data_3SAX
# 
_entry.id   3SAX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.379 
_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 
PDB   3SAX         pdb_00003sax 10.2210/pdb3sax/pdb 
RCSB  RCSB065980   ?            ?                   
WWPDB D_1000065980 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3S9T 'human carbonic anhydrase II with 2-chloro-5-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'      
unspecified 
PDB 3S8X 'human carbonic anhydrase II with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide' 
unspecified 
PDB 3SAP 'human carbonic anhydrase II with 4-{[(5-butyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'                    
unspecified 
PDB 3SBH 'human carbonic anhydrase II with 4-{[(4,6-dimethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide'               
unspecified 
PDB 3SBI .                                                                                                                   
unspecified 
# 
_pdbx_database_status.entry_id                        3SAX 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-06-03 
_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.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Grazulis, S.'     1 
'Manakova, E.'     2 
'Tamulaitiene, G.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Design of [(2-pyrimidinylthio)acetyl]benzenesulfonamides as inhibitors of human carbonic anhydrases.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            51 
_citation.page_first                259 
_citation.page_last                 270 
_citation.year                      2012 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22440859 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2012.02.050 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'  1 ? 
primary 'Zubriene, A.'      2 ? 
primary 'Baranauskiene, L.' 3 ? 
primary 'Tamulaitiene, G.'  4 ? 
primary 'Manakova, E.'      5 ? 
primary 'Kairys, V.'        6 ? 
primary 'Grazulis, S.'      7 ? 
primary 'Tumkevicius, S.'   8 ? 
primary 'Matulis, D.'       9 ? 
# 
_cell.entry_id           3SAX 
_cell.length_a           42.221 
_cell.length_b           41.172 
_cell.length_c           72.197 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.200 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              2 
_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                         3SAX 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.Int_Tables_number                4 
_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 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                               65.409    1   ?       ? ? ? 
3 non-polymer syn '2-chloro-5-{[(5-ethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' 371.862   1   ?       ? ? ? 
4 non-polymer syn BICINE                                                                   163.172   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                     78.133    2   ?       ? ? ? 
6 water       nat water                                                                    18.015    356 ?       ? ? ? 
# 
_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 
_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     469008 
_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            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3SAX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       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  
E50 non-polymer         . '2-chloro-5-{[(5-ethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' ? 'C14 H14 Cl N3 O3 S2' 371.862 
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 
ZN  non-polymer         . 'ZINC ION'                                                               ? 'Zn 2'                65.409  
# 
_exptl.crystals_number   1 
_exptl.entry_id          3SAX 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   40.78 
_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              9 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    
'0.1M Na-bicine pH 9, 2.6M Na-malonate pH 7.55, VAPOR DIFFUSION, SITTING DROP, temperature 298K' 
_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               CCD 
_diffrn_detector.type                   'MAR CCD 165 mm' 
_diffrn_detector.pdbx_collection_date   2010-11-12 
_diffrn_detector.details                'Mirror Bent, vertically focussing' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'Si (111), horizontally focussing' 
_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   0.8123 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE X13' 
_diffrn_source.pdbx_wavelength_list        0.8123 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   X13 
# 
_reflns.entry_id                     3SAX 
_reflns.d_resolution_high            1.10 
_reflns.d_resolution_low             41.172 
_reflns.number_all                   ? 
_reflns.number_obs                   92709 
_reflns.pdbx_netI_over_sigmaI        15.500 
_reflns.pdbx_Rsym_value              0.068 
_reflns.pdbx_redundancy              7.200 
_reflns.percent_possible_obs         93.400 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        7.8 
_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_Rmerge_I_obs            ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
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.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.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
1.10 1.15  ? 63186 ? 0.275 2.6  0.275 ? 5.50  ? 11403 79.20 1  1 
1.15 1.22  ? 76210 ? 0.212 3.3  0.212 ? 6.00  ? 12805 93.60 2  1 
1.22 1.31  ? 72146 ? 0.166 4.3  0.166 ? 6.00  ? 12097 94.40 3  1 
1.31 1.41  ? 67672 ? 0.128 5.5  0.128 ? 6.00  ? 11348 94.90 4  1 
1.41 1.55  ? 63028 ? 0.095 7.1  0.095 ? 6.00  ? 10568 95.90 5  1 
1.55 1.73  ? 57370 ? 0.072 9.1  0.072 ? 6.00  ? 9631  96.50 6  1 
1.73 2.00  ? 50882 ? 0.056 11.3 0.056 ? 5.90  ? 8562  97.20 7  1 
2.00 2.44  ? 99632 ? 0.094 7.2  0.094 ? 13.60 ? 7343  97.80 8  1 
2.44 3.46  ? 79171 ? 0.060 10.9 0.060 ? 13.80 ? 5723  98.60 9  1 
3.46 41.17 ? 39308 ? 0.050 11.9 0.050 ? 12.20 ? 3229  98.90 10 1 
# 
_refine.entry_id                                 3SAX 
_refine.ls_d_res_high                            1.100 
_refine.ls_d_res_low                             35.490 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    94.630 
_refine.ls_number_reflns_obs                     92668 
_refine.ls_number_reflns_all                     92668 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.129 
_refine.ls_R_factor_obs                          0.129 
_refine.ls_R_factor_R_work                       0.126 
_refine.ls_wR_factor_R_work                      0.128 
_refine.ls_R_factor_R_free                       0.158 
_refine.ls_wR_factor_R_free                      0.163 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  9255 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               12.365 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -0.430 
_refine.aniso_B[2][2]                            0.300 
_refine.aniso_B[3][3]                            0.160 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.060 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_refine.overall_SU_R_Cruickshank_DPI             0.035 
_refine.overall_SU_R_free                        0.036 
_refine.pdbx_overall_ESU_R_Free                  0.036 
_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          MR 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.930 
_refine.B_iso_max                                51.87 
_refine.B_iso_min                                3.79 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.01 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      'PDB entry 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_overall_ESU_R                       ? 
_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        2059 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.number_atoms_solvent             356 
_refine_hist.number_atoms_total               2458 
_refine_hist.d_res_high                       1.100 
_refine_hist.d_res_low                        35.490 
# 
loop_
_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 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         2904 0.029  0.022  ? ? 'X-RAY DIFFRACTION' 
r_bond_other_d           1959 0.000  0.020  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      3965 2.524  1.967  ? ? 'X-RAY DIFFRACTION' 
r_angle_other_deg        4819 4.325  3.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   367  7.366  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   133  35.029 25.188 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   481  11.375 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   8    20.752 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           413  0.153  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     3320 0.014  0.020  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_other       571  0.018  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            487  0.276  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbd_other              1566 0.258  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1091 0.187  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_other            1017 0.112  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    245  0.202  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      4    0.081  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   48   0.286  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_other     78   0.277  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 83   0.218  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1761 2.522  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_other           708  3.968  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2870 3.382  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              1143 4.371  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             1095 5.679  4.500  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr       4863 3.279  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free        378  15.369 3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded      4771 5.806  3.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.10 
_refine_ls_shell.d_res_low                        1.128 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               85.140 
_refine_ls_shell.number_reflns_R_work             5507 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.197 
_refine_ls_shell.R_factor_R_free                  0.244 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             628 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                6135 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3SAX 
_struct.title                     
;Crystal structure of human carbonic anhydrase isozyme II with 2-chloro-5-{[(5-ethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3SAX 
_struct_keywords.text            'drug design, sulfonamide, 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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G 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  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
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 
# 
_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 B ZN  . ZN  ? ? A HIS 94  A ZN  262 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  262 1_555 ? ? ? ? ? ? ? 2.008 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C E50 . N23 ? ? A ZN  262 A E50 263 1_555 ? ? ? ? ? ? ? 1.917 ? ? 
# 
_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 -4.48 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 10.17 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 10 ? 
C ? 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      
# 
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 
# 
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 LEU A 211 ? O LEU A 212 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 PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
B 8 9  O ASN A 67  ? O ASN A 67  N LEU A 60  ? N LEU A 60  
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 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
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 
# 
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  262 ? 4  'BINDING SITE FOR RESIDUE ZN A 262'  
AC2 Software A E50 263 ? 15 'BINDING SITE FOR RESIDUE E50 A 263' 
AC3 Software A BCN 264 ? 8  'BINDING SITE FOR RESIDUE BCN A 264' 
AC4 Software A DMS 265 ? 4  'BINDING SITE FOR RESIDUE DMS A 265' 
AC5 Software A DMS 266 ? 4  'BINDING SITE FOR RESIDUE DMS A 266' 
# 
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  E50 C .   ? E50 A 263 . ? 1_555 ? 
5  AC2 15 ASN A 62  ? ASN A 62  . ? 1_555 ? 
6  AC2 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
7  AC2 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
8  AC2 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
9  AC2 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
10 AC2 15 LEU A 140 ? LEU A 141 . ? 1_555 ? 
11 AC2 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
12 AC2 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
13 AC2 15 THR A 198 ? THR A 199 . ? 1_555 ? 
14 AC2 15 THR A 199 ? THR A 200 . ? 1_555 ? 
15 AC2 15 PRO A 201 ? PRO A 202 . ? 1_555 ? 
16 AC2 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
17 AC2 15 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
18 AC2 15 DMS F .   ? DMS A 266 . ? 1_555 ? 
19 AC2 15 HOH G .   ? HOH A 305 . ? 1_555 ? 
20 AC3 8  LYS A 148 ? LYS A 149 . ? 1_555 ? 
21 AC3 8  LYS A 212 ? LYS A 213 . ? 1_555 ? 
22 AC3 8  PRO A 214 ? PRO A 215 . ? 1_555 ? 
23 AC3 8  HOH G .   ? HOH A 287 . ? 1_555 ? 
24 AC3 8  HOH G .   ? HOH A 307 . ? 1_555 ? 
25 AC3 8  HOH G .   ? HOH A 384 . ? 1_555 ? 
26 AC3 8  HOH G .   ? HOH A 392 . ? 1_555 ? 
27 AC3 8  HOH G .   ? HOH A 595 . ? 1_555 ? 
28 AC4 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
29 AC4 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
30 AC4 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
31 AC4 4  HOH G .   ? HOH A 570 . ? 1_555 ? 
32 AC5 4  GLN A 92  ? GLN A 92  . ? 1_555 ? 
33 AC5 4  PHE A 130 ? PHE A 131 . ? 1_555 ? 
34 AC5 4  E50 C .   ? E50 A 263 . ? 1_555 ? 
35 AC5 4  HOH G .   ? HOH A 491 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3SAX 
_atom_sites.fract_transf_matrix[1][1]   0.023685 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005993 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024288 
_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]   0.014288 
_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  
CL 
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 3   ? 13.781  0.098   6.623   1.00 21.98 ? 3   HIS A N    1 
ATOM   2    C  CA   . HIS A 1 3   ? 13.397  -0.991  7.571   1.00 22.13 ? 3   HIS A CA   1 
ATOM   3    C  C    . HIS A 1 3   ? 12.353  -0.475  8.594   1.00 21.83 ? 3   HIS A C    1 
ATOM   4    O  O    . HIS A 1 3   ? 12.666  -0.265  9.817   1.00 27.27 ? 3   HIS A O    1 
ATOM   5    C  CB   . HIS A 1 3   ? 14.612  -1.487  8.321   1.00 21.48 ? 3   HIS A CB   1 
ATOM   6    C  CG   . HIS A 1 3   ? 14.357  -2.677  9.153   1.00 20.81 ? 3   HIS A CG   1 
ATOM   7    N  ND1  . HIS A 1 3   ? 14.425  -3.983  8.682   1.00 24.36 ? 3   HIS A ND1  1 
ATOM   8    C  CD2  . HIS A 1 3   ? 14.058  -2.739  10.482  1.00 19.61 ? 3   HIS A CD2  1 
ATOM   9    C  CE1  . HIS A 1 3   ? 14.181  -4.790  9.707   1.00 25.01 ? 3   HIS A CE1  1 
ATOM   10   N  NE2  . HIS A 1 3   ? 13.977  -4.065  10.804  1.00 25.60 ? 3   HIS A NE2  1 
ATOM   11   N  N    . HIS A 1 4   ? 11.115  -0.305  8.122   1.00 20.71 ? 4   HIS A N    1 
ATOM   12   C  CA   . HIS A 1 4   ? 10.095  0.232   8.989   1.00 20.44 ? 4   HIS A CA   1 
ATOM   13   C  C    . HIS A 1 4   ? 9.280   -0.857  9.595   1.00 16.25 ? 4   HIS A C    1 
ATOM   14   O  O    . HIS A 1 4   ? 9.426   -2.043  9.275   1.00 17.81 ? 4   HIS A O    1 
ATOM   15   C  CB   . HIS A 1 4   ? 9.219   1.115   8.163   1.00 22.57 ? 4   HIS A CB   1 
ATOM   16   C  CG   . HIS A 1 4   ? 8.643   0.446   6.927   1.00 23.91 ? 4   HIS A CG   1 
ATOM   17   N  ND1  . HIS A 1 4   ? 9.080   -0.771  6.447   0.01 23.67 ? 4   HIS A ND1  1 
ATOM   18   C  CD2  . HIS A 1 4   ? 7.667   0.850   6.079   0.01 24.26 ? 4   HIS A CD2  1 
ATOM   19   C  CE1  . HIS A 1 4   ? 8.396   -1.089  5.363   0.01 24.13 ? 4   HIS A CE1  1 
ATOM   20   N  NE2  . HIS A 1 4   ? 7.532   -0.122  5.119   0.01 24.03 ? 4   HIS A NE2  1 
ATOM   21   N  N    . TRP A 1 5   ? 8.429   -0.474  10.532  1.00 16.00 ? 5   TRP A N    1 
ATOM   22   C  CA   . TRP A 1 5   ? 7.674   -1.445  11.284  1.00 13.15 ? 5   TRP A CA   1 
ATOM   23   C  C    . TRP A 1 5   ? 6.666   -2.207  10.464  1.00 13.26 ? 5   TRP A C    1 
ATOM   24   O  O    . TRP A 1 5   ? 6.176   -1.745  9.488   1.00 14.68 ? 5   TRP A O    1 
ATOM   25   C  CB   . TRP A 1 5   ? 7.012   -0.721  12.459  1.00 13.70 ? 5   TRP A CB   1 
ATOM   26   C  CG   . TRP A 1 5   ? 5.789   0.078   12.095  1.00 12.08 ? 5   TRP A CG   1 
ATOM   27   C  CD1  . TRP A 1 5   ? 5.776   1.393   11.828  1.00 14.83 ? 5   TRP A CD1  1 
ATOM   28   C  CD2  . TRP A 1 5   ? 4.422   -0.407  12.046  1.00 11.29 ? 5   TRP A CD2  1 
ATOM   29   N  NE1  . TRP A 1 5   ? 4.472   1.807   11.590  1.00 13.74 ? 5   TRP A NE1  1 
ATOM   30   C  CE2  . TRP A 1 5   ? 3.625   0.706   11.718  1.00 13.29 ? 5   TRP A CE2  1 
ATOM   31   C  CE3  . TRP A 1 5   ? 3.819   -1.637  12.319  1.00 11.51 ? 5   TRP A CE3  1 
ATOM   32   C  CZ2  . TRP A 1 5   ? 2.243   0.593   11.624  1.00 13.42 ? 5   TRP A CZ2  1 
ATOM   33   C  CZ3  . TRP A 1 5   ? 2.433   -1.724  12.165  1.00 11.85 ? 5   TRP A CZ3  1 
ATOM   34   C  CH2  . TRP A 1 5   ? 1.669   -0.605  11.828  1.00 13.60 ? 5   TRP A CH2  1 
ATOM   35   N  N    . GLY A 1 6   ? 6.417   -3.425  10.930  1.00 12.74 ? 6   GLY A N    1 
ATOM   36   C  CA   . GLY A 1 6   ? 5.393   -4.264  10.318  1.00 12.15 ? 6   GLY A CA   1 
ATOM   37   C  C    . GLY A 1 6   ? 5.044   -5.392  11.280  1.00 12.67 ? 6   GLY A C    1 
ATOM   38   O  O    . GLY A 1 6   ? 5.070   -5.257  12.511  1.00 12.47 ? 6   GLY A O    1 
ATOM   39   N  N    A TYR A 1 7   ? 4.564   -6.434  10.526  0.50 11.38 ? 7   TYR A N    1 
ATOM   40   N  N    B TYR A 1 7   ? 4.944   -6.620  10.851  0.50 11.96 ? 7   TYR A N    1 
ATOM   41   C  CA   A TYR A 1 7   ? 4.128   -7.765  11.114  0.50 10.70 ? 7   TYR A CA   1 
ATOM   42   C  CA   B TYR A 1 7   ? 4.496   -7.723  11.770  0.50 11.53 ? 7   TYR A CA   1 
ATOM   43   C  C    A TYR A 1 7   ? 5.059   -9.066  10.779  0.50 14.82 ? 7   TYR A C    1 
ATOM   44   C  C    B TYR A 1 7   ? 5.362   -8.896  11.490  0.50 14.90 ? 7   TYR A C    1 
ATOM   45   O  O    A TYR A 1 7   ? 4.463   -10.149 10.533  0.50 15.77 ? 7   TYR A O    1 
ATOM   46   O  O    B TYR A 1 7   ? 5.063   -10.016 12.126  0.50 13.83 ? 7   TYR A O    1 
ATOM   47   C  CB   A TYR A 1 7   ? 2.617   -7.989  10.891  0.50 9.22  ? 7   TYR A CB   1 
ATOM   48   C  CB   B TYR A 1 7   ? 3.055   -8.079  11.491  0.50 10.12 ? 7   TYR A CB   1 
ATOM   49   C  CG   A TYR A 1 7   ? 1.749   -6.898  11.514  0.50 7.59  ? 7   TYR A CG   1 
ATOM   50   C  CG   B TYR A 1 7   ? 2.107   -7.001  11.975  0.50 9.25  ? 7   TYR A CG   1 
ATOM   51   C  CD1  A TYR A 1 7   ? 1.424   -6.928  12.891  0.50 8.54  ? 7   TYR A CD1  1 
ATOM   52   C  CD1  B TYR A 1 7   ? 1.668   -6.996  13.316  0.50 8.79  ? 7   TYR A CD1  1 
ATOM   53   C  CD2  A TYR A 1 7   ? 1.268   -5.829  10.748  0.50 7.29  ? 7   TYR A CD2  1 
ATOM   54   C  CD2  B TYR A 1 7   ? 1.661   -5.960  11.126  0.50 8.77  ? 7   TYR A CD2  1 
ATOM   55   C  CE1  A TYR A 1 7   ? 0.610   -5.938  13.445  0.50 6.81  ? 7   TYR A CE1  1 
ATOM   56   C  CE1  B TYR A 1 7   ? 0.809   -5.983  13.771  0.50 7.69  ? 7   TYR A CE1  1 
ATOM   57   C  CE2  A TYR A 1 7   ? 0.435   -4.882  11.294  0.50 7.84  ? 7   TYR A CE2  1 
ATOM   58   C  CE2  B TYR A 1 7   ? 0.816   -4.972  11.590  0.50 8.00  ? 7   TYR A CE2  1 
ATOM   59   C  CZ   A TYR A 1 7   ? 0.122   -4.917  12.645  0.50 7.21  ? 7   TYR A CZ   1 
ATOM   60   C  CZ   B TYR A 1 7   ? 0.358   -5.014  12.897  0.50 6.98  ? 7   TYR A CZ   1 
ATOM   61   O  OH   A TYR A 1 7   ? -0.716  -3.942  13.127  0.50 7.34  ? 7   TYR A OH   1 
ATOM   62   O  OH   B TYR A 1 7   ? -0.481  -4.029  13.349  0.50 7.83  ? 7   TYR A OH   1 
ATOM   63   N  N    A GLY A 1 8   ? 6.405   -8.967  10.976  0.50 14.97 ? 8   GLY A N    1 
ATOM   64   N  N    B GLY A 1 8   ? 6.323   -8.749  10.589  0.50 14.35 ? 8   GLY A N    1 
ATOM   65   C  CA   A GLY A 1 8   ? 7.396   -10.086 10.940  0.50 9.49  ? 8   GLY A CA   1 
ATOM   66   C  CA   B GLY A 1 8   ? 7.169   -9.850  10.206  0.50 15.88 ? 8   GLY A CA   1 
ATOM   67   C  C    A GLY A 1 8   ? 8.536   -10.244 12.009  0.50 12.72 ? 8   GLY A C    1 
ATOM   68   C  C    B GLY A 1 8   ? 8.173   -10.161 11.287  0.50 15.32 ? 8   GLY A C    1 
ATOM   69   O  O    A GLY A 1 8   ? 8.564   -9.479  12.969  0.50 14.28 ? 8   GLY A O    1 
ATOM   70   O  O    B GLY A 1 8   ? 8.267   -9.516  12.330  0.50 15.72 ? 8   GLY A O    1 
ATOM   71   N  N    A LYS A 1 9   ? 9.470   -11.218 11.850  0.50 12.46 ? 9   LYS A N    1 
ATOM   72   N  N    B LYS A 1 9   ? 8.975   -11.193 11.050  0.50 17.05 ? 9   LYS A N    1 
ATOM   73   C  CA   A LYS A 1 9   ? 10.459  -11.576 12.798  0.50 12.72 ? 9   LYS A CA   1 
ATOM   74   C  CA   B LYS A 1 9   ? 10.060  -11.623 11.963  0.50 19.04 ? 9   LYS A CA   1 
ATOM   75   C  C    A LYS A 1 9   ? 11.418  -10.456 13.102  0.50 10.98 ? 9   LYS A C    1 
ATOM   76   C  C    B LYS A 1 9   ? 10.963  -10.460 12.158  0.50 16.97 ? 9   LYS A C    1 
ATOM   77   O  O    A LYS A 1 9   ? 11.848  -10.362 14.250  0.50 12.81 ? 9   LYS A O    1 
ATOM   78   O  O    B LYS A 1 9   ? 11.483  -10.237 13.296  0.50 20.06 ? 9   LYS A O    1 
ATOM   79   C  CB   A LYS A 1 9   ? 11.304  -12.656 12.203  0.50 15.24 ? 9   LYS A CB   1 
ATOM   80   C  CB   B LYS A 1 9   ? 10.884  -12.838 11.374  0.50 18.43 ? 9   LYS A CB   1 
ATOM   81   C  CG   A LYS A 1 9   ? 12.371  -13.143 13.184  0.50 17.83 ? 9   LYS A CG   1 
ATOM   82   C  CG   B LYS A 1 9   ? 12.275  -13.073 12.058  0.50 19.80 ? 9   LYS A CG   1 
ATOM   83   C  CD   A LYS A 1 9   ? 13.165  -14.397 12.799  0.50 18.68 ? 9   LYS A CD   1 
ATOM   84   C  CD   B LYS A 1 9   ? 12.691  -14.551 11.883  0.50 21.39 ? 9   LYS A CD   1 
ATOM   85   C  CE   A LYS A 1 9   ? 14.690  -14.343 13.230  0.50 21.59 ? 9   LYS A CE   1 
ATOM   86   C  CE   B LYS A 1 9   ? 14.218  -14.822 12.021  0.50 24.96 ? 9   LYS A CE   1 
ATOM   87   N  NZ   A LYS A 1 9   ? 15.529  -15.580 12.848  0.50 24.13 ? 9   LYS A NZ   1 
ATOM   88   N  NZ   B LYS A 1 9   ? 14.875  -15.676 10.891  0.50 23.68 ? 9   LYS A NZ   1 
ATOM   89   N  N    A HIS A 1 10  ? 11.824  -9.695  12.048  0.50 9.99  ? 10  HIS A N    1 
ATOM   90   N  N    B HIS A 1 10  ? 11.234  -9.762  11.058  0.50 14.48 ? 10  HIS A N    1 
ATOM   91   C  CA   A HIS A 1 10  ? 12.852  -8.682  12.218  0.50 9.41  ? 10  HIS A CA   1 
ATOM   92   C  CA   B HIS A 1 10  ? 12.282  -8.808  11.223  0.50 13.68 ? 10  HIS A CA   1 
ATOM   93   C  C    A HIS A 1 10  ? 12.163  -7.277  12.344  0.50 11.29 ? 10  HIS A C    1 
ATOM   94   C  C    B HIS A 1 10  ? 11.969  -7.390  11.761  0.50 15.90 ? 10  HIS A C    1 
ATOM   95   O  O    A HIS A 1 10  ? 12.936  -6.384  12.827  0.50 13.67 ? 10  HIS A O    1 
ATOM   96   O  O    B HIS A 1 10  ? 12.777  -6.592  12.095  0.50 19.70 ? 10  HIS A O    1 
ATOM   97   C  CB   A HIS A 1 10  ? 13.766  -8.705  10.968  0.50 9.05  ? 10  HIS A CB   1 
ATOM   98   C  CB   B HIS A 1 10  ? 13.146  -8.804  9.977   0.50 11.92 ? 10  HIS A CB   1 
ATOM   99   C  CG   A HIS A 1 10  ? 14.368  -10.046 10.719  0.50 9.51  ? 10  HIS A CG   1 
ATOM   100  C  CG   B HIS A 1 10  ? 13.672  -10.152 9.596   0.50 12.22 ? 10  HIS A CG   1 
ATOM   101  N  ND1  A HIS A 1 10  ? 15.416  -10.511 11.487  0.50 11.09 ? 10  HIS A ND1  1 
ATOM   102  N  ND1  B HIS A 1 10  ? 14.610  -10.850 10.333  0.50 14.56 ? 10  HIS A ND1  1 
ATOM   103  C  CD2  A HIS A 1 10  ? 14.022  -11.029 9.846   0.50 10.91 ? 10  HIS A CD2  1 
ATOM   104  C  CD2  B HIS A 1 10  ? 13.335  -10.956 8.548   0.50 13.04 ? 10  HIS A CD2  1 
ATOM   105  C  CE1  A HIS A 1 10  ? 15.707  -11.721 11.063  0.50 10.93 ? 10  HIS A CE1  1 
ATOM   106  C  CE1  B HIS A 1 10  ? 14.824  -12.019 9.741   0.50 13.34 ? 10  HIS A CE1  1 
ATOM   107  N  NE2  A HIS A 1 10  ? 14.869  -12.070 10.098  0.50 12.15 ? 10  HIS A NE2  1 
ATOM   108  N  NE2  B HIS A 1 10  ? 14.094  -12.093 8.640   0.50 11.95 ? 10  HIS A NE2  1 
ATOM   109  N  N    . ASN A 1 11  ? 10.775  -7.168  12.108  1.00 16.79 ? 11  ASN A N    1 
ATOM   110  C  CA   . ASN A 1 11  ? 10.191  -5.824  12.124  1.00 15.45 ? 11  ASN A CA   1 
ATOM   111  C  C    . ASN A 1 11  ? 8.861   -5.807  12.902  1.00 15.83 ? 11  ASN A C    1 
ATOM   112  O  O    . ASN A 1 11  ? 8.168   -4.784  12.955  1.00 14.65 ? 11  ASN A O    1 
ATOM   113  C  CB   . ASN A 1 11  ? 9.936   -5.091  10.788  1.00 14.81 ? 11  ASN A CB   1 
ATOM   114  C  CG   . ASN A 1 11  ? 8.816   -5.687  9.846   1.00 15.78 ? 11  ASN A CG   1 
ATOM   115  O  OD1  . ASN A 1 11  ? 8.257   -6.675  10.149  1.00 20.21 ? 11  ASN A OD1  1 
ATOM   116  N  ND2  . ASN A 1 11  ? 8.551   -5.082  8.695   1.00 18.50 ? 11  ASN A ND2  1 
ATOM   117  N  N    . GLY A 1 12  ? 8.502   -6.953  13.470  1.00 14.19 ? 12  GLY A N    1 
ATOM   118  C  CA   . GLY A 1 12  ? 7.236   -7.100  14.163  1.00 13.85 ? 12  GLY A CA   1 
ATOM   119  C  C    . GLY A 1 12  ? 7.204   -6.556  15.580  1.00 12.34 ? 12  GLY A C    1 
ATOM   120  O  O    . GLY A 1 12  ? 8.082   -5.872  16.029  1.00 13.81 ? 12  GLY A O    1 
ATOM   121  N  N    . PRO A 1 13  ? 6.074   -6.864  16.268  1.00 11.26 ? 13  PRO A N    1 
ATOM   122  C  CA   . PRO A 1 13  ? 5.847   -6.315  17.593  1.00 11.20 ? 13  PRO A CA   1 
ATOM   123  C  C    . PRO A 1 13  ? 6.987   -6.307  18.557  1.00 10.99 ? 13  PRO A C    1 
ATOM   124  O  O    . PRO A 1 13  ? 7.094   -5.363  19.335  1.00 11.80 ? 13  PRO A O    1 
ATOM   125  C  CB   . PRO A 1 13  ? 4.647   -7.114  18.111  1.00 11.67 ? 13  PRO A CB   1 
ATOM   126  C  CG   . PRO A 1 13  ? 3.853   -7.403  16.870  1.00 11.93 ? 13  PRO A CG   1 
ATOM   127  C  CD   . PRO A 1 13  ? 4.914   -7.592  15.771  1.00 12.91 ? 13  PRO A CD   1 
ATOM   128  N  N    . GLU A 1 14  ? 7.802   -7.314  18.566  1.00 13.24 ? 14  GLU A N    1 
ATOM   129  C  CA   . GLU A 1 14  ? 8.908   -7.403  19.547  1.00 14.95 ? 14  GLU A CA   1 
ATOM   130  C  C    . GLU A 1 14  ? 10.081  -6.446  19.258  1.00 14.35 ? 14  GLU A C    1 
ATOM   131  O  O    . GLU A 1 14  ? 10.980  -6.250  20.073  1.00 16.17 ? 14  GLU A O    1 
ATOM   132  C  CB   . GLU A 1 14  ? 9.413   -8.843  19.655  1.00 17.62 ? 14  GLU A CB   1 
ATOM   133  C  CG   . GLU A 1 14  ? 8.345   -9.854  20.045  1.00 22.29 ? 14  GLU A CG   1 
ATOM   134  C  CD   . GLU A 1 14  ? 7.545   -9.424  21.260  1.00 29.55 ? 14  GLU A CD   1 
ATOM   135  O  OE1  . GLU A 1 14  ? 8.156   -9.177  22.320  1.00 36.28 ? 14  GLU A OE1  1 
ATOM   136  O  OE2  . GLU A 1 14  ? 6.302   -9.337  21.155  1.00 32.76 ? 14  GLU A OE2  1 
ATOM   137  N  N    . HIS A 1 15  ? 10.028  -5.860  18.062  1.00 12.94 ? 15  HIS A N    1 
ATOM   138  C  CA   . HIS A 1 15  ? 11.002  -4.832  17.647  1.00 13.50 ? 15  HIS A CA   1 
ATOM   139  C  C    . HIS A 1 15  ? 10.533  -3.420  17.792  1.00 12.57 ? 15  HIS A C    1 
ATOM   140  O  O    . HIS A 1 15  ? 11.366  -2.457  17.696  1.00 13.42 ? 15  HIS A O    1 
ATOM   141  C  CB   . HIS A 1 15  ? 11.356  -5.049  16.160  1.00 13.31 ? 15  HIS A CB   1 
ATOM   142  C  CG   . HIS A 1 15  ? 12.127  -6.263  15.932  1.00 14.49 ? 15  HIS A CG   1 
ATOM   143  N  ND1  . HIS A 1 15  ? 13.519  -6.313  16.042  1.00 16.89 ? 15  HIS A ND1  1 
ATOM   144  C  CD2  . HIS A 1 15  ? 11.695  -7.478  15.570  1.00 18.56 ? 15  HIS A CD2  1 
ATOM   145  C  CE1  . HIS A 1 15  ? 13.907  -7.551  15.828  1.00 20.69 ? 15  HIS A CE1  1 
ATOM   146  N  NE2  . HIS A 1 15  ? 12.847  -8.292  15.514  1.00 18.73 ? 15  HIS A NE2  1 
ATOM   147  N  N    . TRP A 1 16  ? 9.236   -3.186  17.969  1.00 11.83 ? 16  TRP A N    1 
ATOM   148  C  CA   . TRP A 1 16  ? 8.681   -1.838  17.859  1.00 10.17 ? 16  TRP A CA   1 
ATOM   149  C  C    . TRP A 1 16  ? 9.280   -0.859  18.878  1.00 10.48 ? 16  TRP A C    1 
ATOM   150  O  O    . TRP A 1 16  ? 9.359   0.342   18.595  1.00 11.29 ? 16  TRP A O    1 
ATOM   151  C  CB   . TRP A 1 16  ? 7.149   -1.865  17.946  1.00 9.90  ? 16  TRP A CB   1 
ATOM   152  C  CG   . TRP A 1 16  ? 6.465   -2.536  16.774  1.00 9.14  ? 16  TRP A CG   1 
ATOM   153  C  CD1  . TRP A 1 16  ? 6.973   -2.973  15.592  1.00 9.89  ? 16  TRP A CD1  1 
ATOM   154  C  CD2  . TRP A 1 16  ? 5.045   -2.879  16.745  1.00 9.27  ? 16  TRP A CD2  1 
ATOM   155  N  NE1  . TRP A 1 16  ? 6.015   -3.579  14.865  1.00 10.20 ? 16  TRP A NE1  1 
ATOM   156  C  CE2  . TRP A 1 16  ? 4.788   -3.509  15.523  1.00 9.16  ? 16  TRP A CE2  1 
ATOM   157  C  CE3  . TRP A 1 16  ? 3.989   -2.731  17.690  1.00 8.71  ? 16  TRP A CE3  1 
ATOM   158  C  CZ2  . TRP A 1 16  ? 3.521   -3.954  15.134  1.00 8.91  ? 16  TRP A CZ2  1 
ATOM   159  C  CZ3  . TRP A 1 16  ? 2.734   -3.158  17.301  1.00 8.84  ? 16  TRP A CZ3  1 
ATOM   160  C  CH2  . TRP A 1 16  ? 2.484   -3.746  16.045  1.00 8.73  ? 16  TRP A CH2  1 
ATOM   161  N  N    . HIS A 1 17  ? 9.638   -1.371  20.026  1.00 10.78 ? 17  HIS A N    1 
ATOM   162  C  CA   . HIS A 1 17  ? 10.151  -0.537  21.097  1.00 11.29 ? 17  HIS A CA   1 
ATOM   163  C  C    . HIS A 1 17  ? 11.379  0.319   20.709  1.00 13.09 ? 17  HIS A C    1 
ATOM   164  O  O    . HIS A 1 17  ? 11.679  1.335   21.334  1.00 13.65 ? 17  HIS A O    1 
ATOM   165  C  CB   . HIS A 1 17  ? 10.443  -1.305  22.355  1.00 11.04 ? 17  HIS A CB   1 
ATOM   166  C  CG   . HIS A 1 17  ? 11.669  -2.138  22.289  1.00 13.64 ? 17  HIS A CG   1 
ATOM   167  N  ND1  . HIS A 1 17  ? 12.892  -1.736  22.774  1.00 16.29 ? 17  HIS A ND1  1 
ATOM   168  C  CD2  . HIS A 1 17  ? 11.843  -3.332  21.704  1.00 13.99 ? 17  HIS A CD2  1 
ATOM   169  C  CE1  . HIS A 1 17  ? 13.757  -2.700  22.535  1.00 16.53 ? 17  HIS A CE1  1 
ATOM   170  N  NE2  . HIS A 1 17  ? 13.167  -3.665  21.874  1.00 16.49 ? 17  HIS A NE2  1 
ATOM   171  N  N    . LYS A 1 18  ? 12.184  -0.183  19.775  1.00 12.99 ? 18  LYS A N    1 
ATOM   172  C  CA   . LYS A 1 18  ? 13.408  0.532   19.368  1.00 14.75 ? 18  LYS A CA   1 
ATOM   173  C  C    . LYS A 1 18  ? 13.048  1.863   18.740  1.00 14.63 ? 18  LYS A C    1 
ATOM   174  O  O    . LYS A 1 18  ? 13.699  2.873   19.072  1.00 19.37 ? 18  LYS A O    1 
ATOM   175  C  CB   . LYS A 1 18  ? 14.252  -0.346  18.453  1.00 15.17 ? 18  LYS A CB   1 
ATOM   176  C  CG   . LYS A 1 18  ? 14.880  -1.523  19.180  1.00 14.86 ? 18  LYS A CG   1 
ATOM   177  C  CD   . LYS A 1 18  ? 15.624  -2.452  18.233  1.00 15.54 ? 18  LYS A CD   1 
ATOM   178  C  CE   . LYS A 1 18  ? 14.655  -3.460  17.642  1.00 15.63 ? 18  LYS A CE   1 
ATOM   179  N  NZ   . LYS A 1 18  ? 15.241  -4.325  16.586  1.00 15.20 ? 18  LYS A NZ   1 
ATOM   180  N  N    . ASP A 1 19  ? 12.081  1.932   17.820  1.00 14.54 ? 19  ASP A N    1 
ATOM   181  C  CA   . ASP A 1 19  ? 11.642  3.188   17.229  1.00 14.37 ? 19  ASP A CA   1 
ATOM   182  C  C    . ASP A 1 19  ? 10.576  3.942   18.083  1.00 13.85 ? 19  ASP A C    1 
ATOM   183  O  O    . ASP A 1 19  ? 10.475  5.133   18.004  1.00 14.77 ? 19  ASP A O    1 
ATOM   184  C  CB   . ASP A 1 19  ? 11.123  3.026   15.799  1.00 16.78 ? 19  ASP A CB   1 
ATOM   185  C  CG   . ASP A 1 19  ? 12.218  2.960   14.741  1.00 18.53 ? 19  ASP A CG   1 
ATOM   186  O  OD1  . ASP A 1 19  ? 13.278  3.511   14.942  1.00 23.45 ? 19  ASP A OD1  1 
ATOM   187  O  OD2  . ASP A 1 19  ? 12.001  2.290   13.708  1.00 32.20 ? 19  ASP A OD2  1 
ATOM   188  N  N    . PHE A 1 20  ? 9.867   3.188   18.917  1.00 12.73 ? 20  PHE A N    1 
ATOM   189  C  CA   . PHE A 1 20  ? 8.728   3.695   19.663  1.00 11.13 ? 20  PHE A CA   1 
ATOM   190  C  C    . PHE A 1 20  ? 8.864   3.174   21.116  1.00 11.63 ? 20  PHE A C    1 
ATOM   191  O  O    . PHE A 1 20  ? 8.173   2.201   21.495  1.00 11.05 ? 20  PHE A O    1 
ATOM   192  C  CB   . PHE A 1 20  ? 7.396   3.221   19.003  1.00 12.40 ? 20  PHE A CB   1 
ATOM   193  C  CG   . PHE A 1 20  ? 7.293   3.616   17.568  1.00 12.85 ? 20  PHE A CG   1 
ATOM   194  C  CD1  . PHE A 1 20  ? 6.906   4.870   17.225  1.00 13.81 ? 20  PHE A CD1  1 
ATOM   195  C  CD2  . PHE A 1 20  ? 7.673   2.695   16.547  1.00 14.64 ? 20  PHE A CD2  1 
ATOM   196  C  CE1  . PHE A 1 20  ? 6.851   5.229   15.848  1.00 16.51 ? 20  PHE A CE1  1 
ATOM   197  C  CE2  . PHE A 1 20  ? 7.669   3.039   15.194  1.00 16.39 ? 20  PHE A CE2  1 
ATOM   198  C  CZ   . PHE A 1 20  ? 7.230   4.320   14.897  1.00 16.50 ? 20  PHE A CZ   1 
ATOM   199  N  N    . PRO A 1 21  ? 9.694   3.806   21.946  1.00 12.19 ? 21  PRO A N    1 
ATOM   200  C  CA   . PRO A 1 21  ? 9.971   3.254   23.266  1.00 12.04 ? 21  PRO A CA   1 
ATOM   201  C  C    . PRO A 1 21  ? 8.700   3.206   24.186  1.00 12.03 ? 21  PRO A C    1 
ATOM   202  O  O    . PRO A 1 21  ? 8.755   2.411   25.138  1.00 12.31 ? 21  PRO A O    1 
ATOM   203  C  CB   . PRO A 1 21  ? 11.077  4.199   23.886  1.00 14.78 ? 21  PRO A CB   1 
ATOM   204  C  CG   . PRO A 1 21  ? 11.200  5.210   22.879  1.00 20.27 ? 21  PRO A CG   1 
ATOM   205  C  CD   . PRO A 1 21  ? 10.650  4.881   21.568  1.00 13.86 ? 21  PRO A CD   1 
ATOM   206  N  N    . ILE A 1 22  ? 7.640   3.968   23.894  1.00 11.48 ? 22  ILE A N    1 
ATOM   207  C  CA   . ILE A 1 22  ? 6.380   3.876   24.618  1.00 10.45 ? 22  ILE A CA   1 
ATOM   208  C  C    . ILE A 1 22  ? 5.790   2.458   24.505  1.00 9.82  ? 22  ILE A C    1 
ATOM   209  O  O    . ILE A 1 22  ? 4.897   2.094   25.255  1.00 10.04 ? 22  ILE A O    1 
ATOM   210  C  CB   . ILE A 1 22  ? 5.384   4.934   24.110  1.00 9.89  ? 22  ILE A CB   1 
ATOM   211  C  CG1  . ILE A 1 22  ? 4.352   5.240   25.181  1.00 11.35 ? 22  ILE A CG1  1 
ATOM   212  C  CG2  . ILE A 1 22  ? 4.803   4.570   22.771  1.00 10.42 ? 22  ILE A CG2  1 
ATOM   213  C  CD1  . ILE A 1 22  ? 3.402   6.362   24.762  1.00 15.89 ? 22  ILE A CD1  1 
ATOM   214  N  N    . ALA A 1 23  ? 6.324   1.607   23.609  1.00 10.06 ? 23  ALA A N    1 
ATOM   215  C  CA   . ALA A 1 23  ? 5.864   0.208   23.463  1.00 10.10 ? 23  ALA A CA   1 
ATOM   216  C  C    . ALA A 1 23  ? 5.981   -0.525  24.800  1.00 10.50 ? 23  ALA A C    1 
ATOM   217  O  O    . ALA A 1 23  ? 5.259   -1.537  25.007  1.00 10.35 ? 23  ALA A O    1 
ATOM   218  C  CB   . ALA A 1 23  ? 6.713   -0.538  22.429  1.00 10.69 ? 23  ALA A CB   1 
ATOM   219  N  N    . LYS A 1 24  ? 6.909   -0.100  25.678  1.00 10.86 ? 24  LYS A N    1 
ATOM   220  C  CA   . LYS A 1 24  ? 7.073   -0.693  27.014  1.00 11.50 ? 24  LYS A CA   1 
ATOM   221  C  C    . LYS A 1 24  ? 6.447   0.215   28.113  1.00 12.83 ? 24  LYS A C    1 
ATOM   222  O  O    . LYS A 1 24  ? 6.840   0.100   29.286  1.00 14.33 ? 24  LYS A O    1 
ATOM   223  C  CB   . LYS A 1 24  ? 8.559   -0.942  27.360  1.00 13.03 ? 24  LYS A CB   1 
ATOM   224  C  CG   . LYS A 1 24  ? 9.199   -1.902  26.363  1.00 13.79 ? 24  LYS A CG   1 
ATOM   225  C  CD   . LYS A 1 24  ? 10.650  -2.201  26.759  1.00 18.25 ? 24  LYS A CD   1 
ATOM   226  C  CE   . LYS A 1 24  ? 11.380  -3.119  25.806  1.00 19.02 ? 24  LYS A CE   1 
ATOM   227  N  NZ   . LYS A 1 24  ? 10.953  -4.480  25.944  1.00 25.27 ? 24  LYS A NZ   1 
ATOM   228  N  N    . GLY A 1 25  ? 5.453   1.029   27.788  1.00 11.14 ? 25  GLY A N    1 
ATOM   229  C  CA   . GLY A 1 25  ? 4.849   1.992   28.713  1.00 12.11 ? 25  GLY A CA   1 
ATOM   230  C  C    . GLY A 1 25  ? 3.861   1.367   29.663  1.00 10.55 ? 25  GLY A C    1 
ATOM   231  O  O    . GLY A 1 25  ? 3.669   0.164   29.769  1.00 11.97 ? 25  GLY A O    1 
ATOM   232  N  N    . GLU A 1 26  ? 3.230   2.279   30.359  1.00 12.41 ? 26  GLU A N    1 
ATOM   233  C  CA   . GLU A 1 26  ? 2.327   1.900   31.483  1.00 12.64 ? 26  GLU A CA   1 
ATOM   234  C  C    . GLU A 1 26  ? 0.894   1.645   31.064  1.00 10.52 ? 26  GLU A C    1 
ATOM   235  O  O    . GLU A 1 26  ? 0.122   1.150   31.924  1.00 12.03 ? 26  GLU A O    1 
ATOM   236  C  CB   . GLU A 1 26  ? 2.374   2.999   32.569  1.00 15.16 ? 26  GLU A CB   1 
ATOM   237  C  CG   . GLU A 1 26  ? 3.808   3.191   33.171  1.00 16.58 ? 26  GLU A CG   1 
ATOM   238  C  CD   . GLU A 1 26  ? 4.340   1.913   33.823  1.00 21.92 ? 26  GLU A CD   1 
ATOM   239  O  OE1  . GLU A 1 26  ? 3.606   1.314   34.654  1.00 26.78 ? 26  GLU A OE1  1 
ATOM   240  O  OE2  . GLU A 1 26  ? 5.417   1.474   33.370  1.00 30.08 ? 26  GLU A OE2  1 
ATOM   241  N  N    . ARG A 1 27  ? 0.507   1.949   29.831  1.00 8.48  ? 27  ARG A N    1 
ATOM   242  C  CA   . ARG A 1 27  ? -0.883  1.697   29.456  1.00 7.80  ? 27  ARG A CA   1 
ATOM   243  C  C    . ARG A 1 27  ? -0.983  1.284   28.000  1.00 6.97  ? 27  ARG A C    1 
ATOM   244  O  O    . ARG A 1 27  ? -1.669  1.895   27.168  1.00 7.41  ? 27  ARG A O    1 
ATOM   245  C  CB   . ARG A 1 27  ? -1.781  2.905   29.763  1.00 9.68  ? 27  ARG A CB   1 
ATOM   246  C  CG   . ARG A 1 27  ? -1.411  4.194   29.044  1.00 11.00 ? 27  ARG A CG   1 
ATOM   247  C  CD   . ARG A 1 27  ? -2.406  5.307   29.368  1.00 13.31 ? 27  ARG A CD   1 
ATOM   248  N  NE   . ARG A 1 27  ? -3.569  5.282   28.482  1.00 11.30 ? 27  ARG A NE   1 
ATOM   249  C  CZ   . ARG A 1 27  ? -4.506  6.225   28.448  1.00 9.88  ? 27  ARG A CZ   1 
ATOM   250  N  NH1  . ARG A 1 27  ? -4.425  7.277   29.252  1.00 12.39 ? 27  ARG A NH1  1 
ATOM   251  N  NH2  . ARG A 1 27  ? -5.527  6.117   27.608  1.00 10.46 ? 27  ARG A NH2  1 
ATOM   252  N  N    . GLN A 1 28  ? -0.256  0.198   27.719  1.00 6.64  ? 28  GLN A N    1 
ATOM   253  C  CA   . GLN A 1 28  ? -0.230  -0.338  26.343  1.00 6.03  ? 28  GLN A CA   1 
ATOM   254  C  C    . GLN A 1 28  ? -1.385  -1.294  26.088  1.00 6.35  ? 28  GLN A C    1 
ATOM   255  O  O    . GLN A 1 28  ? -1.878  -1.994  26.988  1.00 6.85  ? 28  GLN A O    1 
ATOM   256  C  CB   . GLN A 1 28  ? 1.127   -1.016  26.092  1.00 6.88  ? 28  GLN A CB   1 
ATOM   257  C  CG   . GLN A 1 28  ? 2.275   0.044   25.990  1.00 7.91  ? 28  GLN A CG   1 
ATOM   258  C  CD   . GLN A 1 28  ? 2.154   0.843   24.725  1.00 7.24  ? 28  GLN A CD   1 
ATOM   259  O  OE1  . GLN A 1 28  ? 2.319   0.290   23.618  1.00 7.32  ? 28  GLN A OE1  1 
ATOM   260  N  NE2  . GLN A 1 28  ? 1.809   2.133   24.813  1.00 7.34  ? 28  GLN A NE2  1 
ATOM   261  N  N    . SER A 1 29  ? -1.756  -1.401  24.798  1.00 5.61  ? 29  SER A N    1 
ATOM   262  C  CA   . SER A 1 29  ? -2.813  -2.264  24.318  1.00 5.27  ? 29  SER A CA   1 
ATOM   263  C  C    . SER A 1 29  ? -2.296  -3.155  23.234  1.00 5.56  ? 29  SER A C    1 
ATOM   264  O  O    . SER A 1 29  ? -1.330  -2.797  22.541  1.00 6.11  ? 29  SER A O    1 
ATOM   265  C  CB   . SER A 1 29  ? -3.970  -1.426  23.811  1.00 5.47  ? 29  SER A CB   1 
ATOM   266  O  OG   . SER A 1 29  ? -4.575  -0.673  24.869  1.00 5.52  ? 29  SER A OG   1 
ATOM   267  N  N    . PRO A 1 30  ? -2.941  -4.276  22.974  1.00 5.34  ? 30  PRO A N    1 
ATOM   268  C  CA   . PRO A 1 30  ? -4.093  -4.843  23.681  1.00 5.08  ? 30  PRO A CA   1 
ATOM   269  C  C    . PRO A 1 30  ? -3.673  -5.505  24.993  1.00 5.47  ? 30  PRO A C    1 
ATOM   270  O  O    . PRO A 1 30  ? -2.491  -5.543  25.320  1.00 6.28  ? 30  PRO A O    1 
ATOM   271  C  CB   . PRO A 1 30  ? -4.618  -5.878  22.681  1.00 5.61  ? 30  PRO A CB   1 
ATOM   272  C  CG   . PRO A 1 30  ? -3.349  -6.453  22.083  1.00 5.92  ? 30  PRO A CG   1 
ATOM   273  C  CD   . PRO A 1 30  ? -2.442  -5.221  21.933  1.00 6.12  ? 30  PRO A CD   1 
ATOM   274  N  N    . VAL A 1 31  ? -4.645  -6.061  25.679  1.00 5.43  ? 31  VAL A N    1 
ATOM   275  C  CA   . VAL A 1 31  ? -4.477  -6.815  26.930  1.00 5.96  ? 31  VAL A CA   1 
ATOM   276  C  C    . VAL A 1 31  ? -5.355  -8.050  26.861  1.00 6.40  ? 31  VAL A C    1 
ATOM   277  O  O    . VAL A 1 31  ? -6.358  -8.110  26.114  1.00 6.59  ? 31  VAL A O    1 
ATOM   278  C  CB   . VAL A 1 31  ? -4.812  -5.960  28.176  1.00 6.55  ? 31  VAL A CB   1 
ATOM   279  C  CG1  . VAL A 1 31  ? -3.844  -4.783  28.303  1.00 7.76  ? 31  VAL A CG1  1 
ATOM   280  C  CG2  . VAL A 1 31  ? -6.259  -5.556  28.231  1.00 7.04  ? 31  VAL A CG2  1 
ATOM   281  N  N    . ASP A 1 32  ? -5.026  -9.034  27.722  1.00 6.55  ? 32  ASP A N    1 
ATOM   282  C  CA   . ASP A 1 32  ? -5.954  -10.145 28.014  1.00 6.36  ? 32  ASP A CA   1 
ATOM   283  C  C    . ASP A 1 32  ? -6.986  -9.594  29.027  1.00 6.79  ? 32  ASP A C    1 
ATOM   284  O  O    . ASP A 1 32  ? -6.660  -8.945  30.023  1.00 8.35  ? 32  ASP A O    1 
ATOM   285  C  CB   . ASP A 1 32  ? -5.211  -11.300 28.612  1.00 7.49  ? 32  ASP A CB   1 
ATOM   286  C  CG   . ASP A 1 32  ? -6.134  -12.489 28.917  1.00 7.68  ? 32  ASP A CG   1 
ATOM   287  O  OD1  . ASP A 1 32  ? -6.838  -12.929 27.988  1.00 7.45  ? 32  ASP A OD1  1 
ATOM   288  O  OD2  . ASP A 1 32  ? -6.182  -12.912 30.100  1.00 10.55 ? 32  ASP A OD2  1 
ATOM   289  N  N    A ILE A 1 33  ? -8.234  -9.981  28.781  0.50 5.85  ? 33  ILE A N    1 
ATOM   290  N  N    B ILE A 1 33  ? -8.253  -9.825  28.721  0.50 6.55  ? 33  ILE A N    1 
ATOM   291  C  CA   A ILE A 1 33  ? -9.417  -9.585  29.577  0.50 6.26  ? 33  ILE A CA   1 
ATOM   292  C  CA   B ILE A 1 33  ? -9.328  -9.478  29.654  0.50 7.94  ? 33  ILE A CA   1 
ATOM   293  C  C    A ILE A 1 33  ? -9.785  -10.829 30.395  0.50 7.08  ? 33  ILE A C    1 
ATOM   294  C  C    B ILE A 1 33  ? -9.482  -10.716 30.541  0.50 6.91  ? 33  ILE A C    1 
ATOM   295  O  O    A ILE A 1 33  ? -10.305 -11.823 29.858  0.50 6.52  ? 33  ILE A O    1 
ATOM   296  O  O    B ILE A 1 33  ? -10.068 -11.727 30.118  0.50 7.62  ? 33  ILE A O    1 
ATOM   297  C  CB   A ILE A 1 33  ? -10.547 -9.103  28.681  0.50 5.50  ? 33  ILE A CB   1 
ATOM   298  C  CB   B ILE A 1 33  ? -10.646 -9.117  28.907  0.50 7.81  ? 33  ILE A CB   1 
ATOM   299  C  CG1  A ILE A 1 33  ? -10.139 -7.919  27.846  0.50 5.39  ? 33  ILE A CG1  1 
ATOM   300  C  CG1  B ILE A 1 33  ? -10.458 -7.861  28.069  0.50 8.44  ? 33  ILE A CG1  1 
