.0210  -0.0135 -0.0175 56  SER D N   
6799 C  CA  . SER D 56  ? 0.1438 0.1356 0.1737 0.0054  -0.0153 0.0007  56  SER D CA  
6800 C  C   . SER D 56  ? 0.1046 0.1549 0.1416 0.0109  0.0035  0.0096  56  SER D C   
6801 O  O   . SER D 56  ? 0.1499 0.1701 0.2003 0.0038  0.0260  0.0017  56  SER D O   
6802 C  CB  . SER D 56  ? 0.0966 0.1369 0.2170 0.0082  -0.0205 -0.0024 56  SER D CB  
6803 O  OG  . SER D 56  ? 0.1258 0.1483 0.1910 0.0088  0.0142  0.0017  56  SER D OG  
6804 N  N   . LEU D 57  ? 0.1513 0.1693 0.1383 0.0222  -0.0182 -0.0188 57  LEU D N   
6805 C  CA  . LEU D 57  ? 0.1542 0.1847 0.1832 0.0217  -0.0313 -0.0019 57  LEU D CA  
6806 C  C   . LEU D 57  ? 0.1507 0.1623 0.1791 0.0137  0.0076  -0.0103 57  LEU D C   
6807 O  O   . LEU D 57  ? 0.1666 0.1744 0.2125 0.0313  -0.0195 -0.0243 57  LEU D O   
6808 C  CB  . LEU D 57  ? 0.2379 0.1687 0.1969 0.0028  -0.0263 -0.0113 57  LEU D CB  
6809 C  CG  . LEU D 57  ? 0.2082 0.2082 0.1976 -0.0082 -0.0026 -0.0348 57  LEU D CG  
6810 C  CD1 . LEU D 57  ? 0.2452 0.2467 0.2134 -0.0355 -0.0076 -0.0010 57  LEU D CD1 
6811 C  CD2 . LEU D 57  ? 0.2711 0.2592 0.4552 0.0103  0.0170  -0.1375 57  LEU D CD2 
6812 N  N   A ARG D 58  ? 0.1926 0.1795 0.1817 0.0788  -0.0417 -0.0120 58  ARG D N   
6813 N  N   B ARG D 58  ? 0.1759 0.1734 0.1251 0.0305  -0.0125 -0.0103 58  ARG D N   
6814 C  CA  A ARG D 58  ? 0.1425 0.1389 0.1805 0.0427  -0.0131 0.0203  58  ARG D CA  
6815 C  CA  B ARG D 58  ? 0.1759 0.1509 0.1012 0.0168  -0.0175 0.0248  58  ARG D CA  
6816 C  C   A ARG D 58  ? 0.1466 0.1773 0.1770 0.0767  -0.0220 -0.0308 58  ARG D C   
6817 C  C   B ARG D 58  ? 0.1052 0.1337 0.0997 0.0012  0.0062  0.0280  58  ARG D C   
6818 O  O   A ARG D 58  ? 0.1520 0.1394 0.2229 0.0303  -0.0366 0.0223  58  ARG D O   
6819 O  O   B ARG D 58  ? 0.0913 0.1127 0.1018 0.0080  0.0236  0.0062  58  ARG D O   
6820 C  CB  A ARG D 58  ? 0.2339 0.1692 0.1624 0.0156  0.0126  0.0157  58  ARG D CB  
6821 C  CB  B ARG D 58  ? 0.1703 0.1052 0.0921 -0.0013 -0.0247 -0.0006 58  ARG D CB  
6822 C  CG  A ARG D 58  ? 0.2633 0.2041 0.2291 0.0142  -0.0199 0.0353  58  ARG D CG  
6823 C  CG  B ARG D 58  ? 0.1642 0.1161 0.1024 -0.0093 -0.0430 0.0361  58  ARG D CG  
6824 C  CD  A ARG D 58  ? 0.2915 0.2867 0.2192 0.0373  0.0038  0.0432  58  ARG D CD  
6825 C  CD  B ARG D 58  ? 0.1468 0.0974 0.0987 0.0063  -0.0256 0.0307  58  ARG D CD  
6826 N  NE  A ARG D 58  ? 0.2861 0.2678 0.3217 -0.0265 0.0478  -0.0527 58  ARG D NE  
6827 N  NE  B ARG D 58  ? 0.1626 0.1177 0.1021 -0.0088 -0.0359 0.0381  58  ARG D NE  
6828 C  CZ  A ARG D 58  ? 0.2263 0.2497 0.1922 0.0987  0.0366  0.1289  58  ARG D CZ  
6829 C  CZ  B ARG D 58  ? 0.1586 0.1523 0.1298 -0.0192 -0.0034 0.0031  58  ARG D CZ  
6830 N  NH1 A ARG D 58  ? 0.2915 0.1933 0.3741 0.0379  0.0926  0.0076  58  ARG D NH1 
6831 N  NH1 B ARG D 58  ? 0.1465 0.1829 0.1998 0.0560  -0.0060 0.0104  58  ARG D NH1 
6832 N  NH2 A ARG D 58  ? 0.2676 0.3704 0.3136 0.0008  0.0326  -0.0599 58  ARG D NH2 
6833 N  NH2 B ARG D 58  ? 0.1577 0.1149 0.1393 0.0092  -0.0304 -0.0023 58  ARG D NH2 
6834 N  N   . ILE D 59  ? 0.1333 0.1617 0.1912 0.0267  -0.0229 -0.0189 59  ILE D N   
6835 C  CA  . ILE D 59  ? 0.1491 0.1402 0.1905 0.0262  -0.0118 -0.0187 59  ILE D CA  
6836 C  C   . ILE D 59  ? 0.1569 0.1644 0.2000 0.0255  -0.0109 -0.0082 59  ILE D C   
6837 O  O   . ILE D 59  ? 0.1517 0.1867 0.1829 0.0282  -0.0307 0.0054  59  ILE D O   
6838 C  CB  . ILE D 59  ? 0.1079 0.1667 0.2379 0.0219  -0.0311 -0.0041 59  ILE D CB  
6839 C  CG1 . ILE D 59  ? 0.1559 0.1628 0.2007 0.0388  -0.0162 -0.0037 59  ILE D CG1 
6840 C  CG2 . ILE D 59  ? 0.1120 0.1771 0.2082 0.0080  -0.0388 0.0001  59  ILE D CG2 
6841 C  CD1 . ILE D 59  ? 0.1396 0.1833 0.2296 0.0153  -0.0248 -0.0099 59  ILE D CD1 
6842 N  N   . LEU D 60  ? 0.1276 0.1492 0.1693 0.0076  0.0027  -0.0010 60  LEU D N   
6843 C  CA  . LEU D 60  ? 0.1799 0.1484 0.1932 0.0187  -0.0087 -0.0146 60  LEU D CA  
6844 C  C   . LEU D 60  ? 0.1619 0.1556 0.1339 0.0272  -0.0230 0.0208  60  LEU D C   
6845 O  O   . LEU D 60  ? 0.1337 0.1621 0.2341 0.0264  -0.0469 0.0038  60  LEU D O   
6846 C  CB  . LEU D 60  ? 0.2063 0.1129 0.2371 0.0131  0.0160  0.0005  60  LEU D CB  
6847 C  CG  . LEU D 60  ? 0.2409 0.2127 0.2759 -0.0386 -0.0049 0.0540  60  LEU D CG  
6848 C  CD1 . LEU D 60  ? 0.3352 0.2124 0.2964 0.0386  -0.0671 0.0781  60  LEU D CD1 
6849 C  CD2 . LEU D 60  ? 0.1902 0.2380 0.4345 -0.0274 -0.0051 0.0515  60  LEU D CD2 
6850 N  N   . ASN D 61  ? 0.1517 0.1468 0.1483 -0.0086 -0.0133 -0.0006 61  ASN D N   
6851 C  CA  . ASN D 61  ? 0.1619 0.1712 0.1647 -0.0051 -0.0066 0.0006  61  ASN D CA  
6852 C  C   . ASN D 61  ? 0.1924 0.2044 0.1554 -0.0219 -0.0274 0.0254  61  ASN D C   
6853 O  O   . ASN D 61  ? 0.2039 0.1766 0.1739 0.0200  -0.0252 0.0368  61  ASN D O   
6854 C  CB  . ASN D 61  ? 0.1667 0.1562 0.1608 0.0003  -0.0178 0.0051  61  ASN D CB  
6855 C  CG  . ASN D 61  ? 0.1351 0.1481 0.1653 0.0201  -0.0293 0.0480  61  ASN D CG  
6856 O  OD1 . ASN D 61  ? 0.1761 0.1766 0.1764 -0.0148 -0.0126 0.0066  61  ASN D OD1 
6857 N  ND2 . ASN D 61  ? 0.1847 0.1707 0.1956 -0.0105 -0.0208 0.0283  61  ASN D ND2 
6858 N  N   . ASN D 62  ? 0.1730 0.1815 0.1933 0.0038  0.0027  0.0656  62  ASN D N   
6859 C  CA  . ASN D 62  ? 0.1581 0.1641 0.1728 -0.0052 0.0003  0.0542  62  ASN D CA  
6860 C  C   . ASN D 62  ? 0.2226 0.2136 0.2422 0.0187  0.0003  0.0241  62  ASN D C   
6861 O  O   . ASN D 62  ? 0.2064 0.2633 0.2443 -0.0443 -0.0186 0.0702  62  ASN D O   
6862 C  CB  . ASN D 62  ? 0.1878 0.1689 0.2770 -0.0242 -0.0178 0.0322  62  ASN D CB  
6863 C  CG  . ASN D 62  ? 0.2186 0.2069 0.2614 -0.0118 -0.0193 -0.0010 62  ASN D CG  
6864 O  OD1 . ASN D 62  ? 0.2402 0.1894 0.2240 0.0010  0.0303  0.0201  62  ASN D OD1 
6865 N  ND2 . ASN D 62  ? 0.2583 0.2912 0.2910 -0.0124 -0.0333 -0.0228 62  ASN D ND2 
6866 N  N   . GLY D 63  ? 0.1556 0.1816 0.1832 0.0178  0.0103  0.0405  63  GLY D N   
6867 C  CA  . GLY D 63  ? 0.2248 0.2439 0.1701 0.0397  0.0015  0.0304  63  GLY D CA  
6868 C  C   . GLY D 63  ? 0.1475 0.1551 0.1500 -0.0049 0.0153  -0.0049 63  GLY D C   
6869 O  O   . GLY D 63  ? 0.2210 0.1865 0.1899 0.0065  0.0218  -0.0031 63  GLY D O   
6870 N  N   . HIS D 64  ? 0.2011 0.1789 0.1763 -0.0161 -0.0277 0.0248  64  HIS D N   
6871 C  CA  . HIS D 64  ? 0.2008 0.1908 0.1874 0.0057  -0.0063 0.0096  64  HIS D CA  
6872 C  C   . HIS D 64  ? 0.1615 0.1759 0.2109 -0.0119 -0.0013 0.0326  64  HIS D C   
6873 O  O   . HIS D 64  ? 0.2217 0.2030 0.1924 0.0454  0.0092  0.0267  64  HIS D O   
6874 C  CB  . HIS D 64  ? 0.1867 0.2389 0.1766 -0.0131 0.0296  0.0132  64  HIS D CB  
6875 C  CG  . HIS D 64  ? 0.1723 0.1766 0.2161 -0.0065 -0.0017 0.0163  64  HIS D CG  
6876 N  ND1 . HIS D 64  ? 0.2274 0.2217 0.2147 -0.0498 -0.0118 0.0000  64  HIS D ND1 
6877 C  CD2 . HIS D 64  ? 0.2655 0.2314 0.1861 0.0086  -0.0553 0.0668  64  HIS D CD2 
6878 C  CE1 . HIS D 64  ? 0.2481 0.2486 0.2020 -0.0509 0.0351  0.0599  64  HIS D CE1 
6879 N  NE2 . HIS D 64  ? 0.2490 0.2741 0.1721 -0.0465 -0.0249 0.0247  64  HIS D NE2 
6880 N  N   . ALA D 65  ? 0.2010 0.1507 0.1517 0.0041  -0.0052 0.0237  65  ALA D N   
6881 C  CA  . ALA D 65  ? 0.1687 0.1800 0.1389 -0.0094 -0.0052 -0.0026 65  ALA D CA  
6882 C  C   . ALA D 65  ? 0.1915 0.1416 0.1684 0.0085  -0.0008 0.0186  65  ALA D C   
6883 O  O   . ALA D 65  ? 0.1743 0.1647 0.1748 0.0034  -0.0113 0.0372  65  ALA D O   
6884 C  CB  . ALA D 65  ? 0.1459 0.2154 0.1899 0.0445  -0.0142 -0.0008 65  ALA D CB  
6885 N  N   . PHE D 66  ? 0.1224 0.1439 0.1423 0.0144  -0.0082 0.0028  66  PHE D N   
6886 C  CA  . PHE D 66  ? 0.1301 0.1712 0.1701 0.0174  -0.0043 -0.0192 66  PHE D CA  
6887 C  C   . PHE D 66  ? 0.1559 0.1493 0.1604 0.0078  -0.0236 -0.0073 66  PHE D C   
6888 O  O   . PHE D 66  ? 0.1712 0.1824 0.2002 -0.0124 -0.0540 0.0118  66  PHE D O   
6889 C  CB  . PHE D 66  ? 0.1466 0.1805 0.1951 -0.0071 -0.0178 -0.0132 66  PHE D CB  
6890 C  CG  . PHE D 66  ? 0.1168 0.1644 0.1730 -0.0421 0.0178  -0.0087 66  PHE D CG  
6891 C  CD1 . PHE D 66  ? 0.1073 0.1642 0.1448 0.0088  0.0269  0.0097  66  PHE D CD1 
6892 C  CD2 . PHE D 66  ? 0.1631 0.1777 0.1705 -0.0140 -0.0103 -0.0115 66  PHE D CD2 
6893 C  CE1 . PHE D 66  ? 0.1586 0.1527 0.1657 -0.0232 0.0182  0.0229  66  PHE D CE1 
6894 C  CE2 . PHE D 66  ? 0.1554 0.1780 0.1917 -0.0313 -0.0210 0.0030  66  PHE D CE2 
6895 C  CZ  . PHE D 66  ? 0.1328 0.1606 0.1881 0.0113  -0.0063 -0.0027 66  PHE D CZ  
6896 N  N   . ASN D 67  ? 0.1290 0.1662 0.2070 0.0132  -0.0220 -0.0155 67  ASN D N   
6897 C  CA  . ASN D 67  ? 0.1814 0.1741 0.1893 0.0379  -0.0065 -0.0375 67  ASN D CA  
6898 C  C   . ASN D 67  ? 0.1479 0.1574 0.2053 0.0160  -0.0153 -0.0006 67  ASN D C   
6899 O  O   . ASN D 67  ? 0.1603 0.2527 0.1800 0.0511  -0.0513 -0.0425 67  ASN D O   
6900 C  CB  . ASN D 67  ? 0.2397 0.2770 0.3212 -0.0599 0.0381  -0.0401 67  ASN D CB  
6901 C  CG  . ASN D 67  ? 0.2048 0.2817 0.3886 0.2100  0.0897  0.0473  67  ASN D CG  
6902 O  OD1 . ASN D 67  ? 0.4307 0.3957 0.6121 -0.0476 -0.0081 -0.0054 67  ASN D OD1 
6903 N  ND2 . ASN D 67  ? 0.2770 0.9778 1.0622 0.0786  0.1510  -0.2444 67  ASN D ND2 
6904 N  N   . VAL D 68  ? 0.1502 0.1267 0.1784 0.0324  0.0138  -0.0185 68  VAL D N   
6905 C  CA  . VAL D 68  ? 0.1522 0.1558 0.1407 -0.0052 0.0223  -0.0445 68  VAL D CA  
6906 C  C   . VAL D 68  ? 0.1289 0.1468 0.1826 0.0124  -0.0177 -0.0147 68  VAL D C   
6907 O  O   . VAL D 68  ? 0.1261 0.1418 0.1926 0.0188  -0.0248 -0.0230 68  VAL D O   
6908 C  CB  . VAL D 68  ? 0.1435 0.1482 0.1793 0.0017  -0.0031 -0.0082 68  VAL D CB  
6909 C  CG1 . VAL D 68  ? 0.1620 0.1874 0.1955 0.0186  0.0406  0.0068  68  VAL D CG1 
6910 C  CG2 . VAL D 68  ? 0.1525 0.1710 0.2430 -0.0209 -0.0261 -0.0196 68  VAL D CG2 
6911 N  N   A GLU D 69  ? 0.1890 0.1367 0.1802 0.0252  -0.0078 -0.0320 69  GLU D N   
6912 N  N   B GLU D 69  ? 0.1554 0.1506 0.1368 0.0031  0.0135  0.0038  69  GLU D N   
6913 C  CA  A GLU D 69  ? 0.1653 0.1513 0.1353 0.0038  0.0311  0.0046  69  GLU D CA  
6914 C  CA  B GLU D 69  ? 0.1414 0.1364 0.1289 0.0183  0.0000  0.0071  69  GLU D CA  
6915 C  C   A GLU D 69  ? 0.1206 0.1680 0.1533 0.0436  0.0052  0.0034  69  GLU D C   
6916 C  C   B GLU D 69  ? 0.1163 0.1802 0.1691 0.0476  -0.0137 -0.0183 69  GLU D C   
6917 O  O   A GLU D 69  ? 0.1217 0.1268 0.1167 0.0324  -0.0077 0.0203  69  GLU D O   
6918 O  O   B GLU D 69  ? 0.1502 0.1161 0.2494 0.0685  0.0244  -0.0317 69  GLU D O   
6919 C  CB  A GLU D 69  ? 0.2545 0.2099 0.2431 0.0509  -0.1253 0.0164  69  GLU D CB  
6920 C  CB  B GLU D 69  ? 0.1583 0.1856 0.1228 0.0082  0.0395  0.0120  69  GLU D CB  
6921 C  CG  A GLU D 69  ? 0.3574 0.3497 0.2989 -0.0239 0.0054  -0.0121 69  GLU D CG  
6922 C  CG  B GLU D 69  ? 0.2522 0.1550 0.2176 -0.0057 0.0697  0.0129  69  GLU D CG  
6923 C  CD  A GLU D 69  ? 0.2445 0.3208 0.3996 -0.0807 -0.0419 0.0666  69  GLU D CD  
6924 C  CD  B GLU D 69  ? 0.2621 0.2384 0.1759 0.0215  -0.0189 0.0198  69  GLU D CD  
6925 O  OE1 A GLU D 69  ? 0.1845 0.2551 0.1125 0.0255  0.0000  -0.0329 69  GLU D OE1 
6926 O  OE1 B GLU D 69  ? 0.3027 0.2707 0.2136 -0.0241 0.0342  0.0140  69  GLU D OE1 
6927 O  OE2 A GLU D 69  ? 0.4309 0.2536 0.4201 -0.0811 0.0472  -0.0228 69  GLU D OE2 
6928 O  OE2 B GLU D 69  ? 0.3274 0.2353 0.1759 0.0362  -0.0007 -0.0120 69  GLU D OE2 
6929 N  N   . PHE D 70  ? 0.1511 0.1277 0.1852 0.0454  -0.0103 -0.0093 70  PHE D N   
6930 C  CA  . PHE D 70  ? 0.1297 0.1355 0.1657 0.0096  -0.0068 0.0000  70  PHE D CA  
6931 C  C   . PHE D 70  ? 0.1599 0.1407 0.1533 0.0296  0.0038  0.0283  70  PHE D C   
6932 O  O   . PHE D 70  ? 0.1814 0.1597 0.2213 0.0031  0.0225  0.0152  70  PHE D O   
6933 C  CB  . PHE D 70  ? 0.1509 0.1401 0.1682 0.0136  -0.0102 -0.0113 70  PHE D CB  
6934 C  CG  . PHE D 70  ? 0.1307 0.1432 0.1876 0.0190  0.0192  -0.0080 70  PHE D CG  
6935 C  CD1 . PHE D 70  ? 0.1365 0.1662 0.1965 0.0399  -0.0098 -0.0034 70  PHE D CD1 
6936 C  CD2 . PHE D 70  ? 0.1493 0.1396 0.1635 0.0115  0.0181  0.0065  70  PHE D CD2 
6937 C  CE1 . PHE D 70  ? 0.2034 0.1755 0.2334 0.0357  -0.0231 0.0362  70  PHE D CE1 
6938 C  CE2 . PHE D 70  ? 0.1405 0.1563 0.1895 0.0261  0.0133  0.0040  70  PHE D CE2 
6939 C  CZ  . PHE D 70  ? 0.1802 0.1414 0.1906 0.0157  -0.0263 -0.0081 70  PHE D CZ  
6940 N  N   A ASP D 71  ? 0.2073 0.1473 0.2226 0.0436  0.0070  -0.0119 71  ASP D N   
6941 N  N   B ASP D 71  ? 0.1949 0.1576 0.1633 0.0207  0.0372  0.0122  71  ASP D N   
6942 C  CA  A ASP D 71  ? 0.2332 0.1504 0.1858 0.0148  -0.0054 0.0066  71  ASP D CA  
6943 C  CA  B ASP D 71  ? 0.1962 0.1569 0.1383 0.0100  0.0502  0.0031  71  ASP D CA  
6944 C  C   A ASP D 71  ? 0.2165 0.1437 0.2422 0.0283  0.0243  -0.0434 71  ASP D C   
6945 C  C   B ASP D 71  ? 0.2332 0.1502 0.2109 0.0373  0.0012  0.0034  71  ASP D C   
6946 O  O   A ASP D 71  ? 0.2177 0.1875 0.2558 0.0179  -0.0276 0.0346  71  ASP D O   
6947 O  O   B ASP D 71  ? 0.1899 0.1768 0.1787 0.0310  0.0118  0.0038  71  ASP D O   
6948 C  CB  A ASP D 71  ? 0.2484 0.1788 0.2176 0.0222  -0.0089 -0.0505 71  ASP D CB  
6949 C  CB  B ASP D 71  ? 0.2123 0.1615 0.1120 0.0419  0.0412  0.0463  71  ASP D CB  
6950 C  CG  A ASP D 71  ? 0.2319 0.1811 0.1980 0.0068  0.0013  -0.0121 71  ASP D CG  
6951 C  CG  B ASP D 71  ? 0.2041 0.1687 0.1942 0.0825  0.0175  0.0085  71  ASP D CG  
6952 O  OD1 A ASP D 71  ? 0.2321 0.1297 0.3012 0.0383  -0.0272 0.0135  71  ASP D OD1 
6953 O  OD1 B ASP D 71  ? 0.1842 0.2445 0.3145 0.0177  0.0719  -0.0201 71  ASP D OD1 
6954 O  OD2 A ASP D 71  ? 0.2509 0.2091 0.2439 -0.0006 0.0357  -0.0144 71  ASP D OD2 
6955 O  OD2 B ASP D 71  ? 0.2849 0.2172 0.3091 -0.0007 -0.0390 0.0062  71  ASP D OD2 
6956 N  N   . ASP D 72  ? 0.2212 0.1193 0.2594 0.0333  0.0013  -0.0034 72  ASP D N   
6957 C  CA  . ASP D 72  ? 0.2467 0.1513 0.1946 -0.0375 -0.0125 0.0109  72  ASP D CA  
6958 C  C   . ASP D 72  ? 0.3228 0.1732 0.3546 0.0217  -0.0136 -0.0406 72  ASP D C   
6959 O  O   . ASP D 72  ? 0.3124 0.1567 0.3273 0.0077  -0.0584 0.0044  72  ASP D O   
6960 C  CB  . ASP D 72  ? 0.2296 0.1795 0.2712 0.0012  -0.0412 0.0388  72  ASP D CB  
6961 C  CG  . ASP D 72  ? 0.2190 0.2363 0.2558 0.0428  -0.0225 -0.0093 72  ASP D CG  
6962 O  OD1 . ASP D 72  ? 0.2093 0.2188 0.2917 0.0502  -0.0162 0.0603  72  ASP D OD1 
6963 O  OD2 . ASP D 72  ? 0.2391 0.1915 0.3032 0.0206  -0.0038 0.0405  72  ASP D OD2 
6964 N  N   . SER D 73  ? 0.3334 0.1491 0.2933 0.0020  -0.0320 0.0100  73  SER D N   
6965 C  CA  . SER D 73  ? 0.4215 0.1439 0.3007 0.0097  -0.0219 -0.0461 73  SER D CA  
6966 C  C   . SER D 73  ? 0.4722 0.2170 0.2655 -0.0649 -0.0001 -0.0310 73  SER D C   
6967 O  O   . SER D 73  ? 0.3501 0.1845 0.3061 -0.0059 0.0342  -0.0114 73  SER D O   
6968 C  CB  . SER D 73  ? 0.3968 0.2123 0.3734 0.0509  0.0252  0.0006  73  SER D CB  
6969 O  OG  . SER D 73  ? 0.3470 0.1488 0.4047 0.0189  -0.0307 -0.0245 73  SER D OG  
6970 N  N   . GLN D 74  ? 0.4435 0.2114 0.2973 0.0144  0.0006  -0.0384 74  GLN D N   
6971 C  CA  . GLN D 74  ? 0.4376 0.2178 0.3219 0.0130  -0.0337 0.0146  74  GLN D CA  
6972 C  C   . GLN D 74  ? 0.3368 0.3287 0.3100 0.0318  -0.0577 -0.0452 74  GLN D C   
6973 O  O   . GLN D 74  ? 0.3095 0.2212 0.2781 -0.0113 0.0251  0.0254  74  GLN D O   
6974 C  CB  . GLN D 74  ? 0.5012 0.2592 0.2942 0.1018  -0.0185 -0.0658 74  GLN D CB  
6975 C  CG  . GLN D 74  ? 0.6445 0.2348 0.4853 0.1076  0.0450  0.0322  74  GLN D CG  
6976 C  CD  . GLN D 74  ? 0.5273 0.4243 0.5651 0.0529  -0.0052 0.0379  74  GLN D CD  
6977 O  OE1 . GLN D 74  ? 0.9919 0.6931 0.5546 0.1212  0.0299  0.1387  74  GLN D OE1 
6978 N  NE2 . GLN D 74  ? 0.5544 0.5544 0.4660 -0.1180 0.0753  -0.0908 74  GLN D NE2 
6979 N  N   . ASP D 75  ? 0.2870 0.3199 0.3389 -0.0493 -0.0386 0.0035  75  ASP D N   
6980 C  CA  . ASP D 75  ? 0.2984 0.3407 0.3686 -0.0720 -0.0137 0.0544  75  ASP D CA  
6981 C  C   . ASP D 75  ? 0.3506 0.3294 0.2775 -0.0838 0.0518  -0.0524 75  ASP D C   
6982 O  O   . ASP D 75  ? 0.5885 0.4409 0.2558 0.0098  0.0241  0.0544  75  ASP D O   
6983 C  CB  . ASP D 75  ? 0.4890 0.5256 0.5217 -0.0551 -0.1409 -0.0894 75  ASP D CB  
6984 C  CG  . ASP D 75  ? 0.7491 0.7074 0.5414 0.2777  -0.1831 -0.4072 75  ASP D CG  
6985 O  OD1 . ASP D 75  ? 0.3474 0.5658 0.3337 0.0414  -0.0244 0.2018  75  ASP D OD1 
6986 O  OD2 . ASP D 75  ? 1.0197 0.6244 0.4542 0.3219  0.1155  -0.0685 75  ASP D OD2 
6987 N  N   . LYS D 76  ? 0.2560 0.2612 0.3675 0.0661  0.0172  0.0102  76  LYS D N   
6988 C  CA  . LYS D 76  ? 0.3528 0.3237 0.6231 0.0188  -0.0549 0.1296  76  LYS D CA  
6989 C  C   . LYS D 76  ? 0.4666 0.3984 0.5194 0.1958  0.1018  0.0355  76  LYS D C   
6990 O  O   . LYS D 76  ? 0.3729 0.6733 0.5386 0.0196  0.2301  0.0425  76  LYS D O   
6991 C  CB  . LYS D 76  ? 0.1875 0.2086 0.6164 0.1247  -0.0434 0.1914  76  LYS D CB  
6992 N  N   . ALA D 77  ? 0.2186 0.3129 0.4047 0.0162  0.1412  0.0162  77  ALA D N   
6993 C  CA  . ALA D 77  ? 0.1859 0.3427 0.3167 0.0283  0.0234  0.0252  77  ALA D CA  
6994 C  C   . ALA D 77  ? 0.2087 0.2772 0.2148 -0.0225 0.0621  0.0192  77  ALA D C   
6995 O  O   . ALA D 77  ? 0.2500 0.3802 0.2176 -0.0586 0.0636  0.0182  77  ALA D O   
6996 C  CB  . ALA D 77  ? 0.2460 0.2702 0.3246 -0.0533 0.0724  0.0443  77  ALA D CB  
6997 N  N   . VAL D 78  ? 0.1782 0.1750 0.2361 0.0394  0.0410  0.0214  78  VAL D N   
6998 C  CA  . VAL D 78  ? 0.1808 0.1904 0.2786 0.0469  0.0315  0.0168  78  VAL D CA  
6999 C  C   . VAL D 78  ? 0.1805 0.1911 0.2089 -0.0031 0.0272  0.0496  78  VAL D C   
7000 O  O   . VAL D 78  ? 0.2093 0.1773 0.2230 0.0149  0.0637  0.0337  78  VAL D O   
7001 C  CB  . VAL D 78  ? 0.2256 0.2490 0.3142 0.0109  -0.0214 -0.0131 78  VAL D CB  
7002 C  CG1 . VAL D 78  ? 0.3097 0.1577 0.4320 0.0379  0.0524  -0.0076 78  VAL D CG1 
7003 C  CG2 . VAL D 78  ? 0.2597 0.2985 0.2694 0.0326  0.0217  0.0166  78  VAL D CG2 
7004 N  N   . LEU D 79  ? 0.1365 0.1520 0.1919 0.0076  0.0097  0.0040  79  LEU D N   
7005 C  CA  . LEU D 79  ? 0.1761 0.1517 0.1815 0.0182  0.0165  0.0116  79  LEU D CA  
7006 C  C   . LEU D 79  ? 0.2133 0.1373 0.1739 0.0003  0.0010  0.0133  79  LEU D C   
7007 O  O   . LEU D 79  ? 0.2019 0.1710 0.1960 -0.0126 -0.0176 0.0245  79  LEU D O   
7008 C  CB  . LEU D 79  ? 0.2344 0.1834 0.1922 0.0269  0.0480  -0.0028 79  LEU D CB  
7009 C  CG  . LEU D 79  ? 0.2159 0.1687 0.1982 -0.0102 0.0337  -0.0030 79  LEU D CG  
7010 C  CD1 . LEU D 79  ? 0.3186 0.1725 0.2260 0.0269  0.0631  0.0282  79  LEU D CD1 
7011 C  CD2 . LEU D 79  ? 0.1854 0.1982 0.1571 0.0185  0.0071  0.0094  79  LEU D CD2 
7012 N  N   . LYS D 80  ? 0.1781 0.1701 0.1944 -0.0093 0.0165  0.0153  80  LYS D N   
7013 C  CA  . LYS D 80  ? 0.2118 0.1738 0.2041 -0.0027 -0.0351 0.0040  80  LYS D CA  
7014 C  C   . LYS D 80  ? 0.2305 0.1996 0.1621 -0.0071 -0.0085 0.0129  80  LYS D C   
7015 O  O   . LYS D 80  ? 0.2057 0.1793 0.1885 0.0099  -0.0060 0.0166  80  LYS D O   
7016 C  CB  . LYS D 80  ? 0.2705 0.1981 0.2341 0.0057  0.0115  0.0020  80  LYS D CB  
7017 C  CG  . LYS D 80  ? 0.2657 0.2414 0.2524 0.0032  0.0068  -0.0171 80  LYS D CG  
7018 C  CD  . LYS D 80  ? 0.4829 0.2949 0.1766 0.0750  0.0815  -0.0140 80  LYS D CD  
7019 N  N   . GLY D 81  ? 0.1911 0.2248 0.1730 0.0041  -0.0087 -0.0034 81  GLY D N   
7020 C  CA  . GLY D 81  ? 0.2655 0.1980 0.1567 0.0357  -0.0204 0.0048  81  GLY D CA  
7021 C  C   . GLY D 81  ? 0.2186 0.2266 0.1649 0.0491  -0.0131 0.0091  81  GLY D C   
7022 O  O   . GLY D 81  ? 0.2194 0.1915 0.1559 -0.0071 0.0260  0.0008  81  GLY D O   
7023 N  N   . GLY D 82  ? 0.2831 0.2093 0.1770 0.0310  0.0412  -0.0083 82  GLY D N   
7024 C  CA  . GLY D 82  ? 0.3741 0.2151 0.2201 0.0359  0.0627  -0.0096 82  GLY D CA  
7025 C  C   . GLY D 82  ? 0.2648 0.2330 0.1647 0.0483  -0.0020 -0.0333 82  GLY D C   
7026 O  O   . GLY D 82  ? 0.3009 0.2878 0.2463 0.0340  -0.0759 -0.0114 82  GLY D O   
7027 N  N   . PRO D 83  ? 0.2459 0.1586 0.1669 0.0434  0.0220  0.0115  83  PRO D N   
7028 C  CA  . PRO D 83  ? 0.1894 0.1594 0.1798 0.0401  0.0267  -0.0324 83  PRO D CA  
7029 C  C   . PRO D 83  ? 0.2111 0.1914 0.2393 0.0147  0.0261  -0.0208 83  PRO D C   
7030 O  O   . PRO D 83  ? 0.2150 0.2224 0.2398 0.0094  0.0215  -0.0114 83  PRO D O   
7031 C  CB  . PRO D 83  ? 0.2188 0.2037 0.1772 0.0236  -0.0284 -0.0610 83  PRO D CB  
7032 C  CG  . PRO D 83  ? 0.1757 0.1982 0.1721 0.0320  0.0034  -0.0238 83  PRO D CG  
7033 C  CD  . PRO D 83  ? 0.2524 0.1698 0.1712 0.0071  0.0355  -0.0127 83  PRO D CD  
7034 N  N   . LEU D 84  ? 0.1730 0.1554 0.1403 0.0031  -0.0049 -0.0065 84  LEU D N   
7035 C  CA  . LEU D 84  ? 0.1838 0.1174 0.1606 -0.0120 0.0007  -0.0024 84  LEU D CA  
7036 C  C   . LEU D 84  ? 0.2248 0.1638 0.1599 0.0208  -0.0028 -0.0366 84  LEU D C   
7037 O  O   . LEU D 84  ? 0.2522 0.1820 0.1737 -0.0130 0.0083  -0.0423 84  LEU D O   
7038 C  CB  . LEU D 84  ? 0.1984 0.1314 0.1224 -0.0034 -0.0161 -0.0144 84  LEU D CB  
7039 C  CG  . LEU D 84  ? 0.1782 0.1423 0.1161 -0.0149 -0.0102 -0.0238 84  LEU D CG  
7040 C  CD1 . LEU D 84  ? 0.1615 0.1874 0.1667 -0.0340 -0.0094 -0.0286 84  LEU D CD1 
7041 C  CD2 . LEU D 84  ? 0.1895 0.1244 0.1073 -0.0102 -0.0089 0.0054  84  LEU D CD2 
7042 N  N   . ASP D 85  ? 0.2276 0.1556 0.2267 -0.0443 -0.0007 -0.0286 85  ASP D N   
7043 C  CA  . ASP D 85  ? 0.2079 0.1644 0.2145 -0.0208 -0.0210 -0.0211 85  ASP D CA  
7044 C  C   . ASP D 85  ? 0.2542 0.1716 0.2452 0.0007  -0.0298 -0.0038 85  ASP D C   
7045 O  O   . ASP D 85  ? 0.3447 0.2648 0.2363 -0.0122 -0.0138 -0.0326 85  ASP D O   
7046 C  CB  . ASP D 85  ? 0.2165 0.1685 0.2653 -0.0206 -0.0267 -0.0615 85  ASP D CB  
7047 C  CG  . ASP D 85  ? 0.2244 0.1915 0.2020 -0.0346 -0.0267 -0.0164 85  ASP D CG  
7048 O  OD1 . ASP D 85  ? 0.1933 0.2709 0.1901 -0.0507 -0.0080 0.0046  85  ASP D OD1 
7049 O  OD2 . ASP D 85  ? 0.2319 0.2594 0.1958 -0.0003 0.0105  0.0590  85  ASP D OD2 
7050 N  N   . GLY D 86  ? 0.2698 0.2626 0.2361 0.0245  0.0193  -0.0020 86  GLY D N   
7051 C  CA  . GLY D 86  ? 0.2364 0.2431 0.2287 -0.0012 -0.0342 -0.0194 86  GLY D CA  
7052 C  C   . GLY D 86  ? 0.2569 0.1964 0.2421 -0.0032 0.0195  0.0171  86  GLY D C   
7053 O  O   . GLY D 86  ? 0.2371 0.2495 0.3010 0.0142  0.0194  0.0874  86  GLY D O   
7054 N  N   A THR D 87  ? 0.1938 0.2240 0.2621 0.0346  0.0146  -0.0723 87  THR D N   
7055 N  N   B THR D 87  ? 0.1917 0.2109 0.2469 0.0159  0.0174  -0.0614 87  THR D N   
7056 C  CA  A THR D 87  ? 0.1996 0.2312 0.1764 0.0165  0.0088  -0.0121 87  THR D CA  
7057 C  CA  B THR D 87  ? 0.1953 0.1899 0.1571 0.0093  0.0023  0.0049  87  THR D CA  
7058 C  C   A THR D 87  ? 0.2075 0.1335 0.1799 0.0001  0.0110  -0.0236 87  THR D C   
7059 C  C   B THR D 87  ? 0.1875 0.1377 0.1660 -0.0027 -0.0085 -0.0156 87  THR D C   
7060 O  O   A THR D 87  ? 0.1662 0.1398 0.1852 0.0196  -0.0122 -0.0065 87  THR D O   
7061 O  O   B THR D 87  ? 0.1782 0.1161 0.1777 -0.0082 -0.0044 -0.0247 87  THR D O   
7062 C  CB  A THR D 87  ? 0.2443 0.2497 0.2181 0.0333  -0.0137 -0.0573 87  THR D CB  
7063 C  CB  B THR D 87  ? 0.2921 0.1833 0.2057 0.0318  0.0300  -0.0080 87  THR D CB  
7064 O  OG1 A THR D 87  ? 0.2795 0.2421 0.2021 -0.0085 -0.0174 -0.0344 87  THR D OG1 
7065 O  OG1 B THR D 87  ? 0.2055 0.1653 0.1827 0.0350  -0.0164 0.0028  87  THR D OG1 
7066 C  CG2 A THR D 87  ? 0.2761 0.2151 0.2759 0.0013  0.0782  -0.0229 87  THR D CG2 
7067 C  CG2 B THR D 87  ? 0.2371 0.1980 0.2105 0.0248  0.0241  -0.0408 87  THR D CG2 
7068 N  N   . TYR D 88  ? 0.1827 0.1439 0.1642 -0.0125 -0.0015 -0.0258 88  TYR D N   
7069 C  CA  . TYR D 88  ? 0.1771 0.1376 0.1382 0.0057  0.0043  0.0044  88  TYR D CA  
7070 C  C   . TYR D 88  ? 0.1723 0.1307 0.1425 0.0122  0.0245  -0.0089 88  TYR D C   
7071 O  O   . TYR D 88  ? 0.1850 0.1962 0.2027 0.0263  0.0282  0.0359  88  TYR D O   
7072 C  CB  . TYR D 88  ? 0.1642 0.1229 0.1554 -0.0038 0.0208  -0.0166 88  TYR D CB  
7073 C  CG  . TYR D 88  ? 0.1572 0.1023 0.1281 0.0006  0.0133  -0.0070 88  TYR D CG  
7074 C  CD1 . TYR D 88  ? 0.1358 0.1184 0.1759 -0.0010 0.0038  -0.0328 88  TYR D CD1 
7075 C  CD2 . TYR D 88  ? 0.1463 0.0904 0.1394 0.0087  0.0109  -0.0071 88  TYR D CD2 
7076 C  CE1 . TYR D 88  ? 0.1389 0.1492 0.1425 -0.0173 0.0052  -0.0217 88  TYR D CE1 
7077 C  CE2 . TYR D 88  ? 0.1347 0.1106 0.1326 0.0063  0.0000  -0.0098 88  TYR D CE2 
7078 C  CZ  . TYR D 88  ? 0.1383 0.1149 0.1317 -0.0118 -0.0035 -0.0137 88  TYR D CZ  
7079 O  OH  . TYR D 88  ? 0.1405 0.1202 0.1463 -0.0104 -0.0104 0.0017  88  TYR D OH  
7080 N  N   . ARG D 89  ? 0.1484 0.0994 0.1671 -0.0024 0.0006  -0.0211 89  ARG D N   
7081 C  CA  . ARG D 89  ? 0.1452 0.1190 0.1538 0.0167  0.0156  0.0035  89  ARG D CA  
7082 C  C   . ARG D 89  ? 0.1253 0.1226 0.1165 0.0040  -0.0109 0.0096  89  ARG D C   
7083 O  O   . ARG D 89  ? 0.1393 0.1100 0.1319 0.0130  -0.0006 0.0038  89  ARG D O   
7084 C  CB  . ARG D 89  ? 0.1720 0.1558 0.2436 0.0000  -0.0171 0.0472  89  ARG D CB  
7085 C  CG  . ARG D 89  ? 0.2002 0.1687 0.3510 0.0328  0.0071  0.0020  89  ARG D CG  
7086 C  CD  . ARG D 89  ? 0.2382 0.1714 0.2822 0.0586  0.0043  -0.0214 89  ARG D CD  
7087 N  NE  . ARG D 89  ? 0.2621 0.1834 0.2860 0.0509  0.0136  -0.0071 89  ARG D NE  
7088 C  CZ  . ARG D 89  ? 0.2623 0.1976 0.2585 0.0359  -0.0377 0.0154  89  ARG D CZ  
7089 N  NH1 . ARG D 89  ? 0.3433 0.1771 0.2687 0.0697  -0.0280 -0.0063 89  ARG D NH1 
7090 N  NH2 . ARG D 89  ? 0.2644 0.2247 0.2165 0.0439  0.0055  0.0206  89  ARG D NH2 
7091 N  N   . LEU D 90  ? 0.1499 0.1272 0.1457 0.0017  -0.0015 -0.0074 90  LEU D N   
7092 C  CA  . LEU D 90  ? 0.1473 0.1287 0.1364 -0.0019 0.0063  -0.0030 90  LEU D CA  
7093 C  C   . LEU D 90  ? 0.1164 0.1170 0.1590 0.0151  -0.0035 0.0031  90  LEU D C   
7094 O  O   . LEU D 90  ? 0.1669 0.1641 0.1964 0.0397  0.0052  0.0074  90  LEU D O   
7095 C  CB  . LEU D 90  ? 0.1518 0.1283 0.1612 0.0089  0.0054  0.0181  90  LEU D CB  
7096 C  CG  . LEU D 90  ? 0.1215 0.1450 0.1851 0.0141  -0.0133 0.0040  90  LEU D CG  
7097 C  CD1 . LEU D 90  ? 0.1439 0.1462 0.2032 0.0038  0.0120  0.0068  90  LEU D CD1 
7098 C  CD2 . LEU D 90  ? 0.1888 0.1642 0.1795 -0.0104 0.0340  0.0138  90  LEU D CD2 
7099 N  N   . ILE D 91  ? 0.1290 0.1150 0.1509 -0.0013 -0.0161 0.0068  91  ILE D N   
7100 C  CA  . ILE D 91  ? 0.1154 0.1457 0.1344 0.0118  -0.0131 -0.0120 91  ILE D CA  
7101 C  C   . ILE D 91  ? 0.1333 0.1084 0.1814 0.0126  -0.0026 0.0017  91  ILE D C   
7102 O  O   . ILE D 91  ? 0.1163 0.1170 0.1764 0.0000  -0.0073 0.0197  91  ILE D O   
7103 C  CB  . ILE D 91  ? 0.1676 0.1130 0.1544 0.0078  -0.0133 0.0130  91  ILE D CB  
7104 C  CG1 . ILE D 91  ? 0.2167 0.1667 0.1835 -0.0165 -0.0366 0.0597  91  ILE D CG1 
7105 C  CG2 . ILE D 91  ? 0.1615 0.1181 0.1899 -0.0015 0.0091  0.0166  91  ILE D CG2 
7106 C  CD1 . ILE D 91  ? 0.2352 0.2255 0.2617 -0.0634 -0.0259 0.0690  91  ILE D CD1 
7107 N  N   . GLN D 92  ? 0.1231 0.1116 0.1637 0.0093  -0.0015 -0.0057 92  GLN D N   
7108 C  CA  . GLN D 92  ? 0.1641 0.0917 0.1705 0.0104  -0.0186 0.0161  92  GLN D CA  
7109 C  C   . GLN D 92  ? 0.1200 0.1107 0.1238 0.0142  -0.0206 0.0087  92  GLN D C   
7110 O  O   . GLN D 92  ? 0.1155 0.1066 0.1656 0.0024  -0.0153 0.0060  92  GLN D O   
7111 C  CB  . GLN D 92  ? 0.1563 0.1606 0.1805 0.0244  0.0017  0.0146  92  GLN D CB  
7112 C  CG  . GLN D 92  ? 0.1798 0.1764 0.1781 0.0082  0.0065  0.0192  92  GLN D CG  
7113 C  CD  . GLN D 92  ? 0.1708 0.1694 0.2036 0.0120  0.0065  0.0205  92  GLN D CD  
7114 O  OE1 . GLN D 92  ? 0.1683 0.1596 0.2702 0.0259  -0.0066 0.0211  92  GLN D OE1 
7115 N  NE2 . GLN D 92  ? 0.2660 0.2878 0.2143 -0.0264 -0.0020 0.0010  92  GLN D NE2 
7116 N  N   . PHE D 93  ? 0.1106 0.0890 0.1656 0.0219  -0.0082 0.0020  93  PHE D N   
7117 C  CA  . PHE D 93  ? 0.1246 0.0945 0.1306 0.0264  -0.0098 0.0120  93  PHE D CA  
7118 C  C   . PHE D 93  ? 0.1032 0.0942 0.1356 -0.0082 -0.0051 0.0208  93  PHE D C   
7119 O  O   . PHE D 93  ? 0.1118 0.1238 0.1511 0.0049  -0.0063 0.0019  93  PHE D O   
7120 C  CB  . PHE D 93  ? 0.0988 0.1290 0.1416 0.0308  0.0093  0.0105  93  PHE D CB  
7121 C  CG  . PHE D 93  ? 0.1150 0.1129 0.1565 0.0049  -0.0063 0.0143  93  PHE D CG  
7122 C  CD1 . PHE D 93  ? 0.1082 0.1522 0.1748 -0.0253 -0.0197 0.0100  93  PHE D CD1 
7123 C  CD2 . PHE D 93  ? 0.1285 0.1430 0.1588 0.0041  0.0114  0.0102  93  PHE D CD2 
7124 C  CE1 . PHE D 93  ? 0.1235 0.1366 0.1969 0.0012  0.0188  -0.0017 93  PHE D CE1 
7125 C  CE2 . PHE D 93  ? 0.1393 0.1274 0.1917 0.0156  -0.0003 -0.0115 93  PHE D CE2 
7126 C  CZ  . PHE D 93  ? 0.1434 0.1319 0.1570 -0.0107 0.0255  0.0104  93  PHE D CZ  
7127 N  N   . HIS D 94  ? 0.1066 0.1133 0.1249 0.0230  0.0057  0.0060  94  HIS D N   
7128 C  CA  . HIS D 94  ? 0.0922 0.0957 0.1281 0.0131  -0.0015 0.0074  94  HIS D CA  
7129 C  C   . HIS D 94  ? 0.1066 0.0985 0.1040 0.0070  -0.0109 -0.0010 94  HIS D C   
7130 O  O   . HIS D 94  ? 0.1001 0.1028 0.1199 0.0043  -0.0201 0.0003  94  HIS D O   
7131 C  CB  . HIS D 94  ? 0.0784 0.1037 0.1278 0.0001  -0.0049 0.0100  94  HIS D CB  
7132 C  CG  . HIS D 94  ? 0.0827 0.0861 0.1140 0.0001  -0.0104 0.0179  94  HIS D CG  
7133 N  ND1 . HIS D 94  ? 0.1133 0.1055 0.1125 -0.0113 -0.0149 0.0098  94  HIS D ND1 
7134 C  CD2 . HIS D 94  ? 0.0881 0.1035 0.1123 -0.0020 -0.0030 0.0190  94  HIS D CD2 
7135 C  CE1 . HIS D 94  ? 0.1156 0.0982 0.1156 -0.0082 0.0063  0.0083  94  HIS D CE1 
7136 N  NE2 . HIS D 94  ? 0.1152 0.1026 0.1009 -0.0115 -0.0259 0.0142  94  HIS D NE2 
7137 N  N   . PHE D 95  ? 0.1128 0.0886 0.1195 0.0043  0.0005  -0.0046 95  PHE D N   
7138 C  CA  . PHE D 95  ? 0.0890 0.0857 0.1322 0.0008  0.0063  -0.0028 95  PHE D CA  
7139 C  C   . PHE D 95  ? 0.1089 0.0987 0.1018 -0.0121 -0.0088 0.0086  95  PHE D C   
7140 O  O   . PHE D 95  ? 0.1240 0.1027 0.1089 0.0049  -0.0028 0.0091  95  PHE D O   
7141 C  CB  . PHE D 95  ? 0.0901 0.1211 0.1150 -0.0104 -0.0093 0.0043  95  PHE D CB  
7142 C  CG  . PHE D 95  ? 0.0933 0.0947 0.1030 -0.0093 -0.0093 0.0120  95  PHE D CG  
7143 C  CD1 . PHE D 95  ? 0.1188 0.0942 0.1477 -0.0135 -0.0066 -0.0027 95  PHE D CD1 
7144 C  CD2 . PHE D 95  ? 0.1080 0.1288 0.0974 -0.0103 0.0073  0.0197  95  PHE D CD2 
7145 C  CE1 . PHE D 95  ? 0.1114 0.1143 0.1398 -0.0068 -0.0115 -0.0080 95  PHE D CE1 
7146 C  CE2 . PHE D 95  ? 0.1386 0.1125 0.1200 -0.0232 0.0212  0.0015  95  PHE D CE2 
7147 C  CZ  . PHE D 95  ? 0.1215 0.1181 0.1270 -0.0243 0.0094  -0.0093 95  PHE D CZ  
7148 N  N   . HIS D 96  ? 0.0951 0.0922 0.1158 -0.0035 -0.0044 -0.0023 96  HIS D N   
7149 C  CA  . HIS D 96  ? 0.1044 0.1014 0.1204 0.0019  -0.0015 -0.0015 96  HIS D CA  
7150 C  C   . HIS D 96  ? 0.1132 0.1098 0.0996 0.0027  -0.0159 -0.0055 96  HIS D C   
7151 O  O   . HIS D 96  ? 0.1263 0.1091 0.1066 -0.0030 -0.0148 -0.0012 96  HIS D O   
7152 C  CB  . HIS D 96  ? 0.1003 0.0885 0.1254 -0.0015 -0.0003 0.0073  96  HIS D CB  
7153 C  CG  . HIS D 96  ? 0.0944 0.0962 0.1003 -0.0092 -0.0031 0.0034  96  HIS D CG  
7154 N  ND1 . HIS D 96  ? 0.1128 0.1036 0.1097 -0.0041 -0.0015 0.0109  96  HIS D ND1 
7155 C  CD2 . HIS D 96  ? 0.1265 0.0859 0.1331 0.0027  0.0153  -0.0122 96  HIS D CD2 
7156 C  CE1 . HIS D 96  ? 0.1321 0.1023 0.1138 0.0092  -0.0044 0.0010  96  HIS D CE1 
7157 N  NE2 . HIS D 96  ? 0.1037 0.0892 0.1046 -0.0038 0.0028  0.0010  96  HIS D NE2 
7158 N  N   . TRP D 97  ? 0.0960 0.1021 0.0983 -0.0172 -0.0073 -0.0013 97  TRP D N   
7159 C  CA  . TRP D 97  ? 0.1127 0.0917 0.1337 0.0026  0.0041  -0.0083 97  TRP D CA  
7160 C  C   . TRP D 97  ? 0.1118 0.1154 0.1161 -0.0199 0.0041  -0.0034 97  TRP D C   
7161 O  O   . TRP D 97  ? 0.1357 0.1075 0.1137 -0.0089 0.0000  -0.0037 97  TRP D O   
7162 C  CB  . TRP D 97  ? 0.0948 0.1019 0.1288 -0.0256 -0.0146 0.0127  97  TRP D CB  
7163 C  CG  . TRP D 97  ? 0.1136 0.1040 0.1121 -0.0024 -0.0034 0.0102  97  TRP D CG  
7164 C  CD1 . TRP D 97  ? 0.1229 0.1134 0.1215 -0.0156 -0.0119 0.0034  97  TRP D CD1 
7165 C  CD2 . TRP D 97  ? 0.1112 0.1045 0.1371 -0.0111 -0.0146 0.0148  97  TRP D CD2 
7166 N  NE1 . TRP D 97  ? 0.1321 0.1075 0.1513 0.0000  -0.0237 -0.0083 97  TRP D NE1 
7167 C  CE2 . TRP D 97  ? 0.1383 0.0988 0.1281 -0.0076 -0.0228 0.0041  97  TRP D CE2 
7168 C  CE3 . TRP D 97  ? 0.1118 0.1084 0.1299 -0.0037 -0.0164 -0.0021 97  TRP D CE3 
7169 C  CZ2 . TRP D 97  ? 0.1432 0.1292 0.1412 0.0167  0.0071  0.0176  97  TRP D CZ2 
7170 C  CZ3 . TRP D 97  ? 0.1436 0.1163 0.1581 0.0076  -0.0120 0.0125  97  TRP D CZ3 
7171 C  CH2 . TRP D 97  ? 0.1369 0.1290 0.1507 -0.0103 -0.0138 0.0066  97  TRP D CH2 
7172 N  N   . GLY D 98  ? 0.1147 0.1048 0.1263 -0.0044 -0.0083 0.0007  98  GLY D N   
7173 C  CA  . GLY D 98  ? 0.1206 0.1091 0.1279 0.0007  -0.0261 -0.0176 98  GLY D CA  
7174 C  C   . GLY D 98  ? 0.1289 0.1188 0.1247 -0.0110 0.0038  -0.0071 98  GLY D C   
7175 O  O   . GLY D 98  ? 0.1314 0.1130 0.1592 -0.0133 -0.0006 -0.0027 98  GLY D O   
7176 N  N   . SER D 99  ? 0.1445 0.1306 0.1554 -0.0135 -0.0260 -0.0315 99  SER D N   
7177 C  CA  . SER D 99  ? 0.1960 0.1371 0.1619 -0.0395 -0.0331 -0.0489 99  SER D CA  
7178 C  C   . SER D 99  ? 0.1429 0.1710 0.1683 -0.0258 -0.0197 -0.0237 99  SER D C   
7179 O  O   . SER D 99  ? 0.1890 0.1793 0.2560 -0.0551 -0.0113 -0.0127 99  SER D O   
7180 C  CB  . SER D 99  ? 0.1838 0.1875 0.1708 -0.0310 -0.0241 -0.0531 99  SER D CB  
7181 O  OG  . SER D 99  ? 0.2003 0.1495 0.1863 0.0027  0.0031  -0.0461 99  SER D OG  
7182 N  N   . LEU D 100 ? 0.1750 0.1326 0.1378 -0.0315 -0.0121 -0.0113 100 LEU D N   
7183 C  CA  . LEU D 100 ? 0.2445 0.1181 0.1845 0.0136  -0.0168 0.0052  100 LEU D CA  
7184 C  C   . LEU D 100 ? 0.1730 0.1608 0.1588 -0.0174 0.0031  0.0135  100 LEU D C   
7185 O  O   . LEU D 100 ? 0.1796 0.1199 0.1921 -0.0152 -0.0126 0.0077  100 LEU D O   
7186 C  CB  . LEU D 100 ? 0.2795 0.1947 0.2326 0.0465  0.0193  0.0239  100 LEU D CB  
7187 C  CG  . LEU D 100 ? 0.4065 0.2431 0.2955 0.0156  -0.0153 -0.0308 100 LEU D CG  
7188 C  CD1 . LEU D 100 ? 0.4277 0.6880 0.5037 0.0788  -0.0461 -0.1633 100 LEU D CD1 
7189 C  CD2 . LEU D 100 ? 0.4144 0.2332 0.3964 -0.0759 -0.1404 -0.1553 100 LEU D CD2 
7190 N  N   . ASP D 101 ? 0.2010 0.1498 0.1474 -0.0028 0.0054  0.0093  101 ASP D N   
7191 C  CA  . ASP D 101 ? 0.1782 0.1367 0.1784 0.0256  -0.0051 -0.0020 101 ASP D CA  
7192 C  C   . ASP D 101 ? 0.1615 0.1319 0.1664 0.0052  -0.0183 0.0013  101 ASP D C   
7193 O  O   . ASP D 101 ? 0.2023 0.1380 0.2154 -0.0040 -0.0065 -0.0206 101 ASP D O   
7194 C  CB  . ASP D 101 ? 0.2134 0.1798 0.2104 0.0361  0.0048  0.0555  101 ASP D CB  
7195 C  CG  . ASP D 101 ? 0.2172 0.1822 0.2346 -0.0109 -0.0133 0.0570  101 ASP D CG  
7196 O  OD1 . ASP D 101 ? 0.1877 0.1876 0.2319 0.0008  -0.0241 0.0449  101 ASP D OD1 
7197 O  OD2 . ASP D 101 ? 0.2497 0.2502 0.3059 -0.0324 0.0196  0.1058  101 ASP D OD2 
7198 N  N   . GLY D 102 ? 0.1841 0.1238 0.1867 0.0125  -0.0006 0.0138  102 GLY D N   
7199 C  CA  . GLY D 102 ? 0.1752 0.1324 0.2134 0.0083  0.0480  0.0109  102 GLY D CA  
7200 C  C   . GLY D 102 ? 0.1642 0.1259 0.1838 0.0041  0.0111  0.0026  102 GLY D C   
7201 O  O   . GLY D 102 ? 0.1666 0.1569 0.1999 0.0126  -0.0127 0.0177  102 GLY D O   
7202 N  N   . GLN D 103 ? 0.1540 0.1371 0.1523 -0.0063 0.0015  0.0052  103 GLN D N   
7203 C  CA  . GLN D 103 ? 0.1082 0.1319 0.1423 0.0000  0.0052  0.0164  103 GLN D CA  
7204 C  C   . GLN D 103 ? 0.1191 0.1054 0.1237 -0.0099 -0.0175 -0.0040 103 GLN D C   
7205 O  O   . GLN D 103 ? 0.1281 0.1168 0.1542 -0.0109 0.0027  -0.0078 103 GLN D O   
7206 C  CB  . GLN D 103 ? 0.1662 0.1342 0.1268 0.0124  -0.0337 -0.0062 103 GLN D CB  
7207 C  CG  . GLN D 103 ? 0.1507 0.1324 0.1416 -0.0148 -0.0253 -0.0258 103 GLN D CG  
7208 C  CD  . GLN D 103 ? 0.2393 0.2045 0.1845 0.0608  -0.0463 -0.0439 103 GLN D CD  
7209 O  OE1 . GLN D 103 ? 0.4014 0.3023 0.2469 0.1585  -0.0760 -0.0662 103 GLN D OE1 
7210 N  NE2 . GLN D 103 ? 0.2233 0.1899 0.1502 0.0133  0.0005  -0.0220 103 GLN D NE2 
7211 N  N   . GLY D 104 ? 0.1344 0.0987 0.1028 -0.0082 -0.0087 -0.0010 104 GLY D N   
7212 C  CA  . GLY D 104 ? 0.1204 0.1102 0.1076 -0.0027 -0.0049 0.0054  104 GLY D CA  
7213 C  C   . GLY D 104 ? 0.0918 0.0985 0.1120 0.0010  -0.0043 0.0048  104 GLY D C   
7214 O  O   . GLY D 104 ? 0.1246 0.1177 0.1042 0.0065  -0.0076 0.0140  104 GLY D O   
7215 N  N   . SER D 105 ? 0.1028 0.1057 0.0949 -0.0207 -0.0108 -0.0062 105 SER D N   
7216 C  CA  . SER D 105 ? 0.1037 0.0967 0.0876 -0.0182 -0.0104 -0.0012 105 SER D CA  
7217 C  C   . SER D 105 ? 0.1041 0.0989 0.0994 -0.0031 0.0031  0.0038  105 SER D C   
7218 O  O   . SER D 105 ? 0.1272 0.1084 0.1263 -0.0105 0.0088  -0.0100 105 SER D O   
7219 C  CB  . SER D 105 ? 0.1057 0.1062 0.1041 0.0060  -0.0144 0.0131  105 SER D CB  
7220 O  OG  . SER D 105 ? 0.1244 0.0816 0.1146 -0.0006 0.0000  0.0076  105 SER D OG  
7221 N  N   . GLU D 106 ? 0.0913 0.0987 0.0976 -0.0097 -0.0091 -0.0019 106 GLU D N   
7222 C  CA  . GLU D 106 ? 0.0976 0.0961 0.1079 0.0076  0.0080  0.0001  106 GLU D CA  
7223 C  C   . GLU D 106 ? 0.0945 0.0906 0.0980 -0.0094 0.0060  0.0006  106 GLU D C   
7224 O  O   . GLU D 106 ? 0.1035 0.0983 0.1003 -0.0026 0.0071  -0.0032 106 GLU D O   
7225 C  CB  . GLU D 106 ? 0.1050 0.0956 0.1052 -0.0001 -0.0140 0.0115  106 GLU D CB  
7226 C  CG  . GLU D 106 ? 0.1173 0.1197 0.1335 -0.0126 -0.0320 0.0304  106 GLU D CG  
7227 C  CD  . GLU D 106 ? 0.1260 0.1143 0.0908 -0.0087 -0.0143 0.0068  106 GLU D CD  
7228 O  OE1 . GLU D 106 ? 0.1362 0.1071 0.1111 -0.0023 0.0024  0.0026  106 GLU D OE1 
7229 O  OE2 . GLU D 106 ? 0.1540 0.1299 0.0974 -0.0135 0.0063  -0.0052 106 GLU D OE2 
7230 N  N   . HIS D 107 ? 0.0969 0.0866 0.0926 0.0068  -0.0024 -0.0068 107 HIS D N   
7231 C  CA  . HIS D 107 ? 0.0976 0.0847 0.0834 0.0005  -0.0076 0.0012  107 HIS D CA  
7232 C  C   . HIS D 107 ? 0.1066 0.0958 0.0996 -0.0133 0.0015  -0.0008 107 HIS D C   
7233 O  O   . HIS D 107 ? 0.1017 0.0954 0.1068 0.0059  -0.0028 0.0059  107 HIS D O   
7234 C  CB  . HIS D 107 ? 0.1222 0.0906 0.0818 -0.0108 0.0027  0.0020  107 HIS D CB  
7235 C  CG  . HIS D 107 ? 0.0971 0.1032 0.0931 -0.0055 -0.0237 0.0010  107 HIS D CG  
7236 N  ND1 . HIS D 107 ? 0.0991 0.0888 0.0856 0.0043  0.0120  0.0000  107 HIS D ND1 
7237 C  CD2 . HIS D 107 ? 0.1039 0.1023 0.0866 -0.0155 0.0114  -0.0147 107 HIS D CD2 
7238 C  CE1 . HIS D 107 ? 0.1019 0.0947 0.0906 -0.0120 -0.0006 -0.0052 107 HIS D CE1 
7239 N  NE2 . HIS D 107 ? 0.1033 0.0940 0.0903 -0.0057 0.0122  -0.0035 107 HIS D NE2 
7240 N  N   . THR D 108 ? 0.1156 0.0949 0.0969 -0.0019 -0.0141 0.0175  108 THR D N   
7241 C  CA  . THR D 108 ? 0.1259 0.0813 0.0978 0.0115  -0.0266 -0.0098 108 THR D CA  
7242 C  C   . THR D 108 ? 0.0848 0.0897 0.0960 -0.0063 0.0006  0.0057  108 THR D C   
7243 O  O   . THR D 108 ? 0.0992 0.1005 0.1012 -0.0065 -0.0013 -0.0103 108 THR D O   
7244 C  CB  . THR D 108 ? 0.0906 0.1355 0.1082 -0.0017 0.0098  -0.0144 108 THR D CB  
7245 O  OG1 . THR D 108 ? 0.1052 0.1206 0.1355 -0.0026 0.0097  -0.0066 108 THR D OG1 
7246 C  CG2 . THR D 108 ? 0.1249 0.1222 0.1176 -0.0024 -0.0133 -0.0027 108 THR D CG2 
7247 N  N   . VAL D 109 ? 0.1107 0.0973 0.1070 0.0152  -0.0082 0.0110  109 VAL D N   
7248 C  CA  . VAL D 109 ? 0.1231 0.0994 0.1093 0.0024  -0.0195 -0.0010 109 VAL D CA  
7249 C  C   . VAL D 109 ? 0.1268 0.1224 0.1103 0.0010  -0.0076 -0.0007 109 VAL D C   
7250 O  O   . VAL D 109 ? 0.1439 0.1123 0.1190 0.0087  0.0038  0.0005  109 VAL D O   
7251 C  CB  . VAL D 109 ? 0.1350 0.1093 0.1170 0.0320  -0.0055 -0.0021 109 VAL D CB  
7252 C  CG1 . VAL D 109 ? 0.1619 0.1540 0.1202 0.0070  -0.0155 0.0054  109 VAL D CG1 
7253 C  CG2 . VAL D 109 ? 0.1292 0.1350 0.1396 0.0410  -0.0023 0.0026  109 VAL D CG2 
7254 N  N   . ASP D 110 ? 0.1058 0.1055 0.1574 0.0176  -0.0266 -0.0013 110 ASP D N   
7255 C  CA  . ASP D 110 ? 0.1599 0.1195 0.1393 0.0390  -0.0142 -0.0178 110 ASP D CA  
7256 C  C   . ASP D 110 ? 0.1242 0.1281 0.1483 0.0237  -0.0148 -0.0205 110 ASP D C   
7257 O  O   . ASP D 110 ? 0.1621 0.1362 0.1678 0.0278  -0.0142 0.0024  110 ASP D O   
7258 C  CB  . ASP D 110 ? 0.1626 0.1563 0.1795 0.0292  -0.0631 0.0132  110 ASP D CB  
7259 C  CG  . ASP D 110 ? 0.1815 0.1432 0.1656 0.0287  -0.0383 -0.0013 110 ASP D CG  
7260 O  OD1 . ASP D 110 ? 0.2041 0.1504 0.1919 0.0299  -0.0241 -0.0034 110 ASP D OD1 
7261 O  OD2 . ASP D 110 ? 0.2163 0.2341 0.1913 0.0604  -0.0245 0.0218  110 ASP D OD2 
7262 N  N   . LYS D 111 ? 0.1274 0.1184 0.1450 0.0060  -0.0059 -0.0109 111 LYS D N   
7263 C  CA  . LYS D 111 ? 0.1342 0.1127 0.1368 0.0186  -0.0027 -0.0199 111 LYS D CA  
7264 C  C   . LYS D 111 ? 0.1457 0.0965 0.1376 0.0066  -0.0160 -0.0027 111 LYS D C   
7265 O  O   . LYS D 111 ? 0.1610 0.1371 0.1290 0.0155  -0.0153 -0.0085 111 LYS D O   
7266 C  CB  . LYS D 111 ? 0.1495 0.1597 0.1899 0.0230  -0.0010 -0.0485 111 LYS D CB  
7267 C  CG  . LYS D 111 ? 0.1509 0.1922 0.2730 0.0201  0.0156  -0.0197 111 LYS D CG  
7268 C  CD  . LYS D 111 ? 0.2269 0.3537 0.1836 -0.0432 0.0294  -0.0173 111 LYS D CD  
7269 C  CE  . LYS D 111 ? 0.2639 0.3758 0.2960 -0.0778 0.0791  -0.0586 111 LYS D CE  
7270 N  NZ  . LYS D 111 ? 0.3145 0.3079 0.2777 0.0375  0.0715  0.0148  111 LYS D NZ  
7271 N  N   . LYS D 112 ? 0.1159 0.0989 0.1545 0.0122  0.0046  -0.0116 112 LYS D N   
7272 C  CA  . LYS D 112 ? 0.1233 0.1249 0.1441 -0.0054 -0.0315 -0.0026 112 LYS D CA  
7273 C  C   . LYS D 112 ? 0.1186 0.1068 0.1179 0.0060  -0.0057 -0.0096 112 LYS D C   
7274 O  O   . LYS D 112 ? 0.1268 0.1009 0.1392 -0.0055 -0.0065 -0.0049 112 LYS D O   
7275 C  CB  . LYS D 112 ? 0.1258 0.1459 0.1597 0.0146  -0.0086 0.0081  112 LYS D CB  
7276 C  CG  . LYS D 112 ? 0.1395 0.1981 0.1504 -0.0234 0.0031  0.0113  112 LYS D CG  
7277 C  CD  . LYS D 112 ? 0.1574 0.2002 0.1798 -0.0003 0.0342  0.0003  112 LYS D CD  
7278 C  CE  . LYS D 112 ? 0.1781 0.2294 0.2271 -0.0168 0.0248  0.0015  112 LYS D CE  
7279 N  NZ  . LYS D 112 ? 0.2418 0.2005 0.3296 -0.0020 0.0582  0.0166  112 LYS D NZ  
7280 N  N   A LYS D 113 ? 0.1177 0.1274 0.1132 0.0021  -0.0183 -0.0046 113 LYS D N   