ATOM   301  C  CG2  A ILE A 1 33  ? -11.773 -8.805  29.595  0.50 7.25  ? 33  ILE A CG2  1 
ATOM   302  C  CG2  B ILE A 1 33  ? -11.871 -9.017  29.926  0.50 8.60  ? 33  ILE A CG2  1 
ATOM   303  C  CD1  A ILE A 1 33  ? -11.166 -7.584  26.728  0.50 6.26  ? 33  ILE A CD1  1 
ATOM   304  C  CD1  B ILE A 1 33  ? -11.522 -7.671  26.943  0.50 10.17 ? 33  ILE A CD1  1 
ATOM   305  N  N    A ASP A 1 34  ? -9.505  -10.766 31.696  0.50 7.16  ? 34  ASP A N    1 
ATOM   306  N  N    B ASP A 1 34  ? -9.028  -10.632 31.780  0.50 7.71  ? 34  ASP A N    1 
ATOM   307  C  CA   A ASP A 1 34  ? -9.790  -11.884 32.609  0.50 6.98  ? 34  ASP A CA   1 
ATOM   308  C  CA   B ASP A 1 34  ? -9.301  -11.651 32.757  0.50 8.37  ? 34  ASP A CA   1 
ATOM   309  C  C    A ASP A 1 34  ? -11.230 -11.615 33.103  0.50 6.41  ? 34  ASP A C    1 
ATOM   310  C  C    B ASP A 1 34  ? -10.707 -11.367 33.282  0.50 8.00  ? 34  ASP A C    1 
ATOM   311  O  O    A ASP A 1 34  ? -11.486 -10.683 33.935  0.50 8.14  ? 34  ASP A O    1 
ATOM   312  O  O    B ASP A 1 34  ? -10.916 -10.380 34.060  0.50 9.40  ? 34  ASP A O    1 
ATOM   313  C  CB   A ASP A 1 34  ? -8.804  -11.858 33.783  0.50 8.51  ? 34  ASP A CB   1 
ATOM   314  C  CB   B ASP A 1 34  ? -8.354  -11.646 33.943  0.50 9.61  ? 34  ASP A CB   1 
ATOM   315  C  CG   A ASP A 1 34  ? -8.830  -13.131 34.598  0.50 10.67 ? 34  ASP A CG   1 
ATOM   316  C  CG   B ASP A 1 34  ? -8.736  -12.685 34.996  0.50 11.21 ? 34  ASP A CG   1 
ATOM   317  O  OD1  A ASP A 1 34  ? -9.308  -13.097 35.752  0.50 16.34 ? 34  ASP A OD1  1 
ATOM   318  O  OD1  B ASP A 1 34  ? -9.932  -13.046 35.135  0.50 14.26 ? 34  ASP A OD1  1 
ATOM   319  O  OD2  A ASP A 1 34  ? -8.349  -14.174 34.096  0.50 14.32 ? 34  ASP A OD2  1 
ATOM   320  O  OD2  B ASP A 1 34  ? -7.814  -13.135 35.701  0.50 17.36 ? 34  ASP A OD2  1 
ATOM   321  N  N    A THR A 1 35  ? -12.187 -12.388 32.614  0.50 7.13  ? 35  THR A N    1 
ATOM   322  N  N    B THR A 1 35  ? -11.663 -12.175 32.882  0.50 7.89  ? 35  THR A N    1 
ATOM   323  C  CA   A THR A 1 35  ? -13.587 -12.091 32.867  0.50 7.16  ? 35  THR A CA   1 
ATOM   324  C  CA   B THR A 1 35  ? -13.057 -11.815 33.110  0.50 8.51  ? 35  THR A CA   1 
ATOM   325  C  C    A THR A 1 35  ? -13.997 -12.210 34.321  0.50 8.04  ? 35  THR A C    1 
ATOM   326  C  C    B THR A 1 35  ? -13.428 -11.966 34.595  0.50 9.21  ? 35  THR A C    1 
ATOM   327  O  O    A THR A 1 35  ? -14.930 -11.512 34.726  0.50 9.47  ? 35  THR A O    1 
ATOM   328  O  O    B THR A 1 35  ? -14.345 -11.268 35.061  0.50 10.24 ? 35  THR A O    1 
ATOM   329  C  CB   A THR A 1 35  ? -14.490 -13.051 32.067  0.50 9.09  ? 35  THR A CB   1 
ATOM   330  C  CB   B THR A 1 35  ? -13.968 -12.712 32.319  0.50 8.33  ? 35  THR A CB   1 
ATOM   331  O  OG1  A THR A 1 35  ? -14.358 -14.359 32.552  0.50 8.59  ? 35  THR A OG1  1 
ATOM   332  O  OG1  B THR A 1 35  ? -13.803 -14.059 32.770  0.50 11.19 ? 35  THR A OG1  1 
ATOM   333  C  CG2  A THR A 1 35  ? -14.250 -13.042 30.539  0.50 11.24 ? 35  THR A CG2  1 
ATOM   334  C  CG2  B THR A 1 35  ? -13.752 -12.563 30.764  0.50 9.32  ? 35  THR A CG2  1 
ATOM   335  N  N    A HIS A 1 36  ? -13.362 -13.071 35.079  0.50 7.45  ? 36  HIS A N    1 
ATOM   336  N  N    B HIS A 1 36  ? -12.667 -12.755 35.345  0.50 10.03 ? 36  HIS A N    1 
ATOM   337  C  CA   A HIS A 1 36  ? -13.610 -13.199 36.499  0.50 8.72  ? 36  HIS A CA   1 
ATOM   338  C  CA   B HIS A 1 36  ? -12.873 -12.944 36.754  0.50 11.49 ? 36  HIS A CA   1 
ATOM   339  C  C    A HIS A 1 36  ? -13.122 -12.080 37.367  0.50 8.91  ? 36  HIS A C    1 
ATOM   340  C  C    B HIS A 1 36  ? -12.386 -11.785 37.571  0.50 11.32 ? 36  HIS A C    1 
ATOM   341  O  O    A HIS A 1 36  ? -13.756 -11.805 38.403  0.50 11.92 ? 36  HIS A O    1 
ATOM   342  O  O    B HIS A 1 36  ? -13.108 -11.358 38.487  0.50 15.89 ? 36  HIS A O    1 
ATOM   343  C  CB   A HIS A 1 36  ? -13.123 -14.558 37.033  0.50 9.15  ? 36  HIS A CB   1 
ATOM   344  C  CB   B HIS A 1 36  ? -12.321 -14.313 37.176  0.50 11.61 ? 36  HIS A CB   1 
ATOM   345  C  CG   A HIS A 1 36  ? -14.035 -15.630 36.579  0.50 9.69  ? 36  HIS A CG   1 
ATOM   346  C  CG   B HIS A 1 36  ? -13.031 -15.447 36.463  0.50 13.28 ? 36  HIS A CG   1 
ATOM   347  N  ND1  A HIS A 1 36  ? -13.739 -16.581 35.599  0.50 12.57 ? 36  HIS A ND1  1 
ATOM   348  N  ND1  B HIS A 1 36  ? -12.509 -16.099 35.372  0.50 15.57 ? 36  HIS A ND1  1 
ATOM   349  C  CD2  A HIS A 1 36  ? -15.350 -15.742 36.881  0.50 10.60 ? 36  HIS A CD2  1 
ATOM   350  C  CD2  B HIS A 1 36  ? -14.318 -15.883 36.566  0.50 18.00 ? 36  HIS A CD2  1 
ATOM   351  C  CE1  A HIS A 1 36  ? -14.848 -17.302 35.425  0.50 11.89 ? 36  HIS A CE1  1 
ATOM   352  C  CE1  B HIS A 1 36  ? -13.374 -16.981 34.922  0.50 14.96 ? 36  HIS A CE1  1 
ATOM   353  N  NE2  A HIS A 1 36  ? -15.815 -16.834 36.209  0.50 14.58 ? 36  HIS A NE2  1 
ATOM   354  N  NE2  B HIS A 1 36  ? -14.484 -16.884 35.635  0.50 19.53 ? 36  HIS A NE2  1 
ATOM   355  N  N    A THR A 1 37  ? -12.052 -11.383 36.936  0.50 11.09 ? 37  THR A N    1 
ATOM   356  N  N    B THR A 1 37  ? -11.300 -11.150 37.143  0.50 11.05 ? 37  THR A N    1 
ATOM   357  C  CA   A THR A 1 37  ? -11.489 -10.287 37.741  0.50 11.16 ? 37  THR A CA   1 
ATOM   358  C  CA   B THR A 1 37  ? -10.752 -9.959  37.743  0.50 12.58 ? 37  THR A CA   1 
ATOM   359  C  C    A THR A 1 37  ? -11.917 -8.916  37.382  0.50 12.61 ? 37  THR A C    1 
ATOM   360  C  C    B THR A 1 37  ? -11.440 -8.669  37.227  0.50 12.35 ? 37  THR A C    1 
ATOM   361  O  O    A THR A 1 37  ? -11.892 -8.023  38.206  0.50 12.40 ? 37  THR A O    1 
ATOM   362  O  O    B THR A 1 37  ? -11.250 -7.620  37.895  0.50 14.53 ? 37  THR A O    1 
ATOM   363  C  CB   A THR A 1 37  ? -9.890  -10.322 37.766  0.50 14.67 ? 37  THR A CB   1 
ATOM   364  C  CB   B THR A 1 37  ? -9.266  -10.006 37.361  0.50 13.71 ? 37  THR A CB   1 
ATOM   365  O  OG1  A THR A 1 37  ? -9.417  -11.402 38.561  0.50 19.25 ? 37  THR A OG1  1 
ATOM   366  O  OG1  B THR A 1 37  ? -8.780  -11.268 37.837  0.50 19.56 ? 37  THR A OG1  1 
ATOM   367  C  CG2  A THR A 1 37  ? -9.196  -9.078  38.275  0.50 14.81 ? 37  THR A CG2  1 
ATOM   368  C  CG2  B THR A 1 37  ? -8.496  -8.784  38.072  0.50 14.05 ? 37  THR A CG2  1 
ATOM   369  N  N    . ALA A 1 38  ? -12.323 -8.726  36.150  1.00 12.96 ? 38  ALA A N    1 
ATOM   370  C  CA   . ALA A 1 38  ? -12.952 -7.473  35.727  1.00 11.98 ? 38  ALA A CA   1 
ATOM   371  C  C    . ALA A 1 38  ? -14.046 -7.133  36.678  1.00 14.73 ? 38  ALA A C    1 
ATOM   372  O  O    . ALA A 1 38  ? -14.690 -7.977  37.183  1.00 18.90 ? 38  ALA A O    1 
ATOM   373  C  CB   . ALA A 1 38  ? -13.489 -7.623  34.315  1.00 11.94 ? 38  ALA A CB   1 
ATOM   374  N  N    . LYS A 1 39  ? -14.134 -5.895  37.065  1.00 13.79 ? 39  LYS A N    1 
ATOM   375  C  CA   . LYS A 1 39  ? -15.035 -5.381  38.081  1.00 15.44 ? 39  LYS A CA   1 
ATOM   376  C  C    . LYS A 1 39  ? -16.305 -4.875  37.380  1.00 13.24 ? 39  LYS A C    1 
ATOM   377  O  O    . LYS A 1 39  ? -16.261 -3.922  36.651  1.00 12.21 ? 39  LYS A O    1 
ATOM   378  C  CB   . LYS A 1 39  ? -14.293 -4.203  38.790  1.00 17.38 ? 39  LYS A CB   1 
ATOM   379  C  CG   . LYS A 1 39  ? -15.025 -3.383  39.808  1.00 19.77 ? 39  LYS A CG   1 
ATOM   380  C  CD   . LYS A 1 39  ? -15.238 -4.122  41.126  1.00 19.21 ? 39  LYS A CD   1 
ATOM   381  C  CE   . LYS A 1 39  ? -16.050 -3.360  42.081  1.00 23.83 ? 39  LYS A CE   1 
ATOM   382  N  NZ   . LYS A 1 39  ? -16.286 -4.109  43.270  1.00 22.27 ? 39  LYS A NZ   1 
ATOM   383  N  N    . TYR A 1 40  ? -17.459 -5.419  37.757  1.00 14.94 ? 40  TYR A N    1 
ATOM   384  C  CA   . TYR A 1 40  ? -18.742 -4.854  37.386  1.00 13.90 ? 40  TYR A CA   1 
ATOM   385  C  C    . TYR A 1 40  ? -18.850 -3.471  38.010  1.00 13.78 ? 40  TYR A C    1 
ATOM   386  O  O    . TYR A 1 40  ? -18.701 -3.313  39.248  1.00 15.93 ? 40  TYR A O    1 
ATOM   387  C  CB   . TYR A 1 40  ? -19.974 -5.706  37.826  1.00 16.93 ? 40  TYR A CB   1 
ATOM   388  C  CG   . TYR A 1 40  ? -21.256 -4.995  37.650  1.00 17.90 ? 40  TYR A CG   1 
ATOM   389  C  CD1  . TYR A 1 40  ? -21.695 -4.591  36.413  1.00 18.80 ? 40  TYR A CD1  1 
ATOM   390  C  CD2  . TYR A 1 40  ? -22.095 -4.771  38.744  1.00 22.25 ? 40  TYR A CD2  1 
ATOM   391  C  CE1  . TYR A 1 40  ? -22.872 -3.896  36.245  1.00 20.12 ? 40  TYR A CE1  1 
ATOM   392  C  CE2  . TYR A 1 40  ? -23.307 -4.121  38.538  1.00 21.76 ? 40  TYR A CE2  1 
ATOM   393  C  CZ   . TYR A 1 40  ? -23.704 -3.679  37.313  1.00 23.42 ? 40  TYR A CZ   1 
ATOM   394  O  OH   . TYR A 1 40  ? -24.934 -3.008  37.155  1.00 26.26 ? 40  TYR A OH   1 
ATOM   395  N  N    . ASP A 1 41  ? -19.150 -2.489  37.191  1.00 12.30 ? 41  ASP A N    1 
ATOM   396  C  CA   . ASP A 1 41  ? -19.229 -1.081  37.687  1.00 13.76 ? 41  ASP A CA   1 
ATOM   397  C  C    . ASP A 1 41  ? -20.624 -0.563  37.410  1.00 15.81 ? 41  ASP A C    1 
ATOM   398  O  O    . ASP A 1 41  ? -20.967 -0.207  36.247  1.00 14.98 ? 41  ASP A O    1 
ATOM   399  C  CB   . ASP A 1 41  ? -18.159 -0.210  37.002  1.00 14.49 ? 41  ASP A CB   1 
ATOM   400  C  CG   . ASP A 1 41  ? -18.104 1.173   37.472  1.00 17.39 ? 41  ASP A CG   1 
ATOM   401  O  OD1  . ASP A 1 41  ? -19.052 1.578   38.247  1.00 18.32 ? 41  ASP A OD1  1 
ATOM   402  O  OD2  . ASP A 1 41  ? -17.110 1.915   37.143  1.00 19.86 ? 41  ASP A OD2  1 
ATOM   403  N  N    . PRO A 1 42  ? -21.473 -0.512  38.440  1.00 17.67 ? 42  PRO A N    1 
ATOM   404  C  CA   . PRO A 1 42  ? -22.829 -0.050  38.214  1.00 20.04 ? 42  PRO A CA   1 
ATOM   405  C  C    . PRO A 1 42  ? -22.889 1.422   37.823  1.00 18.72 ? 42  PRO A C    1 
ATOM   406  O  O    . PRO A 1 42  ? -23.956 1.850   37.387  1.00 24.32 ? 42  PRO A O    1 
ATOM   407  C  CB   . PRO A 1 42  ? -23.463 -0.244  39.603  1.00 21.56 ? 42  PRO A CB   1 
ATOM   408  C  CG   . PRO A 1 42  ? -22.384 -0.097  40.590  1.00 21.78 ? 42  PRO A CG   1 
ATOM   409  C  CD   . PRO A 1 42  ? -21.235 -0.783  39.877  1.00 18.19 ? 42  PRO A CD   1 
ATOM   410  N  N    . SER A 1 43  ? -21.808 2.196   38.009  1.00 18.90 ? 43  SER A N    1 
ATOM   411  C  CA   . SER A 1 43  ? -21.757 3.578   37.544  1.00 20.22 ? 43  SER A CA   1 
ATOM   412  C  C    . SER A 1 43  ? -21.644 3.700   35.991  1.00 19.54 ? 43  SER A C    1 
ATOM   413  O  O    . SER A 1 43  ? -21.854 4.777   35.389  1.00 22.05 ? 43  SER A O    1 
ATOM   414  C  CB   . SER A 1 43  ? -20.621 4.393   38.201  1.00 20.29 ? 43  SER A CB   1 
ATOM   415  O  OG   . SER A 1 43  ? -19.301 4.170   37.785  1.00 22.01 ? 43  SER A OG   1 
ATOM   416  N  N    . LEU A 1 44  ? -21.240 2.620   35.305  1.00 18.95 ? 44  LEU A N    1 
ATOM   417  C  CA   . LEU A 1 44  ? -21.051 2.649   33.833  1.00 16.72 ? 44  LEU A CA   1 
ATOM   418  C  C    . LEU A 1 44  ? -22.384 2.837   33.184  1.00 18.01 ? 44  LEU A C    1 
ATOM   419  O  O    . LEU A 1 44  ? -23.398 2.371   33.660  1.00 22.16 ? 44  LEU A O    1 
ATOM   420  C  CB   . LEU A 1 44  ? -20.291 1.444   33.329  1.00 15.14 ? 44  LEU A CB   1 
ATOM   421  C  CG   . LEU A 1 44  ? -18.848 1.440   33.542  1.00 13.60 ? 44  LEU A CG   1 
ATOM   422  C  CD1  . LEU A 1 44  ? -18.365 0.058   33.215  1.00 15.20 ? 44  LEU A CD1  1 
ATOM   423  C  CD2  . LEU A 1 44  ? -18.115 2.542   32.785  1.00 16.44 ? 44  LEU A CD2  1 
ATOM   424  N  N    . LYS A 1 45  ? -22.419 3.596   32.108  1.00 17.39 ? 45  LYS A N    1 
ATOM   425  C  CA   . LYS A 1 45  ? -23.695 3.838   31.324  1.00 17.22 ? 45  LYS A CA   1 
ATOM   426  C  C    . LYS A 1 45  ? -23.779 2.967   30.136  1.00 15.86 ? 45  LYS A C    1 
ATOM   427  O  O    . LYS A 1 45  ? -22.784 2.433   29.635  1.00 15.57 ? 45  LYS A O    1 
ATOM   428  C  CB   . LYS A 1 45  ? -23.788 5.264   30.933  1.00 17.55 ? 45  LYS A CB   1 
ATOM   429  C  CG   . LYS A 1 45  ? -23.690 6.230   32.044  1.00 21.02 ? 45  LYS A CG   1 
ATOM   430  C  CD   . LYS A 1 45  ? -23.696 7.655   31.755  1.00 24.71 ? 45  LYS A CD   1 
ATOM   431  C  CE   . LYS A 1 45  ? -23.152 8.433   33.019  1.00 30.27 ? 45  LYS A CE   1 
ATOM   432  N  NZ   . LYS A 1 45  ? -23.858 8.110   34.319  1.00 37.71 ? 45  LYS A NZ   1 
ATOM   433  N  N    . PRO A 1 46  ? -25.002 2.770   29.611  1.00 15.58 ? 46  PRO A N    1 
ATOM   434  C  CA   . PRO A 1 46  ? -25.093 2.112   28.291  1.00 15.58 ? 46  PRO A CA   1 
ATOM   435  C  C    . PRO A 1 46  ? -24.274 2.904   27.294  1.00 12.69 ? 46  PRO A C    1 
ATOM   436  O  O    . PRO A 1 46  ? -24.271 4.081   27.362  1.00 14.55 ? 46  PRO A O    1 
ATOM   437  C  CB   . PRO A 1 46  ? -26.607 2.194   27.980  1.00 15.60 ? 46  PRO A CB   1 
ATOM   438  C  CG   . PRO A 1 46  ? -27.304 2.374   29.291  1.00 19.77 ? 46  PRO A CG   1 
ATOM   439  C  CD   . PRO A 1 46  ? -26.317 3.184   30.130  1.00 17.03 ? 46  PRO A CD   1 
ATOM   440  N  N    . LEU A 1 47  ? -23.702 2.157   26.382  1.00 14.77 ? 47  LEU A N    1 
ATOM   441  C  CA   . LEU A 1 47  ? -23.030 2.767   25.307  1.00 12.85 ? 47  LEU A CA   1 
ATOM   442  C  C    . LEU A 1 47  ? -24.061 3.410   24.368  1.00 14.72 ? 47  LEU A C    1 
ATOM   443  O  O    . LEU A 1 47  ? -25.081 2.724   24.101  1.00 19.28 ? 47  LEU A O    1 
ATOM   444  C  CB   . LEU A 1 47  ? -22.155 1.766   24.597  1.00 16.68 ? 47  LEU A CB   1 
ATOM   445  C  CG   . LEU A 1 47  ? -21.133 2.087   23.632  1.00 16.90 ? 47  LEU A CG   1 
ATOM   446  C  CD1  . LEU A 1 47  ? -20.060 2.966   24.369  1.00 18.99 ? 47  LEU A CD1  1 
ATOM   447  C  CD2  . LEU A 1 47  ? -20.520 0.780   23.051  1.00 18.37 ? 47  LEU A CD2  1 
ATOM   448  N  N    . SER A 1 48  ? -23.775 4.602   23.866  1.00 12.47 ? 48  SER A N    1 
ATOM   449  C  CA   . SER A 1 48  ? -24.596 5.245   22.836  1.00 12.75 ? 48  SER A CA   1 
ATOM   450  C  C    . SER A 1 48  ? -23.770 5.272   21.535  1.00 12.60 ? 48  SER A C    1 
ATOM   451  O  O    . SER A 1 48  ? -22.785 5.972   21.402  1.00 11.87 ? 48  SER A O    1 
ATOM   452  C  CB   . SER A 1 48  ? -24.939 6.670   23.281  1.00 13.76 ? 48  SER A CB   1 
ATOM   453  O  OG   . SER A 1 48  ? -25.557 7.404   22.237  1.00 15.10 ? 48  SER A OG   1 
ATOM   454  N  N    . VAL A 1 49  ? -24.270 4.511   20.598  1.00 12.82 ? 49  VAL A N    1 
ATOM   455  C  CA   . VAL A 1 49  ? -23.664 4.414   19.278  1.00 13.91 ? 49  VAL A CA   1 
ATOM   456  C  C    . VAL A 1 49  ? -24.694 4.956   18.259  1.00 15.04 ? 49  VAL A C    1 
ATOM   457  O  O    . VAL A 1 49  ? -25.717 4.382   18.040  1.00 19.67 ? 49  VAL A O    1 
ATOM   458  C  CB   . VAL A 1 49  ? -23.358 2.915   18.904  1.00 15.62 ? 49  VAL A CB   1 
ATOM   459  C  CG1  . VAL A 1 49  ? -22.635 2.784   17.580  1.00 19.43 ? 49  VAL A CG1  1 
ATOM   460  C  CG2  . VAL A 1 49  ? -22.578 2.218   20.015  1.00 17.45 ? 49  VAL A CG2  1 
ATOM   461  N  N    . SER A 1 50  ? -24.351 6.068   17.664  1.00 14.44 ? 50  SER A N    1 
ATOM   462  C  CA   . SER A 1 50  ? -25.302 6.724   16.775  1.00 17.13 ? 50  SER A CA   1 
ATOM   463  C  C    . SER A 1 50  ? -24.658 6.874   15.402  1.00 15.25 ? 50  SER A C    1 
ATOM   464  O  O    . SER A 1 50  ? -24.001 7.849   15.121  1.00 16.31 ? 50  SER A O    1 
ATOM   465  C  CB   . SER A 1 50  ? -25.732 8.095   17.359  1.00 19.11 ? 50  SER A CB   1 
ATOM   466  O  OG   . SER A 1 50  ? -26.359 7.958   18.656  1.00 23.51 ? 50  SER A OG   1 
ATOM   467  N  N    . TYR A 1 51  ? -24.889 5.872   14.535  1.00 14.71 ? 51  TYR A N    1 
ATOM   468  C  CA   . TYR A 1 51  ? -24.295 5.819   13.244  1.00 14.61 ? 51  TYR A CA   1 
ATOM   469  C  C    . TYR A 1 51  ? -25.282 6.066   12.085  1.00 15.90 ? 51  TYR A C    1 
ATOM   470  O  O    . TYR A 1 51  ? -24.864 5.920   10.951  1.00 17.10 ? 51  TYR A O    1 
ATOM   471  C  CB   . TYR A 1 51  ? -23.628 4.402   13.068  1.00 13.36 ? 51  TYR A CB   1 
ATOM   472  C  CG   . TYR A 1 51  ? -22.358 4.119   13.874  1.00 11.01 ? 51  TYR A CG   1 
ATOM   473  C  CD1  . TYR A 1 51  ? -21.619 5.122   14.496  1.00 12.72 ? 51  TYR A CD1  1 
ATOM   474  C  CD2  . TYR A 1 51  ? -21.863 2.858   13.955  1.00 11.02 ? 51  TYR A CD2  1 
ATOM   475  C  CE1  . TYR A 1 51  ? -20.414 4.836   15.195  1.00 10.75 ? 51  TYR A CE1  1 
ATOM   476  C  CE2  . TYR A 1 51  ? -20.723 2.516   14.635  1.00 10.40 ? 51  TYR A CE2  1 
ATOM   477  C  CZ   . TYR A 1 51  ? -19.971 3.546   15.281  1.00 9.94  ? 51  TYR A CZ   1 
ATOM   478  O  OH   . TYR A 1 51  ? -18.806 3.168   15.911  1.00 10.31 ? 51  TYR A OH   1 
ATOM   479  N  N    A ASP A 1 52  ? -26.467 6.621   12.474  0.50 16.54 ? 52  ASP A N    1 
ATOM   480  N  N    B ASP A 1 52  ? -26.540 6.280   12.304  0.50 16.03 ? 52  ASP A N    1 
ATOM   481  C  CA   A ASP A 1 52  ? -27.601 6.910   11.532  0.50 17.73 ? 52  ASP A CA   1 
ATOM   482  C  CA   B ASP A 1 52  ? -27.407 6.522   11.127  0.50 18.42 ? 52  ASP A CA   1 
ATOM   483  C  C    A ASP A 1 52  ? -27.232 7.794   10.364  0.50 17.36 ? 52  ASP A C    1 
ATOM   484  C  C    B ASP A 1 52  ? -26.889 7.567   10.096  0.50 19.84 ? 52  ASP A C    1 
ATOM   485  O  O    A ASP A 1 52  ? -27.724 7.625   9.227   0.50 15.70 ? 52  ASP A O    1 
ATOM   486  O  O    B ASP A 1 52  ? -27.014 7.347   8.814   0.50 20.31 ? 52  ASP A O    1 
ATOM   487  C  CB   A ASP A 1 52  ? -28.871 7.412   12.269  0.50 18.35 ? 52  ASP A CB   1 
ATOM   488  C  CB   B ASP A 1 52  ? -28.759 6.866   11.658  0.50 19.93 ? 52  ASP A CB   1 
ATOM   489  C  CG   A ASP A 1 52  ? -28.598 8.469   13.288  0.50 22.94 ? 52  ASP A CG   1 
ATOM   490  C  CG   B ASP A 1 52  ? -29.657 7.332   10.640  0.50 24.31 ? 52  ASP A CG   1 
ATOM   491  O  OD1  A ASP A 1 52  ? -27.964 8.231   14.361  0.50 26.82 ? 52  ASP A OD1  1 
ATOM   492  O  OD1  B ASP A 1 52  ? -29.856 6.550   9.692   0.50 27.39 ? 52  ASP A OD1  1 
ATOM   493  O  OD2  A ASP A 1 52  ? -29.048 9.591   13.011  0.50 30.64 ? 52  ASP A OD2  1 
ATOM   494  O  OD2  B ASP A 1 52  ? -30.112 8.501   10.762  0.50 33.53 ? 52  ASP A OD2  1 
ATOM   495  N  N    . GLN A 1 53  ? -26.262 8.663   10.590  1.00 19.54 ? 53  GLN A N    1 
ATOM   496  C  CA   . GLN A 1 53  ? -25.821 9.647   9.531   1.00 19.48 ? 53  GLN A CA   1 
ATOM   497  C  C    . GLN A 1 53  ? -24.373 9.388   8.996   1.00 17.84 ? 53  GLN A C    1 
ATOM   498  O  O    . GLN A 1 53  ? -23.766 10.266  8.389   1.00 18.00 ? 53  GLN A O    1 
ATOM   499  C  CB   . GLN A 1 53  ? -26.025 11.093  10.004  1.00 22.26 ? 53  GLN A CB   1 
ATOM   500  C  CG   . GLN A 1 53  ? -27.486 11.428  10.260  1.00 30.46 ? 53  GLN A CG   1 
ATOM   501  C  CD   . GLN A 1 53  ? -28.233 11.323  9.004   1.00 35.06 ? 53  GLN A CD   1 
ATOM   502  O  OE1  . GLN A 1 53  ? -27.762 11.870  7.971   1.00 37.89 ? 53  GLN A OE1  1 
ATOM   503  N  NE2  . GLN A 1 53  ? -29.384 10.602  9.006   1.00 36.56 ? 53  GLN A NE2  1 
ATOM   504  N  N    . ALA A 1 54  ? -23.768 8.281   9.334   1.00 16.94 ? 54  ALA A N    1 
ATOM   505  C  CA   . ALA A 1 54  ? -22.395 8.038   8.895   1.00 15.29 ? 54  ALA A CA   1 
ATOM   506  C  C    . ALA A 1 54  ? -22.201 8.131   7.415   1.00 15.52 ? 54  ALA A C    1 
ATOM   507  O  O    . ALA A 1 54  ? -23.033 7.579   6.650   1.00 21.32 ? 54  ALA A O    1 
ATOM   508  C  CB   . ALA A 1 54  ? -21.836 6.644   9.465   1.00 16.85 ? 54  ALA A CB   1 
ATOM   509  N  N    A THR A 1 55  ? -21.205 8.886   6.997   0.50 12.21 ? 55  THR A N    1 
ATOM   510  N  N    B THR A 1 55  ? -21.060 8.676   6.937   0.50 13.07 ? 55  THR A N    1 
ATOM   511  C  CA   A THR A 1 55  ? -20.870 9.073   5.616   0.50 11.97 ? 55  THR A CA   1 
ATOM   512  C  CA   B THR A 1 55  ? -20.663 8.730   5.498   0.50 12.42 ? 55  THR A CA   1 
ATOM   513  C  C    A THR A 1 55  ? -19.652 8.376   5.404   0.50 9.76  ? 55  THR A C    1 
ATOM   514  C  C    B THR A 1 55  ? -19.101 8.375   5.195   0.50 9.61  ? 55  THR A C    1 
ATOM   515  O  O    A THR A 1 55  ? -18.612 8.965   5.610   0.50 10.44 ? 55  THR A O    1 
ATOM   516  O  O    B THR A 1 55  ? -18.145 9.072   5.590   0.50 10.94 ? 55  THR A O    1 
ATOM   517  C  CB   A THR A 1 55  ? -20.589 10.638  5.257   0.50 14.67 ? 55  THR A CB   1 
ATOM   518  C  CB   B THR A 1 55  ? -21.117 10.119  4.972   0.50 14.46 ? 55  THR A CB   1 
ATOM   519  O  OG1  A THR A 1 55  ? -21.838 11.264  5.326   0.50 15.45 ? 55  THR A OG1  1 
ATOM   520  O  OG1  B THR A 1 55  ? -22.459 10.430  5.426   0.50 23.71 ? 55  THR A OG1  1 
ATOM   521  C  CG2  A THR A 1 55  ? -20.023 10.713  3.719   0.50 12.73 ? 55  THR A CG2  1 
ATOM   522  C  CG2  B THR A 1 55  ? -20.924 10.098  3.473   0.50 10.58 ? 55  THR A CG2  1 
ATOM   523  N  N    A SER A 1 56  ? -19.712 7.141   4.908   0.50 7.84  ? 56  SER A N    1 
ATOM   524  N  N    B SER A 1 56  ? -18.895 7.198   4.582   0.50 8.79  ? 56  SER A N    1 
ATOM   525  C  CA   A SER A 1 56  ? -18.452 6.544   4.468   0.50 7.70  ? 56  SER A CA   1 
ATOM   526  C  CA   B SER A 1 56  ? -17.575 6.681   4.244   0.50 7.98  ? 56  SER A CA   1 
ATOM   527  C  C    A SER A 1 56  ? -17.984 7.191   3.155   0.50 6.64  ? 56  SER A C    1 
ATOM   528  C  C    B SER A 1 56  ? -17.002 7.404   3.002   0.50 8.47  ? 56  SER A C    1 
ATOM   529  O  O    A SER A 1 56  ? -18.815 7.680   2.378   0.50 7.38  ? 56  SER A O    1 
ATOM   530  O  O    B SER A 1 56  ? -17.737 7.873   2.111   0.50 9.09  ? 56  SER A O    1 
ATOM   531  C  CB   A SER A 1 56  ? -18.598 5.031   4.350   0.50 7.25  ? 56  SER A CB   1 
ATOM   532  C  CB   B SER A 1 56  ? -17.609 5.169   4.080   0.50 8.25  ? 56  SER A CB   1 
ATOM   533  O  OG   A SER A 1 56  ? -19.384 4.680   3.198   0.50 7.17  ? 56  SER A OG   1 
ATOM   534  O  OG   B SER A 1 56  ? -18.432 4.784   2.973   0.50 8.59  ? 56  SER A OG   1 
ATOM   535  N  N    A LEU A 1 57  ? -16.670 7.228   2.948   0.50 6.61  ? 57  LEU A N    1 
ATOM   536  N  N    B LEU A 1 57  ? -15.663 7.468   2.913   0.50 8.82  ? 57  LEU A N    1 
ATOM   537  C  CA   A LEU A 1 57  ? -16.113 7.874   1.753   0.50 6.55  ? 57  LEU A CA   1 
ATOM   538  C  CA   B LEU A 1 57  ? -14.994 8.106   1.767   0.50 8.72  ? 57  LEU A CA   1 
ATOM   539  C  C    A LEU A 1 57  ? -15.285 6.917   0.874   0.50 6.36  ? 57  LEU A C    1 
ATOM   540  C  C    B LEU A 1 57  ? -14.216 7.110   0.902   0.50 9.12  ? 57  LEU A C    1 
ATOM   541  O  O    A LEU A 1 57  ? -15.380 6.972   -0.354  0.50 7.31  ? 57  LEU A O    1 
ATOM   542  O  O    B LEU A 1 57  ? -14.399 7.091   -0.331  0.50 9.22  ? 57  LEU A O    1 
ATOM   543  C  CB   A LEU A 1 57  ? -15.309 9.075   2.161   0.50 8.68  ? 57  LEU A CB   1 
ATOM   544  C  CB   B LEU A 1 57  ? -14.092 9.269   2.242   0.50 8.83  ? 57  LEU A CB   1 
ATOM   545  C  CG   A LEU A 1 57  ? -16.091 10.306  2.745   0.50 11.45 ? 57  LEU A CG   1 
ATOM   546  C  CG   B LEU A 1 57  ? -14.770 10.559  2.671   0.50 11.79 ? 57  LEU A CG   1 
ATOM   547  C  CD1  A LEU A 1 57  ? -15.133 11.415  3.214   0.50 12.87 ? 57  LEU A CD1  1 
ATOM   548  C  CD1  B LEU A 1 57  ? -13.751 11.439  3.356   0.50 12.29 ? 57  LEU A CD1  1 
ATOM   549  C  CD2  A LEU A 1 57  ? -17.295 10.850  1.843   0.50 16.07 ? 57  LEU A CD2  1 
ATOM   550  C  CD2  B LEU A 1 57  ? -15.327 11.266  1.426   0.50 15.86 ? 57  LEU A CD2  1 
ATOM   551  N  N    A ARG A 1 58  ? -14.389 6.137   1.521   0.50 6.55  ? 58  ARG A N    1 
ATOM   552  N  N    B ARG A 1 58  ? -13.269 6.426   1.513   0.50 9.11  ? 58  ARG A N    1 
ATOM   553  C  CA   A ARG A 1 58  ? -13.315 5.495   0.774   0.50 6.08  ? 58  ARG A CA   1 
ATOM   554  C  CA   B ARG A 1 58  ? -12.267 5.659   0.805   0.50 8.49  ? 58  ARG A CA   1 
ATOM   555  C  C    A ARG A 1 58  ? -12.809 4.359   1.616   0.50 5.30  ? 58  ARG A C    1 
ATOM   556  C  C    B ARG A 1 58  ? -11.790 4.468   1.601   0.50 7.09  ? 58  ARG A C    1 
ATOM   557  O  O    A ARG A 1 58  ? -12.952 4.338   2.820   0.50 6.58  ? 58  ARG A O    1 
ATOM   558  O  O    B ARG A 1 58  ? -12.011 4.449   2.817   0.50 8.35  ? 58  ARG A O    1 
ATOM   559  C  CB   A ARG A 1 58  ? -12.139 6.538   0.567   0.50 7.31  ? 58  ARG A CB   1 
ATOM   560  C  CB   B ARG A 1 58  ? -11.043 6.550   0.485   0.50 8.80  ? 58  ARG A CB   1 
ATOM   561  C  CG   A ARG A 1 58  ? -11.067 6.134   -0.405  0.50 7.94  ? 58  ARG A CG   1 
ATOM   562  C  CG   B ARG A 1 58  ? -11.269 7.739   -0.521  0.50 11.85 ? 58  ARG A CG   1 
ATOM   563  C  CD   A ARG A 1 58  ? -9.951  7.196   -0.548  0.50 9.88  ? 58  ARG A CD   1 
ATOM   564  C  CD   B ARG A 1 58  ? -10.000 8.418   -1.058  0.50 12.30 ? 58  ARG A CD   1 
ATOM   565  N  NE   A ARG A 1 58  ? -9.049  7.166   0.598   0.50 8.39  ? 58  ARG A NE   1 
ATOM   566  N  NE   B ARG A 1 58  ? -9.160  7.517   -1.864  0.50 13.92 ? 58  ARG A NE   1 
ATOM   567  C  CZ   A ARG A 1 58  ? -7.733  7.334   0.576   0.50 8.42  ? 58  ARG A CZ   1 
ATOM   568  C  CZ   B ARG A 1 58  ? -9.395  7.228   -3.145  0.50 11.44 ? 58  ARG A CZ   1 
ATOM   569  N  NH1  A ARG A 1 58  ? -7.074  7.584   -0.540  0.50 9.73  ? 58  ARG A NH1  1 
ATOM   570  N  NH1  B ARG A 1 58  ? -10.443 7.766   -3.744  0.50 14.15 ? 58  ARG A NH1  1 
ATOM   571  N  NH2  A ARG A 1 58  ? -7.071  7.270   1.715   0.50 7.34  ? 58  ARG A NH2  1 
ATOM   572  N  NH2  B ARG A 1 58  ? -8.601  6.404   -3.825  0.50 14.31 ? 58  ARG A NH2  1 
ATOM   573  N  N    A ILE A 1 59  ? -12.216 3.395   0.928   0.50 5.43  ? 59  ILE A N    1 
ATOM   574  N  N    B ILE A 1 59  ? -11.207 3.515   0.909   0.50 7.72  ? 59  ILE A N    1 
ATOM   575  C  CA   A ILE A 1 59  ? -11.541 2.286   1.595   0.50 5.81  ? 59  ILE A CA   1 
ATOM   576  C  CA   B ILE A 1 59  ? -10.585 2.327   1.530   0.50 6.60  ? 59  ILE A CA   1 
ATOM   577  C  C    A ILE A 1 59  ? -10.079 2.285   1.046   0.50 5.58  ? 59  ILE A C    1 
ATOM   578  C  C    B ILE A 1 59  ? -9.131  2.262   1.027   0.50 8.16  ? 59  ILE A C    1 
ATOM   579  O  O    A ILE A 1 59  ? -9.831  2.398   -0.146  0.50 7.76  ? 59  ILE A O    1 
ATOM   580  O  O    B ILE A 1 59  ? -8.864  2.432   -0.163  0.50 8.54  ? 59  ILE A O    1 
ATOM   581  C  CB   A ILE A 1 59  ? -12.302 0.949   1.310   0.50 6.47  ? 59  ILE A CB   1 
ATOM   582  C  CB   B ILE A 1 59  ? -11.344 1.059   1.264   0.50 8.09  ? 59  ILE A CB   1 
ATOM   583  C  CG1  A ILE A 1 59  ? -11.725 -0.172  2.207   0.50 6.81  ? 59  ILE A CG1  1 
ATOM   584  C  CG1  B ILE A 1 59  ? -10.840 -0.107  2.165   0.50 8.08  ? 59  ILE A CG1  1 
ATOM   585  C  CG2  A ILE A 1 59  ? -12.253 0.510   -0.182  0.50 6.25  ? 59  ILE A CG2  1 
ATOM   586  C  CG2  B ILE A 1 59  ? -11.351 0.642   -0.275  0.50 8.64  ? 59  ILE A CG2  1 
ATOM   587  C  CD1  A ILE A 1 59  ? -12.593 -1.430  2.162   0.50 6.35  ? 59  ILE A CD1  1 
ATOM   588  C  CD1  B ILE A 1 59  ? -11.709 -1.398  1.987   0.50 10.08 ? 59  ILE A CD1  1 
ATOM   589  N  N    A LEU A 1 60  ? -9.121  2.101   1.961   0.50 5.87  ? 60  LEU A N    1 
ATOM   590  N  N    B LEU A 1 60  ? -8.195  2.031   1.952   0.50 6.86  ? 60  LEU A N    1 
ATOM   591  C  CA   A LEU A 1 60  ? -7.670  2.240   1.709   0.50 4.93  ? 60  LEU A CA   1 
ATOM   592  C  CA   B LEU A 1 60  ? -6.761  2.054   1.643   0.50 8.28  ? 60  LEU A CA   1 
ATOM   593  C  C    A LEU A 1 60  ? -6.950  1.041   2.242   0.50 5.10  ? 60  LEU A C    1 
ATOM   594  C  C    B LEU A 1 60  ? -6.050  0.846   2.233   0.50 6.61  ? 60  LEU A C    1 
ATOM   595  O  O    A LEU A 1 60  ? -7.101  0.723   3.441   0.50 4.61  ? 60  LEU A O    1 
ATOM   596  O  O    B LEU A 1 60  ? -6.290  0.488   3.411   0.50 7.80  ? 60  LEU A O    1 
ATOM   597  C  CB   A LEU A 1 60  ? -7.127  3.485   2.431   0.50 5.28  ? 60  LEU A CB   1 
ATOM   598  C  CB   B LEU A 1 60  ? -6.099  3.342   2.264   0.50 10.08 ? 60  LEU A CB   1 
ATOM   599  C  CG   A LEU A 1 60  ? -5.566  3.637   2.415   0.50 5.77  ? 60  LEU A CG   1 
ATOM   600  C  CG   B LEU A 1 60  ? -4.569  3.393   2.280   0.50 10.42 ? 60  LEU A CG   1 
ATOM   601  C  CD1  A LEU A 1 60  ? -5.039  3.901   0.942   0.50 6.75  ? 60  LEU A CD1  1 
ATOM   602  C  CD1  B LEU A 1 60  ? -3.903  3.600   0.966   0.50 12.55 ? 60  LEU A CD1  1 
ATOM   603  C  CD2  A LEU A 1 60  ? -5.128  4.704   3.396   0.50 6.37  ? 60  LEU A CD2  1 
ATOM   604  C  CD2  B LEU A 1 60  ? -4.110  4.576   3.282   0.50 11.69 ? 60  LEU A CD2  1 
ATOM   605  N  N    A ASN A 1 61  ? -6.109  0.406   1.431   0.50 4.47  ? 61  ASN A N    1 
ATOM   606  N  N    B ASN A 1 61  ? -5.209  0.185   1.471   0.50 7.62  ? 61  ASN A N    1 
ATOM   607  C  CA   A ASN A 1 61  ? -5.111  -0.553  1.907   0.50 6.13  ? 61  ASN A CA   1 
ATOM   608  C  CA   B ASN A 1 61  ? -4.254  -0.794  1.984   0.50 6.77  ? 61  ASN A CA   1 
ATOM   609  C  C    A ASN A 1 61  ? -3.874  0.292   2.238   0.50 5.37  ? 61  ASN A C    1 
ATOM   610  C  C    B ASN A 1 61  ? -3.004  0.009   2.341   0.50 7.96  ? 61  ASN A C    1 
ATOM   611  O  O    A ASN A 1 61  ? -3.199  0.835   1.334   0.50 6.12  ? 61  ASN A O    1 
ATOM   612  O  O    B ASN A 1 61  ? -2.281  0.516   1.460   0.50 7.80  ? 61  ASN A O    1 
ATOM   613  C  CB   A ASN A 1 61  ? -4.799  -1.553  0.784   0.50 6.11  ? 61  ASN A CB   1 
ATOM   614  C  CB   B ASN A 1 61  ? -3.944  -1.821  0.883   0.50 7.03  ? 61  ASN A CB   1 
ATOM   615  C  CG   A ASN A 1 61  ? -3.751  -2.594  1.203   0.50 5.54  ? 61  ASN A CG   1 
ATOM   616  C  CG   B ASN A 1 61  ? -2.884  -2.878  1.321   0.50 7.84  ? 61  ASN A CG   1 
ATOM   617  O  OD1  A ASN A 1 61  ? -2.890  -2.288  2.050   0.50 5.98  ? 61  ASN A OD1  1 
ATOM   618  O  OD1  B ASN A 1 61  ? -2.047  -2.609  2.184   0.50 8.78  ? 61  ASN A OD1  1 
ATOM   619  N  ND2  A ASN A 1 61  ? -3.780  -3.761  0.561   0.50 5.84  ? 61  ASN A ND2  1 
ATOM   620  N  ND2  B ASN A 1 61  ? -2.916  -4.077  0.718   0.50 8.44  ? 61  ASN A ND2  1 
ATOM   621  N  N    A ASN A 1 62  ? -3.582  0.414   3.531   0.50 5.30  ? 62  ASN A N    1 
ATOM   622  N  N    B ASN A 1 62  ? -2.702  0.120   3.623   0.50 7.41  ? 62  ASN A N    1 
ATOM   623  C  CA   A ASN A 1 62  ? -2.458  1.232   4.016   0.50 6.31  ? 62  ASN A CA   1 
ATOM   624  C  CA   B ASN A 1 62  ? -1.575  0.890   4.063   0.50 8.11  ? 62  ASN A CA   1 
ATOM   625  C  C    A ASN A 1 62  ? -1.187  0.416   4.230   0.50 7.02  ? 62  ASN A C    1 
ATOM   626  C  C    B ASN A 1 62  ? -0.314  0.026   4.357   0.50 8.86  ? 62  ASN A C    1 
ATOM   627  O  O    A ASN A 1 62  ? -0.179  0.947   4.751   0.50 9.28  ? 62  ASN A O    1 
ATOM   628  O  O    B ASN A 1 62  ? 0.698   0.456   4.963   0.50 9.52  ? 62  ASN A O    1 
ATOM   629  C  CB   A ASN A 1 62  ? -2.827  2.001   5.249   0.50 8.08  ? 62  ASN A CB   1 
ATOM   630  C  CB   B ASN A 1 62  ? -1.924  1.733   5.285   0.50 9.38  ? 62  ASN A CB   1 
ATOM   631  C  CG   A ASN A 1 62  ? -3.095  1.095   6.435   0.50 7.12  ? 62  ASN A CG   1 
ATOM   632  C  CG   B ASN A 1 62  ? -2.220  0.885   6.518   0.50 7.58  ? 62  ASN A CG   1 
ATOM   633  O  OD1  A ASN A 1 62  ? -2.838  -0.100  6.416   0.50 7.62  ? 62  ASN A OD1  1 
ATOM   634  O  OD1  B ASN A 1 62  ? -2.083  -0.321  6.481   0.50 7.89  ? 62  ASN A OD1  1 
ATOM   635  N  ND2  A ASN A 1 62  ? -3.693  1.639   7.430   0.50 12.24 ? 62  ASN A ND2  1 
ATOM   636  N  ND2  B ASN A 1 62  ? -2.564  1.549   7.675   0.50 10.45 ? 62  ASN A ND2  1 
ATOM   637  N  N    A GLY A 1 63  ? -1.172  -0.851  3.789   0.50 6.78  ? 63  GLY A N    1 
ATOM   638  N  N    B GLY A 1 63  ? -0.379  -1.207  3.934   0.50 8.50  ? 63  GLY A N    1 
ATOM   639  C  CA   A GLY A 1 63  ? -0.048  -1.730  3.940   0.50 7.11  ? 63  GLY A CA   1 
ATOM   640  C  CA   B GLY A 1 63  ? 0.668   -2.141  4.154   0.50 9.68  ? 63  GLY A CA   1 
ATOM   641  C  C    A GLY A 1 63  ? 0.118   -2.501  5.232   0.50 9.37  ? 63  GLY A C    1 
ATOM   642  C  C    B GLY A 1 63  ? 0.447   -2.754  5.512   0.50 11.58 ? 63  GLY A C    1 
ATOM   643  O  O    A GLY A 1 63  ? 1.038   -3.235  5.384   0.50 8.76  ? 63  GLY A O    1 
ATOM   644  O  O    B GLY A 1 63  ? 1.339   -3.674  5.855   0.50 10.98 ? 63  GLY A O    1 
ATOM   645  N  N    . HIS A 1 64  ? -0.653  -2.301  6.233   1.00 11.48 ? 64  HIS A N    1 
ATOM   646  C  CA   . HIS A 1 64  ? -0.777  -2.943  7.569   1.00 10.80 ? 64  HIS A CA   1 
ATOM   647  C  C    . HIS A 1 64  ? -2.147  -3.577  7.754   1.00 10.79 ? 64  HIS A C    1 
ATOM   648  O  O    . HIS A 1 64  ? -2.238  -4.624  8.422   1.00 17.24 ? 64  HIS A O    1 
ATOM   649  C  CB   . HIS A 1 64  ? -0.527  -1.917  8.719   1.00 11.94 ? 64  HIS A CB   1 
ATOM   650  C  CG   . HIS A 1 64  ? 0.763   -1.124  8.591   1.00 13.51 ? 64  HIS A CG   1 
ATOM   651  N  ND1  . HIS A 1 64  ? 1.997   -1.742  8.660   1.00 16.00 ? 64  HIS A ND1  1 
ATOM   652  C  CD2  . HIS A 1 64  ? 0.999   0.192   8.370   1.00 16.15 ? 64  HIS A CD2  1 
ATOM   653  C  CE1  . HIS A 1 64  ? 2.951   -0.826  8.570   1.00 18.22 ? 64  HIS A CE1  1 
ATOM   654  N  NE2  . HIS A 1 64  ? 2.374   0.351   8.332   1.00 18.46 ? 64  HIS A NE2  1 
ATOM   655  N  N    . ALA A 1 65  ? -3.176  -2.952  7.253   1.00 10.14 ? 65  ALA A N    1 
ATOM   656  C  CA   . ALA A 1 65  ? -4.542  -3.405  7.242   1.00 10.07 ? 65  ALA A CA   1 
ATOM   657  C  C    . ALA A 1 65  ? -5.279  -2.633  6.138   1.00 10.08 ? 65  ALA A C    1 
ATOM   658  O  O    . ALA A 1 65  ? -4.588  -2.045  5.273   1.00 11.89 ? 65  ALA A O    1 
ATOM   659  C  CB   . ALA A 1 65  ? -5.227  -3.184  8.647   1.00 11.29 ? 65  ALA A CB   1 
ATOM   660  N  N    . PHE A 1 66  ? -6.594  -2.646  6.111   1.00 9.56  ? 66  PHE A N    1 
ATOM   661  C  CA   . PHE A 1 66  ? -7.387  -1.719  5.270   1.00 10.16 ? 66  PHE A CA   1 
ATOM   662  C  C    . PHE A 1 66  ? -8.218  -0.845  6.185   1.00 9.74  ? 66  PHE A C    1 
ATOM   663  O  O    . PHE A 1 66  ? -8.874  -1.301  7.113   1.00 10.15 ? 66  PHE A O    1 
ATOM   664  C  CB   . PHE A 1 66  ? -8.176  -2.421  4.179   1.00 10.27 ? 66  PHE A CB   1 
ATOM   665  C  CG   . PHE A 1 66  ? -9.204  -3.351  4.676   1.00 10.62 ? 66  PHE A CG   1 
ATOM   666  C  CD1  . PHE A 1 66  ? -10.463 -2.905  5.030   1.00 10.90 ? 66  PHE A CD1  1 
ATOM   667  C  CD2  . PHE A 1 66  ? -8.941  -4.711  4.829   1.00 9.86  ? 66  PHE A CD2  1 
ATOM   668  C  CE1  . PHE A 1 66  ? -11.399 -3.762  5.521   1.00 12.00 ? 66  PHE A CE1  1 
ATOM   669  C  CE2  . PHE A 1 66  ? -9.968  -5.576  5.316   1.00 10.49 ? 66  PHE A CE2  1 
ATOM   670  C  CZ   . PHE A 1 66  ? -11.173 -5.123  5.689   1.00 11.39 ? 66  PHE A CZ   1 
ATOM   671  N  N    . ASN A 1 67  ? -8.263  0.466   5.870   1.00 10.84 ? 67  ASN A N    1 
ATOM   672  C  CA   . ASN A 1 67  ? -9.116  1.412   6.600   1.00 10.92 ? 67  ASN A CA   1 
ATOM   673  C  C    . ASN A 1 67  ? -10.374 1.810   5.819   1.00 10.24 ? 67  ASN A C    1 
ATOM   674  O  O    . ASN A 1 67  ? -10.255 2.259   4.619   1.00 12.20 ? 67  ASN A O    1 
ATOM   675  C  CB   . ASN A 1 67  ? -8.401  2.683   6.995   1.00 12.45 ? 67  ASN A CB   1 
ATOM   676  C  CG   . ASN A 1 67  ? -7.317  2.487   7.982   1.00 14.82 ? 67  ASN A CG   1 
ATOM   677  O  OD1  . ASN A 1 67  ? -7.215  1.471   8.702   1.00 13.52 ? 67  ASN A OD1  1 
ATOM   678  N  ND2  . ASN A 1 67  ? -6.431  3.483   8.026   1.00 17.44 ? 67  ASN A ND2  1 
ATOM   679  N  N    A VAL A 1 68  ? -11.619 1.547   6.290   0.50 9.37  ? 68  VAL A N    1 
ATOM   680  N  N    B VAL A 1 68  ? -11.490 1.773   6.363   0.50 9.68  ? 68  VAL A N    1 
ATOM   681  C  CA   A VAL A 1 68  ? -12.953 2.168   5.867   0.50 8.13  ? 68  VAL A CA   1 
ATOM   682  C  CA   B VAL A 1 68  ? -12.476 2.458   5.656   0.50 9.98  ? 68  VAL A CA   1 
ATOM   683  C  C    A VAL A 1 68  ? -12.993 3.613   6.474   0.50 9.04  ? 68  VAL A C    1 
ATOM   684  C  C    B VAL A 1 68  ? -12.625 3.771   6.406   0.50 9.27  ? 68  VAL A C    1 
ATOM   685  O  O    A VAL A 1 68  ? -12.723 3.779   7.704   0.50 10.31 ? 68  VAL A O    1 
ATOM   686  O  O    B VAL A 1 68  ? -13.282 3.754   7.616   0.50 8.64  ? 68  VAL A O    1 
ATOM   687  C  CB   A VAL A 1 68  ? -14.167 1.297   6.142   0.50 9.26  ? 68  VAL A CB   1 
ATOM   688  C  CB   B VAL A 1 68  ? -13.709 1.606   5.869   0.50 12.17 ? 68  VAL A CB   1 
ATOM   689  C  CG1  A VAL A 1 68  ? -15.494 2.056   5.630   0.50 8.55  ? 68  VAL A CG1  1 
ATOM   690  C  CG1  B VAL A 1 68  ? -14.877 2.367   5.353   0.50 12.68 ? 68  VAL A CG1  1 
ATOM   691  C  CG2  A VAL A 1 68  ? -14.011 -0.087  5.395   0.50 9.99  ? 68  VAL A CG2  1 
ATOM   692  C  CG2  B VAL A 1 68  ? -13.571 0.313   5.065   0.50 12.51 ? 68  VAL A CG2  1 
ATOM   693  N  N    A GLU A 1 69  ? -13.098 4.651   5.630   0.50 5.67  ? 69  GLU A N    1 
ATOM   694  N  N    B GLU A 1 69  ? -12.154 4.877   5.695   0.50 10.07 ? 69  GLU A N    1 
ATOM   695  C  CA   A GLU A 1 69  ? -12.948 6.039   6.104   0.50 6.32  ? 69  GLU A CA   1 
ATOM   696  C  CA   B GLU A 1 69  ? -12.060 6.208   6.270   0.50 10.62 ? 69  GLU A CA   1 
ATOM   697  C  C    A GLU A 1 69  ? -14.334 6.737   6.043   0.50 4.66  ? 69  GLU A C    1 
ATOM   698  C  C    B GLU A 1 69  ? -13.342 6.967   5.960   0.50 9.52  ? 69  GLU A C    1 
ATOM   699  O  O    A GLU A 1 69  ? -15.079 6.505   5.110   0.50 6.11  ? 69  GLU A O    1 
ATOM   700  O  O    B GLU A 1 69  ? -13.951 6.850   4.898   0.50 12.06 ? 69  GLU A O    1 
ATOM   701  C  CB   A GLU A 1 69  ? -11.910 6.772   5.221   0.50 4.91  ? 69  GLU A CB   1 
ATOM   702  C  CB   B GLU A 1 69  ? -10.937 6.962   5.564   0.50 13.54 ? 69  GLU A CB   1 
ATOM   703  C  CG   A GLU A 1 69  ? -10.545 6.155   5.195   0.50 5.07  ? 69  GLU A CG   1 
ATOM   704  C  CG   B GLU A 1 69  ? -9.697  6.226   5.423   0.50 16.96 ? 69  GLU A CG   1 
ATOM   705  C  CD   A GLU A 1 69  ? -9.661  6.680   4.112   0.50 6.54  ? 69  GLU A CD   1 
ATOM   706  C  CD   B GLU A 1 69  ? -8.847  6.834   4.375   0.50 19.45 ? 69  GLU A CD   1 
ATOM   707  O  OE1  A GLU A 1 69  ? -10.144 7.422   3.180   0.50 7.40  ? 69  GLU A OE1  1 
ATOM   708  O  OE1  B GLU A 1 69  ? -9.467  7.457   3.460   0.50 28.28 ? 69  GLU A OE1  1 
ATOM   709  O  OE2  A GLU A 1 69  ? -8.441  6.400   4.084   0.50 7.45  ? 69  GLU A OE2  1 
ATOM   710  O  OE2  B GLU A 1 69  ? -7.541  6.765   4.497   0.50 21.74 ? 69  GLU A OE2  1 
ATOM   711  N  N    A PHE A 1 70  ? -14.545 7.622   7.026   0.50 5.85  ? 70  PHE A N    1 
ATOM   712  N  N    B PHE A 1 70  ? -13.715 7.780   6.931   0.50 7.69  ? 70  PHE A N    1 
ATOM   713  C  CA   A PHE A 1 70  ? -15.768 8.393   7.165   0.50 5.04  ? 70  PHE A CA   1 
ATOM   714  C  CA   B PHE A 1 70  ? -14.991 8.502   6.910   0.50 8.12  ? 70  PHE A CA   1 
ATOM   715  C  C    A PHE A 1 70  ? -15.541 9.849   7.113   0.50 6.36  ? 70  PHE A C    1 
ATOM   716  C  C    B PHE A 1 70  ? -14.741 10.002  6.813   0.50 7.24  ? 70  PHE A C    1 
ATOM   717  O  O    A PHE A 1 70  ? -14.474 10.321  7.495   0.50 6.76  ? 70  PHE A O    1 
ATOM   718  O  O    B PHE A 1 70  ? -13.726 10.552  7.263   0.50 7.93  ? 70  PHE A O    1 
ATOM   719  C  CB   A PHE A 1 70  ? -16.501 8.054   8.465   0.50 5.83  ? 70  PHE A CB   1 
ATOM   720  C  CB   B PHE A 1 70  ? -15.801 8.191   8.188   0.50 7.07  ? 70  PHE A CB   1 
ATOM   721  C  CG   A PHE A 1 70  ? -17.081 6.653   8.435   0.50 5.12  ? 70  PHE A CG   1 
ATOM   722  C  CG   B PHE A 1 70  ? -16.355 6.782   8.198   0.50 7.48  ? 70  PHE A CG   1 
ATOM   723  C  CD1  A PHE A 1 70  ? -16.291 5.556   8.631   0.50 5.94  ? 70  PHE A CD1  1 
ATOM   724  C  CD1  B PHE A 1 70  ? -17.713 6.530   7.902   0.50 7.39  ? 70  PHE A CD1  1 
ATOM   725  C  CD2  A PHE A 1 70  ? -18.423 6.431   8.119   0.50 6.05  ? 70  PHE A CD2  1 
ATOM   726  C  CD2  B PHE A 1 70  ? -15.506 5.646   8.433   0.50 8.50  ? 70  PHE A CD2  1 
ATOM   727  C  CE1  A PHE A 1 70  ? -16.775 4.288   8.466   0.50 6.74  ? 70  PHE A CE1  1 
ATOM   728  C  CE1  B PHE A 1 70  ? -18.231 5.272   7.781   0.50 8.11  ? 70  PHE A CE1  1 
ATOM   729  C  CE2  A PHE A 1 70  ? -18.951 5.165   7.981   0.50 6.75  ? 70  PHE A CE2  1 
ATOM   730  C  CE2  B PHE A 1 70  ? -16.045 4.354   8.307   0.50 8.02  ? 70  PHE A CE2  1 
ATOM   731  C  CZ   A PHE A 1 70  ? -18.122 4.059   8.170   0.50 7.61  ? 70  PHE A CZ   1 
ATOM   732  C  CZ   B PHE A 1 70  ? -17.417 4.170   8.035   0.50 8.03  ? 70  PHE A CZ   1 
ATOM   733  N  N    A ASP A 1 71  ? -16.530 10.602  6.645   0.50 8.20  ? 71  ASP A N    1 
ATOM   734  N  N    B ASP A 1 71  ? -15.785 10.661  6.315   0.50 8.70  ? 71  ASP A N    1 
ATOM   735  C  CA   A ASP A 1 71  ? -16.464 12.085  6.711   0.50 9.89  ? 71  ASP A CA   1 
ATOM   736  C  CA   B ASP A 1 71  ? -15.905 12.111  6.440   0.50 9.91  ? 71  ASP A CA   1 
ATOM   737  C  C    A ASP A 1 71  ? -16.593 12.423  8.154   0.50 10.78 ? 71  ASP A C    1 
ATOM   738  C  C    B ASP A 1 71  ? -16.431 12.448  7.854   0.50 10.32 ? 71  ASP A C    1 
ATOM   739  O  O    A ASP A 1 71  ? -17.641 12.183  8.769   0.50 14.33 ? 71  ASP A O    1 
ATOM   740  O  O    B ASP A 1 71  ? -17.635 12.412  8.084   0.50 12.55 ? 71  ASP A O    1 
ATOM   741  C  CB   A ASP A 1 71  ? -17.592 12.698  5.928   0.50 10.42 ? 71  ASP A CB   1 
ATOM   742  C  CB   B ASP A 1 71  ? -16.851 12.652  5.342   0.50 10.47 ? 71  ASP A CB   1 
ATOM   743  C  CG   A ASP A 1 71  ? -17.773 14.233  6.162   0.50 12.61 ? 71  ASP A CG   1 
ATOM   744  C  CG   B ASP A 1 71  ? -17.005 14.164  5.350   0.50 11.75 ? 71  ASP A CG   1 
ATOM   745  O  OD1  A ASP A 1 71  ? -16.868 14.861  6.770   0.50 15.26 ? 71  ASP A OD1  1 
ATOM   746  O  OD1  B ASP A 1 71  ? -16.454 14.828  6.260   0.50 11.79 ? 71  ASP A OD1  1 
ATOM   747  O  OD2  A ASP A 1 71  ? -18.836 14.736  5.749   0.50 18.88 ? 71  ASP A OD2  1 
ATOM   748  O  OD2  B ASP A 1 71  ? -17.606 14.710  4.362   0.50 18.24 ? 71  ASP A OD2  1 
ATOM   749  N  N    . ASP A 1 72  ? -15.524 12.956  8.694   1.00 11.53 ? 72  ASP A N    1 
ATOM   750  C  CA   . ASP A 1 72  ? -15.634 13.381  10.096  1.00 10.94 ? 72  ASP A CA   1 
ATOM   751  C  C    . ASP A 1 72  ? -15.619 14.893  10.221  1.00 13.49 ? 72  ASP A C    1 
ATOM   752  O  O    . ASP A 1 72  ? -15.255 15.415  11.290  1.00 14.80 ? 72  ASP A O    1 
ATOM   753  C  CB   . ASP A 1 72  ? -14.543 12.695  10.972  1.00 11.96 ? 72  ASP A CB   1 
ATOM   754  C  CG   . ASP A 1 72  ? -13.152 13.159  10.618  1.00 11.99 ? 72  ASP A CG   1 
ATOM   755  O  OD1  . ASP A 1 72  ? -13.028 13.935  9.555   1.00 13.33 ? 72  ASP A OD1  1 
ATOM   756  O  OD2  . ASP A 1 72  ? -12.225 12.900  11.362  1.00 13.35 ? 72  ASP A OD2  1 
ATOM   757  N  N    . SER A 1 73  ? -16.039 15.625  9.197   1.00 15.05 ? 73  SER A N    1 
ATOM   758  C  CA   . SER A 1 73  ? -16.078 17.152  9.222   1.00 16.53 ? 73  SER A CA   1 
ATOM   759  C  C    . SER A 1 73  ? -17.418 17.702  9.773   1.00 16.50 ? 73  SER A C    1 
ATOM   760  O  O    . SER A 1 73  ? -17.521 18.904  9.953   1.00 16.54 ? 73  SER A O    1 
ATOM   761  C  CB   . SER A 1 73  ? -15.779 17.636  7.837   1.00 17.29 ? 73  SER A CB   1 
ATOM   762  O  OG   . SER A 1 73  ? -16.883 17.458  7.071   1.00 16.59 ? 73  SER A OG   1 
ATOM   763  N  N    . GLN A 1 74  ? -18.493 16.818  9.856   1.00 12.90 ? 74  GLN A N    1 
ATOM   764  C  CA   . GLN A 1 74  ? -19.803 17.122  10.569  1.00 14.98 ? 74  GLN A CA   1 
ATOM   765  C  C    . GLN A 1 74  ? -20.028 16.075  11.732  1.00 15.73 ? 74  GLN A C    1 
ATOM   766  O  O    . GLN A 1 74  ? -19.358 15.016  11.823  1.00 13.70 ? 74  GLN A O    1 
ATOM   767  C  CB   . GLN A 1 74  ? -21.023 17.238  9.578   1.00 13.71 ? 74  GLN A CB   1 
ATOM   768  C  CG   . GLN A 1 74  ? -20.746 18.107  8.297   1.00 15.60 ? 74  GLN A CG   1 
ATOM   769  C  CD   . GLN A 1 74  ? -21.918 18.158  7.386   1.00 18.33 ? 74  GLN A CD   1 
ATOM   770  O  OE1  . GLN A 1 74  ? -23.059 18.122  7.842   1.00 27.88 ? 74  GLN A OE1  1 
ATOM   771  N  NE2  . GLN A 1 74  ? -21.652 18.336  6.089   1.00 22.86 ? 74  GLN A NE2  1 
ATOM   772  N  N    A ASP A 1 75  ? -20.919 16.456  12.661  0.50 19.13 ? 75  ASP A N    1 
ATOM   773  N  N    B ASP A 1 75  ? -21.005 16.850  12.554  0.50 13.01 ? 75  ASP A N    1 
ATOM   774  C  CA   A ASP A 1 75  ? -21.319 15.710  13.839  0.50 19.29 ? 75  ASP A CA   1 
ATOM   775  C  CA   B ASP A 1 75  ? -21.358 16.108  13.696  0.50 11.04 ? 75  ASP A CA   1 
ATOM   776  C  C    A ASP A 1 75  ? -22.361 14.639  13.361  0.50 19.22 ? 75  ASP A C    1 
ATOM   777  C  C    B ASP A 1 75  ? -22.201 15.017  13.077  0.50 14.83 ? 75  ASP A C    1 
ATOM   778  O  O    A ASP A 1 75  ? -23.587 14.913  13.333  0.50 15.90 ? 75  ASP A O    1 
ATOM   779  O  O    B ASP A 1 75  ? -23.243 15.303  12.575  0.50 18.51 ? 75  ASP A O    1 
ATOM   780  C  CB   A ASP A 1 75  ? -21.955 16.777  14.772  0.50 21.85 ? 75  ASP A CB   1 
ATOM   781  C  CB   B ASP A 1 75  ? -22.181 17.082  14.635  0.50 11.45 ? 75  ASP A CB   1 
ATOM   782  C  CG   A ASP A 1 75  ? -22.144 16.339  16.178  0.50 26.16 ? 75  ASP A CG   1 
ATOM   783  C  CG   B ASP A 1 75  ? -22.883 16.389  15.802  0.50 13.18 ? 75  ASP A CG   1 
ATOM   784  O  OD1  A ASP A 1 75  ? -22.109 15.148  16.474  0.50 30.51 ? 75  ASP A OD1  1 
ATOM   785  O  OD1  B ASP A 1 75  ? -22.513 15.250  16.118  0.50 14.53 ? 75  ASP A OD1  1 
ATOM   786  O  OD2  A ASP A 1 75  ? -22.376 17.224  17.038  0.50 32.93 ? 75  ASP A OD2  1 
ATOM   787  O  OD2  B ASP A 1 75  ? -23.757 17.051  16.423  0.50 17.59 ? 75  ASP A OD2  1 
ATOM   788  N  N    A LYS A 1 76  ? -21.813 13.585  12.744  0.50 18.10 ? 76  LYS A N    1 
ATOM   789  N  N    B LYS A 1 76  ? -21.677 13.792  13.048  0.50 12.48 ? 76  LYS A N    1 
ATOM   790  C  CA   A LYS A 1 76  ? -22.572 12.575  12.001  0.50 18.39 ? 76  LYS A CA   1 
ATOM   791  C  CA   B LYS A 1 76  ? -22.292 12.570  12.571  0.50 12.16 ? 76  LYS A CA   1 
ATOM   792  C  C    A LYS A 1 76  ? -22.570 11.359  12.905  0.50 19.14 ? 76  LYS A C    1 
ATOM   793  C  C    B LYS A 1 76  ? -21.461 11.363  13.092  0.50 10.58 ? 76  LYS A C    1 
ATOM   794  O  O    A LYS A 1 76  ? -23.429 11.248  13.827  0.50 22.88 ? 76  LYS A O    1 
ATOM   795  O  O    B LYS A 1 76  ? -20.211 11.498  13.258  0.50 11.32 ? 76  LYS A O    1 
ATOM   796  C  CB   A LYS A 1 76  ? -21.916 12.294  10.622  0.50 18.59 ? 76  LYS A CB   1 
ATOM   797  C  CB   B LYS A 1 76  ? -22.307 12.503  11.033  0.50 11.96 ? 76  LYS A CB   1 
ATOM   798  C  CG   A LYS A 1 76  ? -22.148 13.483  9.686   0.50 18.47 ? 76  LYS A CG   1 
ATOM   799  C  CG   B LYS A 1 76  ? -23.115 13.592  10.301  0.50 16.45 ? 76  LYS A CG   1 
ATOM   800  C  CD   A LYS A 1 76  ? -21.624 13.236  8.281   0.50 18.28 ? 76  LYS A CD   1 
ATOM   801  C  CD   B LYS A 1 76  ? -23.117 13.443  8.783   0.50 15.71 ? 76  LYS A CD   1 
ATOM   802  C  CE   A LYS A 1 76  ? -22.005 14.330  7.316   0.50 18.65 ? 76  LYS A CE   1 
ATOM   803  C  CE   B LYS A 1 76  ? -23.887 14.520  8.084   0.50 18.64 ? 76  LYS A CE   1 
ATOM   804  N  NZ   A LYS A 1 76  ? -21.590 14.055  5.905   0.50 18.69 ? 76  LYS A NZ   1 
ATOM   805  N  NZ   B LYS A 1 76  ? -23.717 14.432  6.583   0.50 20.79 ? 76  LYS A NZ   1 
ATOM   806  N  N    A ALA A 1 77  ? -21.524 10.566  12.757  0.50 16.66 ? 77  ALA A N    1 
ATOM   807  N  N    B ALA A 1 77  ? -22.096 10.232  13.331  0.50 11.08 ? 77  ALA A N    1 
ATOM   808  C  CA   A ALA A 1 77  ? -21.454 9.298   13.496  0.50 15.13 ? 77  ALA A CA   1 
ATOM   809  C  CA   B ALA A 1 77  ? -21.405 8.987   13.617  0.50 11.78 ? 77  ALA A CA   1 
ATOM   810  C  C    A ALA A 1 77  ? -20.698 9.464   14.841  0.50 13.08 ? 77  ALA A C    1 
ATOM   811  C  C    B ALA A 1 77  ? -20.651 9.128   14.963  0.50 11.32 ? 77  ALA A C    1 
ATOM   812  O  O    A ALA A 1 77  ? -19.492 9.852   14.775  0.50 14.70 ? 77  ALA A O    1 
ATOM   813  O  O    B ALA A 1 77  ? -19.465 9.038   15.112  0.50 11.43 ? 77  ALA A O    1 
ATOM   814  C  CB   A ALA A 1 77  ? -20.793 8.282   12.600  0.50 14.52 ? 77  ALA A CB   1 
ATOM   815  C  CB   B ALA A 1 77  ? -20.441 8.588   12.408  0.50 11.92 ? 77  ALA A CB   1 
ATOM   816  N  N    . VAL A 1 78  ? -21.411 9.249   15.978  1.00 11.92 ? 78  VAL A N    1 
ATOM   817  C  CA   . VAL A 1 78  ? -20.901 9.546   17.314  1.00 12.27 ? 78  VAL A CA   1 
ATOM   818  C  C    . VAL A 1 78  ? -21.022 8.407   18.278  1.00 10.54 ? 78  VAL A C    1 
ATOM   819  O  O    . VAL A 1 78  ? -22.061 7.727   18.345  1.00 12.81 ? 78  VAL A O    1 
ATOM   820  C  CB   . VAL A 1 78  ? -21.781 10.793  17.977  1.00 14.76 ? 78  VAL A CB   1 
ATOM   821  C  CG1  . VAL A 1 78  ? -21.580 11.027  19.499  1.00 17.05 ? 78  VAL A CG1  1 
ATOM   822  C  CG2  . VAL A 1 78  ? -21.382 12.059  17.146  1.00 18.62 ? 78  VAL A CG2  1 
ATOM   823  N  N    . LEU A 1 79  ? -19.955 8.262   19.081  1.00 9.49  ? 79  LEU A N    1 
ATOM   824  C  CA   . LEU A 1 79  ? -19.959 7.400   20.260  1.00 10.15 ? 79  LEU A CA   1 
ATOM   825  C  C    . LEU A 1 79  ? -19.956 8.237   21.494  1.00 9.40  ? 79  LEU A C    1 
ATOM   826  O  O    . LEU A 1 79  ? -19.114 9.167   21.597  1.00 10.65 ? 79  LEU A O    1 
ATOM   827  C  CB   . LEU A 1 79  ? -18.690 6.520   20.147  1.00 10.58 ? 79  LEU A CB   1 
ATOM   828  C  CG   . LEU A 1 79  ? -18.541 5.420   21.153  1.00 10.79 ? 79  LEU A CG   1 
ATOM   829  C  CD1  . LEU A 1 79  ? -19.581 4.290   20.905  1.00 15.68 ? 79  LEU A CD1  1 
ATOM   830  C  CD2  . LEU A 1 79  ? -17.150 4.793   21.118  1.00 10.98 ? 79  LEU A CD2  1 
ATOM   831  N  N    . LYS A 1 80  ? -20.789 7.903   22.437  1.00 10.30 ? 80  LYS A N    1 
ATOM   832  C  CA   . LYS A 1 80  ? -20.833 8.592   23.708  1.00 11.45 ? 80  LYS A CA   1 
ATOM   833  C  C    . LYS A 1 80  ? -21.394 7.676   24.760  1.00 11.44 ? 80  LYS A C    1 
ATOM   834  O  O    . LYS A 1 80  ? -21.667 6.521   24.493  1.00 11.52 ? 80  LYS A O    1 
ATOM   835  C  CB   . LYS A 1 80  ? -21.586 9.922   23.612  1.00 12.95 ? 80  LYS A CB   1 
ATOM   836  C  CG   . LYS A 1 80  ? -22.983 9.777   23.465  1.00 13.86 ? 80  LYS A CG   1 
ATOM   837  C  CD   . LYS A 1 80  ? -23.757 11.071  23.244  1.00 17.83 ? 80  LYS A CD   1 
ATOM   838  C  CE   . LYS A 1 80  ? -25.274 10.871  23.074  1.00 22.17 ? 80  LYS A CE   1 
ATOM   839  N  NZ   . LYS A 1 80  ? -25.922 10.700  24.366  1.00 31.22 ? 80  LYS A NZ   1 
ATOM   840  N  N    . GLY A 1 81  ? -21.533 8.177   25.975  1.00 11.90 ? 81  GLY A N    1 
ATOM   841  C  CA   . GLY A 1 81  ? -22.001 7.312   27.063  1.00 12.98 ? 81  GLY A CA   1 
ATOM   842  C  C    . GLY A 1 81  ? -20.963 6.252   27.360  1.00 12.43 ? 81  GLY A C    1 
ATOM   843  O  O    . GLY A 1 81  ? -19.763 6.468   27.221  1.00 11.70 ? 81  GLY A O    1 
ATOM   844  N  N    . GLY A 1 82  ? -21.443 5.145   27.938  1.00 15.56 ? 82  GLY A N    1 
ATOM   845  C  CA   . GLY A 1 82  ? -20.521 4.119   28.309  1.00 15.07 ? 82  GLY A CA   1 
ATOM   846  C  C    . GLY A 1 82  ? -19.647 4.724   29.444  1.00 14.94 ? 82  GLY A C    1 
ATOM   847  O  O    . GLY A 1 82  ? -20.133 5.386   30.316  1.00 17.70 ? 82  GLY A O    1 
ATOM   848  N  N    . PRO A 1 83  ? -18.284 4.535   29.350  1.00 13.19 ? 83  PRO A N    1 
ATOM   849  C  CA   . PRO A 1 83  ? -17.377 5.166   30.257  1.00 12.67 ? 83  PRO A CA   1 
ATOM   850  C  C    . PRO A 1 83  ? -16.972 6.567   29.898  1.00 12.50 ? 83  PRO A C    1 
ATOM   851  O  O    . PRO A 1 83  ? -16.193 7.185   30.620  1.00 13.84 ? 83  PRO A O    1 
ATOM   852  C  CB   . PRO A 1 83  ? -16.123 4.265   30.119  1.00 12.24 ? 83  PRO A CB   1 
ATOM   853  C  CG   . PRO A 1 83  ? -16.097 3.914   28.716  1.00 11.45 ? 83  PRO A CG   1 
ATOM   854  C  CD   . PRO A 1 83  ? -17.557 3.744   28.346  1.00 12.46 ? 83  PRO A CD   1 
ATOM   855  N  N    . LEU A 1 84  ? -17.438 7.102   28.801  1.00 10.09 ? 84  LEU A N    1 
ATOM   856  C  CA   . LEU A 1 84  ? -16.939 8.319   28.185  1.00 11.02 ? 84  LEU A CA   1 
ATOM   857  C  C    . LEU A 1 84  ? -17.594 9.582   28.752  1.00 11.72 ? 84  LEU A C    1 
ATOM   858  O  O    . LEU A 1 84  ? -18.752 9.617   29.036  1.00 14.32 ? 84  LEU A O    1 
ATOM   859  C  CB   . LEU A 1 84  ? -17.173 8.291   26.709  1.00 9.77  ? 84  LEU A CB   1 
ATOM   860  C  CG   . LEU A 1 84  ? -16.606 7.078   25.972  1.00 8.54  ? 84  LEU A CG   1 
ATOM   861  C  CD1  . LEU A 1 84  ? -17.073 7.036   24.524  1.00 10.06 ? 84  LEU A CD1  1 
ATOM   862  C  CD2  . LEU A 1 84  ? -15.061 7.076   26.035  1.00 10.14 ? 84  LEU A CD2  1 
ATOM   863  N  N    A ASP A 1 85  ? -16.914 10.743  28.631  0.50 13.01 ? 85  ASP A N    1 
ATOM   864  N  N    B ASP A 1 85  ? -16.676 10.533  28.976  0.50 12.36 ? 85  ASP A N    1 
ATOM   865  C  CA   A ASP A 1 85  ? -17.467 12.142  28.879  0.50 12.81 ? 85  ASP A CA   1 
ATOM   866  C  CA   B ASP A 1 85  ? -16.957 11.954  29.192  0.50 13.75 ? 85  ASP A CA   1 
ATOM   867  C  C    A ASP A 1 85  ? -17.316 12.768  27.575  0.50 11.72 ? 85  ASP A C    1 
ATOM   868  C  C    B ASP A 1 85  ? -16.818 12.510  27.782  0.50 14.44 ? 85  ASP A C    1 
ATOM   869  O  O    A ASP A 1 85  ? -16.430 12.524  26.741  0.50 13.15 ? 85  ASP A O    1 
ATOM   870  O  O    B ASP A 1 85  ? -15.719 12.731  27.206  0.50 18.78 ? 85  ASP A O    1 
ATOM   871  C  CB   A ASP A 1 85  ? -16.701 12.865  29.886  0.50 14.74 ? 85  ASP A CB   1 
ATOM   872  C  CB   B ASP A 1 85  ? -15.946 12.602  30.206  0.50 12.64 ? 85  ASP A CB   1 
ATOM   873  C  CG   A ASP A 1 85  ? -16.935 12.354  31.177  0.50 17.19 ? 85  ASP A CG   1 
ATOM   874  C  CG   B ASP A 1 85  ? -16.194 12.109  31.652  0.50 16.47 ? 85  ASP A CG   1 
ATOM   875  O  OD1  A ASP A 1 85  ? -18.065 11.906  31.468  0.50 25.02 ? 85  ASP A OD1  1 
ATOM   876  O  OD1  B ASP A 1 85  ? -17.292 11.522  31.967  0.50 15.75 ? 85  ASP A OD1  1 
ATOM   877  O  OD2  A ASP A 1 85  ? -16.019 12.640  32.014  0.50 28.26 ? 85  ASP A OD2  1 
ATOM   878  O  OD2  B ASP A 1 85  ? -15.331 12.372  32.541  0.50 20.91 ? 85  ASP A OD2  1 
ATOM   879  N  N    A GLY A 1 86  ? -18.313 13.519  27.277  0.50 12.64 ? 86  GLY A N    1 
ATOM   880  N  N    B GLY A 1 86  ? -17.897 12.637  27.115  0.50 14.86 ? 86  GLY A N    1 
ATOM   881  C  CA   A GLY A 1 86  ? -18.370 14.180  26.054  0.50 11.63 ? 86  GLY A CA   1 
ATOM   882  C  CA   B GLY A 1 86  ? -17.830 13.408  25.979  0.50 13.11 ? 86  GLY A CA   1 
ATOM   883  C  C    A GLY A 1 86  ? -18.705 13.276  24.844  0.50 12.26 ? 86  GLY A C    1 
ATOM   884  C  C    B GLY A 1 86  ? -18.141 12.623  24.774  0.50 13.05 ? 86  GLY A C    1 
ATOM   885  O  O    A GLY A 1 86  ? -19.339 12.240  25.027  0.50 12.57 ? 86  GLY A O    1 
ATOM   886  O  O    B GLY A 1 86  ? -18.511 11.453  24.873  0.50 14.69 ? 86  GLY A O    1 
ATOM   887  N  N    A THR A 1 87  ? -18.291 13.652  23.607  0.50 11.41 ? 87  THR A N    1 
ATOM   888  N  N    B THR A 1 87  ? -18.133 13.351  23.667  0.50 11.45 ? 87  THR A N    1 
ATOM   889  C  CA   A THR A 1 87  ? -18.660 13.017  22.322  0.50 11.18 ? 87  THR A CA   1 
ATOM   890  C  CA   B THR A 1 87  ? -18.565 12.832  22.424  0.50 10.39 ? 87  THR A CA   1 
ATOM   891  C  C    A THR A 1 87  ? -17.404 12.656  21.577  0.50 9.46  ? 87  THR A C    1 
ATOM   892  C  C    B THR A 1 87  ? -17.406 12.672  21.481  0.50 9.78  ? 87  THR A C    1 
ATOM   893  O  O    A THR A 1 87  ? -16.450 13.441  21.571  0.50 8.93  ? 87  THR A O    1 
ATOM   894  O  O    B THR A 1 87  ? -16.550 13.560  21.239  0.50 10.39 ? 87  THR A O    1 
ATOM   895  C  CB   A THR A 1 87  ? -19.522 14.037  21.439  0.50 13.71 ? 87  THR A CB   1 
ATOM   896  C  CB   B THR A 1 87  ? -19.650 13.745  21.779  0.50 10.43 ? 87  THR A CB   1 
ATOM   897  O  OG1  A THR A 1 87  ? -20.724 14.426  22.123  0.50 17.77 ? 87  THR A OG1  1 
ATOM   898  O  OG1  B THR A 1 87  ? -19.060 15.071  21.569  0.50 9.62  ? 87  THR A OG1  1 
ATOM   899  C  CG2  A THR A 1 87  ? -19.932 13.478  20.057  0.50 15.39 ? 87  THR A CG2  1 
ATOM   900  C  CG2  B THR A 1 87  ? -21.059 13.883  22.556  0.50 11.23 ? 87  THR A CG2  1 
ATOM   901  N  N    . TYR A 1 88  ? -17.437 11.501  20.899  1.00 8.80  ? 88  TYR A N    1 
ATOM   902  C  CA   . TYR A 1 88  ? -16.352 11.041  20.041  1.00 7.99  ? 88  TYR A CA   1 
ATOM   903  C  C    . TYR A 1 88  ? -16.882 10.744  18.690  1.00 8.80  ? 88  TYR A C    1 
ATOM   904  O  O    . TYR A 1 88  ? -17.854 10.043  18.475  1.00 12.52 ? 88  TYR A O    1 
ATOM   905  C  CB   . TYR A 1 88  ? -15.672 9.830   20.630  1.00 7.98  ? 88  TYR A CB   1 
ATOM   906  C  CG   . TYR A 1 88  ? -14.928 10.034  21.954  1.00 7.41  ? 88  TYR A CG   1 
ATOM   907  C  CD1  . TYR A 1 88  ? -15.578 10.318  23.157  1.00 8.40  ? 88  TYR A CD1  1 
ATOM   908  C  CD2  . TYR A 1 88  ? -13.548 9.903   21.987  1.00 7.00  ? 88  TYR A CD2  1 
ATOM   909  C  CE1  . TYR A 1 88  ? -14.883 10.527  24.339  1.00 8.98  ? 88  TYR A CE1  1 
ATOM   910  C  CE2  . TYR A 1 88  ? -12.854 10.038  23.189  1.00 7.03  ? 88  TYR A CE2  1 
ATOM   911  C  CZ   . TYR A 1 88  ? -13.523 10.316  24.350  1.00 7.28  ? 88  TYR A CZ   1 
ATOM   912  O  OH   . TYR A 1 88  ? -12.842 10.397  25.552  1.00 7.73  ? 88  TYR A OH   1 
ATOM   913  N  N    . ARG A 1 89  ? -16.217 11.248  17.682  1.00 7.77  ? 89  ARG A N    1 
ATOM   914  C  CA   . ARG A 1 89  ? -16.613 11.101  16.261  1.00 8.97  ? 89  ARG A CA   1 
ATOM   915  C  C    . ARG A 1 89  ? -15.866 10.034  15.497  1.00 7.43  ? 89  ARG A C    1 
ATOM   916  O  O    . ARG A 1 89  ? -14.622 9.989   15.518  1.00 7.02  ? 89  ARG A O    1 
ATOM   917  C  CB   . ARG A 1 89  ? -16.413 12.453  15.617  1.00 10.39 ? 89  ARG A CB   1 
ATOM   918  C  CG   . ARG A 1 89  ? -17.145 12.567  14.320  1.00 10.93 ? 89  ARG A CG   1 
ATOM   919  C  CD   . ARG A 1 89  ? -17.034 13.947  13.718  1.00 12.34 ? 89  ARG A CD   1 
ATOM   920  N  NE   . ARG A 1 89  ? -17.664 14.963  14.561  1.00 12.82 ? 89  ARG A NE   1 
ATOM   921  C  CZ   . ARG A 1 89  ? -17.537 16.276  14.385  1.00 10.86 ? 89  ARG A CZ   1 
ATOM   922  N  NH1  . ARG A 1 89  ? -16.799 16.756  13.389  1.00 13.80 ? 89  ARG A NH1  1 
ATOM   923  N  NH2  . ARG A 1 89  ? -18.151 17.112  15.211  1.00 13.16 ? 89  ARG A NH2  1 
ATOM   924  N  N    A LEU A 1 90  ? -16.695 9.180   14.888  0.50 6.14  ? 90  LEU A N    1 
ATOM   925  N  N    B LEU A 1 90  ? -16.527 9.267   14.624  0.50 7.49  ? 90  LEU A N    1 
ATOM   926  C  CA   A LEU A 1 90  ? -16.189 8.122   14.011  0.50 6.51  ? 90  LEU A CA   1 
ATOM   927  C  CA   B LEU A 1 90  ? -15.844 8.136   13.887  0.50 6.59  ? 90  LEU A CA   1 
ATOM   928  C  C    A LEU A 1 90  ? -15.364 8.701   12.863  0.50 6.54  ? 90  LEU A C    1 
ATOM   929  C  C    B LEU A 1 90  ? -14.938 8.707   12.752  0.50 6.60  ? 90  LEU A C    1 
ATOM   930  O  O    A LEU A 1 90  ? -15.809 9.584   12.142  0.50 6.18  ? 90  LEU A O    1 
ATOM   931  O  O    B LEU A 1 90  ? -15.417 9.412   11.851  0.50 8.88  ? 90  LEU A O    1 
ATOM   932  C  CB   A LEU A 1 90  ? -17.355 7.308   13.439  0.50 6.07  ? 90  LEU A CB   1 
ATOM   933  C  CB   B LEU A 1 90  ? -16.901 7.194   13.290  0.50 6.73  ? 90  LEU A CB   1 
ATOM   934  C  CG   A LEU A 1 90  ? -16.960 6.123   12.550  0.50 6.96  ? 90  LEU A CG   1 
ATOM   935  C  CG   B LEU A 1 90  ? -16.405 6.022   12.422  0.50 5.84  ? 90  LEU A CG   1 
ATOM   936  C  CD1  A LEU A 1 90  ? -16.191 5.063   13.380  0.50 6.80  ? 90  LEU A CD1  1 
ATOM   937  C  CD1  B LEU A 1 90  ? -15.619 5.021   13.268  0.50 7.80  ? 90  LEU A CD1  1 
ATOM   938  C  CD2  A LEU A 1 90  ? -18.206 5.590   11.854  0.50 8.13  ? 90  LEU A CD2  1 
ATOM   939  C  CD2  B LEU A 1 90  ? -17.633 5.324   11.818  0.50 7.47  ? 90  LEU A CD2  1 
ATOM   940  N  N    A ILE A 1 91  ? -14.146 8.208   12.702  0.50 5.64  ? 91  ILE A N    1 
ATOM   941  N  N    B ILE A 1 91  ? -13.679 8.288   12.742  0.50 6.53  ? 91  ILE A N    1 
ATOM   942  C  CA   A ILE A 1 91  ? -13.246 8.607   11.607  0.50 5.38  ? 91  ILE A CA   1 
ATOM   943  C  CA   B ILE A 1 91  ? -12.762 8.616   11.651  0.50 6.35  ? 91  ILE A CA   1 
ATOM   944  C  C    A ILE A 1 91  ? -12.954 7.437   10.700  0.50 5.28  ? 91  ILE A C    1 
ATOM   945  C  C    B ILE A 1 91  ? -12.519 7.424   10.711  0.50 6.88  ? 91  ILE A C    1 
ATOM   946  O  O    A ILE A 1 91  ? -12.871 7.624   9.482   0.50 5.76  ? 91  ILE A O    1 
ATOM   947  O  O    B ILE A 1 91  ? -12.437 7.587   9.480   0.50 7.51  ? 91  ILE A O    1 
ATOM   948  C  CB   A ILE A 1 91  ? -11.954 9.287   12.119  0.50 5.65  ? 91  ILE A CB   1 
ATOM   949  C  CB   B ILE A 1 91  ? -11.388 9.208   12.142  0.50 6.32  ? 91  ILE A CB   1 
ATOM   950  C  CG1  A ILE A 1 91  ? -11.033 9.718   10.977  0.50 5.67  ? 91  ILE A CG1  1 
ATOM   951  C  CG1  B ILE A 1 91  ? -10.444 9.470   10.981  0.50 8.04  ? 91  ILE A CG1  1 
ATOM   952  C  CG2  A ILE A 1 91  ? -11.231 8.452   13.156  0.50 6.19  ? 91  ILE A CG2  1 
ATOM   953  C  CG2  B ILE A 1 91  ? -10.688 8.391   13.236  0.50 7.12  ? 91  ILE A CG2  1 
ATOM   954  C  CD1  A ILE A 1 91  ? -9.943  10.699  11.376  0.50 7.48  ? 91  ILE A CD1  1 
ATOM   955  C  CD1  B ILE A 1 91  ? -9.319  10.415  11.313  0.50 9.38  ? 91  ILE A CD1  1 
ATOM   956  N  N    A GLN A 1 92  ? -12.815 6.199   11.208  0.50 6.33  ? 92  GLN A N    1 
ATOM   957  N  N    B GLN A 1 92  ? -12.356 6.189   11.225  0.50 5.79  ? 92  GLN A N    1 
ATOM   958  C  CA   A GLN A 1 92  ? -12.557 5.035   10.356  0.50 5.73  ? 92  GLN A CA   1 
ATOM   959  C  CA   B GLN A 1 92  ? -12.034 5.045   10.376  0.50 5.80  ? 92  GLN A CA   1 
ATOM   960  C  C    A GLN A 1 92  ? -12.766 3.788   11.155  0.50 5.46  ? 92  GLN A C    1 
ATOM   961  C  C    B GLN A 1 92  ? -12.338 3.746   11.140  0.50 6.82  ? 92  GLN A C    1 
ATOM   962  O  O    A GLN A 1 92  ? -12.836 3.799   12.379  0.50 5.57  ? 92  GLN A O    1 
ATOM   963  O  O    B GLN A 1 92  ? -12.320 3.756   12.360  0.50 6.16  ? 92  GLN A O    1 
ATOM   964  C  CB   A GLN A 1 92  ? -11.127 5.021   9.856   0.50 6.65  ? 92  GLN A CB   1 
ATOM   965  C  CB   B GLN A 1 92  ? -10.578 5.092   9.949   0.50 6.83  ? 92  GLN A CB   1 
ATOM   966  C  CG   A GLN A 1 92  ? -10.034 5.142   10.963  0.50 6.66  ? 92  GLN A CG   1 
ATOM   967  C  CG   B GLN A 1 92  ? -9.519  5.037   11.032  0.50 7.79  ? 92  GLN A CG   1 
ATOM   968  C  CD   A GLN A 1 92  ? -9.273  3.861   11.234  0.50 6.57  ? 92  GLN A CD   1 
ATOM   969  C  CD   B GLN A 1 92  ? -8.786  3.725   11.088  0.50 7.85  ? 92  GLN A CD   1 
ATOM   970  O  OE1  A GLN A 1 92  ? -9.846  2.760   11.220  0.50 7.47  ? 92  GLN A OE1  1 
ATOM   971  O  OE1  B GLN A 1 92  ? -9.403  2.647   11.182  0.50 8.08  ? 92  GLN A OE1  1 
ATOM   972  N  NE2  A GLN A 1 92  ? -8.000  3.959   11.496  0.50 9.95  ? 92  GLN A NE2  1 
ATOM   973  N  NE2  B GLN A 1 92  ? -7.501  3.765   11.101  0.50 10.53 ? 92  GLN A NE2  1 
ATOM   974  N  N    A PHE A 1 93  ? -12.856 2.679   10.411  0.50 6.53  ? 93  PHE A N    1 
ATOM   975  N  N    B PHE A 1 93  ? -12.619 2.645   10.421  0.50 8.06  ? 93  PHE A N    1 
ATOM   976  C  CA   A PHE A 1 93  ? -12.502 1.376   10.988  0.50 7.14  ? 93  PHE A CA   1 
ATOM   977  C  CA   B PHE A 1 93  ? -12.720 1.313   11.081  0.50 6.90  ? 93  PHE A CA   1 
ATOM   978  C  C    A PHE A 1 93  ? -11.537 0.546   10.172  0.50 6.96  ? 93  PHE A C    1 
ATOM   979  C  C    B PHE A 1 93  ? -11.797 0.443   10.223  0.50 7.12  ? 93  PHE A C    1 
ATOM   980  O  O    A PHE A 1 93  ? -11.180 0.770   8.984   0.50 7.93  ? 93  PHE A O    1 
ATOM   981  O  O    B PHE A 1 93  ? -11.630 0.657   9.026   0.50 8.01  ? 93  PHE A O    1 
ATOM   982  C  CB   A PHE A 1 93  ? -13.776 0.615   11.165  0.50 6.85  ? 93  PHE A CB   1 
ATOM   983  C  CB   B PHE A 1 93  ? -14.180 0.707   11.364  0.50 6.69  ? 93  PHE A CB   1 
ATOM   984  C  CG   A PHE A 1 93  ? -14.417 0.180   9.882   0.50 6.55  ? 93  PHE A CG   1 
ATOM   985  C  CG   B PHE A 1 93  ? -14.949 0.198   10.158  0.50 6.21  ? 93  PHE A CG   1 
ATOM   986  C  CD1  A PHE A 1 93  ? -13.987 -0.950  9.159   0.50 5.66  ? 93  PHE A CD1  1 
ATOM   987  C  CD1  B PHE A 1 93  ? -14.616 -0.984  9.491   0.50 5.55  ? 93  PHE A CD1  1 
ATOM   988  C  CD2  A PHE A 1 93  ? -15.483 0.940   9.380   0.50 6.92  ? 93  PHE A CD2  1 
ATOM   989  C  CD2  B PHE A 1 93  ? -16.110 0.848   9.748   0.50 5.70  ? 93  PHE A CD2  1 
ATOM   990  C  CE1  A PHE A 1 93  ? -14.622 -1.353  8.030   0.50 7.23  ? 93  PHE A CE1  1 
ATOM   991  C  CE1  B PHE A 1 93  ? -15.356 -1.445  8.370   0.50 5.81  ? 93  PHE A CE1  1 
ATOM   992  C  CE2  A PHE A 1 93  ? -16.122 0.511   8.255   0.50 6.45  ? 93  PHE A CE2  1 
ATOM   993  C  CE2  B PHE A 1 93  ? -16.832 0.373   8.658   0.50 5.45  ? 93  PHE A CE2  1 
ATOM   994  C  CZ   A PHE A 1 93  ? -15.697 -0.576  7.592   0.50 6.38  ? 93  PHE A CZ   1 
ATOM   995  C  CZ   B PHE A 1 93  ? -16.473 -0.734  7.949   0.50 5.00  ? 93  PHE A CZ   1 
ATOM   996  N  N    . HIS A 1 94  ? -11.114 -0.531  10.872  1.00 7.44  ? 94  HIS A N    1 
ATOM   997  C  CA   . HIS A 1 94  ? -10.268 -1.510  10.256  1.00 6.95  ? 94  HIS A CA   1 
ATOM   998  C  C    . HIS A 1 94  ? -10.331 -2.798  11.099  1.00 6.48  ? 94  HIS A C    1 
ATOM   999  O  O    . HIS A 1 94  ? -10.937 -2.802  12.168  1.00 6.98  ? 94  HIS A O    1 
ATOM   1000 C  CB   . HIS A 1 94  ? -8.790  -1.006  10.207  1.00 7.69  ? 94  HIS A CB   1 
ATOM   1001 C  CG   . HIS A 1 94  ? -8.265  -0.734  11.566  1.00 6.25  ? 94  HIS A CG   1 
ATOM   1002 N  ND1  . HIS A 1 94  ? -8.399  0.467   12.203  1.00 6.80  ? 94  HIS A ND1  1 
ATOM   1003 C  CD2  . HIS A 1 94  ? -7.641  -1.573  12.437  1.00 6.48  ? 94  HIS A CD2  1 
ATOM   1004 C  CE1  . HIS A 1 94  ? -7.921  0.342   13.426  1.00 6.26  ? 94  HIS A CE1  1 
ATOM   1005 N  NE2  . HIS A 1 94  ? -7.451  -0.904  13.645  1.00 5.96  ? 94  HIS A NE2  1 
ATOM   1006 N  N    . PHE A 1 95  ? -9.635  -3.821  10.642  1.00 6.85  ? 95  PHE A N    1 
ATOM   1007 C  CA   . PHE A 1 95  ? -9.594  -5.127  11.321  1.00 5.95  ? 95  PHE A CA   1 
ATOM   1008 C  C    . PHE A 1 95  ? -8.151  -5.555  11.508  1.00 6.26  ? 95  PHE A C    1 
ATOM   1009 O  O    . PHE A 1 95  ? -7.231  -5.093  10.822  1.00 7.34  ? 95  PHE A O    1 
ATOM   1010 C  CB   . PHE A 1 95  ? -10.345 -6.209  10.491  1.00 7.03  ? 95  PHE A CB   1 
ATOM   1011 C  CG   . PHE A 1 95  ? -11.753 -5.916  10.161  1.00 6.86  ? 95  PHE A CG   1 
ATOM   1012 C  CD1  . PHE A 1 95  ? -12.807 -6.544  10.832  1.00 7.21  ? 95  PHE A CD1  1 
ATOM   1013 C  CD2  . PHE A 1 95  ? -12.074 -5.071  9.090   1.00 7.75  ? 95  PHE A CD2  1 
ATOM   1014 C  CE1  . PHE A 1 95  ? -14.124 -6.316  10.480  1.00 8.57  ? 95  PHE A CE1  1 
ATOM   1015 C  CE2  . PHE A 1 95  ? -13.382 -4.858  8.755   1.00 8.17  ? 95  PHE A CE2  1 
ATOM   1016 C  CZ   . PHE A 1 95  ? -14.444 -5.457  9.411   1.00 8.13  ? 95  PHE A CZ   1 
ATOM   1017 N  N    . HIS A 1 96  ? -7.968  -6.530  12.406  1.00 5.91  ? 96  HIS A N    1 
ATOM   1018 C  CA   . HIS A 1 96  ? -6.793  -7.342  12.571  1.00 5.94  ? 96  HIS A CA   1 
ATOM   1019 C  C    . HIS A 1 96  ? -7.220  -8.795  12.456  1.00 6.00  ? 96  HIS A C    1 
ATOM   1020 O  O    . HIS A 1 96  ? -8.295  -9.157  12.972  1.00 6.26  ? 96  HIS A O    1 
ATOM   1021 C  CB   . HIS A 1 96  ? -6.126  -7.107  13.967  1.00 6.15  ? 96  HIS A CB   1 
ATOM   1022 C  CG   . HIS A 1 96  ? -5.831  -5.663  14.235  1.00 5.76  ? 96  HIS A CG   1 
ATOM   1023 N  ND1  . HIS A 1 96  ? -4.611  -5.114  14.050  1.00 6.56  ? 96  HIS A ND1  1 
ATOM   1024 C  CD2  . HIS A 1 96  ? -6.651  -4.660  14.604  1.00 5.61  ? 96  HIS A CD2  1 
ATOM   1025 C  CE1  . HIS A 1 96  ? -4.681  -3.821  14.349  1.00 6.45  ? 96  HIS A CE1  1 
ATOM   1026 N  NE2  . HIS A 1 96  ? -5.915  -3.464  14.700  1.00 5.80  ? 96  HIS A NE2  1 
ATOM   1027 N  N    . TRP A 1 97  ? -6.450  -9.635  11.804  1.00 5.76  ? 97  TRP A N    1 
ATOM   1028 C  CA   . TRP A 1 97  ? -6.843  -11.014 11.570  1.00 6.78  ? 97  TRP A CA   1 
ATOM   1029 C  C    . TRP A 1 97  ? -5.628  -11.929 11.455  1.00 6.28  ? 97  TRP A C    1 
ATOM   1030 O  O    . TRP A 1 97  ? -4.474  -11.501 11.373  1.00 6.85  ? 97  TRP A O    1 
ATOM   1031 C  CB   . TRP A 1 97  ? -7.767  -11.115 10.346  1.00 6.67  ? 97  TRP A CB   1 
ATOM   1032 C  CG   . TRP A 1 97  ? -7.094  -10.738 9.042   1.00 6.77  ? 97  TRP A CG   1 
ATOM   1033 C  CD1  . TRP A 1 97  ? -6.425  -11.531 8.197   1.00 7.65  ? 97  TRP A CD1  1 
ATOM   1034 C  CD2  . TRP A 1 97  ? -7.053  -9.428  8.483   1.00 7.91  ? 97  TRP A CD2  1 
ATOM   1035 N  NE1  . TRP A 1 97  ? -5.994  -10.827 7.115   1.00 8.65  ? 97  TRP A NE1  1 
ATOM   1036 C  CE2  . TRP A 1 97  ? -6.354  -9.520  7.279   1.00 8.34  ? 97  TRP A CE2  1 
ATOM   1037 C  CE3  . TRP A 1 97  ? -7.535  -8.160  8.894   1.00 7.52  ? 97  TRP A CE3  1 
ATOM   1038 C  CZ2  . TRP A 1 97  ? -6.149  -8.410  6.413   1.00 8.72  ? 97  TRP A CZ2  1 
ATOM   1039 C  CZ3  . TRP A 1 97  ? -7.315  -7.049  8.048   1.00 7.87  ? 97  TRP A CZ3  1 
ATOM   1040 C  CH2  . TRP A 1 97  ? -6.660  -7.189  6.857   1.00 9.18  ? 97  TRP A CH2  1 
ATOM   1041 N  N    . GLY A 1 98  ? -5.930  -13.226 11.456  1.00 6.54  ? 98  GLY A N    1 
ATOM   1042 C  CA   . GLY A 1 98  ? -4.928  -14.261 11.472  1.00 6.61  ? 98  GLY A CA   1 
ATOM   1043 C  C    . GLY A 1 98  ? -4.713  -14.933 10.156  1.00 7.88  ? 98  GLY A C    1 
ATOM   1044 O  O    . GLY A 1 98  ? -5.455  -14.776 9.187   1.00 8.23  ? 98  GLY A O    1 
ATOM   1045 N  N    . SER A 1 99  ? -3.661  -15.787 10.149  1.00 7.82  ? 99  SER A N    1 
ATOM   1046 C  CA   . SER A 1 99  ? -3.402  -16.750 9.058   1.00 8.80  ? 99  SER A CA   1 
ATOM   1047 C  C    . SER A 1 99  ? -4.334  -17.955 9.132   1.00 9.41  ? 99  SER A C    1 
ATOM   1048 O  O    . SER A 1 99  ? -4.443  -18.701 8.154   1.00 10.94 ? 99  SER A O    1 
ATOM   1049 C  CB   . SER A 1 99  ? -1.962  -17.121 9.026   1.00 10.41 ? 99  SER A CB   1 
ATOM   1050 O  OG   . SER A 1 99  ? -1.539  -17.623 10.263  1.00 10.48 ? 99  SER A OG   1 
ATOM   1051 N  N    . LEU A 1 100 ? -4.913  -18.213 10.291  1.00 9.59  ? 100 LEU A N    1 
ATOM   1052 C  CA   . LEU A 1 100 ? -5.714  -19.342 10.657  1.00 9.90  ? 100 LEU A CA   1 
ATOM   1053 C  C    . LEU A 1 100 ? -6.845  -18.866 11.507  1.00 8.34  ? 100 LEU A C    1 
ATOM   1054 O  O    . LEU A 1 100 ? -6.668  -17.870 12.207  1.00 9.24  ? 100 LEU A O    1 
ATOM   1055 C  CB   . LEU A 1 100 ? -4.863  -20.301 11.593  1.00 15.95 ? 100 LEU A CB   1 
ATOM   1056 C  CG   . LEU A 1 100 ? -3.519  -20.630 11.017  1.00 19.06 ? 100 LEU A CG   1 
ATOM   1057 C  CD1  . LEU A 1 100 ? -2.499  -21.068 12.175  1.00 24.06 ? 100 LEU A CD1  1 
ATOM   1058 C  CD2  . LEU A 1 100 ? -3.829  -21.707 10.055  1.00 23.26 ? 100 LEU A CD2  1 
ATOM   1059 N  N    . ASP A 1 101 ? -7.915  -19.627 11.594  1.00 9.07  ? 101 ASP A N    1 
ATOM   1060 C  CA   . ASP A 1 101 ? -9.086  -19.165 12.343  1.00 8.64  ? 101 ASP A CA   1 
ATOM   1061 C  C    . ASP A 1 101 ? -8.787  -19.088 13.839  1.00 8.36  ? 101 ASP A C    1 
ATOM   1062 O  O    . ASP A 1 101 ? -9.487  -18.352 14.539  1.00 9.77  ? 101 ASP A O    1 
ATOM   1063 C  CB   . ASP A 1 101 ? -10.302 -20.065 12.106  1.00 9.52  ? 101 ASP A CB   1 
ATOM   1064 C  CG   . ASP A 1 101 ? -10.798 -20.135 10.680  1.00 11.47 ? 101 ASP A CG   1 
ATOM   1065 O  OD1  . ASP A 1 101 ? -10.492 -19.265 9.886   1.00 11.23 ? 101 ASP A OD1  1 
ATOM   1066 O  OD2  . ASP A 1 101 ? -11.611 -21.035 10.471  1.00 18.30 ? 101 ASP A OD2  1 
ATOM   1067 N  N    . GLY A 1 102 ? -7.808  -19.871 14.343  1.00 8.80  ? 102 GLY A N    1 
ATOM   1068 C  CA   . GLY A 1 102 ? -7.514  -19.875 15.773  1.00 9.24  ? 102 GLY A CA   1 
ATOM   1069 C  C    . GLY A 1 102 ? -6.716  -18.708 16.303  1.00 7.87  ? 102 GLY A C    1 
ATOM   1070 O  O    . GLY A 1 102 ? -6.370  -18.710 17.487  1.00 9.86  ? 102 GLY A O    1 
ATOM   1071 N  N    . GLN A 1 103 ? -6.418  -17.716 15.511  1.00 7.60  ? 103 GLN A N    1 
ATOM   1072 C  CA   . GLN A 1 103 ? -5.722  -16.518 15.980  1.00 7.74  ? 103 GLN A CA   1 
ATOM   1073 C  C    . GLN A 1 103 ? -6.132  -15.337 15.112  1.00 6.53  ? 103 GLN A C    1 
ATOM   1074 O  O    . GLN A 1 103 ? -6.646  -15.537 14.024  1.00 7.26  ? 103 GLN A O    1 
ATOM   1075 C  CB   . GLN A 1 103 ? -4.194  -16.710 16.017  1.00 8.20  ? 103 GLN A CB   1 
ATOM   1076 C  CG   . GLN A 1 103 ? -3.565  -16.904 14.624  1.00 9.26  ? 103 GLN A CG   1 
ATOM   1077 C  CD   . GLN A 1 103 ? -2.214  -17.429 14.675  1.00 11.88 ? 103 GLN A CD   1 
ATOM   1078 O  OE1  . GLN A 1 103 ? -1.948  -18.290 15.497  1.00 18.02 ? 103 GLN A OE1  1 
ATOM   1079 N  NE2  . GLN A 1 103 ? -1.322  -17.030 13.841  1.00 12.54 ? 103 GLN A NE2  1 
ATOM   1080 N  N    . GLY A 1 104 ? -5.792  -14.124 15.585  1.00 6.26  ? 104 GLY A N    1 
ATOM   1081 C  CA   . GLY A 1 104 ? -6.086  -12.922 14.810  1.00 6.24  ? 104 GLY A CA   1 
ATOM   1082 C  C    . GLY A 1 104 ? -6.522  -11.747 15.656  1.00 5.92  ? 104 GLY A C    1 
ATOM   1083 O  O    . GLY A 1 104 ? -6.249  -10.594 15.279  1.00 6.49  ? 104 GLY A O    1 
ATOM   1084 N  N    . SER A 1 105 ? -7.220  -12.000 16.757  1.00 5.38  ? 105 SER A N    1 
ATOM   1085 C  CA   . SER A 1 105 ? -7.597  -10.897 17.637  1.00 5.54  ? 105 SER A CA   1 
ATOM   1086 C  C    . SER A 1 105 ? -6.407  -10.338 18.370  1.00 5.44  ? 105 SER A C    1 
ATOM   1087 O  O    . SER A 1 105 ? -5.393  -11.028 18.602  1.00 6.12  ? 105 SER A O    1 
ATOM   1088 C  CB   . SER A 1 105 ? -8.755  -11.238 18.568  1.00 5.46  ? 105 SER A CB   1 
ATOM   1089 O  OG   . SER A 1 105 ? -8.409  -12.202 19.555  1.00 5.72  ? 105 SER A OG   1 
ATOM   1090 N  N    . GLU A 1 106 ? -6.535  -9.084  18.791  1.00 4.83  ? 106 GLU A N    1 
ATOM   1091 C  CA   . GLU A 1 106 ? -5.532  -8.376  19.602  1.00 5.42  ? 106 GLU A CA   1 
ATOM   1092 C  C    . GLU A 1 106 ? -5.859  -8.549  21.086  1.00 5.43  ? 106 GLU A C    1 
ATOM   1093 O  O    . GLU A 1 106 ? -5.089  -9.124  21.864  1.00 5.56  ? 106 GLU A O    1 
ATOM   1094 C  CB   . GLU A 1 106 ? -5.457  -6.922  19.161  1.00 5.43  ? 106 GLU A CB   1 
ATOM   1095 C  CG   . GLU A 1 106 ? -4.921  -6.799  17.748  1.00 7.18  ? 106 GLU A CG   1 
ATOM   1096 C  CD   . GLU A 1 106 ? -4.317  -5.484  17.427  1.00 5.83  ? 106 GLU A CD   1 
ATOM   1097 O  OE1  . GLU A 1 106 ? -4.972  -4.457  17.662  1.00 5.66  ? 106 GLU A OE1  1 
ATOM   1098 O  OE2  . GLU A 1 106 ? -3.147  -5.486  16.937  1.00 6.71  ? 106 GLU A OE2  1 
ATOM   1099 N  N    . HIS A 1 107 ? -7.049  -8.077  21.494  1.00 4.91  ? 107 HIS A N    1 
ATOM   1100 C  CA   . HIS A 1 107 ? -7.529  -8.453  22.818  1.00 5.02  ? 107 HIS A CA   1 
ATOM   1101 C  C    . HIS A 1 107 ? -7.852  -9.975  22.814  1.00 5.32  ? 107 HIS A C    1 
ATOM   1102 O  O    . HIS A 1 107 ? -8.182  -10.576 21.805  1.00 5.51  ? 107 HIS A O    1 
ATOM   1103 C  CB   . HIS A 1 107 ? -8.787  -7.666  23.182  1.00 5.06  ? 107 HIS A CB   1 
ATOM   1104 C  CG   . HIS A 1 107 ? -8.466  -6.205  23.340  1.00 4.93  ? 107 HIS A CG   1 
ATOM   1105 N  ND1  . HIS A 1 107 ? -8.514  -5.306  22.296  1.00 5.10  ? 107 HIS A ND1  1 
ATOM   1106 C  CD2  . HIS A 1 107 ? -7.991  -5.494  24.413  1.00 5.09  ? 107 HIS A CD2  1 
ATOM   1107 C  CE1  . HIS A 1 107 ? -8.059  -4.130  22.772  1.00 5.37  ? 107 HIS A CE1  1 
ATOM   1108 N  NE2  . HIS A 1 107 ? -7.740  -4.187  24.023  1.00 5.32  ? 107 HIS A NE2  1 
ATOM   1109 N  N    . THR A 1 108 ? -7.721  -10.547 23.998  1.00 5.58  ? 108 THR A N    1 
ATOM   1110 C  CA   . THR A 1 108 ? -8.106  -11.935 24.284  1.00 5.96  ? 108 THR A CA   1 
ATOM   1111 C  C    . THR A 1 108 ? -9.023  -11.940 25.500  1.00 6.11  ? 108 THR A C    1 
ATOM   1112 O  O    . THR A 1 108 ? -9.055  -10.972 26.269  1.00 6.66  ? 108 THR A O    1 
ATOM   1113 C  CB   . THR A 1 108 ? -6.862  -12.842 24.499  1.00 6.31  ? 108 THR A CB   1 
ATOM   1114 O  OG1  . THR A 1 108 ? -6.021  -12.342 25.524  1.00 6.63  ? 108 THR A OG1  1 
ATOM   1115 C  CG2  . THR A 1 108 ? -6.040  -12.899 23.203  1.00 7.41  ? 108 THR A CG2  1 
ATOM   1116 N  N    . VAL A 1 109 ? -9.805  -13.002 25.646  1.00 5.92  ? 109 VAL A N    1 
ATOM   1117 C  CA   . VAL A 1 109 ? -10.799 -13.122 26.720  1.00 6.91  ? 109 VAL A CA   1 
ATOM   1118 C  C    . VAL A 1 109 ? -10.455 -14.404 27.496  1.00 6.93  ? 109 VAL A C    1 
ATOM   1119 O  O    . VAL A 1 109 ? -10.639 -15.502 26.917  1.00 7.07  ? 109 VAL A O    1 
ATOM   1120 C  CB   . VAL A 1 109 ? -12.220 -13.122 26.182  1.00 6.95  ? 109 VAL A CB   1 
ATOM   1121 C  CG1  . VAL A 1 109 ? -13.229 -13.242 27.333  1.00 9.41  ? 109 VAL A CG1  1 
ATOM   1122 C  CG2  . VAL A 1 109 ? -12.531 -11.856 25.350  1.00 8.32  ? 109 VAL A CG2  1 
ATOM   1123 N  N    . ASP A 1 110 ? -9.933  -14.297 28.685  1.00 7.58  ? 110 ASP A N    1 
ATOM   1124 C  CA   . ASP A 1 110 ? -9.434  -15.515 29.400  1.00 8.24  ? 110 ASP A CA   1 
ATOM   1125 C  C    . ASP A 1 110 ? -8.519  -16.313 28.516  1.00 8.22  ? 110 ASP A C    1 
ATOM   1126 O  O    . ASP A 1 110 ? -8.609  -17.559 28.450  1.00 8.87  ? 110 ASP A O    1 
ATOM   1127 C  CB   . ASP A 1 110 ? -10.589 -16.331 29.942  1.00 9.98  ? 110 ASP A CB   1 
ATOM   1128 C  CG   . ASP A 1 110 ? -11.443 -15.537 30.971  1.00 10.70 ? 110 ASP A CG   1 
ATOM   1129 O  OD1  . ASP A 1 110 ? -10.900 -14.675 31.646  1.00 11.32 ? 110 ASP A OD1  1 
ATOM   1130 O  OD2  . ASP A 1 110 ? -12.646 -15.884 31.101  1.00 12.91 ? 110 ASP A OD2  1 
ATOM   1131 N  N    . LYS A 1 111 ? -7.641  -15.601 27.802  1.00 7.38  ? 111 LYS A N    1 
ATOM   1132 C  CA   . LYS A 1 111 ? -6.626  -16.154 26.893  1.00 7.21  ? 111 LYS A CA   1 
ATOM   1133 C  C    . LYS A 1 111 ? -7.221  -16.643 25.572  1.00 7.67  ? 111 LYS A C    1 
ATOM   1134 O  O    . LYS A 1 111 ? -6.417  -17.031 24.680  1.00 8.61  ? 111 LYS A O    1 
ATOM   1135 C  CB   . LYS A 1 111 ? -5.727  -17.184 27.521  1.00 9.52  ? 111 LYS A CB   1 
ATOM   1136 C  CG   . LYS A 1 111 ? -4.943  -16.615 28.742  1.00 12.58 ? 111 LYS A CG   1 
ATOM   1137 C  CD   . LYS A 1 111 ? -4.038  -15.419 28.422  1.00 15.19 ? 111 LYS A CD   1 
ATOM   1138 C  CE   . LYS A 1 111 ? -3.174  -14.732 29.530  1.00 17.28 ? 111 LYS A CE   1 
ATOM   1139 N  NZ   . LYS A 1 111 ? -2.115  -15.573 29.907  1.00 19.48 ? 111 LYS A NZ   1 
ATOM   1140 N  N    . LYS A 1 112 ? -8.513  -16.622 25.370  1.00 7.20  ? 112 LYS A N    1 
ATOM   1141 C  CA   . LYS A 1 112 ? -9.092  -16.989 24.066  1.00 7.07  ? 112 LYS A CA   1 
ATOM   1142 C  C    . LYS A 1 112 ? -8.735  -15.971 23.009  1.00 6.51  ? 112 LYS A C    1 
ATOM   1143 O  O    . LYS A 1 112 ? -9.008  -14.749 23.222  1.00 6.78  ? 112 LYS A O    1 
ATOM   1144 C  CB   . LYS A 1 112 ? -10.616 -17.040 24.183  1.00 7.97  ? 112 LYS A CB   1 
ATOM   1145 C  CG   . LYS A 1 112 ? -11.333 -17.425 22.846  1.00 8.84  ? 112 LYS A CG   1 
ATOM   1146 C  CD   . LYS A 1 112 ? -12.847 -17.339 22.961  1.00 10.58 ? 112 LYS A CD   1 
ATOM   1147 C  CE   . LYS A 1 112 ? -13.540 -17.571 21.645  1.00 10.89 ? 112 LYS A CE   1 
ATOM   1148 N  NZ   . LYS A 1 112 ? -13.327 -18.929 21.179  1.00 11.35 ? 112 LYS A NZ   1 
ATOM   1149 N  N    A LYS A 1 113 ? -8.159  -16.409 21.915  0.50 6.60  ? 113 LYS A N    1 
ATOM   1150 N  N    B LYS A 1 113 ? -8.340  -16.447 21.839  0.50 6.26  ? 113 LYS A N    1 
ATOM   1151 C  CA   A LYS A 1 113 ? -8.077  -15.642 20.677  0.50 6.47  ? 113 LYS A CA   1 
ATOM   1152 C  CA   B LYS A 1 113 ? -8.002  -15.629 20.690  0.50 6.82  ? 113 LYS A CA   1 
ATOM   1153 C  C    A LYS A 1 113 ? -9.261  -15.884 19.770  0.50 6.51  ? 113 LYS A C    1 
ATOM   1154 C  C    B LYS A 1 113 ? -9.089  -15.860 19.641  0.50 6.12  ? 113 LYS A C    1 
ATOM   1155 O  O    A LYS A 1 113 ? -9.737  -17.045 19.550  0.50 6.55  ? 113 LYS A O    1 
ATOM   1156 O  O    B LYS A 1 113 ? -9.363  -17.019 19.253  0.50 6.29  ? 113 LYS A O    1 
ATOM   1157 C  CB   A LYS A 1 113 ? -6.819  -16.047 19.880  0.50 6.10  ? 113 LYS A CB   1 
ATOM   1158 C  CB   B LYS A 1 113 ? -6.638  -16.084 20.117  0.50 7.69  ? 113 LYS A CB   1 
ATOM   1159 C  CG   A LYS A 1 113 ? -5.477  -15.776 20.634  0.50 6.37  ? 113 LYS A CG   1 
ATOM   1160 C  CG   B LYS A 1 113 ? -5.432  -15.669 20.966  0.50 7.85  ? 113 LYS A CG   1 
ATOM   1161 C  CD   A LYS A 1 113 ? -4.272  -16.413 19.953  0.50 6.97  ? 113 LYS A CD   1 
ATOM   1162 C  CD   B LYS A 1 113 ? -4.174  -16.243 20.394  0.50 9.21  ? 113 LYS A CD   1 
ATOM   1163 C  CE   A LYS A 1 113 ? -2.955  -15.824 20.546  0.50 8.97  ? 113 LYS A CE   1 
ATOM   1164 C  CE   B LYS A 1 113 ? -2.975  -15.694 21.085  0.50 10.41 ? 113 LYS A CE   1 
ATOM   1165 N  NZ   A LYS A 1 113 ? -2.574  -16.485 21.866  0.50 10.05 ? 113 LYS A NZ   1 
ATOM   1166 N  NZ   B LYS A 1 113 ? -1.789  -16.492 20.655  0.50 14.09 ? 113 LYS A NZ   1 
ATOM   1167 N  N    . TYR A 1 114 ? -9.759  -14.772 19.209  1.00 5.94  ? 114 TYR A N    1 
ATOM   1168 C  CA   . TYR A 1 114 ? -10.744 -14.816 18.149  1.00 6.28  ? 114 TYR A CA   1 
ATOM   1169 C  C    . TYR A 1 114 ? -10.078 -14.795 16.783  1.00 5.84  ? 114 TYR A C    1 
ATOM   1170 O  O    . TYR A 1 114 ? -8.875  -14.494 16.664  1.00 6.39  ? 114 TYR A O    1 
ATOM   1171 C  CB   . TYR A 1 114 ? -11.784 -13.710 18.317  1.00 6.09  ? 114 TYR A CB   1 
ATOM   1172 C  CG   . TYR A 1 114 ? -12.760 -13.931 19.462  1.00 6.23  ? 114 TYR A CG   1 
ATOM   1173 C  CD1  . TYR A 1 114 ? -12.479 -13.507 20.728  1.00 7.75  ? 114 TYR A CD1  1 
ATOM   1174 C  CD2  . TYR A 1 114 ? -13.966 -14.537 19.225  1.00 6.91  ? 114 TYR A CD2  1 
ATOM   1175 C  CE1  . TYR A 1 114 ? -13.420 -13.684 21.778  1.00 8.78  ? 114 TYR A CE1  1 
ATOM   1176 C  CE2  . TYR A 1 114 ? -14.925 -14.687 20.237  1.00 8.81  ? 114 TYR A CE2  1 
ATOM   1177 C  CZ   . TYR A 1 114 ? -14.626 -14.257 21.513  1.00 9.53  ? 114 TYR A CZ   1 
ATOM   1178 O  OH   . TYR A 1 114 ? -15.499 -14.387 22.604  1.00 13.76 ? 114 TYR A OH   1 
ATOM   1179 N  N    . ALA A 1 115 ? -10.830 -15.101 15.740  1.00 6.48  ? 115 ALA A N    1 
ATOM   1180 C  CA   . ALA A 1 115 ? -10.300 -15.106 14.359  1.00 6.38  ? 115 ALA A CA   1 
ATOM   1181 C  C    . ALA A 1 115 ? -9.908  -13.741 13.893  1.00 6.30  ? 115 ALA A C    1 
ATOM   1182 O  O    . ALA A 1 115 ? -9.055  -13.580 13.012  1.00 6.76  ? 115 ALA A O    1 
ATOM   1183 C  CB   . ALA A 1 115 ? -11.349 -15.763 13.427  1.00 7.75  ? 115 ALA A CB   1 
ATOM   1184 N  N    . ALA A 1 116 ? -10.578 -12.692 14.400  1.00 6.34  ? 116 ALA A N    1 
ATOM   1185 C  CA   . ALA A 1 116 ? -10.268 -11.305 13.974  1.00 6.29  ? 116 ALA A CA   1 
ATOM   1186 C  C    . ALA A 1 116 ? -10.880 -10.374 14.984  1.00 5.75  ? 116 ALA A C    1 
ATOM   1187 O  O    . ALA A 1 116 ? -11.623 -10.765 15.891  1.00 5.98  ? 116 ALA A O    1 
ATOM   1188 C  CB   . ALA A 1 116 ? -10.810 -11.049 12.543  1.00 6.96  ? 116 ALA A CB   1 
ATOM   1189 N  N    . GLU A 1 117 ? -10.552 -9.079  14.830  1.00 5.87  ? 117 GLU A N    1 
ATOM   1190 C  CA   . GLU A 1 117 ? -11.073 -8.036  15.705  1.00 5.11  ? 117 GLU A CA   1 
ATOM   1191 C  C    . GLU A 1 117 ? -11.246 -6.758  14.871  1.00 5.77  ? 117 GLU A C    1 
ATOM   1192 O  O    . GLU A 1 117 ? -10.334 -6.362  14.130  1.00 6.38  ? 117 GLU A O    1 
ATOM   1193 C  CB   . GLU A 1 117 ? -10.098 -7.819  16.867  1.00 5.60  ? 117 GLU A CB   1 
ATOM   1194 C  CG   . GLU A 1 117 ? -10.585 -6.854  17.938  1.00 5.91  ? 117 GLU A CG   1 
ATOM   1195 C  CD   . GLU A 1 117 ? -9.660  -6.806  19.165  1.00 4.78  ? 117 GLU A CD   1 
ATOM   1196 O  OE1  . GLU A 1 117 ? -8.994  -7.812  19.449  1.00 5.66  ? 117 GLU A OE1  1 
ATOM   1197 O  OE2  . GLU A 1 117 ? -9.626  -5.719  19.810  1.00 5.72  ? 117 GLU A OE2  1 
ATOM   1198 N  N    . LEU A 1 118 ? -12.422 -6.173  14.985  1.00 5.48  ? 118 LEU A N    1 
ATOM   1199 C  CA   . LEU A 1 118 ? -12.809 -4.919  14.338  1.00 5.48  ? 118 LEU A CA   1 
ATOM   1200 C  C    . LEU A 1 118 ? -12.581 -3.768  15.318  1.00 5.57  ? 118 LEU A C    1 
ATOM   1201 O  O    . LEU A 1 118 ? -12.988 -3.855  16.493  1.00 5.60  ? 118 LEU A O    1 
ATOM   1202 C  CB   . LEU A 1 118 ? -14.321 -5.023  14.006  1.00 6.29  ? 118 LEU A CB   1 
ATOM   1203 C  CG   . LEU A 1 118 ? -15.042 -3.725  13.610  1.00 7.03  ? 118 LEU A CG   1 
ATOM   1204 C  CD1  . LEU A 1 118 ? -14.430 -3.070  12.368  1.00 8.03  ? 118 LEU A CD1  1 
ATOM   1205 C  CD2  . LEU A 1 118 ? -16.537 -4.061  13.364  1.00 8.70  ? 118 LEU A CD2  1 
ATOM   1206 N  N    . HIS A 1 119 ? -11.958 -2.712  14.838  1.00 5.29  ? 119 HIS A N    1 
ATOM   1207 C  CA   . HIS A 1 119 ? -11.717 -1.470  15.618  1.00 5.12  ? 119 HIS A CA   1 
ATOM   1208 C  C    . HIS A 1 119 ? -12.402 -0.319  14.913  1.00 5.43  ? 119 HIS A C    1 
ATOM   1209 O  O    . HIS A 1 119 ? -11.996 0.051   13.793  1.00 6.47  ? 119 HIS A O    1 
ATOM   1210 C  CB   . HIS A 1 119 ? -10.215 -1.203  15.716  1.00 5.70  ? 119 HIS A CB   1 
ATOM   1211 C  CG   . HIS A 1 119 ? -9.498  -2.185  16.593  1.00 4.89  ? 119 HIS A CG   1 
ATOM   1212 N  ND1  . HIS A 1 119 ? -8.133  -2.414  16.545  1.00 4.69  ? 119 HIS A ND1  1 
ATOM   1213 C  CD2  . HIS A 1 119 ? -10.017 -3.006  17.551  1.00 5.03  ? 119 HIS A CD2  1 
ATOM   1214 C  CE1  . HIS A 1 119 ? -7.863  -3.347  17.456  1.00 5.56  ? 119 HIS A CE1  1 
ATOM   1215 N  NE2  . HIS A 1 119 ? -8.988  -3.716  18.070  1.00 4.90  ? 119 HIS A NE2  1 
ATOM   1216 N  N    . LEU A 1 120 ? -13.378 0.274   15.565  1.00 5.41  ? 120 LEU A N    1 
ATOM   1217 C  CA   . LEU A 1 120 ? -14.064 1.498   15.133  1.00 6.22  ? 120 LEU A CA   1 
ATOM   1218 C  C    . LEU A 1 120 ? -13.449 2.634   15.937  1.00 5.08  ? 120 LEU A C    1 
ATOM   1219 O  O    . LEU A 1 120 ? -13.558 2.684   17.156  1.00 5.38  ? 120 LEU A O    1 
ATOM   1220 C  CB   . LEU A 1 120 ? -15.574 1.401   15.328  1.00 6.15  ? 120 LEU A CB   1 
ATOM   1221 C  CG   . LEU A 1 120 ? -16.257 0.317   14.458  1.00 7.50  ? 120 LEU A CG   1 
ATOM   1222 C  CD1  . LEU A 1 120 ? -17.121 -0.567  15.327  1.00 10.69 ? 120 LEU A CD1  1 
ATOM   1223 C  CD2  . LEU A 1 120 ? -17.083 1.010   13.343  1.00 9.73  ? 120 LEU A CD2  1 
ATOM   1224 N  N    . VAL A 1 121 ? -12.690 3.501   15.252  1.00 6.00  ? 121 VAL A N    1 
ATOM   1225 C  CA   . VAL A 1 121 ? -11.850 4.513   15.871  1.00 6.37  ? 121 VAL A CA   1 
ATOM   1226 C  C    . VAL A 1 121 ? -12.575 5.865   15.876  1.00 5.68  ? 121 VAL A C    1 
ATOM   1227 O  O    . VAL A 1 121 ? -13.002 6.331   14.822  1.00 6.64  ? 121 VAL A O    1 