7281 N  N   B LYS D 113 ? 0.1188 0.1234 0.1203 0.0005  -0.0163 -0.0133 113 LYS D N   
7282 C  CA  A LYS D 113 ? 0.1143 0.1014 0.1170 0.0083  0.0049  -0.0020 113 LYS D CA  
7283 C  CA  B LYS D 113 ? 0.1167 0.1213 0.1136 0.0120  0.0107  -0.0035 113 LYS D CA  
7284 C  C   A LYS D 113 ? 0.1224 0.0922 0.0980 0.0001  -0.0013 0.0098  113 LYS D C   
7285 C  C   B LYS D 113 ? 0.1382 0.0973 0.1298 0.0037  0.0196  0.0068  113 LYS D C   
7286 O  O   A LYS D 113 ? 0.1116 0.0813 0.1102 0.0043  0.0088  0.0041  113 LYS D O   
7287 O  O   B LYS D 113 ? 0.1574 0.1071 0.1317 -0.0207 0.0019  0.0121  113 LYS D O   
7288 C  CB  A LYS D 113 ? 0.1177 0.1203 0.1240 0.0104  0.0071  -0.0104 113 LYS D CB  
7289 C  CB  B LYS D 113 ? 0.1295 0.1102 0.1220 -0.0006 0.0156  -0.0228 113 LYS D CB  
7290 C  CG  A LYS D 113 ? 0.1335 0.0903 0.1265 0.0049  0.0115  -0.0017 113 LYS D CG  
7291 C  CG  B LYS D 113 ? 0.0908 0.1613 0.1204 0.0107  -0.0010 -0.0245 113 LYS D CG  
7292 C  CD  A LYS D 113 ? 0.1375 0.1511 0.1274 -0.0188 0.0080  -0.0144 113 LYS D CD  
7293 C  CD  B LYS D 113 ? 0.1181 0.1082 0.1246 -0.0019 0.0126  -0.0146 113 LYS D CD  
7294 C  CE  A LYS D 113 ? 0.1836 0.1662 0.1580 -0.0093 0.0337  -0.0126 113 LYS D CE  
7295 C  CE  B LYS D 113 ? 0.0935 0.1714 0.1779 -0.0066 0.0132  -0.0076 113 LYS D CE  
7296 N  NZ  A LYS D 113 ? 0.1875 0.1906 0.2037 0.0000  0.0346  -0.0359 113 LYS D NZ  
7297 N  NZ  B LYS D 113 ? 0.2551 0.2108 0.1813 0.0259  0.0326  -0.0104 113 LYS D NZ  
7298 N  N   . TYR D 114 ? 0.1206 0.1132 0.1204 0.0092  0.0066  -0.0080 114 TYR D N   
7299 C  CA  . TYR D 114 ? 0.1181 0.1070 0.1073 0.0005  0.0099  -0.0055 114 TYR D CA  
7300 C  C   . TYR D 114 ? 0.1216 0.0982 0.1172 0.0060  0.0006  0.0140  114 TYR D C   
7301 O  O   . TYR D 114 ? 0.1208 0.1105 0.1213 -0.0054 -0.0038 0.0065  114 TYR D O   
7302 C  CB  . TYR D 114 ? 0.1633 0.1185 0.0947 0.0318  -0.0030 -0.0148 114 TYR D CB  
7303 C  CG  . TYR D 114 ? 0.1127 0.1240 0.1231 0.0099  0.0100  -0.0024 114 TYR D CG  
7304 C  CD1 . TYR D 114 ? 0.1486 0.1170 0.1687 -0.0171 -0.0111 -0.0132 114 TYR D CD1 
7305 C  CD2 . TYR D 114 ? 0.1615 0.1234 0.1256 0.0062  0.0006  0.0142  114 TYR D CD2 
7306 C  CE1 . TYR D 114 ? 0.1640 0.1658 0.1843 -0.0041 -0.0175 -0.0445 114 TYR D CE1 
7307 C  CE2 . TYR D 114 ? 0.1777 0.1662 0.1551 0.0221  -0.0229 -0.0071 114 TYR D CE2 
7308 C  CZ  . TYR D 114 ? 0.1802 0.1743 0.1604 0.0197  -0.0469 0.0104  114 TYR D CZ  
7309 O  OH  . TYR D 114 ? 0.2551 0.2291 0.1912 0.0241  -0.0595 0.0027  114 TYR D OH  
7310 N  N   . ALA D 115 ? 0.1199 0.1006 0.1391 0.0109  0.0076  0.0149  115 ALA D N   
7311 C  CA  . ALA D 115 ? 0.1295 0.0754 0.1412 -0.0028 0.0000  0.0023  115 ALA D CA  
7312 C  C   . ALA D 115 ? 0.1103 0.0879 0.1140 0.0015  -0.0093 -0.0024 115 ALA D C   
7313 O  O   . ALA D 115 ? 0.1339 0.0961 0.1188 -0.0099 -0.0030 -0.0054 115 ALA D O   
7314 C  CB  . ALA D 115 ? 0.1499 0.1094 0.1592 -0.0102 0.0225  -0.0006 115 ALA D CB  
7315 N  N   . ALA D 116 ? 0.1137 0.0847 0.1216 -0.0005 -0.0097 -0.0046 116 ALA D N   
7316 C  CA  . ALA D 116 ? 0.1039 0.0813 0.1168 -0.0049 -0.0060 0.0000  116 ALA D CA  
7317 C  C   . ALA D 116 ? 0.0949 0.0944 0.0924 0.0005  -0.0010 0.0023  116 ALA D C   
7318 O  O   . ALA D 116 ? 0.0957 0.0983 0.1024 0.0006  -0.0024 0.0113  116 ALA D O   
7319 C  CB  . ALA D 116 ? 0.0965 0.1168 0.1216 -0.0031 -0.0006 0.0109  116 ALA D CB  
7320 N  N   . GLU D 117 ? 0.1042 0.0930 0.1079 -0.0066 -0.0001 0.0010  117 GLU D N   
7321 C  CA  . GLU D 117 ? 0.1005 0.0806 0.1254 0.0082  0.0066  -0.0129 117 GLU D CA  
7322 C  C   . GLU D 117 ? 0.0755 0.0908 0.0924 -0.0081 -0.0149 -0.0006 117 GLU D C   
7323 O  O   . GLU D 117 ? 0.1213 0.1100 0.0997 0.0048  -0.0092 0.0114  117 GLU D O   
7324 C  CB  . GLU D 117 ? 0.0956 0.1093 0.0942 -0.0049 0.0027  0.0041  117 GLU D CB  
7325 C  CG  . GLU D 117 ? 0.0930 0.1080 0.1380 -0.0109 -0.0074 -0.0051 117 GLU D CG  
7326 C  CD  . GLU D 117 ? 0.1190 0.1154 0.0947 0.0000  0.0131  -0.0091 117 GLU D CD  
7327 O  OE1 . GLU D 117 ? 0.1102 0.1019 0.1107 -0.0115 0.0097  -0.0066 117 GLU D OE1 
7328 O  OE2 . GLU D 117 ? 0.0913 0.1107 0.1396 -0.0032 0.0099  0.0015  117 GLU D OE2 
7329 N  N   . LEU D 118 ? 0.1040 0.0895 0.1106 0.0074  0.0116  0.0013  118 LEU D N   
7330 C  CA  . LEU D 118 ? 0.1048 0.0782 0.1028 -0.0013 -0.0066 0.0142  118 LEU D CA  
7331 C  C   . LEU D 118 ? 0.0879 0.1001 0.1010 0.0046  0.0007  0.0141  118 LEU D C   
7332 O  O   . LEU D 118 ? 0.1044 0.0978 0.1015 0.0080  -0.0126 0.0119  118 LEU D O   
7333 C  CB  . LEU D 118 ? 0.0985 0.1071 0.1058 0.0059  0.0015  -0.0046 118 LEU D CB  
7334 C  CG  . LEU D 118 ? 0.1303 0.1035 0.1076 0.0201  0.0137  0.0000  118 LEU D CG  
7335 C  CD1 . LEU D 118 ? 0.1303 0.1068 0.1421 0.0245  0.0172  0.0149  118 LEU D CD1 
7336 C  CD2 . LEU D 118 ? 0.1208 0.1432 0.1310 0.0098  0.0337  -0.0066 118 LEU D CD2 
7337 N  N   . HIS D 119 ? 0.0992 0.0721 0.1032 0.0054  0.0137  0.0081  119 HIS D N   
7338 C  CA  . HIS D 119 ? 0.0933 0.0827 0.1030 -0.0040 0.0049  -0.0049 119 HIS D CA  
7339 C  C   . HIS D 119 ? 0.0976 0.0839 0.1070 -0.0007 -0.0120 -0.0003 119 HIS D C   
7340 O  O   . HIS D 119 ? 0.1132 0.1010 0.1233 0.0000  -0.0119 0.0032  119 HIS D O   
7341 C  CB  . HIS D 119 ? 0.1155 0.0839 0.1136 0.0052  0.0263  -0.0051 119 HIS D CB  
7342 C  CG  . HIS D 119 ? 0.0820 0.0797 0.0773 -0.0162 -0.0076 -0.0059 119 HIS D CG  
7343 N  ND1 . HIS D 119 ? 0.1009 0.0933 0.0789 0.0049  0.0065  0.0107  119 HIS D ND1 
7344 C  CD2 . HIS D 119 ? 0.1044 0.0854 0.1137 0.0020  -0.0048 0.0068  119 HIS D CD2 
7345 C  CE1 . HIS D 119 ? 0.0996 0.0899 0.1141 -0.0068 -0.0003 0.0000  119 HIS D CE1 
7346 N  NE2 . HIS D 119 ? 0.0945 0.1147 0.1221 -0.0031 0.0065  0.0021  119 HIS D NE2 
7347 N  N   . LEU D 120 ? 0.0964 0.0763 0.0962 -0.0030 -0.0024 0.0074  120 LEU D N   
7348 C  CA  . LEU D 120 ? 0.1098 0.0856 0.1147 -0.0020 0.0125  -0.0114 120 LEU D CA  
7349 C  C   . LEU D 120 ? 0.1045 0.0974 0.0980 0.0055  -0.0023 0.0044  120 LEU D C   
7350 O  O   . LEU D 120 ? 0.1033 0.0958 0.1114 0.0046  -0.0093 0.0041  120 LEU D O   
7351 C  CB  . LEU D 120 ? 0.1120 0.1082 0.1128 -0.0054 0.0120  -0.0388 120 LEU D CB  
7352 C  CG  . LEU D 120 ? 0.1225 0.1228 0.1337 0.0054  0.0093  -0.0020 120 LEU D CG  
7353 C  CD1 . LEU D 120 ? 0.1655 0.1423 0.2125 -0.0052 -0.0092 0.0469  120 LEU D CD1 
7354 C  CD2 . LEU D 120 ? 0.1265 0.1667 0.1755 0.0028  0.0303  -0.0291 120 LEU D CD2 
7355 N  N   . VAL D 121 ? 0.1199 0.1068 0.1073 0.0000  -0.0087 0.0092  121 VAL D N   
7356 C  CA  . VAL D 121 ? 0.1228 0.0949 0.1161 -0.0073 0.0020  -0.0019 121 VAL D CA  
7357 C  C   . VAL D 121 ? 0.1290 0.0945 0.1270 0.0037  -0.0107 0.0032  121 VAL D C   
7358 O  O   . VAL D 121 ? 0.1184 0.1133 0.1547 -0.0027 -0.0103 -0.0010 121 VAL D O   
7359 C  CB  . VAL D 121 ? 0.1116 0.0942 0.1233 0.0032  -0.0083 0.0065  121 VAL D CB  
7360 C  CG1 . VAL D 121 ? 0.1504 0.1350 0.1121 -0.0194 0.0103  0.0130  121 VAL D CG1 
7361 C  CG2 . VAL D 121 ? 0.1569 0.1322 0.1316 -0.0010 -0.0140 -0.0348 121 VAL D CG2 
7362 N  N   . HIS D 122 ? 0.1140 0.0885 0.1289 -0.0115 -0.0063 0.0146  122 HIS D N   
7363 C  CA  . HIS D 122 ? 0.1447 0.0926 0.1384 -0.0006 0.0085  -0.0001 122 HIS D CA  
7364 C  C   . HIS D 122 ? 0.1267 0.1073 0.1310 0.0052  0.0040  -0.0030 122 HIS D C   
7365 O  O   . HIS D 122 ? 0.1263 0.0877 0.1506 0.0024  0.0006  -0.0049 122 HIS D O   
7366 C  CB  . HIS D 122 ? 0.1277 0.1032 0.1278 0.0152  0.0076  -0.0017 122 HIS D CB  
7367 C  CG  . HIS D 122 ? 0.1368 0.0910 0.1344 0.0220  -0.0051 0.0142  122 HIS D CG  
7368 N  ND1 . HIS D 122 ? 0.1242 0.0886 0.1213 0.0255  0.0086  0.0051  122 HIS D ND1 
7369 C  CD2 . HIS D 122 ? 0.1322 0.1251 0.1340 0.0119  -0.0063 0.0046  122 HIS D CD2 
7370 C  CE1 . HIS D 122 ? 0.1274 0.1296 0.1535 -0.0073 0.0184  0.0007  122 HIS D CE1 
7371 N  NE2 . HIS D 122 ? 0.1215 0.1306 0.1499 -0.0024 0.0190  -0.0082 122 HIS D NE2 
7372 N  N   . TRP D 123 ? 0.1174 0.1098 0.1312 0.0057  0.0156  0.0068  123 TRP D N   
7373 C  CA  . TRP D 123 ? 0.1513 0.1091 0.1319 -0.0183 -0.0063 0.0035  123 TRP D CA  
7374 C  C   . TRP D 123 ? 0.1349 0.0926 0.1281 -0.0054 0.0046  -0.0003 123 TRP D C   
7375 O  O   . TRP D 123 ? 0.1301 0.1231 0.1471 0.0000  -0.0026 -0.0028 123 TRP D O   
7376 C  CB  . TRP D 123 ? 0.1511 0.1288 0.1660 -0.0010 -0.0255 0.0141  123 TRP D CB  
7377 C  CG  . TRP D 123 ? 0.1639 0.1133 0.1920 0.0082  -0.0017 0.0189  123 TRP D CG  
7378 C  CD1 . TRP D 123 ? 0.1703 0.1544 0.1969 0.0027  0.0113  0.0125  123 TRP D CD1 
7379 C  CD2 . TRP D 123 ? 0.1630 0.1260 0.1723 0.0129  -0.0428 0.0023  123 TRP D CD2 
7380 N  NE1 . TRP D 123 ? 0.1809 0.1421 0.2443 -0.0007 -0.0159 0.0126  123 TRP D NE1 
7381 C  CE2 . TRP D 123 ? 0.1712 0.1228 0.2213 0.0165  -0.0315 0.0013  123 TRP D CE2 
7382 C  CE3 . TRP D 123 ? 0.1717 0.1221 0.2012 0.0012  -0.0388 -0.0003 123 TRP D CE3 
7383 C  CZ2 . TRP D 123 ? 0.2172 0.1437 0.2531 0.0401  -0.0262 0.0275  123 TRP D CZ2 
7384 C  CZ3 . TRP D 123 ? 0.2117 0.1010 0.2531 0.0182  -0.0467 0.0313  123 TRP D CZ3 
7385 C  CH2 . TRP D 123 ? 0.2208 0.1802 0.2240 -0.0065 -0.0425 0.0463  123 TRP D CH2 
7386 N  N   . ASN D 124 ? 0.1289 0.1319 0.1456 0.0001  0.0013  -0.0186 124 ASN D N   
7387 C  CA  . ASN D 124 ? 0.1554 0.1037 0.1809 -0.0071 -0.0125 -0.0291 124 ASN D CA  
7388 C  C   . ASN D 124 ? 0.1405 0.1252 0.1299 -0.0185 0.0000  -0.0085 124 ASN D C   
7389 O  O   . ASN D 124 ? 0.1687 0.1174 0.1450 -0.0040 -0.0051 0.0082  124 ASN D O   
7390 C  CB  . ASN D 124 ? 0.1674 0.1172 0.1730 -0.0208 -0.0088 -0.0204 124 ASN D CB  
7391 C  CG  . ASN D 124 ? 0.1386 0.1130 0.1434 -0.0142 0.0133  0.0041  124 ASN D CG  
7392 O  OD1 . ASN D 124 ? 0.1942 0.1208 0.1718 -0.0093 -0.0063 -0.0262 124 ASN D OD1 
7393 N  ND2 . ASN D 124 ? 0.1696 0.1061 0.1899 -0.0167 -0.0126 0.0000  124 ASN D ND2 
7394 N  N   . THR D 125 ? 0.1484 0.1234 0.1640 0.0052  0.0041  -0.0088 125 THR D N   
7395 C  CA  . THR D 125 ? 0.1678 0.1278 0.2253 0.0110  0.0232  -0.0212 125 THR D CA  
7396 C  C   . THR D 125 ? 0.1971 0.1435 0.1869 0.0023  -0.0175 -0.0164 125 THR D C   
7397 O  O   . THR D 125 ? 0.2280 0.1427 0.2089 0.0155  -0.0221 -0.0062 125 THR D O   
7398 C  CB  . THR D 125 ? 0.2029 0.1547 0.2194 0.0197  0.0186  -0.0068 125 THR D CB  
7399 O  OG1 . THR D 125 ? 0.3194 0.1657 0.2240 0.0373  -0.0146 -0.0491 125 THR D OG1 
7400 C  CG2 . THR D 125 ? 0.2269 0.1793 0.2655 0.0041  0.0505  0.0000  125 THR D CG2 
7401 N  N   . LYS D 126 ? 0.2141 0.1209 0.1987 -0.0263 -0.0261 -0.0260 127 LYS D N   
7402 C  CA  . LYS D 126 ? 0.1980 0.1603 0.2052 -0.0535 -0.0505 -0.0019 127 LYS D CA  
7403 C  C   . LYS D 126 ? 0.1947 0.1274 0.1903 -0.0038 -0.0259 0.0125  127 LYS D C   
7404 O  O   . LYS D 126 ? 0.2703 0.1235 0.2296 -0.0260 -0.0406 0.0276  127 LYS D O   
7405 C  CB  . LYS D 126 ? 0.2012 0.1748 0.2321 -0.0280 -0.0164 0.0008  127 LYS D CB  
7406 C  CG  . LYS D 126 ? 0.2108 0.1676 0.2307 -0.0480 -0.0076 -0.0089 127 LYS D CG  
7407 C  CD  . LYS D 126 ? 0.2454 0.2779 0.2971 -0.0472 -0.0520 0.0879  127 LYS D CD  
7408 C  CE  . LYS D 126 ? 0.3564 0.2892 0.3438 -0.0555 0.0428  0.0359  127 LYS D CE  
7409 N  NZ  . LYS D 126 ? 0.2406 0.4027 0.4690 -0.0012 -0.0577 -0.0419 127 LYS D NZ  
7410 N  N   . TYR D 127 ? 0.1665 0.1450 0.2010 -0.0221 -0.0342 -0.0003 128 TYR D N   
7411 C  CA  . TYR D 127 ? 0.1511 0.1351 0.1937 -0.0005 0.0077  -0.0154 128 TYR D CA  
7412 C  C   . TYR D 127 ? 0.1876 0.0985 0.1624 -0.0296 0.0010  0.0013  128 TYR D C   
7413 O  O   . TYR D 127 ? 0.1924 0.1206 0.1976 -0.0038 -0.0259 0.0001  128 TYR D O   
7414 C  CB  . TYR D 127 ? 0.1859 0.1351 0.1734 -0.0046 -0.0141 -0.0155 128 TYR D CB  
7415 C  CG  . TYR D 127 ? 0.1588 0.1290 0.1888 -0.0065 -0.0219 -0.0017 128 TYR D CG  
7416 C  CD1 . TYR D 127 ? 0.1714 0.1452 0.2082 -0.0263 -0.0010 -0.0366 128 TYR D CD1 
7417 C  CD2 . TYR D 127 ? 0.1700 0.1212 0.1917 0.0104  0.0163  -0.0060 128 TYR D CD2 
7418 C  CE1 . TYR D 127 ? 0.1822 0.1216 0.2305 -0.0085 -0.0326 -0.0233 128 TYR D CE1 
7419 C  CE2 . TYR D 127 ? 0.1741 0.1744 0.1603 -0.0295 -0.0231 -0.0114 128 TYR D CE2 
7420 C  CZ  . TYR D 127 ? 0.1457 0.1349 0.1893 0.0093  -0.0063 -0.0217 128 TYR D CZ  
7421 O  OH  . TYR D 127 ? 0.1549 0.1696 0.2165 -0.0119 -0.0272 -0.0335 128 TYR D OH  
7422 N  N   . GLY D 128 ? 0.1524 0.1172 0.1904 0.0091  -0.0116 0.0081  129 GLY D N   
7423 C  CA  . GLY D 128 ? 0.1700 0.1328 0.1850 0.0100  -0.0423 -0.0015 129 GLY D CA  
7424 C  C   . GLY D 128 ? 0.1493 0.1387 0.1928 0.0024  -0.0160 0.0166  129 GLY D C   
7425 O  O   . GLY D 128 ? 0.1847 0.1170 0.2596 0.0082  -0.0109 0.0281  129 GLY D O   
7426 N  N   . ASP D 129 ? 0.1703 0.1563 0.2127 -0.0107 -0.0320 0.0020  130 ASP D N   
7427 C  CA  . ASP D 129 ? 0.1851 0.1299 0.2282 0.0147  -0.0476 -0.0262 130 ASP D CA  
7428 C  C   . ASP D 129 ? 0.1563 0.1556 0.2363 -0.0252 0.0096  -0.0182 130 ASP D C   
7429 O  O   . ASP D 129 ? 0.1637 0.1402 0.2648 -0.0041 -0.0230 0.0023  130 ASP D O   
7430 C  CB  . ASP D 129 ? 0.1962 0.2278 0.2499 0.0630  -0.0491 -0.0425 130 ASP D CB  
7431 C  CG  . ASP D 129 ? 0.3384 0.1653 0.2560 0.0414  -0.0544 -0.0894 130 ASP D CG  
7432 O  OD1 . ASP D 129 ? 0.3222 0.2739 0.5691 0.0452  0.0671  0.1270  130 ASP D OD1 
7433 O  OD2 . ASP D 129 ? 0.6248 0.3513 0.3165 0.2146  -0.0038 0.0732  130 ASP D OD2 
7434 N  N   . PHE D 130 ? 0.1732 0.1462 0.2481 -0.0115 -0.0513 -0.0252 131 PHE D N   
7435 C  CA  . PHE D 130 ? 0.2034 0.1596 0.2520 -0.0071 -0.0241 0.0281  131 PHE D CA  
7436 C  C   . PHE D 130 ? 0.2023 0.1554 0.2142 0.0054  -0.0223 -0.0005 131 PHE D C   
7437 O  O   . PHE D 130 ? 0.1736 0.1547 0.1919 -0.0148 -0.0206 0.0131  131 PHE D O   
7438 C  CB  . PHE D 130 ? 0.2319 0.1910 0.3021 -0.0631 -0.0434 0.0463  131 PHE D CB  
7439 C  CG  . PHE D 130 ? 0.2960 0.1942 0.3012 -0.0054 -0.0217 -0.0207 131 PHE D CG  
7440 C  CD1 . PHE D 130 ? 0.2172 0.3917 0.4891 -0.0662 -0.0833 -0.1010 131 PHE D CD1 
7441 C  CD2 . PHE D 130 ? 0.2669 0.2433 0.3059 -0.0247 -0.0049 -0.0280 131 PHE D CD2 
7442 C  CE1 . PHE D 130 ? 0.3919 0.6129 0.4557 0.0190  -0.1687 -0.1534 131 PHE D CE1 
7443 C  CE2 . PHE D 130 ? 0.3937 0.3070 0.4381 -0.0233 -0.1444 -0.0524 131 PHE D CE2 
7444 C  CZ  . PHE D 130 ? 0.4524 0.4120 0.4726 0.1451  -0.0791 -0.1092 131 PHE D CZ  
7445 N  N   . GLY D 131 ? 0.2136 0.1682 0.2036 -0.0296 -0.0560 0.0031  132 GLY D N   
7446 C  CA  . GLY D 131 ? 0.1676 0.1851 0.1750 0.0017  -0.0456 -0.0071 132 GLY D CA  
7447 C  C   . GLY D 131 ? 0.1710 0.1734 0.1739 0.0229  -0.0443 0.0207  132 GLY D C   
7448 O  O   . GLY D 131 ? 0.2441 0.1766 0.2213 -0.0281 -0.0081 -0.0083 132 GLY D O   
7449 N  N   . LYS D 132 ? 0.1992 0.1579 0.1953 -0.0076 -0.0535 0.0362  133 LYS D N   
7450 C  CA  . LYS D 132 ? 0.1878 0.1594 0.2129 -0.0060 -0.0518 0.0269  133 LYS D CA  
7451 C  C   . LYS D 132 ? 0.1671 0.1772 0.1452 0.0142  0.0155  0.0063  133 LYS D C   
7452 O  O   . LYS D 132 ? 0.1757 0.1486 0.1915 -0.0251 0.0001  0.0438  133 LYS D O   
7453 C  CB  . LYS D 132 ? 0.2111 0.1405 0.2151 -0.0148 -0.0285 0.0104  133 LYS D CB  
7454 C  CG  . LYS D 132 ? 0.3118 0.1870 0.2702 0.0754  0.0346  0.0423  133 LYS D CG  
7455 C  CD  . LYS D 132 ? 0.4287 0.2490 0.3648 0.0895  0.1152  0.0322  133 LYS D CD  
7456 C  CE  . LYS D 132 ? 0.2919 0.2930 0.6279 -0.1585 0.1783  0.1833  133 LYS D CE  
7457 N  NZ  . LYS D 132 ? 0.5304 0.9476 0.8457 -0.0186 -0.0549 0.0032  133 LYS D NZ  
7458 N  N   . ALA D 133 ? 0.1558 0.1344 0.1587 -0.0116 -0.0142 0.0199  134 ALA D N   
7459 C  CA  . ALA D 133 ? 0.1335 0.1703 0.1596 0.0038  -0.0408 0.0059  134 ALA D CA  
7460 C  C   . ALA D 133 ? 0.1477 0.1265 0.1509 -0.0049 -0.0164 0.0331  134 ALA D C   
7461 O  O   . ALA D 133 ? 0.1342 0.1459 0.1493 -0.0081 -0.0149 0.0151  134 ALA D O   
7462 C  CB  . ALA D 133 ? 0.1908 0.1358 0.1687 -0.0199 -0.0091 0.0205  134 ALA D CB  
7463 N  N   . VAL D 134 ? 0.1623 0.1301 0.1525 -0.0182 -0.0097 0.0156  135 VAL D N   
7464 C  CA  . VAL D 134 ? 0.1563 0.1671 0.1486 0.0012  -0.0254 -0.0077 135 VAL D CA  
7465 C  C   . VAL D 134 ? 0.1888 0.1721 0.1337 0.0185  -0.0153 0.0105  135 VAL D C   
7466 O  O   . VAL D 134 ? 0.1746 0.1777 0.1504 -0.0135 -0.0167 -0.0076 135 VAL D O   
7467 C  CB  . VAL D 134 ? 0.1631 0.1599 0.1865 -0.0211 -0.0516 0.0136  135 VAL D CB  
7468 C  CG1 . VAL D 134 ? 0.2111 0.2152 0.1698 -0.0535 -0.0209 0.0355  135 VAL D CG1 
7469 C  CG2 . VAL D 134 ? 0.2542 0.1976 0.1479 -0.0306 -0.0449 0.0187  135 VAL D CG2 
7470 N  N   . GLN D 135 ? 0.1814 0.1547 0.1660 -0.0274 -0.0324 0.0267  136 GLN D N   
7471 C  CA  . GLN D 135 ? 0.1903 0.1455 0.1805 -0.0046 -0.0082 0.0148  136 GLN D CA  
7472 C  C   . GLN D 135 ? 0.1631 0.1799 0.1551 -0.0102 0.0164  0.0068  136 GLN D C   
7473 O  O   . GLN D 135 ? 0.2057 0.2204 0.2113 -0.0328 0.0076  0.0529  136 GLN D O   
7474 C  CB  . GLN D 135 ? 0.1947 0.1796 0.1861 0.0017  -0.0071 0.0505  136 GLN D CB  
7475 C  CG  . GLN D 135 ? 0.2558 0.2398 0.1813 0.0322  -0.0445 0.0637  136 GLN D CG  
7476 C  CD  . GLN D 135 ? 0.3831 0.2874 0.2637 0.0024  -0.0381 0.1217  136 GLN D CD  
7477 O  OE1 . GLN D 135 ? 0.5800 0.5151 0.4715 -0.0555 0.0183  0.2060  136 GLN D OE1 
7478 N  NE2 . GLN D 135 ? 0.4420 0.4689 0.3648 0.0885  0.0285  0.0719  136 GLN D NE2 
7479 N  N   . GLN D 136 ? 0.1786 0.1365 0.1347 -0.0208 -0.0141 -0.0057 137 GLN D N   
7480 C  CA  . GLN D 136 ? 0.1091 0.1574 0.1884 -0.0267 -0.0344 -0.0017 137 GLN D CA  
7481 C  C   . GLN D 136 ? 0.1525 0.1576 0.1326 -0.0289 -0.0008 -0.0057 137 GLN D C   
7482 O  O   . GLN D 136 ? 0.1570 0.1542 0.1754 -0.0304 -0.0206 -0.0157 137 GLN D O   
7483 C  CB  . GLN D 136 ? 0.1603 0.1554 0.1676 -0.0171 -0.0171 0.0231  137 GLN D CB  
7484 C  CG  . GLN D 136 ? 0.2278 0.1879 0.2797 0.0186  -0.0243 0.0066  137 GLN D CG  
7485 C  CD  . GLN D 136 ? 0.2517 0.3007 0.2314 0.0438  0.0313  0.0057  137 GLN D CD  
7486 O  OE1 . GLN D 136 ? 0.2772 0.2080 0.2608 -0.0522 -0.0096 -0.0027 137 GLN D OE1 
7487 N  NE2 . GLN D 136 ? 0.3307 0.2777 0.2917 0.0017  -0.0566 0.0052  137 GLN D NE2 
7488 N  N   . PRO D 137 ? 0.1387 0.1576 0.1120 -0.0179 0.0089  0.0114  138 PRO D N   
7489 C  CA  . PRO D 137 ? 0.1473 0.1829 0.1793 -0.0010 -0.0208 0.0008  138 PRO D CA  
7490 C  C   . PRO D 137 ? 0.1439 0.1741 0.1574 -0.0142 -0.0232 -0.0178 138 PRO D C   
7491 O  O   . PRO D 137 ? 0.1931 0.1757 0.1615 0.0100  -0.0114 -0.0362 138 PRO D O   
7492 C  CB  . PRO D 137 ? 0.1483 0.2440 0.2949 -0.0110 -0.0294 -0.0311 138 PRO D CB  
7493 C  CG  . PRO D 137 ? 0.2260 0.2328 0.2723 -0.0725 -0.0185 0.0225  138 PRO D CG  
7494 C  CD  . PRO D 137 ? 0.1606 0.2050 0.2254 -0.0573 -0.0057 0.0299  138 PRO D CD  
7495 N  N   . ASP D 138 ? 0.1215 0.1405 0.1395 -0.0170 0.0005  -0.0021 139 ASP D N   
7496 C  CA  . ASP D 138 ? 0.1448 0.1513 0.1184 0.0003  -0.0185 0.0074  139 ASP D CA  
7497 C  C   . ASP D 138 ? 0.1525 0.1173 0.1278 -0.0019 0.0006  0.0126  139 ASP D C   
7498 O  O   . ASP D 138 ? 0.1432 0.1360 0.1427 -0.0129 -0.0043 -0.0034 139 ASP D O   
7499 C  CB  . ASP D 138 ? 0.1513 0.1656 0.1782 -0.0186 -0.0093 -0.0130 139 ASP D CB  
7500 C  CG  . ASP D 138 ? 0.1694 0.1775 0.2048 -0.0193 -0.0097 -0.0151 139 ASP D CG  
7501 O  OD1 . ASP D 138 ? 0.1850 0.1498 0.2009 -0.0109 -0.0269 -0.0253 139 ASP D OD1 
7502 O  OD2 . ASP D 138 ? 0.1973 0.2353 0.2373 -0.0340 -0.0474 -0.0535 139 ASP D OD2 
7503 N  N   . GLY D 139 ? 0.1213 0.1328 0.1376 -0.0086 -0.0254 0.0043  140 GLY D N   
7504 C  CA  . GLY D 139 ? 0.1037 0.1272 0.1683 -0.0065 -0.0020 0.0207  140 GLY D CA  
7505 C  C   . GLY D 139 ? 0.1055 0.1037 0.1233 0.0017  -0.0154 -0.0001 140 GLY D C   
7506 O  O   . GLY D 139 ? 0.1321 0.1098 0.1409 -0.0032 0.0187  -0.0031 140 GLY D O   
7507 N  N   . LEU D 140 ? 0.1261 0.0966 0.1298 0.0021  -0.0003 0.0103  141 LEU D N   
7508 C  CA  . LEU D 140 ? 0.1203 0.1243 0.1057 -0.0083 -0.0200 0.0015  141 LEU D CA  
7509 C  C   . LEU D 140 ? 0.1023 0.1006 0.1283 -0.0093 -0.0070 -0.0049 141 LEU D C   
7510 O  O   . LEU D 140 ? 0.1100 0.0930 0.1233 -0.0093 -0.0068 0.0074  141 LEU D O   
7511 C  CB  . LEU D 140 ? 0.1396 0.1265 0.1093 -0.0041 0.0027  0.0043  141 LEU D CB  
7512 C  CG  . LEU D 140 ? 0.1624 0.1351 0.1517 0.0008  -0.0144 0.0034  141 LEU D CG  
7513 C  CD1 . LEU D 140 ? 0.1869 0.1574 0.1472 -0.0104 -0.0034 -0.0261 141 LEU D CD1 
7514 C  CD2 . LEU D 140 ? 0.1946 0.1666 0.1425 0.0175  -0.0329 -0.0203 141 LEU D CD2 
7515 N  N   . ALA D 141 ? 0.1130 0.1053 0.1082 -0.0105 0.0121  -0.0082 142 ALA D N   
7516 C  CA  . ALA D 141 ? 0.1102 0.1046 0.1161 -0.0126 -0.0048 0.0048  142 ALA D CA  
7517 C  C   . ALA D 141 ? 0.0917 0.1165 0.1049 0.0027  0.0103  0.0003  142 ALA D C   
7518 O  O   . ALA D 141 ? 0.1036 0.1037 0.1414 0.0021  0.0120  0.0098  142 ALA D O   
7519 C  CB  . ALA D 141 ? 0.1260 0.1154 0.1042 0.0092  -0.0013 0.0089  142 ALA D CB  
7520 N  N   . VAL D 142 ? 0.1124 0.0967 0.1003 -0.0074 -0.0032 0.0013  143 VAL D N   
7521 C  CA  . VAL D 142 ? 0.1082 0.0931 0.1138 -0.0081 -0.0020 -0.0060 143 VAL D CA  
7522 C  C   . VAL D 142 ? 0.0948 0.0895 0.1023 0.0026  -0.0074 -0.0010 143 VAL D C   
7523 O  O   . VAL D 142 ? 0.1049 0.1106 0.1168 0.0041  -0.0073 0.0120  143 VAL D O   
7524 C  CB  . VAL D 142 ? 0.1222 0.0994 0.1084 -0.0040 -0.0043 -0.0059 143 VAL D CB  
7525 C  CG1 . VAL D 142 ? 0.1371 0.1035 0.1082 -0.0143 -0.0099 -0.0157 143 VAL D CG1 
7526 C  CG2 . VAL D 142 ? 0.1233 0.1285 0.1194 -0.0125 0.0023  0.0186  143 VAL D CG2 
7527 N  N   . LEU D 143 ? 0.1193 0.0833 0.1091 0.0142  0.0143  0.0015  144 LEU D N   
7528 C  CA  . LEU D 143 ? 0.1041 0.0861 0.1197 -0.0142 0.0114  -0.0052 144 LEU D CA  
7529 C  C   . LEU D 143 ? 0.0791 0.0935 0.0847 0.0040  -0.0030 0.0119  144 LEU D C   
7530 O  O   . LEU D 143 ? 0.1044 0.1098 0.1200 0.0105  -0.0159 0.0051  144 LEU D O   
7531 C  CB  . LEU D 143 ? 0.1199 0.1018 0.1238 0.0015  0.0265  0.0052  144 LEU D CB  
7532 C  CG  . LEU D 143 ? 0.1133 0.1407 0.1077 -0.0078 0.0161  0.0065  144 LEU D CG  
7533 C  CD1 . LEU D 143 ? 0.1414 0.1520 0.1585 0.0237  0.0100  0.0171  144 LEU D CD1 
7534 C  CD2 . LEU D 143 ? 0.1522 0.1473 0.1215 0.0001  0.0606  0.0137  144 LEU D CD2 
7535 N  N   . GLY D 144 ? 0.1014 0.0839 0.1079 0.0082  0.0044  -0.0080 145 GLY D N   
7536 C  CA  . GLY D 144 ? 0.0860 0.0705 0.1024 0.0012  0.0031  0.0099  145 GLY D CA  
7537 C  C   . GLY D 144 ? 0.0945 0.0833 0.1019 0.0111  -0.0006 0.0048  145 GLY D C   
7538 O  O   . GLY D 144 ? 0.1213 0.0967 0.1121 0.0012  -0.0109 -0.0013 145 GLY D O   
7539 N  N   . ILE D 145 ? 0.0924 0.0843 0.0962 0.0007  0.0010  0.0024  146 ILE D N   
7540 C  CA  . ILE D 145 ? 0.0821 0.1003 0.0978 -0.0038 0.0031  0.0087  146 ILE D CA  
7541 C  C   . ILE D 145 ? 0.0922 0.1012 0.1055 -0.0023 -0.0121 0.0103  146 ILE D C   
7542 O  O   . ILE D 145 ? 0.1102 0.1026 0.1070 -0.0062 -0.0020 0.0107  146 ILE D O   
7543 C  CB  . ILE D 145 ? 0.0894 0.1080 0.1247 -0.0020 0.0133  0.0003  146 ILE D CB  
7544 C  CG1 . ILE D 145 ? 0.1270 0.1215 0.1648 -0.0076 0.0153  -0.0285 146 ILE D CG1 
7545 C  CG2 . ILE D 145 ? 0.1436 0.1299 0.1330 -0.0189 0.0416  0.0003  146 ILE D CG2 
7546 C  CD1 . ILE D 145 ? 0.1281 0.1438 0.1599 0.0335  0.0236  0.0263  146 ILE D CD1 
7547 N  N   . PHE D 146 ? 0.0897 0.0912 0.0983 0.0065  0.0167  -0.0046 147 PHE D N   
7548 C  CA  . PHE D 146 ? 0.0888 0.0870 0.1039 0.0019  0.0000  0.0008  147 PHE D CA  
7549 C  C   . PHE D 146 ? 0.1003 0.0936 0.1116 0.0015  0.0031  0.0038  147 PHE D C   
7550 O  O   . PHE D 146 ? 0.1301 0.1130 0.1133 0.0017  0.0065  0.0054  147 PHE D O   
7551 C  CB  . PHE D 146 ? 0.1046 0.0942 0.1161 0.0076  0.0119  0.0115  147 PHE D CB  
7552 C  CG  . PHE D 146 ? 0.0933 0.0778 0.0926 0.0115  0.0133  -0.0048 147 PHE D CG  
7553 C  CD1 . PHE D 146 ? 0.1021 0.0890 0.0974 -0.0057 0.0096  -0.0076 147 PHE D CD1 
7554 C  CD2 . PHE D 146 ? 0.0933 0.0918 0.1281 0.0065  -0.0074 0.0199  147 PHE D CD2 
7555 C  CE1 . PHE D 146 ? 0.0964 0.0904 0.1073 0.0000  -0.0006 0.0108  147 PHE D CE1 
7556 C  CE2 . PHE D 146 ? 0.0982 0.0830 0.1199 0.0077  0.0017  0.0182  147 PHE D CE2 
7557 C  CZ  . PHE D 146 ? 0.0970 0.0848 0.1112 0.0078  -0.0093 0.0111  147 PHE D CZ  
7558 N  N   . LEU D 147 ? 0.1023 0.0940 0.1077 -0.0035 -0.0007 0.0019  148 LEU D N   
7559 C  CA  . LEU D 147 ? 0.0960 0.0904 0.1360 -0.0006 0.0096  0.0006  148 LEU D CA  
7560 C  C   . LEU D 147 ? 0.1216 0.0998 0.1071 -0.0133 -0.0071 0.0051  148 LEU D C   
7561 O  O   . LEU D 147 ? 0.1172 0.1064 0.1313 0.0015  0.0100  0.0071  148 LEU D O   
7562 C  CB  . LEU D 147 ? 0.1305 0.1208 0.1254 0.0015  0.0046  -0.0020 148 LEU D CB  
7563 C  CG  . LEU D 147 ? 0.1585 0.0931 0.1488 -0.0057 -0.0118 0.0208  148 LEU D CG  
7564 C  CD1 . LEU D 147 ? 0.1328 0.0909 0.1847 -0.0120 0.0170  0.0168  148 LEU D CD1 
7565 C  CD2 . LEU D 147 ? 0.1423 0.1172 0.1568 0.0098  -0.0204 0.0110  148 LEU D CD2 
7566 N  N   . LYS D 148 ? 0.1286 0.0951 0.1319 -0.0131 0.0063  0.0065  149 LYS D N   
7567 C  CA  . LYS D 148 ? 0.1387 0.0888 0.1599 0.0086  0.0116  -0.0013 149 LYS D CA  
7568 C  C   . LYS D 148 ? 0.1581 0.1263 0.1395 -0.0030 0.0165  -0.0208 149 LYS D C   
7569 O  O   . LYS D 148 ? 0.1230 0.1391 0.1919 -0.0138 0.0126  -0.0077 149 LYS D O   
7570 C  CB  . LYS D 148 ? 0.1347 0.1428 0.1779 0.0057  -0.0087 0.0165  149 LYS D CB  
7571 C  CG  . LYS D 148 ? 0.1732 0.1685 0.1727 0.0153  -0.0076 0.0219  149 LYS D CG  
7572 C  CD  . LYS D 148 ? 0.2671 0.2574 0.2378 0.0230  -0.0346 0.0542  149 LYS D CD  
7573 C  CE  . LYS D 148 ? 0.2474 0.3668 0.3149 0.0684  0.0118  0.0450  149 LYS D CE  
7574 N  NZ  . LYS D 148 ? 0.4804 0.6194 0.4828 -0.0060 -0.0942 0.2639  149 LYS D NZ  
7575 N  N   . VAL D 149 ? 0.1407 0.1055 0.1689 -0.0091 -0.0076 0.0012  150 VAL D N   
7576 C  CA  . VAL D 149 ? 0.1306 0.1543 0.1813 -0.0073 -0.0076 0.0205  150 VAL D CA  
7577 C  C   . VAL D 149 ? 0.1789 0.1367 0.1923 -0.0104 0.0003  0.0082  150 VAL D C   
7578 O  O   . VAL D 149 ? 0.1590 0.1525 0.1974 0.0170  0.0088  0.0211  150 VAL D O   
7579 C  CB  . VAL D 149 ? 0.1705 0.1541 0.2019 -0.0264 0.0274  0.0252  150 VAL D CB  
7580 C  CG1 . VAL D 149 ? 0.1707 0.1793 0.2251 -0.0324 0.0159  -0.0127 150 VAL D CG1 
7581 C  CG2 . VAL D 149 ? 0.2032 0.2043 0.1738 -0.0333 0.0231  0.0299  150 VAL D CG2 
7582 N  N   . GLY D 150 ? 0.1571 0.1374 0.1957 -0.0222 0.0239  0.0184  151 GLY D N   
7583 C  CA  . GLY D 150 ? 0.1888 0.1588 0.2093 0.0258  0.0410  0.0331  151 GLY D CA  
7584 C  C   . GLY D 150 ? 0.1768 0.1405 0.1775 -0.0066 0.0057  0.0485  151 GLY D C   
7585 O  O   . GLY D 150 ? 0.1874 0.1509 0.2021 -0.0252 0.0082  0.0478  151 GLY D O   
7586 N  N   A SER D 151 ? 0.1628 0.1556 0.1962 -0.0024 0.0460  0.0187  152 SER D N   
7587 N  N   B SER D 151 ? 0.1660 0.1572 0.1960 -0.0063 0.0445  0.0189  152 SER D N   
7588 C  CA  A SER D 151 ? 0.1491 0.1861 0.2104 0.0156  0.0428  0.0174  152 SER D CA  
7589 C  CA  B SER D 151 ? 0.1515 0.1911 0.2132 0.0121  0.0416  0.0190  152 SER D CA  
7590 C  C   A SER D 151 ? 0.1624 0.1639 0.1932 -0.0487 0.0110  0.0109  152 SER D C   
7591 C  C   B SER D 151 ? 0.1676 0.1802 0.2020 -0.0469 0.0027  0.0178  152 SER D C   
7592 O  O   A SER D 151 ? 0.1639 0.1784 0.1732 -0.0524 0.0452  -0.0046 152 SER D O   
7593 O  O   B SER D 151 ? 0.1374 0.1942 0.1836 -0.0438 -0.0024 0.0229  152 SER D O   
7594 C  CB  A SER D 151 ? 0.2420 0.2099 0.2215 0.0012  -0.0135 0.0272  152 SER D CB  
7595 C  CB  B SER D 151 ? 0.2384 0.2181 0.2007 -0.0007 -0.0216 0.0636  152 SER D CB  
7596 O  OG  A SER D 151 ? 0.2370 0.3269 0.1887 -0.0559 0.0304  -0.0296 152 SER D OG  
7597 O  OG  B SER D 151 ? 0.3021 0.2978 0.1860 0.0403  -0.0093 0.1234  152 SER D OG  
7598 N  N   . ALA D 152 ? 0.1698 0.1472 0.1928 -0.0063 0.0131  0.0037  153 ALA D N   
7599 C  CA  . ALA D 152 ? 0.1509 0.1694 0.2005 0.0037  0.0186  0.0015  153 ALA D CA  
7600 C  C   . ALA D 152 ? 0.1680 0.1800 0.1865 -0.0210 0.0161  -0.0081 153 ALA D C   
7601 O  O   . ALA D 152 ? 0.2115 0.1590 0.2071 -0.0176 0.0052  0.0167  153 ALA D O   
7602 C  CB  . ALA D 152 ? 0.1495 0.1869 0.2339 -0.0013 -0.0232 0.0019  153 ALA D CB  
7603 N  N   . LYS D 153 ? 0.1454 0.1411 0.1903 0.0204  0.0060  -0.0110 154 LYS D N   
7604 C  CA  . LYS D 153 ? 0.1642 0.1493 0.2152 0.0083  0.0302  -0.0183 154 LYS D CA  
7605 C  C   . LYS D 153 ? 0.1535 0.1346 0.1396 -0.0076 0.0125  -0.0206 154 LYS D C   
7606 O  O   . LYS D 153 ? 0.1364 0.1651 0.1720 -0.0109 0.0162  0.0200  154 LYS D O   
7607 C  CB  . LYS D 153 ? 0.1310 0.1448 0.2314 0.0015  0.0397  -0.0103 154 LYS D CB  
7608 C  CG  . LYS D 153 ? 0.1330 0.1746 0.2145 0.0148  0.0088  -0.0012 154 LYS D CG  
7609 C  CD  . LYS D 153 ? 0.1450 0.1825 0.2266 -0.0239 0.0170  -0.0149 154 LYS D CD  
7610 C  CE  . LYS D 153 ? 0.1626 0.1911 0.2335 -0.0110 -0.0377 -0.0013 154 LYS D CE  
7611 N  NZ  . LYS D 153 ? 0.2032 0.1808 0.2115 -0.0300 -0.0003 0.0070  154 LYS D NZ  
7612 N  N   . PRO D 154 ? 0.1716 0.1660 0.1416 -0.0136 0.0156  0.0021  155 PRO D N   
7613 C  CA  . PRO D 154 ? 0.1580 0.2142 0.1474 -0.0027 0.0281  0.0384  155 PRO D CA  
7614 C  C   . PRO D 154 ? 0.1662 0.1987 0.1651 -0.0157 0.0082  -0.0122 155 PRO D C   
7615 O  O   . PRO D 154 ? 0.1592 0.2388 0.2143 -0.0063 0.0364  0.0087  155 PRO D O   
7616 C  CB  . PRO D 154 ? 0.2109 0.2439 0.1430 0.0027  0.0273  0.0120  155 PRO D CB  
7617 C  CG  . PRO D 154 ? 0.2084 0.3030 0.2989 0.0261  0.0401  0.0657  155 PRO D CG  
7618 C  CD  . PRO D 154 ? 0.1940 0.1964 0.1301 -0.0132 0.0007  -0.0063 155 PRO D CD  
7619 N  N   . GLY D 155 ? 0.1637 0.1518 0.1698 -0.0179 0.0288  -0.0203 156 GLY D N   
7620 C  CA  . GLY D 155 ? 0.1615 0.1623 0.2169 0.0103  -0.0160 0.0003  156 GLY D CA  
7621 C  C   . GLY D 155 ? 0.1676 0.1917 0.2215 0.0051  0.0277  0.0028  156 GLY D C   
7622 O  O   . GLY D 155 ? 0.2414 0.1989 0.2397 0.0208  0.0241  0.0081  156 GLY D O   
7623 N  N   . LEU D 156 ? 0.1362 0.1626 0.1805 0.0295  0.0233  0.0087  157 LEU D N   
7624 C  CA  . LEU D 156 ? 0.1673 0.1483 0.1924 0.0310  -0.0174 0.0023  157 LEU D CA  
7625 C  C   . LEU D 156 ? 0.1287 0.1177 0.1533 -0.0041 0.0087  0.0083  157 LEU D C   
7626 O  O   . LEU D 156 ? 0.1383 0.1574 0.1617 -0.0006 0.0027  0.0091  157 LEU D O   
7627 C  CB  . LEU D 156 ? 0.1407 0.1850 0.1933 0.0265  0.0186  0.0195  157 LEU D CB  
7628 C  CG  . LEU D 156 ? 0.1472 0.1684 0.1893 0.0027  0.0373  0.0137  157 LEU D CG  
7629 C  CD1 . LEU D 156 ? 0.1739 0.1732 0.2402 -0.0186 0.0340  0.0073  157 LEU D CD1 
7630 C  CD2 . LEU D 156 ? 0.1620 0.1685 0.1881 0.0082  0.0421  -0.0085 157 LEU D CD2 
7631 N  N   . GLN D 157 ? 0.1396 0.1623 0.2106 0.0028  -0.0008 0.0394  158 GLN D N   
7632 C  CA  . GLN D 157 ? 0.1509 0.2104 0.1668 -0.0498 0.0000  0.0148  158 GLN D CA  
7633 C  C   . GLN D 157 ? 0.1675 0.1578 0.1807 -0.0241 0.0147  -0.0089 158 GLN D C   
7634 O  O   . GLN D 157 ? 0.1473 0.1784 0.2026 -0.0068 0.0306  0.0005  158 GLN D O   
7635 C  CB  . GLN D 157 ? 0.1996 0.1827 0.1805 -0.0333 0.0417  0.0171  158 GLN D CB  
7636 C  CG  . GLN D 157 ? 0.2357 0.2181 0.1815 -0.0560 0.0204  -0.0013 158 GLN D CG  
7637 C  CD  . GLN D 157 ? 0.1698 0.1831 0.2649 -0.0126 -0.0263 -0.0176 158 GLN D CD  
7638 O  OE1 . GLN D 157 ? 0.1662 0.1342 0.2678 -0.0140 -0.0066 -0.0076 158 GLN D OE1 
7639 N  NE2 . GLN D 157 ? 0.1869 0.1890 0.2451 -0.0734 0.0091  0.0305  158 GLN D NE2 
7640 N  N   . LYS D 158 ? 0.1176 0.1962 0.2166 0.0038  0.0326  -0.0251 159 LYS D N   
7641 C  CA  . LYS D 158 ? 0.1499 0.1989 0.2151 0.0140  0.0131  -0.0046 159 LYS D CA  
7642 C  C   . LYS D 158 ? 0.1457 0.1910 0.2029 0.0320  -0.0245 0.0286  159 LYS D C   
7643 O  O   . LYS D 158 ? 0.1692 0.2077 0.1983 0.0082  0.0125  0.0322  159 LYS D O   
7644 C  CB  . LYS D 158 ? 0.2039 0.1971 0.2813 0.0516  0.0118  0.0054  159 LYS D CB  
7645 C  CG  . LYS D 158 ? 0.3280 0.3064 0.3310 -0.0217 0.0771  0.0266  159 LYS D CG  
7646 C  CD  . LYS D 158 ? 0.5188 0.5152 0.5009 0.0842  0.0659  -0.1370 159 LYS D CD  
7647 C  CE  . LYS D 158 ? 0.3907 0.6190 0.6736 0.3163  0.2741  -0.1067 159 LYS D CE  
7648 N  NZ  . LYS D 158 ? 0.3907 0.6190 0.5669 0.0863  0.0320  0.0250  159 LYS D NZ  
7649 N  N   . VAL D 159 ? 0.1335 0.1421 0.1789 0.0076  0.0119  -0.0006 160 VAL D N   
7650 C  CA  . VAL D 159 ? 0.1097 0.1966 0.1746 -0.0205 0.0012  -0.0173 160 VAL D CA  
7651 C  C   . VAL D 159 ? 0.1220 0.1404 0.1542 -0.0028 0.0142  0.0017  160 VAL D C   
7652 O  O   . VAL D 159 ? 0.1755 0.1462 0.1885 -0.0062 -0.0003 0.0245  160 VAL D O   
7653 C  CB  . VAL D 159 ? 0.1098 0.1583 0.1858 -0.0098 -0.0111 0.0015  160 VAL D CB  
7654 C  CG1 . VAL D 159 ? 0.1835 0.2136 0.1565 -0.0197 0.0291  0.0690  160 VAL D CG1 
7655 C  CG2 . VAL D 159 ? 0.1592 0.1903 0.2696 -0.0178 -0.0372 -0.0553 160 VAL D CG2 
7656 N  N   . VAL D 160 ? 0.1340 0.1386 0.1755 -0.0077 0.0127  0.0197  161 VAL D N   
7657 C  CA  . VAL D 160 ? 0.1852 0.1825 0.2357 0.0091  -0.0193 0.0197  161 VAL D CA  
7658 C  C   . VAL D 160 ? 0.1723 0.1468 0.1721 -0.0264 0.0078  0.0149  161 VAL D C   
7659 O  O   . VAL D 160 ? 0.2012 0.1994 0.2064 -0.0273 -0.0024 0.0215  161 VAL D O   
7660 C  CB  . VAL D 160 ? 0.2204 0.1572 0.2463 -0.0166 -0.0309 0.0074  161 VAL D CB  
7661 C  CG1 . VAL D 160 ? 0.2134 0.1766 0.2707 -0.0480 -0.0054 0.0132  161 VAL D CG1 
7662 C  CG2 . VAL D 160 ? 0.2506 0.1595 0.3147 -0.0100 -0.0287 0.0037  161 VAL D CG2 
7663 N  N   . ASP D 161 ? 0.1549 0.1926 0.2373 -0.0401 -0.0082 0.0233  162 ASP D N   
7664 C  CA  . ASP D 161 ? 0.1360 0.2345 0.2463 -0.0417 -0.0071 0.0331  162 ASP D CA  
7665 C  C   . ASP D 161 ? 0.1754 0.2267 0.2689 -0.0201 -0.0273 0.0399  162 ASP D C   
7666 O  O   . ASP D 161 ? 0.1914 0.3041 0.2901 -0.0458 -0.0175 0.0646  162 ASP D O   
7667 C  CB  . ASP D 161 ? 0.2499 0.3100 0.2653 -0.0182 0.0097  0.0472  162 ASP D CB  
7668 C  CG  . ASP D 161 ? 0.1840 0.2820 0.3477 -0.0209 -0.0070 0.0122  162 ASP D CG  
7669 O  OD1 . ASP D 161 ? 0.2921 0.2831 0.3616 -0.0584 0.0012  0.0252  162 ASP D OD1 
7670 O  OD2 . ASP D 161 ? 0.2206 0.4636 0.4221 -0.0559 0.0066  -0.0133 162 ASP D OD2 
7671 N  N   . VAL D 162 ? 0.1321 0.2116 0.1962 0.0159  0.0008  0.0353  163 VAL D N   
7672 C  CA  . VAL D 162 ? 0.1504 0.2069 0.2213 -0.0085 0.0052  0.0229  163 VAL D CA  
7673 C  C   . VAL D 162 ? 0.1516 0.1985 0.1962 -0.0041 0.0076  0.0351  163 VAL D C   
7674 O  O   . VAL D 162 ? 0.1712 0.1941 0.2276 -0.0043 -0.0566 0.0384  163 VAL D O   
7675 C  CB  . VAL D 162 ? 0.2213 0.1755 0.3255 0.0313  -0.0027 0.0115  163 VAL D CB  
7676 C  CG1 . VAL D 162 ? 0.2188 0.1647 0.2474 0.0309  0.0219  0.0206  163 VAL D CG1 
7677 C  CG2 . VAL D 162 ? 0.2606 0.2630 0.3639 0.0520  -0.0754 0.0351  163 VAL D CG2 
7678 N  N   . LEU D 163 ? 0.1491 0.1730 0.1906 0.0008  -0.0060 0.0197  164 LEU D N   
7679 C  CA  . LEU D 163 ? 0.1883 0.1994 0.1908 0.0331  -0.0375 0.0109  164 LEU D CA  
7680 C  C   . LEU D 163 ? 0.1447 0.2035 0.1996 0.0051  -0.0260 0.0221  164 LEU D C   
7681 O  O   . LEU D 163 ? 0.1818 0.1948 0.2084 0.0153  -0.0390 0.0253  164 LEU D O   
7682 C  CB  . LEU D 163 ? 0.1766 0.1463 0.1863 0.0148  0.0071  0.0035  164 LEU D CB  
7683 C  CG  . LEU D 163 ? 0.1516 0.1434 0.2066 0.0198  -0.0052 0.0307  164 LEU D CG  
7684 C  CD1 . LEU D 163 ? 0.1737 0.1628 0.2172 0.0483  0.0161  -0.0021 164 LEU D CD1 
7685 C  CD2 . LEU D 163 ? 0.1425 0.1626 0.1613 -0.0040 -0.0251 0.0241  164 LEU D CD2 
7686 N  N   . ASP D 164 ? 0.1748 0.2272 0.2870 -0.0015 -0.0482 0.0432  165 ASP D N   
7687 C  CA  . ASP D 164 ? 0.2312 0.2109 0.3282 -0.0571 -0.0675 0.0472  165 ASP D CA  
7688 C  C   . ASP D 164 ? 0.1849 0.2379 0.2709 0.0046  -0.0610 0.0003  165 ASP D C   
7689 O  O   . ASP D 164 ? 0.3190 0.3278 0.2924 -0.0105 -0.1352 -0.0231 165 ASP D O   
7690 C  CB  . ASP D 164 ? 0.3109 0.2885 0.3964 -0.1395 -0.0606 0.0373  165 ASP D CB  
7691 C  CG  . ASP D 164 ? 0.3438 0.3998 0.4721 -0.1588 0.0251  0.0412  165 ASP D CG  
7692 O  OD1 . ASP D 164 ? 0.5146 0.6477 0.4840 -0.1145 -0.0524 0.1084  165 ASP D OD1 
7693 O  OD2 . ASP D 164 ? 0.6987 1.3781 0.9406 -0.2567 0.0724  0.2084  165 ASP D OD2 
7694 N  N   . SER D 165 ? 0.1531 0.2197 0.2587 0.0007  -0.0197 0.0452  166 SER D N   
7695 C  CA  . SER D 165 ? 0.2194 0.1929 0.2565 0.0299  -0.0322 0.0272  166 SER D CA  
7696 C  C   . SER D 165 ? 0.1791 0.2095 0.2843 0.0284  -0.0368 0.0326  166 SER D C   
7697 O  O   . SER D 165 ? 0.1754 0.2098 0.2623 0.0270  -0.0438 0.0209  166 SER D O   
7698 C  CB  . SER D 165 ? 0.2696 0.2734 0.1933 0.0253  -0.0104 0.0208  166 SER D CB  
7699 O  OG  . SER D 165 ? 0.2185 0.2445 0.2906 0.0383  -0.0262 0.0115  166 SER D OG  
7700 N  N   . ILE D 166 ? 0.1556 0.1887 0.1926 0.0137  -0.0052 0.0234  167 ILE D N   
7701 C  CA  . ILE D 166 ? 0.1660 0.1827 0.2048 -0.0126 -0.0068 0.0133  167 ILE D CA  
7702 C  C   . ILE D 166 ? 0.1832 0.1854 0.2057 -0.0070 -0.0308 0.0049  167 ILE D C   
7703 O  O   . ILE D 166 ? 0.1829 0.1662 0.1982 -0.0122 -0.0355 0.0295  167 ILE D O   
7704 C  CB  . ILE D 166 ? 0.1827 0.1678 0.1872 0.0244  -0.0351 0.0041  167 ILE D CB  
7705 C  CG1 . ILE D 166 ? 0.1527 0.1739 0.1603 -0.0060 -0.0390 0.0083  167 ILE D CG1 
7706 C  CG2 . ILE D 166 ? 0.2109 0.1921 0.2430 0.0286  -0.0043 -0.0505 167 ILE D CG2 
7707 C  CD1 . ILE D 166 ? 0.1771 0.1759 0.1796 -0.0573 -0.0273 0.0154  167 ILE D CD1 
7708 N  N   . LYS D 167 ? 0.1797 0.1703 0.2253 0.0008  -0.0410 0.0102  168 LYS D N   
7709 C  CA  . LYS D 167 ? 0.1759 0.1860 0.1815 -0.0060 -0.0390 0.0280  168 LYS D CA  
7710 C  C   . LYS D 167 ? 0.1741 0.1659 0.2330 -0.0141 -0.0020 0.0008  168 LYS D C   
7711 O  O   . LYS D 167 ? 0.1773 0.1904 0.1881 -0.0076 -0.0340 0.0114  168 LYS D O   
7712 C  CB  . LYS D 167 ? 0.1908 0.2287 0.2463 -0.0430 -0.0384 -0.0187 168 LYS D CB  
7713 C  CG  . LYS D 167 ? 0.1985 0.2312 0.2948 -0.0471 -0.0568 0.0119  168 LYS D CG  
7714 C  CD  . LYS D 167 ? 0.2495 0.3197 0.4498 -0.1321 -0.0445 -0.0635 168 LYS D CD  
7715 C  CE  . LYS D 167 ? 0.4011 0.4613 0.5904 -0.1534 0.0803  -0.1816 168 LYS D CE  
7716 N  NZ  . LYS D 167 ? 0.4373 0.4801 0.4893 -0.1976 -0.0339 -0.0070 168 LYS D NZ  
7717 N  N   . THR D 168 ? 0.1981 0.1820 0.1770 0.0115  -0.0239 0.0126  169 THR D N   
7718 C  CA  . THR D 168 ? 0.1659 0.1859 0.1877 -0.0153 -0.0335 0.0353  169 THR D CA  
7719 C  C   . THR D 168 ? 0.1955 0.1826 0.1562 0.0214  -0.0161 0.0474  169 THR D C   
7720 O  O   . THR D 168 ? 0.2032 0.1723 0.1874 0.0166  -0.0458 0.0109  169 THR D O   
7721 C  CB  . THR D 168 ? 0.2263 0.2037 0.2193 0.0102  -0.0703 0.0427  169 THR D CB  
7722 O  OG1 . THR D 168 ? 0.2389 0.2373 0.2479 0.0229  -0.0222 0.0174  169 THR D OG1 
7723 C  CG2 . THR D 168 ? 0.2016 0.2179 0.2500 0.0151  -0.0269 -0.0144 169 THR D CG2 
7724 N  N   A LYS D 169 ? 0.1721 0.2104 0.2034 -0.0351 -0.0421 0.0211  170 LYS D N   
7725 N  N   B LYS D 169 ? 0.1712 0.2120 0.2059 -0.0335 -0.0399 0.0249  170 LYS D N   
7726 C  CA  A LYS D 169 ? 0.1772 0.1657 0.1556 -0.0024 -0.0208 0.0098  170 LYS D CA  
7727 C  CA  B LYS D 169 ? 0.1772 0.1694 0.1571 -0.0040 -0.0234 0.0091  170 LYS D CA  
7728 C  C   A LYS D 169 ? 0.1964 0.2077 0.1906 0.0329  0.0038  0.0097  170 LYS D C   
7729 C  C   B LYS D 169 ? 0.2082 0.2075 0.1951 0.0283  -0.0041 0.0114  170 LYS D C   
7730 O  O   A LYS D 169 ? 0.2445 0.2727 0.1793 0.0751  -0.0228 0.0329  170 LYS D O   
7731 O  O   B LYS D 169 ? 0.2540 0.2791 0.1856 0.0820  -0.0296 0.0456  170 LYS D O   
7732 C  CB  A LYS D 169 ? 0.1937 0.2003 0.1578 0.0063  -0.0060 -0.0130 170 LYS D CB  
7733 C  CB  B LYS D 169 ? 0.2041 0.2030 0.1622 0.0059  -0.0023 -0.0237 170 LYS D CB  
7734 C  CG  A LYS D 169 ? 0.2035 0.2109 0.1711 -0.0126 0.0038  -0.0093 170 LYS D CG  
7735 C  CG  B LYS D 169 ? 0.2001 0.2217 0.1865 -0.0143 0.0000  -0.0194 170 LYS D CG  
7736 C  CD  A LYS D 169 ? 0.2109 0.2088 0.2129 -0.0136 0.0419  0.0662  170 LYS D CD  
7737 C  CD  B LYS D 169 ? 0.1944 0.2412 0.2084 -0.0124 0.0175  0.0412  170 LYS D CD  
7738 C  CE  A LYS D 169 ? 0.3201 0.2145 0.3298 -0.0537 -0.0346 0.1312  170 LYS D CE  
7739 C  CE  B LYS D 169 ? 0.2800 0.3510 0.2732 -0.0049 -0.0956 -0.0706 170 LYS D CE  
7740 N  NZ  A LYS D 169 ? 0.5015 0.3307 0.2852 0.0551  0.0425  0.0445  170 LYS D NZ  
7741 N  NZ  B LYS D 169 ? 0.3822 0.3330 0.4431 0.0333  0.0273  0.0408  170 LYS D NZ  
7742 N  N   . GLY D 170 ? 0.2002 0.1820 0.1486 0.0324  -0.0138 0.0348  171 GLY D N   
7743 C  CA  . GLY D 170 ? 0.2804 0.1629 0.2345 0.0350  0.0302  0.0557  171 GLY D CA  
7744 C  C   . GLY D 170 ? 0.2813 0.2057 0.1635 0.0026  0.0151  0.0397  171 GLY D C   
7745 O  O   . GLY D 170 ? 0.2606 0.2141 0.3362 0.0322  -0.0262 0.0834  171 GLY D O   
7746 N  N   . LYS D 171 ? 0.1721 0.2027 0.2231 0.0010  -0.0049 0.0522  172 LYS D N   
7747 C  CA  . LYS D 171 ? 0.1930 0.1538 0.1174 0.0348  -0.0129 0.0403  172 LYS D CA  
7748 C  C   . LYS D 171 ? 0.2062 0.1653 0.1365 0.0430  -0.0386 0.0219  172 LYS D C   
7749 O  O   . LYS D 171 ? 0.1798 0.1800 0.1933 0.0306  -0.0524 0.0254  172 LYS D O   
7750 C  CB  . LYS D 171 ? 0.1917 0.1526 0.1529 0.0156  -0.0074 0.0154  172 LYS D CB  
7751 C  CG  . LYS D 171 ? 0.2651 0.2272 0.2203 -0.0237 -0.0559 -0.0361 172 LYS D CG  
7752 C  CD  . LYS D 171 ? 0.3158 0.2847 0.2337 -0.0516 -0.0043 0.0133  172 LYS D CD  
7753 C  CE  . LYS D 171 ? 0.3596 0.5249 0.6784 -0.0648 0.0974  -0.0098 172 LYS D CE  
7754 N  NZ  . LYS D 171 ? 0.4004 0.3801 0.8338 -0.0122 -0.2763 0.2863  172 LYS D NZ  
7755 N  N   . SER D 172 ? 0.1726 0.1673 0.2186 0.0115  -0.0054 0.0019  173 SER D N   
7756 C  CA  . SER D 172 ? 0.1563 0.1782 0.1932 0.0096  -0.0100 0.0269  173 SER D CA  
7757 C  C   . SER D 172 ? 0.1653 0.1808 0.2211 0.0244  -0.0188 0.0443  173 SER D C   
7758 O  O   . SER D 172 ? 0.1651 0.2398 0.2069 0.0335  -0.0551 0.0126  173 SER D O   
7759 C  CB  . SER D 172 ? 0.1558 0.1587 0.1872 0.0244  0.0027  0.0200  173 SER D CB  
7760 O  OG  . SER D 172 ? 0.2799 0.1915 0.2188 0.0737  -0.0542 0.0263  173 SER D OG  
7761 N  N   . ALA D 173 ? 0.1453 0.1730 0.1890 0.0399  -0.0008 0.0152  174 ALA D N   
7762 C  CA  . ALA D 173 ? 0.1838 0.2278 0.1741 -0.0021 0.0129  -0.0390 174 ALA D CA  
7763 C  C   . ALA D 173 ? 0.1653 0.2391 0.1542 0.0502  -0.0339 -0.0258 174 ALA D C   