ATOM   1228 C  CB   . VAL A 1 121 ? -10.538 4.651   15.081  1.00 6.30  ? 121 VAL A CB   1 
ATOM   1229 C  CG1  . VAL A 1 121 ? -9.615  5.723   15.687  1.00 7.10  ? 121 VAL A CG1  1 
ATOM   1230 C  CG2  . VAL A 1 121 ? -9.790  3.275   14.995  1.00 7.12  ? 121 VAL A CG2  1 
ATOM   1231 N  N    . HIS A 1 122 ? -12.656 6.490   17.032  1.00 5.86  ? 122 HIS A N    1 
ATOM   1232 C  CA   . HIS A 1 122 ? -13.364 7.752   17.247  1.00 5.95  ? 122 HIS A CA   1 
ATOM   1233 C  C    . HIS A 1 122 ? -12.451 8.751   17.984  1.00 6.11  ? 122 HIS A C    1 
ATOM   1234 O  O    . HIS A 1 122 ? -11.731 8.328   18.909  1.00 6.53  ? 122 HIS A O    1 
ATOM   1235 C  CB   . HIS A 1 122 ? -14.622 7.553   18.063  1.00 6.06  ? 122 HIS A CB   1 
ATOM   1236 C  CG   . HIS A 1 122 ? -15.525 6.428   17.624  1.00 6.51  ? 122 HIS A CG   1 
ATOM   1237 N  ND1  . HIS A 1 122 ? -15.207 5.115   17.931  1.00 6.44  ? 122 HIS A ND1  1 
ATOM   1238 C  CD2  . HIS A 1 122 ? -16.734 6.385   17.031  1.00 7.44  ? 122 HIS A CD2  1 
ATOM   1239 C  CE1  . HIS A 1 122 ? -16.211 4.352   17.460  1.00 6.33  ? 122 HIS A CE1  1 
ATOM   1240 N  NE2  . HIS A 1 122 ? -17.171 5.060   16.916  1.00 7.18  ? 122 HIS A NE2  1 
ATOM   1241 N  N    . TRP A 1 123 ? -12.539 10.024  17.635  1.00 6.20  ? 123 TRP A N    1 
ATOM   1242 C  CA   . TRP A 1 123 ? -11.754 11.046  18.355  1.00 6.09  ? 123 TRP A CA   1 
ATOM   1243 C  C    . TRP A 1 123 ? -12.660 11.981  19.093  1.00 6.33  ? 123 TRP A C    1 
ATOM   1244 O  O    . TRP A 1 123 ? -13.777 12.357  18.705  1.00 7.54  ? 123 TRP A O    1 
ATOM   1245 C  CB   . TRP A 1 123 ? -10.825 11.817  17.366  1.00 7.45  ? 123 TRP A CB   1 
ATOM   1246 C  CG   . TRP A 1 123 ? -11.497 12.425  16.152  1.00 7.75  ? 123 TRP A CG   1 
ATOM   1247 C  CD1  . TRP A 1 123 ? -11.677 11.831  14.955  1.00 8.75  ? 123 TRP A CD1  1 
ATOM   1248 C  CD2  . TRP A 1 123 ? -12.060 13.762  16.048  1.00 8.76  ? 123 TRP A CD2  1 
ATOM   1249 N  NE1  . TRP A 1 123 ? -12.344 12.651  14.122  1.00 10.41 ? 123 TRP A NE1  1 
ATOM   1250 C  CE2  . TRP A 1 123 ? -12.582 13.846  14.760  1.00 9.77  ? 123 TRP A CE2  1 
ATOM   1251 C  CE3  . TRP A 1 123 ? -12.148 14.891  16.913  1.00 9.53  ? 123 TRP A CE3  1 
ATOM   1252 C  CZ2  . TRP A 1 123 ? -13.221 15.012  14.260  1.00 10.24 ? 123 TRP A CZ2  1 
ATOM   1253 C  CZ3  . TRP A 1 123 ? -12.785 16.003  16.395  1.00 10.51 ? 123 TRP A CZ3  1 
ATOM   1254 C  CH2  . TRP A 1 123 ? -13.243 16.082  15.127  1.00 11.09 ? 123 TRP A CH2  1 
ATOM   1255 N  N    . ASN A 1 124 ? -12.132 12.470  20.233  1.00 6.72  ? 124 ASN A N    1 
ATOM   1256 C  CA   . ASN A 1 124 ? -12.887 13.337  21.159  1.00 7.14  ? 124 ASN A CA   1 
ATOM   1257 C  C    . ASN A 1 124 ? -13.038 14.728  20.558  1.00 7.45  ? 124 ASN A C    1 
ATOM   1258 O  O    . ASN A 1 124 ? -12.020 15.402  20.272  1.00 7.64  ? 124 ASN A O    1 
ATOM   1259 C  CB   . ASN A 1 124 ? -12.062 13.405  22.478  1.00 7.55  ? 124 ASN A CB   1 
ATOM   1260 C  CG   . ASN A 1 124 ? -12.849 14.000  23.621  1.00 7.58  ? 124 ASN A CG   1 
ATOM   1261 O  OD1  . ASN A 1 124 ? -13.721 14.877  23.390  1.00 8.73  ? 124 ASN A OD1  1 
ATOM   1262 N  ND2  . ASN A 1 124 ? -12.560 13.554  24.831  1.00 9.00  ? 124 ASN A ND2  1 
ATOM   1263 N  N    . THR A 1 125 ? -14.274 15.159  20.382  1.00 7.61  ? 125 THR A N    1 
ATOM   1264 C  CA   . THR A 1 125 ? -14.529 16.440  19.710  1.00 8.69  ? 125 THR A CA   1 
ATOM   1265 C  C    . THR A 1 125 ? -13.980 17.611  20.445  1.00 9.34  ? 125 THR A C    1 
ATOM   1266 O  O    . THR A 1 125 ? -13.812 18.674  19.857  1.00 10.45 ? 125 THR A O    1 
ATOM   1267 C  CB   . THR A 1 125 ? -16.025 16.584  19.386  1.00 11.53 ? 125 THR A CB   1 
ATOM   1268 O  OG1  . THR A 1 125 ? -16.795 16.552  20.604  1.00 14.09 ? 125 THR A OG1  1 
ATOM   1269 C  CG2  . THR A 1 125 ? -16.496 15.477  18.296  1.00 13.50 ? 125 THR A CG2  1 
ATOM   1270 N  N    A LYS A 1 126 ? -13.727 17.535  21.645  0.50 7.16  ? 127 LYS A N    1 
ATOM   1271 N  N    B LYS A 1 126 ? -13.509 17.417  21.944  0.50 9.00  ? 127 LYS A N    1 
ATOM   1272 C  CA   A LYS A 1 126 ? -13.183 18.650  22.378  0.50 8.74  ? 127 LYS A CA   1 
ATOM   1273 C  CA   B LYS A 1 126 ? -13.034 18.535  22.651  0.50 9.43  ? 127 LYS A CA   1 
ATOM   1274 C  C    A LYS A 1 126 ? -11.687 18.961  22.015  0.50 8.74  ? 127 LYS A C    1 
ATOM   1275 C  C    B LYS A 1 126 ? -11.701 18.993  21.971  0.50 10.46 ? 127 LYS A C    1 
ATOM   1276 O  O    A LYS A 1 126 ? -11.147 19.998  22.486  0.50 8.06  ? 127 LYS A O    1 
ATOM   1277 O  O    B LYS A 1 126 ? -11.321 20.147  22.113  0.50 13.32 ? 127 LYS A O    1 
ATOM   1278 C  CB   A LYS A 1 126 ? -13.376 18.419  23.884  0.50 8.13  ? 127 LYS A CB   1 
ATOM   1279 C  CB   B LYS A 1 126 ? -12.914 18.264  24.127  0.50 11.35 ? 127 LYS A CB   1 
ATOM   1280 C  CG   A LYS A 1 126 ? -12.272 17.555  24.517  0.50 8.31  ? 127 LYS A CG   1 
ATOM   1281 C  CG   B LYS A 1 126 ? -11.815 17.360  24.513  0.50 12.50 ? 127 LYS A CG   1 
ATOM   1282 C  CD   A LYS A 1 126 ? -12.608 17.217  25.983  0.50 11.18 ? 127 LYS A CD   1 
ATOM   1283 C  CD   B LYS A 1 126 ? -11.915 16.902  26.021  0.50 11.55 ? 127 LYS A CD   1 
ATOM   1284 C  CE   A LYS A 1 126 ? -11.612 16.459  26.725  0.50 12.38 ? 127 LYS A CE   1 
ATOM   1285 C  CE   B LYS A 1 126 ? -11.819 18.054  26.980  0.50 13.81 ? 127 LYS A CE   1 
ATOM   1286 N  NZ   A LYS A 1 126 ? -12.117 15.861  28.070  0.50 13.69 ? 127 LYS A NZ   1 
ATOM   1287 N  NZ   B LYS A 1 126 ? -12.251 17.679  28.348  0.50 16.17 ? 127 LYS A NZ   1 
ATOM   1288 N  N    . TYR A 1 127 ? -11.029 18.127  21.194  1.00 8.47  ? 128 TYR A N    1 
ATOM   1289 C  CA   . TYR A 1 127 ? -9.686  18.427  20.669  1.00 8.70  ? 128 TYR A CA   1 
ATOM   1290 C  C    . TYR A 1 127 ? -9.694  18.776  19.195  1.00 8.72  ? 128 TYR A C    1 
ATOM   1291 O  O    . TYR A 1 127 ? -8.616  19.033  18.629  1.00 8.90  ? 128 TYR A O    1 
ATOM   1292 C  CB   . TYR A 1 127 ? -8.752  17.258  20.971  1.00 8.87  ? 128 TYR A CB   1 
ATOM   1293 C  CG   . TYR A 1 127 ? -8.608  16.953  22.407  1.00 8.32  ? 128 TYR A CG   1 
ATOM   1294 C  CD1  . TYR A 1 127 ? -8.247  17.943  23.344  1.00 9.40  ? 128 TYR A CD1  1 
ATOM   1295 C  CD2  . TYR A 1 127 ? -8.915  15.679  22.932  1.00 8.83  ? 128 TYR A CD2  1 
ATOM   1296 C  CE1  . TYR A 1 127 ? -8.189  17.657  24.684  1.00 9.98  ? 128 TYR A CE1  1 
ATOM   1297 C  CE2  . TYR A 1 127 ? -8.848  15.418  24.270  1.00 8.95  ? 128 TYR A CE2  1 
ATOM   1298 C  CZ   . TYR A 1 127 ? -8.464  16.411  25.210  1.00 9.71  ? 128 TYR A CZ   1 
ATOM   1299 O  OH   . TYR A 1 127 ? -8.411  16.163  26.528  1.00 11.27 ? 128 TYR A OH   1 
ATOM   1300 N  N    . GLY A 1 128 ? -10.870 18.863  18.561  1.00 8.73  ? 129 GLY A N    1 
ATOM   1301 C  CA   . GLY A 1 128 ? -10.968 19.511  17.229  1.00 9.44  ? 129 GLY A CA   1 
ATOM   1302 C  C    . GLY A 1 128 ? -10.633 18.660  16.032  1.00 9.46  ? 129 GLY A C    1 
ATOM   1303 O  O    . GLY A 1 128 ? -11.313 18.789  14.985  1.00 11.08 ? 129 GLY A O    1 
ATOM   1304 N  N    A ASP A 1 129 ? -9.713  17.731  16.130  0.50 9.07  ? 130 ASP A N    1 
ATOM   1305 N  N    B ASP A 1 129 ? -9.501  17.875  16.067  0.50 9.95  ? 130 ASP A N    1 
ATOM   1306 C  CA   A ASP A 1 129 ? -9.582  16.802  15.058  0.50 7.64  ? 130 ASP A CA   1 
ATOM   1307 C  CA   B ASP A 1 129 ? -9.038  16.887  14.986  0.50 9.36  ? 130 ASP A CA   1 
ATOM   1308 C  C    A ASP A 1 129 ? -8.851  15.638  15.610  0.50 5.97  ? 130 ASP A C    1 
ATOM   1309 C  C    B ASP A 1 129 ? -8.231  15.723  15.549  0.50 9.76  ? 130 ASP A C    1 
ATOM   1310 O  O    A ASP A 1 129 ? -8.409  15.601  16.760  0.50 5.95  ? 130 ASP A O    1 
ATOM   1311 O  O    B ASP A 1 129 ? -7.733  15.702  16.697  0.50 9.16  ? 130 ASP A O    1 
ATOM   1312 C  CB   A ASP A 1 129 ? -8.902  17.396  13.814  0.50 8.17  ? 130 ASP A CB   1 
ATOM   1313 C  CB   B ASP A 1 129 ? -8.277  17.615  13.904  0.50 9.31  ? 130 ASP A CB   1 
ATOM   1314 C  CG   A ASP A 1 129 ? -7.462  17.884  14.012  0.50 6.75  ? 130 ASP A CG   1 
ATOM   1315 C  CG   B ASP A 1 129 ? -6.932  18.066  14.350  0.50 10.96 ? 130 ASP A CG   1 
ATOM   1316 O  OD1  A ASP A 1 129 ? -6.789  17.603  15.021  0.50 11.63 ? 130 ASP A OD1  1 
ATOM   1317 O  OD1  B ASP A 1 129 ? -6.557  17.740  15.475  0.50 20.23 ? 130 ASP A OD1  1 
ATOM   1318 O  OD2  A ASP A 1 129 ? -7.004  18.596  13.084  0.50 8.30  ? 130 ASP A OD2  1 
ATOM   1319 O  OD2  B ASP A 1 129 ? -6.325  18.838  13.662  0.50 19.67 ? 130 ASP A OD2  1 
ATOM   1320 N  N    A PHE A 1 130 ? -8.716  14.613  14.762  0.50 5.63  ? 131 PHE A N    1 
ATOM   1321 N  N    B PHE A 1 130 ? -8.108  14.679  14.735  0.50 8.44  ? 131 PHE A N    1 
ATOM   1322 C  CA   A PHE A 1 130 ? -7.999  13.384  15.158  0.50 6.22  ? 131 PHE A CA   1 
ATOM   1323 C  CA   B PHE A 1 130 ? -7.467  13.410  15.178  0.50 7.76  ? 131 PHE A CA   1 
ATOM   1324 C  C    A PHE A 1 130 ? -6.523  13.660  15.519  0.50 6.23  ? 131 PHE A C    1 
ATOM   1325 C  C    B PHE A 1 130 ? -6.010  13.630  15.620  0.50 7.22  ? 131 PHE A C    1 
ATOM   1326 O  O    A PHE A 1 130 ? -6.012  13.085  16.499  0.50 6.05  ? 131 PHE A O    1 
ATOM   1327 O  O    B PHE A 1 130 ? -5.537  13.064  16.606  0.50 7.44  ? 131 PHE A O    1 
ATOM   1328 C  CB   A PHE A 1 130 ? -8.094  12.356  13.998  0.50 5.86  ? 131 PHE A CB   1 
ATOM   1329 C  CB   B PHE A 1 130 ? -7.495  12.433  14.004  0.50 8.41  ? 131 PHE A CB   1 
ATOM   1330 C  CG   A PHE A 1 130 ? -7.345  11.079  14.249  0.50 5.00  ? 131 PHE A CG   1 
ATOM   1331 C  CG   B PHE A 1 130 ? -6.828  11.125  14.272  0.50 7.59  ? 131 PHE A CG   1 
ATOM   1332 C  CD1  A PHE A 1 130 ? -7.967  10.025  14.904  0.50 5.88  ? 131 PHE A CD1  1 
ATOM   1333 C  CD1  B PHE A 1 130 ? -7.464  10.063  14.927  0.50 7.85  ? 131 PHE A CD1  1 
ATOM   1334 C  CD2  A PHE A 1 130 ? -6.006  10.916  13.891  0.50 7.72  ? 131 PHE A CD2  1 
ATOM   1335 C  CD2  B PHE A 1 130 ? -5.494  10.962  13.900  0.50 8.81  ? 131 PHE A CD2  1 
ATOM   1336 C  CE1  A PHE A 1 130 ? -7.291  8.847   15.137  0.50 6.85  ? 131 PHE A CE1  1 
ATOM   1337 C  CE1  B PHE A 1 130 ? -6.794  8.853   15.147  0.50 7.47  ? 131 PHE A CE1  1 
ATOM   1338 C  CE2  A PHE A 1 130 ? -5.371  9.725   14.098  0.50 8.54  ? 131 PHE A CE2  1 
ATOM   1339 C  CE2  B PHE A 1 130 ? -4.844  9.774   14.079  0.50 9.82  ? 131 PHE A CE2  1 
ATOM   1340 C  CZ   A PHE A 1 130 ? -6.038  8.672   14.730  0.50 6.85  ? 131 PHE A CZ   1 
ATOM   1341 C  CZ   B PHE A 1 130 ? -5.508  8.688   14.721  0.50 8.32  ? 131 PHE A CZ   1 
ATOM   1342 N  N    A GLY A 1 131 ? -5.830  14.452  14.688  0.50 6.94  ? 132 GLY A N    1 
ATOM   1343 N  N    B GLY A 1 131 ? -5.249  14.376  14.817  0.50 8.84  ? 132 GLY A N    1 
ATOM   1344 C  CA   A GLY A 1 131 ? -4.382  14.617  14.928  0.50 7.42  ? 132 GLY A CA   1 
ATOM   1345 C  CA   B GLY A 1 131 ? -3.839  14.569  15.151  0.50 9.74  ? 132 GLY A CA   1 
ATOM   1346 C  C    A GLY A 1 131 ? -3.935  15.236  16.257  0.50 8.98  ? 132 GLY A C    1 
ATOM   1347 C  C    B GLY A 1 131 ? -3.749  15.262  16.496  0.50 10.12 ? 132 GLY A C    1 
ATOM   1348 O  O    A GLY A 1 131 ? -2.885  14.901  16.743  0.50 9.07  ? 132 GLY A O    1 
ATOM   1349 O  O    B GLY A 1 131 ? -2.803  14.979  17.275  0.50 9.99  ? 132 GLY A O    1 
ATOM   1350 N  N    . LYS A 1 132 ? -4.666  16.204  16.782  1.00 10.48 ? 133 LYS A N    1 
ATOM   1351 C  CA   . LYS A 1 132 ? -4.533  16.786  18.118  1.00 9.35  ? 133 LYS A CA   1 
ATOM   1352 C  C    . LYS A 1 132 ? -5.043  15.814  19.161  1.00 8.99  ? 133 LYS A C    1 
ATOM   1353 O  O    . LYS A 1 132 ? -4.471  15.729  20.302  1.00 9.13  ? 133 LYS A O    1 
ATOM   1354 C  CB   . LYS A 1 132 ? -5.265  18.127  18.226  1.00 10.32 ? 133 LYS A CB   1 
ATOM   1355 C  CG   . LYS A 1 132 ? -4.577  19.210  17.426  1.00 12.04 ? 133 LYS A CG   1 
ATOM   1356 C  CD   . LYS A 1 132 ? -3.261  19.566  18.149  1.00 20.65 ? 133 LYS A CD   1 
ATOM   1357 C  CE   . LYS A 1 132 ? -2.707  20.914  17.869  1.00 20.36 ? 133 LYS A CE   1 
ATOM   1358 N  NZ   . LYS A 1 132 ? -1.523  21.252  18.829  1.00 27.66 ? 133 LYS A NZ   1 
ATOM   1359 N  N    . ALA A 1 133 ? -6.117  15.073  18.918  1.00 8.31  ? 134 ALA A N    1 
ATOM   1360 C  CA   . ALA A 1 133 ? -6.666  14.133  19.901  1.00 7.71  ? 134 ALA A CA   1 
ATOM   1361 C  C    . ALA A 1 133 ? -5.680  13.083  20.314  1.00 7.48  ? 134 ALA A C    1 
ATOM   1362 O  O    . ALA A 1 133 ? -5.635  12.711  21.490  1.00 7.56  ? 134 ALA A O    1 
ATOM   1363 C  CB   . ALA A 1 133 ? -7.934  13.514  19.345  1.00 7.89  ? 134 ALA A CB   1 
ATOM   1364 N  N    . VAL A 1 134 ? -4.859  12.567  19.399  1.00 7.53  ? 135 VAL A N    1 
ATOM   1365 C  CA   . VAL A 1 134 ? -3.940  11.488  19.774  1.00 8.46  ? 135 VAL A CA   1 
ATOM   1366 C  C    . VAL A 1 134 ? -2.845  11.908  20.714  1.00 8.65  ? 135 VAL A C    1 
ATOM   1367 O  O    . VAL A 1 134 ? -2.150  11.042  21.272  1.00 9.14  ? 135 VAL A O    1 
ATOM   1368 C  CB   . VAL A 1 134 ? -3.325  10.755  18.531  1.00 8.89  ? 135 VAL A CB   1 
ATOM   1369 C  CG1  . VAL A 1 134 ? -4.436  10.048  17.711  1.00 10.46 ? 135 VAL A CG1  1 
ATOM   1370 C  CG2  . VAL A 1 134 ? -2.443  11.644  17.711  1.00 10.12 ? 135 VAL A CG2  1 
ATOM   1371 N  N    . GLN A 1 135 ? -2.681  13.210  20.932  1.00 9.04  ? 136 GLN A N    1 
ATOM   1372 C  CA   . GLN A 1 135 ? -1.707  13.751  21.883  1.00 9.30  ? 136 GLN A CA   1 
ATOM   1373 C  C    . GLN A 1 135 ? -2.292  13.873  23.285  1.00 9.02  ? 136 GLN A C    1 
ATOM   1374 O  O    . GLN A 1 135 ? -1.581  14.439  24.182  1.00 11.29 ? 136 GLN A O    1 
ATOM   1375 C  CB   . GLN A 1 135 ? -1.171  15.095  21.345  1.00 10.71 ? 136 GLN A CB   1 
ATOM   1376 C  CG   . GLN A 1 135 ? -0.525  14.931  19.971  1.00 12.72 ? 136 GLN A CG   1 
ATOM   1377 C  CD   . GLN A 1 135 ? -0.128  16.301  19.453  1.00 17.79 ? 136 GLN A CD   1 
ATOM   1378 O  OE1  . GLN A 1 135 ? -0.606  16.797  18.356  1.00 22.56 ? 136 GLN A OE1  1 
ATOM   1379 N  NE2  . GLN A 1 135 ? 0.789   16.918  20.163  1.00 20.93 ? 136 GLN A NE2  1 
ATOM   1380 N  N    . GLN A 1 136 ? -3.510  13.383  23.523  1.00 8.46  ? 137 GLN A N    1 
ATOM   1381 C  CA   . GLN A 1 136 ? -4.186  13.553  24.800  1.00 7.78  ? 137 GLN A CA   1 
ATOM   1382 C  C    . GLN A 1 136 ? -4.556  12.228  25.408  1.00 7.99  ? 137 GLN A C    1 
ATOM   1383 O  O    . GLN A 1 136 ? -4.908  11.293  24.677  1.00 7.40  ? 137 GLN A O    1 
ATOM   1384 C  CB   . GLN A 1 136 ? -5.428  14.370  24.607  1.00 8.65  ? 137 GLN A CB   1 
ATOM   1385 C  CG   . GLN A 1 136 ? -5.160  15.721  23.887  1.00 12.50 ? 137 GLN A CG   1 
ATOM   1386 C  CD   . GLN A 1 136 ? -4.276  16.673  24.838  1.00 14.58 ? 137 GLN A CD   1 
ATOM   1387 O  OE1  . GLN A 1 136 ? -4.263  16.460  25.977  1.00 20.84 ? 137 GLN A OE1  1 
ATOM   1388 N  NE2  . GLN A 1 136 ? -3.557  17.623  24.309  1.00 20.83 ? 137 GLN A NE2  1 
ATOM   1389 N  N    . PRO A 1 137 ? -4.583  12.109  26.737  1.00 8.14  ? 138 PRO A N    1 
ATOM   1390 C  CA   . PRO A 1 137 ? -4.878  10.773  27.361  1.00 8.52  ? 138 PRO A CA   1 
ATOM   1391 C  C    . PRO A 1 137 ? -6.294  10.281  27.181  1.00 8.17  ? 138 PRO A C    1 
ATOM   1392 O  O    . PRO A 1 137 ? -6.532  9.101   27.289  1.00 10.70 ? 138 PRO A O    1 
ATOM   1393 C  CB   . PRO A 1 137 ? -4.481  10.989  28.809  1.00 10.75 ? 138 PRO A CB   1 
ATOM   1394 C  CG   . PRO A 1 137 ? -4.347  12.330  28.963  1.00 14.78 ? 138 PRO A CG   1 
ATOM   1395 C  CD   . PRO A 1 137 ? -4.074  13.080  27.723  1.00 10.27 ? 138 PRO A CD   1 
ATOM   1396 N  N    . ASP A 1 138 ? -7.223  11.219  26.890  1.00 7.46  ? 139 ASP A N    1 
ATOM   1397 C  CA   . ASP A 1 138 ? -8.616  10.922  26.623  1.00 7.65  ? 139 ASP A CA   1 
ATOM   1398 C  C    . ASP A 1 138 ? -8.974  11.317  25.194  1.00 6.72  ? 139 ASP A C    1 
ATOM   1399 O  O    . ASP A 1 138 ? -10.081 11.734  24.913  1.00 7.50  ? 139 ASP A O    1 
ATOM   1400 C  CB   . ASP A 1 138 ? -9.555  11.571  27.627  1.00 9.33  ? 139 ASP A CB   1 
ATOM   1401 C  CG   . ASP A 1 138 ? -9.473  13.029  27.688  1.00 9.71  ? 139 ASP A CG   1 
ATOM   1402 O  OD1  . ASP A 1 138 ? -8.501  13.629  27.076  1.00 9.85  ? 139 ASP A OD1  1 
ATOM   1403 O  OD2  . ASP A 1 138 ? -10.341 13.595  28.398  1.00 12.23 ? 139 ASP A OD2  1 
ATOM   1404 N  N    . GLY A 1 139 ? -7.993  11.208  24.269  1.00 6.67  ? 140 GLY A N    1 
ATOM   1405 C  CA   . GLY A 1 139 ? -8.221  11.671  22.891  1.00 6.28  ? 140 GLY A CA   1 
ATOM   1406 C  C    . GLY A 1 139 ? -9.081  10.787  22.015  1.00 6.20  ? 140 GLY A C    1 
ATOM   1407 O  O    . GLY A 1 139 ? -9.755  11.291  21.134  1.00 6.22  ? 140 GLY A O    1 
ATOM   1408 N  N    . LEU A 1 140 ? -8.955  9.450   22.174  1.00 6.05  ? 141 LEU A N    1 
ATOM   1409 C  CA   . LEU A 1 140 ? -9.621  8.485   21.329  1.00 5.65  ? 141 LEU A CA   1 
ATOM   1410 C  C    . LEU A 1 140 ? -10.506 7.574   22.126  1.00 5.27  ? 141 LEU A C    1 
ATOM   1411 O  O    . LEU A 1 140 ? -10.222 7.263   23.291  1.00 5.63  ? 141 LEU A O    1 
ATOM   1412 C  CB   . LEU A 1 140 ? -8.669  7.654   20.501  1.00 5.95  ? 141 LEU A CB   1 
ATOM   1413 C  CG   . LEU A 1 140 ? -7.740  8.366   19.522  1.00 6.49  ? 141 LEU A CG   1 
ATOM   1414 C  CD1  . LEU A 1 140 ? -6.950  7.296   18.712  1.00 7.16  ? 141 LEU A CD1  1 
ATOM   1415 C  CD2  . LEU A 1 140 ? -8.393  9.355   18.601  1.00 7.95  ? 141 LEU A CD2  1 
ATOM   1416 N  N    . ALA A 1 141 ? -11.539 7.030   21.486  1.00 5.40  ? 142 ALA A N    1 
ATOM   1417 C  CA   . ALA A 1 141 ? -12.343 5.922   22.018  1.00 5.70  ? 142 ALA A CA   1 
ATOM   1418 C  C    . ALA A 1 141 ? -12.426 4.901   20.870  1.00 5.71  ? 142 ALA A C    1 
ATOM   1419 O  O    . ALA A 1 141 ? -12.798 5.273   19.748  1.00 6.38  ? 142 ALA A O    1 
ATOM   1420 C  CB   . ALA A 1 141 ? -13.726 6.371   22.439  1.00 7.32  ? 142 ALA A CB   1 
ATOM   1421 N  N    A VAL A 1 142 ? -12.093 3.661   21.173  0.50 4.46  ? 143 VAL A N    1 
ATOM   1422 N  N    B VAL A 1 142 ? -11.847 3.714   21.139  0.50 5.11  ? 143 VAL A N    1 
ATOM   1423 C  CA   A VAL A 1 142 ? -12.202 2.575   20.152  0.50 4.21  ? 143 VAL A CA   1 
ATOM   1424 C  CA   B VAL A 1 142 ? -11.858 2.663   20.108  0.50 4.75  ? 143 VAL A CA   1 
ATOM   1425 C  C    A VAL A 1 142 ? -13.213 1.574   20.674  0.50 5.01  ? 143 VAL A C    1 
ATOM   1426 C  C    B VAL A 1 142 ? -12.838 1.612   20.583  0.50 4.36  ? 143 VAL A C    1 
ATOM   1427 O  O    A VAL A 1 142 ? -13.120 1.100   21.815  0.50 4.75  ? 143 VAL A O    1 
ATOM   1428 O  O    B VAL A 1 142 ? -12.704 1.049   21.671  0.50 4.73  ? 143 VAL A O    1 
ATOM   1429 C  CB   A VAL A 1 142 ? -10.869 1.934   19.830  0.50 5.17  ? 143 VAL A CB   1 
ATOM   1430 C  CB   B VAL A 1 142 ? -10.434 2.102   19.804  0.50 5.61  ? 143 VAL A CB   1 
ATOM   1431 C  CG1  A VAL A 1 142 ? -11.063 0.821   18.766  0.50 5.75  ? 143 VAL A CG1  1 
ATOM   1432 C  CG1  B VAL A 1 142 ? -10.538 1.065   18.683  0.50 5.27  ? 143 VAL A CG1  1 
ATOM   1433 C  CG2  A VAL A 1 142 ? -9.850  2.980   19.294  0.50 6.88  ? 143 VAL A CG2  1 
ATOM   1434 C  CG2  B VAL A 1 142 ? -9.488  3.248   19.468  0.50 6.61  ? 143 VAL A CG2  1 
ATOM   1435 N  N    A LEU A 1 143 ? -14.211 1.307   19.812  0.50 4.05  ? 144 LEU A N    1 
ATOM   1436 N  N    B LEU A 1 143 ? -13.793 1.307   19.678  0.50 4.34  ? 144 LEU A N    1 
ATOM   1437 C  CA   A LEU A 1 143 ? -15.157 0.237   20.075  0.50 4.48  ? 144 LEU A CA   1 
ATOM   1438 C  CA   B LEU A 1 143 ? -14.779 0.245   19.882  0.50 4.72  ? 144 LEU A CA   1 
ATOM   1439 C  C    A LEU A 1 143 ? -14.584 -0.978  19.340  0.50 4.41  ? 144 LEU A C    1 
ATOM   1440 C  C    B LEU A 1 143 ? -14.193 -1.017  19.230  0.50 4.51  ? 144 LEU A C    1 
ATOM   1441 O  O    A LEU A 1 143 ? -14.504 -1.005  18.089  0.50 4.39  ? 144 LEU A O    1 
ATOM   1442 O  O    B LEU A 1 143 ? -13.972 -1.062  18.002  0.50 4.51  ? 144 LEU A O    1 
ATOM   1443 C  CB   A LEU A 1 143 ? -16.551 0.667   19.520  0.50 5.12  ? 144 LEU A CB   1 
ATOM   1444 C  CB   B LEU A 1 143 ? -16.106 0.681   19.232  0.50 5.79  ? 144 LEU A CB   1 
ATOM   1445 C  CG   A LEU A 1 143 ? -17.669 -0.288  19.753  0.50 5.95  ? 144 LEU A CG   1 
ATOM   1446 C  CG   B LEU A 1 143 ? -17.250 -0.316  19.388  0.50 6.34  ? 144 LEU A CG   1 
ATOM   1447 C  CD1  A LEU A 1 143 ? -17.926 -0.440  21.255  0.50 8.49  ? 144 LEU A CD1  1 
ATOM   1448 C  CD1  B LEU A 1 143 ? -17.520 -0.720  20.872  0.50 6.66  ? 144 LEU A CD1  1 
ATOM   1449 C  CD2  A LEU A 1 143 ? -18.938 0.190   19.063  0.50 6.41  ? 144 LEU A CD2  1 
ATOM   1450 C  CD2  B LEU A 1 143 ? -18.513 0.210   18.689  0.50 8.36  ? 144 LEU A CD2  1 
ATOM   1451 N  N    A GLY A 1 144 ? -14.263 -2.003  20.129  0.50 5.07  ? 145 GLY A N    1 
ATOM   1452 N  N    B GLY A 1 144 ? -13.917 -2.021  20.054  0.50 4.15  ? 145 GLY A N    1 
ATOM   1453 C  CA   A GLY A 1 144 ? -13.696 -3.260  19.618  0.50 4.44  ? 145 GLY A CA   1 
ATOM   1454 C  CA   B GLY A 1 144 ? -13.335 -3.284  19.584  0.50 4.37  ? 145 GLY A CA   1 
ATOM   1455 C  C    A GLY A 1 144 ? -14.751 -4.348  19.663  0.50 4.62  ? 145 GLY A C    1 
ATOM   1456 C  C    B GLY A 1 144 ? -14.379 -4.395  19.590  0.50 4.38  ? 145 GLY A C    1 
ATOM   1457 O  O    A GLY A 1 144 ? -15.477 -4.476  20.640  0.50 4.90  ? 145 GLY A O    1 
ATOM   1458 O  O    B GLY A 1 144 ? -15.097 -4.587  20.567  0.50 4.97  ? 145 GLY A O    1 
ATOM   1459 N  N    A ILE A 1 145 ? -14.804 -5.136  18.582  0.50 4.21  ? 146 ILE A N    1 
ATOM   1460 N  N    B ILE A 1 145 ? -14.474 -5.113  18.463  0.50 4.12  ? 146 ILE A N    1 
ATOM   1461 C  CA   A ILE A 1 145 ? -15.793 -6.173  18.415  0.50 4.50  ? 146 ILE A CA   1 
ATOM   1462 C  CA   B ILE A 1 145 ? -15.490 -6.151  18.245  0.50 3.80  ? 146 ILE A CA   1 
ATOM   1463 C  C    A ILE A 1 145 ? -15.052 -7.376  17.819  0.50 4.77  ? 146 ILE A C    1 
ATOM   1464 C  C    B ILE A 1 145 ? -14.805 -7.392  17.790  0.50 4.66  ? 146 ILE A C    1 
ATOM   1465 O  O    A ILE A 1 145 ? -14.431 -7.330  16.797  0.50 5.17  ? 146 ILE A O    1 
ATOM   1466 O  O    B ILE A 1 145 ? -14.010 -7.359  16.813  0.50 4.94  ? 146 ILE A O    1 
ATOM   1467 C  CB   A ILE A 1 145 ? -16.946 -5.681  17.518  0.50 4.50  ? 146 ILE A CB   1 
ATOM   1468 C  CB   B ILE A 1 145 ? -16.497 -5.656  17.194  0.50 3.79  ? 146 ILE A CB   1 
ATOM   1469 C  CG1  A ILE A 1 145 ? -17.592 -4.412  18.093  0.50 5.85  ? 146 ILE A CG1  1 
ATOM   1470 C  CG1  B ILE A 1 145 ? -17.168 -4.323  17.659  0.50 4.85  ? 146 ILE A CG1  1 
ATOM   1471 C  CG2  A ILE A 1 145 ? -17.997 -6.758  17.297  0.50 5.69  ? 146 ILE A CG2  1 
ATOM   1472 C  CG2  B ILE A 1 145 ? -17.567 -6.827  16.928  0.50 5.42  ? 146 ILE A CG2  1 
ATOM   1473 C  CD1  A ILE A 1 145 ? -18.669 -3.757  17.159  0.50 5.33  ? 146 ILE A CD1  1 
ATOM   1474 C  CD1  B ILE A 1 145 ? -18.233 -3.799  16.743  0.50 5.36  ? 146 ILE A CD1  1 
ATOM   1475 N  N    . PHE A 1 146 ? -15.098 -8.502  18.504  1.00 5.64  ? 147 PHE A N    1 
ATOM   1476 C  CA   . PHE A 1 146 ? -14.493 -9.772  18.076  1.00 5.46  ? 147 PHE A CA   1 
ATOM   1477 C  C    . PHE A 1 146 ? -15.254 -10.380 16.911  1.00 5.85  ? 147 PHE A C    1 
ATOM   1478 O  O    . PHE A 1 146 ? -16.481 -10.245 16.847  1.00 6.56  ? 147 PHE A O    1 
ATOM   1479 C  CB   . PHE A 1 146 ? -14.511 -10.743 19.250  1.00 5.69  ? 147 PHE A CB   1 
ATOM   1480 C  CG   . PHE A 1 146 ? -13.651 -10.284 20.404  1.00 4.86  ? 147 PHE A CG   1 
ATOM   1481 C  CD1  . PHE A 1 146 ? -12.298 -10.094 20.235  1.00 5.77  ? 147 PHE A CD1  1 
ATOM   1482 C  CD2  . PHE A 1 146 ? -14.189 -10.063 21.650  1.00 6.00  ? 147 PHE A CD2  1 
ATOM   1483 C  CE1  . PHE A 1 146 ? -11.461 -9.718  21.331  1.00 6.51  ? 147 PHE A CE1  1 
ATOM   1484 C  CE2  . PHE A 1 146 ? -13.391 -9.695  22.725  1.00 6.15  ? 147 PHE A CE2  1 
ATOM   1485 C  CZ   . PHE A 1 146 ? -12.050 -9.522  22.569  1.00 6.05  ? 147 PHE A CZ   1 
ATOM   1486 N  N    . LEU A 1 147 ? -14.549 -11.103 16.074  1.00 5.97  ? 148 LEU A N    1 
ATOM   1487 C  CA   . LEU A 1 147 ? -15.125 -11.901 14.949  1.00 6.01  ? 148 LEU A CA   1 
ATOM   1488 C  C    . LEU A 1 147 ? -14.789 -13.357 15.214  1.00 6.00  ? 148 LEU A C    1 
ATOM   1489 O  O    . LEU A 1 147 ? -13.629 -13.725 15.426  1.00 6.48  ? 148 LEU A O    1 
ATOM   1490 C  CB   . LEU A 1 147 ? -14.545 -11.498 13.613  1.00 6.98  ? 148 LEU A CB   1 
ATOM   1491 C  CG   . LEU A 1 147 ? -15.078 -10.227 12.891  1.00 8.14  ? 148 LEU A CG   1 
ATOM   1492 C  CD1  . LEU A 1 147 ? -14.903 -8.964  13.825  1.00 8.60  ? 148 LEU A CD1  1 
ATOM   1493 C  CD2  . LEU A 1 147 ? -14.416 -10.029 11.557  1.00 8.53  ? 148 LEU A CD2  1 
ATOM   1494 N  N    . LYS A 1 148 ? -15.804 -14.204 15.082  1.00 6.59  ? 149 LYS A N    1 
ATOM   1495 C  CA   . LYS A 1 148 ? -15.644 -15.659 15.035  1.00 7.20  ? 149 LYS A CA   1 
ATOM   1496 C  C    . LYS A 1 148 ? -16.123 -16.138 13.680  1.00 7.56  ? 149 LYS A C    1 
ATOM   1497 O  O    . LYS A 1 148 ? -16.939 -15.482 13.033  1.00 8.40  ? 149 LYS A O    1 
ATOM   1498 C  CB   . LYS A 1 148 ? -16.381 -16.360 16.158  1.00 8.25  ? 149 LYS A CB   1 
ATOM   1499 C  CG   . LYS A 1 148 ? -17.882 -16.235 16.109  1.00 10.17 ? 149 LYS A CG   1 
ATOM   1500 C  CD   . LYS A 1 148 ? -18.563 -16.922 17.325  1.00 14.29 ? 149 LYS A CD   1 
ATOM   1501 C  CE   . LYS A 1 148 ? -19.974 -17.065 17.252  1.00 21.43 ? 149 LYS A CE   1 
ATOM   1502 N  NZ   . LYS A 1 148 ? -20.580 -17.955 18.264  1.00 26.80 ? 149 LYS A NZ   1 
ATOM   1503 N  N    . VAL A 1 149 ? -15.641 -17.298 13.266  1.00 8.14  ? 150 VAL A N    1 
ATOM   1504 C  CA   . VAL A 1 149 ? -16.021 -17.896 11.971  1.00 7.63  ? 150 VAL A CA   1 
ATOM   1505 C  C    . VAL A 1 149 ? -17.252 -18.800 12.129  1.00 8.58  ? 150 VAL A C    1 
ATOM   1506 O  O    . VAL A 1 149 ? -17.205 -19.781 12.909  1.00 9.81  ? 150 VAL A O    1 
ATOM   1507 C  CB   . VAL A 1 149 ? -14.798 -18.631 11.381  1.00 8.72  ? 150 VAL A CB   1 
ATOM   1508 C  CG1  . VAL A 1 149 ? -15.198 -19.420 10.101  1.00 11.06 ? 150 VAL A CG1  1 
ATOM   1509 C  CG2  . VAL A 1 149 ? -13.701 -17.626 11.076  1.00 10.50 ? 150 VAL A CG2  1 
ATOM   1510 N  N    . GLY A 1 150 ? -18.283 -18.548 11.401  1.00 8.75  ? 151 GLY A N    1 
ATOM   1511 C  CA   . GLY A 1 150 ? -19.522 -19.333 11.420  1.00 9.89  ? 151 GLY A CA   1 
ATOM   1512 C  C    . GLY A 1 150 ? -20.411 -18.878 10.290  1.00 9.74  ? 151 GLY A C    1 
ATOM   1513 O  O    . GLY A 1 150 ? -20.025 -18.937 9.103   1.00 10.39 ? 151 GLY A O    1 
ATOM   1514 N  N    A SER A 1 151 ? -21.617 -18.405 10.621  0.50 10.55 ? 152 SER A N    1 
ATOM   1515 N  N    B SER A 1 151 ? -21.578 -18.359 10.678  0.50 10.09 ? 152 SER A N    1 
ATOM   1516 C  CA   A SER A 1 151 ? -22.479 -17.808 9.603   0.50 11.21 ? 152 SER A CA   1 
ATOM   1517 C  CA   B SER A 1 151 ? -22.487 -17.715 9.762   0.50 10.01 ? 152 SER A CA   1 
ATOM   1518 C  C    A SER A 1 151 ? -21.908 -16.496 9.108   0.50 10.79 ? 152 SER A C    1 
ATOM   1519 C  C    B SER A 1 151 ? -21.822 -16.488 9.097   0.50 10.20 ? 152 SER A C    1 
ATOM   1520 O  O    A SER A 1 151 ? -21.284 -15.744 9.864   0.50 10.72 ? 152 SER A O    1 
ATOM   1521 O  O    B SER A 1 151 ? -20.957 -15.828 9.686   0.50 9.50  ? 152 SER A O    1 
ATOM   1522 C  CB   A SER A 1 151 ? -23.854 -17.515 10.151  0.50 13.73 ? 152 SER A CB   1 
ATOM   1523 C  CB   B SER A 1 151 ? -23.749 -17.319 10.527  0.50 12.93 ? 152 SER A CB   1 
ATOM   1524 O  OG   A SER A 1 151 ? -23.752 -16.479 11.113  0.50 17.34 ? 152 SER A OG   1 
ATOM   1525 O  OG   B SER A 1 151 ? -24.465 -18.492 10.842  0.50 15.74 ? 152 SER A OG   1 
ATOM   1526 N  N    . ALA A 1 152 ? -22.217 -16.170 7.829   1.00 10.64 ? 153 ALA A N    1 
ATOM   1527 C  CA   . ALA A 1 152 ? -21.772 -14.923 7.210   1.00 10.65 ? 153 ALA A CA   1 
ATOM   1528 C  C    . ALA A 1 152 ? -22.420 -13.703 7.929   1.00 11.80 ? 153 ALA A C    1 
ATOM   1529 O  O    . ALA A 1 152 ? -23.492 -13.777 8.429   1.00 13.01 ? 153 ALA A O    1 
ATOM   1530 C  CB   . ALA A 1 152 ? -22.173 -14.883 5.757   1.00 12.78 ? 153 ALA A CB   1 
ATOM   1531 N  N    . LYS A 1 153 ? -21.684 -12.575 7.879   1.00 10.79 ? 154 LYS A N    1 
ATOM   1532 C  CA   . LYS A 1 153 ? -22.237 -11.282 8.325   1.00 11.34 ? 154 LYS A CA   1 
ATOM   1533 C  C    . LYS A 1 153 ? -22.672 -10.518 7.071   1.00 10.91 ? 154 LYS A C    1 
ATOM   1534 O  O    . LYS A 1 153 ? -21.831 -10.087 6.312   1.00 10.94 ? 154 LYS A O    1 
ATOM   1535 C  CB   . LYS A 1 153 ? -21.226 -10.510 9.124   1.00 11.73 ? 154 LYS A CB   1 
ATOM   1536 C  CG   . LYS A 1 153 ? -21.755 -9.289  9.843   1.00 14.49 ? 154 LYS A CG   1 
ATOM   1537 C  CD   . LYS A 1 153 ? -22.600 -9.682  11.043  1.00 13.97 ? 154 LYS A CD   1 
ATOM   1538 C  CE   . LYS A 1 153 ? -22.669 -8.467  11.901  1.00 17.93 ? 154 LYS A CE   1 
ATOM   1539 N  NZ   . LYS A 1 153 ? -23.644 -8.868  12.827  1.00 19.03 ? 154 LYS A NZ   1 
ATOM   1540 N  N    A PRO A 1 154 ? -24.050 -10.456 6.907   0.50 10.94 ? 155 PRO A N    1 
ATOM   1541 N  N    B PRO A 1 154 ? -23.900 -10.450 6.712   0.50 12.70 ? 155 PRO A N    1 
ATOM   1542 C  CA   A PRO A 1 154 ? -24.599 -9.897  5.648   0.50 10.37 ? 155 PRO A CA   1 
ATOM   1543 C  CA   B PRO A 1 154 ? -24.153 -9.778  5.403   0.50 10.57 ? 155 PRO A CA   1 
ATOM   1544 C  C    A PRO A 1 154 ? -24.155 -8.486  5.504   0.50 8.71  ? 155 PRO A C    1 
ATOM   1545 C  C    B PRO A 1 154 ? -23.524 -8.377  5.190   0.50 9.74  ? 155 PRO A C    1 
ATOM   1546 O  O    A PRO A 1 154 ? -23.776 -8.070  4.387   0.50 9.55  ? 155 PRO A O    1 
ATOM   1547 O  O    B PRO A 1 154 ? -23.065 -8.052  4.041   0.50 9.97  ? 155 PRO A O    1 
ATOM   1548 C  CB   A PRO A 1 154 ? -26.126 -10.104 5.776   0.50 11.09 ? 155 PRO A CB   1 
ATOM   1549 C  CB   B PRO A 1 154 ? -25.668 -9.804  5.358   0.50 11.31 ? 155 PRO A CB   1 
ATOM   1550 C  CG   A PRO A 1 154 ? -26.317 -11.245 6.728   0.50 12.29 ? 155 PRO A CG   1 
ATOM   1551 C  CG   B PRO A 1 154 ? -26.056 -11.085 6.127   0.50 13.34 ? 155 PRO A CG   1 
ATOM   1552 C  CD   A PRO A 1 154 ? -25.170 -10.999 7.742   0.50 12.04 ? 155 PRO A CD   1 
ATOM   1553 C  CD   B PRO A 1 154 ? -25.128 -11.024 7.298   0.50 14.37 ? 155 PRO A CD   1 
ATOM   1554 N  N    A GLY A 1 155 ? -24.083 -7.747  6.578   0.50 7.15  ? 156 GLY A N    1 
ATOM   1555 N  N    B GLY A 1 155 ? -23.459 -7.579  6.252   0.50 7.92  ? 156 GLY A N    1 
ATOM   1556 C  CA   A GLY A 1 155 ? -23.668 -6.363  6.481   0.50 8.67  ? 156 GLY A CA   1 
ATOM   1557 C  CA   B GLY A 1 155 ? -22.962 -6.205  6.211   0.50 8.97  ? 156 GLY A CA   1 
ATOM   1558 C  C    A GLY A 1 155 ? -22.190 -6.134  6.251   0.50 7.52  ? 156 GLY A C    1 
ATOM   1559 C  C    B GLY A 1 155 ? -21.479 -6.045  6.002   0.50 9.00  ? 156 GLY A C    1 
ATOM   1560 O  O    A GLY A 1 155 ? -21.758 -4.989  6.030   0.50 10.18 ? 156 GLY A O    1 
ATOM   1561 O  O    B GLY A 1 155 ? -21.039 -4.966  5.781   0.50 10.35 ? 156 GLY A O    1 
ATOM   1562 N  N    A LEU A 1 156 ? -21.413 -7.207  6.346   0.50 6.54  ? 157 LEU A N    1 
ATOM   1563 N  N    B LEU A 1 156 ? -20.724 -7.133  6.049   0.50 7.32  ? 157 LEU A N    1 
ATOM   1564 C  CA   A LEU A 1 156 ? -19.995 -7.147  6.007   0.50 6.26  ? 157 LEU A CA   1 
ATOM   1565 C  CA   B LEU A 1 156 ? -19.308 -7.122  5.766   0.50 7.65  ? 157 LEU A CA   1 
ATOM   1566 C  C    A LEU A 1 156 ? -19.761 -7.358  4.540   0.50 5.99  ? 157 LEU A C    1 
ATOM   1567 C  C    B LEU A 1 156 ? -19.003 -7.318  4.271   0.50 8.32  ? 157 LEU A C    1 
ATOM   1568 O  O    A LEU A 1 156 ? -18.652 -7.051  4.035   0.50 6.47  ? 157 LEU A O    1 
ATOM   1569 O  O    B LEU A 1 156 ? -17.920 -6.996  3.793   0.50 7.47  ? 157 LEU A O    1 
ATOM   1570 C  CB   A LEU A 1 156 ? -19.217 -8.167  6.839   0.50 7.43  ? 157 LEU A CB   1 
ATOM   1571 C  CB   B LEU A 1 156 ? -18.580 -8.229  6.597   0.50 7.48  ? 157 LEU A CB   1 
ATOM   1572 C  CG   A LEU A 1 156 ? -17.687 -8.274  6.673   0.50 7.69  ? 157 LEU A CG   1 
ATOM   1573 C  CG   B LEU A 1 156 ? -17.025 -8.347  6.452   0.50 8.07  ? 157 LEU A CG   1 
ATOM   1574 C  CD1  A LEU A 1 156 ? -17.008 -6.919  7.081   0.50 9.04  ? 157 LEU A CD1  1 
ATOM   1575 C  CD1  B LEU A 1 156 ? -16.301 -7.041  6.777   0.50 8.23  ? 157 LEU A CD1  1 
ATOM   1576 C  CD2  A LEU A 1 156 ? -17.139 -9.427  7.454   0.50 7.82  ? 157 LEU A CD2  1 
ATOM   1577 C  CD2  B LEU A 1 156 ? -16.466 -9.481  7.323   0.50 8.33  ? 157 LEU A CD2  1 
ATOM   1578 N  N    A GLN A 1 157 ? -20.722 -7.899  3.812   0.50 6.70  ? 158 GLN A N    1 
ATOM   1579 N  N    B GLN A 1 157 ? -19.945 -7.888  3.528   0.50 8.11  ? 158 GLN A N    1 
ATOM   1580 C  CA   A GLN A 1 157 ? -20.436 -8.380  2.426   0.50 6.28  ? 158 GLN A CA   1 
ATOM   1581 C  CA   B GLN A 1 157 ? -19.618 -8.386  2.176   0.50 7.41  ? 158 GLN A CA   1 
ATOM   1582 C  C    A GLN A 1 157 ? -19.976 -7.246  1.508   0.50 6.46  ? 158 GLN A C    1 
ATOM   1583 C  C    B GLN A 1 157 ? -19.171 -7.233  1.269   0.50 7.40  ? 158 GLN A C    1 
ATOM   1584 O  O    A GLN A 1 157 ? -19.050 -7.431  0.638   0.50 6.60  ? 158 GLN A O    1 
ATOM   1585 O  O    B GLN A 1 157 ? -18.302 -7.444  0.424   0.50 8.14  ? 158 GLN A O    1 
ATOM   1586 C  CB   A GLN A 1 157 ? -21.590 -9.159  1.850   0.50 7.89  ? 158 GLN A CB   1 
ATOM   1587 C  CB   B GLN A 1 157 ? -20.789 -9.168  1.614   0.50 9.07  ? 158 GLN A CB   1 
ATOM   1588 C  CG   A GLN A 1 157 ? -21.266 -9.939  0.620   0.50 9.08  ? 158 GLN A CG   1 
ATOM   1589 C  CG   B GLN A 1 157 ? -20.404 -9.933  0.314   0.50 8.27  ? 158 GLN A CG   1 
ATOM   1590 C  CD   A GLN A 1 157 ? -20.106 -10.933 0.814   0.50 7.12  ? 158 GLN A CD   1 
ATOM   1591 C  CD   B GLN A 1 157 ? -19.292 -10.934 0.485   0.50 6.44  ? 158 GLN A CD   1 
ATOM   1592 O  OE1  A GLN A 1 157 ? -19.936 -11.512 1.911   0.50 8.14  ? 158 GLN A OE1  1 
ATOM   1593 O  OE1  B GLN A 1 157 ? -18.473 -11.211 -0.446  0.50 10.69 ? 158 GLN A OE1  1 
ATOM   1594 N  NE2  A GLN A 1 157 ? -19.341 -11.173 -0.269  0.50 10.05 ? 158 GLN A NE2  1 
ATOM   1595 N  NE2  B GLN A 1 157 ? -19.196 -11.485 1.638   0.50 6.88  ? 158 GLN A NE2  1 
ATOM   1596 N  N    A LYS A 1 158 ? -20.586 -6.060  1.658   0.50 6.73  ? 159 LYS A N    1 
ATOM   1597 N  N    B LYS A 1 158 ? -19.731 -6.030  1.415   0.50 7.99  ? 159 LYS A N    1 
ATOM   1598 C  CA   A LYS A 1 158 ? -20.153 -4.932  0.772   0.50 8.52  ? 159 LYS A CA   1 
ATOM   1599 C  CA   B LYS A 1 158 ? -19.342 -4.873  0.568   0.50 8.38  ? 159 LYS A CA   1 
ATOM   1600 C  C    A LYS A 1 158 ? -18.642 -4.639  0.928   0.50 7.60  ? 159 LYS A C    1 
ATOM   1601 C  C    B LYS A 1 158 ? -17.836 -4.593  0.698   0.50 7.76  ? 159 LYS A C    1 
ATOM   1602 O  O    A LYS A 1 158 ? -17.939 -4.294  -0.049  0.50 9.41  ? 159 LYS A O    1 
ATOM   1603 O  O    B LYS A 1 158 ? -17.171 -4.323  -0.282  0.50 9.52  ? 159 LYS A O    1 
ATOM   1604 C  CB   A LYS A 1 158 ? -20.986 -3.668  0.998   0.50 9.49  ? 159 LYS A CB   1 
ATOM   1605 C  CB   B LYS A 1 158 ? -20.158 -3.632  0.931   0.50 9.90  ? 159 LYS A CB   1 
ATOM   1606 C  CG   A LYS A 1 158 ? -20.411 -2.418  0.360   0.50 13.64 ? 159 LYS A CG   1 
ATOM   1607 C  CG   B LYS A 1 158 ? -21.582 -3.642  0.388   0.50 15.86 ? 159 LYS A CG   1 
ATOM   1608 C  CD   A LYS A 1 158 ? -21.287 -1.207  0.640   0.50 15.48 ? 159 LYS A CD   1 
ATOM   1609 C  CD   B LYS A 1 158 ? -21.601 -3.607  -1.134  0.50 21.93 ? 159 LYS A CD   1 
ATOM   1610 C  CE   A LYS A 1 158 ? -20.698 0.058   0.031   0.50 16.88 ? 159 LYS A CE   1 
ATOM   1611 C  CE   B LYS A 1 158 ? -23.025 -3.603  -1.673  0.50 20.56 ? 159 LYS A CE   1 
ATOM   1612 N  NZ   A LYS A 1 158 ? -21.582 1.236   0.248   0.50 16.70 ? 159 LYS A NZ   1 
ATOM   1613 N  NZ   B LYS A 1 158 ? -23.065 -3.815  -3.150  0.50 24.90 ? 159 LYS A NZ   1 
ATOM   1614 N  N    A VAL A 1 159 ? -18.115 -4.774  2.149   0.50 6.64  ? 160 VAL A N    1 
ATOM   1615 N  N    B VAL A 1 159 ? -17.347 -4.675  1.945   0.50 7.54  ? 160 VAL A N    1 
ATOM   1616 C  CA   A VAL A 1 159 ? -16.687 -4.575  2.397   0.50 7.07  ? 160 VAL A CA   1 
ATOM   1617 C  CA   B VAL A 1 159 ? -15.928 -4.535  2.224   0.50 7.34  ? 160 VAL A CA   1 
ATOM   1618 C  C    A VAL A 1 159 ? -15.874 -5.663  1.717   0.50 6.66  ? 160 VAL A C    1 
ATOM   1619 C  C    B VAL A 1 159 ? -15.131 -5.672  1.533   0.50 6.73  ? 160 VAL A C    1 
ATOM   1620 O  O    A VAL A 1 159 ? -14.938 -5.400  1.008   0.50 7.48  ? 160 VAL A O    1 
ATOM   1621 O  O    B VAL A 1 159 ? -14.184 -5.439  0.754   0.50 8.12  ? 160 VAL A O    1 
ATOM   1622 C  CB   A VAL A 1 159 ? -16.398 -4.524  3.926   0.50 7.35  ? 160 VAL A CB   1 
ATOM   1623 C  CB   B VAL A 1 159 ? -15.669 -4.538  3.731   0.50 7.69  ? 160 VAL A CB   1 
ATOM   1624 C  CG1  A VAL A 1 159 ? -14.844 -4.516  4.188   0.50 8.09  ? 160 VAL A CG1  1 
ATOM   1625 C  CG1  B VAL A 1 159 ? -14.143 -4.754  3.993   0.50 9.76  ? 160 VAL A CG1  1 
ATOM   1626 C  CG2  A VAL A 1 159 ? -17.120 -3.364  4.582   0.50 8.44  ? 160 VAL A CG2  1 
ATOM   1627 C  CG2  B VAL A 1 159 ? -16.309 -3.341  4.391   0.50 8.53  ? 160 VAL A CG2  1 
ATOM   1628 N  N    A VAL A 1 160 ? -16.267 -6.917  1.930   0.50 6.36  ? 161 VAL A N    1 
ATOM   1629 N  N    B VAL A 1 160 ? -15.516 -6.934  1.786   0.50 6.76  ? 161 VAL A N    1 
ATOM   1630 C  CA   A VAL A 1 160 ? -15.539 -8.046  1.345   0.50 8.18  ? 161 VAL A CA   1 
ATOM   1631 C  CA   B VAL A 1 160 ? -14.781 -8.042  1.230   0.50 7.50  ? 161 VAL A CA   1 
ATOM   1632 C  C    A VAL A 1 160 ? -15.479 -7.924  -0.159  0.50 7.16  ? 161 VAL A C    1 
ATOM   1633 C  C    B VAL A 1 160 ? -14.666 -8.002  -0.262  0.50 7.62  ? 161 VAL A C    1 
ATOM   1634 O  O    A VAL A 1 160 ? -14.412 -8.178  -0.785  0.50 8.40  ? 161 VAL A O    1 
ATOM   1635 O  O    B VAL A 1 160 ? -13.616 -8.283  -0.814  0.50 8.40  ? 161 VAL A O    1 
ATOM   1636 C  CB   A VAL A 1 160 ? -16.273 -9.423  1.696   0.50 8.72  ? 161 VAL A CB   1 
ATOM   1637 C  CB   B VAL A 1 160 ? -15.369 -9.411  1.820   0.50 11.08 ? 161 VAL A CB   1 
ATOM   1638 C  CG1  A VAL A 1 160 ? -15.898 -10.564 0.868   0.50 10.77 ? 161 VAL A CG1  1 
ATOM   1639 C  CG1  B VAL A 1 160 ? -15.011 -10.643 0.848   0.50 11.71 ? 161 VAL A CG1  1 
ATOM   1640 C  CG2  A VAL A 1 160 ? -15.981 -9.631  3.204   0.50 8.19  ? 161 VAL A CG2  1 
ATOM   1641 C  CG2  B VAL A 1 160 ? -14.886 -9.489  3.294   0.50 14.64 ? 161 VAL A CG2  1 
ATOM   1642 N  N    A ASP A 1 161 ? -16.593 -7.521  -0.802  0.50 8.03  ? 162 ASP A N    1 
ATOM   1643 N  N    B ASP A 1 161 ? -15.722 -7.600  -0.939  0.50 8.18  ? 162 ASP A N    1 
ATOM   1644 C  CA   A ASP A 1 161 ? -16.611 -7.491  -2.272  0.50 8.44  ? 162 ASP A CA   1 
ATOM   1645 C  CA   B ASP A 1 161 ? -15.708 -7.656  -2.397  0.50 9.61  ? 162 ASP A CA   1 
ATOM   1646 C  C    A ASP A 1 161 ? -15.774 -6.359  -2.902  0.50 9.63  ? 162 ASP A C    1 
ATOM   1647 C  C    B ASP A 1 161 ? -14.849 -6.572  -3.033  0.50 10.71 ? 162 ASP A C    1 
ATOM   1648 O  O    A ASP A 1 161 ? -15.503 -6.401  -4.110  0.50 13.20 ? 162 ASP A O    1 
ATOM   1649 O  O    B ASP A 1 161 ? -14.530 -6.758  -4.178  0.50 13.66 ? 162 ASP A O    1 
ATOM   1650 C  CB   A ASP A 1 161 ? -18.057 -7.399  -2.698  0.50 10.52 ? 162 ASP A CB   1 
ATOM   1651 C  CB   B ASP A 1 161 ? -17.127 -7.550  -2.907  0.50 10.99 ? 162 ASP A CB   1 
ATOM   1652 C  CG   A ASP A 1 161 ? -18.762 -8.732  -2.618  0.50 11.93 ? 162 ASP A CG   1 
ATOM   1653 C  CG   B ASP A 1 161 ? -17.862 -8.885  -2.809  0.50 9.80  ? 162 ASP A CG   1 
ATOM   1654 O  OD1  A ASP A 1 161 ? -18.108 -9.810  -2.629  0.50 14.20 ? 162 ASP A OD1  1 
ATOM   1655 O  OD1  B ASP A 1 161 ? -17.227 -9.987  -2.882  0.50 12.66 ? 162 ASP A OD1  1 
ATOM   1656 O  OD2  A ASP A 1 161 ? -20.009 -8.708  -2.485  0.50 14.90 ? 162 ASP A OD2  1 
ATOM   1657 O  OD2  B ASP A 1 161 ? -19.080 -8.908  -2.667  0.50 11.90 ? 162 ASP A OD2  1 
ATOM   1658 N  N    A VAL A 1 162 ? -15.349 -5.348  -2.135  0.50 7.68  ? 163 VAL A N    1 
ATOM   1659 N  N    B VAL A 1 162 ? -14.477 -5.470  -2.338  0.50 9.45  ? 163 VAL A N    1 
ATOM   1660 C  CA   A VAL A 1 162 ? -14.475 -4.315  -2.684  0.50 7.25  ? 163 VAL A CA   1 
ATOM   1661 C  CA   B VAL A 1 162 ? -13.553 -4.441  -2.903  0.50 10.42 ? 163 VAL A CA   1 
ATOM   1662 C  C    A VAL A 1 162 ? -12.976 -4.644  -2.520  0.50 7.62  ? 163 VAL A C    1 
ATOM   1663 C  C    B VAL A 1 162 ? -12.055 -4.780  -2.650  0.50 8.64  ? 163 VAL A C    1 
ATOM   1664 O  O    A VAL A 1 162 ? -12.149 -3.968  -3.126  0.50 7.99  ? 163 VAL A O    1 
ATOM   1665 O  O    B VAL A 1 162 ? -11.168 -4.116  -3.199  0.50 10.07 ? 163 VAL A O    1 
ATOM   1666 C  CB   A VAL A 1 162 ? -14.849 -2.922  -2.092  0.50 9.38  ? 163 VAL A CB   1 
ATOM   1667 C  CB   B VAL A 1 162 ? -13.842 -2.947  -2.295  0.50 11.95 ? 163 VAL A CB   1 
ATOM   1668 C  CG1  A VAL A 1 162 ? -14.304 -2.727  -0.726  0.50 8.49  ? 163 VAL A CG1  1 
ATOM   1669 C  CG1  B VAL A 1 162 ? -13.340 -2.769  -0.925  0.50 11.15 ? 163 VAL A CG1  1 
ATOM   1670 C  CG2  A VAL A 1 162 ? -14.397 -1.743  -2.963  0.50 10.43 ? 163 VAL A CG2  1 
ATOM   1671 C  CG2  B VAL A 1 162 ? -13.464 -1.778  -3.121  0.50 15.00 ? 163 VAL A CG2  1 
ATOM   1672 N  N    A LEU A 1 163 ? -12.618 -5.646  -1.733  0.50 7.77  ? 164 LEU A N    1 
ATOM   1673 N  N    B LEU A 1 163 ? -11.797 -5.797  -1.831  0.50 8.79  ? 164 LEU A N    1 
ATOM   1674 C  CA   A LEU A 1 163 ? -11.235 -5.895  -1.429  0.50 7.74  ? 164 LEU A CA   1 
ATOM   1675 C  CA   B LEU A 1 163 ? -10.411 -6.005  -1.457  0.50 8.37  ? 164 LEU A CA   1 
ATOM   1676 C  C    A LEU A 1 163 ? -10.414 -6.243  -2.664  0.50 7.88  ? 164 LEU A C    1 
ATOM   1677 C  C    B LEU A 1 163 ? -9.481  -6.365  -2.619  0.50 8.95  ? 164 LEU A C    1 
ATOM   1678 O  O    A LEU A 1 163 ? -9.213  -5.939  -2.701  0.50 7.68  ? 164 LEU A O    1 
ATOM   1679 O  O    B LEU A 1 163 ? -8.307  -6.051  -2.589  0.50 9.23  ? 164 LEU A O    1 
ATOM   1680 C  CB   A LEU A 1 163 ? -11.109 -6.959  -0.352  0.50 7.56  ? 164 LEU A CB   1 
ATOM   1681 C  CB   B LEU A 1 163 ? -10.372 -7.077  -0.373  0.50 7.84  ? 164 LEU A CB   1 
ATOM   1682 C  CG   A LEU A 1 163 ? -11.754 -6.596  1.016   0.50 6.86  ? 164 LEU A CG   1 
ATOM   1683 C  CG   B LEU A 1 163 ? -11.018 -6.681  0.965   0.50 7.56  ? 164 LEU A CG   1 
ATOM   1684 C  CD1  A LEU A 1 163 ? -11.559 -7.699  2.091   0.50 7.98  ? 164 LEU A CD1  1 
ATOM   1685 C  CD1  B LEU A 1 163 ? -10.824 -7.846  1.967   0.50 9.37  ? 164 LEU A CD1  1 
ATOM   1686 C  CD2  A LEU A 1 163 ? -11.218 -5.291  1.610   0.50 8.51  ? 164 LEU A CD2  1 
ATOM   1687 C  CD2  B LEU A 1 163 ? -10.461 -5.351  1.536   0.50 9.10  ? 164 LEU A CD2  1 
ATOM   1688 N  N    A ASP A 1 164 ? -11.013 -6.892  -3.652  0.50 8.45  ? 165 ASP A N    1 
ATOM   1689 N  N    B ASP A 1 164 ? -10.009 -7.016  -3.658  0.50 10.19 ? 165 ASP A N    1 
ATOM   1690 C  CA   A ASP A 1 164 ? -10.231 -7.209  -4.879  0.50 10.30 ? 165 ASP A CA   1 
ATOM   1691 C  CA   B ASP A 1 164 ? -9.165  -7.338  -4.835  0.50 11.32 ? 165 ASP A CA   1 
ATOM   1692 C  C    A ASP A 1 164 ? -9.732  -5.964  -5.547  0.50 9.02  ? 165 ASP A C    1 
ATOM   1693 C  C    B ASP A 1 164 ? -8.653  -6.047  -5.524  0.50 11.01 ? 165 ASP A C    1 
ATOM   1694 O  O    A ASP A 1 164 ? -8.743  -6.105  -6.363  0.50 12.14 ? 165 ASP A O    1 
ATOM   1695 O  O    B ASP A 1 164 ? -7.589  -6.100  -6.129  0.50 14.77 ? 165 ASP A O    1 
ATOM   1696 C  CB   A ASP A 1 164 ? -11.054 -8.089  -5.772  0.50 11.58 ? 165 ASP A CB   1 
ATOM   1697 C  CB   B ASP A 1 164 ? -9.882  -8.293  -5.814  0.50 13.03 ? 165 ASP A CB   1 
ATOM   1698 C  CG   A ASP A 1 164 ? -12.065 -7.293  -6.621  0.50 18.39 ? 165 ASP A CG   1 
ATOM   1699 C  CG   B ASP A 1 164 ? -10.953 -7.585  -6.569  0.50 15.18 ? 165 ASP A CG   1 
ATOM   1700 O  OD1  A ASP A 1 164 ? -12.996 -6.717  -6.009  0.50 21.75 ? 165 ASP A OD1  1 
ATOM   1701 O  OD1  B ASP A 1 164 ? -11.972 -7.229  -5.941  0.50 17.35 ? 165 ASP A OD1  1 
ATOM   1702 O  OD2  A ASP A 1 164 ? -11.914 -7.227  -7.898  0.50 21.16 ? 165 ASP A OD2  1 
ATOM   1703 O  OD2  B ASP A 1 164 ? -10.758 -7.225  -7.758  0.50 22.58 ? 165 ASP A OD2  1 
ATOM   1704 N  N    A SER A 1 165 ? -10.375 -4.800  -5.305  0.50 9.46  ? 166 SER A N    1 
ATOM   1705 N  N    B SER A 1 165 ? -9.340  -4.926  -5.349  0.50 10.28 ? 166 SER A N    1 
ATOM   1706 C  CA   A SER A 1 165 ? -9.940  -3.582  -5.936  0.50 9.08  ? 166 SER A CA   1 
ATOM   1707 C  CA   B SER A 1 165 ? -8.916  -3.675  -5.971  0.50 10.35 ? 166 SER A CA   1 
ATOM   1708 C  C    A SER A 1 165 ? -8.824  -2.809  -5.169  0.50 7.98  ? 166 SER A C    1 
ATOM   1709 C  C    B SER A 1 165 ? -7.801  -2.969  -5.176  0.50 9.32  ? 166 SER A C    1 
ATOM   1710 O  O    A SER A 1 165 ? -8.300  -1.803  -5.645  0.50 8.30  ? 166 SER A O    1 
ATOM   1711 O  O    B SER A 1 165 ? -7.213  -1.958  -5.628  0.50 10.26 ? 166 SER A O    1 
ATOM   1712 C  CB   A SER A 1 165 ? -11.118 -2.695  -6.274  0.50 11.29 ? 166 SER A CB   1 
ATOM   1713 C  CB   B SER A 1 165 ? -10.120 -2.747  -6.182  0.50 11.39 ? 166 SER A CB   1 
ATOM   1714 O  OG   A SER A 1 165 ? -11.617 -2.149  -5.110  0.50 11.30 ? 166 SER A OG   1 
ATOM   1715 O  OG   B SER A 1 165 ? -10.501 -2.152  -4.962  0.50 11.78 ? 166 SER A OG   1 
ATOM   1716 N  N    A ILE A 1 166 ? -8.498  -3.274  -3.976  0.50 7.13  ? 167 ILE A N    1 
ATOM   1717 N  N    B ILE A 1 166 ? -7.544  -3.461  -3.964  0.50 8.99  ? 167 ILE A N    1 
ATOM   1718 C  CA   A ILE A 1 166 ? -7.448  -2.657  -3.101  0.50 6.59  ? 167 ILE A CA   1 
ATOM   1719 C  CA   B ILE A 1 166 ? -6.547  -2.815  -3.094  0.50 8.85  ? 167 ILE A CA   1 
ATOM   1720 C  C    A ILE A 1 166 ? -6.446  -3.700  -2.609  0.50 5.90  ? 167 ILE A C    1 
ATOM   1721 C  C    B ILE A 1 166 ? -5.563  -3.891  -2.566  0.50 8.85  ? 167 ILE A C    1 
ATOM   1722 O  O    A ILE A 1 166 ? -6.071  -3.702  -1.468  0.50 5.87  ? 167 ILE A O    1 
ATOM   1723 O  O    B ILE A 1 166 ? -5.193  -3.895  -1.364  0.50 8.55  ? 167 ILE A O    1 
ATOM   1724 C  CB   A ILE A 1 166 ? -8.107  -1.826  -1.945  0.50 6.53  ? 167 ILE A CB   1 
ATOM   1725 C  CB   B ILE A 1 166 ? -7.164  -1.958  -1.932  0.50 8.08  ? 167 ILE A CB   1 
ATOM   1726 C  CG1  A ILE A 1 166 ? -8.995  -2.663  -1.020  0.50 5.87  ? 167 ILE A CG1  1 
ATOM   1727 C  CG1  B ILE A 1 166 ? -8.090  -2.784  -1.014  0.50 7.68  ? 167 ILE A CG1  1 
ATOM   1728 C  CG2  A ILE A 1 166 ? -8.800  -0.557  -2.552  0.50 8.05  ? 167 ILE A CG2  1 
ATOM   1729 C  CG2  B ILE A 1 166 ? -7.887  -0.774  -2.553  0.50 9.80  ? 167 ILE A CG2  1 
ATOM   1730 C  CD1  A ILE A 1 166 ? -9.024  -2.097  0.304   0.50 7.60  ? 167 ILE A CD1  1 
ATOM   1731 C  CD1  B ILE A 1 166 ? -8.216  -2.153  0.415   0.50 8.21  ? 167 ILE A CD1  1 
ATOM   1732 N  N    A LYS A 1 167 ? -6.056  -4.607  -3.508  0.50 6.57  ? 168 LYS A N    1 
ATOM   1733 N  N    B LYS A 1 167 ? -5.123  -4.796  -3.457  0.50 10.01 ? 168 LYS A N    1 
ATOM   1734 C  CA   A LYS A 1 167 ? -5.256  -5.755  -3.077  0.50 6.43  ? 168 LYS A CA   1 
ATOM   1735 C  CA   B LYS A 1 167 ? -4.392  -5.973  -3.004  0.50 10.59 ? 168 LYS A CA   1 
ATOM   1736 C  C    A LYS A 1 167 ? -3.956  -5.376  -2.388  0.50 6.28  ? 168 LYS A C    1 
ATOM   1737 C  C    B LYS A 1 167 ? -3.082  -5.628  -2.269  0.50 8.91  ? 168 LYS A C    1 
ATOM   1738 O  O    A LYS A 1 167 ? -3.548  -5.998  -1.443  0.50 6.07  ? 168 LYS A O    1 
ATOM   1739 O  O    B LYS A 1 167 ? -2.729  -6.259  -1.309  0.50 9.06  ? 168 LYS A O    1 
ATOM   1740 C  CB   A LYS A 1 167 ? -4.946  -6.692  -4.251  0.50 7.61  ? 168 LYS A CB   1 
ATOM   1741 C  CB   B LYS A 1 167 ? -4.047  -6.885  -4.183  0.50 10.43 ? 168 LYS A CB   1 
ATOM   1742 C  CG   A LYS A 1 167 ? -4.195  -7.916  -3.911  0.50 9.19  ? 168 LYS A CG   1 
ATOM   1743 C  CG   B LYS A 1 167 ? -3.491  -8.230  -3.640  0.50 11.16 ? 168 LYS A CG   1 
ATOM   1744 C  CD   A LYS A 1 167 ? -4.049  -8.825  -5.201  0.50 12.84 ? 168 LYS A CD   1 
ATOM   1745 C  CD   B LYS A 1 167 ? -3.382  -9.285  -4.711  0.50 13.73 ? 168 LYS A CD   1 
ATOM   1746 C  CE   A LYS A 1 167 ? -3.331  -10.202 -4.920  0.50 17.72 ? 168 LYS A CE   1 
ATOM   1747 C  CE   B LYS A 1 167 ? -2.451  -8.885  -5.625  0.50 17.43 ? 168 LYS A CE   1 
ATOM   1748 N  NZ   A LYS A 1 167 ? -3.003  -11.012 -6.187  0.50 16.83 ? 168 LYS A NZ   1 
ATOM   1749 N  NZ   B LYS A 1 167 ? -2.322  -9.826  -6.747  0.50 21.81 ? 168 LYS A NZ   1 
ATOM   1750 N  N    A THR A 1 168 ? -3.306  -4.320  -2.900  0.50 6.33  ? 169 THR A N    1 
ATOM   1751 N  N    B THR A 1 168 ? -2.366  -4.605  -2.771  0.50 9.86  ? 169 THR A N    1 
ATOM   1752 C  CA   A THR A 1 168 ? -1.935  -3.999  -2.523  0.50 7.09  ? 169 THR A CA   1 
ATOM   1753 C  CA   B THR A 1 168 ? -1.027  -4.348  -2.336  0.50 10.19 ? 169 THR A CA   1 
ATOM   1754 C  C    A THR A 1 168 ? -1.834  -2.635  -1.866  0.50 6.23  ? 169 THR A C    1 
ATOM   1755 C  C    B THR A 1 168 ? -0.884  -2.974  -1.695  0.50 9.30  ? 169 THR A C    1 
ATOM   1756 O  O    A THR A 1 168 ? -2.697  -1.761  -2.036  0.50 6.48  ? 169 THR A O    1 
ATOM   1757 O  O    B THR A 1 168 ? -1.724  -2.097  -1.871  0.50 9.22  ? 169 THR A O    1 
ATOM   1758 C  CB   A THR A 1 168 ? -0.975  -4.044  -3.803  0.50 8.04  ? 169 THR A CB   1 
ATOM   1759 C  CB   B THR A 1 168 ? -0.047  -4.449  -3.539  0.50 10.31 ? 169 THR A CB   1 
ATOM   1760 O  OG1  A THR A 1 168 ? -1.540  -3.268  -4.874  0.50 8.00  ? 169 THR A OG1  1 
ATOM   1761 O  OG1  B THR A 1 168 ? -0.548  -3.681  -4.660  0.50 12.24 ? 169 THR A OG1  1 
ATOM   1762 C  CG2  A THR A 1 168 ? -0.789  -5.498  -4.270  0.50 8.29  ? 169 THR A CG2  1 
ATOM   1763 C  CG2  B THR A 1 168 ? 0.235   -5.808  -4.007  0.50 12.27 ? 169 THR A CG2  1 
ATOM   1764 N  N    A LYS A 1 169 ? -0.752  -2.459  -1.141  0.50 7.37  ? 170 LYS A N    1 
ATOM   1765 N  N    B LYS A 1 169 ? 0.162   -2.845  -0.879  0.50 9.42  ? 170 LYS A N    1 
ATOM   1766 C  CA   A LYS A 1 169 ? -0.464  -1.263  -0.364  0.50 6.81  ? 170 LYS A CA   1 
ATOM   1767 C  CA   B LYS A 1 169 ? 0.435   -1.606  -0.125  0.50 9.67  ? 170 LYS A CA   1 
ATOM   1768 C  C    A LYS A 1 169 ? -0.559  -0.013  -1.173  0.50 6.99  ? 170 LYS A C    1 
ATOM   1769 C  C    B LYS A 1 169 ? 0.393   -0.420  -1.049  0.50 10.01 ? 170 LYS A C    1 
ATOM   1770 O  O    A LYS A 1 169 ? 0.067   0.109   -2.307  0.50 7.90  ? 170 LYS A O    1 
ATOM   1771 O  O    B LYS A 1 169 ? 1.105   -0.361  -2.068  0.50 11.84 ? 170 LYS A O    1 
ATOM   1772 C  CB   A LYS A 1 169 ? 0.939   -1.392  0.191   0.50 7.00  ? 170 LYS A CB   1 
ATOM   1773 C  CB   B LYS A 1 169 ? 1.818   -1.672  0.524   0.50 9.77  ? 170 LYS A CB   1 
ATOM   1774 C  CG   A LYS A 1 169 ? 1.411   -0.206  1.018   0.50 8.75  ? 170 LYS A CG   1 
ATOM   1775 C  CG   B LYS A 1 169 ? 2.261   -0.468  1.292   0.50 11.19 ? 170 LYS A CG   1 
ATOM   1776 C  CD   A LYS A 1 169 ? 2.715   -0.493  1.680   0.50 9.95  ? 170 LYS A CD   1 
ATOM   1777 C  CD   B LYS A 1 169 ? 3.623   -0.699  2.007   0.50 11.61 ? 170 LYS A CD   1 
ATOM   1778 C  CE   A LYS A 1 169 ? 3.840   -1.054  0.756   0.50 15.25 ? 170 LYS A CE   1 
ATOM   1779 C  CE   B LYS A 1 169 ? 4.810   -0.666  1.123   0.50 19.21 ? 170 LYS A CE   1 
ATOM   1780 N  NZ   A LYS A 1 169 ? 5.020   -1.577  1.522   0.50 20.10 ? 170 LYS A NZ   1 
ATOM   1781 N  NZ   B LYS A 1 169 ? 6.001   -1.226  1.766   0.50 23.61 ? 170 LYS A NZ   1 
ATOM   1782 N  N    A GLY A 1 170 ? -1.319  0.964   -0.664  0.50 7.12  ? 171 GLY A N    1 
ATOM   1783 N  N    B GLY A 1 170 ? -0.325  0.610   -0.619  0.50 8.32  ? 171 GLY A N    1 
ATOM   1784 C  CA   A GLY A 1 170 ? -1.453  2.230   -1.299  0.50 7.28  ? 171 GLY A CA   1 
ATOM   1785 C  CA   B GLY A 1 170 ? -0.411  1.848   -1.352  0.50 9.42  ? 171 GLY A CA   1 
ATOM   1786 C  C    A GLY A 1 170 ? -2.653  2.340   -2.196  0.50 8.74  ? 171 GLY A C    1 
ATOM   1787 C  C    B GLY A 1 170 ? -1.632  2.005   -2.253  0.50 8.91  ? 171 GLY A C    1 
ATOM   1788 O  O    A GLY A 1 170 ? -2.980  3.478   -2.668  0.50 11.06 ? 171 GLY A O    1 
ATOM   1789 O  O    B GLY A 1 170 ? -1.904  3.115   -2.705  0.50 12.38 ? 171 GLY A O    1 
ATOM   1790 N  N    A LYS A 1 171 ? -3.332  1.243   -2.528  0.50 6.69  ? 172 LYS A N    1 
ATOM   1791 N  N    B LYS A 1 171 ? -2.344  0.920   -2.502  0.50 8.44  ? 172 LYS A N    1 
ATOM   1792 C  CA   A LYS A 1 171 ? -4.540  1.298   -3.335  0.50 7.19  ? 172 LYS A CA   1 
ATOM   1793 C  CA   B LYS A 1 171 ? -3.530  1.017   -3.290  0.50 9.04  ? 172 LYS A CA   1 
ATOM   1794 C  C    A LYS A 1 171 ? -5.734  1.719   -2.477  0.50 6.10  ? 172 LYS A C    1 
ATOM   1795 C  C    B LYS A 1 171 ? -4.701  1.509   -2.474  0.50 8.35  ? 172 LYS A C    1 
ATOM   1796 O  O    A LYS A 1 171 ? -5.908  1.305   -1.359  0.50 6.25  ? 172 LYS A O    1 
ATOM   1797 O  O    B LYS A 1 171 ? -4.885  1.070   -1.277  0.50 9.75  ? 172 LYS A O    1 
ATOM   1798 C  CB   A LYS A 1 171 ? -4.795  -0.034  -3.978  0.50 7.62  ? 172 LYS A CB   1 
ATOM   1799 C  CB   B LYS A 1 171 ? -3.853  -0.354  -3.872  0.50 9.74  ? 172 LYS A CB   1 
ATOM   1800 C  CG   A LYS A 1 171 ? -3.829  -0.406  -5.079  0.50 9.40  ? 172 LYS A CG   1 
ATOM   1801 C  CG   B LYS A 1 171 ? -2.776  -0.730  -4.934  0.50 14.21 ? 172 LYS A CG   1 
ATOM   1802 C  CD   A LYS A 1 171 ? -4.339  -1.555  -5.994  0.50 11.66 ? 172 LYS A CD   1 
ATOM   1803 C  CD   B LYS A 1 171 ? -3.252  -1.879  -5.874  0.50 14.50 ? 172 LYS A CD   1 
ATOM   1804 C  CE   A LYS A 1 171 ? -5.412  -1.130  -7.027  0.50 13.89 ? 172 LYS A CE   1 
ATOM   1805 C  CE   B LYS A 1 171 ? -4.079  -1.283  -6.940  0.50 17.61 ? 172 LYS A CE   1 
ATOM   1806 N  NZ   A LYS A 1 171 ? -5.922  -2.179  -8.025  0.50 16.44 ? 172 LYS A NZ   1 
ATOM   1807 N  NZ   B LYS A 1 171 ? -3.291  -0.744  -7.965  0.50 24.09 ? 172 LYS A NZ   1 
ATOM   1808 N  N    A SER A 1 172 ? -6.603  2.490   -3.102  0.50 7.02  ? 173 SER A N    1 
ATOM   1809 N  N    B SER A 1 172 ? -5.514  2.379   -3.069  0.50 8.29  ? 173 SER A N    1 
ATOM   1810 C  CA   A SER A 1 172 ? -7.848  2.949   -2.513  0.50 7.69  ? 173 SER A CA   1 
ATOM   1811 C  CA   B SER A 1 172 ? -6.733  2.850   -2.447  0.50 7.64  ? 173 SER A CA   1 
ATOM   1812 C  C    A SER A 1 172 ? -8.984  2.782   -3.497  0.50 7.84  ? 173 SER A C    1 
ATOM   1813 C  C    B SER A 1 172 ? -7.841  2.913   -3.448  0.50 9.00  ? 173 SER A C    1 
ATOM   1814 O  O    A SER A 1 172 ? -8.766  2.743   -4.729  0.50 9.03  ? 173 SER A O    1 
ATOM   1815 O  O    B SER A 1 172 ? -7.590  2.845   -4.700  0.50 11.54 ? 173 SER A O    1 
ATOM   1816 C  CB   A SER A 1 172 ? -7.733  4.393   -1.988  0.50 7.90  ? 173 SER A CB   1 
ATOM   1817 C  CB   B SER A 1 172 ? -6.544  4.172   -1.835  0.50 9.77  ? 173 SER A CB   1 
ATOM   1818 O  OG   A SER A 1 172 ? -7.613  5.339   -3.025  0.50 11.09 ? 173 SER A OG   1 
ATOM   1819 O  OG   B SER A 1 172 ? -6.348  5.256   -2.783  0.50 12.00 ? 173 SER A OG   1 
ATOM   1820 N  N    A ALA A 1 173 ? -10.216 2.761   -2.988  0.50 7.90  ? 174 ALA A N    1 
ATOM   1821 N  N    B ALA A 1 173 ? -9.067  3.056   -2.997  0.50 9.32  ? 174 ALA A N    1 
ATOM   1822 C  CA   A ALA A 1 173 ? -11.432 2.777   -3.786  0.50 8.40  ? 174 ALA A CA   1 
ATOM   1823 C  CA   B ALA A 1 173 ? -10.264 3.167   -3.845  0.50 10.55 ? 174 ALA A CA   1 
ATOM   1824 C  C    A ALA A 1 173 ? -12.512 3.623   -3.177  0.50 7.72  ? 174 ALA A C    1 
ATOM   1825 C  C    B ALA A 1 173 ? -11.306 4.038   -3.158  0.50 8.94  ? 174 ALA A C    1 
ATOM   1826 O  O    A ALA A 1 173 ? -12.622 3.659   -1.938  0.50 6.54  ? 174 ALA A O    1 
ATOM   1827 O  O    B ALA A 1 173 ? -11.415 4.036   -1.918  0.50 9.37  ? 174 ALA A O    1 
ATOM   1828 C  CB   A ALA A 1 173 ? -11.964 1.324   -4.015  0.50 11.20 ? 174 ALA A CB   1 
ATOM   1829 C  CB   B ALA A 1 173 ? -10.884 1.749   -4.151  0.50 11.28 ? 174 ALA A CB   1 
ATOM   1830 N  N    A ASP A 1 174 ? -13.377 4.197   -4.016  0.50 7.98  ? 175 ASP A N    1 
ATOM   1831 N  N    B ASP A 1 174 ? -12.124 4.704   -3.962  0.50 9.36  ? 175 ASP A N    1 
ATOM   1832 C  CA   A ASP A 1 174 ? -14.533 4.918   -3.489  0.50 7.71  ? 175 ASP A CA   1 
ATOM   1833 C  CA   B ASP A 1 174 ? -13.354 5.306   -3.417  0.50 9.69  ? 175 ASP A CA   1 
ATOM   1834 C  C    A ASP A 1 174 ? -15.402 3.894   -2.742  0.50 7.67  ? 175 ASP A C    1 
ATOM   1835 C  C    B ASP A 1 174 ? -14.276 4.279   -2.767  0.50 9.54  ? 175 ASP A C    1 
ATOM   1836 O  O    A ASP A 1 174 ? -15.550 2.729   -3.168  0.50 8.50  ? 175 ASP A O    1 
ATOM   1837 O  O    B ASP A 1 174 ? -14.378 3.180   -3.242  0.50 10.60 ? 175 ASP A O    1 
ATOM   1838 C  CB   A ASP A 1 174 ? -15.316 5.373   -4.767  0.50 11.13 ? 175 ASP A CB   1 
ATOM   1839 C  CB   B ASP A 1 174 ? -14.127 6.174   -4.413  0.50 11.89 ? 175 ASP A CB   1 
ATOM   1840 C  CG   A ASP A 1 174 ? -14.647 6.590   -5.445  0.50 14.17 ? 175 ASP A CG   1 
ATOM   1841 C  CG   B ASP A 1 174 ? -13.275 7.159   -5.104  0.50 12.96 ? 175 ASP A CG   1 
ATOM   1842 O  OD1  A ASP A 1 174 ? -14.219 7.584   -4.726  0.50 19.83 ? 175 ASP A OD1  1 
ATOM   1843 O  OD1  B ASP A 1 174 ? -13.281 8.351   -4.681  0.50 26.26 ? 175 ASP A OD1  1 
ATOM   1844 O  OD2  A ASP A 1 174 ? -14.704 6.638   -6.732  0.50 14.04 ? 175 ASP A OD2  1 
ATOM   1845 O  OD2  B ASP A 1 174 ? -12.604 6.838   -6.104  0.50 29.57 ? 175 ASP A OD2  1 
ATOM   1846 N  N    A PHE A 1 175 ? -15.999 4.346   -1.647  0.50 6.76  ? 176 PHE A N    1 
ATOM   1847 N  N    B PHE A 1 175 ? -14.893 4.626   -1.643  0.50 8.77  ? 176 PHE A N    1 
ATOM   1848 C  CA   A PHE A 1 175 ? -16.784 3.448   -0.782  0.50 7.53  ? 176 PHE A CA   1 
ATOM   1849 C  CA   B PHE A 1 175 ? -15.710 3.627   -0.951  0.50 9.80  ? 176 PHE A CA   1 
ATOM   1850 C  C    A PHE A 1 175 ? -17.797 4.251   0.001   0.50 7.37  ? 176 PHE A C    1 
ATOM   1851 C  C    B PHE A 1 175 ? -16.811 4.347   -0.132  0.50 8.83  ? 176 PHE A C    1 
ATOM   1852 O  O    A PHE A 1 175 ? -17.636 4.497   1.186   0.50 8.86  ? 176 PHE A O    1 
ATOM   1853 O  O    B PHE A 1 175 ? -16.635 4.672   1.034   0.50 10.09 ? 176 PHE A O    1 
ATOM   1854 C  CB   A PHE A 1 175 ? -15.858 2.667   0.124   0.50 8.78  ? 176 PHE A CB   1 
ATOM   1855 C  CB   B PHE A 1 175 ? -14.815 2.787   -0.002  0.50 9.88  ? 176 PHE A CB   1 
ATOM   1856 C  CG   A PHE A 1 175 ? -16.501 1.395   0.637   0.50 6.07  ? 176 PHE A CG   1 
ATOM   1857 C  CG   B PHE A 1 175 ? -15.466 1.524   0.562   0.50 9.22  ? 176 PHE A CG   1 
ATOM   1858 C  CD1  A PHE A 1 175 ? -16.804 0.350   -0.198  0.50 10.34 ? 176 PHE A CD1  1 
ATOM   1859 C  CD1  B PHE A 1 175 ? -15.733 0.479   -0.270  0.50 11.02 ? 176 PHE A CD1  1 
ATOM   1860 C  CD2  A PHE A 1 175 ? -16.767 1.285   1.989   0.50 9.28  ? 176 PHE A CD2  1 
ATOM   1861 C  CD2  B PHE A 1 175 ? -15.849 1.408   1.882   0.50 9.71  ? 176 PHE A CD2  1 
ATOM   1862 C  CE1  A PHE A 1 175 ? -17.393 -0.789  0.288   0.50 10.48 ? 176 PHE A CE1  1 
ATOM   1863 C  CE1  B PHE A 1 175 ? -16.337 -0.630  0.209   0.50 10.65 ? 176 PHE A CE1  1 
ATOM   1864 C  CE2  A PHE A 1 175 ? -17.384 0.112   2.545   0.50 8.93  ? 176 PHE A CE2  1 
ATOM   1865 C  CE2  B PHE A 1 175 ? -16.374 0.234   2.378   0.50 9.22  ? 176 PHE A CE2  1 
ATOM   1866 C  CZ   A PHE A 1 175 ? -17.672 -0.928  1.705   0.50 8.78  ? 176 PHE A CZ   1 
ATOM   1867 C  CZ   B PHE A 1 175 ? -16.614 -0.789  1.554   0.50 10.17 ? 176 PHE A CZ   1 
ATOM   1868 N  N    A THR A 1 176 ? -18.886 4.572   -0.674  0.50 7.85  ? 177 THR A N    1 
ATOM   1869 N  N    B THR A 1 176 ? -17.902 4.706   -0.809  0.50 8.77  ? 177 THR A N    1 
ATOM   1870 C  CA   A THR A 1 176 ? -19.885 5.448   -0.127  0.50 7.07  ? 177 THR A CA   1 
ATOM   1871 C  CA   B THR A 1 176 ? -18.977 5.462   -0.282  0.50 9.24  ? 177 THR A CA   1 
ATOM   1872 C  C    A THR A 1 176 ? -21.090 4.644   0.334   0.50 7.24  ? 177 THR A C    1 
ATOM   1873 C  C    B THR A 1 176 ? -20.207 4.626   0.090   0.50 8.65  ? 177 THR A C    1 
ATOM   1874 O  O    A THR A 1 176 ? -21.339 3.519   -0.104  0.50 8.36  ? 177 THR A O    1 
ATOM   1875 O  O    B THR A 1 176 ? -20.384 3.513   -0.331  0.50 8.34  ? 177 THR A O    1 
ATOM   1876 C  CB   A THR A 1 176 ? -20.360 6.497   -1.135  0.50 8.16  ? 177 THR A CB   1 
ATOM   1877 C  CB   B THR A 1 176 ? -19.432 6.596   -1.313  0.50 9.14  ? 177 THR A CB   1 
ATOM   1878 O  OG1  A THR A 1 176 ? -20.948 5.856   -2.312  0.50 11.58 ? 177 THR A OG1  1 
ATOM   1879 O  OG1  B THR A 1 176 ? -19.845 6.017   -2.563  0.50 11.64 ? 177 THR A OG1  1 
ATOM   1880 C  CG2  A THR A 1 176 ? -19.200 7.418   -1.488  0.50 14.39 ? 177 THR A CG2  1 
ATOM   1881 C  CG2  B THR A 1 176 ? -18.361 7.595   -1.500  0.50 13.86 ? 177 THR A CG2  1 
ATOM   1882 N  N    A ASN A 1 177 ? -21.861 5.256   1.217   0.50 6.77  ? 178 ASN A N    1 
ATOM   1883 N  N    B ASN A 1 177 ? -21.001 5.208   0.963   0.50 7.74  ? 178 ASN A N    1 
ATOM   1884 C  CA   A ASN A 1 177 ? -23.136 4.735   1.664   0.50 7.39  ? 178 ASN A CA   1 
ATOM   1885 C  CA   B ASN A 1 177 ? -22.255 4.671   1.439   0.50 8.55  ? 178 ASN A CA   1 
ATOM   1886 C  C    A ASN A 1 177 ? -23.027 3.397   2.498   0.50 7.04  ? 178 ASN A C    1 
ATOM   1887 C  C    B ASN A 1 177 ? -22.088 3.356   2.167   0.50 8.63  ? 178 ASN A C    1 
ATOM   1888 O  O    A ASN A 1 177 ? -23.989 2.685   2.562   0.50 11.26 ? 178 ASN A O    1 
ATOM   1889 O  O    B ASN A 1 177 ? -22.968 2.542   2.110   0.50 10.87 ? 178 ASN A O    1 
ATOM   1890 C  CB   A ASN A 1 177 ? -24.159 4.626   0.516   0.50 9.10  ? 178 ASN A CB   1 
ATOM   1891 C  CB   B ASN A 1 177 ? -23.283 4.597   0.264   0.50 9.89  ? 178 ASN A CB   1 
ATOM   1892 C  CG   A ASN A 1 177 ? -24.469 6.009   -0.081  0.50 9.43  ? 178 ASN A CG   1 
ATOM   1893 C  CG   B ASN A 1 177 ? -23.571 5.980   -0.322  0.50 9.05  ? 178 ASN A CG   1 
ATOM   1894 O  OD1  A ASN A 1 177 ? -25.125 6.826   0.546   0.50 12.00 ? 178 ASN A OD1  1 
ATOM   1895 O  OD1  B ASN A 1 177 ? -24.224 6.790   0.333   0.50 9.82  ? 178 ASN A OD1  1 
ATOM   1896 N  ND2  A ASN A 1 177 ? -23.847 6.303   -1.212  0.50 10.32 ? 178 ASN A ND2  1 
ATOM   1897 N  ND2  B ASN A 1 177 ? -23.017 6.269   -1.453  0.50 8.55  ? 178 ASN A ND2  1 
ATOM   1898 N  N    A PHE A 1 178 ? -21.876 3.088   3.048   0.50 7.35  ? 179 PHE A N    1 
ATOM   1899 N  N    B PHE A 1 178 ? -20.959 3.087   2.795   0.50 7.79  ? 179 PHE A N    1 
ATOM   1900 C  CA   A PHE A 1 178 ? -21.749 1.890   3.841   0.50 5.98  ? 179 PHE A CA   1 
ATOM   1901 C  CA   B PHE A 1 178 ? -20.854 1.910   3.644   0.50 7.88  ? 179 PHE A CA   1 
ATOM   1902 C  C    A PHE A 1 178 ? -22.216 2.204   5.253   0.50 6.68  ? 179 PHE A C    1 
ATOM   1903 C  C    B PHE A 1 178 ? -21.440 2.219   4.998   0.50 7.12  ? 179 PHE A C    1 
ATOM   1904 O  O    A PHE A 1 178 ? -21.772 3.180   5.889   0.50 7.46  ? 179 PHE A O    1 
ATOM   1905 O  O    B PHE A 1 178 ? -21.008 3.177   5.647   0.50 9.60  ? 179 PHE A O    1 
ATOM   1906 C  CB   A PHE A 1 178 ? -20.316 1.431   3.870   0.50 6.60  ? 179 PHE A CB   1 
ATOM   1907 C  CB   B PHE A 1 178 ? -19.425 1.410   3.750   0.50 7.92  ? 179 PHE A CB   1 
ATOM   1908 C  CG   A PHE A 1 178 ? -20.167 0.155   4.683   0.50 6.30  ? 179 PHE A CG   1 
ATOM   1909 C  CG   B PHE A 1 178 ? -19.332 0.225   4.617   0.50 7.71  ? 179 PHE A CG   1 
ATOM   1910 C  CD1  A PHE A 1 178 ? -20.610 -1.078  4.154   0.50 8.46  ? 179 PHE A CD1  1 
ATOM   1911 C  CD1  B PHE A 1 178 ? -19.715 -0.992  4.104   0.50 8.61  ? 179 PHE A CD1  1 
ATOM   1912 C  CD2  A PHE A 1 178 ? -19.781 0.217   6.036   0.50 6.08  ? 179 PHE A CD2  1 
ATOM   1913 C  CD2  B PHE A 1 178 ? -19.020 0.329   5.933   0.50 6.84  ? 179 PHE A CD2  1 
ATOM   1914 C  CE1  A PHE A 1 178 ? -20.622 -2.222  4.931   0.50 8.12  ? 179 PHE A CE1  1 
ATOM   1915 C  CE1  B PHE A 1 178 ? -19.722 -2.122  4.870   0.50 9.85  ? 179 PHE A CE1  1 
ATOM   1916 C  CE2  A PHE A 1 178 ? -19.781 -0.997  6.808   0.50 6.27  ? 179 PHE A CE2  1 
ATOM   1917 C  CE2  B PHE A 1 178 ? -18.992 -0.820  6.743   0.50 7.89  ? 179 PHE A CE2  1 
ATOM   1918 C  CZ   A PHE A 1 178 ? -20.170 -2.156  6.261   0.50 6.49  ? 179 PHE A CZ   1 
ATOM   1919 C  CZ   B PHE A 1 178 ? -19.353 -2.022  6.243   0.50 9.82  ? 179 PHE A CZ   1 
ATOM   1920 N  N    A ASP A 1 179 ? -23.078 1.346   5.818   0.50 6.70  ? 180 ASP A N    1 
ATOM   1921 N  N    B ASP A 1 179 ? -22.346 1.374   5.470   0.50 7.78  ? 180 ASP A N    1 
ATOM   1922 C  CA   A ASP A 1 179 ? -23.704 1.608   7.093   0.50 8.32  ? 180 ASP A CA   1 
ATOM   1923 C  CA   B ASP A 1 179 ? -23.039 1.595   6.764   0.50 8.81  ? 180 ASP A CA   1 
ATOM   1924 C  C    A ASP A 1 179 ? -23.061 0.690   8.147   0.50 7.70  ? 180 ASP A C    1 
ATOM   1925 C  C    B ASP A 1 179 ? -22.463 0.680   7.866   0.50 8.03  ? 180 ASP A C    1 
ATOM   1926 O  O    A ASP A 1 179 ? -23.326 -0.512  8.197   0.50 7.52  ? 180 ASP A O    1 
ATOM   1927 O  O    B ASP A 1 179 ? -22.685 -0.537  7.889   0.50 7.61  ? 180 ASP A O    1 
ATOM   1928 C  CB   A ASP A 1 179 ? -25.172 1.276   7.033   0.50 9.05  ? 180 ASP A CB   1 
ATOM   1929 C  CB   B ASP A 1 179 ? -24.533 1.246   6.578   0.50 11.23 ? 180 ASP A CB   1 
ATOM   1930 C  CG   A ASP A 1 179 ? -25.952 1.842   8.196   0.50 11.74 ? 180 ASP A CG   1 
ATOM   1931 C  CG   B ASP A 1 179 ? -25.404 1.504   7.830   0.50 11.17 ? 180 ASP A CG   1 
ATOM   1932 O  OD1  A ASP A 1 179 ? -25.456 1.889   9.347   0.50 9.61  ? 180 ASP A OD1  1 
ATOM   1933 O  OD1  B ASP A 1 179 ? -24.844 1.787   8.913   0.50 10.17 ? 180 ASP A OD1  1 
ATOM   1934 O  OD2  A ASP A 1 179 ? -27.096 2.215   7.956   0.50 16.19 ? 180 ASP A OD2  1 
ATOM   1935 O  OD2  B ASP A 1 179 ? -26.652 1.477   7.791   0.50 19.93 ? 180 ASP A OD2  1 
ATOM   1936 N  N    A PRO A 1 180 ? -22.220 1.273   9.048   0.50 7.87  ? 181 PRO A N    1 
ATOM   1937 N  N    B PRO A 1 180 ? -21.713 1.270   8.815   0.50 8.02  ? 181 PRO A N    1 
ATOM   1938 C  CA   A PRO A 1 180 ? -21.413 0.419   9.975   0.50 9.41  ? 181 PRO A CA   1 
ATOM   1939 C  CA   B PRO A 1 180 ? -21.167 0.402   9.892   0.50 9.50  ? 181 PRO A CA   1 
ATOM   1940 C  C    A PRO A 1 180 ? -22.286 -0.237  10.952  0.50 10.09 ? 181 PRO A C    1 
ATOM   1941 C  C    B PRO A 1 180 ? -22.201 -0.151  10.987  0.50 10.38 ? 181 PRO A C    1 
ATOM   1942 O  O    A PRO A 1 180 ? -21.852 -1.167  11.637  0.50 9.70  ? 181 PRO A O    1 
ATOM   1943 O  O    B PRO A 1 180 ? -21.759 -0.983  11.819  0.50 10.04 ? 181 PRO A O    1 
ATOM   1944 C  CB   A PRO A 1 180 ? -20.469 1.439   10.617  0.50 9.97  ? 181 PRO A CB   1 
ATOM   1945 C  CB   B PRO A 1 180 ? -20.083 1.309   10.441  0.50 10.28 ? 181 PRO A CB   1 
ATOM   1946 C  CG   A PRO A 1 180 ? -21.163 2.769   10.524  0.50 8.51  ? 181 PRO A CG   1 
ATOM   1947 C  CG   B PRO A 1 180 ? -20.626 2.703   10.268  0.50 9.85  ? 181 PRO A CG   1 
ATOM   1948 C  CD   A PRO A 1 180 ? -21.922 2.706   9.185   0.50 7.42  ? 181 PRO A CD   1 
ATOM   1949 C  CD   B PRO A 1 180 ? -21.299 2.662   8.937   0.50 7.70  ? 181 PRO A CD   1 
ATOM   1950 N  N    . ARG A 1 181 ? -23.515 0.214   11.001  1.00 10.32 ? 182 ARG A N    1 
ATOM   1951 C  CA   . ARG A 1 181 ? -24.469 -0.478  11.895  1.00 10.38 ? 182 ARG A CA   1 
ATOM   1952 C  C    . ARG A 1 181 ? -24.590 -1.933  11.539  1.00 11.47 ? 182 ARG A C    1 
ATOM   1953 O  O    . ARG A 1 181 ? -24.911 -2.765  12.433  1.00 13.18 ? 182 ARG A O    1 
ATOM   1954 C  CB   . ARG A 1 181 ? -25.877 0.156   11.873  1.00 12.31 ? 182 ARG A CB   1 
ATOM   1955 C  CG   . ARG A 1 181 ? -25.814 1.599   12.411  1.00 13.09 ? 182 ARG A CG   1 
ATOM   1956 C  CD   . ARG A 1 181 ? -27.168 2.311   12.282  1.00 15.47 ? 182 ARG A CD   1 
ATOM   1957 N  NE   . ARG A 1 181 ? -27.492 2.546   10.899  1.00 15.92 ? 182 ARG A NE   1 
ATOM   1958 C  CZ   . ARG A 1 181 ? -28.566 3.232   10.577  1.00 18.90 ? 182 ARG A CZ   1 
ATOM   1959 N  NH1  . ARG A 1 181 ? -29.383 3.664   11.507  1.00 24.32 ? 182 ARG A NH1  1 
ATOM   1960 N  NH2  . ARG A 1 181 ? -28.849 3.393   9.291   1.00 21.59 ? 182 ARG A NH2  1 
ATOM   1961 N  N    . GLY A 1 182 ? -24.292 -2.340  10.311  1.00 11.82 ? 183 GLY A N    1 
ATOM   1962 C  CA   . GLY A 1 182 ? -24.413 -3.719  9.934   1.00 12.43 ? 183 GLY A CA   1 
ATOM   1963 C  C    . GLY A 1 182 ? -23.213 -4.551  10.428  1.00 12.42 ? 183 GLY A C    1 
ATOM   1964 O  O    . GLY A 1 182 ? -23.194 -5.762  10.096  1.00 15.49 ? 183 GLY A O    1 
ATOM   1965 N  N    A LEU A 1 183 ? -22.490 -4.060  11.391  0.50 9.59  ? 184 LEU A N    1 
ATOM   1966 N  N    B LEU A 1 183 ? -22.065 -3.965  10.991  0.50 9.17  ? 184 LEU A N    1 
ATOM   1967 C  CA   A LEU A 1 183 ? -21.427 -4.813  11.907  0.50 7.97  ? 184 LEU A CA   1 
ATOM   1968 C  CA   B LEU A 1 183 ? -20.857 -4.701  11.539  0.50 8.23  ? 184 LEU A CA   1 
ATOM   1969 C  C    A LEU A 1 183 ? -21.591 -4.969  13.422  0.50 6.66  ? 184 LEU A C    1 
ATOM   1970 C  C    B LEU A 1 183 ? -20.958 -4.962  13.073  0.50 7.83  ? 184 LEU A C    1 
ATOM   1971 O  O    A LEU A 1 183 ? -20.681 -5.515  14.069  0.50 7.81  ? 184 LEU A O    1 
ATOM   1972 O  O    B LEU A 1 183 ? -20.096 -5.599  13.669  0.50 7.82  ? 184 LEU A O    1 
ATOM   1973 C  CB   A LEU A 1 183 ? -20.121 -4.162  11.575  0.50 6.90  ? 184 LEU A CB   1 
ATOM   1974 C  CB   B LEU A 1 183 ? -19.553 -3.921  11.306  0.50 8.18  ? 184 LEU A CB   1 
ATOM   1975 C  CG   A LEU A 1 183 ? -19.857 -3.953  10.081  0.50 7.27  ? 184 LEU A CG   1 
ATOM   1976 C  CG   B LEU A 1 183 ? -19.150 -3.739  9.810   0.50 7.24  ? 184 LEU A CG   1 
ATOM   1977 C  CD1  A LEU A 1 183 ? -18.513 -3.195  10.013  0.50 9.03  ? 184 LEU A CD1  1 
ATOM   1978 C  CD1  B LEU A 1 183 ? -17.865 -2.958  9.716   0.50 9.36  ? 184 LEU A CD1  1 
ATOM   1979 C  CD2  A LEU A 1 183 ? -19.835 -5.241  9.294   0.50 8.36  ? 184 LEU A CD2  1 
ATOM   1980 C  CD2  B LEU A 1 183 ? -18.994 -5.148  9.183   0.50 10.76 ? 184 LEU A CD2  1 
ATOM   1981 N  N    A LEU A 1 184 ? -22.692 -4.503  14.013  0.50 6.91  ? 185 LEU A N    1 
ATOM   1982 N  N    B LEU A 1 184 ? -22.033 -4.465  13.662  0.50 7.73  ? 185 LEU A N    1 
ATOM   1983 C  CA   A LEU A 1 184 ? -22.771 -4.463  15.468  0.50 7.08  ? 185 LEU A CA   1 
ATOM   1984 C  CA   B LEU A 1 184 ? -22.252 -4.621  15.118  0.50 8.20  ? 185 LEU A CA   1 
ATOM   1985 C  C    A LEU A 1 184 ? -23.548 -5.663  15.976  0.50 7.37  ? 185 LEU A C    1 
ATOM   1986 C  C    B LEU A 1 184 ? -22.967 -5.966  15.512  0.50 8.91  ? 185 LEU A C    1 
ATOM   1987 O  O    A LEU A 1 184 ? -24.630 -6.011  15.443  0.50 8.71  ? 185 LEU A O    1 
ATOM   1988 O  O    B LEU A 1 184 ? -23.702 -6.482  14.640  0.50 9.40  ? 185 LEU A O    1 
ATOM   1989 C  CB   A LEU A 1 184 ? -23.498 -3.196  15.926  0.50 5.99  ? 185 LEU A CB   1 
ATOM   1990 C  CB   B LEU A 1 184 ? -23.167 -3.452  15.639  0.50 8.69  ? 185 LEU A CB   1 
ATOM   1991 C  CG   A LEU A 1 184 ? -22.868 -1.894  15.402  0.50 7.01  ? 185 LEU A CG   1 
ATOM   1992 C  CG   B LEU A 1 184 ? -22.582 -2.028  15.458  0.50 8.93  ? 185 LEU A CG   1 
ATOM   1993 C  CD1  A LEU A 1 184 ? -23.602 -0.656  15.982  0.50 8.71  ? 185 LEU A CD1  1 
ATOM   1994 C  CD1  B LEU A 1 184 ? -23.680 -1.018  15.762  0.50 9.98  ? 185 LEU A CD1  1 
ATOM   1995 C  CD2  A LEU A 1 184 ? -21.318 -1.866  15.694  0.50 5.77  ? 185 LEU A CD2  1 
ATOM   1996 C  CD2  B LEU A 1 184 ? -21.346 -1.681  16.301  0.50 9.40  ? 185 LEU A CD2  1 
ATOM   1997 N  N    A PRO A 1 185 ? -22.880 -6.339  16.933  0.50 9.46  ? 186 PRO A N    1 
ATOM   1998 N  N    B PRO A 1 185 ? -22.974 -6.382  16.855  0.50 9.60  ? 186 PRO A N    1 
ATOM   1999 C  CA   A PRO A 1 185 ? -23.460 -7.535  17.352  0.50 9.37  ? 186 PRO A CA   1 
ATOM   2000 C  CA   B PRO A 1 185 ? -23.904 -7.397  17.556  0.50 8.45  ? 186 PRO A CA   1 
ATOM   2001 C  C    A PRO A 1 185 ? -24.772 -7.006  17.807  0.50 8.13  ? 186 PRO A C    1 
ATOM   2002 C  C    B PRO A 1 185 ? -25.141 -6.872  18.390  0.50 7.86  ? 186 PRO A C    1 
ATOM   2003 O  O    A PRO A 1 185 ? -25.051 -5.808  17.722  0.50 8.54  ? 186 PRO A O    1 
ATOM   2004 O  O    B PRO A 1 185 ? -25.303 -5.666  18.593  0.50 6.81  ? 186 PRO A O    1 
ATOM   2005 C  CB   A PRO A 1 185 ? -22.551 -7.976  18.526  0.50 9.59  ? 186 PRO A CB   1 
ATOM   2006 C  CB   B PRO A 1 185 ? -22.934 -8.147  18.439  0.50 8.39  ? 186 PRO A CB   1 
ATOM   2007 C  CG   A PRO A 1 185 ? -21.884 -6.687  19.002  0.50 8.52  ? 186 PRO A CG   1 
ATOM   2008 C  CG   B PRO A 1 185 ? -22.026 -7.009  18.967  0.50 7.94  ? 186 PRO A CG   1 
ATOM   2009 C  CD   A PRO A 1 185 ? -21.669 -5.985  17.701  0.50 7.09  ? 186 PRO A CD   1 
ATOM   2010 C  CD   B PRO A 1 185 ? -21.945 -5.909  17.808  0.50 8.08  ? 186 PRO A CD   1 
ATOM   2011 N  N    A GLU A 1 186 ? -25.588 -7.919  18.326  0.50 9.59  ? 187 GLU A N    1 
ATOM   2012 N  N    B GLU A 1 186 ? -26.008 -7.796  18.838  0.50 8.37  ? 187 GLU A N    1 
ATOM   2013 C  CA   A GLU A 1 186 ? -26.832 -7.534  18.975  0.50 10.39 ? 187 GLU A CA   1 
ATOM   2014 C  CA   B GLU A 1 186 ? -27.224 -7.350  19.489  0.50 9.06  ? 187 GLU A CA   1 
ATOM   2015 C  C    A GLU A 1 186 ? -26.710 -6.726  20.344  0.50 11.11 ? 187 GLU A C    1 
ATOM   2016 C  C    B GLU A 1 186 ? -26.902 -6.623  20.703  0.50 11.53 ? 187 GLU A C    1 
ATOM   2017 O  O    A GLU A 1 186 ? -27.364 -5.669  20.407  0.50 13.90 ? 187 GLU A O    1 
ATOM   2018 O  O    B GLU A 1 186 ? -27.488 -5.572  21.042  0.50 11.60 ? 187 GLU A O    1 
ATOM   2019 C  CB   A GLU A 1 186 ? -27.608 -8.831  19.192  0.50 9.79  ? 187 GLU A CB   1 
ATOM   2020 C  CB   B GLU A 1 186 ? -28.002 -8.587  19.984  0.50 9.55  ? 187 GLU A CB   1 
ATOM   2021 C  CG   A GLU A 1 186 ? -28.882 -8.726  19.949  0.50 12.55 ? 187 GLU A CG   1 
ATOM   2022 C  CG   B GLU A 1 186 ? -28.747 -9.281  18.892  0.50 12.13 ? 187 GLU A CG   1 
ATOM   2023 C  CD   A GLU A 1 186 ? -29.507 -10.041 20.363  0.50 15.16 ? 187 GLU A CD   1 
ATOM   2024 C  CD   B GLU A 1 186 ? -29.455 -10.577 19.307  0.50 13.00 ? 187 GLU A CD   1 
ATOM   2025 O  OE1  A GLU A 1 186 ? -29.326 -11.036 19.618  0.50 15.11 ? 187 GLU A OE1  1 
ATOM   2026 O  OE1  B GLU A 1 186 ? -29.529 -10.866 20.568  0.50 13.47 ? 187 GLU A OE1  1 
ATOM   2027 O  OE2  A GLU A 1 186 ? -30.160 -10.019 21.430  0.50 15.88 ? 187 GLU A OE2  1 
ATOM   2028 O  OE2  B GLU A 1 186 ? -29.926 -11.295 18.385  0.50 17.48 ? 187 GLU A OE2  1 
ATOM   2029 N  N    . SER A 1 187 ? -25.989 -7.190  21.438  1.00 11.59 ? 188 SER A N    1 
ATOM   2030 C  CA   . SER A 1 187 ? -25.727 -6.593  22.703  1.00 11.38 ? 188 SER A CA   1 
ATOM   2031 C  C    . SER A 1 187 ? -24.580 -5.575  22.682  1.00 10.51 ? 188 SER A C    1 
ATOM   2032 O  O    . SER A 1 187 ? -23.558 -5.856  22.044  1.00 11.43 ? 188 SER A O    1 
ATOM   2033 C  CB   . SER A 1 187 ? -25.348 -7.723  23.712  1.00 12.80 ? 188 SER A CB   1 
ATOM   2034 O  OG   . SER A 1 187 ? -25.061 -7.156  25.014  1.00 13.09 ? 188 SER A OG   1 
ATOM   2035 N  N    . LEU A 1 188 ? -24.734 -4.513  23.427  1.00 10.53 ? 189 LEU A N    1 
ATOM   2036 C  CA   . LEU A 1 188 ? -23.671 -3.555  23.665  1.00 10.78 ? 189 LEU A CA   1 
ATOM   2037 C  C    . LEU A 1 188 ? -23.060 -3.709  25.013  1.00 10.46 ? 189 LEU A C    1 
ATOM   2038 O  O    . LEU A 1 188 ? -22.340 -2.804  25.476  1.00 11.94 ? 189 LEU A O    1 
ATOM   2039 C  CB   . LEU A 1 188 ? -24.132 -2.122  23.388  1.00 13.00 ? 189 LEU A CB   1 
ATOM   2040 C  CG   . LEU A 1 188 ? -24.572 -1.705  22.024  1.00 13.98 ? 189 LEU A CG   1 
ATOM   2041 C  CD1  . LEU A 1 188 ? -25.146 -0.273  21.933  1.00 18.07 ? 189 LEU A CD1  1 
ATOM   2042 C  CD2  . LEU A 1 188 ? -23.478 -2.002  20.963  1.00 15.62 ? 189 LEU A CD2  1 
ATOM   2043 N  N    . ASP A 1 189 ? -23.157 -4.880  25.681  1.00 9.75  ? 190 ASP A N    1 
ATOM   2044 C  CA   . ASP A 1 189 ? -22.391 -5.115  26.936  1.00 10.31 ? 190 ASP A CA   1 
ATOM   2045 C  C    . ASP A 1 189 ? -20.901 -5.068  26.611  1.00 7.95  ? 190 ASP A C    1 
ATOM   2046 O  O    . ASP A 1 189 ? -20.471 -5.579  25.565  1.00 7.87  ? 190 ASP A O    1 
ATOM   2047 C  CB   . ASP A 1 189 ? -22.746 -6.465  27.518  1.00 12.15 ? 190 ASP A CB   1 
ATOM   2048 C  CG   . ASP A 1 189 ? -24.163 -6.550  28.193  1.00 16.68 ? 190 ASP A CG   1 
ATOM   2049 O  OD1  . ASP A 1 189 ? -24.761 -5.493  28.351  1.00 22.29 ? 190 ASP A OD1  1 
ATOM   2050 O  OD2  . ASP A 1 189 ? -24.603 -7.658  28.428  1.00 23.29 ? 190 ASP A OD2  1 
ATOM   2051 N  N    . TYR A 1 190 ? -20.116 -4.474  27.507  1.00 8.34  ? 191 TYR A N    1 
ATOM   2052 C  CA   . TYR A 1 190 ? -18.704 -4.213  27.214  1.00 7.39  ? 191 TYR A CA   1 
ATOM   2053 C  C    . TYR A 1 190 ? -17.815 -4.281  28.437  1.00 6.80  ? 191 TYR A C    1 
ATOM   2054 O  O    . TYR A 1 190 ? -18.264 -4.163  29.587  1.00 8.21  ? 191 TYR A O    1 
ATOM   2055 C  CB   . TYR A 1 190 ? -18.552 -2.826  26.539  1.00 7.51  ? 191 TYR A CB   1 
ATOM   2056 C  CG   . TYR A 1 190 ? -18.968 -1.644  27.435  1.00 7.60  ? 191 TYR A CG   1 
ATOM   2057 C  CD1  . TYR A 1 190 ? -18.055 -1.054  28.289  1.00 8.25  ? 191 TYR A CD1  1 
ATOM   2058 C  CD2  . TYR A 1 190 ? -20.254 -1.145  27.360  1.00 8.56  ? 191 TYR A CD2  1 
ATOM   2059 C  CE1  . TYR A 1 190 ? -18.456 -0.006  29.111  1.00 8.67  ? 191 TYR A CE1  1 
ATOM   2060 C  CE2  . TYR A 1 190 ? -20.627 -0.066  28.219  1.00 9.81  ? 191 TYR A CE2  1 
ATOM   2061 C  CZ   . TYR A 1 190 ? -19.742 0.474   29.055  1.00 8.77  ? 191 TYR A CZ   1 
ATOM   2062 O  OH   . TYR A 1 190 ? -20.107 1.495   29.924  1.00 10.90 ? 191 TYR A OH   1 
ATOM   2063 N  N    . TRP A 1 191 ? -16.552 -4.422  28.134  1.00 6.37  ? 192 TRP A N    1 
ATOM   2064 C  CA   . TRP A 1 191 ? -15.438 -4.160  29.074  1.00 6.62  ? 192 TRP A CA   1 
ATOM   2065 C  C    . TRP A 1 191 ? -14.727 -2.877  28.668  1.00 6.13  ? 192 TRP A C    1 
ATOM   2066 O  O    . TRP A 1 191 ? -14.700 -2.532  27.475  1.00 7.01  ? 192 TRP A O    1 
ATOM   2067 C  CB   . TRP A 1 191 ? -14.401 -5.289  29.043  1.00 6.75  ? 192 TRP A CB   1 
ATOM   2068 C  CG   . TRP A 1 191 ? -14.931 -6.632  29.466  1.00 6.87  ? 192 TRP A CG   1 
ATOM   2069 C  CD1  . TRP A 1 191 ? -15.151 -7.050  30.738  1.00 8.83  ? 192 TRP A CD1  1 
ATOM   2070 C  CD2  . TRP A 1 191 ? -15.196 -7.766  28.626  1.00 7.56  ? 192 TRP A CD2  1 
ATOM   2071 N  NE1  . TRP A 1 191 ? -15.555 -8.380  30.727  1.00 9.30  ? 192 TRP A NE1  1 
ATOM   2072 C  CE2  . TRP A 1 191 ? -15.615 -8.838  29.459  1.00 8.60  ? 192 TRP A CE2  1 
ATOM   2073 C  CE3  . TRP A 1 191 ? -15.110 -7.955  27.219  1.00 7.45  ? 192 TRP A CE3  1 
ATOM   2074 C  CZ2  . TRP A 1 191 ? -15.929 -10.101 28.915  1.00 9.49  ? 192 TRP A CZ2  1 
ATOM   2075 C  CZ3  . TRP A 1 191 ? -15.411 -9.201  26.742  1.00 8.49  ? 192 TRP A CZ3  1 
ATOM   2076 C  CH2  . TRP A 1 191 ? -15.787 -10.230 27.574  1.00 9.76  ? 192 TRP A CH2  1 
ATOM   2077 N  N    . THR A 1 192 ? -14.155 -2.170  29.622  1.00 5.99  ? 193 THR A N    1 
ATOM   2078 C  CA   . THR A 1 192 ? -13.422 -0.944  29.285  1.00 6.03  ? 193 THR A CA   1 
ATOM   2079 C  C    . THR A 1 192 ? -12.181 -0.768  30.165  1.00 6.12  ? 193 THR A C    1 
ATOM   2080 O  O    . THR A 1 192 ? -12.166 -1.163  31.336  1.00 7.20  ? 193 THR A O    1 
ATOM   2081 C  CB   . THR A 1 192 ? -14.395 0.267   29.408  1.00 5.88  ? 193 THR A CB   1 
ATOM   2082 O  OG1  . THR A 1 192 ? -13.680 1.474   29.029  1.00 6.63  ? 193 THR A OG1  1 
ATOM   2083 C  CG2  . THR A 1 192 ? -14.904 0.507   30.831  1.00 8.08  ? 193 THR A CG2  1 
ATOM   2084 N  N    . TYR A 1 193 ? -11.145 -0.168  29.584  1.00 5.63  ? 194 TYR A N    1 
ATOM   2085 C  CA   . TYR A 1 193 ? -9.904  0.136   30.310  1.00 6.50  ? 194 TYR A CA   1 
ATOM   2086 C  C    . TYR A 1 193 ? -9.138  1.194   29.528  1.00 5.78  ? 194 TYR A C    1 
ATOM   2087 O  O    . TYR A 1 193 ? -9.369  1.381   28.318  1.00 5.86  ? 194 TYR A O    1 
ATOM   2088 C  CB   . TYR A 1 193 ? -9.074  -1.169  30.498  1.00 6.24  ? 194 TYR A CB   1 
ATOM   2089 C  CG   . TYR A 1 193 ? -8.374  -1.633  29.225  1.00 5.70  ? 194 TYR A CG   1 
ATOM   2090 C  CD1  . TYR A 1 193 ? -9.039  -2.352  28.248  1.00 6.19  ? 194 TYR A CD1  1 
ATOM   2091 C  CD2  . TYR A 1 193 ? -7.050  -1.290  29.003  1.00 6.49  ? 194 TYR A CD2  1 
ATOM   2092 C  CE1  . TYR A 1 193 ? -8.415  -2.684  27.018  1.00 5.75  ? 194 TYR A CE1  1 
ATOM   2093 C  CE2  . TYR A 1 193 ? -6.415  -1.591  27.799  1.00 6.09  ? 194 TYR A CE2  1 
ATOM   2094 C  CZ   . TYR A 1 193 ? -7.086  -2.300  26.816  1.00 5.58  ? 194 TYR A CZ   1 
ATOM   2095 O  OH   . TYR A 1 193 ? -6.430  -2.584  25.653  1.00 5.86  ? 194 TYR A OH   1 
ATOM   2096 N  N    . PRO A 1 194 ? -8.194  1.897   30.176  1.00 6.04  ? 195 PRO A N    1 
ATOM   2097 C  CA   . PRO A 1 194 ? -7.354  2.889   29.500  1.00 6.16  ? 195 PRO A CA   1 
ATOM   2098 C  C    . PRO A 1 194 ? -6.169  2.230   28.861  1.00 5.81  ? 195 PRO A C    1 
ATOM   2099 O  O    . PRO A 1 194 ? -5.433  1.458   29.488  1.00 6.50  ? 195 PRO A O    1 
ATOM   2100 C  CB   . PRO A 1 194 ? -6.898  3.811   30.650  1.00 7.23  ? 195 PRO A CB   1 
ATOM   2101 C  CG   . PRO A 1 194 ? -6.874  2.853   31.851  1.00 7.99  ? 195 PRO A CG   1 
ATOM   2102 C  CD   . PRO A 1 194 ? -7.976  1.891   31.653  1.00 7.47  ? 195 PRO A CD   1 
ATOM   2103 N  N    . GLY A 1 195 ? -5.952  2.535   27.579  1.00 5.60  ? 196 GLY A N    1 
ATOM   2104 C  CA   . GLY A 1 195 ? -4.840  1.955   26.827  1.00 6.09  ? 196 GLY A CA   1 
ATOM   2105 C  C    . GLY A 1 195 ? -4.310  2.841   25.719  1.00 5.56  ? 196 GLY A C    1 
ATOM   2106 O  O    . GLY A 1 195 ? -4.187  4.069   25.878  1.00 5.85  ? 196 GLY A O    1 
ATOM   2107 N  N    . SER A 1 196 ? -3.891  2.185   24.643  1.00 5.72  ? 197 SER A N    1 
ATOM   2108 C  CA   . SER A 1 196 ? -3.062  2.835   23.603  1.00 5.86  ? 197 SER A CA   1 
ATOM   2109 C  C    . SER A 1 196 ? -3.530  2.407   22.226  1.00 5.03  ? 197 SER A C    1 
ATOM   2110 O  O    . SER A 1 196 ? -4.278  1.442   22.063  1.00 5.40  ? 197 SER A O    1 
ATOM   2111 C  CB   . SER A 1 196 ? -1.594  2.427   23.782  1.00 6.50  ? 197 SER A CB   1 
ATOM   2112 O  OG   . SER A 1 196 ? -1.327  1.071   23.360  1.00 6.06  ? 197 SER A OG   1 
ATOM   2113 N  N    . LEU A 1 197 ? -2.957  3.050   21.215  1.00 5.43  ? 198 LEU A N    1 
ATOM   2114 C  CA   . LEU A 1 197 ? -3.036  2.543   19.860  1.00 5.67  ? 198 LEU A CA   1 
ATOM   2115 C  C    . LEU A 1 197 ? -2.288  1.187   19.895  1.00 5.90  ? 198 LEU A C    1 
ATOM   2116 O  O    . LEU A 1 197 ? -1.261  1.017   20.628  1.00 6.30  ? 198 LEU A O    1 
ATOM   2117 C  CB   . LEU A 1 197 ? -2.176  3.401   18.943  1.00 6.47  ? 198 LEU A CB   1 
ATOM   2118 C  CG   . LEU A 1 197 ? -2.821  4.546   18.175  1.00 14.89 ? 198 LEU A CG   1 
ATOM   2119 C  CD1  . LEU A 1 197 ? -3.765  5.421   18.989  1.00 13.56 ? 198 LEU A CD1  1 
ATOM   2120 C  CD2  . LEU A 1 197 ? -1.836  5.355   17.369  1.00 18.32 ? 198 LEU A CD2  1 
ATOM   2121 N  N    . THR A 1 198 ? -2.733  0.186   19.136  1.00 5.61  ? 199 THR A N    1 
ATOM   2122 C  CA   . THR A 1 198 ? -2.046  -1.122  19.048  1.00 6.00  ? 199 THR A CA   1 
ATOM   2123 C  C    . THR A 1 198 ? -1.013  -1.174  17.916  1.00 6.61  ? 199 THR A C    1 
ATOM   2124 O  O    . THR A 1 198 ? -0.384  -2.228  17.759  1.00 6.79  ? 199 THR A O    1 
ATOM   2125 C  CB   . THR A 1 198 ? -3.050  -2.249  18.933  1.00 5.86  ? 199 THR A CB   1 
ATOM   2126 O  OG1  . THR A 1 198 ? -3.645  -2.159  17.620  1.00 5.67  ? 199 THR A OG1  1 
ATOM   2127 C  CG2  . THR A 1 198 ? -4.078  -2.268  20.040  1.00 5.84  ? 199 THR A CG2  1 
ATOM   2128 N  N    . THR A 1 199 ? -0.892  -0.109  17.127  1.00 7.10  ? 200 THR A N    1 
ATOM   2129 C  CA   . THR A 1 199 ? 0.085   0.047   16.087  1.00 7.78  ? 200 THR A CA   1 
ATOM   2130 C  C    . THR A 1 199 ? 0.977   1.232   16.438  1.00 7.56  ? 200 THR A C    1 
ATOM   2131 O  O    . THR A 1 199 ? 0.519   2.198   17.060  1.00 7.80  ? 200 THR A O    1 
ATOM   2132 C  CB   . THR A 1 199 ? -0.554  0.337   14.718  1.00 7.87  ? 200 THR A CB   1 
ATOM   2133 O  OG1  . THR A 1 199 ? -1.370  1.520   14.822  1.00 10.72 ? 200 THR A OG1  1 
ATOM   2134 C  CG2  . THR A 1 199 ? -1.420  -0.805  14.246  1.00 8.70  ? 200 THR A CG2  1 
ATOM   2135 N  N    . PRO A 1 200 ? 2.248   1.200   16.008  1.00 7.94  ? 201 PRO A N    1 
ATOM   2136 C  CA   . PRO A 1 200 ? 3.041   2.462   16.032  1.00 8.62  ? 201 PRO A CA   1 
ATOM   2137 C  C    . PRO A 1 200 ? 2.216   3.595   15.497  1.00 8.93  ? 201 PRO A C    1 
ATOM   2138 O  O    . PRO A 1 200 ? 1.526   3.451   14.500  1.00 10.22 ? 201 PRO A O    1 
ATOM   2139 C  CB   . PRO A 1 200 ? 4.224   2.070   15.149  1.00 9.99  ? 201 PRO A CB   1 
ATOM   2140 C  CG   . PRO A 1 200 ? 4.418   0.603   15.408  1.00 9.94  ? 201 PRO A CG   1 
ATOM   2141 C  CD   . PRO A 1 200 ? 2.994   0.082   15.363  1.00 9.39  ? 201 PRO A CD   1 
ATOM   2142 N  N    . PRO A 1 201 ? 2.255   4.777   16.134  1.00 8.65  ? 202 PRO A N    1 
ATOM   2143 C  CA   . PRO A 1 201 ? 3.202   5.184   17.226  1.00 9.52  ? 202 PRO A CA   1 
ATOM   2144 C  C    . PRO A 1 201 ? 2.821   4.773   18.638  1.00 8.12  ? 202 PRO A C    1 
ATOM   2145 O  O    . PRO A 1 201 ? 3.473   5.219   19.587  1.00 9.21  ? 202 PRO A O    1 
ATOM   2146 C  CB   . PRO A 1 201 ? 3.247   6.707   17.018  1.00 11.18 ? 202 PRO A CB   1 
ATOM   2147 C  CG   . PRO A 1 201 ? 1.836   7.033   16.570  1.00 11.56 ? 202 PRO A CG   1 
ATOM   2148 C  CD   . PRO A 1 201 ? 1.509   5.921   15.593  1.00 10.15 ? 202 PRO A CD   1 
ATOM   2149 N  N    . LEU A 1 202 ? 1.799   3.930   18.824  1.00 7.25  ? 203 LEU A N    1 
ATOM   2150 C  CA   . LEU A 1 202 ? 1.559   3.298   20.173  1.00 6.79  ? 203 LEU A CA   1 
ATOM   2151 C  C    . LEU A 1 202 ? 1.166   4.303   21.242  1.00 6.84  ? 203 LEU A C    1 
ATOM   2152 O  O    . LEU A 1 202 ? 1.340   4.087   22.436  1.00 6.98  ? 203 LEU A O    1 
ATOM   2153 C  CB   . LEU A 1 202 ? 2.696   2.395   20.612  1.00 7.48  ? 203 LEU A CB   1 