7764 O  O   . ALA D 173 ? 0.1601 0.2088 0.1802 0.0276  -0.0286 -0.0116 174 ALA D O   
7765 C  CB  . ALA D 173 ? 0.2494 0.2484 0.2017 -0.0006 0.0181  -0.0076 174 ALA D CB  
7766 N  N   A ASP D 174 ? 0.1865 0.3088 0.2696 0.0671  -0.0038 -0.0913 175 ASP D N   
7767 N  N   B ASP D 174 ? 0.1964 0.1439 0.1608 0.0234  0.0168  -0.0065 175 ASP D N   
7768 C  CA  A ASP D 174 ? 0.1770 0.2660 0.1844 0.0816  -0.0181 -0.0003 175 ASP D CA  
7769 C  CA  B ASP D 174 ? 0.1621 0.2442 0.1452 0.0658  -0.0104 0.0041  175 ASP D CA  
7770 C  C   A ASP D 174 ? 0.1780 0.2454 0.1861 0.0230  -0.0038 0.0005  175 ASP D C   
7771 C  C   B ASP D 174 ? 0.1802 0.1784 0.1606 0.0119  0.0357  -0.0043 175 ASP D C   
7772 O  O   A ASP D 174 ? 0.2070 0.2544 0.3177 0.0154  -0.0626 -0.0247 175 ASP D O   
7773 O  O   B ASP D 174 ? 0.1412 0.1966 0.1553 -0.0136 0.0430  -0.0140 175 ASP D O   
7774 C  CB  A ASP D 174 ? 0.1592 0.3371 0.3222 0.0747  0.0198  -0.0236 175 ASP D CB  
7775 C  CB  B ASP D 174 ? 0.1935 0.2118 0.1974 0.0406  -0.0276 -0.0577 175 ASP D CB  
7776 C  CG  A ASP D 174 ? 0.2337 0.2617 0.3300 0.1310  0.0615  -0.0500 175 ASP D CG  
7777 C  CG  B ASP D 174 ? 0.1813 0.3179 0.2260 0.0549  -0.0524 0.0764  175 ASP D CG  
7778 O  OD1 A ASP D 174 ? 0.4264 0.3361 0.6633 0.0593  -0.0582 -0.0147 175 ASP D OD1 
7779 O  OD1 B ASP D 174 ? 0.2319 0.2987 0.2299 0.0538  0.0057  0.0209  175 ASP D OD1 
7780 O  OD2 A ASP D 174 ? 0.3571 0.3470 0.3889 0.0245  -0.0252 -0.0439 175 ASP D OD2 
7781 O  OD2 B ASP D 174 ? 0.2427 0.4746 0.2897 -0.0127 -0.1178 0.0337  175 ASP D OD2 
7782 N  N   . PHE D 175 ? 0.1779 0.1980 0.2077 0.0205  -0.0241 -0.0028 176 PHE D N   
7783 C  CA  . PHE D 175 ? 0.1312 0.1962 0.2163 0.0071  0.0223  0.0020  176 PHE D CA  
7784 C  C   . PHE D 175 ? 0.1693 0.2118 0.1675 0.0078  -0.0116 0.0035  176 PHE D C   
7785 O  O   . PHE D 175 ? 0.1718 0.2108 0.2138 0.0351  0.0261  -0.0221 176 PHE D O   
7786 C  CB  . PHE D 175 ? 0.1869 0.1745 0.2260 0.0379  0.0206  -0.0161 176 PHE D CB  
7787 C  CG  . PHE D 175 ? 0.1700 0.1854 0.1804 0.0008  -0.0248 -0.0057 176 PHE D CG  
7788 C  CD1 . PHE D 175 ? 0.2222 0.1423 0.2903 0.0087  -0.0639 0.0098  176 PHE D CD1 
7789 C  CD2 . PHE D 175 ? 0.1621 0.2131 0.1802 0.0340  -0.0171 -0.0148 176 PHE D CD2 
7790 C  CE1 . PHE D 175 ? 0.1903 0.1838 0.2224 0.0419  -0.0219 0.0114  176 PHE D CE1 
7791 C  CE2 . PHE D 175 ? 0.2069 0.1581 0.1844 0.0007  0.0207  -0.0256 176 PHE D CE2 
7792 C  CZ  . PHE D 175 ? 0.1902 0.1655 0.2434 0.0254  -0.0148 -0.0445 176 PHE D CZ  
7793 N  N   . THR D 176 ? 0.1640 0.1990 0.2055 0.0068  -0.0125 -0.0226 177 THR D N   
7794 C  CA  . THR D 176 ? 0.1702 0.2039 0.1842 0.0533  -0.0028 -0.0051 177 THR D CA  
7795 C  C   . THR D 176 ? 0.0687 0.1689 0.2102 0.0100  0.0146  0.0111  177 THR D C   
7796 O  O   . THR D 176 ? 0.1475 0.1508 0.2117 0.0377  0.0038  -0.0023 177 THR D O   
7797 C  CB  . THR D 176 ? 0.1703 0.2054 0.2257 0.0346  0.0046  0.0304  177 THR D CB  
7798 O  OG1 . THR D 176 ? 0.1817 0.2312 0.2522 0.0372  -0.0089 -0.0146 177 THR D OG1 
7799 C  CG2 . THR D 176 ? 0.2813 0.2154 0.2186 0.0742  0.0298  0.0463  177 THR D CG2 
7800 N  N   . ASN D 177 ? 0.1353 0.1520 0.1453 0.0333  0.0183  0.0104  178 ASN D N   
7801 C  CA  . ASN D 177 ? 0.1462 0.1766 0.1495 0.0188  0.0423  0.0197  178 ASN D CA  
7802 C  C   . ASN D 177 ? 0.2236 0.1753 0.1811 0.0403  0.0351  0.0093  178 ASN D C   
7803 O  O   . ASN D 177 ? 0.1908 0.2111 0.2614 0.0886  0.0606  0.0707  178 ASN D O   
7804 C  CB  . ASN D 177 ? 0.1689 0.1648 0.1953 0.0310  0.0542  0.0111  178 ASN D CB  
7805 C  CG  . ASN D 177 ? 0.1739 0.1816 0.2002 0.0370  0.0167  -0.0038 178 ASN D CG  
7806 O  OD1 . ASN D 177 ? 0.2456 0.2084 0.2398 0.0311  0.0041  -0.0355 178 ASN D OD1 
7807 N  ND2 . ASN D 177 ? 0.1665 0.1640 0.2111 0.0275  0.0068  0.0170  178 ASN D ND2 
7808 N  N   . PHE D 178 ? 0.1261 0.1466 0.1975 0.0324  0.0000  0.0170  179 PHE D N   
7809 C  CA  . PHE D 178 ? 0.1477 0.1387 0.1614 0.0229  -0.0091 0.0226  179 PHE D CA  
7810 C  C   . PHE D 178 ? 0.1518 0.1438 0.1665 0.0187  0.0065  -0.0059 179 PHE D C   
7811 O  O   . PHE D 178 ? 0.1393 0.1534 0.2048 0.0166  -0.0059 0.0096  179 PHE D O   
7812 C  CB  . PHE D 178 ? 0.1867 0.1617 0.1919 0.0595  -0.0105 0.0098  179 PHE D CB  
7813 C  CG  . PHE D 178 ? 0.1517 0.1489 0.1903 0.0469  -0.0048 0.0272  179 PHE D CG  
7814 C  CD1 . PHE D 178 ? 0.1727 0.1572 0.3025 0.0194  -0.0225 -0.0331 179 PHE D CD1 
7815 C  CD2 . PHE D 178 ? 0.1488 0.1709 0.1732 0.0375  -0.0094 0.0034  179 PHE D CD2 
7816 C  CE1 . PHE D 178 ? 0.1757 0.1750 0.1897 0.0255  -0.0179 0.0027  179 PHE D CE1 
7817 C  CE2 . PHE D 178 ? 0.1764 0.1536 0.1342 0.0308  0.0222  -0.0055 179 PHE D CE2 
7818 C  CZ  . PHE D 178 ? 0.1526 0.1680 0.1574 0.0044  0.0210  0.0189  179 PHE D CZ  
7819 N  N   . ASP D 179 ? 0.1547 0.1813 0.1502 0.0133  0.0244  0.0287  180 ASP D N   
7820 C  CA  . ASP D 179 ? 0.1547 0.1568 0.1865 0.0428  -0.0032 0.0183  180 ASP D CA  
7821 C  C   . ASP D 179 ? 0.1292 0.1563 0.1872 0.0176  0.0034  0.0010  180 ASP D C   
7822 O  O   . ASP D 179 ? 0.1601 0.1558 0.1637 0.0196  -0.0023 0.0185  180 ASP D O   
7823 C  CB  . ASP D 179 ? 0.1676 0.1651 0.1920 0.0430  0.0041  -0.0173 180 ASP D CB  
7824 C  CG  . ASP D 179 ? 0.2030 0.2495 0.1817 0.0060  0.0149  -0.0142 180 ASP D CG  
7825 O  OD1 . ASP D 179 ? 0.1899 0.1777 0.1890 0.0182  0.0110  -0.0041 180 ASP D OD1 
7826 O  OD2 . ASP D 179 ? 0.3332 0.4581 0.1664 -0.0467 0.0667  0.0041  180 ASP D OD2 
7827 N  N   . PRO D 180 ? 0.1517 0.1384 0.1728 0.0148  0.0120  -0.0023 181 PRO D N   
7828 C  CA  . PRO D 180 ? 0.1380 0.1651 0.1568 0.0108  0.0272  0.0066  181 PRO D CA  
7829 C  C   . PRO D 180 ? 0.1322 0.1428 0.1504 0.0044  0.0041  0.0021  181 PRO D C   
7830 O  O   . PRO D 180 ? 0.1547 0.1350 0.1698 0.0159  0.0122  0.0017  181 PRO D O   
7831 C  CB  . PRO D 180 ? 0.1665 0.1770 0.1596 0.0109  0.0307  0.0206  181 PRO D CB  
7832 C  CG  . PRO D 180 ? 0.1213 0.1538 0.2213 0.0041  0.0311  0.0120  181 PRO D CG  
7833 C  CD  . PRO D 180 ? 0.1107 0.1614 0.2016 0.0063  0.0017  0.0127  181 PRO D CD  
7834 N  N   . ARG D 181 ? 0.1272 0.1395 0.1432 0.0024  0.0122  0.0057  182 ARG D N   
7835 C  CA  . ARG D 181 ? 0.1559 0.1448 0.1455 0.0048  0.0320  0.0035  182 ARG D CA  
7836 C  C   . ARG D 181 ? 0.1407 0.1450 0.1471 0.0298  0.0203  -0.0063 182 ARG D C   
7837 O  O   . ARG D 181 ? 0.1495 0.1856 0.2034 0.0236  0.0098  0.0384  182 ARG D O   
7838 C  CB  . ARG D 181 ? 0.1756 0.1705 0.1435 -0.0241 0.0392  -0.0048 182 ARG D CB  
7839 C  CG  . ARG D 181 ? 0.2098 0.1789 0.1692 -0.0031 -0.0126 -0.0311 182 ARG D CG  
7840 C  CD  . ARG D 181 ? 0.2499 0.1994 0.1579 -0.0031 -0.0024 -0.0236 182 ARG D CD  
7841 N  NE  . ARG D 181 ? 0.2398 0.2452 0.1707 0.0412  0.0241  0.0212  182 ARG D NE  
7842 C  CZ  . ARG D 181 ? 0.3418 0.2831 0.2985 0.0712  -0.0041 -0.0657 182 ARG D CZ  
7843 N  NH1 . ARG D 181 ? 0.3312 0.2876 0.2594 0.0465  0.0148  -0.0210 182 ARG D NH1 
7844 N  NH2 . ARG D 181 ? 0.3580 0.3684 0.2949 0.1437  0.0083  0.0500  182 ARG D NH2 
7845 N  N   . GLY D 182 ? 0.1511 0.1430 0.1773 0.0057  0.0272  -0.0127 183 GLY D N   
7846 C  CA  . GLY D 182 ? 0.1383 0.1414 0.2318 0.0097  0.0344  -0.0024 183 GLY D CA  
7847 C  C   . GLY D 182 ? 0.1888 0.1635 0.2023 0.0149  0.0500  0.0040  183 GLY D C   
7848 O  O   . GLY D 182 ? 0.1456 0.1705 0.2384 0.0127  0.0500  -0.0076 183 GLY D O   
7849 N  N   . LEU D 183 ? 0.1445 0.1466 0.1563 0.0148  0.0193  -0.0226 184 LEU D N   
7850 C  CA  . LEU D 183 ? 0.1062 0.1306 0.1454 0.0062  0.0135  -0.0026 184 LEU D CA  
7851 C  C   . LEU D 183 ? 0.1155 0.1429 0.1684 0.0179  0.0034  0.0065  184 LEU D C   
7852 O  O   . LEU D 183 ? 0.1577 0.1556 0.1606 0.0252  0.0339  0.0066  184 LEU D O   
7853 C  CB  . LEU D 183 ? 0.1617 0.1542 0.1387 0.0173  -0.0085 -0.0013 184 LEU D CB  
7854 C  CG  . LEU D 183 ? 0.1380 0.1867 0.1787 0.0152  -0.0078 -0.0054 184 LEU D CG  
7855 C  CD1 . LEU D 183 ? 0.1911 0.1949 0.1726 0.0500  0.0132  -0.0126 184 LEU D CD1 
7856 C  CD2 . LEU D 183 ? 0.1953 0.1563 0.2021 0.0260  -0.0186 -0.0351 184 LEU D CD2 
7857 N  N   . LEU D 184 ? 0.1206 0.1492 0.1527 -0.0012 0.0065  0.0015  185 LEU D N   
7858 C  CA  . LEU D 184 ? 0.1199 0.1425 0.1511 0.0126  0.0083  0.0215  185 LEU D CA  
7859 C  C   . LEU D 184 ? 0.1658 0.1412 0.2506 0.0244  0.0275  0.0522  185 LEU D C   
7860 O  O   . LEU D 184 ? 0.1793 0.2161 0.3185 0.0425  0.0632  0.0812  185 LEU D O   
7861 C  CB  . LEU D 184 ? 0.1441 0.1852 0.1490 0.0096  0.0412  0.0239  185 LEU D CB  
7862 C  CG  . LEU D 184 ? 0.1813 0.1703 0.1407 0.0034  0.0359  0.0076  185 LEU D CG  
7863 C  CD1 . LEU D 184 ? 0.1732 0.2061 0.1800 0.0309  0.0057  -0.0241 185 LEU D CD1 
7864 C  CD2 . LEU D 184 ? 0.1730 0.1683 0.1847 0.0035  0.0384  0.0130  185 LEU D CD2 
7865 N  N   . PRO D 185 ? 0.1380 0.1337 0.1545 -0.0055 0.0423  0.0244  186 PRO D N   
7866 C  CA  . PRO D 185 ? 0.1317 0.1535 0.1504 0.0200  0.0178  0.0170  186 PRO D CA  
7867 C  C   . PRO D 185 ? 0.1559 0.1317 0.1547 0.0089  0.0458  0.0200  186 PRO D C   
7868 O  O   . PRO D 185 ? 0.2003 0.1411 0.1229 0.0211  0.0758  0.0085  186 PRO D O   
7869 C  CB  . PRO D 185 ? 0.1492 0.1470 0.1393 0.0277  0.0209  0.0114  186 PRO D CB  
7870 C  CG  . PRO D 185 ? 0.1448 0.1317 0.1267 0.0187  0.0103  -0.0057 186 PRO D CG  
7871 C  CD  . PRO D 185 ? 0.1059 0.1597 0.1188 0.0129  0.0265  0.0223  186 PRO D CD  
7872 N  N   A GLU D 186 ? 0.1356 0.1714 0.1581 0.0138  0.0458  0.0527  187 GLU D N   
7873 N  N   B GLU D 186 ? 0.1928 0.1576 0.1606 0.0307  0.0335  0.0331  187 GLU D N   
7874 C  CA  A GLU D 186 ? 0.1699 0.1499 0.1662 0.0010  0.0194  0.0289  187 GLU D CA  
7875 C  CA  B GLU D 186 ? 0.1879 0.1768 0.1339 -0.0054 0.0427  0.0474  187 GLU D CA  
7876 C  C   A GLU D 186 ? 0.1430 0.1708 0.0954 0.0195  0.0027  0.0209  187 GLU D C   
7877 C  C   B GLU D 186 ? 0.1935 0.1525 0.1296 0.0236  0.0395  -0.0176 187 GLU D C   
7878 O  O   A GLU D 186 ? 0.1748 0.1836 0.1168 0.0034  0.0007  0.0059  187 GLU D O   
7879 O  O   B GLU D 186 ? 0.1608 0.1833 0.1253 -0.0109 0.0238  -0.0324 187 GLU D O   
7880 C  CB  A GLU D 186 ? 0.1599 0.1808 0.1815 -0.0023 0.0500  0.0658  187 GLU D CB  
7881 C  CB  B GLU D 186 ? 0.2310 0.1367 0.1576 -0.0088 0.0463  0.0313  187 GLU D CB  
7882 C  CG  A GLU D 186 ? 0.3490 0.2062 0.1875 0.0264  0.0526  0.0491  187 GLU D CG  
7883 C  CG  B GLU D 186 ? 0.2111 0.1646 0.2090 -0.0010 -0.0032 0.0098  187 GLU D CG  
7884 C  CD  A GLU D 186 ? 0.2605 0.2579 0.1969 -0.0340 0.0399  0.0931  187 GLU D CD  
7885 C  CD  B GLU D 186 ? 0.2450 0.1836 0.1797 0.0217  -0.0062 -0.0046 187 GLU D CD  
7886 O  OE1 A GLU D 186 ? 0.2134 0.2870 0.2757 0.0055  -0.0287 0.0179  187 GLU D OE1 
7887 O  OE1 B GLU D 186 ? 0.2427 0.1991 0.1998 -0.0054 0.0209  0.0737  187 GLU D OE1 
7888 O  OE2 A GLU D 186 ? 0.3574 0.4104 0.2942 0.1629  0.0054  0.0908  187 GLU D OE2 
7889 O  OE2 B GLU D 186 ? 0.2962 0.2538 0.2330 0.0256  0.0489  -0.0403 187 GLU D OE2 
7890 N  N   . SER D 187 ? 0.1508 0.1881 0.1225 0.0094  0.0559  0.0156  188 SER D N   
7891 C  CA  . SER D 187 ? 0.1941 0.1495 0.1545 0.0070  0.0273  -0.0060 188 SER D CA  
7892 C  C   . SER D 187 ? 0.1511 0.1793 0.1259 -0.0074 0.0388  0.0015  188 SER D C   
7893 O  O   . SER D 187 ? 0.1843 0.2002 0.1576 -0.0038 0.0370  -0.0172 188 SER D O   
7894 C  CB  . SER D 187 ? 0.1885 0.2075 0.1574 0.0282  0.0271  0.0229  188 SER D CB  
7895 O  OG  . SER D 187 ? 0.1770 0.2011 0.1856 0.0115  0.0328  0.0241  188 SER D OG  
7896 N  N   . LEU D 188 ? 0.1847 0.1577 0.1213 -0.0192 0.0379  0.0080  189 LEU D N   
7897 C  CA  . LEU D 188 ? 0.1730 0.1615 0.1238 -0.0055 0.0297  -0.0010 189 LEU D CA  
7898 C  C   . LEU D 188 ? 0.1550 0.1651 0.1321 -0.0089 0.0137  -0.0133 189 LEU D C   
7899 O  O   . LEU D 188 ? 0.1996 0.1894 0.1437 -0.0285 0.0472  -0.0189 189 LEU D O   
7900 C  CB  . LEU D 188 ? 0.1861 0.1549 0.1605 -0.0037 0.0255  -0.0165 189 LEU D CB  
7901 C  CG  . LEU D 188 ? 0.1919 0.1896 0.1520 -0.0237 0.0322  0.0063  189 LEU D CG  
7902 C  CD1 . LEU D 188 ? 0.2093 0.1931 0.2472 0.0225  0.0445  0.0054  189 LEU D CD1 
7903 C  CD2 . LEU D 188 ? 0.1987 0.2590 0.1350 0.0368  0.0590  0.0181  189 LEU D CD2 
7904 N  N   . ASP D 189 ? 0.1753 0.2000 0.1191 0.0329  0.0375  -0.0099 190 ASP D N   
7905 C  CA  . ASP D 189 ? 0.1466 0.1990 0.0983 -0.0020 0.0173  0.0087  190 ASP D CA  
7906 C  C   . ASP D 189 ? 0.1097 0.1276 0.0926 -0.0063 -0.0041 0.0131  190 ASP D C   
7907 O  O   . ASP D 189 ? 0.1310 0.1504 0.1001 -0.0143 0.0049  0.0082  190 ASP D O   
7908 C  CB  . ASP D 189 ? 0.1905 0.2238 0.1486 0.0153  -0.0186 0.0504  190 ASP D CB  
7909 C  CG  . ASP D 189 ? 0.2178 0.3036 0.1949 0.0051  0.0397  0.0271  190 ASP D CG  
7910 O  OD1 . ASP D 189 ? 0.3583 0.4178 0.1256 -0.0635 -0.0031 0.0151  190 ASP D OD1 
7911 O  OD2 . ASP D 189 ? 0.3682 0.4793 0.3226 -0.0131 0.0619  0.1340  190 ASP D OD2 
7912 N  N   . TYR D 190 ? 0.1289 0.1547 0.0997 0.0041  0.0076  0.0127  191 TYR D N   
7913 C  CA  . TYR D 190 ? 0.1116 0.1249 0.0913 0.0038  0.0098  0.0167  191 TYR D CA  
7914 C  C   . TYR D 190 ? 0.1080 0.1195 0.1188 0.0091  -0.0172 -0.0015 191 TYR D C   
7915 O  O   . TYR D 190 ? 0.1182 0.1383 0.0926 -0.0034 -0.0165 0.0046  191 TYR D O   
7916 C  CB  . TYR D 190 ? 0.1182 0.1308 0.1217 0.0114  -0.0144 0.0078  191 TYR D CB  
7917 C  CG  . TYR D 190 ? 0.1125 0.1199 0.1213 0.0198  0.0041  0.0198  191 TYR D CG  
7918 C  CD1 . TYR D 190 ? 0.1154 0.1437 0.1383 -0.0020 -0.0034 0.0188  191 TYR D CD1 
7919 C  CD2 . TYR D 190 ? 0.1466 0.1535 0.1290 0.0337  -0.0226 -0.0093 191 TYR D CD2 
7920 C  CE1 . TYR D 190 ? 0.1517 0.1347 0.1191 0.0010  0.0097  0.0024  191 TYR D CE1 
7921 C  CE2 . TYR D 190 ? 0.1344 0.1418 0.1374 0.0027  -0.0137 0.0119  191 TYR D CE2 
7922 C  CZ  . TYR D 190 ? 0.1254 0.1346 0.1430 0.0218  0.0010  -0.0023 191 TYR D CZ  
7923 O  OH  . TYR D 190 ? 0.1642 0.1531 0.1725 -0.0013 0.0155  -0.0032 191 TYR D OH  
7924 N  N   . TRP D 191 ? 0.1079 0.1211 0.0997 0.0082  0.0001  0.0000  192 TRP D N   
7925 C  CA  . TRP D 191 ? 0.1030 0.1000 0.0947 0.0127  0.0024  0.0017  192 TRP D CA  
7926 C  C   . TRP D 191 ? 0.0850 0.0933 0.0899 -0.0021 -0.0037 -0.0034 192 TRP D C   
7927 O  O   . TRP D 191 ? 0.0985 0.1184 0.0994 -0.0026 -0.0091 0.0062  192 TRP D O   
7928 C  CB  . TRP D 191 ? 0.0996 0.1089 0.1179 -0.0003 -0.0052 -0.0071 192 TRP D CB  
7929 C  CG  . TRP D 191 ? 0.0991 0.1195 0.0978 0.0023  0.0000  -0.0087 192 TRP D CG  
7930 C  CD1 . TRP D 191 ? 0.1213 0.1240 0.1341 0.0066  -0.0115 -0.0019 192 TRP D CD1 
7931 C  CD2 . TRP D 191 ? 0.1216 0.1154 0.1152 0.0108  0.0044  -0.0170 192 TRP D CD2 
7932 N  NE1 . TRP D 191 ? 0.1404 0.1278 0.1551 0.0147  -0.0236 -0.0078 192 TRP D NE1 
7933 C  CE2 . TRP D 191 ? 0.1369 0.1199 0.1218 0.0074  0.0000  -0.0170 192 TRP D CE2 
7934 C  CE3 . TRP D 191 ? 0.1211 0.1389 0.1278 -0.0065 0.0186  -0.0272 192 TRP D CE3 
7935 C  CZ2 . TRP D 191 ? 0.1660 0.1224 0.1438 0.0109  0.0119  0.0054  192 TRP D CZ2 
7936 C  CZ3 . TRP D 191 ? 0.1482 0.1407 0.1048 -0.0122 -0.0129 0.0052  192 TRP D CZ3 
7937 C  CH2 . TRP D 191 ? 0.1601 0.1462 0.1439 0.0142  0.0185  -0.0030 192 TRP D CH2 
7938 N  N   . THR D 192 ? 0.0997 0.0957 0.1057 0.0019  0.0030  0.0060  193 THR D N   
7939 C  CA  . THR D 192 ? 0.1021 0.1005 0.0970 0.0071  0.0143  0.0010  193 THR D CA  
7940 C  C   . THR D 192 ? 0.0929 0.1042 0.1035 -0.0041 0.0115  0.0109  193 THR D C   
7941 O  O   . THR D 192 ? 0.0948 0.1208 0.1053 -0.0060 -0.0023 0.0055  193 THR D O   
7942 C  CB  . THR D 192 ? 0.1033 0.1058 0.1018 0.0211  -0.0201 -0.0124 193 THR D CB  
7943 O  OG1 . THR D 192 ? 0.1137 0.1100 0.1103 -0.0048 -0.0113 0.0030  193 THR D OG1 
7944 C  CG2 . THR D 192 ? 0.1019 0.1356 0.1252 0.0007  -0.0135 -0.0120 193 THR D CG2 
7945 N  N   . TYR D 193 ? 0.1014 0.1193 0.1010 -0.0144 0.0046  0.0046  194 TYR D N   
7946 C  CA  . TYR D 193 ? 0.0931 0.1188 0.0881 0.0024  0.0059  0.0030  194 TYR D CA  
7947 C  C   . TYR D 193 ? 0.0933 0.1026 0.0971 -0.0043 0.0043  -0.0122 194 TYR D C   
7948 O  O   . TYR D 193 ? 0.1055 0.1089 0.0970 -0.0043 -0.0024 -0.0040 194 TYR D O   
7949 C  CB  . TYR D 193 ? 0.1143 0.1215 0.1341 -0.0081 -0.0028 -0.0267 194 TYR D CB  
7950 C  CG  . TYR D 193 ? 0.1018 0.1197 0.1107 0.0020  0.0193  -0.0013 194 TYR D CG  
7951 C  CD1 . TYR D 193 ? 0.0969 0.0888 0.1032 -0.0059 -0.0086 -0.0175 194 TYR D CD1 
7952 C  CD2 . TYR D 193 ? 0.1023 0.1037 0.1070 -0.0094 0.0135  -0.0028 194 TYR D CD2 
7953 C  CE1 . TYR D 193 ? 0.1091 0.0895 0.0773 0.0129  -0.0111 -0.0030 194 TYR D CE1 
7954 C  CE2 . TYR D 193 ? 0.1243 0.1204 0.1277 0.0065  0.0096  -0.0149 194 TYR D CE2 
7955 C  CZ  . TYR D 193 ? 0.1041 0.0782 0.0868 0.0026  0.0000  -0.0013 194 TYR D CZ  
7956 O  OH  . TYR D 193 ? 0.1080 0.0994 0.1096 -0.0119 0.0048  -0.0154 194 TYR D OH  
7957 N  N   . PRO D 194 ? 0.1066 0.1199 0.0970 -0.0170 -0.0038 -0.0023 195 PRO D N   
7958 C  CA  . PRO D 194 ? 0.1197 0.1094 0.1005 -0.0193 -0.0073 -0.0133 195 PRO D CA  
7959 C  C   . PRO D 194 ? 0.1120 0.1071 0.0908 -0.0196 0.0013  -0.0083 195 PRO D C   
7960 O  O   . PRO D 194 ? 0.1124 0.1259 0.1186 -0.0086 0.0052  -0.0120 195 PRO D O   
7961 C  CB  . PRO D 194 ? 0.1559 0.1547 0.1531 -0.0516 -0.0155 -0.0274 195 PRO D CB  
7962 C  CG  . PRO D 194 ? 0.1544 0.1613 0.1304 -0.0405 -0.0010 0.0248  195 PRO D CG  
7963 C  CD  . PRO D 194 ? 0.1049 0.1657 0.1242 -0.0307 0.0010  0.0151  195 PRO D CD  
7964 N  N   . GLY D 195 ? 0.1098 0.1058 0.0863 -0.0167 0.0085  0.0012  196 GLY D N   
7965 C  CA  . GLY D 195 ? 0.1191 0.1283 0.1019 0.0032  -0.0057 -0.0060 196 GLY D CA  
7966 C  C   . GLY D 195 ? 0.1127 0.1017 0.1000 -0.0110 0.0027  -0.0023 196 GLY D C   
7967 O  O   . GLY D 195 ? 0.1191 0.1055 0.0940 -0.0203 0.0071  -0.0006 196 GLY D O   
7968 N  N   . SER D 196 ? 0.1010 0.0996 0.0865 -0.0060 0.0048  -0.0052 197 SER D N   
7969 C  CA  . SER D 196 ? 0.1084 0.1190 0.0839 -0.0104 -0.0076 -0.0066 197 SER D CA  
7970 C  C   . SER D 196 ? 0.1314 0.1021 0.1105 -0.0186 -0.0020 -0.0031 197 SER D C   
7971 O  O   . SER D 196 ? 0.1312 0.1125 0.0904 -0.0302 0.0093  -0.0017 197 SER D O   
7972 C  CB  . SER D 196 ? 0.1337 0.1127 0.1037 -0.0311 0.0193  -0.0097 197 SER D CB  
7973 O  OG  . SER D 196 ? 0.1303 0.1012 0.0904 -0.0219 0.0165  0.0000  197 SER D OG  
7974 N  N   . LEU D 197 ? 0.1121 0.1181 0.0935 -0.0157 -0.0048 -0.0023 198 LEU D N   
7975 C  CA  . LEU D 197 ? 0.1032 0.1141 0.0942 -0.0219 -0.0031 0.0094  198 LEU D CA  
7976 C  C   . LEU D 197 ? 0.1197 0.1155 0.0838 -0.0102 0.0032  0.0049  198 LEU D C   
7977 O  O   . LEU D 197 ? 0.1258 0.1206 0.1023 -0.0129 0.0083  0.0062  198 LEU D O   
7978 C  CB  . LEU D 197 ? 0.1529 0.1483 0.1353 0.0082  -0.0103 0.0107  198 LEU D CB  
7979 C  CG  . LEU D 197 ? 0.1527 0.1258 0.1290 -0.0215 0.0001  0.0211  198 LEU D CG  
7980 C  CD1 . LEU D 197 ? 0.2134 0.1705 0.1725 0.0236  0.0153  0.0766  198 LEU D CD1 
7981 C  CD2 . LEU D 197 ? 0.2145 0.1364 0.1410 0.0006  0.0049  0.0010  198 LEU D CD2 
7982 N  N   . THR D 198 ? 0.1416 0.1100 0.1032 -0.0258 0.0151  -0.0076 199 THR D N   
7983 C  CA  . THR D 198 ? 0.1308 0.1093 0.1028 -0.0361 0.0046  0.0003  199 THR D CA  
7984 C  C   . THR D 198 ? 0.1395 0.1269 0.0921 -0.0057 0.0013  0.0055  199 THR D C   
7985 O  O   . THR D 198 ? 0.1532 0.1328 0.0979 -0.0027 0.0126  0.0008  199 THR D O   
7986 C  CB  . THR D 198 ? 0.1184 0.1003 0.0994 -0.0076 -0.0085 0.0184  199 THR D CB  
7987 O  OG1 . THR D 198 ? 0.1295 0.1272 0.0917 0.0093  0.0035  0.0003  199 THR D OG1 
7988 C  CG2 . THR D 198 ? 0.1387 0.1371 0.1008 -0.0140 -0.0162 -0.0028 199 THR D CG2 
7989 N  N   . THR D 199 ? 0.1676 0.1315 0.1058 -0.0070 -0.0136 0.0092  200 THR D N   
7990 C  CA  . THR D 199 ? 0.1617 0.1491 0.1100 -0.0313 -0.0247 0.0175  200 THR D CA  
7991 C  C   . THR D 199 ? 0.2087 0.1490 0.1360 -0.0243 -0.0066 0.0203  200 THR D C   
7992 O  O   . THR D 199 ? 0.1908 0.1362 0.1234 -0.0076 0.0065  0.0082  200 THR D O   
7993 C  CB  . THR D 199 ? 0.1799 0.2314 0.1448 -0.0337 0.0120  0.0115  200 THR D CB  
7994 O  OG1 . THR D 199 ? 0.2468 0.2149 0.2348 -0.0021 0.0219  -0.0008 200 THR D OG1 
7995 C  CG2 . THR D 199 ? 0.2111 0.1755 0.1868 -0.0467 -0.0062 0.0031  200 THR D CG2 
7996 N  N   . PRO D 200 ? 0.2072 0.1513 0.1263 -0.0384 -0.0038 0.0432  201 PRO D N   
7997 C  CA  . PRO D 200 ? 0.1912 0.1450 0.1290 -0.0263 0.0211  0.0452  201 PRO D CA  
7998 C  C   . PRO D 200 ? 0.1836 0.1524 0.1788 -0.0131 -0.0121 0.0305  201 PRO D C   
7999 O  O   . PRO D 200 ? 0.1994 0.1692 0.1906 0.0013  0.0114  0.0138  201 PRO D O   
8000 C  CB  . PRO D 200 ? 0.2035 0.2163 0.1209 -0.0115 0.0108  0.0266  201 PRO D CB  
8001 C  CG  . PRO D 200 ? 0.2495 0.2166 0.1340 -0.0307 0.0403  0.0148  201 PRO D CG  
8002 C  CD  . PRO D 200 ? 0.2066 0.2020 0.1285 -0.0230 0.0126  0.0141  201 PRO D CD  
8003 N  N   . PRO D 201 ? 0.1696 0.1933 0.1229 -0.0207 -0.0142 0.0294  202 PRO D N   
8004 C  CA  . PRO D 201 ? 0.1708 0.1580 0.1640 -0.0241 -0.0068 0.0491  202 PRO D CA  
8005 C  C   . PRO D 201 ? 0.1770 0.1479 0.1443 -0.0003 0.0121  0.0194  202 PRO D C   
8006 O  O   . PRO D 201 ? 0.1888 0.1633 0.1332 -0.0196 -0.0054 0.0403  202 PRO D O   
8007 C  CB  . PRO D 201 ? 0.2689 0.1614 0.1815 0.0097  0.0129  0.0527  202 PRO D CB  
8008 C  CG  . PRO D 201 ? 0.2177 0.1811 0.2490 -0.0186 0.0157  0.0276  202 PRO D CG  
8009 C  CD  . PRO D 201 ? 0.2125 0.1876 0.1984 -0.0324 0.0184  0.0278  202 PRO D CD  
8010 N  N   . LEU D 202 ? 0.1705 0.1270 0.1012 -0.0051 0.0120  0.0052  203 LEU D N   
8011 C  CA  . LEU D 202 ? 0.1525 0.1116 0.1290 -0.0231 0.0289  0.0137  203 LEU D CA  
8012 C  C   . LEU D 202 ? 0.1299 0.1259 0.1010 -0.0131 0.0197  0.0291  203 LEU D C   
8013 O  O   . LEU D 202 ? 0.1554 0.1317 0.1312 -0.0284 0.0275  -0.0003 203 LEU D O   
8014 C  CB  . LEU D 202 ? 0.1667 0.1199 0.1177 -0.0172 0.0306  -0.0104 203 LEU D CB  
8015 C  CG  . LEU D 202 ? 0.1756 0.1371 0.0838 -0.0242 0.0183  0.0038  203 LEU D CG  
8016 C  CD1 . LEU D 202 ? 0.1962 0.1807 0.1159 -0.0010 0.0276  -0.0116 203 LEU D CD1 
8017 C  CD2 . LEU D 202 ? 0.1854 0.1281 0.1197 -0.0326 0.0070  -0.0026 203 LEU D CD2 
8018 N  N   . LEU D 203 ? 0.1752 0.1371 0.1218 -0.0116 0.0137  0.0120  204 LEU D N   
8019 C  CA  . LEU D 203 ? 0.1863 0.1335 0.1533 -0.0357 -0.0031 0.0307  204 LEU D CA  
8020 C  C   . LEU D 203 ? 0.1583 0.1380 0.1215 -0.0138 0.0184  0.0147  204 LEU D C   
8021 O  O   . LEU D 203 ? 0.1585 0.1233 0.1067 -0.0318 0.0254  0.0065  204 LEU D O   
8022 C  CB  . LEU D 203 ? 0.2280 0.1588 0.1531 0.0104  -0.0208 -0.0087 204 LEU D CB  
8023 C  CG  . LEU D 203 ? 0.2626 0.1817 0.1729 0.0189  0.0078  0.0428  204 LEU D CG  
8024 C  CD1 . LEU D 203 ? 0.3070 0.1926 0.2057 0.0472  -0.0149 0.0192  204 LEU D CD1 
8025 C  CD2 . LEU D 203 ? 0.3560 0.1594 0.2363 -0.0223 0.0432  0.0540  204 LEU D CD2 
8026 N  N   . GLU D 204 ? 0.1699 0.1576 0.1351 -0.0299 -0.0052 -0.0060 205 GLU D N   
8027 C  CA  . GLU D 204 ? 0.1436 0.1256 0.1480 -0.0355 0.0211  -0.0164 205 GLU D CA  
8028 C  C   . GLU D 204 ? 0.1581 0.1612 0.1676 -0.0165 0.0243  -0.0311 205 GLU D C   
8029 O  O   . GLU D 204 ? 0.1860 0.1784 0.1949 -0.0408 0.0263  -0.0434 205 GLU D O   
8030 C  CB  . GLU D 204 ? 0.1590 0.1262 0.1738 -0.0370 0.0489  -0.0087 205 GLU D CB  
8031 C  CG  . GLU D 204 ? 0.1854 0.1549 0.1520 -0.0201 0.0097  -0.0299 205 GLU D CG  
8032 C  CD  . GLU D 204 ? 0.1931 0.1728 0.1906 -0.0197 0.0355  -0.0001 205 GLU D CD  
8033 O  OE1 . GLU D 204 ? 0.2310 0.2045 0.2369 -0.0520 0.1019  -0.0386 205 GLU D OE1 
8034 O  OE2 . GLU D 204 ? 0.1561 0.1735 0.1569 -0.0242 0.0353  -0.0048 205 GLU D OE2 
8035 N  N   . CYS D 205 ? 0.1405 0.1057 0.1277 -0.0087 0.0284  0.0088  206 CYS D N   
8036 C  CA  . CYS D 205 ? 0.1181 0.1181 0.1274 0.0093  0.0041  -0.0006 206 CYS D CA  
8037 C  C   . CYS D 205 ? 0.1244 0.1249 0.1292 -0.0091 0.0021  -0.0093 206 CYS D C   
8038 O  O   . CYS D 205 ? 0.1540 0.1265 0.1450 0.0008  0.0241  0.0012  206 CYS D O   
8039 C  CB  . CYS D 205 ? 0.1624 0.1190 0.1331 0.0099  -0.0116 -0.0094 206 CYS D CB  
8040 S  SG  . CYS D 205 ? 0.1629 0.1414 0.1658 -0.0196 0.0006  -0.0054 206 CYS D SG  
8041 N  N   . VAL D 206 ? 0.1254 0.1125 0.1084 -0.0141 0.0132  0.0028  207 VAL D N   
8042 C  CA  . VAL D 206 ? 0.1204 0.0906 0.0996 -0.0173 0.0113  -0.0012 207 VAL D CA  
8043 C  C   . VAL D 206 ? 0.1103 0.0930 0.0965 -0.0073 0.0174  0.0052  207 VAL D C   
8044 O  O   . VAL D 206 ? 0.1323 0.1288 0.1203 0.0038  0.0187  -0.0087 207 VAL D O   
8045 C  CB  . VAL D 206 ? 0.1199 0.0939 0.1036 -0.0135 0.0148  -0.0093 207 VAL D CB  
8046 C  CG1 . VAL D 206 ? 0.1098 0.1075 0.1138 -0.0226 0.0254  -0.0142 207 VAL D CG1 
8047 C  CG2 . VAL D 206 ? 0.1619 0.1355 0.1039 -0.0024 0.0065  0.0071  207 VAL D CG2 
8048 N  N   . THR D 207 ? 0.1136 0.0960 0.1037 -0.0082 0.0093  0.0024  208 THR D N   
8049 C  CA  . THR D 207 ? 0.1204 0.1167 0.1012 -0.0065 0.0020  -0.0024 208 THR D CA  
8050 C  C   . THR D 207 ? 0.0942 0.0969 0.1009 0.0043  -0.0176 0.0015  208 THR D C   
8051 O  O   . THR D 207 ? 0.1116 0.0885 0.1150 0.0010  0.0142  0.0024  208 THR D O   
8052 C  CB  . THR D 207 ? 0.1301 0.1032 0.1001 -0.0208 0.0136  -0.0114 208 THR D CB  
8053 O  OG1 . THR D 207 ? 0.1439 0.1019 0.1394 -0.0244 -0.0068 -0.0071 208 THR D OG1 
8054 C  CG2 . THR D 207 ? 0.1488 0.1307 0.1209 0.0038  -0.0037 0.0052  208 THR D CG2 
8055 N  N   . TRP D 208 ? 0.1093 0.0913 0.0953 -0.0010 -0.0013 -0.0015 209 TRP D N   
8056 C  CA  . TRP D 208 ? 0.1197 0.0886 0.0859 0.0010  0.0127  0.0005  209 TRP D CA  
8057 C  C   . TRP D 208 ? 0.0929 0.0861 0.0899 -0.0052 -0.0020 0.0021  209 TRP D C   
8058 O  O   . TRP D 208 ? 0.0935 0.0979 0.0924 0.0046  -0.0019 -0.0038 209 TRP D O   
8059 C  CB  . TRP D 208 ? 0.0927 0.1030 0.0929 0.0142  -0.0037 -0.0089 209 TRP D CB  
8060 C  CG  . TRP D 208 ? 0.0863 0.0836 0.0842 0.0034  0.0093  -0.0034 209 TRP D CG  
8061 C  CD1 . TRP D 208 ? 0.1337 0.1017 0.0870 -0.0086 0.0080  0.0182  209 TRP D CD1 
8062 C  CD2 . TRP D 208 ? 0.1062 0.0784 0.1045 -0.0057 0.0098  0.0070  209 TRP D CD2 
8063 N  NE1 . TRP D 208 ? 0.1086 0.1027 0.1062 -0.0031 0.0205  -0.0176 209 TRP D NE1 
8064 C  CE2 . TRP D 208 ? 0.0989 0.1001 0.0951 0.0044  0.0037  -0.0085 209 TRP D CE2 
8065 C  CE3 . TRP D 208 ? 0.0719 0.0843 0.1154 -0.0110 -0.0044 -0.0035 209 TRP D CE3 
8066 C  CZ2 . TRP D 208 ? 0.1146 0.1142 0.1128 -0.0194 -0.0096 -0.0255 209 TRP D CZ2 
8067 C  CZ3 . TRP D 208 ? 0.0872 0.1048 0.1204 -0.0110 -0.0026 -0.0120 209 TRP D CZ3 
8068 C  CH2 . TRP D 208 ? 0.0989 0.1103 0.1206 0.0038  -0.0131 -0.0206 209 TRP D CH2 
8069 N  N   . ILE D 209 ? 0.0895 0.1032 0.0852 -0.0027 0.0066  -0.0082 210 ILE D N   
8070 C  CA  . ILE D 209 ? 0.1001 0.0933 0.0935 0.0013  0.0070  0.0048  210 ILE D CA  
8071 C  C   . ILE D 209 ? 0.0890 0.1003 0.0951 0.0013  -0.0057 0.0093  210 ILE D C   
8072 O  O   . ILE D 209 ? 0.0940 0.1033 0.1154 0.0027  -0.0099 -0.0096 210 ILE D O   
8073 C  CB  . ILE D 209 ? 0.1263 0.0985 0.1019 -0.0005 -0.0013 0.0007  210 ILE D CB  
8074 C  CG1 . ILE D 209 ? 0.1586 0.1071 0.1398 -0.0151 0.0337  -0.0230 210 ILE D CG1 
8075 C  CG2 . ILE D 209 ? 0.1347 0.1445 0.1017 -0.0020 0.0216  0.0034  210 ILE D CG2 
8076 C  CD1 . ILE D 209 ? 0.2012 0.1299 0.1701 0.0271  0.0178  -0.0236 210 ILE D CD1 
8077 N  N   . VAL D 210 ? 0.1156 0.0903 0.0776 0.0000  -0.0066 -0.0048 211 VAL D N   
8078 C  CA  . VAL D 210 ? 0.0935 0.0945 0.0818 0.0007  0.0201  -0.0080 211 VAL D CA  
8079 C  C   . VAL D 210 ? 0.0820 0.0798 0.0895 0.0049  0.0041  -0.0017 211 VAL D C   
8080 O  O   . VAL D 210 ? 0.0997 0.1141 0.1033 0.0054  -0.0041 0.0031  211 VAL D O   
8081 C  CB  . VAL D 210 ? 0.1066 0.1015 0.0780 0.0057  0.0239  -0.0043 211 VAL D CB  
8082 C  CG1 . VAL D 210 ? 0.1237 0.1014 0.1010 -0.0119 0.0249  0.0038  211 VAL D CG1 
8083 C  CG2 . VAL D 210 ? 0.1177 0.1261 0.0920 -0.0091 0.0020  0.0115  211 VAL D CG2 
8084 N  N   . LEU D 211 ? 0.1067 0.1059 0.0854 -0.0006 0.0271  0.0057  212 LEU D N   
8085 C  CA  . LEU D 211 ? 0.1215 0.1066 0.0793 0.0010  0.0147  0.0057  212 LEU D CA  
8086 C  C   . LEU D 211 ? 0.1258 0.1094 0.1068 0.0051  0.0110  0.0062  212 LEU D C   
8087 O  O   . LEU D 211 ? 0.1098 0.1286 0.1145 -0.0163 0.0140  0.0008  212 LEU D O   
8088 C  CB  . LEU D 211 ? 0.1145 0.1084 0.0973 -0.0048 0.0046  0.0109  212 LEU D CB  
8089 C  CG  . LEU D 211 ? 0.0892 0.1269 0.1265 0.0003  0.0131  0.0006  212 LEU D CG  
8090 C  CD1 . LEU D 211 ? 0.1163 0.1699 0.1308 -0.0070 0.0443  0.0234  212 LEU D CD1 
8091 C  CD2 . LEU D 211 ? 0.1348 0.1342 0.0847 0.0046  -0.0030 -0.0043 212 LEU D CD2 
8092 N  N   . LYS D 212 ? 0.1216 0.1271 0.1028 0.0059  0.0068  0.0089  213 LYS D N   
8093 C  CA  . LYS D 212 ? 0.1396 0.1154 0.1305 0.0065  0.0017  0.0122  213 LYS D CA  
8094 C  C   . LYS D 212 ? 0.1258 0.1143 0.1199 0.0193  0.0052  0.0142  213 LYS D C   
8095 O  O   . LYS D 212 ? 0.1877 0.1277 0.1594 0.0136  0.0386  0.0142  213 LYS D O   
8096 C  CB  . LYS D 212 ? 0.1612 0.1660 0.1678 -0.0041 -0.0126 0.0125  213 LYS D CB  
8097 C  CG  . LYS D 212 ? 0.1784 0.1811 0.2509 -0.0166 0.0307  0.0181  213 LYS D CG  
8098 C  CD  . LYS D 212 ? 0.3652 0.3862 0.3504 -0.1413 -0.0087 0.0855  213 LYS D CD  
8099 C  CE  . LYS D 212 ? 0.3862 0.4230 0.5073 0.0870  -0.1351 -0.0700 213 LYS D CE  
8100 N  NZ  . LYS D 212 ? 0.3515 0.3197 0.2481 0.0741  0.0237  -0.0091 213 LYS D NZ  
8101 N  N   . GLU D 213 ? 0.0958 0.1262 0.1195 0.0031  -0.0010 0.0068  214 GLU D N   
8102 C  CA  . GLU D 213 ? 0.1356 0.1377 0.1283 -0.0035 0.0019  -0.0048 214 GLU D CA  
8103 C  C   . GLU D 213 ? 0.1221 0.1221 0.1118 0.0063  0.0126  0.0096  214 GLU D C   
8104 O  O   . GLU D 213 ? 0.1218 0.1167 0.1127 0.0057  0.0109  0.0120  214 GLU D O   
8105 C  CB  . GLU D 213 ? 0.1430 0.1845 0.1314 0.0166  0.0313  -0.0126 214 GLU D CB  
8106 C  CG  . GLU D 213 ? 0.2258 0.2179 0.2003 -0.0107 0.0362  0.0142  214 GLU D CG  
8107 C  CD  . GLU D 213 ? 0.2728 0.2466 0.2070 -0.0205 0.0520  0.0000  214 GLU D CD  
8108 O  OE1 . GLU D 213 ? 0.2355 0.1955 0.1586 -0.0092 0.0692  0.0285  214 GLU D OE1 
8109 O  OE2 . GLU D 213 ? 0.3962 0.3792 0.3856 -0.0852 0.1527  0.0163  214 GLU D OE2 
8110 N  N   . PRO D 214 ? 0.1181 0.1105 0.1191 -0.0017 0.0065  0.0170  215 PRO D N   
8111 C  CA  . PRO D 214 ? 0.1149 0.1084 0.1590 -0.0038 -0.0109 -0.0044 215 PRO D CA  
8112 C  C   . PRO D 214 ? 0.1430 0.1457 0.1238 0.0055  0.0120  0.0175  215 PRO D C   
8113 O  O   . PRO D 214 ? 0.1508 0.1712 0.1416 0.0107  0.0132  0.0322  215 PRO D O   
8114 C  CB  . PRO D 214 ? 0.1299 0.1105 0.1262 0.0000  0.0200  0.0013  215 PRO D CB  
8115 C  CG  . PRO D 214 ? 0.2495 0.1856 0.2064 0.0531  -0.0581 -0.0291 215 PRO D CG  
8116 C  CD  . PRO D 214 ? 0.1705 0.1188 0.1147 0.0234  -0.0174 0.0186  215 PRO D CD  
8117 N  N   . ILE D 215 ? 0.1188 0.1211 0.1283 -0.0115 -0.0054 -0.0171 216 ILE D N   
8118 C  CA  . ILE D 215 ? 0.1233 0.1499 0.1703 0.0126  0.0211  -0.0130 216 ILE D CA  
8119 C  C   . ILE D 215 ? 0.1324 0.1335 0.1314 -0.0102 0.0137  0.0102  216 ILE D C   
8120 O  O   . ILE D 215 ? 0.1472 0.1305 0.1448 -0.0068 0.0190  -0.0024 216 ILE D O   
8121 C  CB  . ILE D 215 ? 0.1466 0.1230 0.1412 0.0142  0.0031  -0.0044 216 ILE D CB  
8122 C  CG1 . ILE D 215 ? 0.1453 0.1583 0.1545 0.0096  -0.0181 0.0089  216 ILE D CG1 
8123 C  CG2 . ILE D 215 ? 0.1757 0.1660 0.1594 -0.0264 0.0104  -0.0207 216 ILE D CG2 
8124 C  CD1 . ILE D 215 ? 0.1456 0.1416 0.1790 0.0023  -0.0131 0.0182  216 ILE D CD1 
8125 N  N   . SER D 216 ? 0.0631 0.0712 0.0824 0.0074  0.0024  -0.0146 217 SER D N   
8126 C  CA  . SER D 216 ? 0.0803 0.0600 0.0881 0.0035  0.0083  -0.0110 217 SER D CA  
8127 C  C   . SER D 216 ? 0.0651 0.0386 0.1001 -0.0052 0.0198  0.0137  217 SER D C   
8128 O  O   . SER D 216 ? 0.0772 0.0763 0.0822 0.0041  0.0221  -0.0052 217 SER D O   
8129 C  CB  . SER D 216 ? 0.1601 0.0644 0.1838 0.0066  -0.0275 0.0562  217 SER D CB  
8130 O  OG  . SER D 216 ? 0.1091 0.1644 0.1547 -0.0133 0.0070  0.0277  217 SER D OG  
8131 N  N   . VAL D 217 ? 0.1385 0.1123 0.1511 -0.0100 -0.0041 0.0131  218 VAL D N   
8132 C  CA  . VAL D 217 ? 0.1513 0.1231 0.1511 0.0184  -0.0019 0.0125  218 VAL D CA  
8133 C  C   . VAL D 217 ? 0.1432 0.1359 0.1825 -0.0129 -0.0060 0.0032  218 VAL D C   
8134 O  O   . VAL D 217 ? 0.1366 0.1332 0.1620 -0.0071 0.0227  0.0217  218 VAL D O   
8135 C  CB  . VAL D 217 ? 0.1630 0.1184 0.1811 -0.0130 0.0155  0.0063  218 VAL D CB  
8136 C  CG1 . VAL D 217 ? 0.1820 0.1071 0.1935 -0.0055 0.0073  0.0055  218 VAL D CG1 
8137 C  CG2 . VAL D 217 ? 0.1825 0.1455 0.1856 -0.0209 0.0375  0.0216  218 VAL D CG2 
8138 N  N   . SER D 218 ? 0.1608 0.1247 0.1629 -0.0057 0.0015  0.0120  219 SER D N   
8139 C  CA  . SER D 218 ? 0.1562 0.1272 0.1834 0.0087  0.0350  -0.0120 219 SER D CA  
8140 C  C   . SER D 218 ? 0.1716 0.1321 0.1563 0.0057  -0.0031 0.0000  219 SER D C   
8141 O  O   . SER D 218 ? 0.1515 0.1438 0.1897 -0.0094 -0.0006 -0.0010 219 SER D O   
8142 C  CB  . SER D 218 ? 0.1335 0.1414 0.1863 -0.0227 0.0098  0.0344  219 SER D CB  
8143 O  OG  . SER D 218 ? 0.1741 0.1635 0.1998 -0.0214 -0.0044 0.0234  219 SER D OG  
8144 N  N   A SER D 219 ? 0.1423 0.1120 0.2011 -0.0001 0.0000  -0.0020 220 SER D N   
8145 N  N   B SER D 219 ? 0.1513 0.1170 0.2050 0.0054  0.0054  -0.0065 220 SER D N   
8146 C  CA  A SER D 219 ? 0.2089 0.1356 0.1915 -0.0160 -0.0043 0.0351  220 SER D CA  
8147 C  CA  B SER D 219 ? 0.2064 0.1274 0.1949 -0.0243 0.0076  0.0311  220 SER D CA  
8148 C  C   A SER D 219 ? 0.1915 0.1186 0.1842 -0.0186 0.0046  0.0110  220 SER D C   
8149 C  C   B SER D 219 ? 0.1831 0.1270 0.2062 -0.0203 0.0074  0.0082  220 SER D C   
8150 O  O   A SER D 219 ? 0.1917 0.1301 0.1896 0.0066  0.0215  0.0046  220 SER D O   
8151 O  O   B SER D 219 ? 0.2276 0.1651 0.1976 0.0044  0.0066  0.0170  220 SER D O   
8152 C  CB  A SER D 219 ? 0.2054 0.1420 0.2436 -0.0141 -0.0019 0.0043  220 SER D CB  
8153 C  CB  B SER D 219 ? 0.1777 0.1339 0.2714 -0.0212 0.0277  -0.0147 220 SER D CB  
8154 O  OG  A SER D 219 ? 0.2116 0.1439 0.2448 0.0126  0.0017  0.0401  220 SER D OG  
8155 O  OG  B SER D 219 ? 0.2003 0.1425 0.2468 0.0423  -0.0113 -0.0024 220 SER D OG  
8156 N  N   . GLU D 220 ? 0.1782 0.1276 0.2175 -0.0258 -0.0013 -0.0157 221 GLU D N   
8157 C  CA  . GLU D 220 ? 0.2274 0.1556 0.2396 0.0076  0.0000  -0.0005 221 GLU D CA  
8158 C  C   . GLU D 220 ? 0.1673 0.1574 0.1931 -0.0070 -0.0006 0.0010  221 GLU D C   
8159 O  O   . GLU D 220 ? 0.2118 0.1703 0.2023 -0.0116 -0.0239 -0.0003 221 GLU D O   
8160 C  CB  . GLU D 220 ? 0.2384 0.1782 0.2527 -0.0357 0.0259  -0.0252 221 GLU D CB  
8161 C  CG  . GLU D 220 ? 0.2072 0.2211 0.3519 -0.0852 -0.0057 -0.0164 221 GLU D CG  
8162 C  CD  . GLU D 220 ? 0.3274 0.2161 0.3679 -0.0320 0.0155  -0.0167 221 GLU D CD  
8163 O  OE1 . GLU D 220 ? 0.2601 0.2109 0.3353 -0.0342 0.0520  0.0186  221 GLU D OE1 
8164 O  OE2 . GLU D 220 ? 0.5257 0.3032 0.5866 -0.1884 -0.0866 0.0250  221 GLU D OE2 
8165 N  N   . GLN D 221 ? 0.1752 0.1225 0.2122 0.0086  -0.0233 -0.0066 222 GLN D N   
8166 C  CA  . GLN D 221 ? 0.1599 0.1224 0.1772 0.0015  -0.0147 0.0135  222 GLN D CA  
8167 C  C   . GLN D 221 ? 0.1459 0.1585 0.2066 -0.0046 0.0040  0.0242  222 GLN D C   
8168 O  O   . GLN D 221 ? 0.1611 0.1691 0.1800 0.0068  -0.0068 0.0293  222 GLN D O   
8169 C  CB  . GLN D 221 ? 0.1472 0.1518 0.1500 0.0023  -0.0057 0.0223  222 GLN D CB  
8170 C  CG  . GLN D 221 ? 0.1624 0.1529 0.1727 0.0131  -0.0006 0.0057  222 GLN D CG  
8171 C  CD  . GLN D 221 ? 0.1630 0.1159 0.1665 -0.0008 -0.0076 0.0043  222 GLN D CD  
8172 O  OE1 . GLN D 221 ? 0.1398 0.1412 0.1667 -0.0043 0.0000  0.0120  222 GLN D OE1 
8173 N  NE2 . GLN D 221 ? 0.1319 0.1272 0.1658 -0.0115 0.0171  0.0089  222 GLN D NE2 
8174 N  N   . VAL D 222 ? 0.1520 0.1466 0.1836 0.0103  -0.0088 0.0121  223 VAL D N   
8175 C  CA  . VAL D 222 ? 0.1542 0.1502 0.1895 0.0377  -0.0199 0.0024  223 VAL D CA  
8176 C  C   . VAL D 222 ? 0.1947 0.1766 0.1748 -0.0023 -0.0060 0.0275  223 VAL D C   
8177 O  O   . VAL D 222 ? 0.1883 0.1653 0.1951 0.0214  0.0000  0.0228  223 VAL D O   
8178 C  CB  . VAL D 222 ? 0.1870 0.2206 0.2714 0.0694  0.0006  0.0461  223 VAL D CB  
8179 C  CG1 . VAL D 222 ? 0.2619 0.2079 0.2691 0.0127  -0.0104 0.0476  223 VAL D CG1 
8180 C  CG2 . VAL D 222 ? 0.2211 0.2416 0.2867 -0.0065 0.0350  -0.0126 223 VAL D CG2 
8181 N  N   . LEU D 223 ? 0.1687 0.1536 0.1869 0.0210  -0.0143 0.0109  224 LEU D N   
8182 C  CA  . LEU D 223 ? 0.1863 0.1811 0.1951 -0.0098 0.0060  0.0175  224 LEU D CA  
8183 C  C   . LEU D 223 ? 0.2263 0.1615 0.1865 -0.0353 0.0189  0.0236  224 LEU D C   
8184 O  O   . LEU D 223 ? 0.2565 0.1935 0.1685 -0.0153 -0.0082 0.0118  224 LEU D O   
8185 C  CB  . LEU D 223 ? 0.2545 0.1802 0.2773 -0.0386 -0.0136 0.0059  224 LEU D CB  
8186 C  CG  . LEU D 223 ? 0.2431 0.2608 0.2779 0.0229  -0.0313 0.0311  224 LEU D CG  
8187 C  CD1 . LEU D 223 ? 0.3425 0.3691 0.3289 -0.0515 0.0428  0.0366  224 LEU D CD1 
8188 C  CD2 . LEU D 223 ? 0.4208 0.2235 0.3210 -0.0799 0.0511  -0.0175 224 LEU D CD2 
8189 N  N   . LYS D 224 ? 0.1869 0.1735 0.2098 0.0119  -0.0060 0.0093  225 LYS D N   
8190 C  CA  . LYS D 224 ? 0.1859 0.1981 0.2046 -0.0214 -0.0049 0.0245  225 LYS D CA  
8191 C  C   . LYS D 224 ? 0.1556 0.1893 0.1737 -0.0116 -0.0188 0.0299  225 LYS D C   
8192 O  O   . LYS D 224 ? 0.1666 0.1935 0.1549 -0.0051 -0.0024 0.0083  225 LYS D O   
8193 C  CB  . LYS D 224 ? 0.1791 0.2057 0.2565 0.0186  0.0098  -0.0131 225 LYS D CB  
8194 C  CG  . LYS D 224 ? 0.2339 0.2680 0.2285 -0.0458 0.0156  0.0241  225 LYS D CG  
8195 C  CD  . LYS D 224 ? 0.3828 0.3596 0.2655 -0.0886 0.1277  0.0533  225 LYS D CD  
8196 C  CE  . LYS D 224 ? 0.2619 0.3801 0.4398 -0.0824 0.0346  0.0348  225 LYS D CE  
8197 N  NZ  . LYS D 224 ? 0.3125 0.4272 0.2885 -0.0670 -0.0834 -0.0163 225 LYS D NZ  
8198 N  N   . PHE D 225 ? 0.1373 0.1489 0.1601 -0.0034 -0.0189 0.0198  226 PHE D N   
8199 C  CA  . PHE D 225 ? 0.1387 0.1199 0.1623 0.0027  -0.0120 0.0057  226 PHE D CA  
8200 C  C   . PHE D 225 ? 0.1650 0.1529 0.1949 -0.0098 -0.0285 0.0188  226 PHE D C   
8201 O  O   . PHE D 225 ? 0.1446 0.1732 0.1515 -0.0100 -0.0417 -0.0085 226 PHE D O   
8202 C  CB  . PHE D 225 ? 0.1621 0.1447 0.1660 -0.0076 -0.0386 -0.0138 226 PHE D CB  
8203 C  CG  . PHE D 225 ? 0.1650 0.1301 0.1509 0.0244  -0.0140 0.0173  226 PHE D CG  
8204 C  CD1 . PHE D 225 ? 0.1859 0.2346 0.2134 0.0364  -0.0087 -0.0322 226 PHE D CD1 
8205 C  CD2 . PHE D 225 ? 0.1856 0.2404 0.2199 -0.0310 -0.0083 -0.0465 226 PHE D CD2 
8206 C  CE1 . PHE D 225 ? 0.2120 0.2160 0.1861 0.0696  0.0038  -0.0175 226 PHE D CE1 
8207 C  CE2 . PHE D 225 ? 0.2400 0.2292 0.2242 -0.0305 -0.0017 -0.0478 226 PHE D CE2 
8208 C  CZ  . PHE D 225 ? 0.2601 0.1951 0.2606 -0.0315 0.0399  -0.0182 226 PHE D CZ  
8209 N  N   . ARG D 226 ? 0.1276 0.1326 0.1728 -0.0012 -0.0199 0.0000  227 ARG D N   
8210 C  CA  . ARG D 226 ? 0.1863 0.1705 0.1611 0.0076  -0.0328 -0.0015 227 ARG D CA  
8211 C  C   . ARG D 226 ? 0.1662 0.1301 0.1414 -0.0223 -0.0023 -0.0008 227 ARG D C   
8212 O  O   . ARG D 226 ? 0.1847 0.1912 0.1509 -0.0083 -0.0196 -0.0121 227 ARG D O   
8213 C  CB  . ARG D 226 ? 0.1385 0.1432 0.1849 0.0017  -0.0419 -0.0326 227 ARG D CB  
8214 C  CG  . ARG D 226 ? 0.1310 0.1605 0.1610 0.0088  -0.0390 -0.0087 227 ARG D CG  
8215 C  CD  . ARG D 226 ? 0.1820 0.1382 0.2127 0.0041  -0.0127 0.0124  227 ARG D CD  
8216 N  NE  . ARG D 226 ? 0.1418 0.1371 0.1885 -0.0007 0.0071  0.0282  227 ARG D NE  
8217 C  CZ  . ARG D 226 ? 0.1355 0.1560 0.1606 -0.0187 -0.0166 0.0368  227 ARG D CZ  
8218 N  NH1 . ARG D 226 ? 0.2055 0.1863 0.2669 -0.0857 -0.0239 0.0267  227 ARG D NH1 
8219 N  NH2 . ARG D 226 ? 0.2075 0.1387 0.2089 -0.0204 -0.0546 0.0498  227 ARG D NH2 
8220 N  N   . LYS D 227 ? 0.1696 0.1542 0.1941 -0.0192 -0.0253 0.0105  228 LYS D N   
8221 C  CA  . LYS D 227 ? 0.1802 0.1942 0.1671 -0.0108 -0.0296 0.0322  228 LYS D CA  
8222 C  C   . LYS D 227 ? 0.1438 0.1599 0.2064 -0.0073 -0.0432 0.0046  228 LYS D C   
8223 O  O   . LYS D 227 ? 0.1721 0.1791 0.1956 -0.0237 -0.0515 0.0197  228 LYS D O   
8224 C  CB  . LYS D 227 ? 0.1687 0.2239 0.2504 0.0256  -0.0104 0.0262  228 LYS D CB  
8225 C  CG  . LYS D 227 ? 0.2172 0.2732 0.2506 -0.0640 -0.0098 0.0377  228 LYS D CG  
8226 C  CD  . LYS D 227 ? 0.2307 0.3738 0.3341 -0.0913 0.0281  0.0119  228 LYS D CD  
8227 C  CE  . LYS D 227 ? 0.4961 0.5810 0.6679 0.0256  -0.1960 0.1199  228 LYS D CE  
8228 N  NZ  . LYS D 227 ? 0.8019 0.3319 0.8338 -0.1753 0.0966  0.0546  228 LYS D NZ  
8229 N  N   . LEU D 228 ? 0.1746 0.1608 0.2044 -0.0186 -0.0373 0.0181  229 LEU D N   
8230 C  CA  . LEU D 228 ? 0.1206 0.1459 0.1791 -0.0148 -0.0480 0.0038  229 LEU D CA  
8231 C  C   . LEU D 228 ? 0.1565 0.1466 0.1777 0.0099  -0.0357 -0.0209 229 LEU D C   
8232 O  O   . LEU D 228 ? 0.1673 0.1418 0.1594 0.0110  -0.0241 0.0129  229 LEU D O   
8233 C  CB  . LEU D 228 ? 0.1317 0.1605 0.1341 -0.0311 -0.0206 -0.0152 229 LEU D CB  
8234 C  CG  . LEU D 228 ? 0.1172 0.1495 0.1353 0.0131  -0.0249 0.0024  229 LEU D CG  
8235 C  CD1 . LEU D 228 ? 0.1518 0.1685 0.1502 -0.0417 -0.0192 -0.0027 229 LEU D CD1 
8236 C  CD2 . LEU D 228 ? 0.1633 0.1847 0.2348 0.0443  -0.0544 0.0124  229 LEU D CD2 
8237 N  N   . ASN D 229 ? 0.1538 0.1789 0.1538 -0.0082 -0.0236 0.0000  230 ASN D N   
8238 C  CA  . ASN D 229 ? 0.1567 0.1928 0.1569 -0.0076 -0.0287 0.0254  230 ASN D CA  
8239 C  C   . ASN D 229 ? 0.1996 0.1800 0.1466 -0.0148 -0.0254 0.0297  230 ASN D C   
8240 O  O   . ASN D 229 ? 0.1714 0.2113 0.2071 0.0020  -0.0623 -0.0068 230 ASN D O   
8241 C  CB  . ASN D 229 ? 0.1669 0.2138 0.1784 -0.0013 -0.0452 0.0055  230 ASN D CB  
8242 C  CG  . ASN D 229 ? 0.1985 0.2116 0.1741 -0.0305 -0.0281 0.0059  230 ASN D CG  
8243 O  OD1 . ASN D 229 ? 0.2872 0.2777 0.2554 -0.0357 -0.1124 -0.0199 230 ASN D OD1 
8244 N  ND2 . ASN D 229 ? 0.2208 0.1940 0.2296 -0.0419 -0.0427 0.0000  230 ASN D ND2 
8245 N  N   . PHE D 230 ? 0.1885 0.1827 0.1717 -0.0255 -0.0461 -0.0132 231 PHE D N   
8246 C  CA  . PHE D 230 ? 0.2120 0.1493 0.1486 -0.0093 -0.0148 -0.0049 231 PHE D CA  
8247 C  C   . PHE D 230 ? 0.2567 0.1915 0.1552 -0.0218 -0.0204 0.0024  231 PHE D C   
8248 O  O   . PHE D 230 ? 0.1978 0.2228 0.2233 -0.0129 -0.0666 0.0288  231 PHE D O   
8249 C  CB  . PHE D 230 ? 0.1962 0.2389 0.1674 0.0049  -0.0296 -0.0111 231 PHE D CB  
8250 C  CG  . PHE D 230 ? 0.1764 0.2010 0.1906 0.0083  -0.0439 -0.0040 231 PHE D CG  
8251 C  CD1 . PHE D 230 ? 0.2355 0.2007 0.1693 -0.0417 -0.0219 0.0348  231 PHE D CD1 
8252 C  CD2 . PHE D 230 ? 0.1908 0.1890 0.1908 0.0005  -0.0049 0.0754  231 PHE D CD2 
8253 C  CE1 . PHE D 230 ? 0.1877 0.2172 0.1795 -0.0271 -0.0441 0.0001  231 PHE D CE1 
8254 C  CE2 . PHE D 230 ? 0.1692 0.1942 0.1806 -0.0175 -0.0174 0.0494  231 PHE D CE2 
8255 C  CZ  . PHE D 230 ? 0.1914 0.1944 0.1565 -0.0252 0.0176  0.0308  231 PHE D CZ  
8256 N  N   . ASN D 231 ? 0.2185 0.2210 0.1678 0.0133  -0.0631 0.0153  232 ASN D N   
8257 C  CA  . ASN D 231 ? 0.2375 0.1782 0.1445 0.0137  -0.0392 0.0062  232 ASN D CA  
8258 C  C   . ASN D 231 ? 0.2050 0.2276 0.1726 0.0021  -0.0211 0.0057  232 ASN D C   
8259 O  O   . ASN D 231 ? 0.1983 0.1978 0.1630 0.0049  -0.0201 -0.0109 232 ASN D O   
8260 C  CB  . ASN D 231 ? 0.2328 0.2102 0.1709 -0.0245 -0.0487 -0.0242 232 ASN D CB  
8261 C  CG  . ASN D 231 ? 0.2233 0.2502 0.2025 -0.0065 -0.0322 0.0000  232 ASN D CG  
8262 O  OD1 . ASN D 231 ? 0.2245 0.1999 0.2088 -0.0359 -0.0285 0.0052  232 ASN D OD1 
8263 N  ND2 . ASN D 231 ? 0.2287 0.2027 0.2899 -0.0006 -0.0498 -0.0199 232 ASN D ND2 
8264 N  N   . GLY D 232 ? 0.2379 0.1754 0.1773 -0.0170 -0.0438 0.0073  233 GLY D N   
8265 C  CA  . GLY D 232 ? 0.2213 0.2239 0.2452 -0.0259 -0.0544 0.0071  233 GLY D CA  
8266 C  C   . GLY D 232 ? 0.2561 0.2245 0.2337 -0.0230 -0.1182 0.0196  233 GLY D C   
8267 O  O   . GLY D 232 ? 0.3134 0.2899 0.3375 0.0057  -0.1617 0.0142  233 GLY D O   
8268 N  N   . GLU D 233 ? 0.2763 0.2741 0.3763 -0.0603 -0.0776 0.0097  234 GLU D N   
8269 C  CA  . GLU D 233 ? 0.3023 0.4230 0.3470 -0.0939 -0.1037 0.0570  234 GLU D CA  
8270 C  C   . GLU D 233 ? 0.4337 0.4564 0.3959 -0.1077 -0.1273 0.0427  234 GLU D C   
8271 O  O   . GLU D 233 ? 0.4036 0.3801 0.3143 -0.1032 -0.2339 0.0198  234 GLU D O   
8272 C  CB  . GLU D 233 ? 0.3055 0.3743 0.3986 -0.0781 -0.1465 0.0340  234 GLU D CB  
8273 C  CG  . GLU D 233 ? 0.3465 0.4009 0.3131 -0.1208 -0.2236 0.1115  234 GLU D CG  
8274 C  CD  . GLU D 233 ? 0.3856 0.4945 0.3314 -0.1079 -0.1265 0.0408  234 GLU D CD  
8275 O  OE1 . GLU D 233 ? 0.4614 0.4907 0.4902 -0.0494 -0.1816 0.0296  234 GLU D OE1 
8276 O  OE2 . GLU D 233 ? 0.5134 0.7760 0.5504 -0.2545 0.0575  0.0538  234 GLU D OE2 
8277 N  N   . GLY D 234 ? 0.5425 0.3149 0.4018 -0.1295 -0.3082 0.0644  235 GLY D N   
8278 C  CA  . GLY D 234 ? 0.5871 0.5346 0.5450 -0.0474 0.0315  -0.0912 235 GLY D CA  
8279 C  C   . GLY D 234 ? 0.3675 0.7013 0.5695 0.3113  -0.2942 0.0702  235 GLY D C   
8280 O  O   . GLY D 234 ? 0.8493 1.0147 0.8138 -0.0483 -0.2355 -0.1508 235 GLY D O   
8281 N  N   . GLU D 235 ? 0.4787 0.5242 0.5615 0.0337  -0.1264 -0.0162 236 GLU D N   
8282 C  CA  . GLU D 235 ? 0.3691 0.3569 0.3770 -0.0679 -0.1429 -0.0189 236 GLU D CA  
8283 C  C   . GLU D 235 ? 0.3188 0.3325 0.2657 0.0308  -0.1062 -0.0313 236 GLU D C   
8284 O  O   . GLU D 235 ? 0.2836 0.3749 0.3032 0.0373  -0.1152 -0.0388 236 GLU D O   
8285 C  CB  . GLU D 235 ? 0.2975 0.3998 0.4250 -0.0966 -0.0775 0.0339  236 GLU D CB  
8286 C  CG  . GLU D 235 ? 0.5695 0.3528 0.4047 -0.0098 -0.2027 0.0322  236 GLU D CG  
8287 C  CD  . GLU D 235 ? 0.5738 0.4779 0.7152 -0.0923 -0.2518 -0.0445 236 GLU D CD  
8288 O  OE1 . GLU D 235 ? 0.5583 0.5123 0.2669 0.0313  0.0085  0.1555  236 GLU D OE1 
8289 O  OE2 . GLU D 235 ? 0.4316 0.4765 0.4818 -0.1010 -0.1362 0.0384  236 GLU D OE2 
8290 N  N   . PRO D 236 ? 0.3165 0.3156 0.2452 0.0098  -0.0733 -0.0364 237 PRO D N   
8291 C  CA  . PRO D 236 ? 0.2978 0.3034 0.1586 0.0099  -0.0531 -0.0384 237 PRO D CA  
8292 C  C   . PRO D 236 ? 0.1960 0.2442 0.1782 -0.0296 -0.0443 -0.0456 237 PRO D C   
8293 O  O   . PRO D 236 ? 0.2172 0.2321 0.2133 -0.0260 -0.0597 -0.0359 237 PRO D O   
8294 C  CB  . PRO D 236 ? 0.2779 0.2651 0.2132 0.0197  -0.0478 -0.0494 237 PRO D CB  
8295 C  CG  . PRO D 236 ? 0.4144 0.2219 0.2707 0.0183  -0.0403 -0.0401 237 PRO D CG  
8296 C  CD  . PRO D 236 ? 0.4323 0.2524 0.2508 0.0187  -0.0631 -0.0882 237 PRO D CD  
8297 N  N   . GLU D 237 ? 0.2685 0.2737 0.1858 -0.0403 -0.0515 -0.0143 238 GLU D N   
8298 C  CA  . GLU D 237 ? 0.2632 0.2558 0.1554 0.0085  -0.0310 0.0289  238 GLU D CA  
8299 C  C   . GLU D 237 ? 0.2617 0.1811 0.1701 -0.0119 -0.0388 -0.0439 238 GLU D C   
8300 O  O   . GLU D 237 ? 0.2296 0.2236 0.2612 -0.0192 -0.0192 -0.0303 238 GLU D O   
8301 C  CB  . GLU D 237 ? 0.2581 0.2373 0.3016 -0.0463 -0.0251 -0.0258 238 GLU D CB  
8302 C  CG  . GLU D 237 ? 0.3711 0.2492 0.2818 -0.0144 -0.0043 -0.0920 238 GLU D CG  
8303 C  CD  . GLU D 237 ? 0.2976 0.2768 0.3576 -0.0553 -0.0357 -0.0847 238 GLU D CD  
8304 O  OE1 . GLU D 237 ? 0.4381 0.3490 0.5177 -0.1412 0.0754  -0.1879 238 GLU D OE1 
8305 O  OE2 . GLU D 237 ? 0.2319 0.3005 0.3054 -0.0646 -0.0395 -0.0065 238 GLU D OE2 
8306 N  N   . GLU D 238 ? 0.1901 0.2120 0.1708 -0.0500 -0.0557 0.0153  239 GLU D N   
8307 C  CA  . GLU D 238 ? 0.2192 0.2578 0.1712 -0.0003 -0.0066 0.0373  239 GLU D CA  
8308 C  C   . GLU D 238 ? 0.2236 0.2023 0.1793 -0.0249 -0.0196 -0.0048 239 GLU D C   
8309 O  O   . GLU D 238 ? 0.2167 0.2020 0.1829 0.0068  -0.0263 0.0030  239 GLU D O   
8310 C  CB  . GLU D 238 ? 0.2393 0.2820 0.1341 -0.0544 -0.0126 -0.0214 239 GLU D CB  
8311 C  CG  . GLU D 238 ? 0.2406 0.2547 0.1574 -0.0249 0.0329  -0.0010 239 GLU D CG  
8312 C  CD  . GLU D 238 ? 0.2705 0.2492 0.2436 -0.0610 0.0000  0.0082  239 GLU D CD  
8313 O  OE1 . GLU D 238 ? 0.3208 0.4251 0.3346 0.0518  -0.0566 -0.0674 239 GLU D OE1 
8314 O  OE2 . GLU D 238 ? 0.3106 0.2786 0.2592 -0.0390 -0.0434 0.0395  239 GLU D OE2 
8315 N  N   . LEU D 239 ? 0.1687 0.1984 0.1773 -0.0055 -0.0395 -0.0055 240 LEU D N   
8316 C  CA  . LEU D 239 ? 0.1870 0.1906 0.1696 0.0043  -0.0149 -0.0251 240 LEU D CA  
8317 C  C   . LEU D 239 ? 0.1630 0.2079 0.1684 0.0207  -0.0015 0.0048  240 LEU D C   
8318 O  O   . LEU D 239 ? 0.1646 0.2055 0.1633 -0.0098 -0.0200 0.0043  240 LEU D O   
8319 C  CB  . LEU D 239 ? 0.2431 0.2145 0.1906 0.0049  -0.0035 0.0054  240 LEU D CB  
8320 C  CG  . LEU D 239 ? 0.2477 0.2317 0.1651 0.0076  -0.0143 -0.0078 240 LEU D CG  
8321 C  CD1 . LEU D 239 ? 0.3612 0.2175 0.3253 -0.0278 0.0247  0.0049  240 LEU D CD1 
8322 C  CD2 . LEU D 239 ? 0.2430 0.1689 0.2211 -0.0187 -0.0456 -0.0403 240 LEU D CD2 
8323 N  N   . MET D 240 ? 0.1533 0.1689 0.1384 0.0066  -0.0410 -0.0041 241 MET D N   
8324 C  CA  . MET D 240 ? 0.1511 0.1486 0.1897 -0.0066 -0.0544 -0.0010 241 MET D CA  
8325 C  C   . MET D 240 ? 0.1547 0.1651 0.1475 -0.0217 -0.0174 -0.0060 241 MET D C   
8326 O  O   . MET D 240 ? 0.1242 0.1714 0.1307 -0.0103 -0.0024 -0.0086 241 MET D O   
8327 C  CB  . MET D 240 ? 0.1895 0.1798 0.1723 -0.0168 -0.0483 -0.0225 241 MET D CB  
8328 C  CG  . MET D 240 ? 0.1814 0.1574 0.1766 -0.0109 -0.0645 0.0241  241 MET D CG  
8329 S  SD  . MET D 240 ? 0.2014 0.1793 0.1708 -0.0065 -0.0313 0.0226  241 MET D SD  
8330 C  CE  . MET D 240 ? 0.1755 0.1843 0.1673 -0.0013 -0.0287 0.0430  241 MET D CE  
8331 N  N   . VAL D 241 ? 0.1322 0.1425 0.1411 -0.0125 -0.0383 0.0006  242 VAL D N   
8332 C  CA  . VAL D 241 ? 0.1238 0.1558 0.1432 -0.0035 -0.0410 0.0129  242 VAL D CA  
8333 C  C   . VAL D 241 ? 0.1359 0.1504 0.1021 -0.0146 -0.0063 -0.0195 242 VAL D C   
8334 O  O   . VAL D 241 ? 0.1560 0.1562 0.1301 -0.0195 -0.0068 -0.0071 242 VAL D O   
8335 C  CB  . VAL D 241 ? 0.1438 0.1450 0.1337 -0.0151 -0.0220 0.0103  242 VAL D CB  
8336 C  CG1 . VAL D 241 ? 0.1818 0.2073 0.1696 -0.0340 -0.0010 0.0093  242 VAL D CG1 
8337 C  CG2 . VAL D 241 ? 0.1840 0.1712 0.1563 -0.0289 -0.0412 -0.0157 242 VAL D CG2 
8338 N  N   . ASP D 242 ? 0.1297 0.1199 0.1463 -0.0115 -0.0320 -0.0094 243 ASP D N   
8339 C  CA  . ASP D 242 ? 0.1430 0.1303 0.1286 -0.0096 -0.0065 -0.0297 243 ASP D CA  
8340 C  C   . ASP D 242 ? 0.1276 0.1349 0.1161 -0.0041 0.0005  0.0006  243 ASP D C   
8341 O  O   . ASP D 242 ? 0.1592 0.1531 0.1483 -0.0231 0.0254  0.0026  243 ASP D O   
8342 C  CB  . ASP D 242 ? 0.1500 0.1267 0.1360 -0.0135 0.0222  -0.0076 243 ASP D CB  
8343 C  CG  . ASP D 242 ? 0.1218 0.1202 0.1243 -0.0201 -0.0348 0.0006  243 ASP D CG  
8344 O  OD1 . ASP D 242 ? 0.1680 0.1294 0.1170 -0.0187 -0.0214 -0.0114 243 ASP D OD1 
8345 O  OD2 . ASP D 242 ? 0.2046 0.1671 0.1611 -0.0408 -0.0255 -0.0368 243 ASP D OD2 
8346 N  N   . ASN D 243 ? 0.1164 0.1028 0.1055 -0.0177 -0.0141 -0.0006 244 ASN D N   
8347 C  CA  . ASN D 243 ? 0.1193 0.1124 0.1453 -0.0233 -0.0227 0.0073  244 ASN D CA  
8348 C  C   . ASN D 243 ? 0.1128 0.1064 0.1024 0.0008  -0.0125 -0.0013 244 ASN D C   
8349 O  O   . ASN D 243 ? 0.1324 0.1168 0.1123 0.0083  -0.0152 -0.0052 244 ASN D O   
8350 C  CB  . ASN D 243 ? 0.1179 0.1369 0.1154 -0.0083 -0.0159 0.0049  244 ASN D CB  
8351 C  CG  . ASN D 243 ? 0.1191 0.1380 0.1191 -0.0087 -0.0189 0.0125  244 ASN D CG  
8352 O  OD1 . ASN D 243 ? 0.1411 0.1305 0.1421 0.0147  -0.0102 0.0143  244 ASN D OD1 
8353 N  ND2 . ASN D 243 ? 0.1741 0.1676 0.1689 0.0494  0.0028  0.0461  244 ASN D ND2 
8354 N  N   . TRP D 244 ? 0.1179 0.1008 0.1075 -0.0142 -0.0126 0.0063  245 TRP D N   
8355 C  CA  . TRP D 244 ? 0.1089 0.0994 0.1017 -0.0129 -0.0098 -0.0038 245 TRP D CA  
8356 C  C   . TRP D 244 ? 0.1316 0.1127 0.1103 -0.0008 -0.0063 -0.0010 245 TRP D C   
8357 O  O   . TRP D 244 ? 0.1395 0.1222 0.1220 -0.0132 0.0000  -0.0109 245 TRP D O   
8358 C  CB  . TRP D 244 ? 0.1430 0.0987 0.0881 0.0091  -0.0008 -0.0162 245 TRP D CB  
8359 C  CG  . TRP D 244 ? 0.1290 0.1010 0.0922 -0.0068 -0.0046 0.0071  245 TRP D CG  
8360 C  CD1 . TRP D 244 ? 0.1215 0.1146 0.1168 0.0155  -0.0153 -0.0065 245 TRP D CD1 
8361 C  CD2 . TRP D 244 ? 0.1115 0.1177 0.1100 -0.0131 -0.0111 0.0024  245 TRP D CD2 
8362 N  NE1 . TRP D 244 ? 0.1317 0.0997 0.1289 -0.0135 -0.0172 -0.0089 245 TRP D NE1 
8363 C  CE2 . TRP D 244 ? 0.1254 0.1150 0.1010 0.0024  -0.0138 -0.0043 245 TRP D CE2 
8364 C  CE3 . TRP D 244 ? 0.1186 0.1441 0.1195 0.0015  -0.0037 0.0049  245 TRP D CE3 
8365 C  CZ2 . TRP D 244 ? 0.1270 0.1262 0.1168 0.0133  0.0049  0.0006  245 TRP D CZ2 
8366 C  CZ3 . TRP D 244 ? 0.1389 0.1346 0.1324 0.0087  -0.0133 0.0041  245 TRP D CZ3 
8367 C  CH2 . TRP D 244 ? 0.1427 0.1586 0.1527 -0.0204 -0.0021 -0.0186 245 TRP D CH2 
8368 N  N   . ARG D 245 ? 0.1159 0.1124 0.0908 -0.0164 -0.0046 0.0100  246 ARG D N   
8369 C  CA  . ARG D 245 ? 0.1217 0.1084 0.1071 -0.0186 0.0074  0.0000  246 ARG D CA  
8370 C  C   . ARG D 245 ? 0.0962 0.1272 0.1073 -0.0154 0.0030  -0.0017 246 ARG D C   
8371 O  O   . ARG D 245 ? 0.1484 0.1378 0.1120 -0.0197 -0.0028 0.0049  246 ARG D O   
8372 C  CB  . ARG D 245 ? 0.1258 0.1138 0.1028 -0.0357 0.0024  -0.0032 246 ARG D CB  
8373 C  CG  . ARG D 245 ? 0.1313 0.1258 0.0953 -0.0271 0.0193  -0.0086 246 ARG D CG  
8374 C  CD  . ARG D 245 ? 0.1465 0.1132 0.1052 -0.0286 0.0138  0.0164  246 ARG D CD  
8375 N  NE  . ARG D 245 ? 0.1507 0.1407 0.0833 -0.0258 0.0057  0.0046  246 ARG D NE  
8376 C  CZ  . ARG D 245 ? 0.1369 0.1393 0.1238 -0.0362 0.0286  -0.0076 246 ARG D CZ  
8377 N  NH1 . ARG D 245 ? 0.1865 0.1547 0.1039 -0.0311 0.0355  0.0092  246 ARG D NH1 
8378 N  NH2 . ARG D 245 ? 0.1730 0.1586 0.1146 -0.0186 0.0416  0.0118  246 ARG D NH2 
8379 N  N   . PRO D 246 ? 0.1371 0.1369 0.1115 -0.0038 -0.0147 -0.0118 247 PRO D N   
8380 C  CA  . PRO D 246 ? 0.1186 0.1244 0.1369 -0.0176 -0.0076 -0.0093 247 PRO D CA  
8381 C  C   . PRO D 246 ? 0.1215 0.1163 0.1015 -0.0052 -0.0044 -0.0035 247 PRO D C   
8382 O  O   . PRO D 246 ? 0.1310 0.1271 0.1068 -0.0115 0.0160  -0.0008 247 PRO D O   
8383 C  CB  . PRO D 246 ? 0.1974 0.1684 0.1689 0.0190  -0.0165 -0.0608 247 PRO D CB  
8384 C  CG  . PRO D 246 ? 0.2917 0.2502 0.1520 0.0588  0.0000  -0.0476 247 PRO D CG  
8385 C  CD  . PRO D 246 ? 0.1910 0.1746 0.1064 0.0007  0.0034  -0.0261 247 PRO D CD  
8386 N  N   . ALA D 247 ? 0.1328 0.1319 0.1301 0.0115  -0.0188 -0.0034 248 ALA D N   
8387 C  CA  . ALA D 247 ? 0.1116 0.1322 0.1225 -0.0076 -0.0041 -0.0021 248 ALA D CA  
8388 C  C   . ALA D 247 ? 0.1532 0.1383 0.1146 -0.0043 0.0115  -0.0194 248 ALA D C   
8389 O  O   . ALA D 247 ? 0.1732 0.1520 0.1435 -0.0060 0.0211  -0.0283 248 ALA D O   
8390 C  CB  . ALA D 247 ? 0.1856 0.1366 0.1513 -0.0087 -0.0342 -0.0176 248 ALA D CB  
8391 N  N   . GLN D 248 ? 0.1222 0.1299 0.1237 -0.0195 0.0035  0.0059  249 GLN D N   
8392 C  CA  . GLN D 248 ? 0.1369 0.1335 0.0996 -0.0109 0.0206  -0.0143 249 GLN D CA  
8393 C  C   . GLN D 248 ? 0.1412 0.1377 0.1357 -0.0054 0.0212  -0.0027 249 GLN D C   
8394 O  O   . GLN D 248 ? 0.1353 0.1605 0.1482 0.0166  0.0028  -0.0234 249 GLN D O   
8395 C  CB  . GLN D 248 ? 0.1470 0.1382 0.1125 -0.0020 0.0277  0.0046  249 GLN D CB  
8396 C  CG  . GLN D 248 ? 0.1826 0.1344 0.1272 0.0149  -0.0115 0.0110  249 GLN D CG  
8397 C  CD  . GLN D 248 ? 0.1441 0.1958 0.1225 -0.0410 0.0073  -0.0052 249 GLN D CD  
8398 O  OE1 . GLN D 248 ? 0.2039 0.2263 0.1459 -0.0472 0.0373  -0.0054 249 GLN D OE1 
8399 N  NE2 . GLN D 248 ? 0.1770 0.1529 0.1378 -0.0219 0.0111  -0.0231 249 GLN D NE2 
8400 N  N   . PRO D 249 ? 0.1450 0.2010 0.1513 -0.0137 0.0210  -0.0339 250 PRO D N   
8401 C  CA  . PRO D 249 ? 0.1474 0.2278 0.1748 0.0129  0.0148  -0.0719 250 PRO D CA  
8402 C  C   . PRO D 249 ? 0.1230 0.1470 0.1378 -0.0041 0.0176  -0.0196 250 PRO D C   
8403 O  O   . PRO D 249 ? 0.1689 0.1762 0.1610 0.0041  0.0388  -0.0263 250 PRO D O   
8404 C  CB  . PRO D 249 ? 0.1668 0.3528 0.2071 -0.0140 0.0738  -0.1090 250 PRO D CB  
8405 C  CG  . PRO D 249 ? 0.1987 0.3512 0.2685 -0.0044 0.0179  -0.0623 250 PRO D CG  
8406 C  CD  . PRO D 249 ? 0.1951 0.2664 0.1475 -0.0021 0.0531  -0.0283 250 PRO D CD  
8407 N  N   . LEU D 250 ? 0.1507 0.1723 0.1635 0.0071  0.0149  -0.0315 251 LEU D N   
8408 C  CA  . LEU D 250 ? 0.1626 0.1703 0.1437 -0.0310 -0.0088 -0.0198 251 LEU D CA  
8409 C  C   . LEU D 250 ? 0.1551 0.1709 0.1518 -0.0220 0.0162  -0.0307 251 LEU D C   
8410 O  O   . LEU D 250 ? 0.1482 0.1633 0.1671 -0.0113 0.0295  -0.0305 251 LEU D O   
8411 C  CB  . LEU D 250 ? 0.1709 0.1497 0.1649 -0.0120 -0.0184 -0.0046 251 LEU D CB  
8412 C  CG  . LEU D 250 ? 0.1726 0.1826 0.1735 -0.0266 -0.0118 -0.0114 251 LEU D CG  
8413 C  CD1 . LEU D 250 ? 0.1402 0.1996 0.1757 -0.0048 -0.0166 0.0209  251 LEU D CD1 
8414 C  CD2 . LEU D 250 ? 0.1808 0.2118 0.2416 0.0107  -0.0366 0.0201  251 LEU D CD2 
8415 N  N   . LYS D 251 ? 0.1781 0.2233 0.2154 -0.0057 0.0215  -0.0283 252 LYS D N   
8416 C  CA  . LYS D 251 ? 0.1340 0.2664 0.2204 -0.0315 0.0017  -0.0641 252 LYS D CA  
8417 C  C   . LYS D 251 ? 0.1919 0.2502 0.2327 -0.0516 0.0546  -0.0388 252 LYS D C   
8418 O  O   . LYS D 251 ? 0.3032 0.4315 0.2560 -0.0828 -0.0351 0.0197  252 LYS D O   
8419 C  CB  . LYS D 251 ? 0.2267 0.2458 0.2754 -0.0502 0.0542  -0.0560 252 LYS D CB  
8420 C  CG  . LYS D 251 ? 0.2404 0.3154 0.2842 -0.0923 -0.0625 -0.0281 252 LYS D CG  
8421 C  CD  . LYS D 251 ? 0.3682 0.4667 0.3055 -0.0746 0.0023  -0.0254 252 LYS D CD  
8422 C  CE  . LYS D 251 ? 0.5117 0.4201 0.2901 -0.0869 -0.0249 -0.0154 252 LYS D CE  
8423 N  NZ  . LYS D 251 ? 0.4435 0.3309 0.4043 0.0719  0.0233  -0.0568 252 LYS D NZ  
8424 N  N   . ASN D 252 ? 0.1981 0.2529 0.2425 -0.0766 0.0540  -0.0579 253 ASN D N   
8425 C  CA  . ASN D 252 ? 0.2583 0.5317 0.2860 -0.1089 0.0725  -0.1528 253 ASN D CA  
8426 C  C   . ASN D 252 ? 0.2111 0.4850 0.2339 -0.0487 0.0144  -0.1263 253 ASN D C   
8427 O  O   . ASN D 252 ? 0.1969 0.4343 0.2953 0.0522  -0.0264 -0.1010 253 ASN D O   
8428 C  CB  . ASN D 252 ? 0.4040 0.6164 0.4305 -0.1924 0.2336  -0.0076 253 ASN D CB  
8429 C  CG  . ASN D 252 ? 0.4138 0.6439 0.7829 0.0557  0.1657  0.0218  253 ASN D CG  
8430 O  OD1 . ASN D 252 ? 0.3364 0.6538 0.7361 -0.0020 0.2354  0.0450  253 ASN D OD1 
8431 N  ND2 . ASN D 252 ? 0.9595 0.6251 0.6919 -0.2065 -0.0741 0.0419  253 ASN D ND2 
8432 N  N   . ARG D 253 ? 0.1396 0.3050 0.1845 0.0256  -0.0093 -0.0311 254 ARG D N   
8433 C  CA  . ARG D 253 ? 0.1114 0.1588 0.1536 -0.0126 -0.0121 -0.0104 254 ARG D CA  
8434 C  C   . ARG D 253 ? 0.1374 0.1847 0.1669 -0.0253 -0.0630 -0.0291 254 ARG D C   
8435 O  O   . ARG D 253 ? 0.2930 0.1881 0.1829 0.0166  -0.0127 -0.0089 254 ARG D O   
8436 C  CB  . ARG D 253 ? 0.1155 0.1283 0.1342 -0.0065 -0.0073 -0.0049 254 ARG D CB  
8437 C  CG  . ARG D 253 ? 0.1098 0.1466 0.1532 -0.0052 -0.0094 0.0065  254 ARG D CG  
8438 C  CD  . ARG D 253 ? 0.0996 0.1471 0.1287 -0.0120 -0.0059 -0.0183 254 ARG D CD  
8439 N  NE  . ARG D 253 ? 0.1136 0.1366 0.1369 -0.0074 0.0060  -0.0187 254 ARG D NE  
8440 C  CZ  . ARG D 253 ? 0.1123 0.1185 0.1228 -0.0163 0.0087  -0.0074 254 ARG D CZ  
8441 N  NH1 . ARG D 253 ? 0.1193 0.1360 0.1316 0.0024  0.0151  0.0148  254 ARG D NH1 
8442 N  NH2 . ARG D 253 ? 0.1353 0.1304 0.1200 -0.0215 0.0176  -0.0167 254 ARG D NH2 
8443 N  N   . GLN D 254 ? 0.1438 0.1714 0.1569 -0.0300 -0.0089 -0.0274 255 GLN D N   
8444 C  CA  . GLN D 254 ? 0.1547 0.2046 0.1780 -0.0149 -0.0170 0.0151  255 GLN D CA  
8445 C  C   . GLN D 254 ? 0.1562 0.1800 0.1800 0.0204  0.0060  -0.0030 255 GLN D C   
8446 O  O   . GLN D 254 ? 0.1665 0.1675 0.2258 -0.0001 0.0315  0.0006  255 GLN D O   
8447 C  CB  . GLN D 254 ? 0.1673 0.2640 0.2285 -0.0540 0.0114  -0.0498 255 GLN D CB  
8448 C  CG  . GLN D 254 ? 0.3379 0.4336 0.3984 -0.0557 0.0463  0.0595  255 GLN D CG  
8449 C  CD  . GLN D 254 ? 0.6682 0.8260 1.1936 0.1595  -0.0719 0.0509  255 GLN D CD  
8450 O  OE1 . GLN D 254 ? 0.7235 1.0470 0.7168 -0.0966 -0.1631 -0.1941 255 GLN D OE1 
8451 N  NE2 . GLN D 254 ? 0.6315 0.5827 0.8513 -0.0410 -0.6024 -0.1186 255 GLN D NE2 
8452 N  N   . ILE D 255 ? 0.1319 0.1714 0.1306 0.0010  0.0265  -0.0131 256 ILE D N   
8453 C  CA  . ILE D 255 ? 0.1267 0.1683 0.1321 -0.0021 0.0041  -0.0245 256 ILE D CA  
8454 C  C   . ILE D 255 ? 0.1474 0.1544 0.1200 0.0311  -0.0041 0.0115  256 ILE D C   
8455 O  O   . ILE D 255 ? 0.1328 0.1626 0.1603 0.0209  -0.0082 0.0041  256 ILE D O   
8456 C  CB  . ILE D 255 ? 0.1256 0.1438 0.1360 -0.0216 0.0126  -0.0076 256 ILE D CB  
8457 C  CG1 . ILE D 255 ? 0.1474 0.1594 0.1364 -0.0142 0.0153  -0.0370 256 ILE D CG1 
8458 C  CG2 . ILE D 255 ? 0.1394 0.1845 0.1676 -0.0030 0.0093  -0.0124 256 ILE D CG2 
8459 C  CD1 . ILE D 255 ? 0.1556 0.1647 0.1655 -0.0326 -0.0077 -0.0186 256 ILE D CD1 
8460 N  N   . LYS D 256 ? 0.1163 0.1353 0.1281 0.0076  0.0113  0.0073  257 LYS D N   
8461 C  CA  . LYS D 256 ? 0.1088 0.1762 0.1353 0.0140  -0.0065 -0.0263 257 LYS D CA  
8462 C  C   . LYS D 256 ? 0.1237 0.1358 0.1371 0.0098  -0.0138 0.0076  257 LYS D C   
8463 O  O   . LYS D 256 ? 0.1306 0.1861 0.1508 -0.0065 -0.0263 0.0439  257 LYS D O   
8464 C  CB  . LYS D 256 ? 0.1659 0.1759 0.1561 -0.0241 -0.0262 -0.0182 257 LYS D CB  
8465 C  CG  . LYS D 256 ? 0.2375 0.2206 0.2393 -0.0877 -0.0329 -0.0172 257 LYS D CG  
8466 C  CD  . LYS D 256 ? 0.3163 0.2445 0.3993 -0.0724 -0.0116 -0.0423 257 LYS D CD  
8467 C  CE  . LYS D 256 ? 0.3127 0.4398 0.6705 -0.1243 0.0310  0.0320  257 LYS D CE  
8468 N  NZ  . LYS D 256 ? 0.2975 0.4977 0.5127 -0.1274 -0.0172 0.0177  257 LYS D NZ  
8469 N  N   . ALA D 257 ? 0.1301 0.1586 0.1409 0.0051  -0.0228 0.0153  258 ALA D N   
8470 C  CA  . ALA D 257 ? 0.1279 0.1694 0.1332 0.0333  -0.0010 0.0052  258 ALA D CA  
8471 C  C   . ALA D 257 ? 0.1335 0.1429 0.1513 0.0091  0.0046  0.0082  258 ALA D C   
8472 O  O   . ALA D 257 ? 0.1314 0.1744 0.1337 -0.0020 -0.0176 -0.0020 258 ALA D O   
8473 C  CB  . ALA D 257 ? 0.1698 0.1535 0.1430 0.0137  0.0167  -0.0026 258 ALA D CB  
8474 N  N   . SER D 258 ? 0.1272 0.1484 0.1317 0.0192  -0.0034 -0.0076 259 SER D N   
8475 C  CA  . SER D 258 ? 0.1484 0.1574 0.1283 0.0133  0.0068  -0.0115 259 SER D CA  
8476 C  C   . SER D 258 ? 0.1718 0.1833 0.1283 -0.0175 -0.0247 -0.0020 259 SER D C   
8477 O  O   . SER D 258 ? 0.2497 0.2599 0.1466 0.0129  -0.0049 -0.0269 259 SER D O   
8478 C  CB  . SER D 258 ? 0.1518 0.1951 0.1199 0.0027  -0.0007 0.0115  259 SER D CB  
8479 O  OG  . SER D 258 ? 0.1452 0.1674 0.1243 0.0218  -0.0157 -0.0021 259 SER D OG  
8480 N  N   . PHE D 259 ? 0.2141 0.2054 0.1527 0.0028  -0.0138 0.0164  260 PHE D N   
8481 C  CA  . PHE D 259 ? 0.2100 0.2377 0.1480 0.0012  -0.0087 0.0401  260 PHE D CA  
8482 C  C   . PHE D 259 ? 0.2238 0.2490 0.2105 0.0076  -0.0487 0.0288  260 PHE D C   
8483 O  O   . PHE D 259 ? 0.2368 0.2023 0.2369 0.0252  -0.0204 0.0355  260 PHE D O   
8484 C  CB  . PHE D 259 ? 0.2439 0.2364 0.1481 -0.0390 0.0119  -0.0060 260 PHE D CB  
8485 C  CG  . PHE D 259 ? 0.2129 0.1978 0.1712 0.0278  0.0087  0.0003  260 PHE D CG  
8486 C  CD1 . PHE D 259 ? 0.1540 0.2029 0.1615 -0.0406 -0.0078 0.0120  260 PHE D CD1 
8487 C  CD2 . PHE D 259 ? 0.2870 0.2021 0.2127 -0.0037 0.0187  0.0154  260 PHE D CD2 
8488 C  CE1 . PHE D 259 ? 0.2170 0.1965 0.2272 -0.0263 0.0164  -0.0252 260 PHE D CE1 
8489 C  CE2 . PHE D 259 ? 0.2937 0.1914 0.2226 0.0040  -0.0255 0.0037  260 PHE D CE2 
8490 C  CZ  . PHE D 259 ? 0.2646 0.1910 0.2400 -0.0076 -0.0087 0.0289  260 PHE D CZ  
8491 N  N   . LYS D 260 ? 0.3865 0.3486 0.3120 0.0087  -0.0538 0.1509  261 LYS D N   
8492 C  CA  . LYS D 260 ? 0.4693 0.3916 0.4351 0.1097  -0.0711 0.0237  261 LYS D CA  
8493 C  C   . LYS D 260 ? 0.4438 0.6762 0.6169 -0.0621 -0.0634 0.1316  261 LYS D C   
8494 O  O   . LYS D 260 ? 0.9261 0.8817 0.4025 0.0364  -0.1067 0.1861  261 LYS D O   
8495 C  CB  . LYS D 260 ? 0.6237 0.2878 0.4334 0.0098  -0.1140 0.2276  261 LYS D CB  
8496 C  CG  . LYS D 260 ? 0.7006 0.5853 0.7203 -0.1067 -0.0553 0.2171  261 LYS D CG  
8497 C  CD  . LYS D 260 ? 0.7192 0.5827 0.4251 -0.0489 -0.1036 0.2894  261 LYS D CD  
8498 C  CE  . LYS D 260 ? 0.9660 0.8597 0.6062 -0.0273 0.0285  -0.0456 261 LYS D CE  
8499 N  NZ  . LYS D 260 ? 0.7096 0.4546 0.5304 -0.0346 -0.1186 0.0740  261 LYS D NZ  
8500 ZN ZN  . ZN  E .   ? 0.1098 0.0989 0.1048 0.0122  -0.0020 -0.0017 301 ZN  A ZN  
8501 O  O16 . WWX F .   ? 0.2585 0.3467 0.3693 0.0736  0.0038  -0.0307 302 WWX A O16 
8502 S  S14 . WWX F .   ? 0.2524 0.2824 0.2865 0.0274  -0.0331 -0.0026 302 WWX A S14 
8503 O  O15 . WWX F .   ? 0.3235 0.2587 0.3899 0.0063  -0.0489 -0.0256 302 WWX A O15 
8504 C  C18 . WWX F .   ? 0.3697 0.3186 0.2851 0.0661  -0.0535 -0.0775 302 WWX A C18 
8505 O  O20 . WWX F .   ? 0.5020 0.3431 0.4320 0.1001  -0.0305 -0.1235 302 WWX A O20 
8506 C  C17 . WWX F .   ? 0.3007 0.3510 0.2407 0.0383  -0.0282 0.0038  302 WWX A C17 
8507 C  C8  . WWX F .   ? 0.2117 0.2538 0.2323 0.0392  -0.0335 -0.0032 302 WWX A C8  
8508 C  C7  . WWX F .   ? 0.2587 0.2075 0.1859 0.0340  -0.0225 0.0074  302 WWX A C7  
8509 F  F12 . WWX F .   ? 0.2992 0.2125 0.2933 0.0513  -0.0428 0.0111  302 WWX A F12 
8510 C  C6  . WWX F .   ? 0.2093 0.1829 0.1893 -0.0024 0.0164  -0.0125 302 WWX A C6  
8511 F  F11 . WWX F .   ? 0.2531 0.1856 0.2073 0.0088  0.0283  0.0098  302 WWX A F11 
8512 C  C9  . WWX F .   ? 0.2159 0.1842 0.2179 0.0416  -0.0124 -0.0087 302 WWX A C9  
8513 C  C10 . WWX F .   ? 0.1748 0.1921 0.2953 0.0237  -0.0037 -0.0055 302 WWX A C10 
8514 F  F13 . WWX F .   ? 0.2168 0.2100 0.2533 0.0571  0.0229  0.0286  302 WWX A F13 
8515 C  C5  . WWX F .   ? 0.1711 0.1944 0.2179 0.0197  0.0324  0.0000  302 WWX A C5  
8516 S  S1  . WWX F .   ? 0.1656 0.1369 0.1993 0.0297  0.0368  0.0087  302 WWX A S1  
8517 O  O3  . WWX F .   ? 0.1840 0.1529 0.3273 0.0732  0.0822  0.0509  302 WWX A O3  
8518 N  N4  . WWX F .   ? 0.1272 0.0878 0.1457 0.0266  0.0302  0.0147  302 WWX A N4  
8519 O  O2  . WWX F .   ? 0.1445 0.1536 0.1832 0.0299  -0.0003 0.0381  302 WWX A O2  
8520 N  N19 . WWX F .   ? 0.2427 0.2046 0.2741 0.0287  -0.0135 0.0156  302 WWX A N19 
8521 C  C21 . WWX F .   ? 0.2623 0.1802 0.2360 0.0037  0.0135  0.0111  302 WWX A C21 
8522 C  C30 . WWX F .   ? 0.1928 0.1570 0.2368 -0.0099 -0.0168 -0.0153 302 WWX A C30 
8523 C  C35 . WWX F .   ? 0.2587 0.2080 0.2960 0.0115  0.0650  -0.0405 302 WWX A C35 
8524 C  C34 . WWX F .   ? 0.2849 0.2612 0.3023 -0.0212 0.0015  0.0199  302 WWX A C34 
8525 C  C33 . WWX F .   ? 0.2551 0.2511 0.1924 -0.0104 0.0130  -0.0485 302 WWX A C33 
8526 C  C32 . WWX F .   ? 0.1969 0.2008 0.2205 0.0240  -0.0364 -0.0776 302 WWX A C32 
8527 C  C31 . WWX F .   ? 0.2017 0.1754 0.2660 0.0035  -0.0397 -0.0450 302 WWX A C31 
8528 C  C22 . WWX F .   ? 0.3695 0.2066 0.3388 0.0491  -0.0007 -0.0684 302 WWX A C22 
8529 O  O29 . WWX F .   ? 0.2989 0.2727 0.3454 0.0516  -0.0555 -0.0242 302 WWX A O29 
8530 C  C23 . WWX F .   ? 0.2707 0.2099 0.2380 0.0088  -0.0359 -0.0603 302 WWX A C23 
8531 C  C28 . WWX F .   ? 0.2386 0.2120 0.3646 0.0333  -0.0421 -0.0013 302 WWX A C28 
8532 C  C27 . WWX F .   ? 0.2709 0.1800 0.3242 0.0063  -0.0263 -0.0458 302 WWX A C27 
8533 C  C26 . WWX F .   ? 0.2547 0.2915 0.2904 -0.0027 -0.0458 -0.0348 302 WWX A C26 
8534 C  C25 . WWX F .   ? 0.2867 0.2633 0.2720 0.0496  -0.0020 0.0017  302 WWX A C25 
8535 C  C24 . WWX F .   ? 0.2874 0.2727 0.2239 0.0163  -0.0144 -0.0273 302 WWX A C24 
8536 S  S   . DMS G .   ? 0.3167 0.3104 0.2549 0.0272  0.0219  -0.0032 303 DMS A S   
8537 O  O   . DMS G .   ? 0.4496 0.3350 0.3077 0.0182  -0.0828 0.0744  303 DMS A O   
8538 C  C1  . DMS G .   ? 0.2633 0.2860 0.2310 -0.0086 -0.0467 0.0527  303 DMS A C1  
8539 C  C2  . DMS G .   ? 0.3716 0.3282 0.2404 0.0449  0.0210  -0.0315 303 DMS A C2  
8540 N  N1  . BCN H .   ? 0.5335 0.3759 0.4981 -0.0214 -0.0793 -0.1494 304 BCN A N1  
8541 C  C1  . BCN H .   ? 0.3646 0.5982 0.6844 0.0003  -0.1174 -0.0485 304 BCN A C1  
8542 C  C2  . BCN H .   ? 0.5436 0.6392 0.8019 -0.1130 0.1372  -0.1189 304 BCN A C2  
8543 O  O21 . BCN H .   ? 0.4018 0.4897 0.4061 0.0188  -0.0978 -0.1606 304 BCN A O21 
8544 O  O22 . BCN H .   ? 0.5806 0.4138 0.8903 -0.0679 0.0395  -0.1244 304 BCN A O22 
8545 C  C3  . BCN H .   ? 0.6179 0.4478 0.5289 0.0151  -0.1569 -0.0397 304 BCN A C3  
8546 C  C4  . BCN H .   ? 0.4065 0.2538 0.3707 -0.0361 -0.0934 -0.1439 304 BCN A C4  
8547 O  O4  . BCN H .   ? 0.5565 0.4185 0.7390 0.1506  0.0586  -0.0038 304 BCN A O4  
8548 C  C5  . BCN H .   ? 0.7167 0.5080 0.6148 -0.2314 0.0544  0.1331  304 BCN A C5  
8549 C  C6  . BCN H .   ? 0.5293 0.4799 0.5856 -0.0344 -0.1182 -0.0187 304 BCN A C6  
8550 O  O6  . BCN H .   ? 0.5884 0.3788 0.5688 -0.0421 0.0131  -0.0236 304 BCN A O6  
8551 ZN ZN  . ZN  I .   ? 0.0978 0.0930 0.0967 0.0082  0.0028  0.0008  301 ZN  B ZN  
8552 O  O16 . WWX J .   ? 0.2734 0.2777 0.4577 0.0529  -0.0261 -0.0700 302 WWX B O16 
8553 S  S14 . WWX J .   ? 0.2524 0.2608 0.3052 0.0102  -0.0177 0.0071  302 WWX B S14 
8554 O  O15 . WWX J .   ? 0.2951 0.2804 0.3215 -0.0141 -0.0193 0.0054  302 WWX B O15 
8555 C  C18 . WWX J .   ? 0.2725 0.3059 0.2700 0.0210  -0.0421 -0.0621 302 WWX B C18 
8556 O  O20 . WWX J .   ? 0.3695 0.3359 0.5442 0.0315  0.0460  -0.1022 302 WWX B O20 
8557 C  C17 . WWX J .   ? 0.2951 0.3720 0.2786 0.0027  -0.0105 0.0142  302 WWX B C17 
8558 C  C8  . WWX J .   ? 0.1905 0.2149 0.2560 0.0386  -0.0342 -0.0052 302 WWX B C8  
8559 C  C7  . WWX J .   ? 0.2432 0.2081 0.1556 0.0092  -0.0153 0.0261  302 WWX B C7  
8560 F  F12 . WWX J .   ? 0.2741 0.2283 0.3129 0.0535  -0.0619 -0.0082 302 WWX B F12 
8561 C  C6  . WWX J .   ? 0.1852 0.1389 0.1860 0.0177  0.0219  -0.0282 302 WWX B C6  
8562 F  F11 . WWX J .   ? 0.2432 0.1526 0.1755 -0.0020 0.0127  -0.0015 302 WWX B F11 
8563 C  C9  . WWX J .   ? 0.2035 0.1784 0.2236 0.0195  -0.0217 0.0098  302 WWX B C9  
8564 C  C10 . WWX J .   ? 0.1795 0.1572 0.2308 0.0078  0.0070  0.0040  302 WWX B C10 
8565 F  F13 . WWX J .   ? 0.2140 0.1895 0.2131 0.0487  0.0155  0.0305  302 WWX B F13 
8566 C  C5  . WWX J .   ? 0.1448 0.1565 0.1840 0.0298  0.0460  -0.0267 302 WWX B C5  
8567 S  S1  . WWX J .   ? 0.1298 0.1251 0.1590 0.0148  0.0324  0.0136  302 WWX B S1  
8568 O  O3  . WWX J .   ? 0.1684 0.1394 0.2581 0.0425  0.0917  0.0469  302 WWX B O3  
8569 N  N4  . WWX J .   ? 0.1436 0.1001 0.1527 0.0188  0.0513  0.0149  302 WWX B N4  
8570 O  O2  . WWX J .   ? 0.1513 0.1717 0.1682 0.0269  0.0057  0.0601  302 WWX B O2  
8571 N  N19 . WWX J .   ? 0.2093 0.1902 0.2310 0.0092  0.0005  0.0068  302 WWX B N19 
8572 C  C21 . WWX J .   ? 0.2854 0.1529 0.2257 -0.0104 0.0027  0.0195  302 WWX B C21 
8573 C  C30 . WWX J .   ? 0.1919 0.1509 0.1994 -0.0162 -0.0089 0.0010  302 WWX B C30 
8574 C  C35 . WWX J .   ? 0.2071 0.1646 0.2716 -0.0035 0.0245  -0.0071 302 WWX B C35 
8575 C  C34 . WWX J .   ? 0.2375 0.2694 0.2824 -0.0142 0.0328  0.0566  302 WWX B C34 
8576 C  C33 . WWX J .   ? 0.2222 0.2080 0.1861 -0.0238 0.0032  -0.0368 302 WWX B C33 
8577 C  C32 . WWX J .   ? 0.1928 0.2001 0.1921 0.0212  0.0023  -0.0225 302 WWX B C32 
8578 C  C31 . WWX J .   ? 0.2111 0.1632 0.2467 0.0055  -0.0148 -0.0037 302 WWX B C31 
8579 C  C22 . WWX J .   ? 0.2630 0.2102 0.2680 0.0471  0.0088  -0.0458 302 WWX B C22 
8580 O  O29 . WWX J .   ? 0.2377 0.2824 0.3109 0.0485  -0.0465 0.0003  302 WWX B O29 
8581 C  C23 . WWX J .   ? 0.2314 0.1998 0.2141 0.0153  0.0094  -0.0388 302 WWX B C23 
8582 C  C28 . WWX J .   ? 0.2005 0.2186 0.3048 0.0121  -0.0285 -0.0238 302 WWX B C28 
8583 C  C27 . WWX J .   ? 0.2894 0.2159 0.3652 0.0452  -0.0186 -0.0504 302 WWX B C27 
8584 C  C26 . WWX J .   ? 0.2813 0.2561 0.2953 0.0414  -0.0220 -0.0185 302 WWX B C26 
8585 C  C25 . WWX J .   ? 0.2930 0.2547 0.2520 0.0388  -0.0062 -0.0296 302 WWX B C25 
8586 C  C24 . WWX J .   ? 0.1872 0.2026 0.1874 -0.0186 -0.0070 -0.0174 302 WWX B C24 
8587 S  S   . DMS K .   ? 0.2890 0.3192 0.2527 0.0282  0.0219  -0.0103 303 DMS B S   
8588 O  O   . DMS K .   ? 0.4117 0.3190 0.3494 -0.0256 -0.0355 0.0646  303 DMS B O   
8589 C  C1  . DMS K .   ? 0.2060 0.2691 0.1949 0.0300  0.0003  0.0267  303 DMS B C1  
8590 C  C2  . DMS K .   ? 0.4517 0.3106 0.1341 0.0098  0.0502  -0.0174 303 DMS B C2  
8591 N  N1  . BCN L .   ? 0.3673 0.4410 0.4632 -0.0135 -0.0496 -0.0326 304 BCN B N1  
8592 C  C1  . BCN L .   ? 0.3571 0.4531 0.3296 0.0122  -0.0031 -0.0626 304 BCN B C1  
8593 C  C2  . BCN L .   ? 0.4807 0.5074 0.4395 -0.0816 0.0065  -0.0544 304 BCN B C2  
8594 O  O21 . BCN L .   ? 0.7763 0.5049 0.6585 -0.0306 0.0531  -0.1259 304 BCN B O21 
8595 O  O22 . BCN L .   ? 0.4212 0.4757 0.5475 -0.0275 0.0068  -0.1685 304 BCN B O22 
8596 C  C3  . BCN L .   ? 0.3693 0.2533 0.3064 -0.0151 -0.0467 -0.0485 304 BCN B C3  
8597 C  C4  . BCN L .   ? 0.4999 0.5317 0.4767 0.0487  -0.0277 0.1303  304 BCN B C4  
8598 O  O4  . BCN L .   ? 0.4449 0.3463 0.3016 -0.0153 0.0043  -0.0483 304 BCN B O4  
8599 C  C5  . BCN L .   ? 0.3334 0.2342 0.2969 -0.0485 -0.0348 -0.0936 304 BCN B C5  
8600 C  C6  . BCN L .   ? 0.4573 0.4545 0.4901 0.0582  -0.0943 -0.1597 304 BCN B C6  
8601 O  O6  . BCN L .   ? 0.7095 0.3752 0.6050 0.0289  -0.0776 0.0103  304 BCN B O6  
8602 ZN ZN  . ZN  M .   ? 0.0989 0.0942 0.0965 -0.0012 0.0000  0.0020  301 ZN  C ZN  
8603 O  O16 . WWX N .   ? 0.3152 0.3301 0.4185 -0.0421 -0.0248 0.0734  302 WWX C O16 
8604 S  S14 . WWX N .   ? 0.2481 0.2617 0.3104 0.0087  -0.0351 -0.0153 302 WWX C S14 
8605 O  O15 . WWX N .   ? 0.3418 0.2572 0.3370 0.0324  0.0035  -0.0467 302 WWX C O15 
8606 C  C18 . WWX N .   ? 0.3465 0.3481 0.2624 0.0220  0.0148  0.0340  302 WWX C C18 
8607 O  O20 . WWX N .   ? 0.3551 0.3339 0.5652 0.0252  -0.0012 0.0700  302 WWX C O20 
8608 C  C17 . WWX N .   ? 0.3221 0.4348 0.2967 0.0081  0.0120  0.0091  302 WWX C C17 
8609 C  C8  . WWX N .   ? 0.2044 0.2132 0.2581 0.0005  -0.0373 -0.0148 302 WWX C C8  
8610 C  C7  . WWX N .   ? 0.2066 0.2059 0.1428 0.0115  0.0147  -0.0199 302 WWX C C7  
8611 F  F12 . WWX N .   ? 0.2831 0.2255 0.2881 -0.0126 -0.0401 -0.0147 302 WWX C F12 
8612 C  C6  . WWX N .   ? 0.1845 0.1328 0.1777 -0.0012 0.0031  0.0118  302 WWX C C6  
8613 F  F11 . WWX N .   ? 0.2366 0.1432 0.1888 -0.0098 -0.0010 -0.0094 302 WWX C F11 
8614 C  C9  . WWX N .   ? 0.2275 0.1825 0.2545 -0.0104 -0.0115 -0.0197 302 WWX C C9  
8615 C  C10 . WWX N .   ? 0.2298 0.1869 0.2463 -0.0152 -0.0046 0.0057  302 WWX C C10 
8616 F  F13 . WWX N .   ? 0.2001 0.1757 0.2106 -0.0253 0.0184  -0.0284 302 WWX C F13 
8617 C  C5  . WWX N .   ? 0.1651 0.1755 0.1887 -0.0220 0.0185  0.0076  302 WWX C C5  
8618 S  S1  . WWX N .   ? 0.1249 0.1333 0.1632 -0.0105 0.0289  -0.0092 302 WWX C S1  
8619 O  O3  . WWX N .   ? 0.1656 0.1462 0.2393 -0.0162 0.0763  -0.0364 302 WWX C O3  
8620 N  N4  . WWX N .   ? 0.1520 0.1012 0.1815 -0.0357 0.0449  -0.0152 302 WWX C N4  
8621 O  O2  . WWX N .   ? 0.1405 0.1791 0.1653 -0.0017 0.0049  -0.0612 302 WWX C O2  
8622 N  N19 . WWX N .   ? 0.2109 0.1877 0.2405 0.0017  -0.0348 -0.0083 302 WWX C N19 
8623 C  C21 . WWX N .   ? 0.3030 0.1483 0.2596 0.0115  -0.0024 -0.0256 302 WWX C C21 
8624 C  C30 . WWX N .   ? 0.2282 0.1790 0.2098 -0.0060 -0.0098 0.0017  302 WWX C C30 
8625 C  C35 . WWX N .   ? 0.2669 0.1869 0.2375 0.0152  0.0087  -0.0120 302 WWX C C35 
8626 C  C34 . WWX N .   ? 0.2737 0.2190 0.2874 0.0526  0.0364  -0.0302 302 WWX C C34 
8627 C  C33 . WWX N .   ? 0.2290 0.2274 0.2247 0.0452  0.0017  0.0456  302 WWX C C33 
8628 C  C32 . WWX N .   ? 0.1743 0.1935 0.1974 0.0010  -0.0261 0.0188  302 WWX C C32 
8629 C  C31 . WWX N .   ? 0.2411 0.1777 0.2326 -0.0038 -0.0375 0.0310  302 WWX C C31 
8630 C  C22 . WWX N .   ? 0.2601 0.1992 0.2755 -0.0364 0.0093  0.0098  302 WWX C C22 
8631 O  O29 . WWX N .   ? 0.2524 0.2752 0.3036 0.0082  -0.0653 -0.0221 302 WWX C O29 
8632 C  C23 . WWX N .   ? 0.2660 0.1851 0.1980 -0.0114 -0.0027 0.0174  302 WWX C C23 
8633 C  C28 . WWX N .   ? 0.2275 0.2224 0.3319 0.0087  -0.0309 -0.0140 302 WWX C C28 
8634 C  C27 . WWX N .   ? 0.3355 0.2522 0.3438 0.0020  0.0496  0.0390  302 WWX C C27 
8635 C  C26 . WWX N .   ? 0.2745 0.2874 0.2091 -0.0463 -0.0300 0.0187  302 WWX C C26 
8636 C  C25 . WWX N .   ? 0.2433 0.2750 0.2678 -0.0245 -0.0065 0.0007  302 WWX C C25 
8637 C  C24 . WWX N .   ? 0.2529 0.2371 0.1915 0.0071  0.0077  0.0197  302 WWX C C24 
8638 S  S   . DMS O .   ? 0.3115 0.3377 0.2330 -0.0074 0.0263  0.0244  303 DMS C S   
8639 O  O   . DMS O .   ? 0.5315 0.3540 0.3005 -0.0098 -0.0460 -0.0873 303 DMS C O   
8640 C  C1  . DMS O .   ? 0.2513 0.2980 0.1669 -0.0685 -0.0298 -0.0148 303 DMS C C1  
8641 C  C2  . DMS O .   ? 0.5432 0.3176 0.2050 0.0278  0.1274  0.0728  303 DMS C C2  
8642 N  N1  . BCN P .   ? 0.3932 0.4918 0.4333 -0.0828 0.0097  0.0469  304 BCN C N1  
8643 C  C1  . BCN P .   ? 0.3452 0.4866 0.3801 -0.0281 0.0816  0.0881  304 BCN C C1  
8644 C  C2  . BCN P .   ? 0.5346 0.4539 0.5927 0.0903  0.0983  0.0606  304 BCN C C2  
8645 O  O21 . BCN P .   ? 0.4334 0.4230 0.7653 -0.0493 0.0324  0.1780  304 BCN C O21 
8646 O  O22 . BCN P .   ? 0.4201 0.5705 0.7267 -0.0091 -0.0205 0.1570  304 BCN C O22 
8647 C  C3  . BCN P .   ? 0.4247 0.2711 0.2930 -0.0270 -0.0425 0.0888  304 BCN C C3  
8648 C  C4  . BCN P .   ? 0.4776 0.5333 0.5006 -0.0599 -0.0540 -0.0945 304 BCN C C4  
8649 O  O4  . BCN P .   ? 0.5113 0.3289 0.3120 -0.0386 0.0008  0.0980  304 BCN C O4  
8650 C  C5  . BCN P .   ? 0.3429 0.2081 0.3474 -0.0080 0.0032  0.1133  304 BCN C C5  
8651 C  C6  . BCN P .   ? 0.5076 0.3352 0.4595 -0.1361 0.0329  0.0724  304 BCN C C6  
8652 O  O6  . BCN P .   ? 0.6820 0.6504 0.6672 0.0856  0.1899  0.2590  304 BCN C O6  
8653 ZN ZN  . ZN  Q .   ? 0.1107 0.1021 0.1080 -0.0057 -0.0020 0.0044  301 ZN  D ZN  
8654 O  O16 . WWX R .   ? 0.3321 0.3364 0.3856 -0.0768 -0.0076 0.0671  302 WWX D O16 
8655 S  S14 . WWX R .   ? 0.2585 0.2994 0.2838 -0.0198 -0.0242 -0.0248 302 WWX D S14 
8656 O  O15 . WWX R .   ? 0.3190 0.3025 0.4176 -0.0292 -0.0421 -0.0559 302 WWX D O15 
8657 C  C18 . WWX R .   ? 0.3106 0.2982 0.2953 0.0680  -0.0575 0.0767  302 WWX D C18 
8658 O  O20 . WWX R .   ? 0.6098 0.3319 0.6042 -0.0882 0.0515  0.1097  302 WWX D O20 
8659 C  C17 . WWX R .   ? 0.3359 0.4244 0.2224 -0.0116 0.0357  -0.0149 302 WWX D C17 
8660 C  C8  . WWX R .   ? 0.2213 0.2389 0.2035 -0.0337 -0.0368 -0.0046 302 WWX D C8  
8661 C  C7  . WWX R .   ? 0.2775 0.2357 0.1939 -0.0115 -0.0057 -0.0333 302 WWX D C7  
8662 F  F12 . WWX R .   ? 0.3156 0.2351 0.2913 -0.0346 -0.0533 -0.0093 302 WWX D F12 
8663 C  C6  . WWX R .   ? 0.2274 0.1632 0.1780 0.0063  0.0284  0.0329  302 WWX D C6  
8664 F  F11 . WWX R .   ? 0.2477 0.1764 0.2272 -0.0233 0.0229  -0.0124 302 WWX D F11 
8665 C  C9  . WWX R .   ? 0.2542 0.1953 0.3021 -0.0458 -0.0137 -0.0179 302 WWX D C9  
8666 C  C10 . WWX R .   ? 0.1946 0.2052 0.2669 -0.0278 0.0104  0.0046  302 WWX D C10 
8667 F  F13 . WWX R .   ? 0.2460 0.1757 0.2585 -0.0502 0.0171  -0.0282 302 WWX D F13 
8668 C  C5  . WWX R .   ? 0.1802 0.2010 0.1960 -0.0212 0.0329  0.0220  302 WWX D C5  
8669 S  S1  . WWX R .   ? 0.1631 0.1389 0.2041 -0.0175 0.0392  -0.0037 302 WWX D S1  
8670 O  O3  . WWX R .   ? 0.2030 0.1604 0.3192 -0.0328 0.0768  -0.0593 302 WWX D O3  
8671 N  N4  . WWX R .   ? 0.1459 0.1019 0.1457 -0.0381 0.0447  -0.0085 302 WWX D N4  
8672 O  O2  . WWX R .   ? 0.1581 0.1851 0.2073 -0.0126 0.0030  -0.0568 302 WWX D O2  
8673 N  N19 . WWX R .   ? 0.2201 0.2205 0.2590 -0.0189 -0.0364 -0.0194 302 WWX D N19 
8674 C  C21 . WWX R .   ? 0.3368 0.2177 0.2793 -0.0269 -0.0085 -0.0087 302 WWX D C21 
8675 C  C30 . WWX R .   ? 0.2021 0.1759 0.2269 0.0253  -0.0384 0.0428  302 WWX D C30 
8676 C  C35 . WWX R .   ? 0.2461 0.2266 0.2460 0.0412  0.0192  -0.0129 302 WWX D C35 
8677 C  C34 . WWX R .   ? 0.2703 0.2696 0.2360 0.0311  -0.0175 -0.0412 302 WWX D C34 
8678 C  C33 . WWX R .   ? 0.2533 0.2118 0.2723 0.0315  -0.0346 -0.0212 302 WWX D C33 
8679 C  C32 . WWX R .   ? 0.2339 0.2433 0.2032 -0.0006 -0.0584 0.0557  302 WWX D C32 
8680 C  C31 . WWX R .   ? 0.2373 0.1998 0.2833 0.0060  -0.0788 0.0140  302 WWX D C31 
8681 C  C22 . WWX R .   ? 0.3379 0.1905 0.3359 -0.0623 -0.0362 0.0048  302 WWX D C22 
8682 O  O29 . WWX R .   ? 0.2741 0.2897 0.3336 -0.0177 -0.0546 0.0092  302 WWX D O29 
8683 C  C23 . WWX R .   ? 0.2910 0.2122 0.2343 -0.0184 -0.0216 0.0595  302 WWX D C23 
8684 C  C28 . WWX R .   ? 0.2825 0.2407 0.3709 -0.0164 -0.0432 0.0137  302 WWX D C28 
8685 C  C27 . WWX R .   ? 0.2962 0.2206 0.2836 -0.0024 -0.0151 0.0091  302 WWX D C27 
8686 C  C26 . WWX R .   ? 0.2969 0.3131 0.2619 0.0644  -0.0401 0.0136  302 WWX D C26 
8687 C  C25 . WWX R .   ? 0.2716 0.2725 0.2935 -0.0159 0.0434  0.0320  302 WWX D C25 
8688 C  C24 . WWX R .   ? 0.3206 0.2572 0.1818 -0.0081 0.0046  0.0303  302 WWX D C24 
8689 S  S   . DMS S .   ? 0.3127 0.3194 0.2522 -0.0131 0.0024  0.0038  303 DMS D S   
8690 O  O   . DMS S .   ? 0.5005 0.3738 0.2296 -0.0710 -0.0467 -0.0841 303 DMS D O   
8691 C  C1  . DMS S .   ? 0.2391 0.2790 0.2366 -0.0006 -0.0326 -0.0286 303 DMS D C1  
8692 C  C2  . DMS S .   ? 0.4171 0.3361 0.2319 -0.0296 0.0234  0.0509  303 DMS D C2  
8693 N  N1  . BCN T .   ? 0.4593 0.7113 0.5167 -0.0046 -0.0255 -0.1075 304 BCN D N1  
8694 C  C1  . BCN T .   ? 0.4255 0.6524 0.3950 0.0003  0.0337  -0.0048 304 BCN D C1  
8695 C  C2  . BCN T .   ? 0.5475 1.2086 0.8499 0.2802  0.0261  0.1138  304 BCN D C2  
8696 O  O21 . BCN T .   ? 0.8945 1.3402 1.0171 0.2750  -0.1030 0.4135  304 BCN D O21 
8697 O  O22 . BCN T .   ? 0.4251 0.5850 0.6068 0.0057  -0.0165 0.1226  304 BCN D O22 
8698 C  C3  . BCN T .   ? 0.4243 0.3452 0.3856 0.0996  -0.0240 0.1115  304 BCN D C3  
8699 C  C4  . BCN T .   ? 0.5397 0.5343 0.6970 -0.0947 -0.1756 -0.0502 304 BCN D C4  
8700 O  O4  . BCN T .   ? 0.5857 0.3555 0.4330 -0.0599 -0.0203 -0.0272 304 BCN D O4  
8701 C  C5  . BCN T .   ? 0.3465 0.2879 0.3452 0.0271  -0.0723 0.1259  304 BCN D C5  
8702 C  C6  . BCN T .   ? 0.4879 0.4848 0.7059 -0.1460 0.0006  0.0120  304 BCN D C6  
8703 O  O6  . BCN T .   ? 0.6644 0.5385 0.8751 0.0176  -0.1737 0.1465  304 BCN D O6  
8704 O  O   . HOH U .   ? 0.1256 0.1272 0.0976 0.0164  -0.0010 -0.0060 401 HOH A O   
8705 O  O   . HOH U .   ? 0.1939 0.2080 0.2099 0.0017  0.0188  -0.0078 402 HOH A O   
8706 O  O   . HOH U .   ? 0.2490 0.2226 0.2017 -0.0881 -0.0395 -0.0125 403 HOH A O   
8707 O  O   . HOH U .   ? 0.2576 0.1490 0.1935 0.0013  -0.0131 -0.0200 404 HOH A O   
8708 O  O   . HOH U .   ? 0.1545 0.1224 0.1127 0.0141  -0.0024 -0.0030 405 HOH A O   
8709 O  O   . HOH U .   ? 0.1202 0.1301 0.1360 0.0140  0.0086  0.0153  406 HOH A O   
8710 O  O   . HOH U .   ? 0.1641 0.1568 0.1493 -0.0108 0.0236  0.0136  407 HOH A O   
8711 O  O   . HOH U .   ? 0.1944 0.1811 0.1262 0.0233  0.0496  0.0132  408 HOH A O   
8712 O  O   . HOH U .   ? 0.2142 0.1604 0.2615 0.0137  -0.0174 -0.0309 409 HOH A O   
8713 O  O   . HOH U .   ? 0.1409 0.1312 0.1480 0.0249  -0.0205 0.0057  410 HOH A O   
8714 O  O   . HOH U .   ? 0.1461 0.1457 0.1310 -0.0013 0.0063  0.0198  411 HOH A O   
8715 O  O   . HOH U .   ? 0.2610 0.2123 0.3203 0.0590  0.1266  0.0474  412 HOH A O   
8716 O  O   . HOH U .   ? 0.1436 0.1097 0.1650 0.0093  -0.0252 -0.0099 413 HOH A O   
8717 O  O   . HOH U .   ? 0.2023 0.2197 0.1102 0.0082  0.0141  0.0135  414 HOH A O   
8718 O  O   . HOH U .   ? 0.3736 0.4424 0.4016 -0.0546 0.1196  -0.0601 415 HOH A O   
8719 O  O   . HOH U .   ? 0.1941 0.2044 0.2019 -0.0201 0.0140  0.0311  416 HOH A O   
8720 O  O   . HOH U .   ? 0.1256 0.1764 0.1671 -0.0054 0.0212  0.0219  417 HOH A O   
8721 O  O   . HOH U .   ? 0.3380 0.1799 0.3515 -0.0082 0.0144  0.0658  418 HOH A O   
8722 O  O   . HOH U .   ? 0.1565 0.1313 0.1665 0.0113  0.0160  0.0121  419 HOH A O   
8723 O  O   . HOH U .   ? 0.2420 0.1831 0.1592 -0.0060 0.0168  -0.0122 420 HOH A O   
8724 O  O   . HOH U .   ? 0.2576 0.1921 0.3894 0.0996  -0.0368 0.0023  421 HOH A O   
8725 O  O   . HOH U .   ? 0.2490 0.2425 0.2664 -0.0206 -0.0540 -0.0540 422 HOH A O   
8726 O  O   . HOH U .   ? 0.2231 0.1377 0.2567 0.0232  -0.0197 0.0329  423 HOH A O   
8727 O  O   . HOH U .   ? 0.3555 0.2770 0.2457 -0.0317 0.0350  0.0675  424 HOH A O   
8728 O  O   . HOH U .   ? 0.1748 0.2176 0.1583 -0.0019 0.0388  0.0125  425 HOH A O   