ATOM   2154 C  CG   . LEU A 1 202 ? 3.021   1.241   19.639  1.00 8.07  ? 203 LEU A CG   1 
ATOM   2155 C  CD1  . LEU A 1 202 ? 4.313   0.572   20.105  1.00 9.96  ? 203 LEU A CD1  1 
ATOM   2156 C  CD2  . LEU A 1 202 ? 1.896   0.223   19.618  1.00 8.60  ? 203 LEU A CD2  1 
ATOM   2157 N  N    . LEU A 1 203 ? 0.581   5.441   20.797  1.00 7.19  ? 204 LEU A N    1 
ATOM   2158 C  CA   . LEU A 1 203 ? 0.312   6.574   21.707  1.00 7.36  ? 204 LEU A CA   1 
ATOM   2159 C  C    . LEU A 1 203 ? -0.758  6.153   22.739  1.00 6.98  ? 204 LEU A C    1 
ATOM   2160 O  O    . LEU A 1 203 ? -1.721  5.430   22.451  1.00 6.80  ? 204 LEU A O    1 
ATOM   2161 C  CB   . LEU A 1 203 ? -0.209  7.771   20.918  1.00 8.38  ? 204 LEU A CB   1 
ATOM   2162 C  CG   . LEU A 1 203 ? 0.906   8.344   19.981  1.00 10.05 ? 204 LEU A CG   1 
ATOM   2163 C  CD1  . LEU A 1 203 ? 0.213   9.395   19.017  1.00 11.70 ? 204 LEU A CD1  1 
ATOM   2164 C  CD2  . LEU A 1 203 ? 2.091   8.997   20.852  1.00 15.00 ? 204 LEU A CD2  1 
ATOM   2165 N  N    . GLU A 1 204 ? -0.567  6.606   23.978  1.00 6.74  ? 205 GLU A N    1 
ATOM   2166 C  CA   . GLU A 1 204 ? -1.355  6.243   25.111  1.00 6.94  ? 205 GLU A CA   1 
ATOM   2167 C  C    . GLU A 1 204 ? -2.547  7.211   25.300  1.00 6.48  ? 205 GLU A C    1 
ATOM   2168 O  O    . GLU A 1 204 ? -2.668  7.984   26.243  1.00 8.54  ? 205 GLU A O    1 
ATOM   2169 C  CB   . GLU A 1 204 ? -0.485  6.091   26.347  1.00 8.08  ? 205 GLU A CB   1 
ATOM   2170 C  CG   . GLU A 1 204 ? 0.405   4.876   26.273  1.00 7.76  ? 205 GLU A CG   1 
ATOM   2171 C  CD   . GLU A 1 204 ? 1.328   4.597   27.418  1.00 8.72  ? 205 GLU A CD   1 
ATOM   2172 O  OE1  . GLU A 1 204 ? 1.674   5.556   28.179  1.00 11.77 ? 205 GLU A OE1  1 
ATOM   2173 O  OE2  . GLU A 1 204 ? 1.762   3.423   27.561  1.00 9.20  ? 205 GLU A OE2  1 
ATOM   2174 N  N    . CYS A 1 205 ? -3.442  7.114   24.328  1.00 6.20  ? 206 CYS A N    1 
ATOM   2175 C  CA   . CYS A 1 205 ? -4.546  8.091   24.128  1.00 6.41  ? 206 CYS A CA   1 
ATOM   2176 C  C    . CYS A 1 205 ? -5.882  7.454   24.011  1.00 5.84  ? 206 CYS A C    1 
ATOM   2177 O  O    . CYS A 1 205 ? -6.823  8.158   23.649  1.00 7.27  ? 206 CYS A O    1 
ATOM   2178 C  CB   . CYS A 1 205 ? -4.233  8.956   22.890  1.00 7.23  ? 206 CYS A CB   1 
ATOM   2179 S  SG   . CYS A 1 205 ? -4.207  7.993   21.343  1.00 7.82  ? 206 CYS A SG   1 
ATOM   2180 N  N    . VAL A 1 206 ? -6.034  6.171   24.286  1.00 6.01  ? 207 VAL A N    1 
ATOM   2181 C  CA   . VAL A 1 206 ? -7.274  5.452   23.943  1.00 5.75  ? 207 VAL A CA   1 
ATOM   2182 C  C    . VAL A 1 206 ? -8.055  5.013   25.185  1.00 6.18  ? 207 VAL A C    1 
ATOM   2183 O  O    . VAL A 1 206 ? -7.494  4.346   26.053  1.00 6.93  ? 207 VAL A O    1 
ATOM   2184 C  CB   . VAL A 1 206 ? -7.000  4.202   23.058  1.00 6.09  ? 207 VAL A CB   1 
ATOM   2185 C  CG1  . VAL A 1 206 ? -8.322  3.469   22.758  1.00 6.07  ? 207 VAL A CG1  1 
ATOM   2186 C  CG2  . VAL A 1 206 ? -6.249  4.567   21.808  1.00 7.13  ? 207 VAL A CG2  1 
ATOM   2187 N  N    . THR A 1 207 ? -9.380  5.299   25.232  1.00 5.49  ? 208 THR A N    1 
ATOM   2188 C  CA   . THR A 1 207 ? -10.307 4.544   26.095  1.00 5.68  ? 208 THR A CA   1 
ATOM   2189 C  C    . THR A 1 207 ? -10.839 3.388   25.259  1.00 5.08  ? 208 THR A C    1 
ATOM   2190 O  O    . THR A 1 207 ? -11.497 3.616   24.240  1.00 5.59  ? 208 THR A O    1 
ATOM   2191 C  CB   . THR A 1 207 ? -11.479 5.417   26.564  1.00 5.76  ? 208 THR A CB   1 
ATOM   2192 O  OG1  . THR A 1 207 ? -10.971 6.576   27.306  1.00 6.89  ? 208 THR A OG1  1 
ATOM   2193 C  CG2  . THR A 1 207 ? -12.383 4.620   27.455  1.00 7.76  ? 208 THR A CG2  1 
ATOM   2194 N  N    . TRP A 1 208 ? -10.472 2.178   25.668  1.00 4.89  ? 209 TRP A N    1 
ATOM   2195 C  CA   . TRP A 1 208 ? -10.924 0.974   24.974  1.00 5.06  ? 209 TRP A CA   1 
ATOM   2196 C  C    . TRP A 1 208 ? -12.309 0.559   25.504  1.00 4.91  ? 209 TRP A C    1 
ATOM   2197 O  O    . TRP A 1 208 ? -12.519 0.508   26.711  1.00 5.46  ? 209 TRP A O    1 
ATOM   2198 C  CB   . TRP A 1 208 ? -9.905  -0.167  25.166  1.00 5.06  ? 209 TRP A CB   1 
ATOM   2199 C  CG   . TRP A 1 208 ? -8.787  -0.067  24.183  1.00 4.96  ? 209 TRP A CG   1 
ATOM   2200 C  CD1  . TRP A 1 208 ? -7.577  0.520   24.366  1.00 6.06  ? 209 TRP A CD1  1 
ATOM   2201 C  CD2  . TRP A 1 208 ? -8.850  -0.452  22.840  1.00 5.01  ? 209 TRP A CD2  1 
ATOM   2202 N  NE1  . TRP A 1 208 ? -6.844  0.522   23.185  1.00 5.80  ? 209 TRP A NE1  1 
ATOM   2203 C  CE2  . TRP A 1 208 ? -7.602  -0.068  22.219  1.00 5.48  ? 209 TRP A CE2  1 
ATOM   2204 C  CE3  . TRP A 1 208 ? -9.807  -1.111  22.059  1.00 4.89  ? 209 TRP A CE3  1 
ATOM   2205 C  CZ2  . TRP A 1 208 ? -7.347  -0.316  20.868  1.00 5.97  ? 209 TRP A CZ2  1 
ATOM   2206 C  CZ3  . TRP A 1 208 ? -9.546  -1.397  20.743  1.00 5.91  ? 209 TRP A CZ3  1 
ATOM   2207 C  CH2  . TRP A 1 208 ? -8.313  -0.967  20.144  1.00 6.47  ? 209 TRP A CH2  1 
ATOM   2208 N  N    . ILE A 1 209 ? -13.167 0.194   24.557  1.00 4.90  ? 210 ILE A N    1 
ATOM   2209 C  CA   . ILE A 1 209 ? -14.518 -0.334  24.852  1.00 5.20  ? 210 ILE A CA   1 
ATOM   2210 C  C    . ILE A 1 209 ? -14.638 -1.595  24.000  1.00 5.38  ? 210 ILE A C    1 
ATOM   2211 O  O    . ILE A 1 209 ? -14.756 -1.485  22.781  1.00 5.93  ? 210 ILE A O    1 
ATOM   2212 C  CB   . ILE A 1 209 ? -15.614 0.729   24.491  1.00 5.83  ? 210 ILE A CB   1 
ATOM   2213 C  CG1  . ILE A 1 209 ? -15.363 2.012   25.332  1.00 6.92  ? 210 ILE A CG1  1 
ATOM   2214 C  CG2  . ILE A 1 209 ? -16.974 0.134   24.757  1.00 7.20  ? 210 ILE A CG2  1 
ATOM   2215 C  CD1  . ILE A 1 209 ? -16.221 3.182   24.842  1.00 9.31  ? 210 ILE A CD1  1 
ATOM   2216 N  N    . VAL A 1 210 ? -14.550 -2.745  24.635  1.00 5.32  ? 211 VAL A N    1 
ATOM   2217 C  CA   . VAL A 1 210 ? -14.505 -4.056  23.938  1.00 5.19  ? 211 VAL A CA   1 
ATOM   2218 C  C    . VAL A 1 210 ? -15.819 -4.752  24.189  1.00 5.56  ? 211 VAL A C    1 
ATOM   2219 O  O    . VAL A 1 210 ? -16.163 -5.039  25.351  1.00 6.14  ? 211 VAL A O    1 
ATOM   2220 C  CB   . VAL A 1 210 ? -13.283 -4.876  24.371  1.00 5.88  ? 211 VAL A CB   1 
ATOM   2221 C  CG1  . VAL A 1 210 ? -13.301 -6.257  23.670  1.00 6.69  ? 211 VAL A CG1  1 
ATOM   2222 C  CG2  . VAL A 1 210 ? -11.980 -4.149  24.111  1.00 6.80  ? 211 VAL A CG2  1 
ATOM   2223 N  N    . LEU A 1 211 ? -16.609 -5.005  23.138  1.00 5.83  ? 212 LEU A N    1 
ATOM   2224 C  CA   . LEU A 1 211 ? -17.885 -5.664  23.305  1.00 5.99  ? 212 LEU A CA   1 
ATOM   2225 C  C    . LEU A 1 211 ? -17.671 -7.147  23.672  1.00 6.42  ? 212 LEU A C    1 
ATOM   2226 O  O    . LEU A 1 211 ? -16.823 -7.861  23.132  1.00 6.82  ? 212 LEU A O    1 
ATOM   2227 C  CB   . LEU A 1 211 ? -18.722 -5.584  22.019  1.00 6.96  ? 212 LEU A CB   1 
ATOM   2228 C  CG   . LEU A 1 211 ? -19.094 -4.154  21.627  1.00 7.56  ? 212 LEU A CG   1 
ATOM   2229 C  CD1  . LEU A 1 211 ? -20.130 -4.203  20.468  1.00 9.91  ? 212 LEU A CD1  1 
ATOM   2230 C  CD2  . LEU A 1 211 ? -19.610 -3.329  22.778  1.00 8.92  ? 212 LEU A CD2  1 
ATOM   2231 N  N    . LYS A 1 212 ? -18.552 -7.644  24.568  1.00 7.29  ? 213 LYS A N    1 
ATOM   2232 C  CA   . LYS A 1 212 ? -18.511 -9.054  24.942  1.00 7.63  ? 213 LYS A CA   1 
ATOM   2233 C  C    . LYS A 1 212 ? -19.003 -9.956  23.848  1.00 7.08  ? 213 LYS A C    1 
ATOM   2234 O  O    . LYS A 1 212 ? -18.488 -11.057 23.689  1.00 8.76  ? 213 LYS A O    1 
ATOM   2235 C  CB   . LYS A 1 212 ? -19.324 -9.277  26.227  1.00 9.42  ? 213 LYS A CB   1 
ATOM   2236 C  CG   . LYS A 1 212 ? -19.449 -10.762 26.634  1.00 11.81 ? 213 LYS A CG   1 
ATOM   2237 C  CD   . LYS A 1 212 ? -20.063 -10.996 27.981  1.00 15.99 ? 213 LYS A CD   1 
ATOM   2238 C  CE   . LYS A 1 212 ? -20.243 -12.387 28.407  1.00 21.18 ? 213 LYS A CE   1 
ATOM   2239 N  NZ   . LYS A 1 212 ? -21.077 -12.503 29.699  1.00 27.33 ? 213 LYS A NZ   1 
ATOM   2240 N  N    . GLU A 1 213 ? -20.029 -9.574  23.098  1.00 6.88  ? 214 GLU A N    1 
ATOM   2241 C  CA   . GLU A 1 213 ? -20.613 -10.434 22.077  1.00 7.56  ? 214 GLU A CA   1 
ATOM   2242 C  C    . GLU A 1 213 ? -19.876 -10.347 20.799  1.00 6.53  ? 214 GLU A C    1 
ATOM   2243 O  O    . GLU A 1 213 ? -19.806 -9.229  20.222  1.00 7.03  ? 214 GLU A O    1 
ATOM   2244 C  CB   . GLU A 1 213 ? -22.090 -10.088 21.868  1.00 8.25  ? 214 GLU A CB   1 
ATOM   2245 C  CG   . GLU A 1 213 ? -22.743 -11.020 20.877  1.00 10.37 ? 214 GLU A CG   1 
ATOM   2246 C  CD   . GLU A 1 213 ? -24.254 -10.900 20.790  1.00 13.27 ? 214 GLU A CD   1 
ATOM   2247 O  OE1  . GLU A 1 213 ? -24.841 -9.929  21.317  1.00 13.67 ? 214 GLU A OE1  1 
ATOM   2248 O  OE2  . GLU A 1 213 ? -24.857 -11.796 20.167  1.00 21.29 ? 214 GLU A OE2  1 
ATOM   2249 N  N    . PRO A 1 214 ? -19.301 -11.429 20.270  1.00 6.82  ? 215 PRO A N    1 
ATOM   2250 C  CA   . PRO A 1 214 ? -18.679 -11.384 18.955  1.00 7.10  ? 215 PRO A CA   1 
ATOM   2251 C  C    . PRO A 1 214 ? -19.686 -11.333 17.845  1.00 7.39  ? 215 PRO A C    1 
ATOM   2252 O  O    . PRO A 1 214 ? -20.862 -11.747 18.034  1.00 9.31  ? 215 PRO A O    1 
ATOM   2253 C  CB   . PRO A 1 214 ? -17.911 -12.707 18.886  1.00 7.19  ? 215 PRO A CB   1 
ATOM   2254 C  CG   . PRO A 1 214 ? -18.791 -13.656 19.665  1.00 12.01 ? 215 PRO A CG   1 
ATOM   2255 C  CD   . PRO A 1 214 ? -19.280 -12.805 20.851  1.00 8.10  ? 215 PRO A CD   1 
ATOM   2256 N  N    . ILE A 1 215 ? -19.283 -10.885 16.687  1.00 7.14  ? 216 ILE A N    1 
ATOM   2257 C  CA   . ILE A 1 215 ? -20.077 -11.107 15.473  1.00 7.34  ? 216 ILE A CA   1 
ATOM   2258 C  C    . ILE A 1 215 ? -19.511 -12.364 14.764  1.00 7.00  ? 216 ILE A C    1 
ATOM   2259 O  O    . ILE A 1 215 ? -18.360 -12.730 14.914  1.00 8.09  ? 216 ILE A O    1 
ATOM   2260 C  CB   . ILE A 1 215 ? -20.073 -9.904  14.520  1.00 8.53  ? 216 ILE A CB   1 
ATOM   2261 C  CG1  . ILE A 1 215 ? -18.656 -9.535  14.021  1.00 9.57  ? 216 ILE A CG1  1 
ATOM   2262 C  CG2  . ILE A 1 215 ? -20.764 -8.707  15.181  1.00 10.41 ? 216 ILE A CG2  1 
ATOM   2263 C  CD1  . ILE A 1 215 ? -18.626 -8.575  12.814  1.00 11.54 ? 216 ILE A CD1  1 
ATOM   2264 N  N    A SER A 1 216 ? -20.403 -13.115 14.121  0.50 7.33  ? 217 SER A N    1 
ATOM   2265 N  N    B SER A 1 216 ? -20.354 -12.929 13.931  0.50 8.88  ? 217 SER A N    1 
ATOM   2266 C  CA   A SER A 1 216 ? -20.036 -14.224 13.186  0.50 8.12  ? 217 SER A CA   1 
ATOM   2267 C  CA   B SER A 1 216 ? -19.963 -14.086 13.138  0.50 8.64  ? 217 SER A CA   1 
ATOM   2268 C  C    A SER A 1 216 ? -19.814 -13.706 11.778  0.50 8.37  ? 217 SER A C    1 
ATOM   2269 C  C    B SER A 1 216 ? -19.785 -13.657 11.708  0.50 8.62  ? 217 SER A C    1 
ATOM   2270 O  O    A SER A 1 216 ? -20.675 -12.953 11.292  0.50 8.84  ? 217 SER A O    1 
ATOM   2271 O  O    B SER A 1 216 ? -20.599 -12.926 11.138  0.50 9.16  ? 217 SER A O    1 
ATOM   2272 C  CB   A SER A 1 216 ? -21.209 -15.288 13.167  0.50 10.66 ? 217 SER A CB   1 
ATOM   2273 C  CB   B SER A 1 216 ? -21.058 -15.181 13.238  0.50 11.99 ? 217 SER A CB   1 
ATOM   2274 O  OG   A SER A 1 216 ? -21.241 -15.922 14.453  0.50 9.48  ? 217 SER A OG   1 
ATOM   2275 O  OG   B SER A 1 216 ? -20.698 -16.345 12.537  0.50 15.63 ? 217 SER A OG   1 
ATOM   2276 N  N    . VAL A 1 217 ? -18.733 -14.141 11.137  1.00 7.83  ? 218 VAL A N    1 
ATOM   2277 C  CA   . VAL A 1 217 ? -18.443 -13.974 9.727   1.00 8.46  ? 218 VAL A CA   1 
ATOM   2278 C  C    . VAL A 1 217 ? -18.194 -15.327 9.160   1.00 8.10  ? 218 VAL A C    1 
ATOM   2279 O  O    . VAL A 1 217 ? -17.816 -16.274 9.850   1.00 8.36  ? 218 VAL A O    1 
ATOM   2280 C  CB   . VAL A 1 217 ? -17.228 -13.053 9.465   1.00 9.26  ? 218 VAL A CB   1 
ATOM   2281 C  CG1  . VAL A 1 217 ? -17.465 -11.662 10.212  1.00 9.85  ? 218 VAL A CG1  1 
ATOM   2282 C  CG2  . VAL A 1 217 ? -15.904 -13.650 9.994   1.00 9.74  ? 218 VAL A CG2  1 
ATOM   2283 N  N    . SER A 1 218 ? -18.330 -15.473 7.849   1.00 8.94  ? 219 SER A N    1 
ATOM   2284 C  CA   . SER A 1 218 ? -18.137 -16.810 7.245   1.00 9.03  ? 219 SER A CA   1 
ATOM   2285 C  C    . SER A 1 218 ? -16.677 -17.055 6.958   1.00 9.22  ? 219 SER A C    1 
ATOM   2286 O  O    . SER A 1 218 ? -15.823 -16.144 6.811   1.00 9.36  ? 219 SER A O    1 
ATOM   2287 C  CB   . SER A 1 218 ? -18.921 -16.970 5.948   1.00 9.80  ? 219 SER A CB   1 
ATOM   2288 O  OG   . SER A 1 218 ? -18.459 -16.091 4.966   1.00 10.73 ? 219 SER A OG   1 
ATOM   2289 N  N    A SER A 1 219 ? -16.296 -18.320 6.814   0.50 8.48  ? 220 SER A N    1 
ATOM   2290 N  N    B SER A 1 219 ? -16.343 -18.315 6.814   0.50 8.50  ? 220 SER A N    1 
ATOM   2291 C  CA   A SER A 1 219 ? -14.931 -18.713 6.340   0.50 11.15 ? 220 SER A CA   1 
ATOM   2292 C  CA   B SER A 1 219 ? -14.987 -18.668 6.460   0.50 11.64 ? 220 SER A CA   1 
ATOM   2293 C  C    A SER A 1 219 ? -14.577 -17.968 5.098   0.50 11.17 ? 220 SER A C    1 
ATOM   2294 C  C    B SER A 1 219 ? -14.597 -18.053 5.106   0.50 10.92 ? 220 SER A C    1 
ATOM   2295 O  O    A SER A 1 219 ? -13.466 -17.359 4.953   0.50 12.18 ? 220 SER A O    1 
ATOM   2296 O  O    B SER A 1 219 ? -13.442 -17.753 4.865   0.50 11.89 ? 220 SER A O    1 
ATOM   2297 C  CB   A SER A 1 219 ? -14.845 -20.270 6.119   0.50 12.30 ? 220 SER A CB   1 
ATOM   2298 C  CB   B SER A 1 219 ? -14.840 -20.202 6.520   0.50 11.34 ? 220 SER A CB   1 
ATOM   2299 O  OG   A SER A 1 219 ? -15.893 -20.805 5.334   0.50 10.87 ? 220 SER A OG   1 
ATOM   2300 O  OG   B SER A 1 219 ? -13.539 -20.596 6.153   0.50 13.53 ? 220 SER A OG   1 
ATOM   2301 N  N    . GLU A 1 220 ? -15.532 -17.930 4.153   1.00 10.49 ? 221 GLU A N    1 
ATOM   2302 C  CA   . GLU A 1 220 ? -15.297 -17.289 2.896   1.00 12.04 ? 221 GLU A CA   1 
ATOM   2303 C  C    . GLU A 1 220 ? -14.979 -15.816 3.055   1.00 11.35 ? 221 GLU A C    1 
ATOM   2304 O  O    . GLU A 1 220 ? -14.126 -15.276 2.306   1.00 12.43 ? 221 GLU A O    1 
ATOM   2305 C  CB   . GLU A 1 220 ? -16.434 -17.450 1.912   1.00 13.45 ? 221 GLU A CB   1 
ATOM   2306 C  CG   . GLU A 1 220 ? -16.738 -18.930 1.494   1.00 16.80 ? 221 GLU A CG   1 
ATOM   2307 C  CD   . GLU A 1 220 ? -17.639 -19.683 2.449   1.00 23.26 ? 221 GLU A CD   1 
ATOM   2308 O  OE1  . GLU A 1 220 ? -18.094 -19.195 3.481   1.00 16.90 ? 221 GLU A OE1  1 
ATOM   2309 O  OE2  . GLU A 1 220 ? -17.894 -20.926 2.237   1.00 32.91 ? 221 GLU A OE2  1 
ATOM   2310 N  N    . GLN A 1 221 ? -15.675 -15.132 3.951   1.00 10.20 ? 222 GLN A N    1 
ATOM   2311 C  CA   . GLN A 1 221 ? -15.369 -13.718 4.178   1.00 10.10 ? 222 GLN A CA   1 
ATOM   2312 C  C    . GLN A 1 221 ? -13.971 -13.507 4.723   1.00 10.19 ? 222 GLN A C    1 
ATOM   2313 O  O    . GLN A 1 221 ? -13.192 -12.657 4.218   1.00 10.71 ? 222 GLN A O    1 
ATOM   2314 C  CB   . GLN A 1 221 ? -16.444 -13.131 5.113   1.00 9.83  ? 222 GLN A CB   1 
ATOM   2315 C  CG   . GLN A 1 221 ? -17.828 -12.988 4.415   1.00 9.66  ? 222 GLN A CG   1 
ATOM   2316 C  CD   . GLN A 1 221 ? -18.922 -12.433 5.272   1.00 9.44  ? 222 GLN A CD   1 
ATOM   2317 O  OE1  . GLN A 1 221 ? -19.049 -12.827 6.483   1.00 9.82  ? 222 GLN A OE1  1 
ATOM   2318 N  NE2  . GLN A 1 221 ? -19.747 -11.563 4.766   1.00 10.81 ? 222 GLN A NE2  1 
ATOM   2319 N  N    . VAL A 1 222 ? -13.591 -14.263 5.758   1.00 10.10 ? 223 VAL A N    1 
ATOM   2320 C  CA   . VAL A 1 222 ? -12.236 -14.084 6.289   1.00 10.99 ? 223 VAL A CA   1 
ATOM   2321 C  C    . VAL A 1 222 ? -11.127 -14.539 5.299   1.00 10.23 ? 223 VAL A C    1 
ATOM   2322 O  O    . VAL A 1 222 ? -10.044 -13.971 5.246   1.00 11.28 ? 223 VAL A O    1 
ATOM   2323 C  CB   . VAL A 1 222 ? -12.061 -14.675 7.691   1.00 13.28 ? 223 VAL A CB   1 
ATOM   2324 C  CG1  . VAL A 1 222 ? -12.085 -16.183 7.714   1.00 15.67 ? 223 VAL A CG1  1 
ATOM   2325 C  CG2  . VAL A 1 222 ? -10.791 -14.090 8.426   1.00 14.03 ? 223 VAL A CG2  1 
ATOM   2326 N  N    . LEU A 1 223 ? -11.424 -15.568 4.507   1.00 11.68 ? 224 LEU A N    1 
ATOM   2327 C  CA   . LEU A 1 223 ? -10.459 -15.974 3.496   1.00 13.07 ? 224 LEU A CA   1 
ATOM   2328 C  C    . LEU A 1 223 ? -10.140 -14.849 2.545   1.00 12.75 ? 224 LEU A C    1 
ATOM   2329 O  O    . LEU A 1 223 ? -9.004  -14.720 2.071   1.00 14.04 ? 224 LEU A O    1 
ATOM   2330 C  CB   . LEU A 1 223 ? -10.970 -17.242 2.752   1.00 15.50 ? 224 LEU A CB   1 
ATOM   2331 C  CG   . LEU A 1 223 ? -10.734 -18.539 3.604   1.00 17.28 ? 224 LEU A CG   1 
ATOM   2332 C  CD1  . LEU A 1 223 ? -11.656 -19.639 3.082   1.00 22.29 ? 224 LEU A CD1  1 
ATOM   2333 C  CD2  . LEU A 1 223 ? -9.198  -18.975 3.664   1.00 19.84 ? 224 LEU A CD2  1 
ATOM   2334 N  N    . LYS A 1 224 ? -11.118 -14.003 2.212   1.00 11.91 ? 225 LYS A N    1 
ATOM   2335 C  CA   . LYS A 1 224 ? -10.857 -12.856 1.358   1.00 13.04 ? 225 LYS A CA   1 
ATOM   2336 C  C    . LYS A 1 224 ? -10.001 -11.780 2.025   1.00 11.23 ? 225 LYS A C    1 
ATOM   2337 O  O    . LYS A 1 224 ? -9.155  -11.172 1.358   1.00 12.60 ? 225 LYS A O    1 
ATOM   2338 C  CB   . LYS A 1 224 ? -12.175 -12.333 0.771   1.00 15.82 ? 225 LYS A CB   1 
ATOM   2339 C  CG   . LYS A 1 224 ? -12.739 -13.421 -0.290  1.00 17.61 ? 225 LYS A CG   1 
ATOM   2340 C  CD   . LYS A 1 224 ? -14.168 -13.203 -0.866  1.00 19.16 ? 225 LYS A CD   1 
ATOM   2341 C  CE   . LYS A 1 224 ? -14.598 -14.147 -2.007  1.00 21.00 ? 225 LYS A CE   1 
ATOM   2342 N  NZ   . LYS A 1 224 ? -15.940 -13.796 -2.694  1.00 24.73 ? 225 LYS A NZ   1 
ATOM   2343 N  N    . PHE A 1 225 ? -10.113 -11.593 3.347   1.00 10.03 ? 226 PHE A N    1 
ATOM   2344 C  CA   . PHE A 1 225 ? -9.218  -10.709 4.038   1.00 10.29 ? 226 PHE A CA   1 
ATOM   2345 C  C    . PHE A 1 225 ? -7.784  -11.228 3.788   1.00 9.89  ? 226 PHE A C    1 
ATOM   2346 O  O    . PHE A 1 225 ? -6.827  -10.458 3.549   1.00 10.54 ? 226 PHE A O    1 
ATOM   2347 C  CB   . PHE A 1 225 ? -9.389  -10.749 5.572   1.00 9.81  ? 226 PHE A CB   1 
ATOM   2348 C  CG   . PHE A 1 225 ? -10.574 -9.983  6.110   1.00 10.22 ? 226 PHE A CG   1 
ATOM   2349 C  CD1  . PHE A 1 225 ? -11.589 -9.500  5.299   1.00 13.31 ? 226 PHE A CD1  1 
ATOM   2350 C  CD2  . PHE A 1 225 ? -10.667 -9.777  7.479   1.00 13.45 ? 226 PHE A CD2  1 
ATOM   2351 C  CE1  . PHE A 1 225 ? -12.669 -8.811  5.859   1.00 14.53 ? 226 PHE A CE1  1 
ATOM   2352 C  CE2  . PHE A 1 225 ? -11.727 -9.101  8.037   1.00 14.49 ? 226 PHE A CE2  1 
ATOM   2353 C  CZ   . PHE A 1 225 ? -12.731 -8.614  7.234   1.00 13.72 ? 226 PHE A CZ   1 
ATOM   2354 N  N    . ARG A 1 226 ? -7.572  -12.559 3.881   1.00 9.26  ? 227 ARG A N    1 
ATOM   2355 C  CA   . ARG A 1 226 ? -6.285  -13.172 3.794   1.00 10.16 ? 227 ARG A CA   1 
ATOM   2356 C  C    . ARG A 1 226 ? -5.657  -13.173 2.394   1.00 11.18 ? 227 ARG A C    1 
ATOM   2357 O  O    . ARG A 1 226 ? -4.511  -13.593 2.281   1.00 11.83 ? 227 ARG A O    1 
ATOM   2358 C  CB   . ARG A 1 226 ? -6.306  -14.606 4.390   1.00 10.54 ? 227 ARG A CB   1 
ATOM   2359 C  CG   . ARG A 1 226 ? -6.759  -14.731 5.833   1.00 10.41 ? 227 ARG A CG   1 
ATOM   2360 C  CD   . ARG A 1 226 ? -6.701  -16.196 6.282   1.00 12.41 ? 227 ARG A CD   1 
ATOM   2361 N  NE   . ARG A 1 226 ? -7.248  -16.342 7.645   1.00 10.37 ? 227 ARG A NE   1 
ATOM   2362 C  CZ   . ARG A 1 226 ? -8.160  -17.221 8.024   1.00 11.60 ? 227 ARG A CZ   1 
ATOM   2363 N  NH1  . ARG A 1 226 ? -8.682  -18.101 7.173   1.00 14.78 ? 227 ARG A NH1  1 
ATOM   2364 N  NH2  . ARG A 1 226 ? -8.679  -17.194 9.204   1.00 11.84 ? 227 ARG A NH2  1 
ATOM   2365 N  N    . LYS A 1 227 ? -6.395  -12.731 1.396   1.00 9.93  ? 228 LYS A N    1 
ATOM   2366 C  CA   . LYS A 1 227 ? -5.867  -12.570 0.036   1.00 12.20 ? 228 LYS A CA   1 
ATOM   2367 C  C    . LYS A 1 227 ? -5.215  -11.197 -0.176  1.00 11.51 ? 228 LYS A C    1 
ATOM   2368 O  O    . LYS A 1 227 ? -4.562  -10.994 -1.206  1.00 13.58 ? 228 LYS A O    1 
ATOM   2369 C  CB   . LYS A 1 227 ? -6.993  -12.800 -1.014  1.00 12.65 ? 228 LYS A CB   1 
ATOM   2370 C  CG   . LYS A 1 227 ? -7.480  -14.187 -1.016  1.00 15.40 ? 228 LYS A CG   1 
ATOM   2371 C  CD   . LYS A 1 227 ? -8.549  -14.364 -2.112  1.00 19.94 ? 228 LYS A CD   1 
ATOM   2372 C  CE   . LYS A 1 227 ? -8.049  -14.230 -3.511  1.00 26.43 ? 228 LYS A CE   1 
ATOM   2373 N  NZ   . LYS A 1 227 ? -9.056  -14.655 -4.484  1.00 33.28 ? 228 LYS A NZ   1 
ATOM   2374 N  N    A LEU A 1 228 ? -5.201  -10.301 0.822   0.50 10.67 ? 229 LEU A N    1 
ATOM   2375 N  N    B LEU A 1 228 ? -5.578  -10.225 0.699   0.50 8.65  ? 229 LEU A N    1 
ATOM   2376 C  CA   A LEU A 1 228 ? -4.349  -9.084  0.737   0.50 10.35 ? 229 LEU A CA   1 
ATOM   2377 C  CA   B LEU A 1 228 ? -4.964  -8.930  0.642   0.50 8.65  ? 229 LEU A CA   1 
ATOM   2378 C  C    A LEU A 1 228 ? -2.826  -9.333  0.892   0.50 11.19 ? 229 LEU A C    1 
ATOM   2379 C  C    B LEU A 1 228 ? -3.461  -9.092  0.730   0.50 7.44  ? 229 LEU A C    1 
ATOM   2380 O  O    A LEU A 1 228 ? -2.402  -10.395 1.356   0.50 11.41 ? 229 LEU A O    1 
ATOM   2381 O  O    B LEU A 1 228 ? -2.904  -10.152 1.171   0.50 7.48  ? 229 LEU A O    1 
ATOM   2382 C  CB   A LEU A 1 228 ? -4.852  -8.076  1.795   0.50 11.41 ? 229 LEU A CB   1 
ATOM   2383 C  CB   B LEU A 1 228 ? -5.470  -8.021  1.768   0.50 7.49  ? 229 LEU A CB   1 
ATOM   2384 C  CG   A LEU A 1 228 ? -6.293  -7.626  1.561   0.50 11.95 ? 229 LEU A CG   1 
ATOM   2385 C  CG   B LEU A 1 228 ? -6.911  -7.568  1.551   0.50 8.14  ? 229 LEU A CG   1 
ATOM   2386 C  CD1  A LEU A 1 228 ? -6.879  -7.094  2.911   0.50 12.79 ? 229 LEU A CD1  1 
ATOM   2387 C  CD1  B LEU A 1 228 ? -7.451  -6.867  2.847   0.50 9.42  ? 229 LEU A CD1  1 
ATOM   2388 C  CD2  A LEU A 1 228 ? -6.241  -6.455  0.521   0.50 12.83 ? 229 LEU A CD2  1 
ATOM   2389 C  CD2  B LEU A 1 228 ? -7.084  -6.491  0.371   0.50 9.36  ? 229 LEU A CD2  1 
ATOM   2390 N  N    A ASN A 1 229 ? -2.036  -8.297  0.549   0.50 10.15 ? 230 ASN A N    1 
ATOM   2391 N  N    B ASN A 1 229 ? -2.765  -8.005  0.335   0.50 7.24  ? 230 ASN A N    1 
ATOM   2392 C  CA   A ASN A 1 229 ? -0.599  -8.360  0.612   0.50 9.26  ? 230 ASN A CA   1 
ATOM   2393 C  CA   B ASN A 1 229 ? -1.324  -8.003  0.380   0.50 6.67  ? 230 ASN A CA   1 
ATOM   2394 C  C    A ASN A 1 229 ? -0.070  -7.249  1.500   0.50 8.74  ? 230 ASN A C    1 
ATOM   2395 C  C    B ASN A 1 229 ? -0.804  -6.849  1.194   0.50 6.96  ? 230 ASN A C    1 
ATOM   2396 O  O    A ASN A 1 229 ? -0.538  -6.073  1.437   0.50 8.12  ? 230 ASN A O    1 
ATOM   2397 O  O    B ASN A 1 229 ? -1.300  -5.728  1.126   0.50 6.53  ? 230 ASN A O    1 
ATOM   2398 C  CB   A ASN A 1 229 ? 0.041   -8.142  -0.778  0.50 9.99  ? 230 ASN A CB   1 
ATOM   2399 C  CB   B ASN A 1 229 ? -0.734  -7.854  -1.085  0.50 7.17  ? 230 ASN A CB   1 
ATOM   2400 C  CG   A ASN A 1 229 ? -0.227  -9.244  -1.780  0.50 11.75 ? 230 ASN A CG   1 
ATOM   2401 C  CG   B ASN A 1 229 ? -0.921  -9.051  -1.997  0.50 11.67 ? 230 ASN A CG   1 
ATOM   2402 O  OD1  A ASN A 1 229 ? -0.783  -10.324 -1.440  0.50 16.82 ? 230 ASN A OD1  1 
ATOM   2403 O  OD1  B ASN A 1 229 ? -1.361  -10.167 -1.630  0.50 10.96 ? 230 ASN A OD1  1 
ATOM   2404 N  ND2  A ASN A 1 229 ? 0.183   -9.020  -2.984  0.50 11.22 ? 230 ASN A ND2  1 
ATOM   2405 N  ND2  B ASN A 1 229 ? -0.458  -8.860  -3.182  0.50 12.14 ? 230 ASN A ND2  1 
ATOM   2406 N  N    A PHE A 1 230 ? 0.946   -7.540  2.276   0.50 9.41  ? 231 PHE A N    1 
ATOM   2407 N  N    B PHE A 1 230 ? 0.264   -7.124  1.977   0.50 7.64  ? 231 PHE A N    1 
ATOM   2408 C  CA   A PHE A 1 230 ? 1.686   -6.477  2.961   0.50 10.56 ? 231 PHE A CA   1 
ATOM   2409 C  CA   B PHE A 1 230 ? 1.011   -6.046  2.658   0.50 6.85  ? 231 PHE A CA   1 
ATOM   2410 C  C    A PHE A 1 230 ? 2.532   -5.688  1.987   0.50 11.17 ? 231 PHE A C    1 
ATOM   2411 C  C    B PHE A 1 230 ? 1.843   -5.261  1.650   0.50 8.40  ? 231 PHE A C    1 
ATOM   2412 O  O    A PHE A 1 230 ? 2.748   -4.466  2.179   0.50 12.03 ? 231 PHE A O    1 
ATOM   2413 O  O    B PHE A 1 230 ? 2.183   -4.087  1.887   0.50 10.54 ? 231 PHE A O    1 
ATOM   2414 C  CB   A PHE A 1 230 ? 2.660   -7.112  3.938   0.50 10.75 ? 231 PHE A CB   1 
ATOM   2415 C  CB   B PHE A 1 230 ? 1.993   -6.603  3.677   0.50 8.04  ? 231 PHE A CB   1 
ATOM   2416 C  CG   A PHE A 1 230 ? 2.028   -7.672  5.222   0.50 11.36 ? 231 PHE A CG   1 
ATOM   2417 C  CG   B PHE A 1 230 ? 1.425   -7.219  4.963   0.50 7.64  ? 231 PHE A CG   1 
ATOM   2418 C  CD1  A PHE A 1 230 ? 1.263   -6.869  6.110   0.50 11.11 ? 231 PHE A CD1  1 
ATOM   2419 C  CD1  B PHE A 1 230 ? 0.623   -6.465  5.806   0.50 8.00  ? 231 PHE A CD1  1 
ATOM   2420 C  CD2  A PHE A 1 230 ? 2.314   -8.969  5.599   0.50 12.11 ? 231 PHE A CD2  1 
ATOM   2421 C  CD2  B PHE A 1 230 ? 1.772   -8.522  5.317   0.50 8.60  ? 231 PHE A CD2  1 
ATOM   2422 C  CE1  A PHE A 1 230 ? 0.765   -7.366  7.285   0.50 10.11 ? 231 PHE A CE1  1 
ATOM   2423 C  CE1  B PHE A 1 230 ? 0.162   -7.001  6.985   0.50 9.82  ? 231 PHE A CE1  1 
ATOM   2424 C  CE2  A PHE A 1 230 ? 1.821   -9.466  6.821   0.50 11.28 ? 231 PHE A CE2  1 
ATOM   2425 C  CE2  B PHE A 1 230 ? 1.288   -9.066  6.547   0.50 8.45  ? 231 PHE A CE2  1 
ATOM   2426 C  CZ   A PHE A 1 230 ? 1.048   -8.674  7.669   0.50 10.94 ? 231 PHE A CZ   1 
ATOM   2427 C  CZ   B PHE A 1 230 ? 0.506   -8.307  7.374   0.50 9.50  ? 231 PHE A CZ   1 
ATOM   2428 N  N    A ASN A 1 231 ? 3.091   -6.336  0.988   0.50 10.21 ? 232 ASN A N    1 
ATOM   2429 N  N    B ASN A 1 231 ? 2.387   -5.954  0.636   0.50 8.54  ? 232 ASN A N    1 
ATOM   2430 C  CA   A ASN A 1 231 ? 4.035   -5.766  -0.020  0.50 10.62 ? 232 ASN A CA   1 
ATOM   2431 C  CA   B ASN A 1 231 ? 3.243   -5.379  -0.393  0.50 8.59  ? 232 ASN A CA   1 
ATOM   2432 C  C    A ASN A 1 231 ? 3.301   -4.829  -0.975  0.50 11.24 ? 232 ASN A C    1 
ATOM   2433 C  C    B ASN A 1 231 ? 2.471   -4.453  -1.300  0.50 8.17  ? 232 ASN A C    1 
ATOM   2434 O  O    A ASN A 1 231 ? 2.069   -4.908  -1.211  0.50 10.16 ? 232 ASN A O    1 
ATOM   2435 O  O    B ASN A 1 231 ? 1.218   -4.507  -1.416  0.50 9.18  ? 232 ASN A O    1 
ATOM   2436 C  CB   A ASN A 1 231 ? 4.706   -6.883  -0.819  0.50 10.47 ? 232 ASN A CB   1 
ATOM   2437 C  CB   B ASN A 1 231 ? 3.866   -6.521  -1.271  0.50 8.50  ? 232 ASN A CB   1 
ATOM   2438 C  CG   A ASN A 1 231 ? 3.705   -7.828  -1.396  0.50 11.16 ? 232 ASN A CG   1 
ATOM   2439 C  CG   B ASN A 1 231 ? 2.842   -7.435  -1.807  0.50 8.61  ? 232 ASN A CG   1 
ATOM   2440 O  OD1  A ASN A 1 231 ? 3.182   -8.691  -0.718  0.50 10.02 ? 232 ASN A OD1  1 
ATOM   2441 O  OD1  B ASN A 1 231 ? 2.293   -8.267  -1.080  0.50 9.52  ? 232 ASN A OD1  1 
ATOM   2442 N  ND2  A ASN A 1 231 ? 3.436   -7.685  -2.688  0.50 11.67 ? 232 ASN A ND2  1 
ATOM   2443 N  ND2  B ASN A 1 231 ? 2.528   -7.282  -3.091  0.50 10.67 ? 232 ASN A ND2  1 
ATOM   2444 N  N    A GLY A 1 232 ? 4.118   -3.977  -1.552  0.50 11.63 ? 233 GLY A N    1 
ATOM   2445 N  N    B GLY A 1 232 ? 3.234   -3.591  -2.004  0.50 8.25  ? 233 GLY A N    1 
ATOM   2446 C  CA   A GLY A 1 232 ? 3.662   -3.196  -2.743  0.50 13.64 ? 233 GLY A CA   1 
ATOM   2447 C  CA   B GLY A 1 232 ? 2.732   -2.855  -3.102  0.50 8.79  ? 233 GLY A CA   1 
ATOM   2448 C  C    A GLY A 1 232 ? 3.465   -3.927  -4.107  0.50 15.27 ? 233 GLY A C    1 
ATOM   2449 C  C    B GLY A 1 232 ? 2.717   -3.611  -4.415  0.50 9.90  ? 233 GLY A C    1 
ATOM   2450 O  O    A GLY A 1 232 ? 4.015   -5.054  -4.264  0.50 17.92 ? 233 GLY A O    1 
ATOM   2451 O  O    B GLY A 1 232 ? 3.329   -4.602  -4.534  0.50 11.49 ? 233 GLY A O    1 
ATOM   2452 N  N    A GLU A 1 233 ? 2.617   -3.334  -5.035  0.50 16.19 ? 234 GLU A N    1 
ATOM   2453 N  N    B GLU A 1 233 ? 1.971   -3.075  -5.417  0.50 9.32  ? 234 GLU A N    1 
ATOM   2454 C  CA   A GLU A 1 233 ? 2.327   -3.820  -6.452  0.50 16.21 ? 234 GLU A CA   1 
ATOM   2455 C  CA   B GLU A 1 233 ? 1.933   -3.653  -6.797  0.50 9.93  ? 234 GLU A CA   1 
ATOM   2456 C  C    A GLU A 1 233 ? 3.658   -3.997  -7.132  0.50 17.27 ? 234 GLU A C    1 
ATOM   2457 C  C    B GLU A 1 233 ? 3.383   -3.656  -7.341  0.50 11.55 ? 234 GLU A C    1 
ATOM   2458 O  O    A GLU A 1 233 ? 4.696   -3.262  -6.895  0.50 18.36 ? 234 GLU A O    1 
ATOM   2459 O  O    B GLU A 1 233 ? 4.157   -2.728  -7.125  0.50 12.39 ? 234 GLU A O    1 
ATOM   2460 C  CB   A GLU A 1 233 ? 1.336   -2.869  -7.273  0.50 15.42 ? 234 GLU A CB   1 
ATOM   2461 C  CB   B GLU A 1 233 ? 1.007   -2.890  -7.690  0.50 10.90 ? 234 GLU A CB   1 
ATOM   2462 C  CG   A GLU A 1 233 ? 0.947   -3.245  -8.794  0.50 16.43 ? 234 GLU A CG   1 
ATOM   2463 C  CG   B GLU A 1 233 ? 0.826   -3.520  -9.109  0.50 11.30 ? 234 GLU A CG   1 
ATOM   2464 C  CD   A GLU A 1 233 ? 0.021   -2.247  -9.568  0.50 16.80 ? 234 GLU A CD   1 
ATOM   2465 C  CD   B GLU A 1 233 ? -0.097  -2.759  -9.986  0.50 15.67 ? 234 GLU A CD   1 
ATOM   2466 O  OE1  A GLU A 1 233 ? -0.234  -1.098  -9.181  0.50 17.19 ? 234 GLU A OE1  1 
ATOM   2467 O  OE1  B GLU A 1 233 ? -0.761  -1.842  -9.463  0.50 26.29 ? 234 GLU A OE1  1 
ATOM   2468 O  OE2  A GLU A 1 233 ? -0.493  -2.634  -10.693 0.50 18.88 ? 234 GLU A OE2  1 
ATOM   2469 O  OE2  B GLU A 1 233 ? -0.040  -2.939  -11.227 0.50 15.34 ? 234 GLU A OE2  1 
ATOM   2470 N  N    A GLY A 1 234 ? 3.654   -5.026  -7.974  0.50 14.94 ? 235 GLY A N    1 
ATOM   2471 N  N    B GLY A 1 234 ? 3.828   -4.787  -7.897  0.50 16.39 ? 235 GLY A N    1 
ATOM   2472 C  CA   A GLY A 1 234 ? 4.874   -5.236  -8.730  0.50 14.04 ? 235 GLY A CA   1 
ATOM   2473 C  CA   B GLY A 1 234 ? 5.244   -4.923  -8.359  0.50 16.50 ? 235 GLY A CA   1 
ATOM   2474 C  C    A GLY A 1 234 ? 5.942   -5.633  -7.717  0.50 12.25 ? 235 GLY A C    1 
ATOM   2475 C  C    B GLY A 1 234 ? 6.348   -5.251  -7.341  0.50 18.96 ? 235 GLY A C    1 
ATOM   2476 O  O    A GLY A 1 234 ? 7.144   -5.717  -8.042  0.50 14.62 ? 235 GLY A O    1 
ATOM   2477 O  O    B GLY A 1 234 ? 7.515   -4.947  -7.658  0.50 20.20 ? 235 GLY A O    1 
ATOM   2478 N  N    A GLU A 1 235 ? 5.566   -5.900  -6.441  0.50 11.83 ? 236 GLU A N    1 
ATOM   2479 N  N    B GLU A 1 235 ? 6.022   -5.884  -6.157  0.50 18.52 ? 236 GLU A N    1 
ATOM   2480 C  CA   A GLU A 1 235 ? 6.526   -6.416  -5.454  0.50 9.61  ? 236 GLU A CA   1 
ATOM   2481 C  CA   B GLU A 1 235 ? 7.010   -6.536  -5.191  0.50 17.44 ? 236 GLU A CA   1 
ATOM   2482 C  C    A GLU A 1 235 ? 6.065   -7.806  -5.109  0.50 12.36 ? 236 GLU A C    1 
ATOM   2483 C  C    B GLU A 1 235 ? 6.784   -8.055  -4.807  0.50 16.03 ? 236 GLU A C    1 
ATOM   2484 O  O    A GLU A 1 235 ? 4.911   -8.158  -5.271  0.50 11.48 ? 236 GLU A O    1 
ATOM   2485 O  O    B GLU A 1 235 ? 5.760   -8.626  -5.034  0.50 18.14 ? 236 GLU A O    1 
ATOM   2486 C  CB   A GLU A 1 235 ? 6.369   -5.621  -4.158  0.50 10.61 ? 236 GLU A CB   1 
ATOM   2487 C  CB   B GLU A 1 235 ? 7.036   -5.828  -3.806  0.50 18.03 ? 236 GLU A CB   1 
ATOM   2488 C  CG   A GLU A 1 235 ? 6.938   -4.198  -4.247  0.50 11.33 ? 236 GLU A CG   1 
ATOM   2489 C  CG   B GLU A 1 235 ? 7.941   -4.640  -3.648  0.50 17.30 ? 236 GLU A CG   1 
ATOM   2490 C  CD   A GLU A 1 235 ? 6.673   -3.316  -3.089  0.50 11.82 ? 236 GLU A CD   1 
ATOM   2491 C  CD   B GLU A 1 235 ? 7.635   -3.772  -2.447  0.50 18.00 ? 236 GLU A CD   1 
ATOM   2492 O  OE1  A GLU A 1 235 ? 6.109   -3.757  -2.067  0.50 11.37 ? 236 GLU A OE1  1 
ATOM   2493 O  OE1  B GLU A 1 235 ? 7.163   -4.304  -1.364  0.50 19.83 ? 236 GLU A OE1  1 
ATOM   2494 O  OE2  A GLU A 1 235 ? 6.966   -2.101  -3.277  0.50 19.13 ? 236 GLU A OE2  1 
ATOM   2495 O  OE2  B GLU A 1 235 ? 7.880   -2.540  -2.634  0.50 21.62 ? 236 GLU A OE2  1 
ATOM   2496 N  N    A PRO A 1 236 ? 6.949   -8.645  -4.635  0.50 9.45  ? 237 PRO A N    1 
ATOM   2497 N  N    B PRO A 1 236 ? 7.775   -8.681  -4.189  0.50 15.77 ? 237 PRO A N    1 
ATOM   2498 C  CA   A PRO A 1 236 ? 6.600   -10.072 -4.271  0.50 10.84 ? 237 PRO A CA   1 
ATOM   2499 C  CA   B PRO A 1 236 ? 7.584   -10.083 -3.769  0.50 15.90 ? 237 PRO A CA   1 
ATOM   2500 C  C    A PRO A 1 236 ? 5.548   -10.100 -3.253  0.50 10.04 ? 237 PRO A C    1 
ATOM   2501 C  C    B PRO A 1 236 ? 6.245   -10.260 -3.032  0.50 14.09 ? 237 PRO A C    1 
ATOM   2502 O  O    A PRO A 1 236 ? 5.467   -9.293  -2.328  0.50 12.67 ? 237 PRO A O    1 
ATOM   2503 O  O    B PRO A 1 236 ? 5.784   -9.272  -2.460  0.50 15.45 ? 237 PRO A O    1 
ATOM   2504 C  CB   A PRO A 1 236 ? 7.887   -10.676 -3.679  0.50 9.90  ? 237 PRO A CB   1 
ATOM   2505 C  CB   B PRO A 1 236 ? 8.755   -10.317 -2.819  0.50 16.57 ? 237 PRO A CB   1 
ATOM   2506 C  CG   A PRO A 1 236 ? 8.891   -9.422  -3.854  0.50 14.24 ? 237 PRO A CG   1 
ATOM   2507 C  CG   B PRO A 1 236 ? 9.826   -9.413  -3.330  0.50 15.75 ? 237 PRO A CG   1 
ATOM   2508 C  CD   A PRO A 1 236 ? 8.423   -8.518  -4.709  0.50 12.72 ? 237 PRO A CD   1 
ATOM   2509 C  CD   B PRO A 1 236 ? 9.133   -8.194  -3.887  0.50 16.69 ? 237 PRO A CD   1 
ATOM   2510 N  N    A GLU A 1 237 ? 4.722   -11.092 -3.445  0.50 9.05  ? 238 GLU A N    1 
ATOM   2511 N  N    B GLU A 1 237 ? 5.622   -11.446 -3.035  0.50 11.69 ? 238 GLU A N    1 
ATOM   2512 C  CA   A GLU A 1 237 ? 3.506   -11.190 -2.672  0.50 9.41  ? 238 GLU A CA   1 
ATOM   2513 C  CA   B GLU A 1 237 ? 4.317   -11.552 -2.380  0.50 11.19 ? 238 GLU A CA   1 
ATOM   2514 C  C    A GLU A 1 237 ? 3.764   -11.536 -1.205  0.50 8.51  ? 238 GLU A C    1 
ATOM   2515 C  C    B GLU A 1 237 ? 4.438   -12.095 -0.981  0.50 10.38 ? 238 GLU A C    1 
ATOM   2516 O  O    A GLU A 1 237 ? 4.369   -12.553 -0.978  0.50 9.01  ? 238 GLU A O    1 
ATOM   2517 O  O    B GLU A 1 237 ? 4.874   -13.247 -0.806  0.50 10.01 ? 238 GLU A O    1 
ATOM   2518 C  CB   A GLU A 1 237 ? 2.562   -12.229 -3.293  0.50 9.91  ? 238 GLU A CB   1 
ATOM   2519 C  CB   B GLU A 1 237 ? 3.320   -12.398 -3.182  0.50 11.10 ? 238 GLU A CB   1 
ATOM   2520 C  CG   A GLU A 1 237 ? 1.112   -12.079 -2.674  0.50 10.58 ? 238 GLU A CG   1 
ATOM   2521 C  CG   B GLU A 1 237 ? 1.939   -12.448 -2.510  0.50 11.04 ? 238 GLU A CG   1 
ATOM   2522 C  CD   A GLU A 1 237 ? 0.066   -12.957 -3.221  0.50 11.45 ? 238 GLU A CD   1 
ATOM   2523 C  CD   B GLU A 1 237 ? 0.834   -13.028 -3.321  0.50 11.84 ? 238 GLU A CD   1 
ATOM   2524 O  OE1  A GLU A 1 237 ? 0.395   -14.118 -3.593  0.50 15.33 ? 238 GLU A OE1  1 
ATOM   2525 O  OE1  B GLU A 1 237 ? 1.113   -13.955 -4.149  0.50 16.14 ? 238 GLU A OE1  1 
ATOM   2526 O  OE2  A GLU A 1 237 ? -1.072  -12.439 -3.367  0.50 10.63 ? 238 GLU A OE2  1 
ATOM   2527 O  OE2  B GLU A 1 237 ? -0.362  -12.545 -3.193  0.50 13.58 ? 238 GLU A OE2  1 
ATOM   2528 N  N    A GLU A 1 238 ? 3.266   -10.753 -0.262  0.50 6.71  ? 239 GLU A N    1 
ATOM   2529 N  N    B GLU A 1 238 ? 3.942   -11.288 -0.024  0.50 8.55  ? 239 GLU A N    1 
ATOM   2530 C  CA   A GLU A 1 238 ? 3.257   -11.018 1.159   0.50 7.40  ? 239 GLU A CA   1 
ATOM   2531 C  CA   B GLU A 1 238 ? 3.851   -11.694 1.358   0.50 9.27  ? 239 GLU A CA   1 
ATOM   2532 C  C    A GLU A 1 238 ? 1.791   -10.921 1.581   0.50 7.59  ? 239 GLU A C    1 
ATOM   2533 C  C    B GLU A 1 238 ? 2.445   -11.464 1.764   0.50 8.24  ? 239 GLU A C    1 
ATOM   2534 O  O    A GLU A 1 238 ? 1.248   -9.827  1.671   0.50 8.28  ? 239 GLU A O    1 
ATOM   2535 O  O    B GLU A 1 238 ? 2.009   -10.283 1.856   0.50 8.89  ? 239 GLU A O    1 
ATOM   2536 C  CB   A GLU A 1 238 ? 4.115   -10.012 1.935   0.50 8.67  ? 239 GLU A CB   1 
ATOM   2537 C  CB   B GLU A 1 238 ? 4.811   -10.881 2.160   0.50 9.67  ? 239 GLU A CB   1 
ATOM   2538 C  CG   A GLU A 1 238 ? 5.564   -9.865  1.610   0.50 14.44 ? 239 GLU A CG   1 
ATOM   2539 C  CG   B GLU A 1 238 ? 6.310   -11.286 1.921   0.50 11.70 ? 239 GLU A CG   1 
ATOM   2540 C  CD   A GLU A 1 238 ? 6.257   -8.645  2.244   0.50 15.95 ? 239 GLU A CD   1 
ATOM   2541 C  CD   B GLU A 1 238 ? 7.268   -10.621 2.878   0.50 11.87 ? 239 GLU A CD   1 
ATOM   2542 O  OE1  A GLU A 1 238 ? 5.684   -7.924  3.107   0.50 17.14 ? 239 GLU A OE1  1 
ATOM   2543 O  OE1  B GLU A 1 238 ? 7.254   -10.919 4.102   0.50 12.35 ? 239 GLU A OE1  1 
ATOM   2544 O  OE2  A GLU A 1 238 ? 7.428   -8.471  1.957   0.50 21.11 ? 239 GLU A OE2  1 
ATOM   2545 O  OE2  B GLU A 1 238 ? 8.020   -9.717  2.468   0.50 11.85 ? 239 GLU A OE2  1 
ATOM   2546 N  N    A LEU A 1 239 ? 1.159   -12.055 1.846   0.50 6.66  ? 240 LEU A N    1 
ATOM   2547 N  N    B LEU A 1 239 ? 1.733   -12.535 2.062   0.50 8.29  ? 240 LEU A N    1 
ATOM   2548 C  CA   A LEU A 1 239 ? -0.228  -12.038 2.219   0.50 5.91  ? 240 LEU A CA   1 
ATOM   2549 C  CA   B LEU A 1 239 ? 0.314   -12.376 2.375   0.50 8.56  ? 240 LEU A CA   1 
ATOM   2550 C  C    A LEU A 1 239 ? -0.441  -11.209 3.499   0.50 4.85  ? 240 LEU A C    1 
ATOM   2551 C  C    B LEU A 1 239 ? 0.173   -11.573 3.710   0.50 7.10  ? 240 LEU A C    1 
ATOM   2552 O  O    A LEU A 1 239 ? 0.296   -11.340 4.469   0.50 5.61  ? 240 LEU A O    1 
ATOM   2553 O  O    B LEU A 1 239 ? 0.919   -11.769 4.720   0.50 8.43  ? 240 LEU A O    1 
ATOM   2554 C  CB   A LEU A 1 239 ? -0.828  -13.437 2.406   0.50 6.42  ? 240 LEU A CB   1 
ATOM   2555 C  CB   B LEU A 1 239 ? -0.335  -13.704 2.564   0.50 9.20  ? 240 LEU A CB   1 
ATOM   2556 C  CG   A LEU A 1 239 ? -0.750  -14.336 1.131   0.50 9.18  ? 240 LEU A CG   1 
ATOM   2557 C  CG   B LEU A 1 239 ? -0.638  -14.579 1.328   0.50 10.49 ? 240 LEU A CG   1 
ATOM   2558 C  CD1  A LEU A 1 239 ? -1.249  -15.717 1.261   0.50 14.36 ? 240 LEU A CD1  1 
ATOM   2559 C  CD1  B LEU A 1 239 ? 0.573   -15.031 0.342   0.50 14.83 ? 240 LEU A CD1  1 
ATOM   2560 C  CD2  A LEU A 1 239 ? -1.520  -13.712 0.112   0.50 6.99  ? 240 LEU A CD2  1 
ATOM   2561 C  CD2  B LEU A 1 239 ? -1.376  -15.755 1.875   0.50 10.46 ? 240 LEU A CD2  1 
ATOM   2562 N  N    A MET A 1 240 ? -1.479  -10.389 3.488   0.50 5.53  ? 241 MET A N    1 
ATOM   2563 N  N    B MET A 1 240 ? -0.841  -10.701 3.704   0.50 7.38  ? 241 MET A N    1 
ATOM   2564 C  CA   A MET A 1 240 ? -1.894  -9.591  4.687   0.50 5.13  ? 241 MET A CA   1 
ATOM   2565 C  CA   B MET A 1 240 ? -1.221  -9.859  4.874   0.50 7.37  ? 241 MET A CA   1 
ATOM   2566 C  C    A MET A 1 240 ? -2.663  -10.482 5.635   0.50 5.08  ? 241 MET A C    1 
ATOM   2567 C  C    B MET A 1 240 ? -2.064  -10.771 5.797   0.50 8.21  ? 241 MET A C    1 
ATOM   2568 O  O    A MET A 1 240 ? -3.860  -10.615 5.554   0.50 6.00  ? 241 MET A O    1 
ATOM   2569 O  O    B MET A 1 240 ? -3.278  -10.906 5.622   0.50 8.21  ? 241 MET A O    1 
ATOM   2570 C  CB   A MET A 1 240 ? -2.727  -8.405  4.216   0.50 5.99  ? 241 MET A CB   1 
ATOM   2571 C  CB   B MET A 1 240 ? -2.015  -8.640  4.409   0.50 8.00  ? 241 MET A CB   1 
ATOM   2572 C  CG   A MET A 1 240 ? -3.130  -7.462  5.392   0.50 6.21  ? 241 MET A CG   1 
ATOM   2573 C  CG   B MET A 1 240 ? -2.409  -7.695  5.605   0.50 6.98  ? 241 MET A CG   1 
ATOM   2574 S  SD   A MET A 1 240 ? -4.068  -6.019  4.875   0.50 6.62  ? 241 MET A SD   1 
ATOM   2575 S  SD   B MET A 1 240 ? -3.327  -6.270  5.104   0.50 9.22  ? 241 MET A SD   1 
ATOM   2576 C  CE   A MET A 1 240 ? -2.786  -4.902  4.176   0.50 6.31  ? 241 MET A CE   1 
ATOM   2577 C  CE   B MET A 1 240 ? -1.990  -5.196  4.486   0.50 8.56  ? 241 MET A CE   1 
ATOM   2578 N  N    A VAL A 1 241 ? -1.902  -11.105 6.546   0.50 5.30  ? 242 VAL A N    1 
ATOM   2579 N  N    B VAL A 1 241 ? -1.338  -11.377 6.746   0.50 8.26  ? 242 VAL A N    1 
ATOM   2580 C  CA   A VAL A 1 241 ? -2.395  -11.998 7.605   0.50 6.02  ? 242 VAL A CA   1 
ATOM   2581 C  CA   B VAL A 1 241 ? -1.945  -12.233 7.760   0.50 7.59  ? 242 VAL A CA   1 
ATOM   2582 C  C    A VAL A 1 241 ? -1.477  -11.805 8.865   0.50 6.98  ? 242 VAL A C    1 
ATOM   2583 C  C    B VAL A 1 241 ? -1.220  -11.983 8.982   0.50 8.31  ? 242 VAL A C    1 
ATOM   2584 O  O    A VAL A 1 241 ? -0.363  -11.325 8.779   0.50 7.24  ? 242 VAL A O    1 
ATOM   2585 O  O    B VAL A 1 241 ? -0.026  -11.648 8.985   0.50 8.68  ? 242 VAL A O    1 
ATOM   2586 C  CB   A VAL A 1 241 ? -2.335  -13.513 7.135   0.50 6.41  ? 242 VAL A CB   1 
ATOM   2587 C  CB   B VAL A 1 241 ? -1.881  -13.756 7.400   0.50 6.70  ? 242 VAL A CB   1 
ATOM   2588 C  CG1  A VAL A 1 241 ? -3.348  -13.729 5.947   0.50 7.65  ? 242 VAL A CG1  1 
ATOM   2589 C  CG1  B VAL A 1 241 ? -2.835  -14.070 6.153   0.50 9.06  ? 242 VAL A CG1  1 
ATOM   2590 C  CG2  A VAL A 1 241 ? -0.909  -13.936 6.813   0.50 7.06  ? 242 VAL A CG2  1 
ATOM   2591 C  CG2  B VAL A 1 241 ? -0.436  -14.220 7.211   0.50 8.76  ? 242 VAL A CG2  1 
ATOM   2592 N  N    . ASP A 1 242 ? -1.968  -12.188 10.061  1.00 7.80  ? 243 ASP A N    1 
ATOM   2593 C  CA   . ASP A 1 242 ? -1.297  -12.054 11.357  1.00 7.65  ? 243 ASP A CA   1 
ATOM   2594 C  C    . ASP A 1 242 ? -0.807  -10.604 11.594  1.00 8.32  ? 243 ASP A C    1 
ATOM   2595 O  O    . ASP A 1 242 ? 0.315   -10.371 12.077  1.00 9.55  ? 243 ASP A O    1 
ATOM   2596 C  CB   . ASP A 1 242 ? -0.198  -13.118 11.560  1.00 8.42  ? 243 ASP A CB   1 
ATOM   2597 C  CG   . ASP A 1 242 ? -0.775  -14.513 11.672  1.00 8.33  ? 243 ASP A CG   1 
ATOM   2598 O  OD1  . ASP A 1 242 ? -1.855  -14.679 12.304  1.00 8.12  ? 243 ASP A OD1  1 
ATOM   2599 O  OD2  . ASP A 1 242 ? -0.184  -15.448 11.059  1.00 10.37 ? 243 ASP A OD2  1 
ATOM   2600 N  N    . ASN A 1 243 ? -1.716  -9.682  11.292  1.00 7.28  ? 244 ASN A N    1 
ATOM   2601 C  CA   . ASN A 1 243 ? -1.453  -8.238  11.498  1.00 7.61  ? 244 ASN A CA   1 
ATOM   2602 C  C    . ASN A 1 243 ? -2.002  -7.776  12.893  1.00 6.64  ? 244 ASN A C    1 
ATOM   2603 O  O    . ASN A 1 243 ? -2.651  -6.750  12.984  1.00 7.79  ? 244 ASN A O    1 
ATOM   2604 C  CB   . ASN A 1 243 ? -1.999  -7.382  10.360  1.00 7.51  ? 244 ASN A CB   1 
ATOM   2605 C  CG   . ASN A 1 243 ? -3.466  -7.554  10.146  1.00 8.18  ? 244 ASN A CG   1 
ATOM   2606 O  OD1  . ASN A 1 243 ? -4.114  -8.423  10.739  1.00 8.49  ? 244 ASN A OD1  1 
ATOM   2607 N  ND2  . ASN A 1 243 ? -4.057  -6.733  9.315   1.00 12.73 ? 244 ASN A ND2  1 
ATOM   2608 N  N    . TRP A 1 244 ? -1.724  -8.557  13.933  1.00 6.59  ? 245 TRP A N    1 
ATOM   2609 C  CA   . TRP A 1 244 ? -2.132  -8.331  15.313  1.00 6.66  ? 245 TRP A CA   1 
ATOM   2610 C  C    . TRP A 1 244 ? -0.935  -8.216  16.227  1.00 6.55  ? 245 TRP A C    1 
ATOM   2611 O  O    . TRP A 1 244 ? 0.056   -8.957  16.110  1.00 7.87  ? 245 TRP A O    1 
ATOM   2612 C  CB   . TRP A 1 244 ? -3.113  -9.417  15.802  1.00 6.22  ? 245 TRP A CB   1 
ATOM   2613 C  CG   . TRP A 1 244 ? -2.633  -10.842 15.636  1.00 6.67  ? 245 TRP A CG   1 
ATOM   2614 C  CD1  . TRP A 1 244 ? -2.775  -11.578 14.499  1.00 6.78  ? 245 TRP A CD1  1 
ATOM   2615 C  CD2  . TRP A 1 244 ? -2.070  -11.705 16.596  1.00 6.34  ? 245 TRP A CD2  1 
ATOM   2616 N  NE1  . TRP A 1 244 ? -2.240  -12.846 14.675  1.00 7.13  ? 245 TRP A NE1  1 