8729 O  O   . HOH U .   ? 0.1940 0.1680 0.2463 0.0132  0.0144  -0.0196 426 HOH A O   
8730 O  O   . HOH U .   ? 0.1998 0.1811 0.1888 0.0102  0.0082  0.0262  427 HOH A O   
8731 O  O   . HOH U .   ? 0.3722 0.4499 0.2152 0.0693  0.0335  -0.0322 428 HOH A O   
8732 O  O   . HOH U .   ? 0.2556 0.2389 0.2745 -0.0408 0.0582  0.0335  429 HOH A O   
8733 O  O   . HOH U .   ? 0.3564 0.2118 0.2763 -0.0259 0.0671  0.0859  430 HOH A O   
8734 O  O   . HOH U .   ? 0.2213 0.1453 0.3280 -0.0065 0.0162  0.0005  431 HOH A O   
8735 O  O   . HOH U .   ? 0.2020 0.2249 0.2808 0.0085  0.0057  0.0157  432 HOH A O   
8736 O  O   . HOH U .   ? 0.2425 0.2847 0.2445 0.0048  0.0886  0.0612  433 HOH A O   
8737 O  O   . HOH U .   ? 0.1973 0.2784 0.3280 0.0000  -0.0781 0.0137  434 HOH A O   
8738 O  O   . HOH U .   ? 0.1809 0.1428 0.2242 0.0218  -0.0046 -0.0245 435 HOH A O   
8739 O  O   . HOH U .   ? 0.2034 0.2030 0.1813 0.0239  -0.0582 0.0233  436 HOH A O   
8740 O  O   . HOH U .   ? 0.1960 0.2345 0.2114 -0.0287 -0.0192 0.0003  437 HOH A O   
8741 O  O   . HOH U .   ? 0.3521 0.2646 0.4747 -0.0110 -0.1477 -0.0384 438 HOH A O   
8742 O  O   . HOH U .   ? 0.3386 0.2373 0.3012 0.0513  -0.0187 -0.0284 439 HOH A O   
8743 O  O   . HOH U .   ? 0.4494 0.2953 0.2964 -0.1121 -0.0364 -0.1006 440 HOH A O   
8744 O  O   . HOH U .   ? 0.2878 0.2707 0.3449 0.0799  -0.0197 -0.0653 441 HOH A O   
8745 O  O   . HOH U .   ? 0.2808 0.2441 0.2493 -0.0401 -0.0040 -0.0103 442 HOH A O   
8746 O  O   . HOH U .   ? 0.2816 0.3072 0.2745 0.0059  -0.0564 -0.0410 443 HOH A O   
8747 O  O   . HOH U .   ? 0.1689 0.1773 0.2429 -0.0357 0.0108  -0.0113 444 HOH A O   
8748 O  O   . HOH U .   ? 0.3395 0.2910 0.4595 -0.0564 -0.0147 -0.0225 445 HOH A O   
8749 O  O   . HOH U .   ? 0.3822 0.1987 0.3068 -0.0467 -0.0445 0.0489  446 HOH A O   
8750 O  O   . HOH U .   ? 0.1457 0.4878 0.3788 -0.0012 0.0364  -0.1174 447 HOH A O   
8751 O  O   . HOH U .   ? 0.4826 0.3619 0.3565 -0.0851 0.1067  0.1282  448 HOH A O   
8752 O  O   . HOH U .   ? 0.2060 0.2748 0.3316 0.0487  -0.0286 -0.0252 449 HOH A O   
8753 O  O   . HOH U .   ? 0.2290 0.2387 0.3515 0.0115  -0.0285 -0.0555 450 HOH A O   
8754 O  O   . HOH U .   ? 0.5443 0.3023 0.3445 -0.0912 -0.0176 -0.0612 451 HOH A O   
8755 O  O   . HOH U .   ? 0.2057 0.2105 0.2502 -0.0305 -0.0164 0.0071  452 HOH A O   
8756 O  O   . HOH U .   ? 0.4672 0.2922 0.3853 -0.0105 0.0737  -0.0093 453 HOH A O   
8757 O  O   . HOH U .   ? 0.1895 0.2260 0.2768 -0.0088 0.0333  -0.0098 454 HOH A O   
8758 O  O   . HOH U .   ? 0.2145 0.2969 0.2030 0.0518  -0.0120 0.0244  455 HOH A O   
8759 O  O   . HOH U .   ? 0.1709 0.1793 0.2140 0.0188  -0.0485 0.0063  456 HOH A O   
8760 O  O   . HOH U .   ? 0.3165 0.2432 0.3052 0.0259  -0.0460 0.0105  457 HOH A O   
8761 O  O   . HOH U .   ? 0.2935 0.3526 0.3650 0.0896  0.0038  -0.0485 458 HOH A O   
8762 O  O   . HOH U .   ? 0.1958 0.1770 0.2370 -0.0164 0.0077  -0.0151 459 HOH A O   
8763 O  O   . HOH U .   ? 0.4724 0.2788 0.2806 -0.1098 -0.1259 0.0436  460 HOH A O   
8764 O  O   . HOH U .   ? 0.2676 0.3165 0.1948 0.0286  0.0242  -0.0447 461 HOH A O   
8765 O  O   . HOH U .   ? 0.2811 0.2723 0.2782 0.0480  0.0568  0.0225  462 HOH A O   
8766 O  O   . HOH U .   ? 0.3102 0.1615 0.2779 0.0074  0.0035  0.0120  463 HOH A O   
8767 O  O   . HOH U .   ? 0.2797 0.5993 0.4825 -0.0355 -0.1794 -0.0887 464 HOH A O   
8768 O  O   . HOH U .   ? 0.2721 0.2283 0.3339 0.0136  0.0019  -0.0392 465 HOH A O   
8769 O  O   . HOH U .   ? 0.2556 0.1935 0.3249 -0.0215 0.0392  -0.0231 466 HOH A O   
8770 O  O   . HOH U .   ? 0.2379 0.5097 0.4783 0.0013  0.0251  -0.1149 467 HOH A O   
8771 O  O   . HOH U .   ? 0.3003 0.3697 0.2942 0.0174  0.0417  -0.0856 468 HOH A O   
8772 O  O   . HOH U .   ? 0.2712 0.2429 0.2678 -0.0272 -0.0357 0.0206  469 HOH A O   
8773 O  O   . HOH U .   ? 0.2220 0.2156 0.3106 0.0678  -0.0465 -0.0227 470 HOH A O   
8774 O  O   . HOH U .   ? 0.2813 0.2309 0.1464 0.0041  0.0684  -0.0007 471 HOH A O   
8775 O  O   . HOH U .   ? 0.3776 0.4273 0.2438 -0.0759 0.0482  0.0057  472 HOH A O   
8776 O  O   . HOH U .   ? 0.4059 0.6973 0.4172 -0.2594 -0.1208 0.1816  473 HOH A O   
8777 O  O   . HOH U .   ? 0.3765 0.3486 0.2400 0.0000  0.1027  -0.0315 474 HOH A O   
8778 O  O   . HOH U .   ? 0.5623 0.4675 0.3472 -0.0126 -0.0198 -0.0628 475 HOH A O   
8779 O  O   . HOH U .   ? 0.1904 0.1716 0.2768 0.0012  -0.0115 0.0071  476 HOH A O   
8780 O  O   . HOH U .   ? 0.2490 0.2248 0.2115 0.0223  0.0089  -0.0065 477 HOH A O   
8781 O  O   . HOH U .   ? 0.3704 0.3458 0.2755 -0.0621 0.0326  0.0074  478 HOH A O   
8782 O  O   . HOH U .   ? 0.3030 0.3131 0.3025 -0.0659 -0.1032 -0.0229 479 HOH A O   
8783 O  O   . HOH U .   ? 0.3671 0.3285 0.2179 -0.0137 0.0465  0.0612  480 HOH A O   
8784 O  O   . HOH U .   ? 0.2718 0.2140 0.3242 0.0277  0.0131  -0.0037 481 HOH A O   
8785 O  O   . HOH U .   ? 0.2350 0.1953 0.2824 0.0234  -0.0313 -0.0281 482 HOH A O   
8786 O  O   . HOH U .   ? 0.3519 0.2454 0.3300 0.1282  0.0683  -0.1041 483 HOH A O   
8787 O  O   . HOH U .   ? 0.2239 0.2962 0.2940 0.0333  0.0005  -0.0288 484 HOH A O   
8788 O  O   . HOH U .   ? 0.2117 0.1888 0.2240 0.0309  -0.0105 0.0013  485 HOH A O   
8789 O  O   . HOH U .   ? 0.3332 0.1980 0.3583 0.0247  -0.0083 -0.0189 486 HOH A O   
8790 O  O   . HOH U .   ? 0.4753 0.4146 0.4081 0.0318  -0.1297 0.0406  487 HOH A O   
8791 O  O   . HOH U .   ? 0.2946 0.2730 0.2655 0.0847  -0.1207 -0.0044 488 HOH A O   
8792 O  O   . HOH U .   ? 0.3210 0.3021 0.2806 0.0631  0.0238  0.0119  489 HOH A O   
8793 O  O   . HOH U .   ? 0.4702 0.4453 0.4647 0.1441  -0.0617 -0.0676 490 HOH A O   
8794 O  O   . HOH U .   ? 0.2052 0.2558 0.3046 0.0049  0.0062  0.0221  491 HOH A O   
8795 O  O   . HOH U .   ? 0.4406 0.2768 0.4000 0.0922  -0.1842 -0.0087 492 HOH A O   
8796 O  O   . HOH U .   ? 0.3271 0.2935 0.2036 0.0048  -0.0238 0.0324  493 HOH A O   
8797 O  O   . HOH U .   ? 0.3443 0.2219 0.2452 0.0085  0.1425  -0.0452 494 HOH A O   
8798 O  O   . HOH U .   ? 0.1838 0.2644 0.2263 0.0315  -0.0206 -0.0038 495 HOH A O   
8799 O  O   . HOH U .   ? 0.3068 0.2298 0.4133 0.0203  0.0355  0.0247  496 HOH A O   
8800 O  O   . HOH U .   ? 0.2231 0.2346 0.1915 0.0089  0.0362  0.0344  497 HOH A O   
8801 O  O   . HOH U .   ? 0.2621 0.4147 0.4445 -0.1277 0.0087  -0.0040 498 HOH A O   
8802 O  O   . HOH U .   ? 0.5569 0.4848 0.2221 -0.0211 -0.1592 -0.0822 499 HOH A O   
8803 O  O   . HOH U .   ? 0.2680 0.2606 0.1976 0.0833  -0.0238 0.0038  500 HOH A O   
8804 O  O   . HOH U .   ? 0.2257 0.1958 0.3946 -0.0114 -0.0197 -0.0076 501 HOH A O   
8805 O  O   . HOH U .   ? 0.4578 0.3916 0.3452 -0.0742 -0.0065 0.0546  502 HOH A O   
8806 O  O   . HOH U .   ? 0.3152 0.3395 0.3661 0.0124  0.0076  -0.0092 503 HOH A O   
8807 O  O   . HOH U .   ? 0.2994 0.2057 0.3732 -0.0157 -0.0531 0.0199  504 HOH A O   
8808 O  O   . HOH U .   ? 0.3097 0.2479 0.2973 0.0417  0.0074  -0.0265 505 HOH A O   
8809 O  O   . HOH U .   ? 0.2628 0.3675 0.2581 -0.0166 -0.0640 0.0300  506 HOH A O   
8810 O  O   . HOH U .   ? 0.3208 0.2694 0.1719 -0.0531 -0.0026 0.0348  507 HOH A O   
8811 O  O   . HOH U .   ? 0.2359 0.2407 0.3472 -0.0876 -0.0184 -0.0456 508 HOH A O   
8812 O  O   . HOH U .   ? 0.1838 0.3903 0.2987 -0.0120 0.0162  0.0754  509 HOH A O   
8813 O  O   . HOH U .   ? 0.3515 0.3330 0.3510 -0.0666 -0.0026 -0.0454 510 HOH A O   
8814 O  O   . HOH U .   ? 0.3151 0.2614 0.3339 -0.0606 0.0120  0.0436  511 HOH A O   
8815 O  O   . HOH U .   ? 0.4189 0.1671 0.2248 0.0156  -0.0157 0.0087  512 HOH A O   
8816 O  O   . HOH U .   ? 0.2324 0.2458 0.2599 0.0125  -0.0335 0.0172  513 HOH A O   
8817 O  O   . HOH U .   ? 0.2888 0.3136 0.2515 0.1146  -0.0570 -0.0661 514 HOH A O   
8818 O  O   . HOH U .   ? 0.3328 0.3467 0.2323 0.0794  -0.0546 -0.0687 515 HOH A O   
8819 O  O   . HOH U .   ? 0.3368 0.2310 0.3316 0.0507  -0.0166 -0.0031 516 HOH A O   
8820 O  O   . HOH U .   ? 0.2996 0.3104 0.3134 0.1216  -0.0274 -0.0122 517 HOH A O   
8821 O  O   . HOH U .   ? 0.3276 0.3206 0.4463 -0.0456 -0.0698 -0.0579 518 HOH A O   
8822 O  O   . HOH U .   ? 0.3856 0.2500 0.2290 -0.0586 -0.0146 -0.0513 519 HOH A O   
8823 O  O   . HOH U .   ? 0.2299 0.2454 0.2971 -0.0038 0.0579  0.0755  520 HOH A O   
8824 O  O   . HOH U .   ? 0.2524 0.3068 0.2874 -0.0120 0.0377  -0.0630 521 HOH A O   
8825 O  O   . HOH U .   ? 0.5990 0.3041 0.3806 -0.1275 0.0460  0.0032  522 HOH A O   
8826 O  O   . HOH U .   ? 0.3605 0.3339 0.3323 0.0803  0.0571  -0.0241 523 HOH A O   
8827 O  O   . HOH U .   ? 0.2768 0.3291 0.3639 0.0037  0.0331  -0.0217 524 HOH A O   
8828 O  O   . HOH U .   ? 0.4552 0.3287 0.2213 -0.0750 -0.0099 -0.0154 525 HOH A O   
8829 O  O   . HOH U .   ? 0.5584 0.5899 0.2811 -0.1624 0.0109  0.0712  526 HOH A O   
8830 O  O   . HOH U .   ? 0.4208 0.2678 0.3486 0.0507  -0.0091 0.0057  527 HOH A O   
8831 O  O   . HOH U .   ? 0.3714 0.4528 0.4323 -0.0020 0.0577  0.0653  528 HOH A O   
8832 O  O   . HOH U .   ? 0.3959 0.3140 0.3562 0.0793  -0.1898 0.0066  529 HOH A O   
8833 O  O   . HOH U .   ? 0.3542 0.2463 0.4236 0.0280  0.0010  0.0137  530 HOH A O   
8834 O  O   . HOH U .   ? 0.2940 0.2177 0.3632 -0.0408 0.0702  -0.0208 531 HOH A O   
8835 O  O   . HOH U .   ? 0.2459 0.3377 0.5378 0.0873  -0.0046 -0.0702 532 HOH A O   
8836 O  O   . HOH U .   ? 0.3359 0.3896 0.1468 0.0441  -0.0195 -0.0170 533 HOH A O   
8837 O  O   . HOH U .   ? 0.4814 0.4923 0.4872 0.0092  0.0636  0.0869  534 HOH A O   
8838 O  O   . HOH U .   ? 0.3393 0.5314 0.2538 -0.0238 0.0873  0.0320  535 HOH A O   
8839 O  O   . HOH U .   ? 0.5637 0.3073 0.4283 -0.1027 0.0386  -0.1181 536 HOH A O   
8840 O  O   . HOH U .   ? 0.3052 0.3634 0.4724 0.0657  -0.0282 0.1534  537 HOH A O   
8841 O  O   . HOH U .   ? 0.3276 0.2951 0.3422 0.1499  0.0516  0.0958  538 HOH A O   
8842 O  O   . HOH U .   ? 0.2583 0.2257 0.4248 0.0278  -0.0227 0.0104  539 HOH A O   
8843 O  O   . HOH U .   ? 0.5137 0.3533 0.2416 0.0895  0.0612  -0.0498 540 HOH A O   
8844 O  O   . HOH U .   ? 0.3377 0.3898 0.4647 -0.1432 -0.2274 0.0962  541 HOH A O   
8845 O  O   . HOH U .   ? 0.4345 0.4356 0.3253 -0.0013 0.0296  -0.0355 542 HOH A O   
8846 O  O   . HOH U .   ? 0.5192 0.2628 0.2280 -0.0269 -0.0917 0.0051  543 HOH A O   
8847 O  O   . HOH U .   ? 0.3569 0.5792 0.3795 0.0241  0.0882  -0.0266 544 HOH A O   
8848 O  O   . HOH U .   ? 0.5921 0.3885 0.5478 0.0151  -0.0282 -0.0625 545 HOH A O   
8849 O  O   . HOH U .   ? 0.3134 0.3362 0.3716 -0.0199 -0.0688 -0.0293 546 HOH A O   
8850 O  O   . HOH U .   ? 0.5665 0.5670 0.2962 -0.0965 0.0309  -0.1957 547 HOH A O   
8851 O  O   . HOH U .   ? 0.2608 0.4222 0.4379 0.0379  -0.0276 -0.0208 548 HOH A O   
8852 O  O   . HOH U .   ? 0.3007 0.4022 0.2068 0.0269  0.0181  0.0003  549 HOH A O   
8853 O  O   . HOH U .   ? 0.2822 0.2314 0.4516 0.0460  0.0538  0.1275  550 HOH A O   
8854 O  O   . HOH U .   ? 0.2431 0.3700 0.4541 -0.0251 0.0586  -0.0938 551 HOH A O   
8855 O  O   . HOH U .   ? 0.3765 0.4513 0.4005 -0.0584 0.0767  -0.0513 552 HOH A O   
8856 O  O   . HOH U .   ? 0.3483 0.3167 0.2653 0.0182  -0.0414 0.0357  553 HOH A O   
8857 O  O   . HOH U .   ? 0.4624 0.3795 0.3948 0.0114  0.0515  -0.1150 554 HOH A O   
8858 O  O   . HOH U .   ? 0.2673 0.2775 0.4212 0.0110  0.1533  0.0335  555 HOH A O   
8859 O  O   . HOH U .   ? 0.3804 0.4564 0.3989 -0.2207 0.0289  -0.0164 556 HOH A O   
8860 O  O   . HOH U .   ? 0.5602 0.3878 0.3662 0.0747  -0.0080 0.0086  557 HOH A O   
8861 O  O   . HOH U .   ? 0.3407 0.4484 0.5576 0.0467  0.1562  -0.1416 558 HOH A O   
8862 O  O   . HOH U .   ? 0.3713 0.4789 0.3883 -0.2052 -0.1033 0.1647  559 HOH A O   
8863 O  O   . HOH U .   ? 0.3585 0.4722 0.2772 -0.0935 0.1805  -0.1005 560 HOH A O   
8864 O  O   . HOH U .   ? 0.4661 0.4214 0.4309 0.1583  0.0640  -0.0118 561 HOH A O   
8865 O  O   . HOH U .   ? 0.4417 0.3808 0.4733 0.1133  -0.0315 0.0035  562 HOH A O   
8866 O  O   . HOH U .   ? 0.5123 0.6284 0.6335 -0.0052 0.1433  -0.0099 563 HOH A O   
8867 O  O   . HOH U .   ? 0.4002 0.3179 0.2628 -0.0326 0.0142  0.0174  564 HOH A O   
8868 O  O   . HOH U .   ? 0.4962 0.5781 0.2851 -0.1585 -0.0329 -0.1765 565 HOH A O   
8869 O  O   . HOH U .   ? 0.2899 0.3763 0.3741 -0.0843 -0.0234 0.1762  566 HOH A O   
8870 O  O   . HOH U .   ? 0.4289 0.4452 0.3625 -0.1465 -0.1430 0.1858  567 HOH A O   
8871 O  O   . HOH U .   ? 0.8356 0.3134 0.5375 -0.0974 0.0791  0.0281  568 HOH A O   
8872 O  O   . HOH U .   ? 0.5059 0.6209 0.2021 -0.0588 0.1072  -0.1699 569 HOH A O   
8873 O  O   . HOH U .   ? 0.4061 0.6485 0.3770 0.1685  0.0012  -0.0458 570 HOH A O   
8874 O  O   . HOH U .   ? 0.4999 0.4549 0.5875 0.0663  0.1432  0.0958  571 HOH A O   
8875 O  O   . HOH U .   ? 0.3817 0.5037 0.3330 -0.0887 0.0992  -0.0388 572 HOH A O   
8876 O  O   . HOH U .   ? 0.3668 0.3914 0.3650 0.0152  -0.0287 0.0048  573 HOH A O   
8877 O  O   . HOH U .   ? 0.4025 0.4970 0.4817 -0.0274 0.0500  -0.1164 574 HOH A O   
8878 O  O   . HOH U .   ? 0.5766 0.6577 0.3052 0.0120  -0.0595 -0.0954 575 HOH A O   
8879 O  O   . HOH U .   ? 0.2064 0.3269 0.3833 0.0282  0.0318  -0.0698 576 HOH A O   
8880 O  O   . HOH U .   ? 0.4711 0.3662 0.2806 -0.0526 -0.0471 -0.0685 577 HOH A O   
8881 O  O   . HOH U .   ? 0.5435 0.2869 0.2675 -0.0008 0.0447  -0.0542 578 HOH A O   
8882 O  O   . HOH U .   ? 0.6061 0.5989 0.2703 0.1534  -0.0364 0.0412  579 HOH A O   
8883 O  O   . HOH U .   ? 0.4700 0.3079 0.3652 -0.0788 0.0034  0.1115  580 HOH A O   
8884 O  O   . HOH U .   ? 0.3350 0.4826 0.3404 -0.0153 -0.0135 0.0023  581 HOH A O   
8885 O  O   . HOH U .   ? 0.3274 0.3693 0.3332 -0.0136 0.0706  0.1076  582 HOH A O   
8886 O  O   . HOH U .   ? 0.4138 0.2912 0.4351 0.0866  -0.0188 0.0226  583 HOH A O   
8887 O  O   . HOH U .   ? 0.3763 0.4542 0.4478 -0.0130 0.0157  0.0496  584 HOH A O   
8888 O  O   . HOH U .   ? 0.5134 0.3273 0.4822 0.0921  0.1331  0.0070  585 HOH A O   
8889 O  O   . HOH U .   ? 0.4473 0.5834 0.3334 -0.1772 -0.1281 0.0207  586 HOH A O   
8890 O  O   . HOH U .   ? 0.2845 0.4449 0.3283 -0.0852 0.1028  -0.0381 587 HOH A O   
8891 O  O   . HOH U .   ? 0.5322 0.3677 0.5480 0.0471  -0.0869 0.0608  588 HOH A O   
8892 O  O   . HOH U .   ? 0.4610 0.6035 0.4334 -0.1630 -0.0105 -0.0595 589 HOH A O   
8893 O  O   . HOH U .   ? 0.6718 0.4122 0.4372 0.1993  0.2000  0.0361  590 HOH A O   
8894 O  O   . HOH U .   ? 0.3671 0.3910 0.4077 -0.0931 -0.1040 -0.0966 591 HOH A O   
8895 O  O   . HOH U .   ? 0.3939 0.3339 0.2287 0.0375  0.0822  -0.0060 592 HOH A O   
8896 O  O   . HOH U .   ? 0.3727 0.3535 0.3431 -0.0643 -0.0085 -0.0478 593 HOH A O   
8897 O  O   . HOH U .   ? 0.3856 0.2838 0.5296 0.0509  -0.0806 -0.0048 594 HOH A O   
8898 O  O   . HOH U .   ? 0.4250 0.3806 0.3267 -0.1010 0.0222  0.0926  595 HOH A O   
8899 O  O   . HOH U .   ? 0.2944 0.4866 0.4740 -0.0086 0.0729  0.0252  596 HOH A O   
8900 O  O   . HOH U .   ? 0.8641 0.2301 0.2680 -0.1041 0.1164  -0.1168 597 HOH A O   
8901 O  O   . HOH U .   ? 0.4983 0.5432 0.2474 -0.0340 -0.0529 -0.0992 598 HOH A O   
8902 O  O   . HOH U .   ? 0.3407 0.3761 0.5863 -0.0308 0.0912  0.1342  599 HOH A O   
8903 O  O   . HOH U .   ? 0.4957 0.6176 0.4912 0.0164  0.1454  -0.0659 600 HOH A O   
8904 O  O   . HOH U .   ? 0.6051 0.2091 0.3327 -0.0348 0.0113  -0.0041 601 HOH A O   
8905 O  O   . HOH U .   ? 0.3312 0.5814 0.5597 -0.1098 -0.1083 0.1171  602 HOH A O   
8906 O  O   . HOH U .   ? 0.5131 0.2723 0.4208 -0.0331 -0.1045 0.0837  603 HOH A O   
8907 O  O   . HOH U .   ? 0.3204 0.4842 0.4207 0.0126  0.0231  0.0768  604 HOH A O   
8908 O  O   . HOH U .   ? 0.5018 0.3833 0.4862 0.0834  0.1755  -0.0487 605 HOH A O   
8909 O  O   . HOH U .   ? 0.5062 0.3986 0.4671 -0.0573 0.0582  -0.1167 606 HOH A O   
8910 O  O   . HOH U .   ? 0.5304 0.4611 0.4502 -0.1966 0.1032  0.0353  607 HOH A O   
8911 O  O   . HOH U .   ? 0.3208 0.3285 0.5789 -0.0771 -0.1062 -0.0346 608 HOH A O   
8912 O  O   . HOH U .   ? 0.5009 0.4447 0.5719 0.0137  0.0662  -0.2141 609 HOH A O   
8913 O  O   . HOH U .   ? 0.5370 0.5001 0.5041 -0.0001 0.1045  0.1581  610 HOH A O   
8914 O  O   . HOH U .   ? 0.4800 0.3576 0.3506 -0.1248 -0.0153 0.0315  611 HOH A O   
8915 O  O   . HOH U .   ? 0.3510 0.4390 0.3569 -0.0035 0.0599  0.0032  612 HOH A O   
8916 O  O   . HOH U .   ? 0.8561 0.4999 0.4517 0.0976  -0.0142 0.0657  613 HOH A O   
8917 O  O   . HOH U .   ? 0.3707 0.4930 0.6017 0.1768  0.2298  0.0294  614 HOH A O   
8918 O  O   . HOH U .   ? 0.3163 0.4925 0.5275 -0.1006 -0.0465 0.0175  615 HOH A O   
8919 O  O   . HOH U .   ? 0.4641 0.6061 0.4230 0.2440  -0.0366 -0.0621 616 HOH A O   
8920 O  O   . HOH U .   ? 0.5551 0.6585 0.5184 0.0531  -0.0511 -0.2926 617 HOH A O   
8921 O  O   . HOH U .   ? 0.4326 0.5820 0.4007 0.0447  -0.0315 0.1009  618 HOH A O   
8922 O  O   . HOH U .   ? 0.3122 0.3555 0.3398 0.0746  0.0076  0.0000  619 HOH A O   
8923 O  O   . HOH U .   ? 0.2698 0.2757 0.3143 -0.0848 -0.0518 0.0203  620 HOH A O   
8924 O  O   . HOH U .   ? 0.4417 0.3208 0.3307 -0.0372 0.0408  0.0653  621 HOH A O   
8925 O  O   . HOH U .   ? 0.2994 0.5141 0.8156 0.0769  -0.0982 -0.2694 622 HOH A O   
8926 O  O   . HOH U .   ? 0.3294 0.4045 0.2246 -0.0068 0.0342  0.0549  623 HOH A O   
8927 O  O   . HOH U .   ? 0.1766 0.4915 0.8159 0.0599  0.1324  -0.0144 624 HOH A O   
8928 O  O   . HOH U .   ? 0.3012 0.5163 0.2976 -0.1092 -0.0071 -0.0842 625 HOH A O   
8929 O  O   . HOH U .   ? 0.4646 0.5454 0.3075 0.0746  -0.0166 -0.1194 626 HOH A O   
8930 O  O   . HOH U .   ? 0.2272 0.5347 0.7343 -0.0640 -0.1084 0.0829  627 HOH A O   
8931 O  O   . HOH U .   ? 0.5142 0.4027 0.3838 0.1010  -0.1635 -0.0542 628 HOH A O   
8932 O  O   . HOH U .   ? 0.4334 0.2703 0.4672 -0.0044 0.1119  -0.0329 629 HOH A O   
8933 O  O   . HOH U .   ? 0.6549 1.0367 0.4058 0.1902  -0.0645 -0.1238 630 HOH A O   
8934 O  O   . HOH U .   ? 0.6072 0.4620 0.2797 0.0723  0.1066  0.0688  631 HOH A O   
8935 O  O   . HOH U .   ? 0.5094 0.4065 0.5371 0.1598  -0.2401 -0.1808 632 HOH A O   
8936 O  O   . HOH U .   ? 0.4587 0.4041 0.6183 0.0210  0.0361  0.0482  633 HOH A O   
8937 O  O   . HOH U .   ? 0.4835 0.2319 0.4570 0.0044  0.0109  -0.0051 634 HOH A O   
8938 O  O   . HOH U .   ? 0.4889 0.4907 0.4142 0.0690  -0.0575 -0.1014 635 HOH A O   
8939 O  O   . HOH U .   ? 0.5012 0.2712 0.5088 -0.0019 -0.0553 -0.0649 636 HOH A O   
8940 O  O   . HOH U .   ? 0.3021 0.3684 0.5015 0.0305  -0.0057 -0.0434 637 HOH A O   
8941 O  O   . HOH U .   ? 0.4146 0.3858 0.5981 -0.1063 0.0703  -0.0408 638 HOH A O   
8942 O  O   . HOH U .   ? 0.2996 0.2682 0.2565 -0.0265 -0.0071 0.0292  639 HOH A O   
8943 O  O   . HOH U .   ? 0.4535 0.4954 0.3741 0.0126  0.0644  -0.0315 640 HOH A O   
8944 O  O   . HOH U .   ? 0.2773 0.6007 0.3018 -0.0216 0.0265  0.0423  641 HOH A O   
8945 O  O   . HOH U .   ? 0.5461 0.6122 0.5773 0.0244  0.0777  -0.0703 642 HOH A O   
8946 O  O   . HOH U .   ? 0.4352 0.4787 0.7224 0.0573  -0.1013 0.0997  643 HOH A O   
8947 O  O   . HOH U .   ? 0.2445 0.2272 0.2998 0.0078  0.0074  0.0800  644 HOH A O   
8948 O  O   . HOH U .   ? 0.3262 0.2703 0.2046 0.0049  -0.0236 -0.0156 645 HOH A O   
8949 O  O   . HOH U .   ? 0.3287 0.4552 0.4512 -0.1932 -0.0949 0.0851  646 HOH A O   
8950 O  O   . HOH U .   ? 0.3723 0.4646 0.3300 0.0274  0.0076  0.1171  647 HOH A O   
8951 O  O   . HOH U .   ? 0.3996 0.4156 0.3005 0.0165  0.0659  0.0918  648 HOH A O   
8952 O  O   . HOH U .   ? 0.6733 0.6291 0.2953 -0.1781 0.1518  -0.1562 649 HOH A O   
8953 O  O   . HOH U .   ? 0.3409 0.4330 0.3398 0.0155  0.0000  0.0320  650 HOH A O   
8954 O  O   . HOH U .   ? 0.5440 0.2912 0.3264 0.0143  -0.0087 0.0644  651 HOH A O   
8955 O  O   . HOH U .   ? 0.3294 0.5313 0.2680 -0.0132 0.0210  -0.0533 652 HOH A O   
8956 O  O   . HOH V .   ? 0.1319 0.1238 0.0894 0.0027  -0.0088 0.0000  401 HOH B O   
8957 O  O   . HOH V .   ? 0.2053 0.1953 0.2457 -0.0274 0.0272  -0.0167 402 HOH B O   
8958 O  O   . HOH V .   ? 0.2314 0.2087 0.1999 -0.0810 -0.0533 -0.0309 403 HOH B O   
8959 O  O   . HOH V .   ? 0.2734 0.1529 0.1678 0.0073  -0.0167 -0.0062 404 HOH B O   
8960 O  O   . HOH V .   ? 0.1432 0.1115 0.1230 0.0120  -0.0114 -0.0092 405 HOH B O   
8961 O  O   . HOH V .   ? 0.1028 0.1186 0.1272 0.0102  0.0059  0.0103  406 HOH B O   
8962 O  O   . HOH V .   ? 0.1475 0.1529 0.1463 -0.0126 0.0209  0.0077  407 HOH B O   
8963 O  O   . HOH V .   ? 0.2029 0.1747 0.1292 0.0182  0.0472  0.0020  408 HOH B O   
8964 O  O   . HOH V .   ? 0.2165 0.1464 0.1859 0.0086  0.0243  -0.0414 409 HOH B O   
8965 O  O   . HOH V .   ? 0.1468 0.1265 0.1203 0.0071  -0.0037 -0.0028 410 HOH B O   
8966 O  O   . HOH V .   ? 0.1360 0.1303 0.1271 0.0001  0.0083  0.0162  411 HOH B O   
8967 O  O   . HOH V .   ? 0.1960 0.2404 0.3316 0.0013  0.1045  0.0299  412 HOH B O   
8968 O  O   . HOH V .   ? 0.1373 0.1150 0.1650 0.0015  -0.0377 -0.0083 413 HOH B O   
8969 O  O   . HOH V .   ? 0.1669 0.2075 0.1324 0.0219  0.0434  0.0185  414 HOH B O   
8970 O  O   . HOH V .   ? 0.5659 0.4093 0.4265 -0.0057 0.1639  -0.0372 415 HOH B O   
8971 O  O   . HOH V .   ? 0.2185 0.1932 0.1743 0.0027  0.0225  0.0230  416 HOH B O   
8972 O  O   . HOH V .   ? 0.1102 0.1574 0.1620 -0.0130 0.0212  -0.0013 417 HOH B O   
8973 O  O   . HOH V .   ? 0.3097 0.1795 0.3680 -0.0174 0.0438  0.0529  418 HOH B O   
8974 O  O   . HOH V .   ? 0.1387 0.1158 0.1554 -0.0007 0.0146  -0.0001 419 HOH B O   
8975 O  O   . HOH V .   ? 0.2134 0.1734 0.1360 -0.0041 0.0144  -0.0133 420 HOH B O   
8976 O  O   . HOH V .   ? 0.2382 0.1822 0.2673 0.0685  -0.0255 0.0041  421 HOH B O   
8977 O  O   . HOH V .   ? 0.2323 0.2330 0.1574 -0.0122 -0.0509 -0.0276 422 HOH B O   
8978 O  O   . HOH V .   ? 0.2175 0.1265 0.2522 0.0105  -0.0087 0.0236  423 HOH B O   
8979 O  O   . HOH V .   ? 0.3113 0.2405 0.2430 0.0065  -0.0076 0.0274  424 HOH B O   
8980 O  O   . HOH V .   ? 0.1374 0.2142 0.1699 -0.0255 0.0395  -0.0190 425 HOH B O   
8981 O  O   . HOH V .   ? 0.1947 0.1366 0.1782 0.0060  0.0227  -0.0054 426 HOH B O   
8982 O  O   . HOH V .   ? 0.1668 0.1734 0.1430 -0.0143 0.0006  0.0071  427 HOH B O   
8983 O  O   . HOH V .   ? 0.4283 0.4718 0.3343 0.1657  -0.0238 0.0458  428 HOH B O   
8984 O  O   . HOH V .   ? 0.2364 0.2441 0.2892 -0.0093 0.0384  0.0000  429 HOH B O   
8985 O  O   . HOH V .   ? 0.3052 0.2044 0.2698 -0.0229 0.0496  0.0729  430 HOH B O   
8986 O  O   . HOH V .   ? 0.1805 0.1495 0.2249 0.0052  0.0287  0.0162  431 HOH B O   
8987 O  O   . HOH V .   ? 0.2255 0.1921 0.1815 -0.0010 0.0131  0.0093  432 HOH B O   
8988 O  O   . HOH V .   ? 0.2739 0.3801 0.1642 -0.0126 0.0782  0.0445  433 HOH B O   
8989 O  O   . HOH V .   ? 0.1835 0.2425 0.3389 -0.0254 -0.0674 -0.0194 434 HOH B O   
8990 O  O   . HOH V .   ? 0.1716 0.1525 0.1508 0.0068  -0.0068 -0.0177 435 HOH B O   
8991 O  O   . HOH V .   ? 0.2608 0.2588 0.2125 0.0238  -0.0754 0.0293  436 HOH B O   
8992 O  O   . HOH V .   ? 0.1777 0.2199 0.2055 -0.0439 0.0320  -0.0054 437 HOH B O   
8993 O  O   . HOH V .   ? 0.2494 0.2673 0.4334 -0.0362 -0.0711 -0.0364 438 HOH B O   
8994 O  O   . HOH V .   ? 0.3014 0.2502 0.2793 0.0227  0.0307  -0.0208 439 HOH B O   
8995 O  O   . HOH V .   ? 0.3456 0.2451 0.1923 -0.0646 -0.0406 -0.0375 440 HOH B O   
8996 O  O   . HOH V .   ? 0.2364 0.2201 0.3012 0.0648  0.0211  -0.0544 441 HOH B O   
8997 O  O   . HOH V .   ? 0.2992 0.2412 0.2247 -0.0439 0.0289  0.0147  442 HOH B O   
8998 O  O   . HOH V .   ? 0.3813 0.3630 0.2813 0.0410  -0.0648 -0.0817 443 HOH B O   
8999 O  O   . HOH V .   ? 0.1578 0.1671 0.2619 -0.0187 0.0284  0.0196  444 HOH B O   
9000 O  O   . HOH V .   ? 0.4305 0.3023 0.4843 -0.0480 -0.0441 -0.0750 445 HOH B O   
9001 O  O   . HOH V .   ? 0.3499 0.2278 0.3452 -0.0960 -0.0340 0.0812  446 HOH B O   
9002 O  O   . HOH V .   ? 0.1411 0.4097 0.2831 0.0131  0.0130  -0.0724 447 HOH B O   
9003 O  O   . HOH V .   ? 0.3449 0.3104 0.3413 -0.0533 0.0879  0.0979  448 HOH B O   
9004 O  O   . HOH V .   ? 0.2231 0.2863 0.3301 0.0419  0.0443  -0.0711 449 HOH B O   
9005 O  O   . HOH V .   ? 0.4226 0.4501 0.5956 -0.1248 -0.0344 -0.0196 450 HOH B O   
9006 O  O   . HOH V .   ? 0.2509 0.1985 0.4369 0.0070  -0.0850 -0.0658 451 HOH B O   
9007 O  O   . HOH V .   ? 0.5665 0.4661 0.2666 -0.0294 0.0015  -0.0964 452 HOH B O   
9008 O  O   . HOH V .   ? 0.4340 0.5058 0.3319 0.1375  -0.2117 -0.0351 453 HOH B O   
9009 O  O   . HOH V .   ? 0.2263 0.2640 0.3325 -0.1005 -0.0216 0.0119  454 HOH B O   
9010 O  O   . HOH V .   ? 0.1905 0.2210 0.2124 -0.0078 0.0209  -0.0237 455 HOH B O   
9011 O  O   . HOH V .   ? 0.2361 0.3513 0.2782 0.0463  0.0006  0.0295  456 HOH B O   
9012 O  O   . HOH V .   ? 0.1389 0.1578 0.2019 0.0152  -0.0230 -0.0088 457 HOH B O   
9013 O  O   . HOH V .   ? 0.3163 0.2574 0.2125 0.0295  0.0080  0.0584  458 HOH B O   
9014 O  O   . HOH V .   ? 0.2743 0.3129 0.3063 0.0732  -0.0399 -0.0054 459 HOH B O   
9015 O  O   . HOH V .   ? 0.1896 0.1770 0.1902 -0.0182 0.0226  -0.0024 460 HOH B O   
9016 O  O   . HOH V .   ? 0.3246 0.2310 0.2332 -0.0771 -0.0322 -0.0116 461 HOH B O   
9017 O  O   . HOH V .   ? 0.4031 0.2721 0.3327 -0.0469 -0.0593 -0.0054 462 HOH B O   
9018 O  O   . HOH V .   ? 0.2736 0.2788 0.1702 0.0241  0.0491  -0.0280 463 HOH B O   
9019 O  O   . HOH V .   ? 0.4248 0.4664 0.4470 0.1463  0.0649  0.0837  464 HOH B O   
9020 O  O   . HOH V .   ? 0.2887 0.2485 0.2759 0.0410  0.0218  -0.0283 465 HOH B O   
9021 O  O   . HOH V .   ? 0.2707 0.1914 0.2072 0.0020  -0.0102 0.0177  466 HOH B O   
9022 O  O   . HOH V .   ? 0.4424 0.5892 0.4654 -0.0582 -0.1476 0.0035  467 HOH B O   
9023 O  O   . HOH V .   ? 0.1922 0.1978 0.2272 -0.0111 -0.0220 0.0121  468 HOH B O   
9024 O  O   . HOH V .   ? 0.1921 0.1990 0.2217 -0.0052 0.0275  -0.0165 469 HOH B O   
9025 O  O   . HOH V .   ? 0.3163 0.3867 0.2490 -0.0160 0.0232  -0.0581 470 HOH B O   
9026 O  O   . HOH V .   ? 0.2924 0.5231 0.5394 0.0087  0.0948  -0.0120 471 HOH B O   
9027 O  O   . HOH V .   ? 0.1935 0.2106 0.2675 -0.0020 -0.0295 0.0230  472 HOH B O   
9028 O  O   . HOH V .   ? 0.2267 0.2032 0.2730 0.0068  0.0000  0.0436  473 HOH B O   
9029 O  O   . HOH V .   ? 0.2698 0.1843 0.2060 0.0198  0.0599  0.0098  474 HOH B O   
9030 O  O   . HOH V .   ? 0.6294 0.4563 0.3635 -0.2214 -0.0992 0.0533  475 HOH B O   
9031 O  O   . HOH V .   ? 0.2791 0.2964 0.1860 0.0555  -0.0151 0.0172  476 HOH B O   
9032 O  O   . HOH V .   ? 0.3088 0.3612 0.1980 -0.0610 0.0961  -0.0142 477 HOH B O   
9033 O  O   . HOH V .   ? 0.4455 0.4005 0.3025 -0.0031 0.0228  -0.0469 478 HOH B O   
9034 O  O   . HOH V .   ? 0.2179 0.1642 0.2184 0.0115  0.0285  0.0063  479 HOH B O   
9035 O  O   . HOH V .   ? 0.2639 0.2102 0.2357 0.0017  -0.0472 0.0052  480 HOH B O   
9036 O  O   . HOH V .   ? 0.3265 0.2404 0.1856 -0.0357 0.0493  0.0359  481 HOH B O   
9037 O  O   . HOH V .   ? 0.4269 0.3558 0.2687 0.0200  0.1395  -0.0157 482 HOH B O   
9038 O  O   . HOH V .   ? 0.3531 0.4853 0.3082 -0.2269 -0.2073 -0.0287 483 HOH B O   
9039 O  O   . HOH V .   ? 0.2244 0.1937 0.2728 0.0211  0.0275  0.0055  484 HOH B O   
9040 O  O   . HOH V .   ? 0.3213 0.1981 0.2470 0.0295  0.0281  -0.0062 485 HOH B O   
9041 O  O   . HOH V .   ? 0.2502 0.1974 0.2655 0.0474  0.0617  -0.0500 486 HOH B O   
9042 O  O   . HOH V .   ? 0.4668 0.3684 0.5372 0.1102  0.1573  -0.0634 487 HOH B O   
9043 O  O   . HOH V .   ? 0.2922 0.2985 0.3298 0.0705  0.0161  0.0148  488 HOH B O   
9044 O  O   . HOH V .   ? 0.1647 0.1651 0.2007 0.0020  -0.0010 -0.0119 489 HOH B O   
9045 O  O   . HOH V .   ? 0.2784 0.1755 0.2278 0.0438  -0.0174 0.0146  490 HOH B O   
9046 O  O   . HOH V .   ? 0.4316 0.2908 0.4244 0.0505  0.0745  0.0013  491 HOH B O   
9047 O  O   . HOH V .   ? 0.2687 0.2527 0.2671 0.0782  -0.1507 -0.0280 492 HOH B O   
9048 O  O   . HOH V .   ? 0.3122 0.3037 0.1809 0.0258  -0.0107 0.0357  493 HOH B O   
9049 O  O   . HOH V .   ? 0.4120 0.4009 0.4290 0.0798  0.0249  0.0082  494 HOH B O   
9050 O  O   . HOH V .   ? 0.2077 0.2483 0.3075 0.0219  -0.0199 -0.0038 495 HOH B O   
9051 O  O   . HOH V .   ? 0.3152 0.3456 0.3165 0.0428  -0.0992 -0.0026 496 HOH B O   
9052 O  O   . HOH V .   ? 0.3434 0.2964 0.2443 -0.0031 0.0066  -0.0175 497 HOH B O   
9053 O  O   . HOH V .   ? 0.2617 0.1921 0.2188 0.0087  0.0962  -0.0425 498 HOH B O   
9054 O  O   . HOH V .   ? 0.1938 0.2583 0.2156 -0.0012 -0.0706 0.0277  499 HOH B O   
9055 O  O   . HOH V .   ? 0.2815 0.2066 0.3862 0.0342  0.0392  0.0604  500 HOH B O   
9056 O  O   . HOH V .   ? 0.4108 0.2400 0.3914 -0.0851 0.0230  -0.0820 501 HOH B O   
9057 O  O   . HOH V .   ? 0.3731 0.2994 0.2132 -0.0200 0.0209  0.0020  502 HOH B O   
9058 O  O   . HOH V .   ? 0.2384 0.3743 0.3637 -0.1371 0.0386  -0.0740 503 HOH B O   
9059 O  O   . HOH V .   ? 0.3517 0.2933 0.2538 -0.0659 -0.0754 0.0553  504 HOH B O   
9060 O  O   . HOH V .   ? 0.3948 0.3905 0.1750 -0.0026 -0.0355 -0.0024 505 HOH B O   
9061 O  O   . HOH V .   ? 0.2739 0.2842 0.2745 0.0832  -0.0351 0.0024  506 HOH B O   
9062 O  O   . HOH V .   ? 0.2036 0.1721 0.2651 0.0085  -0.0220 -0.0206 507 HOH B O   
9063 O  O   . HOH V .   ? 0.5110 0.3977 0.3892 -0.1174 -0.0006 0.0577  508 HOH B O   
9064 O  O   . HOH V .   ? 0.2560 0.2745 0.2727 -0.0188 -0.0132 0.0063  509 HOH B O   
9065 O  O   . HOH V .   ? 0.3366 0.2646 0.2635 -0.0114 -0.0196 -0.0472 510 HOH B O   
9066 O  O   . HOH V .   ? 0.2090 0.2208 0.1545 -0.0324 0.0068  0.0085  511 HOH B O   
9067 O  O   . HOH V .   ? 0.3368 0.2213 0.3481 -0.0829 0.0087  -0.0223 512 HOH B O   
9068 O  O   . HOH V .   ? 0.2131 0.2341 0.1993 0.0015  0.0258  0.0037  513 HOH B O   
9069 O  O   . HOH V .   ? 0.3366 0.2851 0.2172 -0.0688 0.0281  -0.0263 514 HOH B O   
9070 O  O   . HOH V .   ? 0.3379 0.2865 0.2470 -0.0105 0.0005  0.0148  515 HOH B O   
9071 O  O   . HOH V .   ? 0.3296 0.2621 0.1586 -0.0401 -0.0082 0.0293  516 HOH B O   
9072 O  O   . HOH V .   ? 0.2617 0.2705 0.3379 -0.0052 0.1263  0.0439  517 HOH B O   
9073 O  O   . HOH V .   ? 0.2483 0.3289 0.4065 0.0449  -0.1731 -0.0694 518 HOH B O   
9074 O  O   . HOH V .   ? 0.3118 0.2685 0.2892 -0.0184 -0.0560 -0.0582 519 HOH B O   
9075 O  O   . HOH V .   ? 0.3003 0.2208 0.3195 -0.0020 -0.0663 0.0417  520 HOH B O   
9076 O  O   . HOH V .   ? 0.3030 0.3082 0.2242 -0.0939 0.0328  0.0151  521 HOH B O   
9077 O  O   . HOH V .   ? 0.4146 0.1965 0.2294 0.0260  -0.0621 -0.0015 522 HOH B O   
9078 O  O   . HOH V .   ? 0.3151 0.3183 0.3370 -0.0091 0.1018  0.1225  523 HOH B O   
9079 O  O   . HOH V .   ? 0.2334 0.2795 0.3673 -0.0869 -0.0077 -0.0700 524 HOH B O   
9080 O  O   . HOH V .   ? 0.4654 0.3134 0.3528 -0.0405 -0.0149 -0.0262 525 HOH B O   
9081 O  O   . HOH V .   ? 0.3028 0.2149 0.2971 0.0293  0.0443  -0.0057 526 HOH B O   
9082 O  O   . HOH V .   ? 0.2486 0.3459 0.3352 0.0447  0.0082  -0.0478 527 HOH B O   
9083 O  O   . HOH V .   ? 0.3603 0.2809 0.2354 0.0353  -0.0961 0.0244  528 HOH B O   
9084 O  O   . HOH V .   ? 0.3934 0.2725 0.2357 0.0869  0.0575  0.0386  529 HOH B O   
9085 O  O   . HOH V .   ? 0.2224 0.1897 0.3088 0.0098  -0.0406 0.0102  530 HOH B O   
9086 O  O   . HOH V .   ? 0.2989 0.2940 0.2881 0.0104  -0.0040 -0.1071 531 HOH B O   
9087 O  O   . HOH V .   ? 0.2772 0.2842 0.2915 0.0046  0.0694  -0.0267 532 HOH B O   
9088 O  O   . HOH V .   ? 0.3111 0.4088 0.3443 -0.0744 -0.0353 0.0842  533 HOH B O   
9089 O  O   . HOH V .   ? 0.3695 0.3134 0.3285 0.1000  -0.1209 0.0706  534 HOH B O   
9090 O  O   . HOH V .   ? 0.3043 0.2775 0.3483 0.0625  -0.0588 0.0313  535 HOH B O   
9091 O  O   . HOH V .   ? 0.3549 0.4088 0.3242 0.0472  0.0098  -0.2090 536 HOH B O   
9092 O  O   . HOH V .   ? 0.2596 0.2878 0.3059 -0.0010 -0.0450 0.0007  537 HOH B O   
9093 O  O   . HOH V .   ? 0.2194 0.2678 0.3569 -0.0697 -0.0060 0.1485  538 HOH B O   
9094 O  O   . HOH V .   ? 0.2370 0.3242 0.2685 -0.0108 0.0170  0.0192  539 HOH B O   
9095 O  O   . HOH V .   ? 0.2885 0.1729 0.1872 0.1039  0.0043  -0.0013 540 HOH B O   
9096 O  O   . HOH V .   ? 0.3082 0.2592 0.3828 0.0815  -0.0599 -0.0674 541 HOH B O   
9097 O  O   . HOH V .   ? 0.3039 0.3826 0.4959 0.0754  0.1437  -0.1826 542 HOH B O   
9098 O  O   . HOH V .   ? 0.1845 0.2608 0.4036 0.0196  -0.0571 0.0125  543 HOH B O   
9099 O  O   . HOH V .   ? 0.2357 0.3686 0.3722 0.0310  0.0582  0.0054  544 HOH B O   
9100 O  O   . HOH V .   ? 0.3104 0.3388 0.3233 -0.0416 -0.0147 0.0181  545 HOH B O   
9101 O  O   . HOH V .   ? 0.4909 0.4593 0.2420 -0.1464 0.0068  0.0954  546 HOH B O   
9102 O  O   . HOH V .   ? 0.3323 0.4562 0.3382 0.0019  0.0883  -0.0568 547 HOH B O   
9103 O  O   . HOH V .   ? 0.3079 0.3630 0.3580 0.1679  -0.1162 -0.0746 548 HOH B O   
9104 O  O   . HOH V .   ? 0.3596 0.2910 0.4138 0.0816  -0.0129 0.1209  549 HOH B O   
9105 O  O   . HOH V .   ? 0.2585 0.3160 0.3768 0.1401  0.0988  0.0678  550 HOH B O   
9106 O  O   . HOH V .   ? 0.3064 0.3655 0.3558 -0.1185 -0.1547 0.0715  551 HOH B O   
9107 O  O   . HOH V .   ? 0.2181 0.3928 0.3860 0.0010  -0.0658 0.0375  552 HOH B O   
9108 O  O   . HOH V .   ? 0.1938 0.3605 0.5372 0.0489  0.0080  0.1419  553 HOH B O   
9109 O  O   . HOH V .   ? 0.3375 0.4047 0.5343 0.0803  0.1634  -0.0351 554 HOH B O   
9110 O  O   . HOH V .   ? 0.6399 0.2458 0.2086 0.1009  0.1032  0.0719  555 HOH B O   
9111 O  O   . HOH V .   ? 0.4273 0.3161 0.2933 0.0667  0.0384  -0.0487 556 HOH B O   
9112 O  O   . HOH V .   ? 0.3030 0.3292 0.3260 -0.0758 -0.0208 -0.0116 557 HOH B O   
9113 O  O   . HOH V .   ? 0.3824 0.4049 0.2662 0.0091  0.0297  -0.0157 558 HOH B O   
9114 O  O   . HOH V .   ? 0.4061 0.3136 0.3386 0.0526  0.0057  -0.1247 559 HOH B O   
9115 O  O   . HOH V .   ? 0.2549 0.4081 0.5313 0.0185  -0.0776 -0.0480 560 HOH B O   
9116 O  O   . HOH V .   ? 0.2630 0.2059 0.3364 -0.0172 -0.0068 0.0445  561 HOH B O   
9117 O  O   . HOH V .   ? 0.2761 0.2709 0.1924 -0.0129 0.0221  0.0201  562 HOH B O   
9118 O  O   . HOH V .   ? 0.2829 0.3107 0.2176 0.0115  -0.0240 0.0749  563 HOH B O   
9119 O  O   . HOH V .   ? 0.5733 0.3418 0.2966 0.0082  0.1022  0.1630  564 HOH B O   
9120 O  O   . HOH V .   ? 0.3330 0.3151 0.2312 -0.0509 -0.0666 0.0326  565 HOH B O   
9121 O  O   . HOH V .   ? 0.3684 0.4113 0.3522 0.0211  -0.0226 -0.1106 566 HOH B O   
9122 O  O   . HOH V .   ? 0.3386 0.4002 0.3064 -0.1128 -0.0632 0.0838  567 HOH B O   
9123 O  O   . HOH V .   ? 0.2698 0.4247 0.3953 -0.0606 -0.0313 -0.0233 568 HOH B O   
9124 O  O   . HOH V .   ? 0.3720 0.4499 0.4167 -0.0710 0.0028  -0.0287 569 HOH B O   
9125 O  O   . HOH V .   ? 0.5475 0.3161 0.2648 -0.0272 -0.0136 -0.0579 570 HOH B O   
9126 O  O   . HOH V .   ? 0.2389 0.4765 0.4582 -0.0178 -0.0247 0.0976  571 HOH B O   
9127 O  O   . HOH V .   ? 0.5325 0.5641 0.2242 -0.0174 -0.1190 -0.0549 572 HOH B O   
9128 O  O   . HOH V .   ? 0.6392 0.5774 0.2687 -0.0846 0.0734  -0.1076 573 HOH B O   
9129 O  O   . HOH V .   ? 0.3000 0.5539 0.7154 -0.2036 -0.0494 -0.0768 574 HOH B O   
9130 O  O   . HOH V .   ? 0.5343 0.3416 0.4135 0.1040  0.0652  0.0542  575 HOH B O   
9131 O  O   . HOH V .   ? 0.7397 0.5275 0.9328 0.0797  -0.0772 0.3075  576 HOH B O   
9132 O  O   . HOH V .   ? 0.6123 0.2558 0.2439 -0.1036 0.1150  -0.0921 577 HOH B O   
9133 O  O   . HOH V .   ? 0.4108 0.5985 0.3010 -0.0267 0.1143  -0.0502 578 HOH B O   
9134 O  O   . HOH V .   ? 0.3926 0.2933 0.3729 -0.0094 -0.0811 -0.0243 579 HOH B O   
9135 O  O   . HOH V .   ? 0.6058 0.4955 0.3916 -0.0377 0.0505  -0.0386 580 HOH B O   
9136 O  O   . HOH V .   ? 0.3745 0.4153 0.3257 0.0403  -0.1228 -0.0662 581 HOH B O   
9137 O  O   . HOH V .   ? 0.3754 0.3998 0.5067 -0.0626 -0.0746 0.0362  582 HOH B O   
9138 O  O   . HOH V .   ? 0.3634 0.5960 0.5006 0.0719  -0.0405 0.0205  583 HOH B O   
9139 O  O   . HOH V .   ? 0.6126 0.4474 0.2466 -0.1680 -0.0063 -0.0507 584 HOH B O   
9140 O  O   . HOH V .   ? 0.4775 0.3359 0.4463 -0.0328 0.0729  0.1605  585 HOH B O   
9141 O  O   . HOH V .   ? 0.3222 0.3066 0.3353 -0.1190 0.0421  0.0703  586 HOH B O   
9142 O  O   . HOH V .   ? 0.7972 0.6071 0.8095 -0.2370 -0.0791 0.0498  587 HOH B O   
9143 O  O   . HOH V .   ? 0.4876 0.3544 0.2694 -0.0518 0.0190  0.0310  588 HOH B O   
9144 O  O   . HOH V .   ? 0.3447 0.6019 0.6916 0.0899  0.0846  0.0190  589 HOH B O   
9145 O  O   . HOH V .   ? 0.4095 0.2818 0.3503 0.0351  0.0868  -0.0461 590 HOH B O   
9146 O  O   . HOH V .   ? 0.3341 0.5146 0.2750 -0.0187 -0.0359 -0.0476 591 HOH B O   
9147 O  O   . HOH V .   ? 0.4266 0.4208 0.4787 -0.0432 0.0658  -0.0549 592 HOH B O   
9148 O  O   . HOH V .   ? 0.5412 0.3494 0.5878 -0.2838 -0.0601 0.2178  593 HOH B O   
9149 O  O   . HOH V .   ? 0.3506 0.2809 0.4171 -0.1032 -0.0962 -0.0500 594 HOH B O   
9150 O  O   . HOH V .   ? 0.4627 0.2930 0.2572 -0.0487 -0.0031 0.0886  595 HOH B O   
9151 O  O   . HOH V .   ? 0.3494 0.2266 0.3355 -0.0590 -0.0714 0.0491  596 HOH B O   
9152 O  O   . HOH V .   ? 0.3828 0.4738 0.2458 0.0031  0.0373  -0.0485 597 HOH B O   
9153 O  O   . HOH V .   ? 0.5388 0.6485 0.3158 -0.1252 0.0617  -0.2309 598 HOH B O   
9154 O  O   . HOH V .   ? 0.4711 0.2240 0.3366 0.0505  0.0370  -0.0395 599 HOH B O   
9155 O  O   . HOH V .   ? 0.5083 0.5293 0.2443 0.0729  0.0960  0.0626  600 HOH B O   
9156 O  O   . HOH V .   ? 0.5198 0.4582 0.2903 -0.0593 -0.0548 -0.0217 601 HOH B O   
9157 O  O   . HOH V .   ? 0.4652 0.3637 0.2617 -0.0685 0.1190  -0.0375 602 HOH B O   
9158 O  O   . HOH V .   ? 0.3652 0.4162 0.5048 0.1044  -0.0119 -0.1718 603 HOH B O   
9159 O  O   . HOH V .   ? 0.4463 0.3546 0.5928 -0.0037 -0.0131 0.0194  604 HOH B O   
9160 O  O   . HOH V .   ? 0.4667 0.3533 0.3828 0.0997  0.0863  0.0527  605 HOH B O   
9161 O  O   . HOH V .   ? 0.5044 0.4941 0.3422 0.0773  0.1571  -0.0373 606 HOH B O   
9162 O  O   . HOH V .   ? 0.4013 0.3777 0.2890 0.0342  -0.1370 0.0608  607 HOH B O   
9163 O  O   . HOH V .   ? 0.3501 0.4566 0.5576 -0.0379 0.0498  -0.0021 608 HOH B O   
9164 O  O   . HOH V .   ? 0.3224 0.4138 0.4355 -0.0747 -0.0666 -0.0337 609 HOH B O   
9165 O  O   . HOH V .   ? 0.3233 0.3684 0.3495 0.0219  0.0295  -0.1132 610 HOH B O   
9166 O  O   . HOH V .   ? 0.6342 0.3673 0.2352 0.0681  0.0006  -0.0797 611 HOH B O   
9167 O  O   . HOH V .   ? 0.4568 0.2973 0.3700 -0.0017 0.0469  -0.0987 612 HOH B O   
9168 O  O   . HOH V .   ? 0.5906 0.5882 0.2707 -0.0697 0.0856  -0.0590 613 HOH B O   
9169 O  O   . HOH V .   ? 0.4933 0.3529 0.3682 -0.0912 -0.0227 0.0975  614 HOH B O   
9170 O  O   . HOH V .   ? 0.2438 0.5090 0.4938 -0.0820 0.0957  -0.0326 615 HOH B O   
9171 O  O   . HOH V .   ? 0.3621 0.4293 0.4634 0.0487  0.0945  -0.0568 616 HOH B O   
9172 O  O   . HOH V .   ? 0.3289 0.6212 0.5134 0.0275  -0.0331 -0.0428 617 HOH B O   
9173 O  O   . HOH V .   ? 0.2581 0.3605 0.5583 -0.1018 -0.0808 0.0109  618 HOH B O   
9174 O  O   . HOH V .   ? 0.2418 0.3161 0.3702 -0.0241 0.0674  0.0917  619 HOH B O   
9175 O  O   . HOH V .   ? 0.3264 0.5782 0.4176 0.1494  -0.0472 0.0627  620 HOH B O   
9176 O  O   . HOH V .   ? 0.3643 0.4891 0.3840 0.0277  0.1735  -0.0255 621 HOH B O   
9177 O  O   . HOH V .   ? 0.3533 0.4153 0.3991 0.1213  0.0127  -0.1200 622 HOH B O   
9178 O  O   . HOH V .   ? 0.4131 0.4843 0.3201 -0.0781 -0.0649 -0.0324 623 HOH B O   
9179 O  O   . HOH V .   ? 0.5618 0.4229 0.3458 -0.0121 -0.0829 0.0746  624 HOH B O   
9180 O  O   . HOH V .   ? 0.3052 0.3842 0.3115 -0.0414 -0.0105 0.0763  625 HOH B O   
9181 O  O   . HOH V .   ? 0.5231 0.3874 0.4532 0.1766  0.0688  0.0975  626 HOH B O   
9182 O  O   . HOH V .   ? 0.7185 0.6762 0.5522 -0.0335 -0.0085 -0.0734 627 HOH B O   
9183 O  O   . HOH V .   ? 0.5372 0.4172 0.3021 0.1327  -0.1156 -0.0803 628 HOH B O   
9184 O  O   . HOH V .   ? 0.3353 0.5591 0.3966 0.0791  -0.0542 -0.0957 629 HOH B O   
9185 O  O   . HOH V .   ? 0.3802 0.5047 0.3935 -0.0425 -0.0263 0.0857  630 HOH B O   
9186 O  O   . HOH V .   ? 0.7178 1.1700 0.5867 0.0759  -0.0797 0.0652  631 HOH B O   
9187 O  O   . HOH V .   ? 0.3666 0.4377 0.5059 0.0808  0.0860  0.0754  632 HOH B O   
9188 O  O   . HOH V .   ? 0.2386 0.2646 0.3203 0.0590  -0.0207 -0.0434 633 HOH B O   
9189 O  O   . HOH V .   ? 0.2603 0.2802 0.3531 0.0788  0.0275  -0.0439 634 HOH B O   
9190 O  O   . HOH V .   ? 0.3341 0.3397 0.2919 0.0763  -0.0741 0.0399  635 HOH B O   
9191 O  O   . HOH V .   ? 0.3923 0.3080 0.2560 -0.0395 -0.0104 0.0196  636 HOH B O   
9192 O  O   . HOH V .   ? 0.3424 0.4079 0.4178 0.0037  0.0019  0.0450  637 HOH B O   
9193 O  O   . HOH V .   ? 0.2851 0.3585 0.3206 -0.0355 0.0939  0.0203  638 HOH B O   
9194 O  O   . HOH V .   ? 0.5314 0.4366 0.2806 -0.1581 0.3055  -0.1574 639 HOH B O   
9195 O  O   . HOH V .   ? 0.4355 0.3296 0.4571 0.1158  -0.0878 -0.0049 640 HOH B O   
9196 O  O   . HOH V .   ? 0.3424 0.2849 0.2728 -0.0164 0.0502  0.0228  641 HOH B O   
9197 O  O   . HOH V .   ? 0.3251 0.3468 0.3684 -0.0168 -0.0111 -0.0174 642 HOH B O   
9198 O  O   . HOH V .   ? 0.3986 0.5773 0.2888 -0.1163 -0.0535 0.0132  643 HOH B O   
9199 O  O   . HOH V .   ? 0.5637 0.4538 0.3037 -0.0417 -0.0979 0.1023  644 HOH B O   
9200 O  O   . HOH V .   ? 0.4351 0.4027 0.3657 -0.0198 0.0509  -0.0285 645 HOH B O   
9201 O  O   . HOH V .   ? 0.8371 0.2960 0.3170 -0.3208 0.0149  0.1579  646 HOH B O   
9202 O  O   . HOH V .   ? 0.4472 0.4824 0.4294 -0.0662 0.0643  -0.1171 647 HOH B O   
9203 O  O   . HOH V .   ? 0.4178 0.4305 0.3246 -0.1988 -0.0899 0.0679  648 HOH B O   
9204 O  O   . HOH V .   ? 0.3844 0.3273 0.3303 0.0606  0.0211  0.0197  649 HOH B O   
9205 O  O   . HOH V .   ? 0.4308 0.4459 0.4113 0.0171  -0.0120 0.1340  650 HOH B O   
9206 O  O   . HOH V .   ? 0.5113 0.5065 0.2775 0.0193  0.0428  0.0656  651 HOH B O   
9207 O  O   . HOH V .   ? 0.4413 0.4000 0.3242 -0.0745 -0.0043 0.0697  652 HOH B O   
9208 O  O   . HOH V .   ? 0.3723 0.3797 0.6769 -0.0127 -0.1168 -0.0930 653 HOH B O   
9209 O  O   . HOH V .   ? 0.3176 0.4083 0.4453 -0.0399 0.0255  0.0186  654 HOH B O   
9210 O  O   . HOH V .   ? 0.7378 0.5516 0.3537 -0.1240 0.0197  -0.0504 655 HOH B O   
9211 O  O   . HOH V .   ? 0.2944 0.5645 0.3585 0.0220  -0.0819 0.0575  656 HOH B O   
9212 O  O   . HOH V .   ? 0.3564 0.4208 0.6277 0.0948  0.0392  -0.0266 657 HOH B O   
9213 O  O   . HOH V .   ? 0.3330 0.4693 0.1890 -0.0017 0.0218  -0.0146 658 HOH B O   
9214 O  O   . HOH V .   ? 0.4786 0.3689 0.2831 0.0762  -0.0546 -0.0098 659 HOH B O   
9215 O  O   . HOH V .   ? 0.3919 0.6765 0.4955 -0.0658 -0.0384 -0.1896 660 HOH B O   
9216 O  O   . HOH V .   ? 0.4183 0.4886 0.3977 -0.0782 -0.0608 -0.1247 661 HOH B O   
9217 O  O   . HOH V .   ? 0.3650 0.4718 0.4616 -0.0353 -0.0820 -0.1295 662 HOH B O   
9218 O  O   . HOH V .   ? 0.5735 0.6197 0.4526 0.0375  -0.1316 0.0658  663 HOH B O   
9219 O  O   . HOH V .   ? 0.2476 0.3149 0.3867 0.0557  0.0140  0.0595  664 HOH B O   
9220 O  O   . HOH V .   ? 0.6610 0.6098 0.6340 -0.1298 0.2608  -0.1298 665 HOH B O   
9221 O  O   . HOH W .   ? 0.1277 0.1211 0.0900 0.0005  -0.0121 0.0027  401 HOH C O   
9222 O  O   . HOH W .   ? 0.2011 0.1867 0.2257 0.0333  0.0255  0.0137  402 HOH C O   
9223 O  O   . HOH W .   ? 0.2328 0.1951 0.2202 0.0997  -0.0390 0.0187  403 HOH C O   
9224 O  O   . HOH W .   ? 0.0978 0.1145 0.1412 0.0031  0.0099  -0.0118 404 HOH C O   
9225 O  O   . HOH W .   ? 0.1484 0.1258 0.1228 -0.0207 -0.0163 0.0074  405 HOH C O   
9226 O  O   . HOH W .   ? 0.2106 0.1729 0.1200 -0.0132 0.0452  -0.0093 406 HOH C O   
9227 O  O   . HOH W .   ? 0.1879 0.2069 0.1079 -0.0168 0.0410  -0.0241 407 HOH C O   
9228 O  O   . HOH W .   ? 0.1350 0.1115 0.1547 0.0010  -0.0293 0.0071  408 HOH C O   
9229 O  O   . HOH W .   ? 0.1947 0.2642 0.3111 -0.0252 0.1141  -0.0377 409 HOH C O   
9230 O  O   . HOH W .   ? 0.2628 0.1457 0.1772 -0.0120 0.0119  -0.0006 410 HOH C O   
9231 O  O   . HOH W .   ? 0.1224 0.1342 0.1297 0.0189  0.0167  -0.0142 411 HOH C O   
9232 O  O   . HOH W .   ? 0.1337 0.2073 0.1719 0.0281  0.0379  0.0163  412 HOH C O   
9233 O  O   . HOH W .   ? 0.1782 0.1614 0.1435 0.0292  0.0008  -0.0184 413 HOH C O   
9234 O  O   . HOH W .   ? 0.2021 0.1405 0.1793 0.0000  0.0131  0.0126  414 HOH C O   
9235 O  O   . HOH W .   ? 0.1105 0.1608 0.1720 0.0293  0.0239  -0.0049 415 HOH C O   
9236 O  O   . HOH W .   ? 0.1270 0.1339 0.1256 -0.0023 -0.0107 -0.0044 416 HOH C O   
9237 O  O   . HOH W .   ? 0.2393 0.2458 0.1879 0.0296  -0.0357 0.0668  417 HOH C O   
9238 O  O   . HOH W .   ? 0.2240 0.1258 0.2364 0.0186  -0.0173 -0.0232 418 HOH C O   
9239 O  O   . HOH W .   ? 0.1611 0.1486 0.1441 0.0230  0.0126  -0.0114 419 HOH C O   
9240 O  O   . HOH W .   ? 0.2195 0.2044 0.1879 0.0105  0.0080  -0.0031 420 HOH C O   
9241 O  O   . HOH W .   ? 0.2046 0.1727 0.1696 0.0063  0.0118  -0.0023 421 HOH C O   
9242 O  O   . HOH W .   ? 0.2854 0.1599 0.3759 0.0137  0.0366  -0.0894 422 HOH C O   
9243 O  O   . HOH W .   ? 0.3037 0.2321 0.2858 -0.0834 -0.1606 0.0137  423 HOH C O   
9244 O  O   . HOH W .   ? 0.4471 0.4970 0.2953 -0.2134 -0.0259 -0.0649 424 HOH C O   
9245 O  O   . HOH W .   ? 0.2159 0.1608 0.2422 -0.0006 0.0383  -0.0238 425 HOH C O   
9246 O  O   . HOH W .   ? 0.2601 0.3501 0.1657 0.0080  0.0627  -0.0303 426 HOH C O   
9247 O  O   . HOH W .   ? 0.2339 0.1628 0.2256 -0.0635 -0.0138 0.0000  427 HOH C O   
9248 O  O   . HOH W .   ? 0.1888 0.1443 0.1764 -0.0088 0.0283  0.0007  428 HOH C O   
9249 O  O   . HOH W .   ? 0.2301 0.2289 0.2014 -0.0122 -0.0830 -0.0439 429 HOH C O   
9250 O  O   . HOH W .   ? 0.1883 0.1362 0.1696 0.0148  -0.0034 0.0087  430 HOH C O   
9251 O  O   . HOH W .   ? 0.1874 0.4280 0.2538 -0.0489 0.0225  0.0956  431 HOH C O   
9252 O  O   . HOH W .   ? 0.2190 0.1737 0.1349 0.0021  0.0266  0.0197  432 HOH C O   
9253 O  O   . HOH W .   ? 0.1326 0.1172 0.1404 -0.0013 0.0190  0.0027  433 HOH C O   
9254 O  O   . HOH W .   ? 0.1825 0.1974 0.3136 0.0035  -0.0007 -0.0331 434 HOH C O   
9255 O  O   . HOH W .   ? 0.2050 0.2558 0.2996 0.0265  -0.0637 0.0485  435 HOH C O   
9256 O  O   . HOH W .   ? 0.2369 0.2199 0.2782 -0.0240 0.0119  0.0306  436 HOH C O   
9257 O  O   . HOH W .   ? 0.3142 0.2327 0.3005 0.0148  -0.0037 0.0271  437 HOH C O   
9258 O  O   . HOH W .   ? 0.3574 0.2143 0.3190 0.0478  -0.0384 -0.0974 438 HOH C O   
9259 O  O   . HOH W .   ? 0.2666 0.2249 0.2178 -0.0015 -0.0379 -0.0243 439 HOH C O   
9260 O  O   . HOH W .   ? 0.3080 0.2167 0.2348 0.0340  -0.0271 0.0148  440 HOH C O   
9261 O  O   . HOH W .   ? 0.4081 0.4307 0.2152 -0.0265 0.0869  0.0820  441 HOH C O   
9262 O  O   . HOH W .   ? 0.2944 0.2348 0.2431 0.0043  -0.0219 0.0044  442 HOH C O   
9263 O  O   . HOH W .   ? 0.3461 0.4383 0.5042 0.0266  -0.0914 0.0970  443 HOH C O   
9264 O  O   . HOH W .   ? 0.3411 0.3503 0.2436 -0.0606 -0.0168 0.0724  444 HOH C O   
9265 O  O   . HOH W .   ? 0.1811 0.2188 0.1809 0.0024  0.0270  0.0054  445 HOH C O   
9266 O  O   . HOH W .   ? 0.3934 0.3810 0.2157 0.0258  0.0203  -0.0208 446 HOH C O   
9267 O  O   . HOH W .   ? 0.1818 0.2689 0.3652 -0.0197 0.0198  0.0683  447 HOH C O   
9268 O  O   . HOH W .   ? 0.2669 0.2737 0.4063 0.0546  -0.0719 0.0357  448 HOH C O   
9269 O  O   . HOH W .   ? 0.3849 0.2820 0.4420 0.0568  0.1032  0.0725  449 HOH C O   
9270 O  O   . HOH W .   ? 0.2863 0.2016 0.2439 0.0080  -0.0277 -0.0496 450 HOH C O   
9271 O  O   . HOH W .   ? 0.1816 0.1683 0.2847 0.0344  0.0273  -0.0006 451 HOH C O   
9272 O  O   . HOH W .   ? 0.2578 0.2592 0.2483 -0.0254 -0.0065 -0.0421 452 HOH C O   
9273 O  O   . HOH W .   ? 0.2052 0.1978 0.2281 0.0467  0.0346  -0.0063 453 HOH C O   
9274 O  O   . HOH W .   ? 0.2183 0.2666 0.2114 0.0063  0.0136  -0.0132 454 HOH C O   
9275 O  O   . HOH W .   ? 0.3147 0.4201 0.3350 0.1697  -0.1250 -0.0153 455 HOH C O   
9276 O  O   . HOH W .   ? 0.1489 0.1707 0.1867 -0.0051 -0.0383 0.0038  456 HOH C O   
9277 O  O   . HOH W .   ? 0.2477 0.2522 0.2091 0.0573  0.0138  -0.0032 457 HOH C O   
9278 O  O   . HOH W .   ? 0.2156 0.2545 0.3174 0.1035  0.0003  -0.0206 458 HOH C O   
9279 O  O   . HOH W .   ? 0.4753 0.3794 0.4025 0.0489  0.1225  0.0231  459 HOH C O   
9280 O  O   . HOH W .   ? 0.3328 0.3253 0.3375 0.0546  0.1101  -0.1121 460 HOH C O   
9281 O  O   . HOH W .   ? 0.3504 0.2849 0.2327 -0.0071 0.0057  0.0285  461 HOH C O   
9282 O  O   . HOH W .   ? 0.3100 0.3619 0.4435 0.0052  -0.0159 0.0243  462 HOH C O   
9283 O  O   . HOH W .   ? 0.2210 0.2046 0.2763 -0.0001 -0.0183 0.0062  463 HOH C O   
9284 O  O   . HOH W .   ? 0.1897 0.2116 0.2003 0.0080  -0.0401 -0.0082 464 HOH C O   
9285 O  O   . HOH W .   ? 0.2034 0.1787 0.1717 0.0135  0.0026  -0.0157 465 HOH C O   
9286 O  O   . HOH W .   ? 0.2035 0.2003 0.2273 0.0222  0.0015  0.0091  466 HOH C O   
9287 O  O   . HOH W .   ? 0.3091 0.3160 0.3068 -0.0193 0.0043  0.0026  467 HOH C O   
9288 O  O   . HOH W .   ? 0.2409 0.2039 0.3043 -0.0298 -0.0013 -0.0657 468 HOH C O   
9289 O  O   . HOH W .   ? 0.2711 0.2258 0.2696 0.0080  0.0006  -0.0694 469 HOH C O   
9290 O  O   . HOH W .   ? 0.4679 0.3246 0.4211 0.0454  -0.0005 -0.0518 470 HOH C O   
9291 O  O   . HOH W .   ? 0.1630 0.3402 0.3106 0.0676  0.0195  0.0666  471 HOH C O   
9292 O  O   . HOH W .   ? 0.2226 0.3619 0.2050 -0.0454 -0.0109 -0.0337 472 HOH C O   
9293 O  O   . HOH W .   ? 0.2303 0.2734 0.3246 -0.0104 -0.0278 0.0463  473 HOH C O   
9294 O  O   . HOH W .   ? 0.4552 0.3675 0.3314 0.0461  0.1277  0.0163  474 HOH C O   
9295 O  O   . HOH W .   ? 0.2946 0.2621 0.1973 0.0097  0.0302  -0.0063 475 HOH C O   
9296 O  O   . HOH W .   ? 0.2928 0.1709 0.2287 -0.0044 0.0881  0.0397  476 HOH C O   
9297 O  O   . HOH W .   ? 0.2944 0.2364 0.2944 -0.0155 -0.0306 -0.0013 477 HOH C O   
9298 O  O   . HOH W .   ? 0.2815 0.4851 0.4373 0.1186  -0.1115 -0.1819 478 HOH C O   
9299 O  O   . HOH W .   ? 0.3835 0.4077 0.4690 -0.0406 0.0513  -0.0184 479 HOH C O   
9300 O  O   . HOH W .   ? 0.2016 0.1486 0.2117 0.0308  0.0256  -0.0152 480 HOH C O   
9301 O  O   . HOH W .   ? 0.4408 0.8661 0.6445 -0.2010 -0.3106 0.0551  481 HOH C O   
9302 O  O   . HOH W .   ? 0.2551 0.2477 0.3973 0.0694  -0.0571 0.0767  482 HOH C O   
9303 O  O   . HOH W .   ? 0.5613 0.2703 0.3337 0.0137  -0.0275 -0.0480 483 HOH C O   
9304 O  O   . HOH W .   ? 0.2381 0.1914 0.2712 0.0141  0.0340  -0.0176 484 HOH C O   
9305 O  O   . HOH W .   ? 0.2669 0.2081 0.2150 0.0241  0.0688  0.0043  485 HOH C O   
9306 O  O   . HOH W .   ? 0.6525 0.4690 0.1991 -0.0283 0.0174  -0.0439 486 HOH C O   
9307 O  O   . HOH W .   ? 0.3224 0.3456 0.1941 0.0366  0.0746  -0.0217 487 HOH C O   
9308 O  O   . HOH W .   ? 0.5802 0.6134 0.3093 0.1083  0.0326  -0.0918 488 HOH C O   
9309 O  O   . HOH W .   ? 0.3348 0.3217 0.2018 -0.0041 -0.0456 -0.0208 489 HOH C O   
9310 O  O   . HOH W .   ? 0.3224 0.2021 0.2772 -0.0226 -0.0089 -0.0065 490 HOH C O   
9311 O  O   . HOH W .   ? 0.5594 0.3555 0.4769 0.0696  -0.0401 -0.1686 491 HOH C O   
9312 O  O   . HOH W .   ? 0.2425 0.3305 0.3307 -0.0727 0.0221  0.0259  492 HOH C O   
9313 O  O   . HOH W .   ? 0.4410 0.2409 0.4149 0.0753  -0.0331 0.0799  493 HOH C O   
9314 O  O   . HOH W .   ? 0.2910 0.3025 0.1875 -0.0078 0.0648  0.0254  494 HOH C O   
9315 O  O   . HOH W .   ? 0.2538 0.1775 0.3091 -0.0272 0.0250  -0.0288 495 HOH C O   
9316 O  O   . HOH W .   ? 0.4007 0.4106 0.2748 0.0896  -0.0201 -0.0892 496 HOH C O   
9317 O  O   . HOH W .   ? 0.2630 0.1935 0.2179 -0.0136 -0.0197 -0.0171 497 HOH C O   
9318 O  O   . HOH W .   ? 0.2579 0.4356 0.4146 0.0156  0.0732  0.0619  498 HOH C O   
9319 O  O   . HOH W .   ? 0.3037 0.2766 0.2429 -0.0679 -0.0220 -0.0120 499 HOH C O   
9320 O  O   . HOH W .   ? 0.2741 0.2660 0.3014 -0.0456 0.0052  0.0120  500 HOH C O   
9321 O  O   . HOH W .   ? 0.4549 0.3450 0.3458 -0.1636 0.1195  -0.1240 501 HOH C O   
9322 O  O   . HOH W .   ? 0.3014 0.2881 0.4280 -0.0406 -0.0081 -0.0974 502 HOH C O   
9323 O  O   . HOH W .   ? 0.2606 0.2242 0.3339 0.0878  -0.0157 0.0584  503 HOH C O   
9324 O  O   . HOH W .   ? 0.5281 0.4882 0.2831 0.1519  -0.0293 0.0303  504 HOH C O   
9325 O  O   . HOH W .   ? 0.4341 0.5386 0.4614 0.2087  0.0162  -0.1904 505 HOH C O   
9326 O  O   . HOH W .   ? 0.2156 0.2134 0.2635 0.0177  0.0428  -0.0237 506 HOH C O   
9327 O  O   . HOH W .   ? 0.4196 0.5045 0.4711 0.0300  0.0081  0.0057  507 HOH C O   
9328 O  O   . HOH W .   ? 0.2025 0.2344 0.1527 0.0601  0.0162  -0.0110 508 HOH C O   
9329 O  O   . HOH W .   ? 0.1551 0.1861 0.2023 -0.0044 0.0017  0.0249  509 HOH C O   
9330 O  O   . HOH W .   ? 0.2982 0.3233 0.2287 0.1252  -0.0006 -0.0289 510 HOH C O   
9331 O  O   . HOH W .   ? 0.2479 0.2533 0.2703 0.0386  -0.0542 0.0182  511 HOH C O   
9332 O  O   . HOH W .   ? 0.2703 0.2951 0.2572 -0.0261 -0.0712 -0.0372 512 HOH C O   
9333 O  O   . HOH W .   ? 0.2003 0.1874 0.2452 -0.0057 -0.0211 0.0167  513 HOH C O   
9334 O  O   . HOH W .   ? 0.3316 0.2820 0.1357 0.0086  0.0060  -0.0200 514 HOH C O   
9335 O  O   . HOH W .   ? 0.3801 0.3310 0.2129 0.0590  -0.0060 0.0549  515 HOH C O   
9336 O  O   . HOH W .   ? 0.3573 0.2036 0.4016 0.0544  -0.0133 -0.0037 516 HOH C O   
9337 O  O   . HOH W .   ? 0.2811 0.3607 0.3341 -0.0120 -0.0414 0.0353  517 HOH C O   
9338 O  O   . HOH W .   ? 0.2536 0.2606 0.3474 0.0197  0.1185  -0.0573 518 HOH C O   
9339 O  O   . HOH W .   ? 0.4381 0.1881 0.2303 -0.0239 -0.0386 -0.0071 519 HOH C O   
9340 O  O   . HOH W .   ? 0.3009 0.3355 0.3136 -0.0107 0.1171  -0.1092 520 HOH C O   
9341 O  O   . HOH W .   ? 0.2558 0.2210 0.3019 0.0057  0.0208  0.0326  521 HOH C O   
9342 O  O   . HOH W .   ? 0.3941 0.3273 0.2919 -0.0454 0.0010  -0.0081 522 HOH C O   
9343 O  O   . HOH W .   ? 0.2096 0.3837 0.4273 -0.0337 -0.1242 0.1036  523 HOH C O   
9344 O  O   . HOH W .   ? 0.2820 0.2594 0.3095 -0.0876 -0.0293 0.0469  524 HOH C O   
9345 O  O   . HOH W .   ? 0.2563 0.2072 0.2858 -0.0439 0.0663  0.0625  525 HOH C O   
9346 O  O   . HOH W .   ? 0.2299 0.2921 0.3709 0.0690  0.0030  -0.1084 526 HOH C O   
9347 O  O   . HOH W .   ? 0.3779 0.2987 0.2748 0.0203  0.0129  0.0750  527 HOH C O   
9348 O  O   . HOH W .   ? 0.3562 0.2657 0.3237 0.0781  -0.0522 0.0164  528 HOH C O   
9349 O  O   . HOH W .   ? 0.3231 0.4083 0.1518 -0.0194 0.0062  -0.0166 529 HOH C O   
9350 O  O   . HOH W .   ? 0.2669 0.3244 0.2402 -0.0091 0.0551  0.0254  530 HOH C O   
9351 O  O   . HOH W .   ? 0.3206 0.3955 0.2675 0.0000  -0.0165 0.0628  531 HOH C O   
9352 O  O   . HOH W .   ? 0.2124 0.2691 0.2922 0.0098  -0.0254 -0.0253 532 HOH C O   
9353 O  O   . HOH W .   ? 0.2858 0.4767 0.3718 0.1033  0.0006  0.0137  533 HOH C O   
9354 O  O   . HOH W .   ? 0.2804 0.2739 0.1876 0.0271  0.0346  -0.0006 534 HOH C O   
9355 O  O   . HOH W .   ? 0.3366 0.3310 0.3454 -0.0631 -0.1207 -0.0502 535 HOH C O   
9356 O  O   . HOH W .   ? 0.1850 0.2500 0.4201 -0.0035 -0.0731 -0.0100 536 HOH C O   
9357 O  O   . HOH W .   ? 0.2741 0.2953 0.2504 -0.0121 -0.0100 -0.0590 537 HOH C O   
9358 O  O   . HOH W .   ? 0.2775 0.2454 0.3136 0.0331  -0.0590 -0.0489 538 HOH C O   
9359 O  O   . HOH W .   ? 0.2193 0.2599 0.2840 -0.0080 0.0081  -0.0248 539 HOH C O   
9360 O  O   . HOH W .   ? 0.4233 0.2445 0.2570 -0.0631 0.0381  -0.0401 540 HOH C O   
9361 O  O   . HOH W .   ? 0.2930 0.2933 0.2800 0.0449  -0.0188 -0.0560 541 HOH C O   
9362 O  O   . HOH W .   ? 0.3671 0.2822 0.3104 -0.0436 -0.0781 -0.0082 542 HOH C O   
9363 O  O   . HOH W .   ? 0.2680 0.2556 0.2935 0.0005  -0.0295 -0.0149 543 HOH C O   
9364 O  O   . HOH W .   ? 0.2978 0.2987 0.3373 -0.0630 -0.1151 0.0329  544 HOH C O   
9365 O  O   . HOH W .   ? 0.3228 0.2168 0.2624 0.0675  0.0006  0.0080  545 HOH C O   
9366 O  O   . HOH W .   ? 0.1788 0.4938 0.4573 0.0456  -0.0692 -0.1451 546 HOH C O   
9367 O  O   . HOH W .   ? 0.3179 0.4059 0.3869 -0.0174 -0.0171 0.1880  547 HOH C O   
9368 O  O   . HOH W .   ? 0.3140 0.2856 0.3899 0.1112  -0.1198 0.0781  548 HOH C O   
9369 O  O   . HOH W .   ? 0.3425 0.3610 0.3565 -0.1263 -0.0791 0.1018  549 HOH C O   
9370 O  O   . HOH W .   ? 0.3869 0.3441 0.4004 0.1483  -0.0171 -0.0553 550 HOH C O   
9371 O  O   . HOH W .   ? 0.3199 0.3592 0.2982 0.0003  0.0540  -0.0401 551 HOH C O   
9372 O  O   . HOH W .   ? 0.4384 0.3160 0.2759 -0.0838 0.0582  0.0273  552 HOH C O   
9373 O  O   . HOH W .   ? 0.4056 0.4101 0.4126 -0.0882 -0.0724 -0.0119 553 HOH C O   
9374 O  O   . HOH W .   ? 0.3262 0.3113 0.2899 0.0790  -0.0115 -0.0729 554 HOH C O   
9375 O  O   . HOH W .   ? 0.4406 0.4325 0.7404 0.0656  -0.0617 0.0103  555 HOH C O   
9376 O  O   . HOH W .   ? 0.3165 0.3100 0.2251 0.0645  -0.0417 0.0086  556 HOH C O   
9377 O  O   . HOH W .   ? 0.5777 0.4801 0.3849 0.0342  -0.1456 0.0741  557 HOH C O   
9378 O  O   . HOH W .   ? 0.2676 0.3781 0.3826 0.1354  -0.1450 -0.0621 558 HOH C O   
9379 O  O   . HOH W .   ? 0.6093 0.2969 0.2962 -0.0035 0.0724  0.0926  559 HOH C O   
9380 O  O   . HOH W .   ? 0.4178 0.3574 0.2570 0.0017  0.0104  0.0148  560 HOH C O   
9381 O  O   . HOH W .   ? 0.6402 0.3228 0.5496 -0.1650 0.0683  -0.0961 561 HOH C O   
9382 O  O   . HOH W .   ? 0.5023 0.3700 0.3012 -0.0653 -0.1290 -0.0742 562 HOH C O   
9383 O  O   . HOH W .   ? 0.4210 0.4848 0.3817 0.0035  0.0493  -0.0944 563 HOH C O   
9384 O  O   . HOH W .   ? 0.2727 0.3028 0.3912 -0.1084 0.0781  -0.0353 564 HOH C O   
9385 O  O   . HOH W .   ? 0.1901 0.3580 0.6549 0.0003  -0.0215 -0.1636 565 HOH C O   
9386 O  O   . HOH W .   ? 0.5587 0.4050 0.3998 -0.0441 0.2228  -0.0586 566 HOH C O   
9387 O  O   . HOH W .   ? 0.6234 0.5331 0.6179 0.2725  -0.0350 0.0603  567 HOH C O   
9388 O  O   . HOH W .   ? 0.6057 0.5479 0.1102 0.1257  -0.1655 0.1005  568 HOH C O   
9389 O  O   . HOH W .   ? 0.5368 0.5559 0.3075 -0.0068 -0.0918 0.0366  569 HOH C O   
9390 O  O   . HOH W .   ? 0.5706 0.5382 0.3501 -0.0175 -0.1031 -0.2008 570 HOH C O   
9391 O  O   . HOH W .   ? 0.5031 0.3379 0.4038 0.0649  0.1083  -0.1337 571 HOH C O   
9392 O  O   . HOH W .   ? 0.3533 0.3853 0.5385 -0.1386 0.1185  0.1396  572 HOH C O   
9393 O  O   . HOH W .   ? 0.4376 0.6044 0.2127 0.0910  -0.0395 -0.0516 573 HOH C O   
9394 O  O   . HOH W .   ? 0.6604 0.3639 0.4478 -0.1641 0.1086  -0.1076 574 HOH C O   
9395 O  O   . HOH W .   ? 0.3806 0.4275 0.3580 0.1953  -0.0896 -0.0423 575 HOH C O   
9396 O  O   . HOH W .   ? 0.3339 0.3382 0.4287 0.0553  -0.0137 0.0094  576 HOH C O   
9397 O  O   . HOH W .   ? 0.3569 0.4539 0.5706 0.0758  -0.0957 0.0339  577 HOH C O   
9398 O  O   . HOH W .   ? 0.3810 0.6423 0.3393 -0.1371 -0.1295 -0.0750 578 HOH C O   
9399 O  O   . HOH W .   ? 0.3458 0.3707 0.6195 -0.0606 0.1330  0.1127  579 HOH C O   
9400 O  O   . HOH W .   ? 0.3564 0.4593 0.4113 -0.0273 0.0606  -0.0196 580 HOH C O   
9401 O  O   . HOH W .   ? 0.4793 0.2980 0.2485 0.0306  0.0663  -0.0315 581 HOH C O   
9402 O  O   . HOH W .   ? 0.3314 0.4126 0.4889 -0.0908 0.1657  0.0104  582 HOH C O   
9403 O  O   . HOH W .   ? 0.3413 0.2721 0.3533 -0.0478 0.0305  0.0108  583 HOH C O   
9404 O  O   . HOH W .   ? 0.2682 0.4859 0.4063 0.0617  -0.0544 -0.0285 584 HOH C O   
9405 O  O   . HOH W .   ? 0.4284 0.3991 0.2741 -0.0038 0.0234  0.0245  585 HOH C O   
9406 O  O   . HOH W .   ? 0.3574 0.4866 0.4327 0.0308  -0.1199 0.0518  586 HOH C O   
9407 O  O   . HOH W .   ? 0.4352 0.2924 0.4262 -0.0571 -0.0309 0.1067  587 HOH C O   
9408 O  O   . HOH W .   ? 0.9401 0.4110 0.3118 0.1165  0.2276  -0.2554 588 HOH C O   
9409 O  O   . HOH W .   ? 0.6222 0.5788 0.3368 -0.1298 0.0562  0.0878  589 HOH C O   
9410 O  O   . HOH W .   ? 0.5914 0.4330 0.1447 0.0738  0.1184  0.0070  590 HOH C O   
9411 O  O   . HOH W .   ? 0.5877 0.5971 0.2124 -0.1420 0.0806  -0.0381 591 HOH C O   
9412 O  O   . HOH W .   ? 0.3634 0.7002 0.4126 0.0832  -0.1942 -0.2944 592 HOH C O   
9413 O  O   . HOH W .   ? 0.3075 0.3670 0.4409 -0.0209 0.1414  -0.0566 593 HOH C O   
9414 O  O   . HOH W .   ? 0.5005 0.3474 0.3858 -0.0873 0.0683  -0.0784 594 HOH C O   
9415 O  O   . HOH W .   ? 0.5544 0.4844 0.3091 0.0777  -0.0716 -0.0540 595 HOH C O   
9416 O  O   . HOH W .   ? 0.2811 0.3634 0.3600 0.1168  -0.0028 -0.0175 596 HOH C O   
9417 O  O   . HOH W .   ? 0.4097 0.3556 0.3786 0.0208  -0.0891 -0.0577 597 HOH C O   
9418 O  O   . HOH W .   ? 0.3763 0.5001 0.2748 0.0311  0.0155  0.0710  598 HOH C O   
9419 O  O   . HOH W .   ? 0.4510 0.3783 0.2623 0.0293  -0.0705 0.0137  599 HOH C O   
9420 O  O   . HOH W .   ? 0.3402 0.3433 0.4934 -0.0513 -0.0505 -0.0315 600 HOH C O   
9421 O  O   . HOH W .   ? 0.3704 0.4243 0.3653 0.0496  0.0060  0.0423  601 HOH C O   
9422 O  O   . HOH W .   ? 0.3781 0.5085 0.2606 -0.1257 0.0785  -0.0197 602 HOH C O   
9423 O  O   . HOH W .   ? 0.3873 0.2879 0.3364 0.0518  0.0803  -0.0010 603 HOH C O   
9424 O  O   . HOH W .   ? 0.3797 0.3616 0.3628 -0.0359 -0.1711 0.0500  604 HOH C O   
9425 O  O   . HOH W .   ? 0.2996 0.4857 0.3623 0.1054  -0.0189 0.0046  605 HOH C O   
9426 O  O   . HOH W .   ? 0.5300 0.3420 0.2755 -0.1424 -0.0080 0.0513  606 HOH C O   
9427 O  O   . HOH W .   ? 0.5182 0.3109 0.3860 -0.0071 -0.0756 0.0548  607 HOH C O   
9428 O  O   . HOH W .   ? 0.4860 0.7128 0.2357 -0.0144 -0.0465 -0.0252 608 HOH C O   
9429 O  O   . HOH W .   ? 0.4869 0.5909 0.4144 -0.0441 0.0089  -0.0515 609 HOH C O   
9430 O  O   . HOH W .   ? 0.4477 0.4300 0.5376 0.0208  -0.1005 0.0441  610 HOH C O   
9431 O  O   . HOH W .   ? 0.5770 0.3271 0.3734 0.0476  0.0662  -0.1228 611 HOH C O   
9432 O  O   . HOH W .   ? 0.2470 0.3817 0.3623 -0.0208 -0.0020 0.0675  612 HOH C O   
9433 O  O   . HOH W .   ? 0.3813 0.2903 0.3594 0.0189  0.0240  0.0727  613 HOH C O   
9434 O  O   . HOH W .   ? 0.3242 0.3720 0.3995 0.0900  -0.0785 -0.0026 614 HOH C O   
9435 O  O   . HOH W .   ? 0.3962 0.2601 0.3176 0.1017  0.0303  -0.0397 615 HOH C O   
9436 O  O   . HOH W .   ? 0.6935 0.5382 0.8463 0.2075  0.2811  0.1550  616 HOH C O   
9437 O  O   . HOH W .   ? 0.3370 0.3756 0.3671 0.0206  -0.0688 -0.0020 617 HOH C O   
9438 O  O   . HOH W .   ? 0.4158 0.3404 0.4054 0.0135  -0.0366 0.0215  618 HOH C O   
9439 O  O   . HOH W .   ? 0.2998 0.4563 0.3524 0.0441  0.0383  0.0111  619 HOH C O   
9440 O  O   . HOH W .   ? 0.4230 0.5400 0.6916 0.0340  0.3267  0.0049  620 HOH C O   
9441 O  O   . HOH W .   ? 0.3837 0.6935 0.4373 -0.0584 -0.0221 -0.0586 621 HOH C O   
9442 O  O   . HOH W .   ? 0.4269 0.4607 0.4449 0.0165  -0.2384 -0.1030 622 HOH C O   
9443 O  O   . HOH W .   ? 0.4528 0.3217 0.3686 0.0608  -0.0168 -0.0030 623 HOH C O   
9444 O  O   . HOH W .   ? 0.4011 0.3233 0.3657 -0.0403 0.1019  -0.0888 624 HOH C O   
9445 O  O   . HOH W .   ? 0.2779 0.2488 0.3316 -0.0395 -0.0272 -0.0196 625 HOH C O   
9446 O  O   . HOH W .   ? 0.3957 0.3616 0.3996 -0.0810 0.0299  0.0077  626 HOH C O   
9447 O  O   . HOH W .   ? 0.4133 0.3043 0.3510 -0.0443 0.1011  0.0197  627 HOH C O   
9448 O  O   . HOH W .   ? 0.4381 0.4557 0.2624 0.0012  0.0665  0.0021  628 HOH C O   
9449 O  O   . HOH W .   ? 0.4654 0.4424 0.5297 0.0573  -0.1826 -0.1215 629 HOH C O   
9450 O  O   . HOH W .   ? 0.4833 0.5785 0.4232 0.0265  0.2197  0.0811  630 HOH C O   
9451 O  O   . HOH W .   ? 0.3176 0.4941 0.3813 -0.0516 0.0082  -0.0649 631 HOH C O   
9452 O  O   . HOH W .   ? 0.4160 0.4153 0.2800 -0.0102 -0.0124 0.0439  632 HOH C O   
9453 O  O   . HOH W .   ? 0.2975 0.2992 0.3447 -0.0035 0.0716  0.0184  633 HOH C O   
9454 O  O   . HOH W .   ? 0.4427 0.4628 0.4898 0.1504  0.1046  -0.0204 634 HOH C O   
9455 O  O   . HOH W .   ? 0.5115 0.4844 0.3070 -0.0606 -0.1014 0.0876  635 HOH C O   
9456 O  O   . HOH W .   ? 0.6028 0.5331 0.2960 -0.1055 -0.0326 0.1555  636 HOH C O   
9457 O  O   . HOH W .   ? 0.4639 0.3849 0.3987 0.1125  -0.0935 -0.1427 637 HOH C O   
9458 O  O   . HOH W .   ? 0.4399 0.4683 0.3420 -0.0366 0.1262  -0.0430 638 HOH C O   
9459 O  O   . HOH W .   ? 0.4783 0.4180 0.3666 -0.0520 0.0745  -0.0952 639 HOH C O   
9460 O  O   . HOH W .   ? 0.3161 0.2454 0.2084 0.0650  -0.0175 0.0461  640 HOH C O   
9461 O  O   . HOH W .   ? 0.4556 0.2980 0.4735 -0.1482 0.1497  -0.0386 641 HOH C O   
9462 O  O   . HOH W .   ? 0.3255 0.5217 0.2547 -0.0394 0.0438  0.0496  642 HOH C O   
9463 O  O   . HOH W .   ? 0.3386 0.2608 0.1960 -0.0094 0.0012  -0.0200 643 HOH C O   
9464 O  O   . HOH W .   ? 0.4699 0.4355 0.5393 0.1132  0.1133  -0.1107 644 HOH C O   
9465 O  O   . HOH W .   ? 0.3819 0.4194 0.4628 0.0992  -0.0630 0.1234  645 HOH C O   
9466 O  O   . HOH W .   ? 0.4040 0.4975 0.3054 0.0136  0.0640  -0.0060 646 HOH C O   
9467 O  O   . HOH W .   ? 0.4754 0.4894 0.2910 -0.0816 0.0346  0.1028  647 HOH C O   
9468 O  O   . HOH W .   ? 0.3628 0.5241 0.2565 0.0346  -0.0478 0.0976  648 HOH C O   
9469 O  O   . HOH W .   ? 0.3479 0.4108 0.4736 0.0454  -0.0359 -0.0182 649 HOH C O   
9470 O  O   . HOH W .   ? 0.3416 0.2267 0.3226 0.0668  -0.0685 -0.0568 650 HOH C O   
9471 O  O   . HOH W .   ? 0.3869 0.5318 0.5144 0.0419  0.1574  0.0504  651 HOH C O   
9472 O  O   . HOH W .   ? 0.4201 0.3652 0.5321 0.1162  -0.1650 -0.1234 652 HOH C O   
9473 O  O   . HOH W .   ? 0.6595 0.4625 0.3404 0.3303  0.3517  0.0051  653 HOH C O   
9474 O  O   . HOH X .   ? 0.1212 0.1310 0.0942 -0.0017 0.0000  0.0074  401 HOH D O   
9475 O  O   . HOH X .   ? 0.1754 0.2088 0.2278 0.0097  0.0375  -0.0120 402 HOH D O   
9476 O  O   . HOH X .   ? 0.2475 0.2082 0.2159 0.1036  -0.0423 0.0138  403 HOH D O   
9477 O  O   . HOH X .   ? 0.1272 0.1272 0.1502 -0.0104 0.0119  -0.0217 404 HOH D O   
9478 O  O   . HOH X .   ? 0.1492 0.1310 0.1191 -0.0120 0.0024  0.0119  405 HOH D O   
9479 O  O   . HOH X .   ? 0.1845 0.1773 0.1296 -0.0232 0.0353  -0.0236 406 HOH D O   
9480 O  O   . HOH X .   ? 0.2133 0.2170 0.0973 -0.0335 0.0153  -0.0206 407 HOH D O   
9481 O  O   . HOH X .   ? 0.1344 0.1224 0.1456 -0.0038 -0.0122 0.0168  408 HOH D O   
9482 O  O   . HOH X .   ? 0.2263 0.2612 0.3707 -0.0687 0.1624  -0.0337 409 HOH D O   
9483 O  O   . HOH X .   ? 0.2818 0.1560 0.1741 -0.0020 -0.0027 0.0103  410 HOH D O   
9484 O  O   . HOH X .   ? 0.1335 0.1445 0.1296 0.0000  0.0010  -0.0351 411 HOH D O   
9485 O  O   . HOH X .   ? 0.1635 0.2147 0.1538 0.0051  0.0564  -0.0048 412 HOH D O   
9486 O  O   . HOH X .   ? 0.1947 0.1665 0.1860 0.0164  -0.0028 -0.0186 413 HOH D O   
9487 O  O   . HOH X .   ? 0.2100 0.1680 0.2393 -0.0115 0.0032  0.0148  414 HOH D O   
9488 O  O   . HOH X .   ? 0.1238 0.1811 0.1668 0.0094  0.0264  -0.0082 415 HOH D O   
9489 O  O   . HOH X .   ? 0.1290 0.1535 0.1313 -0.0153 -0.0288 -0.0063 416 HOH D O   
9490 O  O   . HOH X .   ? 0.2797 0.2307 0.2718 0.0088  -0.0502 0.0252  417 HOH D O   
9491 O  O   . HOH X .   ? 0.2470 0.1387 0.2924 -0.0105 -0.0351 -0.0434 418 HOH D O   
9492 O  O   . HOH X .   ? 0.1716 0.1642 0.1495 0.0010  -0.0001 -0.0111 419 HOH D O   
9493 O  O   . HOH X .   ? 0.2029 0.2152 0.2506 0.0024  0.0003  -0.0315 420 HOH D O   
9494 O  O   . HOH X .   ? 0.1930 0.1841 0.1734 0.0167  0.0057  -0.0151 421 HOH D O   
9495 O  O   . HOH X .   ? 0.3133 0.1678 0.3404 -0.0015 0.0335  -0.0901 422 HOH D O   
9496 O  O   . HOH X .   ? 0.2750 0.2391 0.2721 -0.0460 -0.1114 0.0081  423 HOH D O   
9497 O  O   . HOH X .   ? 0.3598 0.4524 0.2269 -0.0439 0.0958  0.0099  424 HOH D O   
9498 O  O   . HOH X .   ? 0.2141 0.1650 0.2969 0.0044  0.0032  0.0049  425 HOH D O   
9499 O  O   . HOH X .   ? 0.2296 0.2531 0.2373 0.0133  0.0702  -0.0667 426 HOH D O   
9500 O  O   . HOH X .   ? 0.2342 0.1820 0.3759 -0.0524 -0.0549 0.0242  427 HOH D O   
9501 O  O   . HOH X .   ? 0.2075 0.1570 0.2319 -0.0074 0.0046  0.0041  428 HOH D O   
9502 O  O   . HOH X .   ? 0.1532 0.1978 0.1893 -0.0055 -0.0390 -0.0111 429 HOH D O   
9503 O  O   . HOH X .   ? 0.2073 0.1482 0.2285 0.0040  0.0153  0.0222  430 HOH D O   
9504 O  O   . HOH X .   ? 0.1527 0.5414 0.3371 -0.0320 0.0403  0.1036  431 HOH D O   
9505 O  O   . HOH X .   ? 0.2463 0.1920 0.1511 -0.0107 0.0151  0.0252  432 HOH D O   
9506 O  O   . HOH X .   ? 0.1544 0.1331 0.1466 0.0046  -0.0015 -0.0040 433 HOH D O   
9507 O  O   . HOH X .   ? 0.2359 0.1937 0.3014 -0.0255 -0.0307 -0.0395 434 HOH D O   
9508 O  O   . HOH X .   ? 0.2019 0.2806 0.3628 0.0071  -0.0573 0.0077  435 HOH D O   
9509 O  O   . HOH X .   ? 0.2775 0.2614 0.3111 -0.1006 -0.0333 0.0263  436 HOH D O   
9510 O  O   . HOH X .   ? 0.3325 0.2804 0.3050 -0.0221 -0.0359 0.0082  437 HOH D O   
9511 O  O   . HOH X .   ? 0.3355 0.2188 0.2816 0.0219  -0.0505 -0.0478 438 HOH D O   
9512 O  O   . HOH X .   ? 0.2666 0.2066 0.1984 -0.0383 -0.0253 -0.0173 439 HOH D O   
9513 O  O   . HOH X .   ? 0.3045 0.2736 0.2509 0.0228  0.0166  0.0054  440 HOH D O   
9514 O  O   . HOH X .   ? 0.2716 0.4187 0.2476 -0.0038 0.0472  0.0240  441 HOH D O   
9515 O  O   . HOH X .   ? 0.3172 0.2793 0.2626 0.0027  0.0416  -0.0159 442 HOH D O   
9516 O  O   . HOH X .   ? 0.2567 0.5030 0.4120 0.0461  -0.1375 0.1250  443 HOH D O   
9517 O  O   . HOH X .   ? 0.2908 0.3077 0.2452 0.0258  -0.0394 0.0428  444 HOH D O   
9518 O  O   . HOH X .   ? 0.2096 0.2163 0.2321 -0.0071 0.0239  0.0135  445 HOH D O   
9519 O  O   . HOH X .   ? 0.4958 0.4194 0.2705 0.0041  -0.0764 0.0206  446 HOH D O   
9520 O  O   . HOH X .   ? 0.1976 0.2506 0.3102 -0.0133 -0.0171 0.0294  447 HOH D O   
9521 O  O   . HOH X .   ? 0.3160 0.2666 0.4613 0.0082  -0.1412 0.0540  448 HOH D O   
9522 O  O   . HOH X .   ? 0.5041 0.3005 0.2797 0.0976  -0.0281 0.0162  449 HOH D O   
9523 O  O   . HOH X .   ? 0.2958 0.1942 0.2298 -0.0208 -0.0183 -0.0307 450 HOH D O   
9524 O  O   . HOH X .   ? 0.1527 0.1861 0.2118 0.0335  0.0230  0.0043  451 HOH D O   
9525 O  O   . HOH X .   ? 0.3210 0.2691 0.3228 -0.0337 -0.0553 -0.0233 452 HOH D O   
9526 O  O   . HOH X .   ? 0.1928 0.2163 0.2335 0.0148  0.0024  0.0131  453 HOH D O   
9527 O  O   . HOH X .   ? 0.2296 0.3172 0.2757 0.0198  0.0127  0.0564  454 HOH D O   
9528 O  O   . HOH X .   ? 0.3186 0.3485 0.2797 0.0935  -0.1280 0.0247  455 HOH D O   
9529 O  O   . HOH X .   ? 0.1601 0.1788 0.2010 -0.0250 -0.0511 0.0003  456 HOH D O   
9530 O  O   . HOH X .   ? 0.2624 0.2433 0.2894 0.0573  -0.0207 0.0300  457 HOH D O   
9531 O  O   . HOH X .   ? 0.2084 0.2375 0.2337 0.0640  -0.0041 0.0164  458 HOH D O   
9532 O  O   . HOH X .   ? 0.3138 0.3937 0.3986 0.0496  0.0694  0.0035  459 HOH D O   
9533 O  O   . HOH X .   ? 0.3815 0.3623 0.3404 0.0636  0.0825  -0.0883 460 HOH D O   
9534 O  O   . HOH X .   ? 0.2269 0.2327 0.2062 -0.0304 0.0425  -0.0126 461 HOH D O   
9535 O  O   . HOH X .   ? 0.2418 0.2002 0.3012 -0.0461 0.0031  0.0187  462 HOH D O   
9536 O  O   . HOH X .   ? 0.3928 0.3158 0.4496 0.0553  -0.0199 -0.0480 463 HOH D O   
9537 O  O   . HOH X .   ? 0.2536 0.2427 0.3535 -0.0406 -0.0243 0.0177  464 HOH D O   
9538 O  O   . HOH X .   ? 0.1899 0.2115 0.2231 -0.0401 -0.0119 -0.0040 465 HOH D O   
9539 O  O   . HOH X .   ? 0.2069 0.1685 0.2185 0.0153  0.0179  0.0176  466 HOH D O   
9540 O  O   . HOH X .   ? 0.2380 0.2107 0.2863 0.0203  0.0026  0.0135  467 HOH D O   
9541 O  O   . HOH X .   ? 0.3134 0.3434 0.3646 0.0264  -0.0303 0.0425  468 HOH D O   
9542 O  O   . HOH X .   ? 0.3386 0.2276 0.2953 0.0266  0.0505  -0.0863 469 HOH D O   
9543 O  O   . HOH X .   ? 0.4273 0.4214 0.4484 0.0844  -0.0335 -0.0226 470 HOH D O   
9544 O  O   . HOH X .   ? 0.2619 0.3300 0.4429 0.0846  -0.0331 -0.0135 471 HOH D O   
9545 O  O   . HOH X .   ? 0.1894 0.4460 0.4402 0.0803  0.0288  0.0062  472 HOH D O   
9546 O  O   . HOH X .   ? 0.2176 0.3179 0.1779 -0.0379 -0.0153 -0.0414 473 HOH D O   
9547 O  O   . HOH X .   ? 0.1906 0.2894 0.2933 -0.0302 -0.0019 0.0104  474 HOH D O   
9548 O  O   . HOH X .   ? 0.3271 0.3303 0.2806 -0.0035 0.0421  -0.0546 475 HOH D O   
9549 O  O   . HOH X .   ? 0.2984 0.4068 0.2472 0.0251  0.0416  -0.0212 476 HOH D O   
9550 O  O   . HOH X .   ? 0.3336 0.2361 0.2220 -0.0049 0.0922  0.0441  477 HOH D O   
9551 O  O   . HOH X .   ? 0.3158 0.2554 0.2640 -0.0218 0.0183  -0.0388 478 HOH D O   
9552 O  O   . HOH X .   ? 0.4866 0.3488 0.3019 0.0164  -0.0617 -0.0511 479 HOH D O   
9553 O  O   . HOH X .   ? 0.2005 0.1696 0.2621 0.0322  0.0000  -0.0091 480 HOH D O   
9554 O  O   . HOH X .   ? 0.3691 0.4668 0.3339 -0.0255 -0.0035 0.0164  481 HOH D O   
9555 O  O   . HOH X .   ? 0.2030 0.2842 0.3485 0.0210  -0.0590 0.0410  482 HOH D O   
9556 O  O   . HOH X .   ? 0.4894 0.3707 0.4063 -0.0641 -0.0138 0.0417  483 HOH D O   
9557 O  O   . HOH X .   ? 0.2768 0.2258 0.3208 -0.0273 0.0476  0.0125  484 HOH D O   
9558 O  O   . HOH X .   ? 0.2795 0.2161 0.1448 -0.0034 0.0671  -0.0026 485 HOH D O   
9559 O  O   . HOH X .   ? 0.3368 0.3262 0.1850 0.0153  0.0795  -0.0023 486 HOH D O   
9560 O  O   . HOH X .   ? 0.5059 0.4768 0.2290 0.0445  -0.0192 -0.0599 487 HOH D O   
9561 O  O   . HOH X .   ? 0.3666 0.3294 0.2649 -0.0271 -0.0339 -0.0315 488 HOH D O   
9562 O  O   . HOH X .   ? 0.2402 0.2380 0.2827 -0.0259 -0.0093 0.0013  489 HOH D O   
9563 O  O   . HOH X .   ? 0.2799 0.4215 0.3770 -0.1222 -0.0066 0.0107  490 HOH D O   
9564 O  O   . HOH X .   ? 0.4108 0.3084 0.3959 0.1216  0.0847  0.0970  491 HOH D O   
9565 O  O   . HOH X .   ? 0.3373 0.3348 0.2012 0.0161  0.0476  0.0749  492 HOH D O   
9566 O  O   . HOH X .   ? 0.2601 0.2249 0.3955 -0.0487 0.0791  -0.0825 493 HOH D O   
9567 O  O   . HOH X .   ? 0.4581 0.4891 0.2129 0.0307  0.0171  -0.0531 494 HOH D O   
9568 O  O   . HOH X .   ? 0.3436 0.2170 0.3068 -0.0320 -0.0143 0.0199  495 HOH D O   
9569 O  O   . HOH X .   ? 0.2520 0.4728 0.4530 0.0107  0.0226  0.0196  496 HOH D O   
9570 O  O   . HOH X .   ? 0.2754 0.2506 0.1984 -0.0886 -0.0306 -0.0006 497 HOH D O   
9571 O  O   . HOH X .   ? 0.2294 0.2872 0.3768 -0.0412 0.0000  0.0210  498 HOH D O   
9572 O  O   . HOH X .   ? 0.3984 0.2678 0.5588 -0.0518 -0.0131 -0.1333 499 HOH D O   
9573 O  O   . HOH X .   ? 0.3910 0.6658 0.3160 0.1685  0.0110  0.1446  500 HOH D O   
9574 O  O   . HOH X .   ? 0.2680 0.2269 0.3147 0.0899  -0.0046 0.0627  501 HOH D O   
9575 O  O   . HOH X .   ? 0.6970 0.6179 0.5029 0.0366  -0.0049 -0.0188 502 HOH D O   
9576 O  O   . HOH X .   ? 0.2529 0.2350 0.2635 0.0333  0.0562  -0.0452 503 HOH D O   
9577 O  O   . HOH X .   ? 0.4399 0.4713 0.5188 0.0250  -0.0408 0.0315  504 HOH D O   
9578 O  O   . HOH X .   ? 0.3407 0.3009 0.1684 0.0662  -0.0051 -0.0441 505 HOH D O   
9579 O  O   . HOH X .   ? 0.3147 0.3172 0.2389 0.0085  -0.0348 0.0419  506 HOH D O   
9580 O  O   . HOH X .   ? 0.4939 0.1509 0.2382 -0.0231 -0.0241 -0.0149 507 HOH D O   
9581 O  O   . HOH X .   ? 0.2378 0.1906 0.2117 -0.0222 0.0070  0.0199  508 HOH D O   
9582 O  O   . HOH X .   ? 0.2962 0.3659 0.2617 -0.0449 -0.0280 -0.0482 509 HOH D O   
9583 O  O   . HOH X .   ? 0.2926 0.2416 0.3754 0.0399  -0.0701 -0.0544 510 HOH D O   
9584 O  O   . HOH X .   ? 0.2254 0.4052 0.3411 -0.0253 0.0423  -0.0914 511 HOH D O   
9585 O  O   . HOH X .   ? 0.3129 0.3431 0.1703 -0.0127 -0.0089 0.0238  512 HOH D O   
9586 O  O   . HOH X .   ? 0.2646 0.3149 0.2452 -0.0844 -0.0214 0.0434  513 HOH D O   
9587 O  O   . HOH X .   ? 0.3546 0.2299 0.2260 0.0439  -0.0006 0.0289  514 HOH D O   
9588 O  O   . HOH X .   ? 0.3819 0.2339 0.3391 0.0551  -0.0438 -0.0785 515 HOH D O   
9589 O  O   . HOH X .   ? 0.4606 0.3957 0.2161 0.1158  -0.0126 -0.0719 516 HOH D O   
9590 O  O   . HOH X .   ? 0.2409 0.2504 0.2588 -0.0027 -0.0533 -0.0183 517 HOH D O   
9591 O  O   . HOH X .   ? 0.3614 0.3368 0.2588 0.0913  -0.0930 -0.0599 518 HOH D O   
9592 O  O   . HOH X .   ? 0.4212 0.3054 0.3422 -0.0799 -0.0219 0.0361  519 HOH D O   
9593 O  O   . HOH X .   ? 0.4097 0.3603 0.3167 -0.0819 -0.1653 0.0241  520 HOH D O   
9594 O  O   . HOH X .   ? 0.2967 0.3492 0.2391 -0.0423 -0.0584 0.0661  521 HOH D O   
9595 O  O   . HOH X .   ? 0.3820 0.2858 0.2632 -0.0833 -0.0648 0.0118  522 HOH D O   
9596 O  O   . HOH X .   ? 0.2475 0.2759 0.4438 -0.0118 0.1396  -0.0423 523 HOH D O   
9597 O  O   . HOH X .   ? 0.2874 0.2500 0.2287 0.0219  0.0175  -0.0264 524 HOH D O   
9598 O  O   . HOH X .   ? 0.3045 0.5207 0.4194 -0.0006 0.0812  -0.0454 525 HOH D O   
9599 O  O   . HOH X .   ? 0.2727 0.2736 0.2743 0.0483  -0.0102 -0.0355 526 HOH D O   
9600 O  O   . HOH X .   ? 0.2896 0.3585 0.3495 0.0428  -0.0232 -0.0326 527 HOH D O   
9601 O  O   . HOH X .   ? 0.2348 0.1773 0.3914 -0.0059 -0.0252 0.0182  528 HOH D O   
9602 O  O   . HOH X .   ? 0.3219 0.3806 0.4090 0.0024  -0.0980 0.0938  529 HOH D O   
9603 O  O   . HOH X .   ? 0.3980 0.3217 0.2463 0.0275  0.0472  0.0544  530 HOH D O   
9604 O  O   . HOH X .   ? 0.3361 0.2409 0.3231 -0.1347 0.0478  0.0778  531 HOH D O   
9605 O  O   . HOH X .   ? 0.2276 0.2804 0.3594 -0.0529 -0.0131 -0.0414 532 HOH D O   
9606 O  O   . HOH X .   ? 0.4993 0.4239 0.2451 0.1703  0.0074  -0.0746 533 HOH D O   
9607 O  O   . HOH X .   ? 0.3208 0.3118 0.4531 -0.0115 -0.1587 -0.0702 534 HOH D O   
9608 O  O   . HOH X .   ? 0.4323 0.2777 0.4066 0.0184  0.0882  -0.0234 535 HOH D O   
9609 O  O   . HOH X .   ? 0.2375 0.3752 0.3971 -0.0266 -0.0557 -0.0226 536 HOH D O   
9610 O  O   . HOH X .   ? 0.2904 0.3251 0.3853 -0.1406 -0.0715 0.0438  537 HOH D O   
9611 O  O   . HOH X .   ? 0.4196 0.2793 0.4477 0.0196  0.0627  0.0456  538 HOH D O   
9612 O  O   . HOH X .   ? 0.3582 0.4198 0.5691 0.0115  -0.0628 0.1225  539 HOH D O   
9613 O  O   . HOH X .   ? 0.5756 0.3086 0.2452 -0.0143 0.0212  0.0778  540 HOH D O   
9614 O  O   . HOH X .   ? 0.3592 0.3551 0.3345 -0.0746 0.0118  -0.0065 541 HOH D O   
9615 O  O   . HOH X .   ? 0.5788 0.1827 0.3587 0.0579  -0.0020 -0.0208 542 HOH D O   
9616 O  O   . HOH X .   ? 0.4029 0.3154 0.2637 -0.0342 -0.1167 -0.0496 543 HOH D O   
9617 O  O   . HOH X .   ? 0.2759 0.3788 0.2960 0.0791  0.0401  0.0217  544 HOH D O   
9618 O  O   . HOH X .   ? 0.4841 0.3244 0.2612 -0.1006 0.0408  0.0285  545 HOH D O   
9619 O  O   . HOH X .   ? 0.3420 0.4528 0.4088 0.1027  -0.1287 0.1218  546 HOH D O   
9620 O  O   . HOH X .   ? 0.3113 0.3664 0.4578 0.0653  -0.0092 -0.2155 547 HOH D O   
9621 O  O   . HOH X .   ? 0.4453 0.3107 0.4503 -0.0768 -0.0542 0.0051  548 HOH D O   
9622 O  O   . HOH X .   ? 0.3321 0.2326 0.4115 -0.0163 -0.0003 -0.0308 549 HOH D O   
9623 O  O   . HOH X .   ? 0.3605 0.2980 0.3980 -0.0851 -0.1572 0.0043  550 HOH D O   
9624 O  O   . HOH X .   ? 0.4459 0.3215 0.4471 -0.1140 -0.0326 0.0013  551 HOH D O   
9625 O  O   . HOH X .   ? 0.5351 0.5253 0.2540 0.0156  -0.0894 0.0979  552 HOH D O   
9626 O  O   . HOH X .   ? 0.3352 0.4602 0.3438 0.0816  0.1011  -0.0344 553 HOH D O   
9627 O  O   . HOH X .   ? 0.4086 0.3598 0.3106 -0.0013 0.0842  -0.1106 554 HOH D O   
9628 O  O   . HOH X .   ? 0.3477 0.2982 0.3001 0.0427  0.0273  0.0003  555 HOH D O   
9629 O  O   . HOH X .   ? 0.4822 0.5195 0.2989 0.1225  -0.0702 -0.1902 556 HOH D O   
9630 O  O   . HOH X .   ? 0.3851 0.2702 0.4016 0.1046  -0.0878 0.0026  557 HOH D O   
9631 O  O   . HOH X .   ? 0.4904 0.2703 0.3364 0.0844  -0.1363 -0.0485 558 HOH D O   
9632 O  O   . HOH X .   ? 0.5013 0.4172 0.3892 -0.0120 -0.0086 0.0277  559 HOH D O   
9633 O  O   . HOH X .   ? 0.3176 0.4366 0.4941 -0.0190 0.0952  0.1368  560 HOH D O   
9634 O  O   . HOH X .   ? 0.3472 0.3307 0.3828 -0.1322 0.0060  -0.1075 561 HOH D O   
9635 O  O   . HOH X .   ? 0.5146 0.3673 0.5834 -0.0992 0.0485  -0.0467 562 HOH D O   
9636 O  O   . HOH X .   ? 0.3201 0.3617 0.3355 0.0513  -0.0826 -0.0054 563 HOH D O   
9637 O  O   . HOH X .   ? 0.4409 0.4126 0.2975 0.0214  -0.0088 -0.0947 564 HOH D O   
9638 O  O   . HOH X .   ? 0.4449 0.5257 0.3210 0.0573  0.1546  0.0291  565 HOH D O   
9639 O  O   . HOH X .   ? 0.3668 0.4180 0.3643 -0.0627 0.0860  0.0052  566 HOH D O   
9640 O  O   . HOH X .   ? 0.3152 0.3817 0.4670 0.0987  -0.1721 -0.0688 567 HOH D O   
9641 O  O   . HOH X .   ? 0.4009 0.2662 0.2143 0.0430  -0.0115 -0.0322 568 HOH D O   
9642 O  O   . HOH X .   ? 0.5070 0.6286 0.4596 -0.0329 -0.0835 0.1264  569 HOH D O   
9643 O  O   . HOH X .   ? 0.4707 0.2784 0.4884 -0.0776 0.1022  0.0298  570 HOH D O   
9644 O  O   . HOH X .   ? 0.3623 0.4122 0.6003 0.0734  -0.0681 -0.0452 571 HOH D O   
9645 O  O   . HOH X .   ? 0.4266 0.3127 0.4280 0.0688  0.0962  -0.0988 572 HOH D O   
9646 O  O   . HOH X .   ? 0.3524 0.4763 0.3501 0.0910  0.1448  0.0483  573 HOH D O   
9647 O  O   . HOH X .   ? 0.5372 0.2820 0.3553 0.0227  -0.1330 -0.0253 574 HOH D O   
9648 O  O   . HOH X .   ? 0.3819 0.5558 0.3176 -0.0361 0.0267  0.0965  575 HOH D O   
9649 O  O   . HOH X .   ? 0.4153 0.3506 0.2549 -0.0144 -0.0054 -0.0615 576 HOH D O   
9650 O  O   . HOH X .   ? 0.4765 0.3610 0.2567 0.0184  0.0375  0.0068  577 HOH D O   
9651 O  O   . HOH X .   ? 0.5022 0.2682 0.4205 0.0865  -0.0010 0.0024  578 HOH D O   
9652 O  O   . HOH X .   ? 0.5346 0.3226 0.3197 -0.0992 0.0046  0.0619  579 HOH D O   
9653 O  O   . HOH X .   ? 0.4580 0.5437 0.3603 -0.0837 0.1411  -0.0107 580 HOH D O   
9654 O  O   . HOH X .   ? 0.5127 0.5522 0.2854 -0.0666 0.0694  -0.0786 581 HOH D O   
9655 O  O   . HOH X .   ? 0.4204 0.3953 0.2903 0.0829  -0.0870 0.0383  582 HOH D O   
9656 O  O   . HOH X .   ? 0.6086 0.4557 0.5703 -0.0772 0.0010  -0.0989 583 HOH D O   
9657 O  O   . HOH X .   ? 0.2642 0.6420 0.5447 0.1782  -0.0971 0.0529  584 HOH D O   
9658 O  O   . HOH X .   ? 0.3091 0.3847 0.4174 0.1367  -0.1118 -0.0693 585 HOH D O   
9659 O  O   . HOH X .   ? 0.4241 0.4111 0.3844 0.0908  -0.0584 -0.0636 586 HOH D O   
9660 O  O   . HOH X .   ? 0.3194 0.2702 0.4215 -0.0274 0.0049  -0.0038 587 HOH D O   
9661 O  O   . HOH X .   ? 0.3551 0.7746 0.3677 -0.0137 0.0828  -0.1585 588 HOH D O   
9662 O  O   . HOH X .   ? 0.4689 0.2922 0.3682 0.0601  0.1198  0.0065  589 HOH D O   
9663 O  O   . HOH X .   ? 0.4325 0.6934 0.2824 -0.0786 0.0463  -0.0507 590 HOH D O   
9664 O  O   . HOH X .   ? 0.3066 0.5468 0.1953 -0.0619 0.0734  -0.0709 591 HOH D O   
9665 O  O   . HOH X .   ? 0.5698 0.4591 0.4548 0.0076  -0.0904 -0.1246 592 HOH D O   
9666 O  O   . HOH X .   ? 0.3070 0.4190 0.3932 -0.0631 -0.0872 0.0057  593 HOH D O   
9667 O  O   . HOH X .   ? 0.4769 0.3436 0.5235 -0.0028 0.1508  -0.1392 594 HOH D O   
9668 O  O   . HOH X .   ? 0.3662 0.4732 0.2949 -0.0970 0.0599  -0.0304 595 HOH D O   
9669 O  O   . HOH X .   ? 0.4685 0.4208 0.5286 0.1933  0.0829  0.0062  596 HOH D O   
9670 O  O   . HOH X .   ? 0.2705 0.4246 0.5033 -0.0966 0.1431  0.1376  597 HOH D O   
9671 O  O   . HOH X .   ? 0.4805 0.3427 0.3914 0.0104  -0.1705 -0.0601 598 HOH D O   
9672 O  O   . HOH X .   ? 0.5170 0.4607 0.3019 0.0709  -0.0320 0.0091  599 HOH D O   
9673 O  O   . HOH X .   ? 0.3768 0.4919 0.3720 0.1368  -0.1213 -0.0227 600 HOH D O   
9674 O  O   . HOH X .   ? 0.3826 0.2728 0.6897 -0.1273 0.1257  -0.1030 601 HOH D O   
9675 O  O   . HOH X .   ? 0.5083 0.5630 0.4122 -0.1067 0.0557  -0.1413 602 HOH D O   
9676 O  O   . HOH X .   ? 0.4320 0.3314 0.5426 -0.1174 -0.0255 0.0187  603 HOH D O   
9677 O  O   . HOH X .   ? 0.4029 0.6945 0.3346 -0.0626 0.0366  0.1039  604 HOH D O   
9678 O  O   . HOH X .   ? 0.3034 0.3364 0.3504 0.0727  -0.0472 -0.0057 605 HOH D O   
9679 O  O   . HOH X .   ? 0.3258 0.4074 0.3016 0.0648  0.0813  -0.0285 606 HOH D O   
9680 O  O   . HOH X .   ? 0.3278 0.3305 0.3704 -0.0467 0.0623  -0.1296 607 HOH D O   
9681 O  O   . HOH X .   ? 0.2703 0.3323 0.4648 0.0375  0.0443  -0.0028 608 HOH D O   
9682 O  O   . HOH X .   ? 0.3436 0.4244 0.5206 -0.0024 -0.1111 -0.0828 609 HOH D O   
9683 O  O   . HOH X .   ? 0.5514 0.3007 0.4528 0.0443  -0.0410 -0.0405 610 HOH D O   
9684 O  O   . HOH X .   ? 0.4169 0.3253 0.3357 0.0286  0.0020  -0.0746 611 HOH D O   
9685 O  O   . HOH X .   ? 0.4589 0.4618 0.4542 -0.0288 -0.0929 -0.1291 612 HOH D O   
9686 O  O   . HOH X .   ? 0.3671 0.3055 0.2436 0.0879  -0.0194 0.0590  613 HOH D O   
9687 O  O   . HOH X .   ? 0.6198 0.4578 0.6481 0.0366  0.3145  0.1058  614 HOH D O   
9688 O  O   . HOH X .   ? 0.5587 0.5956 0.3582 -0.0804 0.0913  -0.1464 615 HOH D O   
9689 O  O   . HOH X .   ? 0.6546 0.6019 0.3147 -0.0595 -0.0661 0.0917  616 HOH D O   
9690 O  O   . HOH X .   ? 0.2809 0.5462 0.4984 0.1042  -0.0856 -0.0491 617 HOH D O   
9691 O  O   . HOH X .   ? 0.3680 0.5942 0.4201 0.0253  0.0266  -0.0874 618 HOH D O   
9692 O  O   . HOH X .   ? 0.2802 0.4435 0.5910 0.0297  0.0812  0.0149  619 HOH D O   
9693 O  O   . HOH X .   ? 0.6043 0.3542 0.4138 -0.0173 0.0914  0.1035  620 HOH D O   