ATOM   2617 C  CE2  . TRP A 1 244 ? -1.823  -12.947 15.966  1.00 6.84  ? 245 TRP A CE2  1 
ATOM   2618 C  CE3  . TRP A 1 244 ? -1.764  -11.555 17.957  1.00 7.35  ? 245 TRP A CE3  1 
ATOM   2619 C  CZ2  . TRP A 1 244 ? -1.237  -14.022 16.660  1.00 8.05  ? 245 TRP A CZ2  1 
ATOM   2620 C  CZ3  . TRP A 1 244 ? -1.245  -12.649 18.642  1.00 8.50  ? 245 TRP A CZ3  1 
ATOM   2621 C  CH2  . TRP A 1 244 ? -0.962  -13.859 17.965  1.00 8.76  ? 245 TRP A CH2  1 
ATOM   2622 N  N    . ARG A 1 245 ? -1.052  -7.321  17.185  1.00 6.20  ? 246 ARG A N    1 
ATOM   2623 C  CA   . ARG A 1 245 ? -0.139  -7.218  18.329  1.00 6.71  ? 246 ARG A CA   1 
ATOM   2624 C  C    . ARG A 1 245 ? -0.615  -8.145  19.473  1.00 6.22  ? 246 ARG A C    1 
ATOM   2625 O  O    . ARG A 1 245 ? -1.825  -8.117  19.763  1.00 6.78  ? 246 ARG A O    1 
ATOM   2626 C  CB   . ARG A 1 245 ? -0.065  -5.781  18.818  1.00 6.57  ? 246 ARG A CB   1 
ATOM   2627 C  CG   . ARG A 1 245 ? 1.083   -5.525  19.839  1.00 6.86  ? 246 ARG A CG   1 
ATOM   2628 C  CD   . ARG A 1 245 ? 0.963   -4.136  20.488  1.00 7.26  ? 246 ARG A CD   1 
ATOM   2629 N  NE   . ARG A 1 245 ? 2.206   -3.865  21.192  1.00 7.44  ? 246 ARG A NE   1 
ATOM   2630 C  CZ   . ARG A 1 245 ? 2.435   -2.837  22.036  1.00 7.15  ? 246 ARG A CZ   1 
ATOM   2631 N  NH1  . ARG A 1 245 ? 1.452   -2.086  22.415  1.00 7.81  ? 246 ARG A NH1  1 
ATOM   2632 N  NH2  . ARG A 1 245 ? 3.670   -2.604  22.468  1.00 9.30  ? 246 ARG A NH2  1 
ATOM   2633 N  N    A PRO A 1 246 ? 0.291   -8.969  20.033  0.50 7.07  ? 247 PRO A N    1 
ATOM   2634 N  N    B PRO A 1 246 ? 0.279   -8.856  20.123  0.50 6.57  ? 247 PRO A N    1 
ATOM   2635 C  CA   A PRO A 1 246 ? -0.047  -9.798  21.204  0.50 6.19  ? 247 PRO A CA   1 
ATOM   2636 C  CA   B PRO A 1 246 ? -0.254  -9.703  21.174  0.50 6.77  ? 247 PRO A CA   1 
ATOM   2637 C  C    A PRO A 1 246 ? -0.470  -8.970  22.421  0.50 6.61  ? 247 PRO A C    1 
ATOM   2638 C  C    B PRO A 1 246 ? -0.516  -8.924  22.436  0.50 6.83  ? 247 PRO A C    1 
ATOM   2639 O  O    A PRO A 1 246 ? -0.138  -7.774  22.541  0.50 7.21  ? 247 PRO A O    1 
ATOM   2640 O  O    B PRO A 1 246 ? -0.107  -7.753  22.606  0.50 7.25  ? 247 PRO A O    1 
ATOM   2641 C  CB   A PRO A 1 246 ? 1.270   -10.533 21.517  0.50 7.94  ? 247 PRO A CB   1 
ATOM   2642 C  CB   B PRO A 1 246 ? 0.857   -10.702 21.392  0.50 7.64  ? 247 PRO A CB   1 
ATOM   2643 C  CG   A PRO A 1 246 ? 1.937   -10.609 20.195  0.50 8.11  ? 247 PRO A CG   1 
ATOM   2644 C  CG   B PRO A 1 246 ? 2.166   -9.897  20.992  0.50 10.51 ? 247 PRO A CG   1 
ATOM   2645 C  CD   A PRO A 1 246 ? 1.670   -9.261  19.563  0.50 7.88  ? 247 PRO A CD   1 
ATOM   2646 C  CD   B PRO A 1 246 ? 1.740   -9.028  19.928  0.50 8.46  ? 247 PRO A CD   1 
ATOM   2647 N  N    . ALA A 1 247 ? -1.117  -9.595  23.395  1.00 7.70  ? 248 ALA A N    1 
ATOM   2648 C  CA   . ALA A 1 247 ? -1.469  -8.976  24.688  1.00 7.46  ? 248 ALA A CA   1 
ATOM   2649 C  C    . ALA A 1 247 ? -0.240  -8.471  25.396  1.00 7.75  ? 248 ALA A C    1 
ATOM   2650 O  O    . ALA A 1 247 ? 0.815   -9.133  25.441  1.00 8.41  ? 248 ALA A O    1 
ATOM   2651 C  CB   . ALA A 1 247 ? -2.255  -9.992  25.552  1.00 9.49  ? 248 ALA A CB   1 
ATOM   2652 N  N    . GLN A 1 248 ? -0.380  -7.273  26.010  1.00 7.29  ? 249 GLN A N    1 
ATOM   2653 C  CA   . GLN A 1 248 ? 0.673   -6.541  26.709  1.00 7.52  ? 249 GLN A CA   1 
ATOM   2654 C  C    . GLN A 1 248 ? 0.393   -6.578  28.210  1.00 8.59  ? 249 GLN A C    1 
ATOM   2655 O  O    . GLN A 1 248 ? -0.751  -6.781  28.633  1.00 8.44  ? 249 GLN A O    1 
ATOM   2656 C  CB   . GLN A 1 248 ? 0.734   -5.124  26.201  1.00 8.07  ? 249 GLN A CB   1 
ATOM   2657 C  CG   . GLN A 1 248 ? 1.063   -5.042  24.684  1.00 8.40  ? 249 GLN A CG   1 
ATOM   2658 C  CD   . GLN A 1 248 ? 2.399   -5.702  24.348  1.00 9.66  ? 249 GLN A CD   1 
ATOM   2659 O  OE1  . GLN A 1 248 ? 3.438   -5.366  24.934  1.00 12.37 ? 249 GLN A OE1  1 
ATOM   2660 N  NE2  . GLN A 1 248 ? 2.391   -6.641  23.384  1.00 10.15 ? 249 GLN A NE2  1 
ATOM   2661 N  N    . PRO A 1 249 ? 1.398   -6.262  29.032  1.00 10.14 ? 250 PRO A N    1 
ATOM   2662 C  CA   . PRO A 1 249 ? 1.192   -6.263  30.475  1.00 11.25 ? 250 PRO A CA   1 
ATOM   2663 C  C    . PRO A 1 249 ? 0.133   -5.264  30.912  1.00 9.41  ? 250 PRO A C    1 
ATOM   2664 O  O    . PRO A 1 249 ? 0.154   -4.101  30.547  1.00 10.05 ? 250 PRO A O    1 
ATOM   2665 C  CB   . PRO A 1 249 ? 2.603   -5.878  31.026  1.00 13.34 ? 250 PRO A CB   1 
ATOM   2666 C  CG   . PRO A 1 249 ? 3.586   -6.316  29.987  1.00 14.69 ? 250 PRO A CG   1 
ATOM   2667 C  CD   . PRO A 1 249 ? 2.809   -6.038  28.684  1.00 12.45 ? 250 PRO A CD   1 
ATOM   2668 N  N    . LEU A 1 250 ? -0.740  -5.757  31.804  1.00 9.92  ? 251 LEU A N    1 
ATOM   2669 C  CA   . LEU A 1 250 ? -1.803  -4.926  32.348  1.00 9.26  ? 251 LEU A CA   1 
ATOM   2670 C  C    . LEU A 1 250 ? -1.279  -3.807  33.266  1.00 9.35  ? 251 LEU A C    1 
ATOM   2671 O  O    . LEU A 1 250 ? -1.857  -2.751  33.307  1.00 9.46  ? 251 LEU A O    1 
ATOM   2672 C  CB   . LEU A 1 250 ? -2.845  -5.794  33.080  1.00 10.62 ? 251 LEU A CB   1 
ATOM   2673 C  CG   . LEU A 1 250 ? -4.144  -5.065  33.502  1.00 11.55 ? 251 LEU A CG   1 
ATOM   2674 C  CD1  . LEU A 1 250 ? -4.909  -4.478  32.296  1.00 12.11 ? 251 LEU A CD1  1 
ATOM   2675 C  CD2  . LEU A 1 250 ? -5.051  -6.032  34.308  1.00 14.11 ? 251 LEU A CD2  1 
ATOM   2676 N  N    . LYS A 1 251 ? -0.227  -4.101  33.988  1.00 11.24 ? 252 LYS A N    1 
ATOM   2677 C  CA   . LYS A 1 251 ? 0.425   -3.043  34.879  1.00 11.39 ? 252 LYS A CA   1 
ATOM   2678 C  C    . LYS A 1 251 ? -0.644  -2.474  35.816  1.00 12.34 ? 252 LYS A C    1 
ATOM   2679 O  O    . LYS A 1 251 ? -1.457  -3.321  36.331  1.00 14.21 ? 252 LYS A O    1 
ATOM   2680 C  CB   . LYS A 1 251 ? 1.227   -2.063  34.069  1.00 12.38 ? 252 LYS A CB   1 
ATOM   2681 C  CG   . LYS A 1 251 ? 2.403   -2.719  33.329  1.00 15.89 ? 252 LYS A CG   1 
ATOM   2682 C  CD   . LYS A 1 251 ? 3.270   -1.797  32.571  1.00 16.52 ? 252 LYS A CD   1 
ATOM   2683 C  CE   . LYS A 1 251 ? 4.465   -2.417  32.075  1.00 20.61 ? 252 LYS A CE   1 
ATOM   2684 N  NZ   . LYS A 1 251 ? 5.347   -1.512  31.304  1.00 24.15 ? 252 LYS A NZ   1 
ATOM   2685 N  N    . ASN A 1 252 ? -0.635  -1.236  36.106  1.00 11.45 ? 253 ASN A N    1 
ATOM   2686 C  CA   . ASN A 1 252 ? -1.488  -0.752  37.086  1.00 15.88 ? 253 ASN A CA   1 
ATOM   2687 C  C    . ASN A 1 252 ? -2.819  -0.354  36.451  1.00 15.58 ? 253 ASN A C    1 
ATOM   2688 O  O    . ASN A 1 252 ? -3.134  0.828   36.424  1.00 18.37 ? 253 ASN A O    1 
ATOM   2689 C  CB   . ASN A 1 252 ? -0.759  0.428   37.838  1.00 19.20 ? 253 ASN A CB   1 
ATOM   2690 C  CG   . ASN A 1 252 ? -1.525  0.954   39.008  1.00 21.51 ? 253 ASN A CG   1 
ATOM   2691 O  OD1  . ASN A 1 252 ? -2.093  0.172   39.809  1.00 32.91 ? 253 ASN A OD1  1 
ATOM   2692 N  ND2  . ASN A 1 252 ? -1.526  2.273   39.159  1.00 23.30 ? 253 ASN A ND2  1 
ATOM   2693 N  N    . ARG A 1 253 ? -3.585  -1.317  35.908  1.00 13.93 ? 254 ARG A N    1 
ATOM   2694 C  CA   . ARG A 1 253 ? -4.893  -0.970  35.401  1.00 10.40 ? 254 ARG A CA   1 
ATOM   2695 C  C    . ARG A 1 253 ? -5.997  -1.904  35.860  1.00 10.39 ? 254 ARG A C    1 
ATOM   2696 O  O    . ARG A 1 253 ? -5.734  -3.062  36.112  1.00 16.84 ? 254 ARG A O    1 
ATOM   2697 C  CB   . ARG A 1 253 ? -4.826  -0.971  33.879  1.00 8.52  ? 254 ARG A CB   1 
ATOM   2698 C  CG   . ARG A 1 253 ? -3.912  0.172   33.365  1.00 8.64  ? 254 ARG A CG   1 
ATOM   2699 C  CD   . ARG A 1 253 ? -3.791  0.196   31.860  1.00 8.33  ? 254 ARG A CD   1 
ATOM   2700 N  NE   . ARG A 1 253 ? -2.973  -0.967  31.396  1.00 7.60  ? 254 ARG A NE   1 
ATOM   2701 C  CZ   . ARG A 1 253 ? -2.738  -1.261  30.135  1.00 6.60  ? 254 ARG A CZ   1 
ATOM   2702 N  NH1  . ARG A 1 253 ? -3.342  -0.560  29.179  1.00 6.47  ? 254 ARG A NH1  1 
ATOM   2703 N  NH2  . ARG A 1 253 ? -1.914  -2.235  29.816  1.00 7.25  ? 254 ARG A NH2  1 
ATOM   2704 N  N    A GLN A 1 254 ? -7.210  -1.358  35.876  0.50 9.97  ? 255 GLN A N    1 
ATOM   2705 N  N    B GLN A 1 254 ? -7.223  -1.407  35.906  0.50 10.47 ? 255 GLN A N    1 
ATOM   2706 C  CA   A GLN A 1 254 ? -8.438  -2.058  36.139  0.50 10.47 ? 255 GLN A CA   1 
ATOM   2707 C  CA   B GLN A 1 254 ? -8.381  -2.204  36.209  0.50 11.15 ? 255 GLN A CA   1 
ATOM   2708 C  C    A GLN A 1 254 ? -9.196  -2.164  34.839  0.50 8.76  ? 255 GLN A C    1 
ATOM   2709 C  C    B GLN A 1 254 ? -9.348  -2.175  35.019  0.50 10.48 ? 255 GLN A C    1 
ATOM   2710 O  O    A GLN A 1 254 ? -9.352  -1.168  34.113  0.50 9.32  ? 255 GLN A O    1 
ATOM   2711 O  O    B GLN A 1 254 ? -9.790  -1.122  34.550  0.50 12.41 ? 255 GLN A O    1 
ATOM   2712 C  CB   A GLN A 1 254 ? -9.305  -1.298  37.166  0.50 13.32 ? 255 GLN A CB   1 
ATOM   2713 C  CB   B GLN A 1 254 ? -9.071  -1.660  37.442  0.50 12.94 ? 255 GLN A CB   1 
ATOM   2714 C  CG   A GLN A 1 254 ? -8.659  -1.231  38.538  0.50 19.34 ? 255 GLN A CG   1 
ATOM   2715 C  CG   B GLN A 1 254 ? -10.261 -2.338  37.779  0.50 19.44 ? 255 GLN A CG   1 
ATOM   2716 C  CD   A GLN A 1 254 ? -8.105  -2.493  39.018  0.50 27.59 ? 255 GLN A CD   1 
ATOM   2717 C  CD   B GLN A 1 254 ? -10.132 -3.142  39.021  0.50 21.71 ? 255 GLN A CD   1 
ATOM   2718 O  OE1  A GLN A 1 254 ? -8.585  -3.572  38.668  0.50 36.73 ? 255 GLN A OE1  1 
ATOM   2719 O  OE1  B GLN A 1 254 ? -9.201  -3.947  39.195  0.50 28.65 ? 255 GLN A OE1  1 
ATOM   2720 N  NE2  A GLN A 1 254 ? -7.092  -2.396  39.914  0.50 31.41 ? 255 GLN A NE2  1 
ATOM   2721 N  NE2  B GLN A 1 254 ? -11.150 -2.998  39.911  0.50 17.86 ? 255 GLN A NE2  1 
ATOM   2722 N  N    . ILE A 1 255 ? -9.727  -3.353  34.560  1.00 8.94  ? 256 ILE A N    1 
ATOM   2723 C  CA   . ILE A 1 255 ? -10.731 -3.544  33.526  1.00 8.08  ? 256 ILE A CA   1 
ATOM   2724 C  C    . ILE A 1 255 ? -12.090 -3.591  34.211  1.00 8.60  ? 256 ILE A C    1 
ATOM   2725 O  O    . ILE A 1 255 ? -12.294 -4.291  35.192  1.00 9.86  ? 256 ILE A O    1 
ATOM   2726 C  CB   . ILE A 1 255 ? -10.462 -4.797  32.683  1.00 7.72  ? 256 ILE A CB   1 
ATOM   2727 C  CG1  . ILE A 1 255 ? -9.020  -4.787  32.158  1.00 8.73  ? 256 ILE A CG1  1 
ATOM   2728 C  CG2  . ILE A 1 255 ? -11.569 -4.962  31.593  1.00 9.56  ? 256 ILE A CG2  1 
ATOM   2729 C  CD1  . ILE A 1 255 ? -8.664  -6.015  31.303  1.00 10.33 ? 256 ILE A CD1  1 
ATOM   2730 N  N    . LYS A 1 256 ? -13.009 -2.770  33.739  1.00 8.11  ? 257 LYS A N    1 
ATOM   2731 C  CA   . LYS A 1 256 ? -14.392 -2.666  34.237  1.00 8.80  ? 257 LYS A CA   1 
ATOM   2732 C  C    . LYS A 1 256 ? -15.359 -3.279  33.282  1.00 9.06  ? 257 LYS A C    1 
ATOM   2733 O  O    . LYS A 1 256 ? -15.204 -3.155  32.053  1.00 10.61 ? 257 LYS A O    1 
ATOM   2734 C  CB   . LYS A 1 256 ? -14.737 -1.204  34.523  1.00 9.25  ? 257 LYS A CB   1 
ATOM   2735 C  CG   . LYS A 1 256 ? -13.736 -0.591  35.554  1.00 13.73 ? 257 LYS A CG   1 
ATOM   2736 C  CD   . LYS A 1 256 ? -13.845 0.777   35.947  1.00 17.23 ? 257 LYS A CD   1 
ATOM   2737 C  CE   . LYS A 1 256 ? -12.628 1.189   36.824  1.00 19.71 ? 257 LYS A CE   1 
ATOM   2738 N  NZ   . LYS A 1 256 ? -12.678 2.560   37.419  1.00 23.36 ? 257 LYS A NZ   1 
ATOM   2739 N  N    . ALA A 1 257 ? -16.417 -3.899  33.818  1.00 9.14  ? 258 ALA A N    1 
ATOM   2740 C  CA   . ALA A 1 257 ? -17.480 -4.532  33.043  1.00 9.45  ? 258 ALA A CA   1 
ATOM   2741 C  C    . ALA A 1 257 ? -18.745 -3.723  33.244  1.00 9.25  ? 258 ALA A C    1 
ATOM   2742 O  O    . ALA A 1 257 ? -19.086 -3.287  34.359  1.00 10.96 ? 258 ALA A O    1 
ATOM   2743 C  CB   . ALA A 1 257 ? -17.729 -5.998  33.486  1.00 10.87 ? 258 ALA A CB   1 
ATOM   2744 N  N    . SER A 1 258 ? -19.509 -3.565  32.129  1.00 9.15  ? 259 SER A N    1 
ATOM   2745 C  CA   . SER A 1 258 ? -20.781 -2.853  32.130  1.00 10.48 ? 259 SER A CA   1 
ATOM   2746 C  C    . SER A 1 258 ? -21.939 -3.757  32.598  1.00 11.51 ? 259 SER A C    1 
ATOM   2747 O  O    . SER A 1 258 ? -23.062 -3.255  32.702  1.00 15.24 ? 259 SER A O    1 
ATOM   2748 C  CB   . SER A 1 258 ? -21.079 -2.302  30.761  1.00 11.10 ? 259 SER A CB   1 
ATOM   2749 O  OG   . SER A 1 258 ? -21.500 -3.307  29.863  1.00 10.04 ? 259 SER A OG   1 
ATOM   2750 N  N    . PHE A 1 259 ? -21.665 -5.020  32.766  1.00 12.52 ? 260 PHE A N    1 
ATOM   2751 C  CA   . PHE A 1 259 ? -22.667 -6.090  32.953  1.00 14.11 ? 260 PHE A CA   1 
ATOM   2752 C  C    . PHE A 1 259 ? -22.196 -7.000  34.089  1.00 17.17 ? 260 PHE A C    1 
ATOM   2753 O  O    . PHE A 1 259 ? -20.991 -7.160  34.356  1.00 17.97 ? 260 PHE A O    1 
ATOM   2754 C  CB   . PHE A 1 259 ? -22.833 -6.868  31.670  1.00 13.87 ? 260 PHE A CB   1 
ATOM   2755 C  CG   . PHE A 1 259 ? -21.576 -7.565  31.210  1.00 13.48 ? 260 PHE A CG   1 
ATOM   2756 C  CD1  . PHE A 1 259 ? -20.558 -6.893  30.514  1.00 11.26 ? 260 PHE A CD1  1 
ATOM   2757 C  CD2  . PHE A 1 259 ? -21.316 -8.907  31.621  1.00 16.88 ? 260 PHE A CD2  1 
ATOM   2758 C  CE1  . PHE A 1 259 ? -19.358 -7.582  30.222  1.00 14.11 ? 260 PHE A CE1  1 
ATOM   2759 C  CE2  . PHE A 1 259 ? -20.140 -9.551  31.275  1.00 17.63 ? 260 PHE A CE2  1 
ATOM   2760 C  CZ   . PHE A 1 259 ? -19.124 -8.887  30.646  1.00 15.68 ? 260 PHE A CZ   1 
ATOM   2761 N  N    . LYS A 1 260 ? -23.261 -7.655  34.648  1.00 23.37 ? 261 LYS A N    1 
ATOM   2762 C  CA   . LYS A 1 260 ? -23.350 -8.901  35.481  1.00 29.15 ? 261 LYS A CA   1 
ATOM   2763 C  C    . LYS A 1 260 ? -22.555 -8.710  36.725  1.00 35.33 ? 261 LYS A C    1 
ATOM   2764 O  O    . LYS A 1 260 ? -23.090 -8.248  37.766  1.00 39.10 ? 261 LYS A O    1 
ATOM   2765 C  CB   . LYS A 1 260 ? -22.955 -10.212 34.762  1.00 30.66 ? 261 LYS A CB   1 
ATOM   2766 C  CG   . LYS A 1 260 ? -23.907 -10.645 33.596  1.00 33.03 ? 261 LYS A CG   1 
ATOM   2767 C  CD   . LYS A 1 260 ? -23.493 -11.983 32.816  1.00 33.99 ? 261 LYS A CD   1 
ATOM   2768 C  CE   . LYS A 1 260 ? -21.993 -12.269 32.836  1.00 35.78 ? 261 LYS A CE   1 
ATOM   2769 N  NZ   . LYS A 1 260 ? -21.549 -13.514 32.218  1.00 39.03 ? 261 LYS A NZ   1 
ATOM   2770 O  OXT  . LYS A 1 260 ? -21.350 -9.015  36.617  1.00 41.71 ? 261 LYS A OXT  1 
HETATM 2771 ZN ZN   . ZN  B 2 .   ? -6.679  -1.714  15.321  1.00 5.39  ? 262 ZN  A ZN   1 
HETATM 2772 N  N1   . E50 C 3 .   ? -0.491  4.896   11.195  1.00 23.15 ? 263 E50 A N1   1 
HETATM 2773 C  C2   . E50 C 3 .   ? -1.411  4.150   11.785  1.00 19.91 ? 263 E50 A C2   1 
HETATM 2774 N  N3   . E50 C 3 .   ? -2.090  4.566   12.889  1.00 20.08 ? 263 E50 A N3   1 
HETATM 2775 C  C4   . E50 C 3 .   ? -1.894  5.807   13.456  1.00 21.10 ? 263 E50 A C4   1 
HETATM 2776 C  C5   . E50 C 3 .   ? -0.927  6.633   12.891  1.00 22.24 ? 263 E50 A C5   1 
HETATM 2777 C  C6   . E50 C 3 .   ? -0.256  6.137   11.746  1.00 25.08 ? 263 E50 A C6   1 
HETATM 2778 S  S7   . E50 C 3 .   ? -1.711  2.594   11.048  1.00 21.06 ? 263 E50 A S7   1 
HETATM 2779 C  C8   . E50 C 3 .   ? -2.999  1.978   12.156  1.00 13.96 ? 263 E50 A C8   1 
HETATM 2780 C  C9   . E50 C 3 .   ? -4.179  2.921   12.273  1.00 13.56 ? 263 E50 A C9   1 
HETATM 2781 O  O10  . E50 C 3 .   ? -4.544  3.582   11.244  1.00 17.74 ? 263 E50 A O10  1 
HETATM 2782 C  C11  . E50 C 3 .   ? -0.594  8.031   13.407  1.00 24.19 ? 263 E50 A C11  1 
HETATM 2783 C  C12  . E50 C 3 .   ? -1.299  8.338   14.767  1.00 20.90 ? 263 E50 A C12  1 
HETATM 2784 C  C13  . E50 C 3 .   ? -4.857  3.083   13.629  1.00 12.21 ? 263 E50 A C13  1 
HETATM 2785 C  C14  . E50 C 3 .   ? -4.981  2.057   14.551  1.00 10.04 ? 263 E50 A C14  1 
HETATM 2786 C  C15  . E50 C 3 .   ? -5.620  2.254   15.772  1.00 7.90  ? 263 E50 A C15  1 
HETATM 2787 C  C16  . E50 C 3 .   ? -6.078  3.546   16.067  1.00 9.84  ? 263 E50 A C16  1 
HETATM 2788 C  C17  . E50 C 3 .   ? -5.908  4.595   15.206  1.00 10.39 ? 263 E50 A C17  1 
HETATM 2789 C  C18  . E50 C 3 .   ? -5.301  4.368   13.962  1.00 12.10 ? 263 E50 A C18  1 
HETATM 2790 S  S19  . E50 C 3 .   ? -5.982  0.813   16.806  1.00 7.54  ? 263 E50 A S19  1 
HETATM 2791 O  O20  . E50 C 3 .   ? -5.340  1.055   18.079  1.00 7.36  ? 263 E50 A O20  1 
HETATM 2792 CL CL21 . E50 C 3 .   ? -6.851  3.810   17.576  1.00 10.35 ? 263 E50 A CL21 1 
HETATM 2793 O  O22  . E50 C 3 .   ? -7.437  0.770   16.790  1.00 7.40  ? 263 E50 A O22  1 
HETATM 2794 N  N23  . E50 C 3 .   ? -5.428  -0.478  16.083  1.00 6.38  ? 263 E50 A N23  1 
HETATM 2795 N  N1   . BCN D 4 .   ? -20.501 -14.649 23.312  1.00 21.22 ? 264 BCN A N1   1 
HETATM 2796 C  C1   . BCN D 4 .   ? -19.718 -14.293 24.437  1.00 20.30 ? 264 BCN A C1   1 
HETATM 2797 C  C2   . BCN D 4 .   ? -19.949 -15.201 25.567  1.00 20.46 ? 264 BCN A C2   1 
HETATM 2798 O  O21  . BCN D 4 .   ? -20.922 -15.963 25.638  1.00 24.55 ? 264 BCN A O21  1 
HETATM 2799 O  O22  . BCN D 4 .   ? -19.306 -15.041 26.626  1.00 23.34 ? 264 BCN A O22  1 
HETATM 2800 C  C3   . BCN D 4 .   ? -20.129 -15.563 22.386  1.00 12.94 ? 264 BCN A C3   1 
HETATM 2801 C  C4   . BCN D 4 .   ? -20.510 -16.628 21.454  1.00 27.26 ? 264 BCN A C4   1 
HETATM 2802 O  O4   . BCN D 4 .   ? -21.150 -16.241 20.180  1.00 25.08 ? 264 BCN A O4   1 
HETATM 2803 C  C5   . BCN D 4 .   ? -21.700 -13.975 23.089  1.00 14.43 ? 264 BCN A C5   1 
HETATM 2804 C  C6   . BCN D 4 .   ? -21.717 -13.145 24.347  1.00 28.36 ? 264 BCN A C6   1 
HETATM 2805 O  O6   . BCN D 4 .   ? -22.678 -12.334 24.882  1.00 23.19 ? 264 BCN A O6   1 
HETATM 2806 S  S    . DMS E 5 .   ? 1.335   -11.744 14.992  1.00 16.94 ? 265 DMS A S    1 
HETATM 2807 O  O    . DMS E 5 .   ? 2.456   -10.543 14.457  1.00 23.40 ? 265 DMS A O    1 
HETATM 2808 C  C1   . DMS E 5 .   ? 2.044   -13.170 14.587  1.00 17.05 ? 265 DMS A C1   1 
HETATM 2809 C  C2   . DMS E 5 .   ? 1.669   -11.600 16.640  1.00 18.00 ? 265 DMS A C2   1 
HETATM 2810 S  S    . DMS F 5 .   ? -5.482  7.203   11.141  1.00 17.86 ? 266 DMS A S    1 
HETATM 2811 O  O    . DMS F 5 .   ? -6.788  6.473   10.652  1.00 18.31 ? 266 DMS A O    1 
HETATM 2812 C  C1   . DMS F 5 .   ? -4.304  6.695   9.795   1.00 23.10 ? 266 DMS A C1   1 
HETATM 2813 C  C2   . DMS F 5 .   ? -5.666  8.926   10.813  1.00 21.39 ? 266 DMS A C2   1 
HETATM 2814 O  O    . HOH G 6 .   ? -17.696 6.197   38.712  1.00 24.48 ? 126 HOH A O    1 
HETATM 2815 O  O    . HOH G 6 .   ? -27.427 -7.570  26.268  1.00 32.27 ? 267 HOH A O    1 
HETATM 2816 O  O    A HOH G 6 .   ? 2.405   3.185   -4.943  0.50 27.02 ? 268 HOH A O    1 
HETATM 2817 O  O    B HOH G 6 .   ? 1.142   3.123   -4.882  0.50 22.02 ? 268 HOH A O    1 
HETATM 2818 O  O    . HOH G 6 .   ? -1.017  2.761   45.792  1.00 23.33 ? 269 HOH A O    1 
HETATM 2819 O  O    . HOH G 6 .   ? 5.608   -14.133 8.793   1.00 31.36 ? 270 HOH A O    1 
HETATM 2820 O  O    . HOH G 6 .   ? 8.894   -11.311 6.570   1.00 38.60 ? 271 HOH A O    1 
HETATM 2821 O  O    . HOH G 6 .   ? 9.986   -8.238  3.706   1.00 33.27 ? 272 HOH A O    1 
HETATM 2822 O  O    . HOH G 6 .   ? -11.194 -11.149 -3.018  1.00 32.21 ? 273 HOH A O    1 
HETATM 2823 O  O    . HOH G 6 .   ? 10.197  5.792   13.028  1.00 37.26 ? 274 HOH A O    1 
HETATM 2824 O  O    . HOH G 6 .   ? -0.622  6.611   32.191  1.00 26.20 ? 275 HOH A O    1 
HETATM 2825 O  O    . HOH G 6 .   ? 6.419   5.335   28.850  1.00 29.01 ? 276 HOH A O    1 
HETATM 2826 O  O    . HOH G 6 .   ? -16.607 -14.636 29.007  1.00 32.93 ? 277 HOH A O    1 
HETATM 2827 O  O    A HOH G 6 .   ? -20.953 13.814  1.784   0.50 18.17 ? 278 HOH A O    1 
HETATM 2828 O  O    B HOH G 6 .   ? -21.908 13.999  2.597   0.50 21.33 ? 278 HOH A O    1 
HETATM 2829 O  O    . HOH G 6 .   ? -0.445  13.854  27.332  1.00 25.11 ? 279 HOH A O    1 
HETATM 2830 O  O    . HOH G 6 .   ? 1.282   9.830   26.986  1.00 29.25 ? 280 HOH A O    1 
HETATM 2831 O  O    . HOH G 6 .   ? 5.491   9.153   22.012  1.00 27.20 ? 281 HOH A O    1 
HETATM 2832 O  O    A HOH G 6 .   ? -24.547 -17.428 6.715   0.50 22.59 ? 282 HOH A O    1 
HETATM 2833 O  O    B HOH G 6 .   ? -23.380 -18.060 5.919   0.50 16.36 ? 282 HOH A O    1 
HETATM 2834 O  O    . HOH G 6 .   ? 0.809   -9.920  -5.443  1.00 25.77 ? 283 HOH A O    1 
HETATM 2835 O  O    . HOH G 6 .   ? -14.693 0.356   40.185  1.00 30.62 ? 284 HOH A O    1 
HETATM 2836 O  O    . HOH G 6 .   ? 6.669   -5.665  6.835   1.00 29.08 ? 285 HOH A O    1 
HETATM 2837 O  O    . HOH G 6 .   ? 0.307   19.446  17.605  1.00 37.53 ? 286 HOH A O    1 
HETATM 2838 O  O    . HOH G 6 .   ? -22.781 -9.624  25.427  1.00 17.59 ? 287 HOH A O    1 
HETATM 2839 O  O    . HOH G 6 .   ? 1.355   -16.018 -1.829  1.00 31.66 ? 288 HOH A O    1 
HETATM 2840 O  O    . HOH G 6 .   ? 4.838   -3.494  3.089   1.00 28.89 ? 289 HOH A O    1 
HETATM 2841 O  O    . HOH G 6 .   ? 11.923  -6.879  -2.008  1.00 33.61 ? 290 HOH A O    1 
HETATM 2842 O  O    . HOH G 6 .   ? 10.485  6.674   15.501  1.00 33.39 ? 291 HOH A O    1 
HETATM 2843 O  O    . HOH G 6 .   ? -6.593  5.293   -6.280  1.00 29.94 ? 292 HOH A O    1 
HETATM 2844 O  O    . HOH G 6 .   ? -16.873 0.398   -4.012  1.00 38.37 ? 293 HOH A O    1 
HETATM 2845 O  O    . HOH G 6 .   ? -15.137 8.325   34.990  1.00 32.36 ? 294 HOH A O    1 
HETATM 2846 O  O    A HOH G 6 .   ? -1.319  -4.190  43.225  0.50 16.43 ? 295 HOH A O    1 
HETATM 2847 O  O    B HOH G 6 .   ? -1.509  -2.955  43.969  0.50 21.05 ? 295 HOH A O    1 
HETATM 2848 O  O    . HOH G 6 .   ? 7.496   -1.084  -5.563  1.00 30.80 ? 296 HOH A O    1 
HETATM 2849 O  O    . HOH G 6 .   ? 11.211  -3.525  7.760   1.00 29.24 ? 297 HOH A O    1 
HETATM 2850 O  O    . HOH G 6 .   ? -1.651  18.036  15.403  1.00 36.87 ? 298 HOH A O    1 
HETATM 2851 O  O    . HOH G 6 .   ? 2.126   7.974   28.241  1.00 37.30 ? 299 HOH A O    1 
HETATM 2852 O  O    . HOH G 6 .   ? 6.941   -10.623 -7.872  1.00 26.92 ? 300 HOH A O    1 
HETATM 2853 O  O    . HOH G 6 .   ? -24.749 -20.340 8.820   1.00 40.49 ? 301 HOH A O    1 
HETATM 2854 O  O    . HOH G 6 .   ? 5.211   -10.687 18.761  1.00 30.57 ? 302 HOH A O    1 
HETATM 2855 O  O    . HOH G 6 .   ? -19.955 17.065  23.221  1.00 31.06 ? 303 HOH A O    1 
HETATM 2856 O  O    . HOH G 6 .   ? 10.904  -0.415  3.238   1.00 51.87 ? 304 HOH A O    1 
HETATM 2857 O  O    . HOH G 6 .   ? -2.628  -0.197  10.168  1.00 28.22 ? 305 HOH A O    1 
HETATM 2858 O  O    A HOH G 6 .   ? -18.777 -23.940 -3.518  0.50 32.06 ? 306 HOH A O    1 
HETATM 2859 O  O    B HOH G 6 .   ? -17.827 -24.056 -4.255  0.50 22.49 ? 306 HOH A O    1 
HETATM 2860 O  O    . HOH G 6 .   ? -25.108 -11.093 24.060  1.00 27.90 ? 307 HOH A O    1 
HETATM 2861 O  O    . HOH G 6 .   ? 5.800   0.841   8.531   1.00 30.16 ? 308 HOH A O    1 
HETATM 2862 O  O    . HOH G 6 .   ? -12.089 13.210  5.069   1.00 30.15 ? 309 HOH A O    1 
HETATM 2863 O  O    . HOH G 6 .   ? -15.363 -10.164 37.791  1.00 29.85 ? 310 HOH A O    1 
HETATM 2864 O  O    . HOH G 6 .   ? 1.476   -17.623 7.204   1.00 25.93 ? 311 HOH A O    1 
HETATM 2865 O  O    A HOH G 6 .   ? -27.168 -10.316 14.682  0.50 16.22 ? 312 HOH A O    1 
HETATM 2866 O  O    B HOH G 6 .   ? -25.722 -9.651  14.767  0.50 20.13 ? 312 HOH A O    1 
HETATM 2867 O  O    . HOH G 6 .   ? 5.753   2.515   -3.435  1.00 31.05 ? 313 HOH A O    1 
HETATM 2868 O  O    . HOH G 6 .   ? -14.901 9.353   31.738  1.00 34.77 ? 314 HOH A O    1 
HETATM 2869 O  O    . HOH G 6 .   ? -3.419  17.655  14.102  1.00 32.60 ? 315 HOH A O    1 
HETATM 2870 O  O    . HOH G 6 .   ? 15.347  -1.256  26.098  1.00 19.92 ? 316 HOH A O    1 
HETATM 2871 O  O    . HOH G 6 .   ? 4.504   -10.871 -7.304  1.00 37.74 ? 317 HOH A O    1 
HETATM 2872 O  O    . HOH G 6 .   ? -25.327 -1.668  -0.093  1.00 31.33 ? 318 HOH A O    1 
HETATM 2873 O  O    . HOH G 6 .   ? -4.575  17.152  11.988  1.00 28.91 ? 319 HOH A O    1 
HETATM 2874 O  O    . HOH G 6 .   ? 3.250   2.675   -0.061  1.00 28.73 ? 320 HOH A O    1 
HETATM 2875 O  O    . HOH G 6 .   ? 12.746  -9.535  5.263   1.00 33.76 ? 321 HOH A O    1 
HETATM 2876 O  O    . HOH G 6 .   ? -17.930 -12.174 31.471  1.00 28.07 ? 322 HOH A O    1 
HETATM 2877 O  O    . HOH G 6 .   ? 6.408   -8.129  -10.450 1.00 32.78 ? 323 HOH A O    1 
HETATM 2878 O  O    . HOH G 6 .   ? -4.402  -1.630  38.053  1.00 29.20 ? 324 HOH A O    1 
HETATM 2879 O  O    . HOH G 6 .   ? -25.563 -8.647  11.136  1.00 21.07 ? 325 HOH A O    1 
HETATM 2880 O  O    . HOH G 6 .   ? 1.087   -10.076 28.820  1.00 32.03 ? 326 HOH A O    1 
HETATM 2881 O  O    . HOH G 6 .   ? 11.828  -6.475  7.796   1.00 29.36 ? 327 HOH A O    1 
HETATM 2882 O  O    . HOH G 6 .   ? 9.830   -9.317  -7.444  1.00 42.57 ? 328 HOH A O    1 
HETATM 2883 O  O    . HOH G 6 .   ? -19.647 17.997  17.750  1.00 28.26 ? 329 HOH A O    1 
HETATM 2884 O  O    . HOH G 6 .   ? -24.290 -14.284 19.563  1.00 31.86 ? 330 HOH A O    1 
HETATM 2885 O  O    . HOH G 6 .   ? -26.712 -6.196  4.942   1.00 32.62 ? 331 HOH A O    1 
HETATM 2886 O  O    . HOH G 6 .   ? 4.477   -0.864  -5.340  1.00 29.90 ? 332 HOH A O    1 
HETATM 2887 O  O    . HOH G 6 .   ? 10.288  -8.834  8.519   1.00 29.80 ? 333 HOH A O    1 
HETATM 2888 O  O    . HOH G 6 .   ? -1.310  -1.304  -12.902 1.00 41.12 ? 334 HOH A O    1 
HETATM 2889 O  O    . HOH G 6 .   ? -26.052 12.241  13.351  1.00 44.21 ? 335 HOH A O    1 
HETATM 2890 O  O    . HOH G 6 .   ? 3.905   -2.525  5.112   1.00 36.63 ? 336 HOH A O    1 
HETATM 2891 O  O    . HOH G 6 .   ? 9.199   7.590   19.177  1.00 34.15 ? 337 HOH A O    1 
HETATM 2892 O  O    . HOH G 6 .   ? 1.430   10.642  15.490  1.00 36.40 ? 338 HOH A O    1 
HETATM 2893 O  O    . HOH G 6 .   ? 1.694   -9.850  31.255  1.00 35.84 ? 339 HOH A O    1 
HETATM 2894 O  O    . HOH G 6 .   ? 3.075   8.947   13.777  1.00 41.71 ? 340 HOH A O    1 
HETATM 2895 O  O    . HOH G 6 .   ? 6.583   8.442   18.216  1.00 30.91 ? 341 HOH A O    1 
HETATM 2896 O  O    . HOH G 6 .   ? 5.001   11.406  20.040  1.00 36.60 ? 342 HOH A O    1 
HETATM 2897 O  O    . HOH G 6 .   ? 4.553   -11.231 23.535  1.00 38.13 ? 343 HOH A O    1 
HETATM 2898 O  O    . HOH G 6 .   ? -4.801  -0.099  40.738  1.00 40.63 ? 344 HOH A O    1 
HETATM 2899 O  O    . HOH G 6 .   ? -13.646 14.433  6.289   1.00 35.85 ? 345 HOH A O    1 
HETATM 2900 O  O    . HOH G 6 .   ? 11.280  -3.156  -4.286  1.00 35.63 ? 346 HOH A O    1 
HETATM 2901 O  O    . HOH G 6 .   ? -1.905  -21.525 25.838  1.00 33.53 ? 347 HOH A O    1 
HETATM 2902 O  O    . HOH G 6 .   ? 4.680   -5.916  34.087  1.00 38.04 ? 348 HOH A O    1 
HETATM 2903 O  O    . HOH G 6 .   ? -8.525  -15.476 33.118  0.50 25.51 ? 349 HOH A O    1 
HETATM 2904 O  O    . HOH G 6 .   ? -20.908 -0.229  -2.128  1.00 31.81 ? 350 HOH A O    1 
HETATM 2905 O  O    . HOH G 6 .   ? -10.616 -5.623  38.598  1.00 27.87 ? 351 HOH A O    1 
HETATM 2906 O  O    . HOH G 6 .   ? -18.044 19.100  5.958   1.00 14.73 ? 352 HOH A O    1 
HETATM 2907 O  O    . HOH G 6 .   ? 7.938   -9.491  16.764  1.00 19.86 ? 353 HOH A O    1 
HETATM 2908 O  O    . HOH G 6 .   ? 10.314  -10.806 16.243  1.00 21.44 ? 354 HOH A O    1 
HETATM 2909 O  O    . HOH G 6 .   ? -0.552  12.072  14.108  1.00 34.40 ? 355 HOH A O    1 
HETATM 2910 O  O    . HOH G 6 .   ? 14.612  0.102   15.166  1.00 26.27 ? 356 HOH A O    1 
HETATM 2911 O  O    . HOH G 6 .   ? -4.536  -13.612 18.111  1.00 6.95  ? 357 HOH A O    1 
HETATM 2912 O  O    . HOH G 6 .   ? -1.244  -4.020  15.740  1.00 7.47  ? 358 HOH A O    1 
HETATM 2913 O  O    . HOH G 6 .   ? -17.089 -8.453  20.456  1.00 6.97  ? 359 HOH A O    1 
HETATM 2914 O  O    . HOH G 6 .   ? -3.511  -11.215 20.968  1.00 7.32  ? 360 HOH A O    1 
HETATM 2915 O  O    . HOH G 6 .   ? -10.657 8.694   25.684  1.00 8.20  ? 361 HOH A O    1 
HETATM 2916 O  O    . HOH G 6 .   ? -8.784  -3.827  7.922   1.00 8.30  ? 362 HOH A O    1 
HETATM 2917 O  O    . HOH G 6 .   ? -3.435  -13.329 25.221  1.00 8.42  ? 363 HOH A O    1 
HETATM 2918 O  O    . HOH G 6 .   ? -2.096  -12.377 22.919  1.00 8.23  ? 364 HOH A O    1 
HETATM 2919 O  O    . HOH G 6 .   ? -12.960 -17.262 16.937  1.00 8.88  ? 365 HOH A O    1 
HETATM 2920 O  O    . HOH G 6 .   ? -2.519  -8.802  29.208  1.00 9.76  ? 366 HOH A O    1 
HETATM 2921 O  O    . HOH G 6 .   ? -10.446 -18.352 17.132  1.00 8.81  ? 367 HOH A O    1 
HETATM 2922 O  O    . HOH G 6 .   ? -8.019  -15.496 11.390  1.00 8.34  ? 368 HOH A O    1 
HETATM 2923 O  O    . HOH G 6 .   ? -3.858  -15.964 24.417  1.00 10.07 ? 369 HOH A O    1 
HETATM 2924 O  O    . HOH G 6 .   ? -18.034 -20.407 7.988   1.00 11.02 ? 370 HOH A O    1 
HETATM 2925 O  O    . HOH G 6 .   ? -21.703 -7.233  23.710  1.00 10.28 ? 371 HOH A O    1 
HETATM 2926 O  O    . HOH G 6 .   ? -6.813  -20.302 19.585  1.00 9.80  ? 372 HOH A O    1 
HETATM 2927 O  O    . HOH G 6 .   ? -16.159 -12.398 24.516  1.00 11.02 ? 373 HOH A O    1 
HETATM 2928 O  O    . HOH G 6 .   ? -13.108 -16.899 26.792  1.00 11.18 ? 374 HOH A O    1 
HETATM 2929 O  O    . HOH G 6 .   ? -14.767 -18.583 18.761  1.00 10.72 ? 375 HOH A O    1 
HETATM 2930 O  O    . HOH G 6 .   ? 1.222   -1.512  29.563  1.00 12.55 ? 376 HOH A O    1 
HETATM 2931 O  O    . HOH G 6 .   ? 4.902   -4.915  21.083  1.00 12.34 ? 377 HOH A O    1 
HETATM 2932 O  O    . HOH G 6 .   ? -13.538 -18.569 14.618  1.00 10.41 ? 378 HOH A O    1 
HETATM 2933 O  O    . HOH G 6 .   ? -10.754 -19.490 20.185  1.00 11.51 ? 379 HOH A O    1 
HETATM 2934 O  O    . HOH G 6 .   ? 3.641   5.038   29.877  1.00 16.36 ? 380 HOH A O    1 
HETATM 2935 O  O    . HOH G 6 .   ? -13.908 -21.292 15.251  1.00 12.59 ? 381 HOH A O    1 
HETATM 2936 O  O    . HOH G 6 .   ? 8.110   -1.688  -10.549 1.00 15.58 ? 382 HOH A O    1 
HETATM 2937 O  O    . HOH G 6 .   ? -4.788  0.994   43.672  1.00 20.38 ? 383 HOH A O    1 
HETATM 2938 O  O    . HOH G 6 .   ? -17.495 -16.173 22.121  1.00 15.40 ? 384 HOH A O    1 
HETATM 2939 O  O    A HOH G 6 .   ? -22.289 5.778   4.912   0.50 9.21  ? 385 HOH A O    1 
HETATM 2940 O  O    B HOH G 6 .   ? -21.397 5.779   4.547   0.50 9.62  ? 385 HOH A O    1 
HETATM 2941 O  O    . HOH G 6 .   ? -15.055 -21.142 17.778  1.00 12.97 ? 386 HOH A O    1 
HETATM 2942 O  O    . HOH G 6 .   ? -13.935 10.295  28.053  1.00 13.80 ? 387 HOH A O    1 
HETATM 2943 O  O    . HOH G 6 .   ? -19.312 10.086  8.872   1.00 12.76 ? 388 HOH A O    1 
HETATM 2944 O  O    . HOH G 6 .   ? -18.023 10.738  11.347  1.00 13.49 ? 389 HOH A O    1 
HETATM 2945 O  O    . HOH G 6 .   ? -9.588  -7.993  34.257  1.00 18.41 ? 390 HOH A O    1 
HETATM 2946 O  O    . HOH G 6 .   ? -2.580  -3.197  11.455  1.00 14.45 ? 391 HOH A O    1 
HETATM 2947 O  O    . HOH G 6 .   ? -16.904 -14.019 26.499  1.00 14.62 ? 392 HOH A O    1 
HETATM 2948 O  O    . HOH G 6 .   ? -3.327  3.968   40.820  1.00 16.00 ? 393 HOH A O    1 
HETATM 2949 O  O    . HOH G 6 .   ? 1.178   8.853   24.379  1.00 15.22 ? 394 HOH A O    1 
HETATM 2950 O  O    . HOH G 6 .   ? 7.574   6.099   21.703  1.00 14.78 ? 395 HOH A O    1 
HETATM 2951 O  O    . HOH G 6 .   ? -24.987 -7.693  9.032   1.00 17.06 ? 396 HOH A O    1 
HETATM 2952 O  O    . HOH G 6 .   ? -24.228 8.568   20.236  1.00 15.15 ? 397 HOH A O    1 
HETATM 2953 O  O    . HOH G 6 .   ? 5.383   7.102   20.297  1.00 14.71 ? 398 HOH A O    1 
HETATM 2954 O  O    . HOH G 6 .   ? 8.604   -3.849  21.110  1.00 13.67 ? 399 HOH A O    1 
HETATM 2955 O  O    . HOH G 6 .   ? -22.225 -18.300 13.507  1.00 16.49 ? 400 HOH A O    1 
HETATM 2956 O  O    . HOH G 6 .   ? -16.406 -9.960  33.107  1.00 15.44 ? 401 HOH A O    1 
HETATM 2957 O  O    . HOH G 6 .   ? -15.490 -21.905 13.144  1.00 11.18 ? 402 HOH A O    1 
HETATM 2958 O  O    . HOH G 6 .   ? -24.091 -0.726  26.602  1.00 16.09 ? 403 HOH A O    1 
HETATM 2959 O  O    . HOH G 6 .   ? -1.178  -11.188 29.095  1.00 14.61 ? 404 HOH A O    1 
HETATM 2960 O  O    . HOH G 6 .   ? -20.406 10.684  26.973  1.00 14.46 ? 405 HOH A O    1 
HETATM 2961 O  O    A HOH G 6 .   ? 0.060   -1.120  -4.792  0.50 8.71  ? 406 HOH A O    1 
HETATM 2962 O  O    B HOH G 6 .   ? 0.541   -1.402  -4.646  0.50 15.19 ? 406 HOH A O    1 
HETATM 2963 O  O    . HOH G 6 .   ? -16.270 15.851  23.859  1.00 14.24 ? 407 HOH A O    1 
HETATM 2964 O  O    . HOH G 6 .   ? -17.029 -17.928 20.112  1.00 18.59 ? 408 HOH A O    1 
HETATM 2965 O  O    . HOH G 6 .   ? -0.523  10.854  23.502  1.00 13.12 ? 409 HOH A O    1 
HETATM 2966 O  O    . HOH G 6 .   ? -12.094 2.647   31.161  1.00 15.31 ? 410 HOH A O    1 
HETATM 2967 O  O    . HOH G 6 .   ? -6.858  -14.943 31.661  1.00 16.03 ? 411 HOH A O    1 
HETATM 2968 O  O    . HOH G 6 .   ? -10.311 14.654  12.312  1.00 14.10 ? 412 HOH A O    1 
HETATM 2969 O  O    . HOH G 6 .   ? -8.582  -19.906 26.833  1.00 16.29 ? 413 HOH A O    1 
HETATM 2970 O  O    . HOH G 6 .   ? -9.098  -5.835  36.084  1.00 15.04 ? 414 HOH A O    1 
HETATM 2971 O  O    . HOH G 6 .   ? -22.936 -5.868  2.634   1.00 18.97 ? 415 HOH A O    1 
HETATM 2972 O  O    . HOH G 6 .   ? -8.516  -14.723 40.878  1.00 13.59 ? 416 HOH A O    1 
HETATM 2973 O  O    . HOH G 6 .   ? -14.072 14.180  27.311  1.00 17.48 ? 417 HOH A O    1 
HETATM 2974 O  O    . HOH G 6 .   ? 4.191   -3.408  26.632  1.00 17.03 ? 418 HOH A O    1 
HETATM 2975 O  O    . HOH G 6 .   ? 2.616   -4.292  7.912   1.00 17.40 ? 419 HOH A O    1 
HETATM 2976 O  O    . HOH G 6 .   ? -23.390 -2.960  6.657   1.00 18.79 ? 420 HOH A O    1 
HETATM 2977 O  O    . HOH G 6 .   ? 6.813   -14.689 -6.378  1.00 15.05 ? 421 HOH A O    1 
HETATM 2978 O  O    . HOH G 6 .   ? -1.945  -17.515 25.647  1.00 23.77 ? 422 HOH A O    1 
HETATM 2979 O  O    A HOH G 6 .   ? -23.329 -0.742  3.805   0.50 14.09 ? 423 HOH A O    1 
HETATM 2980 O  O    B HOH G 6 .   ? -24.354 -0.700  4.133   0.50 12.91 ? 423 HOH A O    1 
HETATM 2981 O  O    . HOH G 6 .   ? -6.278  -19.803 23.861  1.00 15.00 ? 424 HOH A O    1 
HETATM 2982 O  O    . HOH G 6 .   ? -10.681 8.478   7.770   1.00 18.62 ? 425 HOH A O    1 
HETATM 2983 O  O    . HOH G 6 .   ? -1.415  -13.108 27.133  1.00 23.68 ? 426 HOH A O    1 
HETATM 2984 O  O    . HOH G 6 .   ? -0.337  -14.423 22.221  1.00 16.41 ? 427 HOH A O    1 
HETATM 2985 O  O    . HOH G 6 .   ? -8.311  14.608  10.487  1.00 23.44 ? 428 HOH A O    1 
HETATM 2986 O  O    A HOH G 6 .   ? -4.339  -12.066 32.041  0.50 13.19 ? 429 HOH A O    1 
HETATM 2987 O  O    B HOH G 6 .   ? -5.064  -11.973 32.287  0.50 13.64 ? 429 HOH A O    1 
HETATM 2988 O  O    . HOH G 6 .   ? -6.213  15.225  11.905  1.00 21.01 ? 430 HOH A O    1 
HETATM 2989 O  O    . HOH G 6 .   ? -7.388  -8.681  32.756  1.00 14.77 ? 431 HOH A O    1 
HETATM 2990 O  O    . HOH G 6 .   ? -21.289 -19.586 6.521   1.00 18.88 ? 432 HOH A O    1 
HETATM 2991 O  O    A HOH G 6 .   ? -16.356 -11.700 41.529  0.50 19.00 ? 433 HOH A O    1 
HETATM 2992 O  O    B HOH G 6 .   ? -16.608 -11.104 42.114  0.50 13.43 ? 433 HOH A O    1 
HETATM 2993 O  O    . HOH G 6 .   ? -17.806 -21.174 17.573  1.00 18.55 ? 434 HOH A O    1 
HETATM 2994 O  O    . HOH G 6 .   ? -8.370  -17.567 35.045  1.00 18.77 ? 435 HOH A O    1 
HETATM 2995 O  O    . HOH G 6 .   ? -4.288  -1.164  11.835  1.00 15.58 ? 436 HOH A O    1 
HETATM 2996 O  O    . HOH G 6 .   ? -10.613 -20.341 25.094  1.00 13.90 ? 437 HOH A O    1 
HETATM 2997 O  O    . HOH G 6 .   ? -11.215 1.139   33.600  1.00 17.43 ? 438 HOH A O    1 
HETATM 2998 O  O    . HOH G 6 .   ? -26.868 -2.399  14.568  1.00 15.80 ? 439 HOH A O    1 
HETATM 2999 O  O    . HOH G 6 .   ? -0.666  -8.620  32.599  1.00 23.06 ? 440 HOH A O    1 
HETATM 3000 O  O    . HOH G 6 .   ? -22.996 -11.595 13.989  1.00 19.18 ? 441 HOH A O    1 
HETATM 3001 O  O    . HOH G 6 .   ? 2.523   -13.311 5.219   1.00 19.49 ? 442 HOH A O    1 
HETATM 3002 O  O    . HOH G 6 .   ? -3.567  -12.946 -2.852  1.00 22.53 ? 443 HOH A O    1 
HETATM 3003 O  O    . HOH G 6 .   ? -8.567  -15.503 36.799  1.00 22.44 ? 444 HOH A O    1 
HETATM 3004 O  O    . HOH G 6 .   ? 9.744   -4.931  -7.900  1.00 22.93 ? 445 HOH A O    1 
HETATM 3005 O  O    . HOH G 6 .   ? -31.004 1.350   26.069  1.00 21.77 ? 446 HOH A O    1 
HETATM 3006 O  O    . HOH G 6 .   ? -28.829 0.255   24.573  1.00 18.51 ? 447 HOH A O    1 
HETATM 3007 O  O    . HOH G 6 .   ? -11.071 15.335  32.423  1.00 15.80 ? 448 HOH A O    1 
HETATM 3008 O  O    . HOH G 6 .   ? -3.459  -23.114 21.450  1.00 16.38 ? 449 HOH A O    1 
HETATM 3009 O  O    . HOH G 6 .   ? -26.170 -6.384  13.118  1.00 19.72 ? 450 HOH A O    1 
HETATM 3010 O  O    . HOH G 6 .   ? 1.902   -15.677 9.292   1.00 19.33 ? 451 HOH A O    1 
HETATM 3011 O  O    . HOH G 6 .   ? -4.889  -20.700 21.529  1.00 15.69 ? 452 HOH A O    1 
HETATM 3012 O  O    . HOH G 6 .   ? -15.557 9.003   -2.131  1.00 21.03 ? 453 HOH A O    1 
HETATM 3013 O  O    . HOH G 6 .   ? -4.763  -12.726 41.047  1.00 20.00 ? 454 HOH A O    1 
HETATM 3014 O  O    . HOH G 6 .   ? -4.833  -7.406  38.028  1.00 23.82 ? 455 HOH A O    1 
HETATM 3015 O  O    . HOH G 6 .   ? -29.172 -5.785  24.478  1.00 21.13 ? 456 HOH A O    1 
HETATM 3016 O  O    . HOH G 6 .   ? -10.707 4.897   31.084  1.00 18.14 ? 457 HOH A O    1 
HETATM 3017 O  O    . HOH G 6 .   ? 4.290   -6.477  7.860   1.00 21.30 ? 458 HOH A O    1 
HETATM 3018 O  O    . HOH G 6 .   ? 11.118  -3.164  -12.254 1.00 17.98 ? 459 HOH A O    1 
HETATM 3019 O  O    . HOH G 6 .   ? -11.141 -19.674 7.294   1.00 22.54 ? 460 HOH A O    1 
HETATM 3020 O  O    . HOH G 6 .   ? -23.460 -13.189 11.292  1.00 16.83 ? 461 HOH A O    1 
HETATM 3021 O  O    . HOH G 6 .   ? -18.692 -21.208 14.716  1.00 16.29 ? 462 HOH A O    1 
HETATM 3022 O  O    . HOH G 6 .   ? -1.993  -11.839 31.729  1.00 28.28 ? 463 HOH A O    1 
HETATM 3023 O  O    . HOH G 6 .   ? -26.215 3.390   15.520  1.00 22.82 ? 464 HOH A O    1 
HETATM 3024 O  O    . HOH G 6 .   ? -9.915  1.526   39.248  1.00 26.19 ? 465 HOH A O    1 
HETATM 3025 O  O    . HOH G 6 .   ? 10.435  -7.072  -8.788  1.00 23.04 ? 466 HOH A O    1 
HETATM 3026 O  O    A HOH G 6 .   ? 0.886   -6.835  34.629  0.50 18.69 ? 467 HOH A O    1 
HETATM 3027 O  O    B HOH G 6 .   ? 1.722   -6.096  34.469  0.50 12.76 ? 467 HOH A O    1 
HETATM 3028 O  O    . HOH G 6 .   ? -5.915  -4.596  -6.548  1.00 27.76 ? 468 HOH A O    1 
HETATM 3029 O  O    . HOH G 6 .   ? -4.225  -8.577  31.328  1.00 17.73 ? 469 HOH A O    1 
HETATM 3030 O  O    . HOH G 6 .   ? -14.094 3.641   33.315  1.00 20.46 ? 470 HOH A O    1 
HETATM 3031 O  O    . HOH G 6 .   ? -1.554  11.553  26.014  1.00 20.28 ? 471 HOH A O    1 
HETATM 3032 O  O    . HOH G 6 .   ? 1.317   -11.857 25.104  1.00 21.94 ? 472 HOH A O    1 
HETATM 3033 O  O    . HOH G 6 .   ? -8.241  21.761  21.773  1.00 10.14 ? 473 HOH A O    1 
HETATM 3034 O  O    . HOH G 6 .   ? -12.466 12.468  29.359  1.00 22.10 ? 474 HOH A O    1 
HETATM 3035 O  O    . HOH G 6 .   ? 1.753   12.438  22.896  1.00 25.74 ? 475 HOH A O    1 
HETATM 3036 O  O    . HOH G 6 .   ? -10.718 -19.012 34.663  1.00 19.06 ? 476 HOH A O    1 
HETATM 3037 O  O    . HOH G 6 .   ? -11.057 -15.148 34.314  0.50 19.73 ? 477 HOH A O    1 
HETATM 3038 O  O    . HOH G 6 .   ? -24.830 -9.434  1.907   1.00 22.18 ? 478 HOH A O    1 
HETATM 3039 O  O    A HOH G 6 .   ? -16.991 -19.433 35.290  0.50 18.42 ? 479 HOH A O    1 
HETATM 3040 O  O    B HOH G 6 .   ? -18.073 -19.492 35.422  0.50 13.88 ? 479 HOH A O    1 
HETATM 3041 O  O    . HOH G 6 .   ? -13.123 -22.254 8.617   1.00 20.37 ? 480 HOH A O    1 
HETATM 3042 O  O    . HOH G 6 .   ? -21.324 -20.628 14.609  1.00 23.89 ? 481 HOH A O    1 
HETATM 3043 O  O    . HOH G 6 .   ? -4.837  7.620   5.795   1.00 18.45 ? 482 HOH A O    1 
HETATM 3044 O  O    . HOH G 6 .   ? -19.772 14.832  16.544  1.00 18.81 ? 483 HOH A O    1 
HETATM 3045 O  O    . HOH G 6 .   ? -21.734 -21.601 12.316  1.00 20.45 ? 484 HOH A O    1 
HETATM 3046 O  O    . HOH G 6 .   ? -5.164  2.228   37.431  1.00 22.31 ? 485 HOH A O    1 
HETATM 3047 O  O    . HOH G 6 .   ? -15.179 -20.081 23.161  1.00 23.02 ? 486 HOH A O    1 
HETATM 3048 O  O    . HOH G 6 .   ? 4.361   -2.491  29.094  1.00 22.74 ? 487 HOH A O    1 
HETATM 3049 O  O    . HOH G 6 .   ? -23.680 16.793  2.707   1.00 24.14 ? 488 HOH A O    1 
HETATM 3050 O  O    . HOH G 6 .   ? 10.068  -2.607  13.917  1.00 22.62 ? 489 HOH A O    1 
HETATM 3051 O  O    . HOH G 6 .   ? -18.524 -12.356 -3.635  1.00 20.25 ? 490 HOH A O    1 
HETATM 3052 O  O    . HOH G 6 .   ? -8.283  7.580   8.347   1.00 19.93 ? 491 HOH A O    1 
HETATM 3053 O  O    . HOH G 6 .   ? -7.240  -16.790 1.435   1.00 18.60 ? 492 HOH A O    1 
HETATM 3054 O  O    . HOH G 6 .   ? -22.093 3.908   -2.958  1.00 25.79 ? 493 HOH A O    1 
HETATM 3055 O  O    . HOH G 6 .   ? -2.728  -14.442 37.052  1.00 26.64 ? 494 HOH A O    1 
HETATM 3056 O  O    . HOH G 6 .   ? 6.442   -5.544  3.876   1.00 29.27 ? 495 HOH A O    1 
HETATM 3057 O  O    A HOH G 6 .   ? -27.669 -7.076  7.674   0.50 20.07 ? 496 HOH A O    1 
HETATM 3058 O  O    B HOH G 6 .   ? -26.872 -6.547  7.593   0.50 26.11 ? 496 HOH A O    1 
HETATM 3059 O  O    . HOH G 6 .   ? -10.335 15.812  29.641  1.00 25.11 ? 497 HOH A O    1 
HETATM 3060 O  O    . HOH G 6 .   ? -33.631 -4.655  23.778  1.00 21.27 ? 498 HOH A O    1 
HETATM 3061 O  O    . HOH G 6 .   ? -0.478  13.904  16.137  1.00 21.63 ? 499 HOH A O    1 
HETATM 3062 O  O    . HOH G 6 .   ? -24.375 -7.015  0.361   1.00 30.47 ? 500 HOH A O    1 
HETATM 3063 O  O    . HOH G 6 .   ? -12.723 3.699   -6.858  1.00 29.45 ? 501 HOH A O    1 
HETATM 3064 O  O    . HOH G 6 .   ? -19.670 -20.694 4.847   1.00 24.43 ? 502 HOH A O    1 
HETATM 3065 O  O    . HOH G 6 .   ? 2.452   -11.436 9.377   1.00 20.85 ? 503 HOH A O    1 
HETATM 3066 O  O    . HOH G 6 .   ? 11.768  -9.758  -0.810  1.00 25.64 ? 504 HOH A O    1 
HETATM 3067 O  O    . HOH G 6 .   ? -34.029 3.148   27.833  1.00 25.58 ? 505 HOH A O    1 
HETATM 3068 O  O    . HOH G 6 .   ? -24.212 0.031   1.362   1.00 30.62 ? 506 HOH A O    1 
HETATM 3069 O  O    . HOH G 6 .   ? -9.359  -10.045 -1.256  1.00 22.19 ? 507 HOH A O    1 
HETATM 3070 O  O    . HOH G 6 .   ? 2.853   -13.525 8.027   1.00 22.17 ? 508 HOH A O    1 
HETATM 3071 O  O    . HOH G 6 .   ? -8.457  0.722   -6.518  1.00 29.29 ? 509 HOH A O    1 
HETATM 3072 O  O    . HOH G 6 .   ? -16.457 7.332   36.722  1.00 21.23 ? 510 HOH A O    1 
HETATM 3073 O  O    . HOH G 6 .   ? -12.875 -8.915  -3.058  1.00 29.09 ? 511 HOH A O    1 
HETATM 3074 O  O    . HOH G 6 .   ? -26.065 6.148   27.250  1.00 20.70 ? 512 HOH A O    1 
HETATM 3075 O  O    . HOH G 6 .   ? -26.951 -3.958  25.155  1.00 18.81 ? 513 HOH A O    1 
HETATM 3076 O  O    . HOH G 6 .   ? 0.479   0.615   -6.750  1.00 34.72 ? 514 HOH A O    1 
HETATM 3077 O  O    . HOH G 6 .   ? -24.739 4.735   8.278   1.00 29.93 ? 515 HOH A O    1 
HETATM 3078 O  O    . HOH G 6 .   ? -6.022  -20.896 26.319  1.00 21.34 ? 516 HOH A O    1 
HETATM 3079 O  O    . HOH G 6 .   ? 2.858   1.085   -6.277  1.00 31.18 ? 517 HOH A O    1 