9694 O  O   . HOH X .   ? 0.6723 0.4836 0.3856 0.1112  0.2538  0.0208  621 HOH D O   
9695 O  O   . HOH X .   ? 0.3488 0.5397 0.4991 -0.1966 0.1199  -0.0900 622 HOH D O   
9696 O  O   . HOH X .   ? 0.3583 0.2384 0.4275 -0.0024 0.0555  0.0399  623 HOH D O   
9697 O  O   . HOH X .   ? 0.3646 0.3404 0.2545 0.0252  0.0649  0.0049  624 HOH D O   
9698 O  O   . HOH X .   ? 0.4204 0.3941 0.5397 -0.1103 -0.0284 0.0670  625 HOH D O   
9699 O  O   . HOH X .   ? 0.4496 0.3896 0.5001 0.0366  0.1000  -0.0969 626 HOH D O   
9700 O  O   . HOH X .   ? 0.4199 0.4255 0.3091 0.0441  0.1545  0.0251  627 HOH D O   
9701 O  O   . HOH X .   ? 0.3282 0.3452 0.4959 0.0635  -0.0513 0.0394  628 HOH D O   
9702 O  O   . HOH X .   ? 0.3896 0.4492 0.4506 0.0270  -0.0932 -0.0482 629 HOH D O   
9703 O  O   . HOH X .   ? 0.4666 0.3637 0.3953 0.0926  -0.1257 -0.1015 630 HOH D O   
9704 O  O   . HOH X .   ? 0.3761 0.3540 0.4061 -0.0463 0.0948  -0.0441 631 HOH D O   
9705 O  O   . HOH X .   ? 0.5054 0.5184 0.4284 0.0688  -0.2328 0.0098  632 HOH D O   
9706 O  O   . HOH X .   ? 0.6104 0.3668 0.5256 -0.2224 0.1042  -0.0274 633 HOH D O   
9707 O  O   . HOH X .   ? 0.1896 0.4557 0.5275 0.0082  -0.0870 -0.1260 634 HOH D O   
9708 O  O   . HOH X .   ? 0.5231 0.6455 0.2247 0.0275  -0.0623 -0.0454 635 HOH D O   
9709 O  O   . HOH X .   ? 0.2958 0.2709 0.2930 -0.0254 0.0154  -0.1145 636 HOH D O   
9710 O  O   . HOH X .   ? 0.5723 0.7918 0.2384 -0.0847 0.0909  -0.0974 637 HOH D O   
9711 O  O   . HOH X .   ? 0.4782 0.5511 0.3483 -0.0313 0.0573  0.1661  638 HOH D O   
9712 O  O   . HOH X .   ? 0.3946 0.4000 0.2800 0.0738  0.1871  0.1412  639 HOH D O   
9713 O  O   . HOH X .   ? 0.4253 0.3589 0.3036 -0.0273 0.0359  0.0568  640 HOH D O   
9714 O  O   . HOH X .   ? 0.4319 0.3993 0.4981 0.0529  0.0447  -0.0595 641 HOH D O   
9715 O  O   . HOH X .   ? 0.2560 0.3208 0.4702 0.0702  -0.0438 -0.0120 642 HOH D O   
9716 O  O   . HOH X .   ? 0.3213 0.4492 0.3235 -0.0138 -0.0368 -0.0654 643 HOH D O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   HIS 3   3   3   HIS HIS B . n 
B 1 4   HIS 4   4   4   HIS HIS B . n 
B 1 5   TRP 5   5   5   TRP TRP B . n 
B 1 6   GLY 6   6   6   GLY GLY B . n 
B 1 7   TYR 7   7   7   TYR TYR B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  ASN 11  11  11  ASN ASN B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  TRP 16  16  16  TRP TRP B . n 
B 1 17  HIS 17  17  17  HIS HIS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  PRO 21  21  21  PRO PRO B . n 
B 1 22  ILE 22  22  22  ILE ILE B . n 
B 1 23  ALA 23  23  23  ALA ALA B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  GLN 28  28  28  GLN GLN B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PRO 30  30  30  PRO PRO B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  THR 35  35  35  THR THR B . n 
B 1 36  HIS 36  36  36  HIS HIS B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  TYR 40  40  40  TYR TYR B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  GLN 53  53  53  GLN GLN B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASN 61  61  61  ASN ASN B . n 
B 1 62  ASN 62  62  62  ASN ASN B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  LEU 79  79  79  LEU LEU B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  THR 87  87  87  THR THR B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  GLN 92  92  92  GLN GLN B . n 
B 1 93  PHE 93  93  93  PHE PHE B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  TRP 97  97  97  TRP TRP B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 THR 108 108 108 THR THR B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 LYS 113 113 113 LYS LYS B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLU 117 117 117 GLU GLU B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 HIS 122 122 122 HIS HIS B . n 
B 1 123 TRP 123 123 123 TRP TRP B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 LYS 126 127 127 LYS LYS B . n 
B 1 127 TYR 127 128 128 TYR TYR B . n 
B 1 128 GLY 128 129 129 GLY GLY B . n 
B 1 129 ASP 129 130 130 ASP ASP B . n 
B 1 130 PHE 130 131 131 PHE PHE B . n 
B 1 131 GLY 131 132 132 GLY GLY B . n 
B 1 132 LYS 132 133 133 LYS LYS B . n 
B 1 133 ALA 133 134 134 ALA ALA B . n 
B 1 134 VAL 134 135 135 VAL VAL B . n 
B 1 135 GLN 135 136 136 GLN GLN B . n 
B 1 136 GLN 136 137 137 GLN GLN B . n 
B 1 137 PRO 137 138 138 PRO PRO B . n 
B 1 138 ASP 138 139 139 ASP ASP B . n 
B 1 139 GLY 139 140 140 GLY GLY B . n 
B 1 140 LEU 140 141 141 LEU LEU B . n 
B 1 141 ALA 141 142 142 ALA ALA B . n 
B 1 142 VAL 142 143 143 VAL VAL B . n 
B 1 143 LEU 143 144 144 LEU LEU B . n 
B 1 144 GLY 144 145 145 GLY GLY B . n 
B 1 145 ILE 145 146 146 ILE ILE B . n 
B 1 146 PHE 146 147 147 PHE PHE B . n 
B 1 147 LEU 147 148 148 LEU LEU B . n 
B 1 148 LYS 148 149 149 LYS LYS B . n 
B 1 149 VAL 149 150 150 VAL VAL B . n 
B 1 150 GLY 150 151 151 GLY GLY B . n 
B 1 151 SER 151 152 152 SER SER B . n 
B 1 152 ALA 152 153 153 ALA ALA B . n 
B 1 153 LYS 153 154 154 LYS LYS B . n 
B 1 154 PRO 154 155 155 PRO PRO B . n 
B 1 155 GLY 155 156 156 GLY GLY B . n 
B 1 156 LEU 156 157 157 LEU LEU B . n 
B 1 157 GLN 157 158 158 GLN GLN B . n 
B 1 158 LYS 158 159 159 LYS LYS B . n 
B 1 159 VAL 159 160 160 VAL VAL B . n 
B 1 160 VAL 160 161 161 VAL VAL B . n 
B 1 161 ASP 161 162 162 ASP ASP B . n 
B 1 162 VAL 162 163 163 VAL VAL B . n 
B 1 163 LEU 163 164 164 LEU LEU B . n 
B 1 164 ASP 164 165 165 ASP ASP B . n 
B 1 165 SER 165 166 166 SER SER B . n 
B 1 166 ILE 166 167 167 ILE ILE B . n 
B 1 167 LYS 167 168 168 LYS LYS B . n 
B 1 168 THR 168 169 169 THR THR B . n 
B 1 169 LYS 169 170 170 LYS LYS B . n 
B 1 170 GLY 170 171 171 GLY GLY B . n 
B 1 171 LYS 171 172 172 LYS LYS B . n 
B 1 172 SER 172 173 173 SER SER B . n 
B 1 173 ALA 173 174 174 ALA ALA B . n 
B 1 174 ASP 174 175 175 ASP ASP B . n 
B 1 175 PHE 175 176 176 PHE PHE B . n 
B 1 176 THR 176 177 177 THR THR B . n 
B 1 177 ASN 177 178 178 ASN ASN B . n 
B 1 178 PHE 178 179 179 PHE PHE B . n 
B 1 179 ASP 179 180 180 ASP ASP B . n 
B 1 180 PRO 180 181 181 PRO PRO B . n 
B 1 181 ARG 181 182 182 ARG ARG B . n 
B 1 182 GLY 182 183 183 GLY GLY B . n 
B 1 183 LEU 183 184 184 LEU LEU B . n 
B 1 184 LEU 184 185 185 LEU LEU B . n 
B 1 185 PRO 185 186 186 PRO PRO B . n 
B 1 186 GLU 186 187 187 GLU GLU B . n 
B 1 187 SER 187 188 188 SER SER B . n 
B 1 188 LEU 188 189 189 LEU LEU B . n 
B 1 189 ASP 189 190 190 ASP ASP B . n 
B 1 190 TYR 190 191 191 TYR TYR B . n 
B 1 191 TRP 191 192 192 TRP TRP B . n 
B 1 192 THR 192 193 193 THR THR B . n 
B 1 193 TYR 193 194 194 TYR TYR B . n 
B 1 194 PRO 194 195 195 PRO PRO B . n 
B 1 195 GLY 195 196 196 GLY GLY B . n 
B 1 196 SER 196 197 197 SER SER B . n 
B 1 197 LEU 197 198 198 LEU LEU B . n 
B 1 198 THR 198 199 199 THR THR B . n 
B 1 199 THR 199 200 200 THR THR B . n 
B 1 200 PRO 200 201 201 PRO PRO B . n 
B 1 201 PRO 201 202 202 PRO PRO B . n 
B 1 202 LEU 202 203 203 LEU LEU B . n 
B 1 203 LEU 203 204 204 LEU LEU B . n 
B 1 204 GLU 204 205 205 GLU GLU B . n 
B 1 205 CYS 205 206 206 CYS CYS B . n 
B 1 206 VAL 206 207 207 VAL VAL B . n 
B 1 207 THR 207 208 208 THR THR B . n 
B 1 208 TRP 208 209 209 TRP TRP B . n 
B 1 209 ILE 209 210 210 ILE ILE B . n 
B 1 210 VAL 210 211 211 VAL VAL B . n 
B 1 211 LEU 211 212 212 LEU LEU B . n 
B 1 212 LYS 212 213 213 LYS LYS B . n 
B 1 213 GLU 213 214 214 GLU GLU B . n 
B 1 214 PRO 214 215 215 PRO PRO B . n 
B 1 215 ILE 215 216 216 ILE ILE B . n 
B 1 216 SER 216 217 217 SER SER B . n 
B 1 217 VAL 217 218 218 VAL VAL B . n 
B 1 218 SER 218 219 219 SER SER B . n 
B 1 219 SER 219 220 220 SER SER B . n 
B 1 220 GLU 220 221 221 GLU GLU B . n 
B 1 221 GLN 221 222 222 GLN GLN B . n 
B 1 222 VAL 222 223 223 VAL VAL B . n 
B 1 223 LEU 223 224 224 LEU LEU B . n 
B 1 224 LYS 224 225 225 LYS LYS B . n 
B 1 225 PHE 225 226 226 PHE PHE B . n 
B 1 226 ARG 226 227 227 ARG ARG B . n 
B 1 227 LYS 227 228 228 LYS LYS B . n 
B 1 228 LEU 228 229 229 LEU LEU B . n 
B 1 229 ASN 229 230 230 ASN ASN B . n 
B 1 230 PHE 230 231 231 PHE PHE B . n 
B 1 231 ASN 231 232 232 ASN ASN B . n 
B 1 232 GLY 232 233 233 GLY GLY B . n 
B 1 233 GLU 233 234 234 GLU GLU B . n 
B 1 234 GLY 234 235 235 GLY GLY B . n 
B 1 235 GLU 235 236 236 GLU GLU B . n 
B 1 236 PRO 236 237 237 PRO PRO B . n 
B 1 237 GLU 237 238 238 GLU GLU B . n 
B 1 238 GLU 238 239 239 GLU GLU B . n 
B 1 239 LEU 239 240 240 LEU LEU B . n 
B 1 240 MET 240 241 241 MET MET B . n 
B 1 241 VAL 241 242 242 VAL VAL B . n 
B 1 242 ASP 242 243 243 ASP ASP B . n 
B 1 243 ASN 243 244 244 ASN ASN B . n 
B 1 244 TRP 244 245 245 TRP TRP B . n 
B 1 245 ARG 245 246 246 ARG ARG B . n 
B 1 246 PRO 246 247 247 PRO PRO B . n 
B 1 247 ALA 247 248 248 ALA ALA B . n 
B 1 248 GLN 248 249 249 GLN GLN B . n 
B 1 249 PRO 249 250 250 PRO PRO B . n 
B 1 250 LEU 250 251 251 LEU LEU B . n 
B 1 251 LYS 251 252 252 LYS LYS B . n 
B 1 252 ASN 252 253 253 ASN ASN B . n 
B 1 253 ARG 253 254 254 ARG ARG B . n 
B 1 254 GLN 254 255 255 GLN GLN B . n 
B 1 255 ILE 255 256 256 ILE ILE B . n 
B 1 256 LYS 256 257 257 LYS LYS B . n 
B 1 257 ALA 257 258 258 ALA ALA B . n 
B 1 258 SER 258 259 259 SER SER B . n 
B 1 259 PHE 259 260 260 PHE PHE B . n 
B 1 260 LYS 260 261 261 LYS LYS B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   HIS 3   3   3   HIS HIS C . n 
C 1 4   HIS 4   4   4   HIS HIS C . n 
C 1 5   TRP 5   5   5   TRP TRP C . n 
C 1 6   GLY 6   6   6   GLY GLY C . n 
C 1 7   TYR 7   7   7   TYR TYR C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  HIS 10  10  10  HIS HIS C . n 
C 1 11  ASN 11  11  11  ASN ASN C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  GLU 14  14  14  GLU GLU C . n 
C 1 15  HIS 15  15  15  HIS HIS C . n 
C 1 16  TRP 16  16  16  TRP TRP C . n 
C 1 17  HIS 17  17  17  HIS HIS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  ASP 19  19  19  ASP ASP C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  PRO 21  21  21  PRO PRO C . n 
C 1 22  ILE 22  22  22  ILE ILE C . n 
C 1 23  ALA 23  23  23  ALA ALA C . n 
C 1 24  LYS 24  24  24  LYS LYS C . n 
C 1 25  GLY 25  25  25  GLY GLY C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  ARG 27  27  27  ARG ARG C . n 
C 1 28  GLN 28  28  28  GLN GLN C . n 
C 1 29  SER 29  29  29  SER SER C . n 
C 1 30  PRO 30  30  30  PRO PRO C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  ASP 32  32  32  ASP ASP C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  ASP 34  34  34  ASP ASP C . n 
C 1 35  THR 35  35  35  THR THR C . n 
C 1 36  HIS 36  36  36  HIS HIS C . n 
C 1 37  THR 37  37  37  THR THR C . n 
C 1 38  ALA 38  38  38  ALA ALA C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  TYR 40  40  40  TYR TYR C . n 
C 1 41  ASP 41  41  41  ASP ASP C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  LYS 45  45  45  LYS LYS C . n 
C 1 46  PRO 46  46  46  PRO PRO C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  SER 48  48  48  SER SER C . n 
C 1 49  VAL 49  49  49  VAL VAL C . n 
C 1 50  SER 50  50  50  SER SER C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  GLN 53  53  53  GLN GLN C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  THR 55  55  55  THR THR C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  LEU 57  57  57  LEU LEU C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  ILE 59  59  59  ILE ILE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  ASN 61  61  61  ASN ASN C . n 
C 1 62  ASN 62  62  62  ASN ASN C . n 
C 1 63  GLY 63  63  63  GLY GLY C . n 
C 1 64  HIS 64  64  64  HIS HIS C . n 
C 1 65  ALA 65  65  65  ALA ALA C . n 
C 1 66  PHE 66  66  66  PHE PHE C . n 
C 1 67  ASN 67  67  67  ASN ASN C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  GLU 69  69  69  GLU GLU C . n 
C 1 70  PHE 70  70  70  PHE PHE C . n 
C 1 71  ASP 71  71  71  ASP ASP C . n 
C 1 72  ASP 72  72  72  ASP ASP C . n 
C 1 73  SER 73  73  73  SER SER C . n 
C 1 74  GLN 74  74  74  GLN GLN C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  LYS 76  76  76  LYS LYS C . n 
C 1 77  ALA 77  77  77  ALA ALA C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  LYS 80  80  80  LYS LYS C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  PRO 83  83  83  PRO PRO C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  GLY 86  86  86  GLY GLY C . n 
C 1 87  THR 87  87  87  THR THR C . n 
C 1 88  TYR 88  88  88  TYR TYR C . n 
C 1 89  ARG 89  89  89  ARG ARG C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  ILE 91  91  91  ILE ILE C . n 
C 1 92  GLN 92  92  92  GLN GLN C . n 
C 1 93  PHE 93  93  93  PHE PHE C . n 
C 1 94  HIS 94  94  94  HIS HIS C . n 
C 1 95  PHE 95  95  95  PHE PHE C . n 
C 1 96  HIS 96  96  96  HIS HIS C . n 
C 1 97  TRP 97  97  97  TRP TRP C . n 
C 1 98  GLY 98  98  98  GLY GLY C . n 
C 1 99  SER 99  99  99  SER SER C . n 
C 1 100 LEU 100 100 100 LEU LEU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 GLN 103 103 103 GLN GLN C . n 
C 1 104 GLY 104 104 104 GLY GLY C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 GLU 106 106 106 GLU GLU C . n 
C 1 107 HIS 107 107 107 HIS HIS C . n 
C 1 108 THR 108 108 108 THR THR C . n 
C 1 109 VAL 109 109 109 VAL VAL C . n 
C 1 110 ASP 110 110 110 ASP ASP C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 LYS 112 112 112 LYS LYS C . n 
C 1 113 LYS 113 113 113 LYS LYS C . n 
C 1 114 TYR 114 114 114 TYR TYR C . n 
C 1 115 ALA 115 115 115 ALA ALA C . n 
C 1 116 ALA 116 116 116 ALA ALA C . n 
C 1 117 GLU 117 117 117 GLU GLU C . n 
C 1 118 LEU 118 118 118 LEU LEU C . n 
C 1 119 HIS 119 119 119 HIS HIS C . n 
C 1 120 LEU 120 120 120 LEU LEU C . n 
C 1 121 VAL 121 121 121 VAL VAL C . n 
C 1 122 HIS 122 122 122 HIS HIS C . n 
C 1 123 TRP 123 123 123 TRP TRP C . n 
C 1 124 ASN 124 124 124 ASN ASN C . n 
C 1 125 THR 125 125 125 THR THR C . n 
C 1 126 LYS 126 127 127 LYS LYS C . n 
C 1 127 TYR 127 128 128 TYR TYR C . n 
C 1 128 GLY 128 129 129 GLY GLY C . n 
C 1 129 ASP 129 130 130 ASP ASP C . n 
C 1 130 PHE 130 131 131 PHE PHE C . n 
C 1 131 GLY 131 132 132 GLY GLY C . n 
C 1 132 LYS 132 133 133 LYS LYS C . n 
C 1 133 ALA 133 134 134 ALA ALA C . n 
C 1 134 VAL 134 135 135 VAL VAL C . n 
C 1 135 GLN 135 136 136 GLN GLN C . n 
C 1 136 GLN 136 137 137 GLN GLN C . n 
C 1 137 PRO 137 138 138 PRO PRO C . n 
C 1 138 ASP 138 139 139 ASP ASP C . n 
C 1 139 GLY 139 140 140 GLY GLY C . n 
C 1 140 LEU 140 141 141 LEU LEU C . n 
C 1 141 ALA 141 142 142 ALA ALA C . n 
C 1 142 VAL 142 143 143 VAL VAL C . n 
C 1 143 LEU 143 144 144 LEU LEU C . n 
C 1 144 GLY 144 145 145 GLY GLY C . n 
C 1 145 ILE 145 146 146 ILE ILE C . n 
C 1 146 PHE 146 147 147 PHE PHE C . n 
C 1 147 LEU 147 148 148 LEU LEU C . n 
C 1 148 LYS 148 149 149 LYS LYS C . n 
C 1 149 VAL 149 150 150 VAL VAL C . n 
C 1 150 GLY 150 151 151 GLY GLY C . n 
C 1 151 SER 151 152 152 SER SER C . n 
C 1 152 ALA 152 153 153 ALA ALA C . n 
C 1 153 LYS 153 154 154 LYS LYS C . n 
C 1 154 PRO 154 155 155 PRO PRO C . n 
C 1 155 GLY 155 156 156 GLY GLY C . n 
C 1 156 LEU 156 157 157 LEU LEU C . n 
C 1 157 GLN 157 158 158 GLN GLN C . n 
C 1 158 LYS 158 159 159 LYS LYS C . n 
C 1 159 VAL 159 160 160 VAL VAL C . n 
C 1 160 VAL 160 161 161 VAL VAL C . n 
C 1 161 ASP 161 162 162 ASP ASP C . n 
C 1 162 VAL 162 163 163 VAL VAL C . n 
C 1 163 LEU 163 164 164 LEU LEU C . n 
C 1 164 ASP 164 165 165 ASP ASP C . n 
C 1 165 SER 165 166 166 SER SER C . n 
C 1 166 ILE 166 167 167 ILE ILE C . n 
C 1 167 LYS 167 168 168 LYS LYS C . n 
C 1 168 THR 168 169 169 THR THR C . n 
C 1 169 LYS 169 170 170 LYS LYS C . n 
C 1 170 GLY 170 171 171 GLY GLY C . n 
C 1 171 LYS 171 172 172 LYS LYS C . n 
C 1 172 SER 172 173 173 SER SER C . n 
C 1 173 ALA 173 174 174 ALA ALA C . n 
C 1 174 ASP 174 175 175 ASP ASP C . n 
C 1 175 PHE 175 176 176 PHE PHE C . n 
C 1 176 THR 176 177 177 THR THR C . n 
C 1 177 ASN 177 178 178 ASN ASN C . n 
C 1 178 PHE 178 179 179 PHE PHE C . n 
C 1 179 ASP 179 180 180 ASP ASP C . n 
C 1 180 PRO 180 181 181 PRO PRO C . n 
C 1 181 ARG 181 182 182 ARG ARG C . n 
C 1 182 GLY 182 183 183 GLY GLY C . n 
C 1 183 LEU 183 184 184 LEU LEU C . n 
C 1 184 LEU 184 185 185 LEU LEU C . n 
C 1 185 PRO 185 186 186 PRO PRO C . n 
C 1 186 GLU 186 187 187 GLU GLU C . n 
C 1 187 SER 187 188 188 SER SER C . n 
C 1 188 LEU 188 189 189 LEU LEU C . n 
C 1 189 ASP 189 190 190 ASP ASP C . n 
C 1 190 TYR 190 191 191 TYR TYR C . n 
C 1 191 TRP 191 192 192 TRP TRP C . n 
C 1 192 THR 192 193 193 THR THR C . n 
C 1 193 TYR 193 194 194 TYR TYR C . n 
C 1 194 PRO 194 195 195 PRO PRO C . n 
C 1 195 GLY 195 196 196 GLY GLY C . n 
C 1 196 SER 196 197 197 SER SER C . n 
C 1 197 LEU 197 198 198 LEU LEU C . n 
C 1 198 THR 198 199 199 THR THR C . n 
C 1 199 THR 199 200 200 THR THR C . n 
C 1 200 PRO 200 201 201 PRO PRO C . n 
C 1 201 PRO 201 202 202 PRO PRO C . n 
C 1 202 LEU 202 203 203 LEU LEU C . n 
C 1 203 LEU 203 204 204 LEU LEU C . n 
C 1 204 GLU 204 205 205 GLU GLU C . n 
C 1 205 CYS 205 206 206 CYS CYS C . n 
C 1 206 VAL 206 207 207 VAL VAL C . n 
C 1 207 THR 207 208 208 THR THR C . n 
C 1 208 TRP 208 209 209 TRP TRP C . n 
C 1 209 ILE 209 210 210 ILE ILE C . n 
C 1 210 VAL 210 211 211 VAL VAL C . n 
C 1 211 LEU 211 212 212 LEU LEU C . n 
C 1 212 LYS 212 213 213 LYS LYS C . n 
C 1 213 GLU 213 214 214 GLU GLU C . n 
C 1 214 PRO 214 215 215 PRO PRO C . n 
C 1 215 ILE 215 216 216 ILE ILE C . n 
C 1 216 SER 216 217 217 SER SER C . n 
C 1 217 VAL 217 218 218 VAL VAL C . n 
C 1 218 SER 218 219 219 SER SER C . n 
C 1 219 SER 219 220 220 SER SER C . n 
C 1 220 GLU 220 221 221 GLU GLU C . n 
C 1 221 GLN 221 222 222 GLN GLN C . n 
C 1 222 VAL 222 223 223 VAL VAL C . n 
C 1 223 LEU 223 224 224 LEU LEU C . n 
C 1 224 LYS 224 225 225 LYS LYS C . n 
C 1 225 PHE 225 226 226 PHE PHE C . n 
C 1 226 ARG 226 227 227 ARG ARG C . n 
C 1 227 LYS 227 228 228 LYS LYS C . n 
C 1 228 LEU 228 229 229 LEU LEU C . n 
C 1 229 ASN 229 230 230 ASN ASN C . n 
C 1 230 PHE 230 231 231 PHE PHE C . n 
C 1 231 ASN 231 232 232 ASN ASN C . n 
C 1 232 GLY 232 233 233 GLY GLY C . n 
C 1 233 GLU 233 234 234 GLU GLU C . n 
C 1 234 GLY 234 235 235 GLY GLY C . n 
C 1 235 GLU 235 236 236 GLU GLU C . n 
C 1 236 PRO 236 237 237 PRO PRO C . n 
C 1 237 GLU 237 238 238 GLU GLU C . n 
C 1 238 GLU 238 239 239 GLU GLU C . n 
C 1 239 LEU 239 240 240 LEU LEU C . n 
C 1 240 MET 240 241 241 MET MET C . n 
C 1 241 VAL 241 242 242 VAL VAL C . n 
C 1 242 ASP 242 243 243 ASP ASP C . n 
C 1 243 ASN 243 244 244 ASN ASN C . n 
C 1 244 TRP 244 245 245 TRP TRP C . n 
C 1 245 ARG 245 246 246 ARG ARG C . n 
C 1 246 PRO 246 247 247 PRO PRO C . n 
C 1 247 ALA 247 248 248 ALA ALA C . n 
C 1 248 GLN 248 249 249 GLN GLN C . n 
C 1 249 PRO 249 250 250 PRO PRO C . n 
C 1 250 LEU 250 251 251 LEU LEU C . n 
C 1 251 LYS 251 252 252 LYS LYS C . n 
C 1 252 ASN 252 253 253 ASN ASN C . n 
C 1 253 ARG 253 254 254 ARG ARG C . n 
C 1 254 GLN 254 255 255 GLN GLN C . n 
C 1 255 ILE 255 256 256 ILE ILE C . n 
C 1 256 LYS 256 257 257 LYS LYS C . n 
C 1 257 ALA 257 258 258 ALA ALA C . n 
C 1 258 SER 258 259 259 SER SER C . n 
C 1 259 PHE 259 260 260 PHE PHE C . n 
C 1 260 LYS 260 261 261 LYS LYS C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   HIS 3   3   3   HIS HIS D . n 
D 1 4   HIS 4   4   4   HIS HIS D . n 
D 1 5   TRP 5   5   5   TRP TRP D . n 
D 1 6   GLY 6   6   6   GLY GLY D . n 
D 1 7   TYR 7   7   7   TYR TYR D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  HIS 10  10  10  HIS HIS D . n 
D 1 11  ASN 11  11  11  ASN ASN D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  GLU 14  14  14  GLU GLU D . n 
D 1 15  HIS 15  15  15  HIS HIS D . n 
D 1 16  TRP 16  16  16  TRP TRP D . n 
D 1 17  HIS 17  17  17  HIS HIS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  ASP 19  19  19  ASP ASP D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  PRO 21  21  21  PRO PRO D . n 
D 1 22  ILE 22  22  22  ILE ILE D . n 
D 1 23  ALA 23  23  23  ALA ALA D . n 
D 1 24  LYS 24  24  24  LYS LYS D . n 
D 1 25  GLY 25  25  25  GLY GLY D . n 
D 1 26  GLU 26  26  26  GLU GLU D . n 
D 1 27  ARG 27  27  27  ARG ARG D . n 
D 1 28  GLN 28  28  28  GLN GLN D . n 
D 1 29  SER 29  29  29  SER SER D . n 
D 1 30  PRO 30  30  30  PRO PRO D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  ASP 32  32  32  ASP ASP D . n 
D 1 33  ILE 33  33  33  ILE ILE D . n 
D 1 34  ASP 34  34  34  ASP ASP D . n 
D 1 35  THR 35  35  35  THR THR D . n 
D 1 36  HIS 36  36  36  HIS HIS D . n 
D 1 37  THR 37  37  37  THR THR D . n 
D 1 38  ALA 38  38  38  ALA ALA D . n 
D 1 39  LYS 39  39  39  LYS LYS D . n 
D 1 40  TYR 40  40  40  TYR TYR D . n 
D 1 41  ASP 41  41  41  ASP ASP D . n 
D 1 42  PRO 42  42  42  PRO PRO D . n 
D 1 43  SER 43  43  43  SER SER D . n 
D 1 44  LEU 44  44  44  LEU LEU D . n 
D 1 45  LYS 45  45  45  LYS LYS D . n 
D 1 46  PRO 46  46  46  PRO PRO D . n 
D 1 47  LEU 47  47  47  LEU LEU D . n 
D 1 48  SER 48  48  48  SER SER D . n 
D 1 49  VAL 49  49  49  VAL VAL D . n 
D 1 50  SER 50  50  50  SER SER D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  GLN 53  53  53  GLN GLN D . n 
D 1 54  ALA 54  54  54  ALA ALA D . n 
D 1 55  THR 55  55  55  THR THR D . n 
D 1 56  SER 56  56  56  SER SER D . n 
D 1 57  LEU 57  57  57  LEU LEU D . n 
D 1 58  ARG 58  58  58  ARG ARG D . n 
D 1 59  ILE 59  59  59  ILE ILE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  ASN 61  61  61  ASN ASN D . n 
D 1 62  ASN 62  62  62  ASN ASN D . n 
D 1 63  GLY 63  63  63  GLY GLY D . n 
D 1 64  HIS 64  64  64  HIS HIS D . n 
D 1 65  ALA 65  65  65  ALA ALA D . n 
D 1 66  PHE 66  66  66  PHE PHE D . n 
D 1 67  ASN 67  67  67  ASN ASN D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  GLU 69  69  69  GLU GLU D . n 
D 1 70  PHE 70  70  70  PHE PHE D . n 
D 1 71  ASP 71  71  71  ASP ASP D . n 
D 1 72  ASP 72  72  72  ASP ASP D . n 
D 1 73  SER 73  73  73  SER SER D . n 
D 1 74  GLN 74  74  74  GLN GLN D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  LYS 76  76  76  LYS LYS D . n 
D 1 77  ALA 77  77  77  ALA ALA D . n 
D 1 78  VAL 78  78  78  VAL VAL D . n 
D 1 79  LEU 79  79  79  LEU LEU D . n 
D 1 80  LYS 80  80  80  LYS LYS D . n 
D 1 81  GLY 81  81  81  GLY GLY D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  PRO 83  83  83  PRO PRO D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  ASP 85  85  85  ASP ASP D . n 
D 1 86  GLY 86  86  86  GLY GLY D . n 
D 1 87  THR 87  87  87  THR THR D . n 
D 1 88  TYR 88  88  88  TYR TYR D . n 
D 1 89  ARG 89  89  89  ARG ARG D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  ILE 91  91  91  ILE ILE D . n 
D 1 92  GLN 92  92  92  GLN GLN D . n 
D 1 93  PHE 93  93  93  PHE PHE D . n 
D 1 94  HIS 94  94  94  HIS HIS D . n 
D 1 95  PHE 95  95  95  PHE PHE D . n 
D 1 96  HIS 96  96  96  HIS HIS D . n 
D 1 97  TRP 97  97  97  TRP TRP D . n 
D 1 98  GLY 98  98  98  GLY GLY D . n 
D 1 99  SER 99  99  99  SER SER D . n 
D 1 100 LEU 100 100 100 LEU LEU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 GLN 103 103 103 GLN GLN D . n 
D 1 104 GLY 104 104 104 GLY GLY D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 GLU 106 106 106 GLU GLU D . n 
D 1 107 HIS 107 107 107 HIS HIS D . n 
D 1 108 THR 108 108 108 THR THR D . n 
D 1 109 VAL 109 109 109 VAL VAL D . n 
D 1 110 ASP 110 110 110 ASP ASP D . n 
D 1 111 LYS 111 111 111 LYS LYS D . n 
D 1 112 LYS 112 112 112 LYS LYS D . n 
D 1 113 LYS 113 113 113 LYS LYS D . n 
D 1 114 TYR 114 114 114 TYR TYR D . n 
D 1 115 ALA 115 115 115 ALA ALA D . n 
D 1 116 ALA 116 116 116 ALA ALA D . n 
D 1 117 GLU 117 117 117 GLU GLU D . n 
D 1 118 LEU 118 118 118 LEU LEU D . n 
D 1 119 HIS 119 119 119 HIS HIS D . n 
D 1 120 LEU 120 120 120 LEU LEU D . n 
D 1 121 VAL 121 121 121 VAL VAL D . n 
D 1 122 HIS 122 122 122 HIS HIS D . n 
D 1 123 TRP 123 123 123 TRP TRP D . n 
D 1 124 ASN 124 124 124 ASN ASN D . n 
D 1 125 THR 125 125 125 THR THR D . n 
D 1 126 LYS 126 127 127 LYS LYS D . n 
D 1 127 TYR 127 128 128 TYR TYR D . n 
D 1 128 GLY 128 129 129 GLY GLY D . n 
D 1 129 ASP 129 130 130 ASP ASP D . n 
D 1 130 PHE 130 131 131 PHE PHE D . n 
D 1 131 GLY 131 132 132 GLY GLY D . n 
D 1 132 LYS 132 133 133 LYS LYS D . n 
D 1 133 ALA 133 134 134 ALA ALA D . n 
D 1 134 VAL 134 135 135 VAL VAL D . n 
D 1 135 GLN 135 136 136 GLN GLN D . n 
D 1 136 GLN 136 137 137 GLN GLN D . n 
D 1 137 PRO 137 138 138 PRO PRO D . n 
D 1 138 ASP 138 139 139 ASP ASP D . n 
D 1 139 GLY 139 140 140 GLY GLY D . n 
D 1 140 LEU 140 141 141 LEU LEU D . n 
D 1 141 ALA 141 142 142 ALA ALA D . n 
D 1 142 VAL 142 143 143 VAL VAL D . n 
D 1 143 LEU 143 144 144 LEU LEU D . n 
D 1 144 GLY 144 145 145 GLY GLY D . n 
D 1 145 ILE 145 146 146 ILE ILE D . n 
D 1 146 PHE 146 147 147 PHE PHE D . n 
D 1 147 LEU 147 148 148 LEU LEU D . n 
D 1 148 LYS 148 149 149 LYS LYS D . n 
D 1 149 VAL 149 150 150 VAL VAL D . n 
D 1 150 GLY 150 151 151 GLY GLY D . n 
D 1 151 SER 151 152 152 SER SER D . n 
D 1 152 ALA 152 153 153 ALA ALA D . n 
D 1 153 LYS 153 154 154 LYS LYS D . n 
D 1 154 PRO 154 155 155 PRO PRO D . n 
D 1 155 GLY 155 156 156 GLY GLY D . n 
D 1 156 LEU 156 157 157 LEU LEU D . n 
D 1 157 GLN 157 158 158 GLN GLN D . n 
D 1 158 LYS 158 159 159 LYS LYS D . n 
D 1 159 VAL 159 160 160 VAL VAL D . n 
D 1 160 VAL 160 161 161 VAL VAL D . n 
D 1 161 ASP 161 162 162 ASP ASP D . n 
D 1 162 VAL 162 163 163 VAL VAL D . n 
D 1 163 LEU 163 164 164 LEU LEU D . n 
D 1 164 ASP 164 165 165 ASP ASP D . n 
D 1 165 SER 165 166 166 SER SER D . n 
D 1 166 ILE 166 167 167 ILE ILE D . n 
D 1 167 LYS 167 168 168 LYS LYS D . n 
D 1 168 THR 168 169 169 THR THR D . n 
D 1 169 LYS 169 170 170 LYS LYS D . n 
D 1 170 GLY 170 171 171 GLY GLY D . n 
D 1 171 LYS 171 172 172 LYS LYS D . n 
D 1 172 SER 172 173 173 SER SER D . n 
D 1 173 ALA 173 174 174 ALA ALA D . n 
D 1 174 ASP 174 175 175 ASP ASP D . n 
D 1 175 PHE 175 176 176 PHE PHE D . n 
D 1 176 THR 176 177 177 THR THR D . n 
D 1 177 ASN 177 178 178 ASN ASN D . n 
D 1 178 PHE 178 179 179 PHE PHE D . n 
D 1 179 ASP 179 180 180 ASP ASP D . n 
D 1 180 PRO 180 181 181 PRO PRO D . n 
D 1 181 ARG 181 182 182 ARG ARG D . n 
D 1 182 GLY 182 183 183 GLY GLY D . n 
D 1 183 LEU 183 184 184 LEU LEU D . n 
D 1 184 LEU 184 185 185 LEU LEU D . n 
D 1 185 PRO 185 186 186 PRO PRO D . n 
D 1 186 GLU 186 187 187 GLU GLU D . n 
D 1 187 SER 187 188 188 SER SER D . n 
D 1 188 LEU 188 189 189 LEU LEU D . n 
D 1 189 ASP 189 190 190 ASP ASP D . n 
D 1 190 TYR 190 191 191 TYR TYR D . n 
D 1 191 TRP 191 192 192 TRP TRP D . n 
D 1 192 THR 192 193 193 THR THR D . n 
D 1 193 TYR 193 194 194 TYR TYR D . n 
D 1 194 PRO 194 195 195 PRO PRO D . n 
D 1 195 GLY 195 196 196 GLY GLY D . n 
D 1 196 SER 196 197 197 SER SER D . n 
D 1 197 LEU 197 198 198 LEU LEU D . n 
D 1 198 THR 198 199 199 THR THR D . n 
D 1 199 THR 199 200 200 THR THR D . n 
D 1 200 PRO 200 201 201 PRO PRO D . n 
D 1 201 PRO 201 202 202 PRO PRO D . n 
D 1 202 LEU 202 203 203 LEU LEU D . n 
D 1 203 LEU 203 204 204 LEU LEU D . n 
D 1 204 GLU 204 205 205 GLU GLU D . n 
D 1 205 CYS 205 206 206 CYS CYS D . n 
D 1 206 VAL 206 207 207 VAL VAL D . n 
D 1 207 THR 207 208 208 THR THR D . n 
D 1 208 TRP 208 209 209 TRP TRP D . n 
D 1 209 ILE 209 210 210 ILE ILE D . n 
D 1 210 VAL 210 211 211 VAL VAL D . n 
D 1 211 LEU 211 212 212 LEU LEU D . n 
D 1 212 LYS 212 213 213 LYS LYS D . n 
D 1 213 GLU 213 214 214 GLU GLU D . n 
D 1 214 PRO 214 215 215 PRO PRO D . n 
D 1 215 ILE 215 216 216 ILE ILE D . n 
D 1 216 SER 216 217 217 SER SER D . n 
D 1 217 VAL 217 218 218 VAL VAL D . n 
D 1 218 SER 218 219 219 SER SER D . n 
D 1 219 SER 219 220 220 SER SER D . n 
D 1 220 GLU 220 221 221 GLU GLU D . n 
D 1 221 GLN 221 222 222 GLN GLN D . n 
D 1 222 VAL 222 223 223 VAL VAL D . n 
D 1 223 LEU 223 224 224 LEU LEU D . n 
D 1 224 LYS 224 225 225 LYS LYS D . n 
D 1 225 PHE 225 226 226 PHE PHE D . n 
D 1 226 ARG 226 227 227 ARG ARG D . n 
D 1 227 LYS 227 228 228 LYS LYS D . n 
D 1 228 LEU 228 229 229 LEU LEU D . n 
D 1 229 ASN 229 230 230 ASN ASN D . n 
D 1 230 PHE 230 231 231 PHE PHE D . n 
D 1 231 ASN 231 232 232 ASN ASN D . n 
D 1 232 GLY 232 233 233 GLY GLY D . n 
D 1 233 GLU 233 234 234 GLU GLU D . n 
D 1 234 GLY 234 235 235 GLY GLY D . n 
D 1 235 GLU 235 236 236 GLU GLU D . n 
D 1 236 PRO 236 237 237 PRO PRO D . n 
D 1 237 GLU 237 238 238 GLU GLU D . n 
D 1 238 GLU 238 239 239 GLU GLU D . n 
D 1 239 LEU 239 240 240 LEU LEU D . n 
D 1 240 MET 240 241 241 MET MET D . n 
D 1 241 VAL 241 242 242 VAL VAL D . n 
D 1 242 ASP 242 243 243 ASP ASP D . n 
D 1 243 ASN 243 244 244 ASN ASN D . n 
D 1 244 TRP 244 245 245 TRP TRP D . n 
D 1 245 ARG 245 246 246 ARG ARG D . n 
D 1 246 PRO 246 247 247 PRO PRO D . n 
D 1 247 ALA 247 248 248 ALA ALA D . n 
D 1 248 GLN 248 249 249 GLN GLN D . n 
D 1 249 PRO 249 250 250 PRO PRO D . n 
D 1 250 LEU 250 251 251 LEU LEU D . n 
D 1 251 LYS 251 252 252 LYS LYS D . n 
D 1 252 ASN 252 253 253 ASN ASN D . n 
D 1 253 ARG 253 254 254 ARG ARG D . n 
D 1 254 GLN 254 255 255 GLN GLN D . n 
D 1 255 ILE 255 256 256 ILE ILE D . n 
D 1 256 LYS 256 257 257 LYS LYS D . n 
D 1 257 ALA 257 258 258 ALA ALA D . n 
D 1 258 SER 258 259 259 SER SER D . n 
D 1 259 PHE 259 260 260 PHE PHE D . n 
D 1 260 LYS 260 261 261 LYS LYS D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 ZN  1   301 2    ZN  ZN  A . 
F 3 WWX 1   302 1    WWX WWX A . 
G 4 DMS 1   303 2    DMS DMS A . 
H 5 BCN 1   304 4    BCN BCN A . 
I 2 ZN  1   301 3    ZN  ZN  B . 
J 3 WWX 1   302 2    WWX WWX B . 
K 4 DMS 1   303 1    DMS DMS B . 
L 5 BCN 1   304 3    BCN BCN B . 
M 2 ZN  1   301 1    ZN  ZN  C . 
N 3 WWX 1   302 3    WWX WWX C . 
O 4 DMS 1   303 4    DMS DMS C . 
P 5 BCN 1   304 2    BCN BCN C . 
Q 2 ZN  1   301 4    ZN  ZN  D . 
R 3 WWX 1   302 4    WWX WWX D . 
S 4 DMS 1   303 3    DMS DMS D . 
T 5 BCN 1   304 1    BCN BCN D . 
U 6 HOH 1   401 1    HOH HOH A . 
U 6 HOH 2   402 5    HOH HOH A . 
U 6 HOH 3   403 9    HOH HOH A . 
U 6 HOH 4   404 16   HOH HOH A . 
U 6 HOH 5   405 17   HOH HOH A . 
U 6 HOH 6   406 19   HOH HOH A . 
U 6 HOH 7   407 26   HOH HOH A . 
U 6 HOH 8   408 27   HOH HOH A . 
U 6 HOH 9   409 31   HOH HOH A . 
U 6 HOH 10  410 36   HOH HOH A . 
U 6 HOH 11  411 37   HOH HOH A . 
U 6 HOH 12  412 40   HOH HOH A . 
U 6 HOH 13  413 41   HOH HOH A . 
U 6 HOH 14  414 44   HOH HOH A . 
U 6 HOH 15  415 52   HOH HOH A . 
U 6 HOH 16  416 53   HOH HOH A . 
U 6 HOH 17  417 57   HOH HOH A . 
U 6 HOH 18  418 67   HOH HOH A . 
U 6 HOH 19  419 72   HOH HOH A . 
U 6 HOH 20  420 76   HOH HOH A . 
U 6 HOH 21  421 80   HOH HOH A . 
U 6 HOH 22  422 85   HOH HOH A . 
U 6 HOH 23  423 87   HOH HOH A . 
U 6 HOH 24  424 92   HOH HOH A . 
U 6 HOH 25  425 94   HOH HOH A . 
U 6 HOH 26  426 96   HOH HOH A . 
U 6 HOH 27  427 97   HOH HOH A . 
U 6 HOH 28  428 104  HOH HOH A . 
U 6 HOH 29  429 115  HOH HOH A . 
U 6 HOH 30  430 117  HOH HOH A . 
U 6 HOH 31  431 131  HOH HOH A . 
U 6 HOH 32  432 137  HOH HOH A . 
U 6 HOH 33  433 139  HOH HOH A . 
U 6 HOH 34  434 141  HOH HOH A . 
U 6 HOH 35  435 143  HOH HOH A . 
U 6 HOH 36  436 153  HOH HOH A . 
U 6 HOH 37  437 160  HOH HOH A . 
U 6 HOH 38  438 162  HOH HOH A . 
U 6 HOH 39  439 164  HOH HOH A . 
U 6 HOH 40  440 166  HOH HOH A . 
U 6 HOH 41  441 173  HOH HOH A . 
U 6 HOH 42  442 178  HOH HOH A . 
U 6 HOH 43  443 187  HOH HOH A . 
U 6 HOH 44  444 190  HOH HOH A . 
U 6 HOH 45  445 192  HOH HOH A . 
U 6 HOH 46  446 195  HOH HOH A . 
U 6 HOH 47  447 204  HOH HOH A . 
U 6 HOH 48  448 206  HOH HOH A . 
U 6 HOH 49  449 207  HOH HOH A . 
U 6 HOH 50  450 218  HOH HOH A . 
U 6 HOH 51  451 226  HOH HOH A . 
U 6 HOH 52  452 229  HOH HOH A . 
U 6 HOH 53  453 232  HOH HOH A . 
U 6 HOH 54  454 234  HOH HOH A . 
U 6 HOH 55  455 238  HOH HOH A . 
U 6 HOH 56  456 244  HOH HOH A . 
U 6 HOH 57  457 245  HOH HOH A . 
U 6 HOH 58  458 247  HOH HOH A . 
U 6 HOH 59  459 250  HOH HOH A . 
U 6 HOH 60  460 258  HOH HOH A . 
U 6 HOH 61  461 261  HOH HOH A . 
U 6 HOH 62  462 267  HOH HOH A . 
U 6 HOH 63  463 270  HOH HOH A . 
U 6 HOH 64  464 278  HOH HOH A . 
U 6 HOH 65  465 281  HOH HOH A . 
U 6 HOH 66  466 283  HOH HOH A . 
U 6 HOH 67  467 285  HOH HOH A . 
U 6 HOH 68  468 286  HOH HOH A . 
U 6 HOH 69  469 290  HOH HOH A . 
U 6 HOH 70  470 297  HOH HOH A . 
U 6 HOH 71  471 299  HOH HOH A . 
U 6 HOH 72  472 302  HOH HOH A . 
U 6 HOH 73  473 304  HOH HOH A . 
U 6 HOH 74  474 308  HOH HOH A . 
U 6 HOH 75  475 310  HOH HOH A . 
U 6 HOH 76  476 312  HOH HOH A . 
U 6 HOH 77  477 315  HOH HOH A . 
U 6 HOH 78  478 317  HOH HOH A . 
U 6 HOH 79  479 321  HOH HOH A . 
U 6 HOH 80  480 323  HOH HOH A . 
U 6 HOH 81  481 333  HOH HOH A . 
U 6 HOH 82  482 335  HOH HOH A . 
U 6 HOH 83  483 336  HOH HOH A . 
U 6 HOH 84  484 346  HOH HOH A . 
U 6 HOH 85  485 351  HOH HOH A . 
U 6 HOH 86  486 357  HOH HOH A . 
U 6 HOH 87  487 358  HOH HOH A . 
U 6 HOH 88  488 364  HOH HOH A . 
U 6 HOH 89  489 365  HOH HOH A . 
U 6 HOH 90  490 368  HOH HOH A . 
U 6 HOH 91  491 369  HOH HOH A . 
U 6 HOH 92  492 374  HOH HOH A . 
U 6 HOH 93  493 376  HOH HOH A . 
U 6 HOH 94  494 387  HOH HOH A . 
U 6 HOH 95  495 390  HOH HOH A . 
U 6 HOH 96  496 392  HOH HOH A . 
U 6 HOH 97  497 397  HOH HOH A . 
U 6 HOH 98  498 401  HOH HOH A . 
U 6 HOH 99  499 405  HOH HOH A . 
U 6 HOH 100 500 406  HOH HOH A . 
U 6 HOH 101 501 415  HOH HOH A . 
U 6 HOH 102 502 419  HOH HOH A . 
U 6 HOH 103 503 423  HOH HOH A . 
U 6 HOH 104 504 431  HOH HOH A . 
U 6 HOH 105 505 433  HOH HOH A . 
U 6 HOH 106 506 440  HOH HOH A . 
U 6 HOH 107 507 442  HOH HOH A . 
U 6 HOH 108 508 447  HOH HOH A . 
U 6 HOH 109 509 455  HOH HOH A . 
U 6 HOH 110 510 460  HOH HOH A . 
U 6 HOH 111 511 461  HOH HOH A . 
U 6 HOH 112 512 462  HOH HOH A . 
U 6 HOH 113 513 464  HOH HOH A . 
U 6 HOH 114 514 475  HOH HOH A . 
U 6 HOH 115 515 481  HOH HOH A . 
U 6 HOH 116 516 493  HOH HOH A . 
U 6 HOH 117 517 502  HOH HOH A . 
U 6 HOH 118 518 505  HOH HOH A . 
U 6 HOH 119 519 506  HOH HOH A . 
U 6 HOH 120 520 517  HOH HOH A . 
U 6 HOH 121 521 518  HOH HOH A . 
U 6 HOH 122 522 535  HOH HOH A . 
U 6 HOH 123 523 539  HOH HOH A . 
U 6 HOH 124 524 541  HOH HOH A . 
U 6 HOH 125 525 543  HOH HOH A . 
U 6 HOH 126 526 545  HOH HOH A . 
U 6 HOH 127 527 548  HOH HOH A . 
U 6 HOH 128 528 549  HOH HOH A . 
U 6 HOH 129 529 550  HOH HOH A . 
U 6 HOH 130 530 560  HOH HOH A . 
U 6 HOH 131 531 563  HOH HOH A . 
U 6 HOH 132 532 568  HOH HOH A . 
U 6 HOH 133 533 571  HOH HOH A . 
U 6 HOH 134 534 579  HOH HOH A . 
U 6 HOH 135 535 583  HOH HOH A . 
U 6 HOH 136 536 589  HOH HOH A . 
U 6 HOH 137 537 591  HOH HOH A . 
U 6 HOH 138 538 592  HOH HOH A . 
U 6 HOH 139 539 598  HOH HOH A . 
U 6 HOH 140 540 600  HOH HOH A . 
U 6 HOH 141 541 601  HOH HOH A . 
U 6 HOH 142 542 606  HOH HOH A . 
U 6 HOH 143 543 611  HOH HOH A . 
U 6 HOH 144 544 613  HOH HOH A . 
U 6 HOH 145 545 614  HOH HOH A . 
U 6 HOH 146 546 615  HOH HOH A . 
U 6 HOH 147 547 622  HOH HOH A . 
U 6 HOH 148 548 627  HOH HOH A . 
U 6 HOH 149 549 628  HOH HOH A . 
U 6 HOH 150 550 631  HOH HOH A . 
U 6 HOH 151 551 633  HOH HOH A . 
U 6 HOH 152 552 636  HOH HOH A . 
U 6 HOH 153 553 644  HOH HOH A . 
U 6 HOH 154 554 648  HOH HOH A . 
U 6 HOH 155 555 649  HOH HOH A . 
U 6 HOH 156 556 650  HOH HOH A . 
U 6 HOH 157 557 651  HOH HOH A . 
U 6 HOH 158 558 652  HOH HOH A . 
U 6 HOH 159 559 653  HOH HOH A . 
U 6 HOH 160 560 660  HOH HOH A . 
U 6 HOH 161 561 675  HOH HOH A . 
U 6 HOH 162 562 680  HOH HOH A . 
U 6 HOH 163 563 681  HOH HOH A . 
U 6 HOH 164 564 684  HOH HOH A . 
U 6 HOH 165 565 685  HOH HOH A . 
U 6 HOH 166 566 690  HOH HOH A . 
U 6 HOH 167 567 693  HOH HOH A . 
U 6 HOH 168 568 697  HOH HOH A . 
U 6 HOH 169 569 703  HOH HOH A . 
U 6 HOH 170 570 705  HOH HOH A . 
U 6 HOH 171 571 707  HOH HOH A . 
U 6 HOH 172 572 711  HOH HOH A . 
U 6 HOH 173 573 717  HOH HOH A . 
U 6 HOH 174 574 721  HOH HOH A . 
U 6 HOH 175 575 730  HOH HOH A . 
U 6 HOH 176 576 731  HOH HOH A . 
U 6 HOH 177 577 733  HOH HOH A . 
U 6 HOH 178 578 736  HOH HOH A . 
U 6 HOH 179 579 738  HOH HOH A . 
U 6 HOH 180 580 740  HOH HOH A . 
U 6 HOH 181 581 744  HOH HOH A . 
U 6 HOH 182 582 745  HOH HOH A . 
U 6 HOH 183 583 746  HOH HOH A . 
U 6 HOH 184 584 748  HOH HOH A . 
U 6 HOH 185 585 750  HOH HOH A . 
U 6 HOH 186 586 752  HOH HOH A . 
U 6 HOH 187 587 754  HOH HOH A . 
U 6 HOH 188 588 755  HOH HOH A . 
U 6 HOH 189 589 757  HOH HOH A . 
U 6 HOH 190 590 759  HOH HOH A . 
U 6 HOH 191 591 761  HOH HOH A . 
U 6 HOH 192 592 762  HOH HOH A . 
U 6 HOH 193 593 764  HOH HOH A . 
U 6 HOH 194 594 781  HOH HOH A . 
U 6 HOH 195 595 786  HOH HOH A . 
U 6 HOH 196 596 791  HOH HOH A . 
U 6 HOH 197 597 795  HOH HOH A . 
U 6 HOH 198 598 804  HOH HOH A . 
U 6 HOH 199 599 810  HOH HOH A . 
U 6 HOH 200 600 823  HOH HOH A . 
U 6 HOH 201 601 824  HOH HOH A . 
U 6 HOH 202 602 826  HOH HOH A . 
U 6 HOH 203 603 836  HOH HOH A . 
U 6 HOH 204 604 839  HOH HOH A . 
U 6 HOH 205 605 840  HOH HOH A . 
U 6 HOH 206 606 842  HOH HOH A . 
U 6 HOH 207 607 847  HOH HOH A . 
U 6 HOH 208 608 856  HOH HOH A . 
U 6 HOH 209 609 858  HOH HOH A . 
U 6 HOH 210 610 861  HOH HOH A . 
U 6 HOH 211 611 863  HOH HOH A . 
U 6 HOH 212 612 865  HOH HOH A . 
U 6 HOH 213 613 866  HOH HOH A . 
U 6 HOH 214 614 867  HOH HOH A . 
U 6 HOH 215 615 869  HOH HOH A . 
U 6 HOH 216 616 871  HOH HOH A . 
U 6 HOH 217 617 873  HOH HOH A . 
U 6 HOH 218 618 874  HOH HOH A . 
U 6 HOH 219 619 877  HOH HOH A . 
U 6 HOH 220 620 888  HOH HOH A . 
U 6 HOH 221 621 891  HOH HOH A . 
U 6 HOH 222 622 903  HOH HOH A . 
U 6 HOH 223 623 905  HOH HOH A . 
U 6 HOH 224 624 916  HOH HOH A . 
U 6 HOH 225 625 917  HOH HOH A . 
U 6 HOH 226 626 924  HOH HOH A . 
U 6 HOH 227 627 926  HOH HOH A . 
U 6 HOH 228 628 930  HOH HOH A . 
U 6 HOH 229 629 934  HOH HOH A . 
U 6 HOH 230 630 939  HOH HOH A . 
U 6 HOH 231 631 944  HOH HOH A . 
U 6 HOH 232 632 956  HOH HOH A . 
U 6 HOH 233 633 957  HOH HOH A . 
U 6 HOH 234 634 958  HOH HOH A . 
U 6 HOH 235 635 962  HOH HOH A . 
U 6 HOH 236 636 965  HOH HOH A . 
U 6 HOH 237 637 967  HOH HOH A . 
U 6 HOH 238 638 968  HOH HOH A . 
U 6 HOH 239 639 972  HOH HOH A . 
U 6 HOH 240 640 989  HOH HOH A . 
U 6 HOH 241 641 991  HOH HOH A . 
U 6 HOH 242 642 993  HOH HOH A . 
U 6 HOH 243 643 995  HOH HOH A . 
U 6 HOH 244 644 997  HOH HOH A . 
U 6 HOH 245 645 998  HOH HOH A . 
U 6 HOH 246 646 999  HOH HOH A . 
U 6 HOH 247 647 1003 HOH HOH A . 
U 6 HOH 248 648 1007 HOH HOH A . 
U 6 HOH 249 649 1008 HOH HOH A . 
U 6 HOH 250 650 1009 HOH HOH A . 
U 6 HOH 251 651 1010 HOH HOH A . 
U 6 HOH 252 652 1011 HOH HOH A . 
V 6 HOH 1   401 2    HOH HOH B . 
V 6 HOH 2   402 6    HOH HOH B . 
V 6 HOH 3   403 10   HOH HOH B . 
V 6 HOH 4   404 15   HOH HOH B . 
V 6 HOH 5   405 18   HOH HOH B . 
V 6 HOH 6   406 22   HOH HOH B . 
V 6 HOH 7   407 25   HOH HOH B . 
V 6 HOH 8   408 28   HOH HOH B . 
V 6 HOH 9   409 32   HOH HOH B . 
V 6 HOH 10  410 35   HOH HOH B . 
V 6 HOH 11  411 38   HOH HOH B . 
V 6 HOH 12  412 39   HOH HOH B . 
V 6 HOH 13  413 42   HOH HOH B . 
V 6 HOH 14  414 43   HOH HOH B . 
V 6 HOH 15  415 51   HOH HOH B . 
V 6 HOH 16  416 54   HOH HOH B . 
V 6 HOH 17  417 58   HOH HOH B . 
V 6 HOH 18  418 68   HOH HOH B . 
V 6 HOH 19  419 71   HOH HOH B . 
V 6 HOH 20  420 75   HOH HOH B . 
V 6 HOH 21  421 79   HOH HOH B . 
V 6 HOH 22  422 86   HOH HOH B . 
V 6 HOH 23  423 88   HOH HOH B . 
V 6 HOH 24  424 91   HOH HOH B . 
V 6 HOH 25  425 93   HOH HOH B . 
V 6 HOH 26  426 95   HOH HOH B . 
V 6 HOH 27  427 98   HOH HOH B . 
V 6 HOH 28  428 103  HOH HOH B . 
V 6 HOH 29  429 116  HOH HOH B . 
V 6 HOH 30  430 118  HOH HOH B . 
V 6 HOH 31  431 132  HOH HOH B . 
V 6 HOH 32  432 138  HOH HOH B . 
V 6 HOH 33  433 140  HOH HOH B . 
V 6 HOH 34  434 142  HOH HOH B . 
V 6 HOH 35  435 144  HOH HOH B . 
V 6 HOH 36  436 154  HOH HOH B . 
V 6 HOH 37  437 159  HOH HOH B . 
V 6 HOH 38  438 161  HOH HOH B . 
V 6 HOH 39  439 163  HOH HOH B . 
V 6 HOH 40  440 165  HOH HOH B . 
V 6 HOH 41  441 174  HOH HOH B . 
V 6 HOH 42  442 177  HOH HOH B . 
V 6 HOH 43  443 188  HOH HOH B . 
V 6 HOH 44  444 189  HOH HOH B . 
V 6 HOH 45  445 191  HOH HOH B . 
V 6 HOH 46  446 196  HOH HOH B . 
V 6 HOH 47  447 203  HOH HOH B . 
V 6 HOH 48  448 205  HOH HOH B . 
V 6 HOH 49  449 208  HOH HOH B . 
V 6 HOH 50  450 213  HOH HOH B . 
V 6 HOH 51  451 219  HOH HOH B . 
V 6 HOH 52  452 220  HOH HOH B . 
V 6 HOH 53  453 225  HOH HOH B . 
V 6 HOH 54  454 230  HOH HOH B . 
V 6 HOH 55  455 233  HOH HOH B . 
V 6 HOH 56  456 237  HOH HOH B . 
V 6 HOH 57  457 243  HOH HOH B . 
V 6 HOH 58  458 246  HOH HOH B . 
V 6 HOH 59  459 248  HOH HOH B . 
V 6 HOH 60  460 249  HOH HOH B . 
V 6 HOH 61  461 256  HOH HOH B . 
V 6 HOH 62  462 257  HOH HOH B . 
V 6 HOH 63  463 262  HOH HOH B . 
V 6 HOH 64  464 264  HOH HOH B . 
V 6 HOH 65  465 268  HOH HOH B . 
V 6 HOH 66  466 269  HOH HOH B . 
V 6 HOH 67  467 277  HOH HOH B . 
V 6 HOH 68  468 282  HOH HOH B . 
V 6 HOH 69  469 284  HOH HOH B . 
V 6 HOH 70  470 287  HOH HOH B . 
V 6 HOH 71  471 288  HOH HOH B . 
V 6 HOH 72  472 289  HOH HOH B . 
V 6 HOH 73  473 298  HOH HOH B . 
V 6 HOH 74  474 300  HOH HOH B . 
V 6 HOH 75  475 301  HOH HOH B . 
V 6 HOH 76  476 303  HOH HOH B . 
V 6 HOH 77  477 307  HOH HOH B . 
V 6 HOH 78  478 311  HOH HOH B . 
V 6 HOH 79  479 313  HOH HOH B . 
V 6 HOH 80  480 314  HOH HOH B . 
V 6 HOH 81  481 316  HOH HOH B . 
V 6 HOH 82  482 320  HOH HOH B . 
V 6 HOH 83  483 322  HOH HOH B . 
V 6 HOH 84  484 332  HOH HOH B . 
V 6 HOH 85  485 334  HOH HOH B . 
V 6 HOH 86  486 337  HOH HOH B . 
V 6 HOH 87  487 345  HOH HOH B . 
V 6 HOH 88  488 347  HOH HOH B . 
V 6 HOH 89  489 350  HOH HOH B . 
V 6 HOH 90  490 359  HOH HOH B . 
V 6 HOH 91  491 360  HOH HOH B . 
V 6 HOH 92  492 363  HOH HOH B . 
V 6 HOH 93  493 366  HOH HOH B . 
V 6 HOH 94  494 367  HOH HOH B . 
V 6 HOH 95  495 372  HOH HOH B . 
V 6 HOH 96  496 373  HOH HOH B . 
V 6 HOH 97  497 375  HOH HOH B . 
V 6 HOH 98  498 388  HOH HOH B . 
V 6 HOH 99  499 389  HOH HOH B . 
V 6 HOH 100 500 391  HOH HOH B . 