HETATM 3080 O  O    . HOH G 6 .   ? -2.607  6.318   5.921   1.00 26.33 ? 518 HOH A O    1 
HETATM 3081 O  O    . HOH G 6 .   ? -30.474 -0.298  16.230  1.00 19.82 ? 519 HOH A O    1 
HETATM 3082 O  O    . HOH G 6 .   ? -25.353 11.066  19.603  1.00 24.57 ? 520 HOH A O    1 
HETATM 3083 O  O    . HOH G 6 .   ? 2.609   4.341   11.965  1.00 24.73 ? 521 HOH A O    1 
HETATM 3084 O  O    . HOH G 6 .   ? -37.102 -7.301  22.366  1.00 24.09 ? 522 HOH A O    1 
HETATM 3085 O  O    . HOH G 6 .   ? 1.947   -7.111  -8.335  1.00 28.67 ? 523 HOH A O    1 
HETATM 3086 O  O    . HOH G 6 .   ? -25.652 -10.649 17.794  1.00 20.47 ? 524 HOH A O    1 
HETATM 3087 O  O    A HOH G 6 .   ? -21.556 7.889   2.054   0.50 8.52  ? 525 HOH A O    1 
HETATM 3088 O  O    B HOH G 6 .   ? -20.523 7.937   1.702   0.50 9.38  ? 525 HOH A O    1 
HETATM 3089 O  O    . HOH G 6 .   ? -15.579 -16.418 25.808  1.00 25.66 ? 526 HOH A O    1 
HETATM 3090 O  O    . HOH G 6 .   ? 12.020  -9.683  -5.615  1.00 22.40 ? 527 HOH A O    1 
HETATM 3091 O  O    . HOH G 6 .   ? 0.312   -0.070  -14.964 1.00 28.10 ? 528 HOH A O    1 
HETATM 3092 O  O    . HOH G 6 .   ? -2.546  -19.249 21.462  1.00 22.25 ? 529 HOH A O    1 
HETATM 3093 O  O    . HOH G 6 .   ? -20.078 -25.337 19.117  1.00 23.49 ? 530 HOH A O    1 
HETATM 3094 O  O    . HOH G 6 .   ? -4.893  -9.685  33.693  1.00 28.75 ? 531 HOH A O    1 
HETATM 3095 O  O    . HOH G 6 .   ? -4.769  -15.900 0.659   1.00 23.18 ? 532 HOH A O    1 
HETATM 3096 O  O    . HOH G 6 .   ? -2.688  6.054   -0.805  1.00 26.04 ? 533 HOH A O    1 
HETATM 3097 O  O    . HOH G 6 .   ? -6.080  -23.485 27.620  1.00 25.89 ? 534 HOH A O    1 
HETATM 3098 O  O    . HOH G 6 .   ? -1.099  -17.559 -1.899  1.00 27.10 ? 535 HOH A O    1 
HETATM 3099 O  O    . HOH G 6 .   ? -15.107 2.440   38.875  1.00 21.46 ? 536 HOH A O    1 
HETATM 3100 O  O    A HOH G 6 .   ? -24.257 -16.506 3.612   0.50 21.70 ? 537 HOH A O    1 
HETATM 3101 O  O    B HOH G 6 .   ? -22.779 -17.190 3.260   0.50 14.49 ? 537 HOH A O    1 
HETATM 3102 O  O    . HOH G 6 .   ? -8.395  -1.385  41.427  1.00 31.71 ? 538 HOH A O    1 
HETATM 3103 O  O    . HOH G 6 .   ? 3.752   9.896   23.926  1.00 24.12 ? 539 HOH A O    1 
HETATM 3104 O  O    . HOH G 6 .   ? -24.120 -2.883  29.329  1.00 26.27 ? 540 HOH A O    1 
HETATM 3105 O  O    A HOH G 6 .   ? -11.782 -24.856 9.173   0.50 16.86 ? 541 HOH A O    1 
HETATM 3106 O  O    B HOH G 6 .   ? -12.588 -25.191 7.961   0.50 18.05 ? 541 HOH A O    1 
HETATM 3107 O  O    . HOH G 6 .   ? -26.472 -7.723  30.322  1.00 32.63 ? 542 HOH A O    1 
HETATM 3108 O  O    . HOH G 6 .   ? -5.060  -13.876 38.628  1.00 29.19 ? 543 HOH A O    1 
HETATM 3109 O  O    . HOH G 6 .   ? 3.265   2.886   8.150   1.00 34.22 ? 544 HOH A O    1 
HETATM 3110 O  O    . HOH G 6 .   ? -2.449  -0.025  44.351  1.00 30.54 ? 545 HOH A O    1 
HETATM 3111 O  O    . HOH G 6 .   ? -3.879  -15.635 -2.302  1.00 29.75 ? 546 HOH A O    1 
HETATM 3112 O  O    . HOH G 6 .   ? 0.985   3.107   -18.074 1.00 26.02 ? 547 HOH A O    1 
HETATM 3113 O  O    . HOH G 6 .   ? 1.922   -14.170 20.810  1.00 25.70 ? 548 HOH A O    1 
HETATM 3114 O  O    . HOH G 6 .   ? -27.729 2.671   23.751  1.00 28.41 ? 549 HOH A O    1 
HETATM 3115 O  O    . HOH G 6 .   ? -1.195  -6.071  36.563  1.00 24.27 ? 550 HOH A O    1 
HETATM 3116 O  O    . HOH G 6 .   ? -10.185 -26.119 5.656   1.00 27.97 ? 551 HOH A O    1 
HETATM 3117 O  O    A HOH G 6 .   ? -8.253  11.760  0.178   0.50 13.69 ? 552 HOH A O    1 
HETATM 3118 O  O    B HOH G 6 .   ? -7.443  12.704  0.972   0.50 17.76 ? 552 HOH A O    1 
HETATM 3119 O  O    . HOH G 6 .   ? -30.663 -7.057  22.544  1.00 26.70 ? 553 HOH A O    1 
HETATM 3120 O  O    . HOH G 6 .   ? -10.084 -23.545 10.089  1.00 22.18 ? 554 HOH A O    1 
HETATM 3121 O  O    . HOH G 6 .   ? -26.405 2.768   21.037  1.00 22.23 ? 555 HOH A O    1 
HETATM 3122 O  O    . HOH G 6 .   ? -29.227 -3.754  13.529  1.00 26.19 ? 556 HOH A O    1 
HETATM 3123 O  O    . HOH G 6 .   ? -20.666 8.256   30.236  1.00 24.42 ? 557 HOH A O    1 
HETATM 3124 O  O    . HOH G 6 .   ? 9.450   2.004   12.262  1.00 27.70 ? 558 HOH A O    1 
HETATM 3125 O  O    . HOH G 6 .   ? -11.598 1.074   -7.701  1.00 30.81 ? 559 HOH A O    1 
HETATM 3126 O  O    . HOH G 6 .   ? -25.157 8.748   26.225  1.00 27.75 ? 560 HOH A O    1 
HETATM 3127 O  O    . HOH G 6 .   ? -28.078 5.022   25.459  1.00 32.46 ? 561 HOH A O    1 
HETATM 3128 O  O    . HOH G 6 .   ? -2.130  4.398   7.743   1.00 28.61 ? 562 HOH A O    1 
HETATM 3129 O  O    . HOH G 6 .   ? -14.279 0.611   42.866  1.00 27.65 ? 563 HOH A O    1 
HETATM 3130 O  O    A HOH G 6 .   ? -16.403 -15.883 32.750  0.50 19.19 ? 564 HOH A O    1 
HETATM 3131 O  O    B HOH G 6 .   ? -16.501 -14.741 33.604  0.50 21.05 ? 564 HOH A O    1 
HETATM 3132 O  O    . HOH G 6 .   ? 6.659   -0.574  -1.113  1.00 32.94 ? 565 HOH A O    1 
HETATM 3133 O  O    A HOH G 6 .   ? -5.315  3.457   -5.788  0.50 18.16 ? 566 HOH A O    1 
HETATM 3134 O  O    B HOH G 6 .   ? -4.565  3.287   -5.718  0.50 14.43 ? 566 HOH A O    1 
HETATM 3135 O  O    . HOH G 6 .   ? -22.956 15.239  18.983  1.00 33.01 ? 567 HOH A O    1 
HETATM 3136 O  O    . HOH G 6 .   ? -5.646  -12.422 -5.020  1.00 30.60 ? 568 HOH A O    1 
HETATM 3137 O  O    . HOH G 6 .   ? -17.246 -7.502  39.816  1.00 29.98 ? 569 HOH A O    1 
HETATM 3138 O  O    . HOH G 6 .   ? 3.412   -13.777 12.460  1.00 30.79 ? 570 HOH A O    1 
HETATM 3139 O  O    A HOH G 6 .   ? -14.721 -8.280  -5.484  0.50 16.68 ? 571 HOH A O    1 
HETATM 3140 O  O    B HOH G 6 .   ? -13.719 -8.798  -5.336  0.50 15.06 ? 571 HOH A O    1 
HETATM 3141 O  O    . HOH G 6 .   ? -7.168  -10.133 -4.498  1.00 27.87 ? 572 HOH A O    1 
HETATM 3142 O  O    . HOH G 6 .   ? -25.128 9.629   12.928  1.00 24.75 ? 573 HOH A O    1 
HETATM 3143 O  O    . HOH G 6 .   ? -16.917 18.698  22.556  1.00 35.38 ? 574 HOH A O    1 
HETATM 3144 O  O    . HOH G 6 .   ? -22.974 -14.811 16.219  1.00 26.37 ? 575 HOH A O    1 
HETATM 3145 O  O    . HOH G 6 .   ? -4.680  0.453   9.620   1.00 25.38 ? 576 HOH A O    1 
HETATM 3146 O  O    . HOH G 6 .   ? -12.300 4.236   35.186  1.00 32.93 ? 577 HOH A O    1 
HETATM 3147 O  O    . HOH G 6 .   ? -18.589 -9.051  34.717  1.00 28.27 ? 578 HOH A O    1 
HETATM 3148 O  O    . HOH G 6 .   ? 3.102   1.053   -2.049  1.00 33.80 ? 579 HOH A O    1 
HETATM 3149 O  O    . HOH G 6 .   ? -16.434 5.414   -8.050  1.00 27.20 ? 580 HOH A O    1 
HETATM 3150 O  O    . HOH G 6 .   ? -28.340 5.745   19.092  1.00 35.21 ? 581 HOH A O    1 
HETATM 3151 O  O    . HOH G 6 .   ? -12.984 -0.643  -6.109  1.00 31.60 ? 582 HOH A O    1 
HETATM 3152 O  O    . HOH G 6 .   ? -13.602 -16.660 -0.153  1.00 33.58 ? 583 HOH A O    1 
HETATM 3153 O  O    . HOH G 6 .   ? -1.931  -4.654  -7.131  1.00 22.34 ? 584 HOH A O    1 
HETATM 3154 O  O    . HOH G 6 .   ? -6.886  -8.428  -7.070  1.00 29.55 ? 585 HOH A O    1 
HETATM 3155 O  O    . HOH G 6 .   ? -26.984 4.865   6.479   1.00 36.95 ? 586 HOH A O    1 
HETATM 3156 O  O    . HOH G 6 .   ? -23.247 -0.508  34.533  1.00 26.67 ? 587 HOH A O    1 
HETATM 3157 O  O    . HOH G 6 .   ? -20.238 14.061  29.268  1.00 33.51 ? 588 HOH A O    1 
HETATM 3158 O  O    . HOH G 6 .   ? -16.013 3.650   35.534  1.00 26.55 ? 589 HOH A O    1 
HETATM 3159 O  O    . HOH G 6 .   ? -14.843 5.732   37.036  1.00 24.75 ? 590 HOH A O    1 
HETATM 3160 O  O    . HOH G 6 .   ? -16.971 -11.463 36.630  1.00 24.73 ? 591 HOH A O    1 
HETATM 3161 O  O    . HOH G 6 .   ? -23.414 -11.140 17.052  1.00 23.94 ? 592 HOH A O    1 
HETATM 3162 O  O    . HOH G 6 .   ? -0.800  18.680  21.996  1.00 33.20 ? 593 HOH A O    1 
HETATM 3163 O  O    . HOH G 6 .   ? -7.284  -8.636  -2.392  1.00 26.51 ? 594 HOH A O    1 
HETATM 3164 O  O    . HOH G 6 .   ? -22.065 -14.155 18.609  1.00 23.23 ? 595 HOH A O    1 
HETATM 3165 O  O    . HOH G 6 .   ? -1.357  4.385   -4.849  1.00 31.80 ? 596 HOH A O    1 
HETATM 3166 O  O    . HOH G 6 .   ? 6.652   -1.796  -7.998  1.00 26.80 ? 597 HOH A O    1 
HETATM 3167 O  O    . HOH G 6 .   ? -7.566  8.072   29.656  1.00 20.17 ? 598 HOH A O    1 
HETATM 3168 O  O    . HOH G 6 .   ? -5.394  -13.665 34.470  1.00 37.72 ? 599 HOH A O    1 
HETATM 3169 O  O    . HOH G 6 .   ? -25.606 4.458   4.151   1.00 32.20 ? 600 HOH A O    1 
HETATM 3170 O  O    . HOH G 6 .   ? -0.391  -3.308  39.622  1.00 33.25 ? 601 HOH A O    1 
HETATM 3171 O  O    . HOH G 6 .   ? -24.761 11.977  6.281   1.00 24.97 ? 602 HOH A O    1 
HETATM 3172 O  O    . HOH G 6 .   ? -19.404 14.026  9.209   1.00 26.95 ? 603 HOH A O    1 
HETATM 3173 O  O    . HOH G 6 .   ? 0.463   7.285   29.994  1.00 26.23 ? 604 HOH A O    1 
HETATM 3174 O  O    . HOH G 6 .   ? -19.866 -4.202  41.579  1.00 31.54 ? 605 HOH A O    1 
HETATM 3175 O  O    . HOH G 6 .   ? -25.821 7.999   6.115   1.00 30.19 ? 606 HOH A O    1 
HETATM 3176 O  O    . HOH G 6 .   ? 5.700   -12.860 11.352  1.00 39.50 ? 607 HOH A O    1 
HETATM 3177 O  O    . HOH G 6 .   ? -6.164  -11.709 36.646  1.00 30.15 ? 608 HOH A O    1 
HETATM 3178 O  O    . HOH G 6 .   ? -24.508 13.592  20.548  1.00 30.64 ? 609 HOH A O    1 
HETATM 3179 O  O    . HOH G 6 .   ? -12.983 -22.350 12.259  1.00 21.75 ? 610 HOH A O    1 
HETATM 3180 O  O    . HOH G 6 .   ? 0.481   -19.508 10.741  1.00 27.87 ? 611 HOH A O    1 
HETATM 3181 O  O    . HOH G 6 .   ? -4.677  -8.180  -8.383  1.00 37.93 ? 612 HOH A O    1 
HETATM 3182 O  O    . HOH G 6 .   ? -12.063 9.375   3.224   1.00 19.99 ? 613 HOH A O    1 
HETATM 3183 O  O    . HOH G 6 .   ? 2.062   -4.261  -12.416 1.00 31.04 ? 614 HOH A O    1 
HETATM 3184 O  O    . HOH G 6 .   ? -27.949 6.369   21.552  1.00 27.13 ? 615 HOH A O    1 
HETATM 3185 O  O    . HOH G 6 .   ? 6.190   -2.763  6.836   1.00 30.92 ? 616 HOH A O    1 
HETATM 3186 O  O    . HOH G 6 .   ? -3.644  5.565   -3.017  1.00 24.83 ? 617 HOH A O    1 
HETATM 3187 O  O    . HOH G 6 .   ? -10.367 3.189   37.637  1.00 26.37 ? 618 HOH A O    1 
HETATM 3188 O  O    . HOH G 6 .   ? 6.169   -11.091 15.610  1.00 26.84 ? 619 HOH A O    1 
HETATM 3189 O  O    . HOH G 6 .   ? -0.916  -6.829  -8.005  1.00 36.49 ? 620 HOH A O    1 
HETATM 3190 O  O    . HOH G 6 .   ? -1.160  21.021  23.616  1.00 35.69 ? 621 HOH A 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 3   ? 0.2594 0.2933 0.2824 -0.0109 -0.0076 0.0143  3   HIS A N    
2    C  CA   . HIS A 3   ? 0.2608 0.2937 0.2865 -0.0017 -0.0006 0.0131  3   HIS A CA   
3    C  C    . HIS A 3   ? 0.2551 0.3188 0.2554 0.0031  0.0043  0.0178  3   HIS A C    
4    O  O    . HIS A 3   ? 0.3564 0.3964 0.2833 -0.0175 -0.0575 -0.0313 3   HIS A O    
5    C  CB   . HIS A 3   ? 0.2486 0.2815 0.2860 -0.0478 -0.0264 0.0130  3   HIS A CB   
6    C  CG   . HIS A 3   ? 0.2470 0.2565 0.2870 -0.0381 -0.0296 0.0082  3   HIS A CG   
7    N  ND1  . HIS A 3   ? 0.3215 0.2660 0.3382 0.0392  -0.0326 0.0104  3   HIS A ND1  
8    C  CD2  . HIS A 3   ? 0.2815 0.2210 0.2425 -0.0337 -0.0186 0.0428  3   HIS A CD2  
9    C  CE1  . HIS A 3   ? 0.3264 0.2858 0.3382 0.0027  0.0087  0.0126  3   HIS A CE1  
10   N  NE2  . HIS A 3   ? 0.3310 0.2915 0.3501 -0.0639 -0.0324 0.0015  3   HIS A NE2  
11   N  N    . HIS A 4   ? 0.2272 0.2912 0.2685 -0.0120 0.0285  0.0200  4   HIS A N    
12   C  CA   . HIS A 4   ? 0.2253 0.2515 0.3000 -0.0216 0.0551  0.0285  4   HIS A CA   
13   C  C    . HIS A 4   ? 0.1967 0.1641 0.2565 -0.0335 0.0838  0.0288  4   HIS A C    
14   O  O    . HIS A 4   ? 0.2210 0.1720 0.2838 -0.0175 0.1010  0.0164  4   HIS A O    
15   C  CB   . HIS A 4   ? 0.2423 0.3093 0.3061 -0.0320 0.0544  0.0560  4   HIS A CB   
16   C  CG   . HIS A 4   ? 0.3000 0.3100 0.2985 0.0065  0.0575  0.0057  4   HIS A CG   
17   N  ND1  . HIS A 4   ? 0.2949 0.3021 0.3025 -0.0015 0.0162  0.0068  4   HIS A ND1  
18   C  CD2  . HIS A 4   ? 0.3036 0.3088 0.3093 -0.0027 0.0195  0.0038  4   HIS A CD2  
19   C  CE1  . HIS A 4   ? 0.2998 0.3097 0.3075 -0.0010 0.0108  0.0063  4   HIS A CE1  
20   N  NE2  . HIS A 4   ? 0.2989 0.3079 0.3064 -0.0006 0.0109  0.0035  4   HIS A NE2  
21   N  N    . TRP A 5   ? 0.1956 0.1335 0.2790 -0.0342 0.0904  0.0097  5   TRP A N    
22   C  CA   . TRP A 5   ? 0.1592 0.1229 0.2177 -0.0270 0.0863  -0.0034 5   TRP A CA   
23   C  C    . TRP A 5   ? 0.1737 0.1172 0.2131 -0.0096 0.1001  -0.0013 5   TRP A C    
24   O  O    . TRP A 5   ? 0.2205 0.1197 0.2174 -0.0298 0.0957  -0.0015 5   TRP A O    
25   C  CB   . TRP A 5   ? 0.1736 0.1146 0.2321 -0.0210 0.0623  -0.0186 5   TRP A CB   
26   C  CG   . TRP A 5   ? 0.1780 0.0969 0.1838 -0.0447 0.0557  -0.0063 5   TRP A CG   
27   C  CD1  . TRP A 5   ? 0.1967 0.1308 0.2360 -0.0348 0.0907  -0.0136 5   TRP A CD1  
28   C  CD2  . TRP A 5   ? 0.1549 0.0960 0.1781 -0.0137 0.0522  -0.0296 5   TRP A CD2  
29   N  NE1  . TRP A 5   ? 0.2166 0.1102 0.1953 -0.0082 0.0582  0.0217  5   TRP A NE1  
30   C  CE2  . TRP A 5   ? 0.1789 0.1624 0.1635 0.0115  0.0540  0.0099  5   TRP A CE2  
31   C  CE3  . TRP A 5   ? 0.1504 0.1213 0.1657 -0.0195 0.0537  -0.0388 5   TRP A CE3  
32   C  CZ2  . TRP A 5   ? 0.2161 0.1581 0.1356 0.0370  0.0274  -0.0153 5   TRP A CZ2  
33   C  CZ3  . TRP A 5   ? 0.1711 0.1270 0.1520 -0.0132 0.0397  -0.0458 5   TRP A CZ3  
34   C  CH2  . TRP A 5   ? 0.1651 0.1949 0.1569 0.0057  0.0408  -0.0502 5   TRP A CH2  
35   N  N    . GLY A 6   ? 0.1736 0.1058 0.2044 -0.0166 0.0921  -0.0121 6   GLY A N    
36   C  CA   . GLY A 6   ? 0.1847 0.0895 0.1874 -0.0020 0.0798  -0.0140 6   GLY A CA   
37   C  C    . GLY A 6   ? 0.1456 0.0978 0.2379 0.0031  0.0996  -0.0196 6   GLY A C    
38   O  O    . GLY A 6   ? 0.1629 0.1037 0.2071 0.0082  0.0828  -0.0076 6   GLY A O    
39   N  N    A TYR A 7   ? 0.1640 0.0736 0.1949 0.0155  0.0549  0.0038  7   TYR A N    
40   N  N    B TYR A 7   ? 0.1206 0.0861 0.2476 -0.0062 0.1001  -0.0386 7   TYR A N    
41   C  CA   A TYR A 7   ? 0.1420 0.0712 0.1933 0.0091  0.0315  -0.0098 7   TYR A CA   
42   C  CA   B TYR A 7   ? 0.1344 0.0991 0.2045 -0.0230 0.0785  -0.0458 7   TYR A CA   
43   C  C    A TYR A 7   ? 0.1721 0.1330 0.2581 -0.0074 0.0251  -0.0176 7   TYR A C    
44   C  C    B TYR A 7   ? 0.1700 0.1272 0.2689 -0.0232 0.0917  -0.0527 7   TYR A C    
45   O  O    A TYR A 7   ? 0.2050 0.0863 0.3079 0.0200  0.0427  -0.0070 7   TYR A O    
46   O  O    B TYR A 7   ? 0.1105 0.0570 0.3578 -0.0087 0.1089  -0.0658 7   TYR A O    
47   C  CB   A TYR A 7   ? 0.1366 0.0714 0.1425 -0.0253 0.0346  -0.0170 7   TYR A CB   
48   C  CB   B TYR A 7   ? 0.1418 0.0929 0.1500 -0.0247 0.0408  -0.0386 7   TYR A CB   
49   C  CG   A TYR A 7   ? 0.1019 0.0904 0.0960 -0.0026 0.0208  -0.0102 7   TYR A CG   
50   C  CG   B TYR A 7   ? 0.1407 0.0724 0.1382 -0.0328 0.0153  -0.0390 7   TYR A CG   
51   C  CD1  A TYR A 7   ? 0.1394 0.0639 0.1213 -0.0377 -0.0159 0.0204  7   TYR A CD1  
52   C  CD1  B TYR A 7   ? 0.0987 0.0939 0.1414 0.0003  0.0333  -0.0023 7   TYR A CD1  
53   C  CD2  A TYR A 7   ? 0.1128 0.0569 0.1073 -0.0119 -0.0093 -0.0151 7   TYR A CD2  
54   C  CD2  B TYR A 7   ? 0.1373 0.1064 0.0897 -0.0231 0.0153  -0.0065 7   TYR A CD2  
55   C  CE1  A TYR A 7   ? 0.1190 0.0627 0.0771 -0.0421 0.0215  -0.0226 7   TYR A CE1  
56   C  CE1  B TYR A 7   ? 0.0985 0.0572 0.1365 0.0048  0.0137  -0.0204 7   TYR A CE1  
57   C  CE2  A TYR A 7   ? 0.1364 0.0755 0.0861 0.0060  -0.0024 -0.0186 7   TYR A CE2  
58   C  CE2  B TYR A 7   ? 0.1061 0.0922 0.1055 -0.0210 0.0329  0.0046  7   TYR A CE2  
59   C  CZ   A TYR A 7   ? 0.1278 0.0546 0.0915 -0.0211 -0.0167 0.0230  7   TYR A CZ   
60   C  CZ   B TYR A 7   ? 0.1073 0.0710 0.0868 -0.0131 0.0088  -0.0315 7   TYR A CZ   
61   O  OH   A TYR A 7   ? 0.1447 0.0631 0.0710 -0.0062 0.0230  -0.0151 7   TYR A OH   
62   O  OH   B TYR A 7   ? 0.1018 0.0639 0.1317 0.0006  0.0048  -0.0035 7   TYR A OH   
63   N  N    A GLY A 8   ? 0.1863 0.1592 0.2233 0.0166  -0.0166 -0.0211 8   GLY A N    
64   N  N    B GLY A 8   ? 0.1750 0.0820 0.2881 -0.0091 0.1303  -0.0324 8   GLY A N    
65   C  CA   A GLY A 8   ? 0.0917 0.0900 0.1787 -0.0041 -0.0046 -0.0489 8   GLY A CA   
66   C  CA   B GLY A 8   ? 0.1838 0.1358 0.2838 -0.0186 0.0803  -0.0240 8   GLY A CA   
67   C  C    A GLY A 8   ? 0.1362 0.1416 0.2054 -0.0125 0.0060  -0.0500 8   GLY A C    
68   C  C    B GLY A 8   ? 0.1806 0.1393 0.2621 0.0287  0.0701  -0.0395 8   GLY A C    
69   O  O    A GLY A 8   ? 0.1881 0.1405 0.2138 -0.0502 0.0559  -0.0776 8   GLY A O    
70   O  O    B GLY A 8   ? 0.1391 0.1526 0.3055 0.0126  0.0856  -0.0236 8   GLY A O    
71   N  N    A LYS A 9   ? 0.1425 0.1177 0.2132 -0.0147 -0.0113 -0.0631 9   LYS A N    
72   N  N    B LYS A 9   ? 0.1761 0.1838 0.2881 0.0258  0.0388  -0.0304 9   LYS A N    
73   C  CA   A LYS A 9   ? 0.1387 0.1533 0.1913 -0.0195 -0.0197 -0.0176 9   LYS A CA   
74   C  CA   B LYS A 9   ? 0.2354 0.1838 0.3041 0.0126  0.0219  -0.0264 9   LYS A CA   
75   C  C    A LYS A 9   ? 0.1102 0.1348 0.1723 -0.0441 0.0038  -0.0159 9   LYS A C    
76   C  C    B LYS A 9   ? 0.1951 0.1721 0.2775 0.0104  0.0379  -0.0121 9   LYS A C    
77   O  O    A LYS A 9   ? 0.1450 0.1896 0.1523 -0.0549 -0.0237 -0.0057 9   LYS A O    
78   O  O    B LYS A 9   ? 0.2244 0.2434 0.2942 0.0403  0.0421  -0.0303 9   LYS A O    
79   C  CB   A LYS A 9   ? 0.1660 0.2393 0.1736 -0.0052 -0.0174 -0.0417 9   LYS A CB   
80   C  CB   B LYS A 9   ? 0.2324 0.1577 0.3100 0.0020  0.0060  -0.0131 9   LYS A CB   
81   C  CG   A LYS A 9   ? 0.2423 0.1958 0.2393 0.0287  -0.0120 -0.0065 9   LYS A CG   
82   C  CG   B LYS A 9   ? 0.2402 0.2034 0.3086 0.0320  0.0087  -0.0151 9   LYS A CG   
83   C  CD   A LYS A 9   ? 0.2190 0.2258 0.2648 0.0226  -0.0080 -0.0098 9   LYS A CD   
84   C  CD   B LYS A 9   ? 0.2842 0.2161 0.3125 0.0096  -0.0057 -0.0119 9   LYS A CD   
85   C  CE   A LYS A 9   ? 0.2454 0.3005 0.2745 0.0436  -0.0208 -0.0126 9   LYS A CE   
86   C  CE   B LYS A 9   ? 0.3046 0.3032 0.3407 0.0199  0.0026  -0.0137 9   LYS A CE   
87   N  NZ   A LYS A 9   ? 0.3203 0.2984 0.2982 0.0504  0.0000  -0.0199 9   LYS A NZ   
88   N  NZ   B LYS A 9   ? 0.2761 0.2770 0.3467 0.0553  -0.0030 -0.0020 9   LYS A NZ   
89   N  N    A HIS A 10  ? 0.1106 0.1307 0.1382 -0.0043 -0.0054 -0.0091 10  HIS A N    
90   N  N    B HIS A 10  ? 0.1335 0.1387 0.2779 0.0584  0.0706  -0.0136 10  HIS A N    
91   C  CA   A HIS A 10  ? 0.1142 0.1181 0.1254 0.0010  0.0077  -0.0282 10  HIS A CA   
92   C  CA   B HIS A 10  ? 0.1463 0.1351 0.2384 0.0274  0.0715  -0.0232 10  HIS A CA   
93   C  C    A HIS A 10  ? 0.1378 0.1067 0.1845 -0.0065 0.0562  -0.0071 10  HIS A C    
94   C  C    B HIS A 10  ? 0.1599 0.1768 0.2673 0.0344  0.1093  -0.0062 10  HIS A C    
95   O  O    A HIS A 10  ? 0.1759 0.1362 0.2073 0.0313  0.0680  -0.0046 10  HIS A O    
96   O  O    B HIS A 10  ? 0.2133 0.2323 0.3030 0.0242  0.0898  -0.0373 10  HIS A O    
97   C  CB   A HIS A 10  ? 0.0820 0.1158 0.1459 -0.0087 -0.0065 -0.0043 10  HIS A CB   
98   C  CB   B HIS A 10  ? 0.1115 0.1224 0.2188 0.0186  0.0631  -0.0233 10  HIS A CB   
99   C  CG   A HIS A 10  ? 0.0909 0.1404 0.1298 0.0109  -0.0214 -0.0051 10  HIS A CG   
100  C  CG   B HIS A 10  ? 0.1319 0.1484 0.1841 0.0013  0.0296  -0.0423 10  HIS A CG   
101  N  ND1  A HIS A 10  ? 0.1039 0.1337 0.1835 0.0214  0.0178  -0.0208 10  HIS A ND1  
102  N  ND1  B HIS A 10  ? 0.1764 0.1924 0.1843 0.0414  0.0023  -0.0375 10  HIS A ND1  
103  C  CD2  A HIS A 10  ? 0.1125 0.1560 0.1459 -0.0020 -0.0261 -0.0535 10  HIS A CD2  
104  C  CD2  B HIS A 10  ? 0.1416 0.1845 0.1694 0.0076  0.0252  -0.0573 10  HIS A CD2  
105  C  CE1  A HIS A 10  ? 0.1133 0.1005 0.2016 0.0476  -0.0120 -0.0104 10  HIS A CE1  
106  C  CE1  B HIS A 10  ? 0.1474 0.1362 0.2233 0.0527  0.0071  -0.0263 10  HIS A CE1  
107  N  NE2  A HIS A 10  ? 0.1811 0.1228 0.1577 -0.0026 0.0040  -0.0461 10  HIS A NE2  
108  N  NE2  B HIS A 10  ? 0.1630 0.1734 0.1177 0.0146  0.0051  -0.0357 10  HIS A NE2  
109  N  N    . ASN A 11  ? 0.1796 0.1463 0.3120 0.0129  0.1093  0.0137  11  ASN A N    
110  C  CA   . ASN A 11  ? 0.1893 0.1351 0.2628 0.0181  0.1045  -0.0057 11  ASN A CA   
111  C  C    . ASN A 11  ? 0.1879 0.1572 0.2565 0.0221  0.1110  0.0228  11  ASN A C    
112  O  O    . ASN A 11  ? 0.1509 0.1228 0.2829 0.0491  0.1272  0.0109  11  ASN A O    
113  C  CB   . ASN A 11  ? 0.1798 0.1233 0.2597 0.0447  0.1421  -0.0037 11  ASN A CB   
114  C  CG   . ASN A 11  ? 0.2138 0.1348 0.2511 0.0315  0.1515  -0.0302 11  ASN A CG   
115  O  OD1  . ASN A 11  ? 0.2454 0.1587 0.3637 -0.0131 0.1247  0.0156  11  ASN A OD1  
116  N  ND2  . ASN A 11  ? 0.2484 0.1541 0.3005 -0.0120 0.1164  0.0000  11  ASN A ND2  
117  N  N    . GLY A 12  ? 0.1529 0.1154 0.2707 0.0046  0.1128  -0.0007 12  GLY A N    
118  C  CA   . GLY A 12  ? 0.1391 0.1224 0.2648 0.0156  0.0991  0.0082  12  GLY A CA   
119  C  C    . GLY A 12  ? 0.1465 0.0775 0.2449 0.0184  0.0891  0.0175  12  GLY A C    
120  O  O    . GLY A 12  ? 0.1216 0.0935 0.3095 0.0186  0.0776  0.0204  12  GLY A O    
121  N  N    . PRO A 13  ? 0.1120 0.0904 0.2255 -0.0031 0.0675  -0.0148 13  PRO A N    
122  C  CA   . PRO A 13  ? 0.1107 0.0838 0.2312 -0.0027 0.0524  -0.0120 13  PRO A CA   
123  C  C    . PRO A 13  ? 0.1228 0.0798 0.2148 0.0043  0.0421  -0.0006 13  PRO A C    
124  O  O    . PRO A 13  ? 0.1190 0.1023 0.2272 -0.0125 0.0513  -0.0287 13  PRO A O    
125  C  CB   . PRO A 13  ? 0.1450 0.0864 0.2118 -0.0024 0.0696  -0.0284 13  PRO A CB   
126  C  CG   . PRO A 13  ? 0.1562 0.0856 0.2115 -0.0194 0.0733  -0.0277 13  PRO A CG   
127  C  CD   . PRO A 13  ? 0.1553 0.1213 0.2140 0.0186  0.0755  -0.0074 13  PRO A CD   
128  N  N    . GLU A 14  ? 0.1574 0.0780 0.2678 0.0013  0.0571  0.0006  14  GLU A N    
129  C  CA   . GLU A 14  ? 0.1754 0.1142 0.2786 0.0184  0.0392  0.0262  14  GLU A CA   
130  C  C    . GLU A 14  ? 0.1416 0.1120 0.2915 0.0384  0.0513  0.0013  14  GLU A C    
131  O  O    . GLU A 14  ? 0.1741 0.1304 0.3100 0.0509  0.0474  0.0428  14  GLU A O    
132  C  CB   . GLU A 14  ? 0.2456 0.1254 0.2985 0.0254  0.0284  0.0498  14  GLU A CB   
133  C  CG   . GLU A 14  ? 0.3097 0.1748 0.3623 0.0005  0.0239  0.0339  14  GLU A CG   
134  C  CD   . GLU A 14  ? 0.3628 0.3856 0.3745 0.0310  0.0054  -0.0173 14  GLU A CD   
135  O  OE1  . GLU A 14  ? 0.4438 0.5072 0.4275 0.0087  -0.0397 -0.0148 14  GLU A OE1  
136  O  OE2  . GLU A 14  ? 0.3937 0.4603 0.3907 0.0432  0.0126  -0.0291 14  GLU A OE2  
137  N  N    . HIS A 15  ? 0.0985 0.0976 0.2955 0.0253  0.0388  0.0091  15  HIS A N    
138  C  CA   . HIS A 15  ? 0.1091 0.1152 0.2887 0.0282  0.0471  0.0038  15  HIS A CA   
139  C  C    . HIS A 15  ? 0.0982 0.0939 0.2854 0.0230  0.0366  0.0006  15  HIS A C    
140  O  O    . HIS A 15  ? 0.0762 0.1075 0.3262 0.0178  0.0419  0.0318  15  HIS A O    
141  C  CB   . HIS A 15  ? 0.0899 0.0974 0.3183 0.0269  0.0509  0.0239  15  HIS A CB   
142  C  CG   . HIS A 15  ? 0.1438 0.1423 0.2646 0.0269  0.0480  0.0309  15  HIS A CG   
143  N  ND1  . HIS A 15  ? 0.1355 0.1914 0.3149 0.0626  0.0244  -0.0087 15  HIS A ND1  
144  C  CD2  . HIS A 15  ? 0.2002 0.1822 0.3228 0.0445  0.0741  0.0147  15  HIS A CD2  
145  C  CE1  . HIS A 15  ? 0.2741 0.2323 0.2799 0.0599  0.0125  -0.0081 15  HIS A CE1  
146  N  NE2  . HIS A 15  ? 0.2551 0.1861 0.2705 0.0662  0.0599  0.0197  15  HIS A NE2  
147  N  N    . TRP A 16  ? 0.0825 0.1026 0.2644 0.0098  0.0414  0.0062  16  TRP A N    
148  C  CA   . TRP A 16  ? 0.0776 0.0852 0.2235 0.0082  0.0287  -0.0104 16  TRP A CA   
149  C  C    . TRP A 16  ? 0.0728 0.0895 0.2360 0.0103  0.0118  -0.0057 16  TRP A C    
150  O  O    . TRP A 16  ? 0.0863 0.0917 0.2509 0.0034  0.0003  0.0086  16  TRP A O    
151  C  CB   . TRP A 16  ? 0.0678 0.0979 0.2102 0.0129  0.0211  -0.0156 16  TRP A CB   
152  C  CG   . TRP A 16  ? 0.0931 0.0666 0.1876 0.0000  0.0068  -0.0070 16  TRP A CG   
153  C  CD1  . TRP A 16  ? 0.1215 0.0789 0.1752 0.0114  0.0373  0.0015  16  TRP A CD1  
154  C  CD2  . TRP A 16  ? 0.0922 0.0653 0.1946 0.0164  0.0373  -0.0135 16  TRP A CD2  
155  N  NE1  . TRP A 16  ? 0.1075 0.1008 0.1793 0.0120  0.0460  -0.0236 16  TRP A NE1  
156  C  CE2  . TRP A 16  ? 0.1186 0.0627 0.1665 0.0015  0.0485  -0.0113 16  TRP A CE2  
157  C  CE3  . TRP A 16  ? 0.0815 0.0678 0.1818 0.0051  0.0203  -0.0231 16  TRP A CE3  
158  C  CZ2  . TRP A 16  ? 0.1097 0.0766 0.1524 -0.0060 0.0320  -0.0076 16  TRP A CZ2  
159  C  CZ3  . TRP A 16  ? 0.0842 0.0776 0.1738 0.0065  0.0412  -0.0184 16  TRP A CZ3  
160  C  CH2  . TRP A 16  ? 0.1009 0.0766 0.1542 -0.0140 0.0322  -0.0241 16  TRP A CH2  
161  N  N    . HIS A 17  ? 0.0721 0.0944 0.2431 -0.0023 0.0070  0.0000  17  HIS A N    
162  C  CA   . HIS A 17  ? 0.0741 0.1049 0.2500 0.0046  0.0040  0.0204  17  HIS A CA   
163  C  C    . HIS A 17  ? 0.0710 0.1233 0.3030 -0.0074 0.0000  0.0196  17  HIS A C    
164  O  O    . HIS A 17  ? 0.0845 0.1362 0.2980 -0.0203 -0.0219 0.0098  17  HIS A O    
165  C  CB   . HIS A 17  ? 0.0956 0.1032 0.2206 -0.0054 -0.0057 0.0096  17  HIS A CB   
166  C  CG   . HIS A 17  ? 0.1114 0.1272 0.2795 0.0005  0.0099  0.0351  17  HIS A CG   
167  N  ND1  . HIS A 17  ? 0.0983 0.2073 0.3134 0.0049  -0.0027 0.0803  17  HIS A ND1  
168  C  CD2  . HIS A 17  ? 0.1076 0.1342 0.2897 0.0173  0.0024  0.0428  17  HIS A CD2  
169  C  CE1  . HIS A 17  ? 0.0872 0.2152 0.3257 0.0175  -0.0023 0.0644  17  HIS A CE1  
170  N  NE2  . HIS A 17  ? 0.1262 0.1699 0.3303 0.0408  -0.0071 0.0746  17  HIS A NE2  
171  N  N    . LYS A 18  ? 0.0680 0.1053 0.3201 -0.0010 0.0013  0.0344  18  LYS A N    
172  C  CA   . LYS A 18  ? 0.0829 0.1562 0.3212 -0.0092 0.0052  0.0317  18  LYS A CA   
173  C  C    . LYS A 18  ? 0.0933 0.1553 0.3073 -0.0103 -0.0109 0.0487  18  LYS A C    
174  O  O    . LYS A 18  ? 0.1421 0.1922 0.4018 -0.0529 -0.0590 0.0957  18  LYS A O    
175  C  CB   . LYS A 18  ? 0.0965 0.1606 0.3192 0.0074  -0.0038 0.0577  18  LYS A CB   
176  C  CG   . LYS A 18  ? 0.0790 0.1817 0.3039 0.0109  0.0193  0.0621  18  LYS A CG   
177  C  CD   . LYS A 18  ? 0.0885 0.1962 0.3057 0.0160  0.0126  0.0527  18  LYS A CD   
178  C  CE   . LYS A 18  ? 0.1179 0.1597 0.3161 0.0399  0.0277  0.0688  18  LYS A CE   
179  N  NZ   . LYS A 18  ? 0.0838 0.2125 0.2813 0.0834  0.0353  0.0798  18  LYS A NZ   
180  N  N    . ASP A 19  ? 0.0891 0.1553 0.3079 -0.0015 0.0121  0.0370  19  ASP A N    
181  C  CA   . ASP A 19  ? 0.1307 0.1163 0.2989 -0.0052 0.0126  0.0472  19  ASP A CA   
182  C  C    . ASP A 19  ? 0.0870 0.1177 0.3215 -0.0048 0.0147  0.0317  19  ASP A C    
183  O  O    . ASP A 19  ? 0.1330 0.1048 0.3233 -0.0140 0.0205  0.0414  19  ASP A O    
184  C  CB   . ASP A 19  ? 0.1364 0.2057 0.2953 0.0219  0.0035  0.0494  19  ASP A CB   
185  C  CG   . ASP A 19  ? 0.1577 0.2572 0.2892 0.0130  0.0017  -0.0118 19  ASP A CG   
186  O  OD1  . ASP A 19  ? 0.1923 0.3298 0.3689 -0.0129 0.0450  0.0753  19  ASP A OD1  
187  O  OD2  . ASP A 19  ? 0.3756 0.4671 0.3808 -0.0187 -0.0154 -0.0715 19  ASP A OD2  
188  N  N    . PHE A 20  ? 0.0877 0.0974 0.2984 0.0020  -0.0129 0.0326  20  PHE A N    
189  C  CA   . PHE A 20  ? 0.0904 0.0854 0.2470 -0.0114 -0.0077 0.0031  20  PHE A CA   
190  C  C    . PHE A 20  ? 0.0949 0.0833 0.2635 -0.0052 0.0059  0.0010  20  PHE A C    
191  O  O    . PHE A 20  ? 0.1039 0.0882 0.2276 -0.0143 -0.0091 0.0062  20  PHE A O    
192  C  CB   . PHE A 20  ? 0.1005 0.1146 0.2558 -0.0120 -0.0082 0.0108  20  PHE A CB   
193  C  CG   . PHE A 20  ? 0.0829 0.1444 0.2608 -0.0282 0.0093  0.0252  20  PHE A CG   
194  C  CD1  . PHE A 20  ? 0.1286 0.1454 0.2506 -0.0017 0.0283  0.0533  20  PHE A CD1  
195  C  CD2  . PHE A 20  ? 0.0803 0.1901 0.2858 -0.0288 0.0209  0.0132  20  PHE A CD2  
196  C  CE1  . PHE A 20  ? 0.1687 0.1781 0.2806 -0.0151 -0.0162 0.0603  20  PHE A CE1  
197  C  CE2  . PHE A 20  ? 0.1447 0.2034 0.2745 -0.0068 0.0309  0.0136  20  PHE A CE2  
198  C  CZ   . PHE A 20  ? 0.1096 0.2418 0.2757 -0.0315 0.0093  0.0571  20  PHE A CZ   
199  N  N    . PRO A 21  ? 0.1028 0.1067 0.2535 -0.0287 -0.0096 -0.0026 21  PRO A N    
200  C  CA   . PRO A 21  ? 0.0926 0.1238 0.2409 -0.0240 -0.0174 -0.0043 21  PRO A CA   
201  C  C    . PRO A 21  ? 0.0953 0.0917 0.2698 -0.0167 -0.0248 -0.0304 21  PRO A C    
202  O  O    . PRO A 21  ? 0.1019 0.1136 0.2522 -0.0081 -0.0381 -0.0005 21  PRO A O    
203  C  CB   . PRO A 21  ? 0.0863 0.2019 0.2732 -0.0582 -0.0526 0.0015  21  PRO A CB   
204  C  CG   . PRO A 21  ? 0.2236 0.2055 0.3409 -0.0815 -0.0597 0.0000  21  PRO A CG   
205  C  CD   . PRO A 21  ? 0.1005 0.1441 0.2822 -0.0230 -0.0277 0.0162  21  PRO A CD   
206  N  N    . ILE A 22  ? 0.0994 0.0863 0.2506 -0.0170 -0.0283 -0.0131 22  ILE A N    
207  C  CA   . ILE A 22  ? 0.0958 0.0899 0.2111 -0.0153 -0.0362 -0.0297 22  ILE A CA   
208  C  C    . ILE A 22  ? 0.0642 0.0899 0.2190 -0.0034 -0.0425 -0.0151 22  ILE A C    
209  O  O    . ILE A 22  ? 0.0863 0.0929 0.2023 -0.0015 -0.0182 -0.0172 22  ILE A O    
210  C  CB   . ILE A 22  ? 0.1014 0.0845 0.1897 -0.0141 -0.0309 -0.0270 22  ILE A CB   
211  C  CG1  . ILE A 22  ? 0.1118 0.0935 0.2260 0.0017  -0.0392 -0.0653 22  ILE A CG1  
212  C  CG2  . ILE A 22  ? 0.1163 0.1057 0.1739 -0.0163 -0.0232 -0.0185 22  ILE A CG2  
213  C  CD1  . ILE A 22  ? 0.1655 0.1351 0.3030 0.0000  -0.0108 -0.0153 22  ILE A CD1  
214  N  N    . ALA A 23  ? 0.0714 0.0948 0.2161 -0.0119 -0.0244 -0.0052 23  ALA A N    
215  C  CA   . ALA A 23  ? 0.0969 0.0836 0.2032 -0.0148 -0.0065 -0.0198 23  ALA A CA   
216  C  C    . ALA A 23  ? 0.1046 0.0908 0.2036 0.0043  -0.0129 -0.0148 23  ALA A C    
217  O  O    . ALA A 23  ? 0.1140 0.0944 0.1847 -0.0141 -0.0148 -0.0099 23  ALA A O    
218  C  CB   . ALA A 23  ? 0.0863 0.0917 0.2281 0.0015  -0.0153 -0.0366 23  ALA A CB   
219  N  N    . LYS A 24  ? 0.1118 0.0996 0.2010 -0.0124 -0.0305 -0.0003 24  LYS A N    
220  C  CA   . LYS A 24  ? 0.0976 0.1190 0.2201 -0.0026 -0.0331 0.0074  24  LYS A CA   
221  C  C    . LYS A 24  ? 0.1349 0.1349 0.2178 -0.0148 -0.0408 -0.0065 24  LYS A C    
222  O  O    . LYS A 24  ? 0.1432 0.1798 0.2213 0.0096  -0.0472 -0.0126 24  LYS A O    
223  C  CB   . LYS A 24  ? 0.1140 0.1553 0.2258 -0.0035 -0.0362 0.0230  24  LYS A CB   
224  C  CG   . LYS A 24  ? 0.1163 0.1809 0.2266 0.0233  -0.0093 0.0272  24  LYS A CG   
225  C  CD   . LYS A 24  ? 0.1727 0.2310 0.2897 0.0427  0.0099  0.0220  24  LYS A CD   
226  C  CE   . LYS A 24  ? 0.1709 0.2353 0.3165 0.0318  0.0098  0.0166  24  LYS A CE   
227  N  NZ   . LYS A 24  ? 0.2445 0.2872 0.4283 -0.0010 0.0320  -0.0126 24  LYS A NZ   
228  N  N    . GLY A 25  ? 0.1185 0.1247 0.1800 0.0031  -0.0406 -0.0237 25  GLY A N    
229  C  CA   . GLY A 25  ? 0.1292 0.1305 0.2005 -0.0068 -0.0421 -0.0366 25  GLY A CA   
230  C  C    . GLY A 25  ? 0.1253 0.1251 0.1504 -0.0109 -0.0432 -0.0274 25  GLY A C    
231  O  O    . GLY A 25  ? 0.1326 0.1638 0.1585 -0.0006 -0.0432 -0.0219 25  GLY A O    
232  N  N    . GLU A 26  ? 0.1344 0.1702 0.1669 -0.0258 -0.0474 -0.0498 26  GLU A N    
233  C  CA   . GLU A 26  ? 0.1619 0.1707 0.1477 -0.0082 -0.0357 -0.0372 26  GLU A CA   
234  C  C    . GLU A 26  ? 0.1279 0.1434 0.1285 -0.0176 -0.0193 -0.0274 26  GLU A C    
235  O  O    . GLU A 26  ? 0.1779 0.1851 0.0940 -0.0197 -0.0443 -0.0115 26  GLU A O    
236  C  CB   . GLU A 26  ? 0.1902 0.2240 0.1617 -0.0248 -0.0562 -0.0843 26  GLU A CB   
237  C  CG   . GLU A 26  ? 0.2127 0.2606 0.1565 -0.0049 -0.0537 -0.0856 26  GLU A CG   
238  C  CD   . GLU A 26  ? 0.2671 0.3486 0.2172 -0.0296 -0.0810 -0.0540 26  GLU A CD   
239  O  OE1  . GLU A 26  ? 0.2980 0.4133 0.3061 0.0035  -0.0500 -0.0313 26  GLU A OE1  
240  O  OE2  . GLU A 26  ? 0.3097 0.4338 0.3993 0.0493  -0.1111 -0.0458 26  GLU A OE2  
241  N  N    . ARG A 27  ? 0.1366 0.0881 0.0976 -0.0093 -0.0364 -0.0216 27  ARG A N    
242  C  CA   . ARG A 27  ? 0.1251 0.0639 0.1073 0.0000  -0.0274 -0.0203 27  ARG A CA   
243  C  C    . ARG A 27  ? 0.1048 0.0572 0.1027 -0.0132 -0.0207 -0.0059 27  ARG A C    
244  O  O    . ARG A 27  ? 0.1054 0.0811 0.0949 0.0043  -0.0167 -0.0159 27  ARG A O    
245  C  CB   . ARG A 27  ? 0.1547 0.1093 0.1039 0.0000  -0.0241 -0.0350 27  ARG A CB   
246  C  CG   . ARG A 27  ? 0.1443 0.1242 0.1493 -0.0017 -0.0162 -0.0183 27  ARG A CG   
247  C  CD   . ARG A 27  ? 0.2096 0.1694 0.1269 0.0132  -0.0299 -0.0159 27  ARG A CD   
248  N  NE   . ARG A 27  ? 0.2179 0.0913 0.1199 -0.0232 -0.0043 -0.0142 27  ARG A NE   
249  C  CZ   . ARG A 27  ? 0.1527 0.1159 0.1066 0.0109  -0.0098 0.0087  27  ARG A CZ   
250  N  NH1  . ARG A 27  ? 0.1660 0.1590 0.1457 0.0120  -0.0007 -0.0777 27  ARG A NH1  
251  N  NH2  . ARG A 27  ? 0.1396 0.1159 0.1419 0.0005  -0.0076 -0.0219 27  ARG A NH2  
252  N  N    . GLN A 28  ? 0.1012 0.0563 0.0949 0.0038  -0.0263 -0.0054 28  GLN A N    
253  C  CA   . GLN A 28  ? 0.0802 0.0521 0.0969 0.0015  -0.0200 -0.0041 28  GLN A CA   
254  C  C    . GLN A 28  ? 0.0930 0.0525 0.0956 0.0054  0.0035  0.0049  28  GLN A C    
255  O  O    . GLN A 28  ? 0.1039 0.0784 0.0776 -0.0109 -0.0249 -0.0114 28  GLN A O    
256  C  CB   . GLN A 28  ? 0.0827 0.0768 0.1019 0.0049  -0.0227 -0.0005 28  GLN A CB   
257  C  CG   . GLN A 28  ? 0.0890 0.0811 0.1305 0.0003  -0.0208 -0.0335 28  GLN A CG   
258  C  CD   . GLN A 28  ? 0.0870 0.0746 0.1133 0.0020  -0.0254 -0.0076 28  GLN A CD   
259  O  OE1  . GLN A 28  ? 0.0870 0.0748 0.1163 -0.0126 -0.0096 -0.0194 28  GLN A OE1  
260  N  NE2  . GLN A 28  ? 0.0939 0.0739 0.1111 -0.0031 -0.0198 -0.0194 28  GLN A NE2  
261  N  N    . SER A 29  ? 0.0933 0.0511 0.0687 0.0026  -0.0020 -0.0068 29  SER A N    
262  C  CA   . SER A 29  ? 0.0845 0.0375 0.0782 -0.0110 -0.0126 -0.0154 29  SER A CA   
263  C  C    . SER A 29  ? 0.0821 0.0526 0.0764 -0.0118 -0.0109 0.0000  29  SER A C    
264  O  O    . SER A 29  ? 0.0935 0.0476 0.0908 0.0020  -0.0037 -0.0076 29  SER A O    
265  C  CB   . SER A 29  ? 0.0820 0.0494 0.0762 0.0007  0.0019  -0.0103 29  SER A CB   
266  O  OG   . SER A 29  ? 0.0854 0.0421 0.0821 0.0070  -0.0037 -0.0126 29  SER A OG   
267  N  N    . PRO A 30  ? 0.0791 0.0482 0.0755 0.0115  -0.0142 -0.0088 30  PRO A N    
268  C  CA   . PRO A 30  ? 0.0802 0.0354 0.0775 0.0041  -0.0109 0.0076  30  PRO A CA   
269  C  C    . PRO A 30  ? 0.0803 0.0447 0.0829 0.0006  0.0020  -0.0099 30  PRO A C    
270  O  O    . PRO A 30  ? 0.0969 0.0545 0.0872 0.0020  -0.0182 -0.0035 30  PRO A O    
271  C  CB   . PRO A 30  ? 0.0978 0.0406 0.0745 0.0068  -0.0164 -0.0119 30  PRO A CB   
272  C  CG   . PRO A 30  ? 0.0872 0.0539 0.0838 0.0048  -0.0043 -0.0046 30  PRO A CG   
273  C  CD   . PRO A 30  ? 0.0852 0.0608 0.0863 0.0040  -0.0027 -0.0015 30  PRO A CD   
274  N  N    . VAL A 31  ? 0.0847 0.0491 0.0727 0.0096  -0.0082 -0.0038 31  VAL A N    
275  C  CA   . VAL A 31  ? 0.1076 0.0527 0.0660 0.0024  -0.0118 0.0071  31  VAL A CA   
276  C  C    . VAL A 31  ? 0.1118 0.0529 0.0784 0.0165  -0.0085 -0.0017 31  VAL A C    
277  O  O    . VAL A 31  ? 0.1233 0.0465 0.0806 0.0027  -0.0074 0.0099  31  VAL A O    
278  C  CB   . VAL A 31  ? 0.1199 0.0526 0.0762 0.0052  -0.0165 -0.0010 31  VAL A CB   
279  C  CG1  . VAL A 31  ? 0.1410 0.0683 0.0856 -0.0043 -0.0098 -0.0013 31  VAL A CG1  
280  C  CG2  . VAL A 31  ? 0.1163 0.0608 0.0904 0.0211  0.0046  -0.0071 31  VAL A CG2  
281  N  N    . ASP A 32  ? 0.1208 0.0530 0.0748 0.0052  -0.0285 -0.0023 32  ASP A N    
282  C  CA   . ASP A 32  ? 0.1114 0.0511 0.0791 0.0074  -0.0108 0.0071  32  ASP A CA   
283  C  C    . ASP A 32  ? 0.1432 0.0482 0.0666 0.0065  -0.0142 -0.0010 32  ASP A C    
284  O  O    . ASP A 32  ? 0.1378 0.0903 0.0890 0.0020  -0.0126 -0.0162 32  ASP A O    
285  C  CB   . ASP A 32  ? 0.1374 0.0728 0.0744 0.0270  -0.0304 -0.0003 32  ASP A CB   
286  C  CG   . ASP A 32  ? 0.1317 0.0606 0.0994 0.0108  0.0003  0.0088  32  ASP A CG   
287  O  OD1  . ASP A 32  ? 0.1398 0.0485 0.0949 0.0063  -0.0210 0.0074  32  ASP A OD1  
288  O  OD2  . ASP A 32  ? 0.2319 0.0872 0.0816 -0.0226 -0.0186 0.0227  32  ASP A OD2  
289  N  N    A ILE A 33  ? 0.1262 0.0477 0.0482 0.0071  0.0000  -0.0126 33  ILE A N    
290  N  N    B ILE A 33  ? 0.1231 0.0472 0.0784 0.0171  -0.0107 0.0164  33  ILE A N    
291  C  CA   A ILE A 33  ? 0.1199 0.0542 0.0639 -0.0015 -0.0136 -0.0120 33  ILE A CA   
292  C  CA   B ILE A 33  ? 0.1389 0.0748 0.0879 0.0208  0.0000  0.0040  33  ILE A CA   
293  C  C    A ILE A 33  ? 0.1490 0.0485 0.0715 0.0010  0.0043  0.0159  33  ILE A C    
294  C  C    B ILE A 33  ? 0.1188 0.0671 0.0768 0.0126  0.0015  -0.0131 33  ILE A C    
295  O  O    A ILE A 33  ? 0.1368 0.0405 0.0705 -0.0104 -0.0109 0.0164  33  ILE A O    
296  O  O    B ILE A 33  ? 0.1333 0.0899 0.0662 0.0165  -0.0038 -0.0082 33  ILE A O    
297  C  CB   A ILE A 33  ? 0.1028 0.0482 0.0579 0.0110  0.0182  -0.0006 33  ILE A CB   
298  C  CB   B ILE A 33  ? 0.1391 0.0678 0.0899 0.0077  -0.0038 0.0017  33  ILE A CB   
299  C  CG1  A ILE A 33  ? 0.0966 0.0465 0.0617 0.0082  -0.0102 -0.0012 33  ILE A CG1  
300  C  CG1  B ILE A 33  ? 0.1303 0.0836 0.1067 0.0054  0.0218  0.0137  33  ILE A CG1  
301  C  CG2  A ILE A 33  ? 0.1427 0.0450 0.0879 -0.0131 0.0141  0.0071  33  ILE A CG2  
302  C  CG2  B ILE A 33  ? 0.1158 0.1265 0.0843 0.0249  0.0381  0.0130  33  ILE A CG2  
303  C  CD1  A ILE A 33  ? 0.0922 0.0662 0.0794 -0.0210 -0.0207 0.0108  33  ILE A CD1  
304  C  CD1  B ILE A 33  ? 0.1416 0.1319 0.1128 0.0114  -0.0035 0.0881  33  ILE A CD1  
305  N  N    A ASP A 34  ? 0.1265 0.0671 0.0784 -0.0034 0.0062  -0.0010 34  ASP A N    
306  N  N    B ASP A 34  ? 0.1405 0.0878 0.0645 -0.0085 -0.0205 0.0065  34  ASP A N    
307  C  CA   A ASP A 34  ? 0.1242 0.0635 0.0775 0.0107  -0.0175 0.0263  34  ASP A CA   
308  C  CA   B ASP A 34  ? 0.1438 0.0921 0.0820 0.0184  -0.0115 0.0097  34  ASP A CA   
309  C  C    A ASP A 34  ? 0.1242 0.0640 0.0554 -0.0087 0.0073  0.0252  34  ASP A C    
310  C  C    B ASP A 34  ? 0.1462 0.0903 0.0676 0.0060  -0.0195 0.0216  34  ASP A C    
311  O  O    A ASP A 34  ? 0.1576 0.0876 0.0639 0.0046  0.0017  0.0119  34  ASP A O    
312  O  O    B ASP A 34  ? 0.1646 0.1132 0.0793 0.0148  -0.0121 -0.0097 34  ASP A O    
313  C  CB   A ASP A 34  ? 0.1535 0.0829 0.0869 0.0178  -0.0085 0.0172  34  ASP A CB   
314  C  CB   B ASP A 34  ? 0.1720 0.0879 0.1053 0.0115  -0.0220 0.0355  34  ASP A CB   
315  C  CG   A ASP A 34  ? 0.2027 0.1186 0.0841 0.0093  -0.0012 0.0070  34  ASP A CG   
316  C  CG   B ASP A 34  ? 0.2039 0.1242 0.0978 -0.0065 0.0000  0.0051  34  ASP A CG   
317  O  OD1  A ASP A 34  ? 0.3269 0.1177 0.1764 0.0935  0.0469  0.0020  34  ASP A OD1  
318  O  OD1  B ASP A 34  ? 0.2454 0.1888 0.1075 0.0219  0.0000  0.0907  34  ASP A OD1  
319  O  OD2  A ASP A 34  ? 0.3222 0.1116 0.1102 0.0564  -0.0170 -0.0035 34  ASP A OD2  
320  O  OD2  B ASP A 34  ? 0.3052 0.1824 0.1721 0.0068  -0.0137 0.0612  34  ASP A OD2  
321  N  N    A THR A 35  ? 0.1287 0.0651 0.0772 0.0015  -0.0003 0.0397  35  THR A N    
322  N  N    B THR A 35  ? 0.1306 0.0864 0.0825 0.0109  -0.0099 -0.0023 35  THR A N    
323  C  CA   A THR A 35  ? 0.1084 0.0854 0.0782 0.0082  -0.0164 0.0351  35  THR A CA   
324  C  CA   B THR A 35  ? 0.1434 0.0838 0.0961 0.0198  -0.0187 -0.0003 35  THR A CA   
325  C  C    A THR A 35  ? 0.1221 0.0920 0.0912 0.0070  -0.0120 0.0233  35  THR A C    
326  C  C    B THR A 35  ? 0.1427 0.0854 0.1220 0.0192  0.0031  0.0304  35  THR A C    
327  O  O    A THR A 35  ? 0.1410 0.1274 0.0913 0.0240  -0.0142 0.0439  35  THR A O    
328  O  O    B THR A 35  ? 0.1497 0.1163 0.1228 0.0456  -0.0098 -0.0172 35  THR A O    
329  C  CB   A THR A 35  ? 0.1088 0.1411 0.0952 0.0043  -0.0241 0.0024  35  THR A CB   
330  C  CB   B THR A 35  ? 0.1184 0.0777 0.1202 -0.0006 -0.0007 0.0148  35  THR A CB   
331  O  OG1  A THR A 35  ? 0.1304 0.0939 0.1019 -0.0080 0.0203  0.0260  35  THR A OG1  
332  O  OG1  B THR A 35  ? 0.1418 0.1495 0.1337 -0.0103 0.0060  0.0230  35  THR A OG1  
333  C  CG2  A THR A 35  ? 0.1556 0.1502 0.1212 -0.0092 -0.0164 0.0328  35  THR A CG2  
334  C  CG2  B THR A 35  ? 0.1612 0.1145 0.0785 0.0054  -0.0143 0.0091  35  THR A CG2  
335  N  N    A HIS A 36  ? 0.1380 0.0775 0.0676 0.0059  -0.0067 0.0462  36  HIS A N    
336  N  N    B HIS A 36  ? 0.1791 0.1019 0.1000 0.0193  0.0236  0.0195  36  HIS A N    
337  C  CA   A HIS A 36  ? 0.1365 0.1118 0.0829 0.0062  0.0024  0.0515  36  HIS A CA   
338  C  CA   B HIS A 36  ? 0.2102 0.1247 0.1017 0.0129  0.0239  0.0197  36  HIS A CA   
339  C  C    A HIS A 36  ? 0.1653 0.1100 0.0631 0.0219  -0.0006 0.0399  36  HIS A C    
340  C  C    B HIS A 36  ? 0.2301 0.1224 0.0775 0.0132  0.0320  -0.0035 36  HIS A C    
341  O  O    A HIS A 36  ? 0.1815 0.1786 0.0929 0.0206  -0.0031 0.0361  36  HIS A O    
342  O  O    B HIS A 36  ? 0.2617 0.2239 0.1181 -0.0197 0.0480  -0.0368 36  HIS A O    
343  C  CB   A HIS A 36  ? 0.1386 0.1222 0.0869 0.0074  -0.0074 0.0399  36  HIS A CB   
344  C  CB   B HIS A 36  ? 0.2224 0.1054 0.1133 0.0068  0.0351  0.0076  36  HIS A CB   
345  C  CG   A HIS A 36  ? 0.1992 0.0768 0.0921 0.0020  -0.0401 0.0414  36  HIS A CG   
346  C  CG   B HIS A 36  ? 0.2624 0.1085 0.1335 0.0197  0.0000  0.0644  36  HIS A CG   
347  N  ND1  A HIS A 36  ? 0.2560 0.1247 0.0969 0.0401  0.0124  0.0285  36  HIS A ND1  
348  N  ND1  B HIS A 36  ? 0.2978 0.1414 0.1522 0.0403  -0.0430 0.0878  36  HIS A ND1  
349  C  CD2  A HIS A 36  ? 0.1587 0.1096 0.1344 0.0502  0.0171  0.0031  36  HIS A CD2  
350  C  CD2  B HIS A 36  ? 0.3082 0.1586 0.2172 -0.0065 0.0017  0.0173  36  HIS A CD2  
351  C  CE1  A HIS A 36  ? 0.2416 0.0776 0.1326 0.0137  -0.0163 0.0186  36  HIS A CE1  
352  C  CE1  B HIS A 36  ? 0.2840 0.1457 0.1386 0.0397  -0.0443 0.0566  36  HIS A CE1  
353  N  NE2  A HIS A 36  ? 0.2743 0.1018 0.1780 -0.0229 -0.0313 0.0170  36  HIS A NE2  
354  N  NE2  B HIS A 36  ? 0.2973 0.2046 0.2400 -0.0114 -0.0220 0.0109  36  HIS A NE2  
355  N  N    A THR A 37  ? 0.1865 0.1242 0.1105 0.0015  0.0175  0.0308  37  THR A N    
356  N  N    B THR A 37  ? 0.2057 0.1134 0.1005 0.0399  0.0184  0.0060  37  THR A N    
357  C  CA   A THR A 37  ? 0.2147 0.0996 0.1098 0.0087  0.0166  0.0406  37  THR A CA   
358  C  CA   B THR A 37  ? 0.2282 0.1254 0.1242 0.0266  0.0208  0.0335  37  THR A CA   
359  C  C    A THR A 37  ? 0.2316 0.1368 0.1106 0.0146  0.0308  0.0284  37  THR A C    
360  C  C    B THR A 37  ? 0.2445 0.1143 0.1105 0.0549  0.0175  0.0232  37  THR A C    
361  O  O    A THR A 37  ? 0.2179 0.1380 0.1152 0.0243  0.0097  0.0041  37  THR A O    
362  O  O    B THR A 37  ? 0.2725 0.1341 0.1455 0.0390  0.0167  0.0394  37  THR A O    
363  C  CB   A THR A 37  ? 0.2104 0.1676 0.1793 0.0263  0.0115  0.0288  37  THR A CB   
364  C  CB   B THR A 37  ? 0.2199 0.0913 0.2099 0.0258  -0.0071 0.0754  37  THR A CB   
365  O  OG1  A THR A 37  