V 6 HOH 101 501 396  HOH HOH B . 
V 6 HOH 102 502 398  HOH HOH B . 
V 6 HOH 103 503 402  HOH HOH B . 
V 6 HOH 104 504 403  HOH HOH B . 
V 6 HOH 105 505 404  HOH HOH B . 
V 6 HOH 106 506 407  HOH HOH B . 
V 6 HOH 107 507 414  HOH HOH B . 
V 6 HOH 108 508 420  HOH HOH B . 
V 6 HOH 109 509 422  HOH HOH B . 
V 6 HOH 110 510 424  HOH HOH B . 
V 6 HOH 111 511 425  HOH HOH B . 
V 6 HOH 112 512 428  HOH HOH B . 
V 6 HOH 113 513 435  HOH HOH B . 
V 6 HOH 114 514 437  HOH HOH B . 
V 6 HOH 115 515 445  HOH HOH B . 
V 6 HOH 116 516 451  HOH HOH B . 
V 6 HOH 117 517 458  HOH HOH B . 
V 6 HOH 118 518 463  HOH HOH B . 
V 6 HOH 119 519 465  HOH HOH B . 
V 6 HOH 120 520 467  HOH HOH B . 
V 6 HOH 121 521 470  HOH HOH B . 
V 6 HOH 122 522 474  HOH HOH B . 
V 6 HOH 123 523 478  HOH HOH B . 
V 6 HOH 124 524 479  HOH HOH B . 
V 6 HOH 125 525 482  HOH HOH B . 
V 6 HOH 126 526 483  HOH HOH B . 
V 6 HOH 127 527 485  HOH HOH B . 
V 6 HOH 128 528 486  HOH HOH B . 
V 6 HOH 129 529 491  HOH HOH B . 
V 6 HOH 130 530 492  HOH HOH B . 
V 6 HOH 131 531 495  HOH HOH B . 
V 6 HOH 132 532 503  HOH HOH B . 
V 6 HOH 133 533 504  HOH HOH B . 
V 6 HOH 134 534 509  HOH HOH B . 
V 6 HOH 135 535 513  HOH HOH B . 
V 6 HOH 136 536 514  HOH HOH B . 
V 6 HOH 137 537 515  HOH HOH B . 
V 6 HOH 138 538 516  HOH HOH B . 
V 6 HOH 139 539 519  HOH HOH B . 
V 6 HOH 140 540 523  HOH HOH B . 
V 6 HOH 141 541 525  HOH HOH B . 
V 6 HOH 142 542 526  HOH HOH B . 
V 6 HOH 143 543 527  HOH HOH B . 
V 6 HOH 144 544 529  HOH HOH B . 
V 6 HOH 145 545 530  HOH HOH B . 
V 6 HOH 146 546 531  HOH HOH B . 
V 6 HOH 147 547 533  HOH HOH B . 
V 6 HOH 148 548 540  HOH HOH B . 
V 6 HOH 149 549 554  HOH HOH B . 
V 6 HOH 150 550 562  HOH HOH B . 
V 6 HOH 151 551 564  HOH HOH B . 
V 6 HOH 152 552 565  HOH HOH B . 
V 6 HOH 153 553 567  HOH HOH B . 
V 6 HOH 154 554 569  HOH HOH B . 
V 6 HOH 155 555 572  HOH HOH B . 
V 6 HOH 156 556 577  HOH HOH B . 
V 6 HOH 157 557 578  HOH HOH B . 
V 6 HOH 158 558 584  HOH HOH B . 
V 6 HOH 159 559 593  HOH HOH B . 
V 6 HOH 160 560 609  HOH HOH B . 
V 6 HOH 161 561 610  HOH HOH B . 
V 6 HOH 162 562 618  HOH HOH B . 
V 6 HOH 163 563 632  HOH HOH B . 
V 6 HOH 164 564 638  HOH HOH B . 
V 6 HOH 165 565 639  HOH HOH B . 
V 6 HOH 166 566 640  HOH HOH B . 
V 6 HOH 167 567 641  HOH HOH B . 
V 6 HOH 168 568 643  HOH HOH B . 
V 6 HOH 169 569 647  HOH HOH B . 
V 6 HOH 170 570 654  HOH HOH B . 
V 6 HOH 171 571 655  HOH HOH B . 
V 6 HOH 172 572 661  HOH HOH B . 
V 6 HOH 173 573 663  HOH HOH B . 
V 6 HOH 174 574 669  HOH HOH B . 
V 6 HOH 175 575 671  HOH HOH B . 
V 6 HOH 176 576 673  HOH HOH B . 
V 6 HOH 177 577 678  HOH HOH B . 
V 6 HOH 178 578 686  HOH HOH B . 
V 6 HOH 179 579 687  HOH HOH B . 
V 6 HOH 180 580 691  HOH HOH B . 
V 6 HOH 181 581 699  HOH HOH B . 
V 6 HOH 182 582 700  HOH HOH B . 
V 6 HOH 183 583 701  HOH HOH B . 
V 6 HOH 184 584 710  HOH HOH B . 
V 6 HOH 185 585 713  HOH HOH B . 
V 6 HOH 186 586 714  HOH HOH B . 
V 6 HOH 187 587 715  HOH HOH B . 
V 6 HOH 188 588 719  HOH HOH B . 
V 6 HOH 189 589 722  HOH HOH B . 
V 6 HOH 190 590 732  HOH HOH B . 
V 6 HOH 191 591 735  HOH HOH B . 
V 6 HOH 192 592 739  HOH HOH B . 
V 6 HOH 193 593 756  HOH HOH B . 
V 6 HOH 194 594 763  HOH HOH B . 
V 6 HOH 195 595 765  HOH HOH B . 
V 6 HOH 196 596 766  HOH HOH B . 
V 6 HOH 197 597 773  HOH HOH B . 
V 6 HOH 198 598 774  HOH HOH B . 
V 6 HOH 199 599 777  HOH HOH B . 
V 6 HOH 200 600 778  HOH HOH B . 
V 6 HOH 201 601 780  HOH HOH B . 
V 6 HOH 202 602 782  HOH HOH B . 
V 6 HOH 203 603 788  HOH HOH B . 
V 6 HOH 204 604 789  HOH HOH B . 
V 6 HOH 205 605 792  HOH HOH B . 
V 6 HOH 206 606 794  HOH HOH B . 
V 6 HOH 207 607 796  HOH HOH B . 
V 6 HOH 208 608 798  HOH HOH B . 
V 6 HOH 209 609 802  HOH HOH B . 
V 6 HOH 210 610 806  HOH HOH B . 
V 6 HOH 211 611 808  HOH HOH B . 
V 6 HOH 212 612 809  HOH HOH B . 
V 6 HOH 213 613 812  HOH HOH B . 
V 6 HOH 214 614 813  HOH HOH B . 
V 6 HOH 215 615 815  HOH HOH B . 
V 6 HOH 216 616 822  HOH HOH B . 
V 6 HOH 217 617 830  HOH HOH B . 
V 6 HOH 218 618 832  HOH HOH B . 
V 6 HOH 219 619 834  HOH HOH B . 
V 6 HOH 220 620 843  HOH HOH B . 
V 6 HOH 221 621 844  HOH HOH B . 
V 6 HOH 222 622 849  HOH HOH B . 
V 6 HOH 223 623 851  HOH HOH B . 
V 6 HOH 224 624 852  HOH HOH B . 
V 6 HOH 225 625 853  HOH HOH B . 
V 6 HOH 226 626 855  HOH HOH B . 
V 6 HOH 227 627 859  HOH HOH B . 
V 6 HOH 228 628 860  HOH HOH B . 
V 6 HOH 229 629 864  HOH HOH B . 
V 6 HOH 230 630 872  HOH HOH B . 
V 6 HOH 231 631 876  HOH HOH B . 
V 6 HOH 232 632 880  HOH HOH B . 
V 6 HOH 233 633 881  HOH HOH B . 
V 6 HOH 234 634 882  HOH HOH B . 
V 6 HOH 235 635 883  HOH HOH B . 
V 6 HOH 236 636 885  HOH HOH B . 
V 6 HOH 237 637 889  HOH HOH B . 
V 6 HOH 238 638 892  HOH HOH B . 
V 6 HOH 239 639 893  HOH HOH B . 
V 6 HOH 240 640 894  HOH HOH B . 
V 6 HOH 241 641 896  HOH HOH B . 
V 6 HOH 242 642 904  HOH HOH B . 
V 6 HOH 243 643 906  HOH HOH B . 
V 6 HOH 244 644 910  HOH HOH B . 
V 6 HOH 245 645 919  HOH HOH B . 
V 6 HOH 246 646 920  HOH HOH B . 
V 6 HOH 247 647 923  HOH HOH B . 
V 6 HOH 248 648 929  HOH HOH B . 
V 6 HOH 249 649 935  HOH HOH B . 
V 6 HOH 250 650 936  HOH HOH B . 
V 6 HOH 251 651 938  HOH HOH B . 
V 6 HOH 252 652 942  HOH HOH B . 
V 6 HOH 253 653 946  HOH HOH B . 
V 6 HOH 254 654 954  HOH HOH B . 
V 6 HOH 255 655 960  HOH HOH B . 
V 6 HOH 256 656 961  HOH HOH B . 
V 6 HOH 257 657 964  HOH HOH B . 
V 6 HOH 258 658 973  HOH HOH B . 
V 6 HOH 259 659 978  HOH HOH B . 
V 6 HOH 260 660 979  HOH HOH B . 
V 6 HOH 261 661 980  HOH HOH B . 
V 6 HOH 262 662 990  HOH HOH B . 
V 6 HOH 263 663 994  HOH HOH B . 
V 6 HOH 264 664 1002 HOH HOH B . 
V 6 HOH 265 665 1012 HOH HOH B . 
W 6 HOH 1   401 3    HOH HOH C . 
W 6 HOH 2   402 8    HOH HOH C . 
W 6 HOH 3   403 11   HOH HOH C . 
W 6 HOH 4   404 13   HOH HOH C . 
W 6 HOH 5   405 20   HOH HOH C . 
W 6 HOH 6   406 23   HOH HOH C . 
W 6 HOH 7   407 30   HOH HOH C . 
W 6 HOH 8   408 33   HOH HOH C . 
W 6 HOH 9   409 46   HOH HOH C . 
W 6 HOH 10  410 48   HOH HOH C . 
W 6 HOH 11  411 50   HOH HOH C . 
W 6 HOH 12  412 56   HOH HOH C . 
W 6 HOH 13  413 60   HOH HOH C . 
W 6 HOH 14  414 61   HOH HOH C . 
W 6 HOH 15  415 65   HOH HOH C . 
W 6 HOH 16  416 66   HOH HOH C . 
W 6 HOH 17  417 69   HOH HOH C . 
W 6 HOH 18  418 73   HOH HOH C . 
W 6 HOH 19  419 77   HOH HOH C . 
W 6 HOH 20  420 82   HOH HOH C . 
W 6 HOH 21  421 83   HOH HOH C . 
W 6 HOH 22  422 89   HOH HOH C . 
W 6 HOH 23  423 100  HOH HOH C . 
W 6 HOH 24  424 102  HOH HOH C . 
W 6 HOH 25  425 106  HOH HOH C . 
W 6 HOH 26  426 108  HOH HOH C . 
W 6 HOH 27  427 110  HOH HOH C . 
W 6 HOH 28  428 111  HOH HOH C . 
W 6 HOH 29  429 114  HOH HOH C . 
W 6 HOH 30  430 119  HOH HOH C . 
W 6 HOH 31  431 122  HOH HOH C . 
W 6 HOH 32  432 123  HOH HOH C . 
W 6 HOH 33  433 125  HOH HOH C . 
W 6 HOH 34  434 127  HOH HOH C . 
W 6 HOH 35  435 129  HOH HOH C . 
W 6 HOH 36  436 133  HOH HOH C . 
W 6 HOH 37  437 135  HOH HOH C . 
W 6 HOH 38  438 146  HOH HOH C . 
W 6 HOH 39  439 147  HOH HOH C . 
W 6 HOH 40  440 149  HOH HOH C . 
W 6 HOH 41  441 151  HOH HOH C . 
W 6 HOH 42  442 155  HOH HOH C . 
W 6 HOH 43  443 157  HOH HOH C . 
W 6 HOH 44  444 167  HOH HOH C . 
W 6 HOH 45  445 169  HOH HOH C . 
W 6 HOH 46  446 172  HOH HOH C . 
W 6 HOH 47  447 176  HOH HOH C . 
W 6 HOH 48  448 180  HOH HOH C . 
W 6 HOH 49  449 181  HOH HOH C . 
W 6 HOH 50  450 184  HOH HOH C . 
W 6 HOH 51  451 186  HOH HOH C . 
W 6 HOH 52  452 193  HOH HOH C . 
W 6 HOH 53  453 198  HOH HOH C . 
W 6 HOH 54  454 200  HOH HOH C . 
W 6 HOH 55  455 201  HOH HOH C . 
W 6 HOH 56  456 209  HOH HOH C . 
W 6 HOH 57  457 211  HOH HOH C . 
W 6 HOH 58  458 214  HOH HOH C . 
W 6 HOH 59  459 216  HOH HOH C . 
W 6 HOH 60  460 221  HOH HOH C . 
W 6 HOH 61  461 223  HOH HOH C . 
W 6 HOH 62  462 231  HOH HOH C . 
W 6 HOH 63  463 235  HOH HOH C . 
W 6 HOH 64  464 240  HOH HOH C . 
W 6 HOH 65  465 241  HOH HOH C . 
W 6 HOH 66  466 251  HOH HOH C . 
W 6 HOH 67  467 254  HOH HOH C . 
W 6 HOH 68  468 255  HOH HOH C . 
W 6 HOH 69  469 260  HOH HOH C . 
W 6 HOH 70  470 266  HOH HOH C . 
W 6 HOH 71  471 272  HOH HOH C . 
W 6 HOH 72  472 273  HOH HOH C . 
W 6 HOH 73  473 275  HOH HOH C . 
W 6 HOH 74  474 280  HOH HOH C . 
W 6 HOH 75  475 291  HOH HOH C . 
W 6 HOH 76  476 293  HOH HOH C . 
W 6 HOH 77  477 296  HOH HOH C . 
W 6 HOH 78  478 305  HOH HOH C . 
W 6 HOH 79  479 309  HOH HOH C . 
W 6 HOH 80  480 318  HOH HOH C . 
W 6 HOH 81  481 325  HOH HOH C . 
W 6 HOH 82  482 326  HOH HOH C . 
W 6 HOH 83  483 328  HOH HOH C . 
W 6 HOH 84  484 331  HOH HOH C . 
W 6 HOH 85  485 339  HOH HOH C . 
W 6 HOH 86  486 340  HOH HOH C . 
W 6 HOH 87  487 341  HOH HOH C . 
W 6 HOH 88  488 343  HOH HOH C . 
W 6 HOH 89  489 348  HOH HOH C . 
W 6 HOH 90  490 353  HOH HOH C . 
W 6 HOH 91  491 354  HOH HOH C . 
W 6 HOH 92  492 355  HOH HOH C . 
W 6 HOH 93  493 361  HOH HOH C . 
W 6 HOH 94  494 371  HOH HOH C . 
W 6 HOH 95  495 377  HOH HOH C . 
W 6 HOH 96  496 379  HOH HOH C . 
W 6 HOH 97  497 382  HOH HOH C . 
W 6 HOH 98  498 383  HOH HOH C . 
W 6 HOH 99  499 385  HOH HOH C . 
W 6 HOH 100 500 393  HOH HOH C . 
W 6 HOH 101 501 395  HOH HOH C . 
W 6 HOH 102 502 399  HOH HOH C . 
W 6 HOH 103 503 408  HOH HOH C . 
W 6 HOH 104 504 411  HOH HOH C . 
W 6 HOH 105 505 412  HOH HOH C . 
W 6 HOH 106 506 416  HOH HOH C . 
W 6 HOH 107 507 421  HOH HOH C . 
W 6 HOH 108 508 426  HOH HOH C . 
W 6 HOH 109 509 427  HOH HOH C . 
W 6 HOH 110 510 429  HOH HOH C . 
W 6 HOH 111 511 430  HOH HOH C . 
W 6 HOH 112 512 434  HOH HOH C . 
W 6 HOH 113 513 436  HOH HOH C . 
W 6 HOH 114 514 443  HOH HOH C . 
W 6 HOH 115 515 444  HOH HOH C . 
W 6 HOH 116 516 446  HOH HOH C . 
W 6 HOH 117 517 448  HOH HOH C . 
W 6 HOH 118 518 450  HOH HOH C . 
W 6 HOH 119 519 453  HOH HOH C . 
W 6 HOH 120 520 454  HOH HOH C . 
W 6 HOH 121 521 456  HOH HOH C . 
W 6 HOH 122 522 457  HOH HOH C . 
W 6 HOH 123 523 466  HOH HOH C . 
W 6 HOH 124 524 469  HOH HOH C . 
W 6 HOH 125 525 471  HOH HOH C . 
W 6 HOH 126 526 472  HOH HOH C . 
W 6 HOH 127 527 476  HOH HOH C . 
W 6 HOH 128 528 477  HOH HOH C . 
W 6 HOH 129 529 487  HOH HOH C . 
W 6 HOH 130 530 494  HOH HOH C . 
W 6 HOH 131 531 496  HOH HOH C . 
W 6 HOH 132 532 497  HOH HOH C . 
W 6 HOH 133 533 498  HOH HOH C . 
W 6 HOH 134 534 499  HOH HOH C . 
W 6 HOH 135 535 500  HOH HOH C . 
W 6 HOH 136 536 508  HOH HOH C . 
W 6 HOH 137 537 510  HOH HOH C . 
W 6 HOH 138 538 511  HOH HOH C . 
W 6 HOH 139 539 520  HOH HOH C . 
W 6 HOH 140 540 528  HOH HOH C . 
W 6 HOH 141 541 532  HOH HOH C . 
W 6 HOH 142 542 538  HOH HOH C . 
W 6 HOH 143 543 551  HOH HOH C . 
W 6 HOH 144 544 556  HOH HOH C . 
W 6 HOH 145 545 561  HOH HOH C . 
W 6 HOH 146 546 570  HOH HOH C . 
W 6 HOH 147 547 573  HOH HOH C . 
W 6 HOH 148 548 574  HOH HOH C . 
W 6 HOH 149 549 575  HOH HOH C . 
W 6 HOH 150 550 576  HOH HOH C . 
W 6 HOH 151 551 582  HOH HOH C . 
W 6 HOH 152 552 590  HOH HOH C . 
W 6 HOH 153 553 596  HOH HOH C . 
W 6 HOH 154 554 604  HOH HOH C . 
W 6 HOH 155 555 605  HOH HOH C . 
W 6 HOH 156 556 607  HOH HOH C . 
W 6 HOH 157 557 608  HOH HOH C . 
W 6 HOH 158 558 612  HOH HOH C . 
W 6 HOH 159 559 616  HOH HOH C . 
W 6 HOH 160 560 617  HOH HOH C . 
W 6 HOH 161 561 621  HOH HOH C . 
W 6 HOH 162 562 630  HOH HOH C . 
W 6 HOH 163 563 635  HOH HOH C . 
W 6 HOH 164 564 637  HOH HOH C . 
W 6 HOH 165 565 646  HOH HOH C . 
W 6 HOH 166 566 656  HOH HOH C . 
W 6 HOH 167 567 662  HOH HOH C . 
W 6 HOH 168 568 664  HOH HOH C . 
W 6 HOH 169 569 665  HOH HOH C . 
W 6 HOH 170 570 666  HOH HOH C . 
W 6 HOH 171 571 668  HOH HOH C . 
W 6 HOH 172 572 676  HOH HOH C . 
W 6 HOH 173 573 679  HOH HOH C . 
W 6 HOH 174 574 682  HOH HOH C . 
W 6 HOH 175 575 683  HOH HOH C . 
W 6 HOH 176 576 688  HOH HOH C . 
W 6 HOH 177 577 689  HOH HOH C . 
W 6 HOH 178 578 694  HOH HOH C . 
W 6 HOH 179 579 695  HOH HOH C . 
W 6 HOH 180 580 698  HOH HOH C . 
W 6 HOH 181 581 702  HOH HOH C . 
W 6 HOH 182 582 704  HOH HOH C . 
W 6 HOH 183 583 708  HOH HOH C . 
W 6 HOH 184 584 712  HOH HOH C . 
W 6 HOH 185 585 720  HOH HOH C . 
W 6 HOH 186 586 723  HOH HOH C . 
W 6 HOH 187 587 724  HOH HOH C . 
W 6 HOH 188 588 725  HOH HOH C . 
W 6 HOH 189 589 726  HOH HOH C . 
W 6 HOH 190 590 727  HOH HOH C . 
W 6 HOH 191 591 729  HOH HOH C . 
W 6 HOH 192 592 743  HOH HOH C . 
W 6 HOH 193 593 747  HOH HOH C . 
W 6 HOH 194 594 749  HOH HOH C . 
W 6 HOH 195 595 751  HOH HOH C . 
W 6 HOH 196 596 753  HOH HOH C . 
W 6 HOH 197 597 760  HOH HOH C . 
W 6 HOH 198 598 767  HOH HOH C . 
W 6 HOH 199 599 768  HOH HOH C . 
W 6 HOH 200 600 769  HOH HOH C . 
W 6 HOH 201 601 771  HOH HOH C . 
W 6 HOH 202 602 776  HOH HOH C . 
W 6 HOH 203 603 783  HOH HOH C . 
W 6 HOH 204 604 785  HOH HOH C . 
W 6 HOH 205 605 790  HOH HOH C . 
W 6 HOH 206 606 793  HOH HOH C . 
W 6 HOH 207 607 797  HOH HOH C . 
W 6 HOH 208 608 799  HOH HOH C . 
W 6 HOH 209 609 800  HOH HOH C . 
W 6 HOH 210 610 803  HOH HOH C . 
W 6 HOH 211 611 805  HOH HOH C . 
W 6 HOH 212 612 807  HOH HOH C . 
W 6 HOH 213 613 811  HOH HOH C . 
W 6 HOH 214 614 816  HOH HOH C . 
W 6 HOH 215 615 818  HOH HOH C . 
W 6 HOH 216 616 819  HOH HOH C . 
W 6 HOH 217 617 820  HOH HOH C . 
W 6 HOH 218 618 827  HOH HOH C . 
W 6 HOH 219 619 828  HOH HOH C . 
W 6 HOH 220 620 829  HOH HOH C . 
W 6 HOH 221 621 845  HOH HOH C . 
W 6 HOH 222 622 868  HOH HOH C . 
W 6 HOH 223 623 870  HOH HOH C . 
W 6 HOH 224 624 875  HOH HOH C . 
W 6 HOH 225 625 887  HOH HOH C . 
W 6 HOH 226 626 890  HOH HOH C . 
W 6 HOH 227 627 900  HOH HOH C . 
W 6 HOH 228 628 902  HOH HOH C . 
W 6 HOH 229 629 915  HOH HOH C . 
W 6 HOH 230 630 922  HOH HOH C . 
W 6 HOH 231 631 933  HOH HOH C . 
W 6 HOH 232 632 941  HOH HOH C . 
W 6 HOH 233 633 943  HOH HOH C . 
W 6 HOH 234 634 945  HOH HOH C . 
W 6 HOH 235 635 947  HOH HOH C . 
W 6 HOH 236 636 948  HOH HOH C . 
W 6 HOH 237 637 950  HOH HOH C . 
W 6 HOH 238 638 959  HOH HOH C . 
W 6 HOH 239 639 966  HOH HOH C . 
W 6 HOH 240 640 970  HOH HOH C . 
W 6 HOH 241 641 971  HOH HOH C . 
W 6 HOH 242 642 974  HOH HOH C . 
W 6 HOH 243 643 976  HOH HOH C . 
W 6 HOH 244 644 977  HOH HOH C . 
W 6 HOH 245 645 981  HOH HOH C . 
W 6 HOH 246 646 983  HOH HOH C . 
W 6 HOH 247 647 984  HOH HOH C . 
W 6 HOH 248 648 987  HOH HOH C . 
W 6 HOH 249 649 992  HOH HOH C . 
W 6 HOH 250 650 1004 HOH HOH C . 
W 6 HOH 251 651 1005 HOH HOH C . 
W 6 HOH 252 652 1006 HOH HOH C . 
W 6 HOH 253 653 1013 HOH HOH C . 
X 6 HOH 1   401 4    HOH HOH D . 
X 6 HOH 2   402 7    HOH HOH D . 
X 6 HOH 3   403 12   HOH HOH D . 
X 6 HOH 4   404 14   HOH HOH D . 
X 6 HOH 5   405 21   HOH HOH D . 
X 6 HOH 6   406 24   HOH HOH D . 
X 6 HOH 7   407 29   HOH HOH D . 
X 6 HOH 8   408 34   HOH HOH D . 
X 6 HOH 9   409 45   HOH HOH D . 
X 6 HOH 10  410 47   HOH HOH D . 
X 6 HOH 11  411 49   HOH HOH D . 
X 6 HOH 12  412 55   HOH HOH D . 
X 6 HOH 13  413 59   HOH HOH D . 
X 6 HOH 14  414 62   HOH HOH D . 
X 6 HOH 15  415 63   HOH HOH D . 
X 6 HOH 16  416 64   HOH HOH D . 
X 6 HOH 17  417 70   HOH HOH D . 
X 6 HOH 18  418 74   HOH HOH D . 
X 6 HOH 19  419 78   HOH HOH D . 
X 6 HOH 20  420 81   HOH HOH D . 
X 6 HOH 21  421 84   HOH HOH D . 
X 6 HOH 22  422 90   HOH HOH D . 
X 6 HOH 23  423 99   HOH HOH D . 
X 6 HOH 24  424 101  HOH HOH D . 
X 6 HOH 25  425 105  HOH HOH D . 
X 6 HOH 26  426 107  HOH HOH D . 
X 6 HOH 27  427 109  HOH HOH D . 
X 6 HOH 28  428 112  HOH HOH D . 
X 6 HOH 29  429 113  HOH HOH D . 
X 6 HOH 30  430 120  HOH HOH D . 
X 6 HOH 31  431 121  HOH HOH D . 
X 6 HOH 32  432 124  HOH HOH D . 
X 6 HOH 33  433 126  HOH HOH D . 
X 6 HOH 34  434 128  HOH HOH D . 
X 6 HOH 35  435 130  HOH HOH D . 
X 6 HOH 36  436 134  HOH HOH D . 
X 6 HOH 37  437 136  HOH HOH D . 
X 6 HOH 38  438 145  HOH HOH D . 
X 6 HOH 39  439 148  HOH HOH D . 
X 6 HOH 40  440 150  HOH HOH D . 
X 6 HOH 41  441 152  HOH HOH D . 
X 6 HOH 42  442 156  HOH HOH D . 
X 6 HOH 43  443 158  HOH HOH D . 
X 6 HOH 44  444 168  HOH HOH D . 
X 6 HOH 45  445 170  HOH HOH D . 
X 6 HOH 46  446 171  HOH HOH D . 
X 6 HOH 47  447 175  HOH HOH D . 
X 6 HOH 48  448 179  HOH HOH D . 
X 6 HOH 49  449 182  HOH HOH D . 
X 6 HOH 50  450 183  HOH HOH D . 
X 6 HOH 51  451 185  HOH HOH D . 
X 6 HOH 52  452 194  HOH HOH D . 
X 6 HOH 53  453 197  HOH HOH D . 
X 6 HOH 54  454 199  HOH HOH D . 
X 6 HOH 55  455 202  HOH HOH D . 
X 6 HOH 56  456 210  HOH HOH D . 
X 6 HOH 57  457 212  HOH HOH D . 
X 6 HOH 58  458 215  HOH HOH D . 
X 6 HOH 59  459 217  HOH HOH D . 
X 6 HOH 60  460 222  HOH HOH D . 
X 6 HOH 61  461 224  HOH HOH D . 
X 6 HOH 62  462 227  HOH HOH D . 
X 6 HOH 63  463 228  HOH HOH D . 
X 6 HOH 64  464 236  HOH HOH D . 
X 6 HOH 65  465 239  HOH HOH D . 
X 6 HOH 66  466 242  HOH HOH D . 
X 6 HOH 67  467 252  HOH HOH D . 
X 6 HOH 68  468 253  HOH HOH D . 
X 6 HOH 69  469 259  HOH HOH D . 
X 6 HOH 70  470 263  HOH HOH D . 
X 6 HOH 71  471 265  HOH HOH D . 
X 6 HOH 72  472 271  HOH HOH D . 
X 6 HOH 73  473 274  HOH HOH D . 
X 6 HOH 74  474 276  HOH HOH D . 
X 6 HOH 75  475 279  HOH HOH D . 
X 6 HOH 76  476 292  HOH HOH D . 
X 6 HOH 77  477 294  HOH HOH D . 
X 6 HOH 78  478 295  HOH HOH D . 
X 6 HOH 79  479 306  HOH HOH D . 
X 6 HOH 80  480 319  HOH HOH D . 
X 6 HOH 81  481 324  HOH HOH D . 
X 6 HOH 82  482 327  HOH HOH D . 
X 6 HOH 83  483 329  HOH HOH D . 
X 6 HOH 84  484 330  HOH HOH D . 
X 6 HOH 85  485 338  HOH HOH D . 
X 6 HOH 86  486 342  HOH HOH D . 
X 6 HOH 87  487 344  HOH HOH D . 
X 6 HOH 88  488 349  HOH HOH D . 
X 6 HOH 89  489 352  HOH HOH D . 
X 6 HOH 90  490 356  HOH HOH D . 
X 6 HOH 91  491 362  HOH HOH D . 
X 6 HOH 92  492 370  HOH HOH D . 
X 6 HOH 93  493 378  HOH HOH D . 
X 6 HOH 94  494 380  HOH HOH D . 
X 6 HOH 95  495 381  HOH HOH D . 
X 6 HOH 96  496 384  HOH HOH D . 
X 6 HOH 97  497 386  HOH HOH D . 
X 6 HOH 98  498 394  HOH HOH D . 
X 6 HOH 99  499 400  HOH HOH D . 
X 6 HOH 100 500 409  HOH HOH D . 
X 6 HOH 101 501 410  HOH HOH D . 
X 6 HOH 102 502 413  HOH HOH D . 
X 6 HOH 103 503 417  HOH HOH D . 
X 6 HOH 104 504 418  HOH HOH D . 
X 6 HOH 105 505 432  HOH HOH D . 
X 6 HOH 106 506 438  HOH HOH D . 
X 6 HOH 107 507 439  HOH HOH D . 
X 6 HOH 108 508 441  HOH HOH D . 
X 6 HOH 109 509 449  HOH HOH D . 
X 6 HOH 110 510 452  HOH HOH D . 
X 6 HOH 111 511 459  HOH HOH D . 
X 6 HOH 112 512 468  HOH HOH D . 
X 6 HOH 113 513 473  HOH HOH D . 
X 6 HOH 114 514 480  HOH HOH D . 
X 6 HOH 115 515 484  HOH HOH D . 
X 6 HOH 116 516 488  HOH HOH D . 
X 6 HOH 117 517 489  HOH HOH D . 
X 6 HOH 118 518 490  HOH HOH D . 
X 6 HOH 119 519 501  HOH HOH D . 
X 6 HOH 120 520 507  HOH HOH D . 
X 6 HOH 121 521 512  HOH HOH D . 
X 6 HOH 122 522 521  HOH HOH D . 
X 6 HOH 123 523 522  HOH HOH D . 
X 6 HOH 124 524 524  HOH HOH D . 
X 6 HOH 125 525 534  HOH HOH D . 
X 6 HOH 126 526 536  HOH HOH D . 
X 6 HOH 127 527 537  HOH HOH D . 
X 6 HOH 128 528 542  HOH HOH D . 
X 6 HOH 129 529 544  HOH HOH D . 
X 6 HOH 130 530 546  HOH HOH D . 
X 6 HOH 131 531 547  HOH HOH D . 
X 6 HOH 132 532 552  HOH HOH D . 
X 6 HOH 133 533 553  HOH HOH D . 
X 6 HOH 134 534 555  HOH HOH D . 
X 6 HOH 135 535 557  HOH HOH D . 
X 6 HOH 136 536 558  HOH HOH D . 
X 6 HOH 137 537 559  HOH HOH D . 
X 6 HOH 138 538 566  HOH HOH D . 
X 6 HOH 139 539 580  HOH HOH D . 
X 6 HOH 140 540 581  HOH HOH D . 
X 6 HOH 141 541 585  HOH HOH D . 
X 6 HOH 142 542 586  HOH HOH D . 
X 6 HOH 143 543 587  HOH HOH D . 
X 6 HOH 144 544 588  HOH HOH D . 
X 6 HOH 145 545 594  HOH HOH D . 
X 6 HOH 146 546 595  HOH HOH D . 
X 6 HOH 147 547 597  HOH HOH D . 
X 6 HOH 148 548 599  HOH HOH D . 
X 6 HOH 149 549 602  HOH HOH D . 
X 6 HOH 150 550 603  HOH HOH D . 
X 6 HOH 151 551 619  HOH HOH D . 
X 6 HOH 152 552 620  HOH HOH D . 
X 6 HOH 153 553 623  HOH HOH D . 
X 6 HOH 154 554 624  HOH HOH D . 
X 6 HOH 155 555 625  HOH HOH D . 
X 6 HOH 156 556 626  HOH HOH D . 
X 6 HOH 157 557 629  HOH HOH D . 
X 6 HOH 158 558 634  HOH HOH D . 
X 6 HOH 159 559 642  HOH HOH D . 
X 6 HOH 160 560 645  HOH HOH D . 
X 6 HOH 161 561 657  HOH HOH D . 
X 6 HOH 162 562 658  HOH HOH D . 
X 6 HOH 163 563 659  HOH HOH D . 
X 6 HOH 164 564 667  HOH HOH D . 
X 6 HOH 165 565 670  HOH HOH D . 
X 6 HOH 166 566 672  HOH HOH D . 
X 6 HOH 167 567 674  HOH HOH D . 
X 6 HOH 168 568 677  HOH HOH D . 
X 6 HOH 169 569 692  HOH HOH D . 
X 6 HOH 170 570 696  HOH HOH D . 
X 6 HOH 171 571 706  HOH HOH D . 
X 6 HOH 172 572 709  HOH HOH D . 
X 6 HOH 173 573 716  HOH HOH D . 
X 6 HOH 174 574 718  HOH HOH D . 
X 6 HOH 175 575 728  HOH HOH D . 
X 6 HOH 176 576 734  HOH HOH D . 
X 6 HOH 177 577 737  HOH HOH D . 
X 6 HOH 178 578 741  HOH HOH D . 
X 6 HOH 179 579 742  HOH HOH D . 
X 6 HOH 180 580 758  HOH HOH D . 
X 6 HOH 181 581 770  HOH HOH D . 
X 6 HOH 182 582 772  HOH HOH D . 
X 6 HOH 183 583 775  HOH HOH D . 
X 6 HOH 184 584 779  HOH HOH D . 
X 6 HOH 185 585 784  HOH HOH D . 
X 6 HOH 186 586 787  HOH HOH D . 
X 6 HOH 187 587 801  HOH HOH D . 
X 6 HOH 188 588 814  HOH HOH D . 
X 6 HOH 189 589 817  HOH HOH D . 
X 6 HOH 190 590 821  HOH HOH D . 
X 6 HOH 191 591 825  HOH HOH D . 
X 6 HOH 192 592 831  HOH HOH D . 
X 6 HOH 193 593 833  HOH HOH D . 
X 6 HOH 194 594 835  HOH HOH D . 
X 6 HOH 195 595 837  HOH HOH D . 
X 6 HOH 196 596 838  HOH HOH D . 
X 6 HOH 197 597 841  HOH HOH D . 
X 6 HOH 198 598 846  HOH HOH D . 
X 6 HOH 199 599 848  HOH HOH D . 
X 6 HOH 200 600 850  HOH HOH D . 
X 6 HOH 201 601 854  HOH HOH D . 
X 6 HOH 202 602 857  HOH HOH D . 
X 6 HOH 203 603 862  HOH HOH D . 
X 6 HOH 204 604 878  HOH HOH D . 
X 6 HOH 205 605 879  HOH HOH D . 
X 6 HOH 206 606 884  HOH HOH D . 
X 6 HOH 207 607 886  HOH HOH D . 
X 6 HOH 208 608 895  HOH HOH D . 
X 6 HOH 209 609 897  HOH HOH D . 
X 6 HOH 210 610 898  HOH HOH D . 
X 6 HOH 211 611 899  HOH HOH D . 
X 6 HOH 212 612 901  HOH HOH D . 
X 6 HOH 213 613 907  HOH HOH D . 
X 6 HOH 214 614 908  HOH HOH D . 
X 6 HOH 215 615 909  HOH HOH D . 
X 6 HOH 216 616 911  HOH HOH D . 
X 6 HOH 217 617 912  HOH HOH D . 
X 6 HOH 218 618 913  HOH HOH D . 
X 6 HOH 219 619 914  HOH HOH D . 
X 6 HOH 220 620 918  HOH HOH D . 
X 6 HOH 221 621 921  HOH HOH D . 
X 6 HOH 222 622 925  HOH HOH D . 
X 6 HOH 223 623 927  HOH HOH D . 
X 6 HOH 224 624 928  HOH HOH D . 
X 6 HOH 225 625 931  HOH HOH D . 
X 6 HOH 226 626 932  HOH HOH D . 
X 6 HOH 227 627 937  HOH HOH D . 
X 6 HOH 228 628 940  HOH HOH D . 
X 6 HOH 229 629 949  HOH HOH D . 
X 6 HOH 230 630 951  HOH HOH D . 
X 6 HOH 231 631 952  HOH HOH D . 
X 6 HOH 232 632 953  HOH HOH D . 
X 6 HOH 233 633 955  HOH HOH D . 
X 6 HOH 234 634 963  HOH HOH D . 
X 6 HOH 235 635 969  HOH HOH D . 
X 6 HOH 236 636 975  HOH HOH D . 
X 6 HOH 237 637 982  HOH HOH D . 
X 6 HOH 238 638 985  HOH HOH D . 
X 6 HOH 239 639 986  HOH HOH D . 
X 6 HOH 240 640 988  HOH HOH D . 
X 6 HOH 241 641 996  HOH HOH D . 
X 6 HOH 242 642 1000 HOH HOH D . 
X 6 HOH 243 643 1001 HOH HOH D . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
3 author_and_software_defined_assembly PISA monomeric 1 
4 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,F,G,H,U 
2 1 B,I,J,K,L,V 
3 1 C,M,N,O,P,W 
4 1 D,Q,R,S,T,X 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 104.7 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.4 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 100.1 ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? F WWX .   ? A WWX 302 ? 1_555 113.6 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? F WWX .   ? A WWX 302 ? 1_555 115.6 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N4  ? F WWX .   ? A WWX 302 ? 1_555 110.7 ? 
7  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 103.7 ? 
8  NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 111.8 ? 
9  NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 99.1  ? 
10 NE2 ? B HIS 94  ? B HIS 94  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N4  ? J WWX .   ? B WWX 302 ? 1_555 114.3 ? 
11 NE2 ? B HIS 96  ? B HIS 96  ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N4  ? J WWX .   ? B WWX 302 ? 1_555 115.7 ? 
12 ND1 ? B HIS 119 ? B HIS 119 ? 1_555 ZN ? I ZN . ? B ZN 301 ? 1_555 N4  ? J WWX .   ? B WWX 302 ? 1_555 111.2 ? 
13 NE2 ? C HIS 94  ? C HIS 94  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 96  ? C HIS 96  ? 1_555 103.3 ? 
14 NE2 ? C HIS 94  ? C HIS 94  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 119 ? C HIS 119 ? 1_555 111.5 ? 
15 NE2 ? C HIS 96  ? C HIS 96  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 119 ? C HIS 119 ? 1_555 99.1  ? 
16 NE2 ? C HIS 94  ? C HIS 94  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N4  ? N WWX .   ? C WWX 302 ? 1_555 116.0 ? 
17 NE2 ? C HIS 96  ? C HIS 96  ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N4  ? N WWX .   ? C WWX 302 ? 1_555 115.4 ? 
18 ND1 ? C HIS 119 ? C HIS 119 ? 1_555 ZN ? M ZN . ? C ZN 301 ? 1_555 N4  ? N WWX .   ? C WWX 302 ? 1_555 110.1 ? 
19 NE2 ? D HIS 94  ? D HIS 94  ? 1_555 ZN ? Q ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 96  ? D HIS 96  ? 1_555 103.8 ? 
20 NE2 ? D HIS 94  ? D HIS 94  ? 1_555 ZN ? Q ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 119 ? D HIS 119 ? 1_555 111.5 ? 
21 NE2 ? D HIS 96  ? D HIS 96  ? 1_555 ZN ? Q ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 119 ? D HIS 119 ? 1_555 99.7  ? 
22 NE2 ? D HIS 94  ? D HIS 94  ? 1_555 ZN ? Q ZN . ? D ZN 301 ? 1_555 N4  ? R WWX .   ? D WWX 302 ? 1_555 114.3 ? 
23 NE2 ? D HIS 96  ? D HIS 96  ? 1_555 ZN ? Q ZN . ? D ZN 301 ? 1_555 N4  ? R WWX .   ? D WWX 302 ? 1_555 115.5 ? 
24 ND1 ? D HIS 119 ? D HIS 119 ? 1_555 ZN ? Q ZN . ? D ZN 301 ? 1_555 N4  ? R WWX .   ? D WWX 302 ? 1_555 111.0 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-04-15 
2 'Structure model' 1 1 2018-05-16 
3 'Structure model' 1 2 2023-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Refinement description' 
3 3 'Structure model' 'Data collection'        
4 3 'Structure model' 'Database references'    
5 3 'Structure model' 'Derived calculations'   
6 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' diffrn_source                 
2 2 'Structure model' software                      
3 3 'Structure model' chem_comp_atom                
4 3 'Structure model' chem_comp_bond                
5 3 'Structure model' database_2                    
6 3 'Structure model' pdbx_initial_refinement_model 
7 3 'Structure model' pdbx_struct_conn_angle        
8 3 'Structure model' struct_conn                   
9 3 'Structure model' struct_site                   
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
2  2 'Structure model' '_software.version'                           
3  3 'Structure model' '_database_2.pdbx_DOI'                        
4  3 'Structure model' '_database_2.pdbx_database_accession'         
5  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_asym_id'  
6  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
7  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
8  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 3 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_asym_id'  
13 3 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
14 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_asym_id'  
15 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
16 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
17 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
18 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
19 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
20 3 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
21 3 'Structure model' '_pdbx_struct_conn_angle.value'               
22 3 'Structure model' '_struct_conn.pdbx_dist_value'                
23 3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'             
24 3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
25 3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
26 3 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
27 3 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
28 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
29 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
30 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'             
31 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
32 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
33 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
34 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
35 3 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
36 3 'Structure model' '_struct_site.pdbx_auth_asym_id'              
37 3 'Structure model' '_struct_site.pdbx_auth_comp_id'              
38 3 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
_phasing.method   MR 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC      5.6.0117 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
SCALA       3.3.20   2011/05/18      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk 'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 2 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 3 
HKL-2000    .        ?               ?       ?                    ?                     'data collection' ? ?          ? 4 
XDS         .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 5 
MOLREP      .        ?               ?       ?                    ?                     phasing           ? ?          ? 6 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 650 ? ? O   A HOH 651 ? ? 2.03 
2 1 OE2 A GLU 214 ? ? O   A HOH 629 ? ? 2.04 
3 1 ND2 D ASN 62  ? ? ND2 D ASN 67  ? ? 2.06 
4 1 ND1 B HIS 36  ? ? O   B HOH 445 ? ? 2.06 
5 1 ND2 D ASN 67  ? ? O16 D WWX 302 ? ? 2.08 
6 1 OG  B SER 73  ? ? O   B HOH 633 ? ? 2.13 
7 1 O   C HOH 486 ? ? O   D HOH 553 ? ? 2.15 
8 1 ND2 A ASN 67  ? A O16 A WWX 302 ? ? 2.15 
9 1 O   A HOH 535 ? ? O   A HOH 610 ? ? 2.16 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CG A HIS 4   ? ? CD2 A HIS 4   ? ? 1.420 1.354 0.066 0.009 N 
2  1 CD A GLU 69  ? B OE1 A GLU 69  ? B 1.320 1.252 0.068 0.011 N 
3  1 CG B HIS 3   ? ? CD2 B HIS 3   ? ? 1.423 1.354 0.069 0.009 N 
4  1 CG B HIS 4   ? ? CD2 B HIS 4   ? ? 1.414 1.354 0.060 0.009 N 
5  1 CG B HIS 10  ? ? CD2 B HIS 10  ? ? 1.429 1.354 0.075 0.009 N 
6  1 CG C HIS 3   ? ? CD2 C HIS 3   ? ? 1.421 1.354 0.067 0.009 N 
7  1 CG C HIS 4   ? ? CD2 C HIS 4   ? ? 1.416 1.354 0.062 0.009 N 
8  1 CG C HIS 10  ? ? CD2 C HIS 10  ? ? 1.414 1.354 0.060 0.009 N 
9  1 CG C HIS 122 ? ? CD2 C HIS 122 ? ? 1.409 1.354 0.055 0.009 N 
10 1 CG D HIS 3   ? ? CD2 D HIS 3   ? ? 1.426 1.354 0.072 0.009 N 
11 1 CG D HIS 36  ? ? CD2 D HIS 36  ? ? 1.410 1.354 0.056 0.009 N 
12 1 CG D HIS 122 ? ? CD2 D HIS 122 ? ? 1.409 1.354 0.055 0.009 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              58 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              58 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              58 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                124.54 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            4.24 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 76  ? ? -124.04 -87.29  
2  1 LYS A 111 ? ? 75.25   -5.23   
3  1 PHE A 176 ? ? -151.47 80.68   
4  1 PHE A 176 ? ? -156.47 80.68   
5  1 ASN A 244 ? ? -98.11  50.26   
6  1 LYS A 252 ? ? 60.37   -131.74 
7  1 LYS A 252 ? ? 60.37   -138.90 
8  1 ASN B 11  ? ? -141.11 12.43   
9  1 ARG B 27  ? ? -143.31 56.23   
10 1 LYS B 76  ? ? -113.19 -87.25  
11 1 LYS B 111 ? ? 75.68   -2.76   
12 1 PHE B 176 ? ? -152.39 73.54   
13 1 ASN B 244 ? ? -98.44  50.34   
14 1 LYS B 252 ? ? 54.12   -138.90 
15 1 ASN B 253 ? ? -69.55  1.10    
16 1 ARG C 27  ? ? -142.87 56.47   
17 1 LYS C 76  ? ? -112.83 -88.07  
18 1 ASN C 244 ? ? -97.11  49.65   
19 1 LYS C 252 ? ? 53.26   -135.71 
20 1 ASN D 11  ? ? -140.23 11.14   
21 1 LYS D 76  ? ? -112.08 -82.81  
22 1 LYS D 111 ? ? 72.20   -1.87   
23 1 PHE D 176 ? ? -157.91 79.26   
24 1 ASN D 244 ? ? -96.60  50.50   
25 1 LYS D 252 ? ? 60.77   -134.23 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD ? A LYS 9   CD 
2  1 Y 1 A LYS 9   ? CE ? A LYS 9   CE 
3  1 Y 1 A LYS 9   ? NZ ? A LYS 9   NZ 
4  1 Y 1 A LYS 80  ? CE ? A LYS 80  CE 
5  1 Y 1 A LYS 80  ? NZ ? A LYS 80  NZ 
6  1 Y 1 B LYS 9   ? CD ? B LYS 9   CD 
7  1 Y 1 B LYS 9   ? CE ? B LYS 9   CE 
8  1 Y 1 B LYS 9   ? NZ ? B LYS 9   NZ 
9  1 Y 1 B LYS 45  ? CE ? B LYS 45  CE 
10 1 Y 1 B LYS 45  ? NZ ? B LYS 45  NZ 
11 1 Y 1 B LYS 76  ? CE ? B LYS 76  CE 
12 1 Y 1 B LYS 76  ? NZ ? B LYS 76  NZ 
13 1 Y 1 B LYS 80  ? CE ? B LYS 80  CE 
14 1 Y 1 B LYS 80  ? NZ ? B LYS 80  NZ 
15 1 Y 1 C LYS 9   ? CD ? C LYS 9   CD 
16 1 Y 1 C LYS 9   ? CE ? C LYS 9   CE 
17 1 Y 1 C LYS 9   ? NZ ? C LYS 9   NZ 
18 1 Y 1 C LYS 80  ? CE ? C LYS 80  CE 
19 1 Y 1 C LYS 80  ? NZ ? C LYS 80  NZ 
20 1 Y 1 C LYS 261 ? CG ? C LYS 260 CG 
21 1 Y 1 C LYS 261 ? CD ? C LYS 260 CD 
22 1 Y 1 C LYS 261 ? CE ? C LYS 260 CE 
23 1 Y 1 C LYS 261 ? NZ ? C LYS 260 NZ 
24 1 Y 1 D LYS 45  ? CE ? D LYS 45  CE 
25 1 Y 1 D LYS 45  ? NZ ? D LYS 45  NZ 
26 1 Y 1 D LYS 76  ? CG ? D LYS 76  CG 
27 1 Y 1 D LYS 76  ? CD ? D LYS 76  CD 
28 1 Y 1 D LYS 76  ? CE ? D LYS 76  CE 
29 1 Y 1 D LYS 76  ? NZ ? D LYS 76  NZ 
30 1 Y 1 D LYS 80  ? CE ? D LYS 80  CE 
31 1 Y 1 D LYS 80  ? NZ ? D LYS 80  NZ 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
4 1 Y 1 B MET 1 ? B MET 1 
5 1 Y 1 B SER 2 ? B SER 2 
6 1 Y 1 C MET 1 ? C MET 1 
7 1 Y 1 C SER 2 ? C SER 2 
8 1 Y 1 D MET 1 ? D MET 1 
9 1 Y 1 D SER 2 ? D SER 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
PHE N    N  N N 284 
PHE CA   C  N S 285 
PHE C    C  N N 286 
PHE O    O  N N 287 
PHE CB   C  N N 288 
PHE CG   C  Y N 289 
PHE CD1  C  Y N 290 
PHE CD2  C  Y N 291 
PHE CE1  C  Y N 292 
PHE CE2  C  Y N 293 
PHE CZ   C  Y N 294 
PHE OXT  O  N N 295 
PHE H    H  N N 296 
PHE H2   H  N N 297 
PHE HA   H  N N 298 
PHE HB2  H  N N 299 
PHE HB3  H  N N 300 
PHE HD1  H  N N 301 
PHE HD2  H  N N 302 
PHE HE1  H  N N 303 
PHE HE2  H  N N 304 
PHE HZ   H  N N 305 
PHE HXT  H  N N 306 
PRO N    N  N N 307 
PRO CA   C  N S 308 
PRO C    C  N N 309 
PRO O    O  N N 310 
PRO CB   C  N N 311 
PRO CG   C  N N 312 
PRO CD   C  N N 313 
PRO OXT  O  N N 314 
PRO H    H  N N 315 
PRO HA   H  N N 316 
PRO HB2  H  N N 317 
PRO HB3  H  N N 318 
PRO HG2  H  N N 319 
PRO HG3  H  N N 320 
PRO HD2  H  N N 321 
PRO HD3  H  N N 322 
PRO HXT  H  N N 323 
SER N    N  N N 324 
SER CA   C  N S 325 
SER C    C  N N 326 
SER O    O  N N 327 
SER CB   C  N N 328 
SER OG   O  N N 329 
SER OXT  O  N N 330 
SER H    H  N N 331 
SER H2   H  N N 332 
SER HA   H  N N 333 
SER HB2  H  N N 334 
SER HB3  H  N N 335 
SER HG   H  N N 336 
SER HXT  H  N N 337 
THR N    N  N N 338 
THR CA   C  N S 339 
THR C    C  N N 340 
THR O    O  N N 341 
THR CB   C  N R 342 
THR OG1  O  N N 343 
THR CG2  C  N N 344 
THR OXT  O  N N 345 
THR H    H  N N 346 
THR H2   H  N N 347 
THR HA   H  N N 348 
THR HB   H  N N 349 
THR HG1  H  N N 350 
THR HG21 H  N N 351 
THR HG22 H  N N 352 
THR HG23 H  N N 353 
THR HXT  H  N N 354 
TRP N    N  N N 355 
TRP CA   C  N S 356 
TRP C    C  N N 357 
TRP O    O  N N 358 
TRP CB   C  N N 359 
TRP CG   C  Y N 360 
TRP CD1  C  Y N 361 
TRP CD2  C  Y N 362 
TRP NE1  N  Y N 363 
TRP CE2  C  Y N 364 
TRP CE3  C  Y N 365 
TRP CZ2  C  Y N 366 
TRP CZ3  C  Y N 367 
TRP CH2  C  Y N 368 
TRP OXT  O  N N 369 
TRP H    H  N N 370 
TRP H2   H  N N 371 
TRP HA   H  N N 372 
TRP HB2  H  N N 373 
TRP HB3  H  N N 374 
TRP HD1  H  N N 375 
TRP HE1  H  N N 376 
TRP HE3  H  N N 377 
TRP HZ2  H  N N 378 
TRP HZ3  H  N N 379 
TRP HH2  H  N N 380 
TRP HXT  H  N N 381 
TYR N    N  N N 382 
TYR CA   C  N S 383 
TYR C    C  N N 384 
TYR O    O  N N 385 
TYR CB   C  N N 386 
TYR CG   C  Y N 387 
TYR CD1  C  Y N 388 
TYR CD2  C  Y N 389 
TYR CE1  C  Y N 390 
TYR CE2  C  Y N 391 
TYR CZ   C  Y N 392 
TYR OH   O  N N 393 
TYR OXT  O  N N 394 
TYR H    H  N N 395 
TYR H2   H  N N 396 
TYR HA   H  N N 397 
TYR HB2  H  N N 398 
TYR HB3  H  N N 399 
TYR HD1  H  N N 400 
TYR HD2  H  N N 401 
TYR HE1  H  N N 402 
TYR HE2  H  N N 403 
TYR HH   H  N N 404 
TYR HXT  H  N N 405 
VAL N    N  N N 406 
VAL CA   C  N S 407 
VAL C    C  N N 408 
VAL O    O  N N 409 
VAL CB   C  N N 410 
VAL CG1  C  N N 411 
VAL CG2  C  N N 412 
VAL OXT  O  N N 413 
VAL H    H  N N 414 
VAL H2   H  N N 415 
VAL HA   H  N N 416 
VAL HB   H  N N 417 
VAL HG11 H  N N 418 
VAL HG12 H  N N 419 
VAL HG13 H  N N 420 
VAL HG21 H  N N 421 
VAL HG22 H  N N 422 
VAL HG23 H  N N 423 
VAL HXT  H  N N 424 
WWX O16  O  N N 425 
WWX S14  S  N N 426 
WWX O15  O  N N 427 
WWX C18  C  N N 428 
WWX O20  O  N N 429 
WWX C17  C  N N 430 
WWX C8   C  Y N 431 
WWX C7   C  Y N 432 
WWX F12  F  N N 433 
WWX C6   C  Y N 434 
WWX F11  F  N N 435 
WWX C9   C  Y N 436 
WWX C10  C  Y N 437 
WWX F13  F  N N 438 
WWX C5   C  Y N 439 
WWX S1   S  N N 440 
WWX O3   O  N N 441 
WWX N4   N  N N 442 
WWX O2   O  N N 443 
WWX N19  N  N N 444 
WWX C21  C  N R 445 
WWX C30  C  Y N 446 
WWX C35  C  Y N 447 
WWX C34  C  Y N 448 
WWX C33  C  Y N 449 
WWX C32  C  Y N 450 
WWX C31  C  Y N 451 
WWX C22  C  N S 452 
WWX O29  O  N N 453 
WWX C23  C  Y N 454 
WWX C28  C  Y N 455 
WWX C27  C  Y N 456 
WWX C26  C  Y N 457 
WWX C25  C  Y N 458 
WWX C24  C  Y N 459 
WWX H1   H  N N 460 
WWX H2   H  N N 461 
WWX H3   H  N N 462 
WWX H4   H  N N 463 
WWX H5   H  N N 464 
WWX H6   H  N N 465 
WWX H7   H  N N 466 
WWX H8   H  N N 467 
WWX H9   H  N N 468 
WWX H10  H  N N 469 
WWX H11  H  N N 470 
WWX H12  H  N N 471 
WWX H13  H  N N 472 
WWX H14  H  N N 473 
WWX H15  H  N N 474 
WWX H16  H  N N 475 
WWX H17  H  N N 476 
WWX H18  H  N N 477 
WWX H19  H  N N 478 
WWX H20  H  N N 479 
WWX H21  H  N N 480 
ZN  ZN   ZN N N 481 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
GLN N   CA   sing N N 115 
GLN N   H    sing N N 116 
GLN N   H2   sing N N 117 
GLN CA  C    sing N N 118 
GLN CA  CB   sing N N 119 
GLN CA  HA   sing N N 120 
GLN C   O    doub N N 121 
GLN C   OXT  sing N N 122 
GLN CB  CG   sing N N 123 
GLN CB  HB2  sing N N 124 
GLN CB  HB3  sing N N 125 
GLN CG  CD   sing N N 126 
GLN CG  HG2  sing N N 127 
GLN CG  HG3  sing N N 128 
GLN CD  OE1  doub N N 129 
GLN CD  NE2  sing N N 130 
GLN NE2 HE21 sing N N 131 
GLN NE2 HE22 sing N N 132 
GLN OXT HXT  sing N N 133 
GLU N   CA   sing N N 134 
GLU N   H    sing N N 135 
GLU N   H2   sing N N 136 
GLU CA  C    sing N N 137 
GLU CA  CB   sing N N 138 
GLU CA  HA   sing N N 139 
GLU C   O    doub N N 140 
GLU C   OXT  sing N N 141 
GLU CB  CG   sing N N 142 
GLU CB  HB2  sing N N 143 
GLU CB  HB3  sing N N 144 
GLU CG  CD   sing N N 145 
GLU CG  HG2  sing N N 146 
GLU CG  HG3  sing N N 147 
GLU CD  OE1  doub N N 148 
GLU CD  OE2  sing N N 149 
GLU OE2 HE2  sing N N 150 
GLU OXT HXT  sing N N 151 
GLY N   CA   sing N N 152 
GLY N   H    sing N N 153 
GLY N   H2   sing N N 154 
GLY CA  C    sing N N 155 
GLY CA  HA2  sing N N 156 
GLY CA  HA3  sing N N 157 
GLY C   O    doub N N 158 
GLY C   OXT  sing N N 159 
GLY OXT HXT  sing N N 160 
HIS N   CA   sing N N 161 
HIS N   H    sing N N 162 
HIS N   H2   sing N N 163 
HIS CA  C    sing N N 164 
HIS CA  CB   sing N N 165 
HIS CA  HA   sing N N 166 
HIS C   O    doub N N 167 
HIS C   OXT  sing N N 168 
HIS CB  CG   sing N N 169 
HIS CB  HB2  sing N N 170 
HIS CB  HB3  sing N N 171 
HIS CG  ND1  sing Y N 172 
HIS CG  CD2  doub Y N 173 
HIS ND1 CE1  doub Y N 174 
HIS ND1 HD1  sing N N 175 
HIS CD2 NE2  sing Y N 176 
HIS CD2 HD2  sing N N 177 
HIS CE1 NE2  sing Y N 178 
HIS CE1 HE1  sing N N 179 
HIS NE2 HE2  sing N N 180 
HIS OXT HXT  sing N N 181 
HOH O   H1   sing N N 182 
HOH O   H2   sing N N 183 
ILE N   CA   sing N N 184 
ILE N   H    sing N N 185 
ILE N   H2   sing N N 186 
ILE CA  C    sing N N 187 
ILE CA  CB   sing N N 188 
ILE CA  HA   sing N N 189 
ILE C   O    doub N N 190 
ILE C   OXT  sing N N 191 
ILE CB  CG1  sing N N 192 
ILE CB  CG2  sing N N 193 
ILE CB  HB   sing N N 194 
ILE CG1 CD1  sing N N 195 
ILE CG1 HG12 sing N N 196 
ILE CG1 HG13 sing N N 197 
ILE CG2 HG21 sing N N 198 
ILE CG2 HG22 sing N N 199 
ILE CG2 HG23 sing N N 200 
ILE CD1 HD11 sing N N 201 
ILE CD1 HD12 sing N N 202 
ILE CD1 HD13 sing N N 203 
ILE OXT HXT  sing N N 204 
LEU N   CA   sing N N 205 
LEU N   H    sing N N 206 
LEU N   H2   sing N N 207 
LEU CA  C    sing N N 208 
LEU CA  CB   sing N N 209 
LEU CA  HA   sing N N 210 
LEU C   O    doub N N 211 
LEU C   OXT  sing N N 212 
LEU CB  CG   sing N N 213 
LEU CB  HB2  sing N N 214 
LEU CB  HB3  sing N N 215 
LEU CG  CD1  sing N N 216 
LEU CG  CD2  sing N N 217 
LEU CG  HG   sing N N 218 
LEU CD1 HD11 sing N N 219 
LEU CD1 HD12 sing N N 220 
LEU CD1 HD13 sing N N 221 
LEU CD2 HD21 sing N N 222 
LEU CD2 HD22 sing N N 223 
LEU CD2 HD23 sing N N 224 
LEU OXT HXT  sing N N 225 
LYS N   CA   sing N N 226 
LYS N   H    sing N N 227 
LYS N   H2   sing N N 228 
LYS CA  C    sing N N 229 
LYS CA  CB   sing N N 230 
LYS CA  HA   sing N N 231 
LYS C   O    doub N N 232 
LYS C   OXT  sing N N 233 
LYS CB  CG   sing N N 234 
LYS CB  HB2  sing N N 235 
LYS CB  HB3  sing N N 236 
LYS CG  CD   sing N N 237 
LYS CG  HG2  sing N N 238 
LYS CG  HG3  sing N N 239 
LYS CD  CE   sing N N 240 
LYS CD  HD2  sing N N 241 
LYS CD  HD3  sing N N 242 
LYS CE  NZ   sing N N 243 
LYS CE  HE2  sing N N 244 
LYS CE  HE3  sing N N 245 
LYS NZ  HZ1  sing N N 246 
LYS NZ  HZ2  sing N N 247 
LYS NZ  HZ3  sing N N 248 
LYS OXT HXT  sing N N 249 
MET N   CA   sing N N 250 
MET N   H    sing N N 251 
MET N   H2   sing N N 252 
MET CA  C    sing N N 253 
MET CA  CB   sing N N 254 
MET CA  HA   sing N N 255 
MET C   O    doub N N 256 
MET C   OXT  sing N N 257 
MET CB  CG   sing N N 258 
MET CB  HB2  sing N N 259 
MET CB  HB3  sing N N 260 
MET CG  SD   sing N N 261 
MET CG  HG2  sing N N 262 
MET CG  HG3  sing N N 263 
MET SD  CE   sing N N 264 
MET CE  HE1  sing N N 265 
MET CE  HE2  sing N N 266 
MET CE  HE3  sing N N 267 
MET OXT HXT  sing N N 268 
PHE N   CA   sing N N 269 
PHE N   H    sing N N 270 
PHE N   H2   sing N N 271 
PHE CA  C    sing N N 272 
PHE CA  CB   sing N N 273 
PHE CA  HA   sing N N 274 
PHE C   O    doub N N 275 
PHE C   OXT  sing N N 276 
PHE CB  CG   sing N N 277 
PHE CB  HB2  sing N N 278 
PHE CB  HB3  sing N N 279 
PHE CG  CD1  doub Y N 280 
PHE CG  CD2  sing Y N 281 
PHE CD1 CE1  sing Y N 282 
PHE CD1 HD1  sing N N 283 
PHE CD2 CE2  doub Y N 284 
PHE CD2 HD2  sing N N 285 
PHE CE1 CZ   doub Y N 286 
PHE CE1 HE1  sing N N 287 
PHE CE2 CZ   sing Y N 288 
PHE CE2 HE2  sing N N 289 
PHE CZ  HZ   sing N N 290 
PHE OXT HXT  sing N N 291 
PRO N   CA   sing N N 292 
PRO N   CD   sing N N 293 
PRO N   H    sing N N 294 
PRO CA  C    sing N N 295 
PRO CA  CB   sing N N 296 
PRO CA  HA   sing N N 297 
PRO C   O    doub N N 298 
PRO C   OXT  sing N N 299 
PRO CB  CG   sing N N 300 
PRO CB  HB2  sing N N 301 
PRO CB  HB3  sing N N 302 
PRO CG  CD   sing N N 303 
PRO CG  HG2  sing N N 304 
PRO CG  HG3  sing N N 305 
PRO CD  HD2  sing N N 306 
PRO CD  HD3  sing N N 307 
PRO OXT HXT  sing N N 308 
SER N   CA   sing N N 309 
SER N   H    sing N N 310 
SER N   H2   sing N N 311 
SER CA  C    sing N N 312 
SER CA  CB   sing N N 313 
SER CA  HA   sing N N 314 
SER C   O    doub N N 315 
SER C   OXT  sing N N 316 
SER CB  OG   sing N N 317 
SER CB  HB2  sing N N 318 
SER CB  HB3  sing N N 319 
SER OG  HG   sing N N 320 
SER OXT HXT  sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
WWX O20 C18  sing N N 408 
WWX C18 C17  sing N N 409 
WWX C17 S14  sing N N 410 
WWX C25 C26  doub Y N 411 
WWX C25 C24  sing Y N 412 
WWX C26 C27  sing Y N 413 
WWX C24 C23  doub Y N 414 
WWX C27 C28  doub Y N 415 
WWX C23 C28  sing Y N 416 
WWX C23 C22  sing N N 417 
WWX O29 C22  sing N N 418 
WWX C22 C21  sing N N 419 
WWX O15 S14  doub N N 420 
WWX S14 O16  doub N N 421 
WWX S14 C8   sing N N 422 
WWX F12 C7   sing N N 423 
WWX C8  C7   doub Y N 424 
WWX C8  C9   sing Y N 425 
WWX C7  C6   sing Y N 426 
WWX C21 N19  sing N N 427 
WWX C21 C30  sing N N 428 
WWX N19 C9   sing N N 429 
WWX F11 C6   sing N N 430 
WWX C9  C10  doub Y N 431 
WWX C6  C5   doub Y N 432 
WWX C10 C5   sing Y N 433 
WWX C10 F13  sing N N 434 
WWX C5  S1   sing N N 435 
WWX C30 C31  doub Y N 436 
WWX C30 C35  sing Y N 437 
WWX C31 C32  sing Y N 438 
WWX C35 C34  doub Y N 439 
WWX O3  S1   doub N N 440 
WWX N4  S1   sing N N 441 
WWX S1  O2   doub N N 442 
WWX C32 C33  doub Y N 443 
WWX C34 C33  sing Y N 444 
WWX C18 H1   sing N N 445 
WWX C18 H2   sing N N 446 
WWX O20 H3   sing N N 447 
WWX C17 H4   sing N N 448 
WWX C17 H5   sing N N 449 
WWX N4  H6   sing N N 450 
WWX N4  H7   sing N N 451 
WWX N19 H8   sing N N 452 
WWX C21 H9   sing N N 453 
WWX C35 H10  sing N N 454 
WWX C34 H11  sing N N 455 
WWX C33 H12  sing N N 456 
WWX C32 H13  sing N N 457 
WWX C31 H14  sing N N 458 
WWX C22 H15  sing N N 459 
WWX O29 H16  sing N N 460 
WWX C28 H17  sing N N 461 
WWX C27 H18  sing N N 462 
WWX C26 H19  sing N N 463 
WWX C25 H20  sing N N 464 
WWX C24 H21  sing N N 465 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                                                      ZN  
3 '2,3,6-trifluoro-5-{[(1R,2S)-2-hydroxy-1,2-diphenylethyl]amino}-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide' WWX 
4 'DIMETHYL SULFOXIDE'                                                                                            DMS 
5 BICINE                                                                                                          BCN 
6 water                                                                                                           HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
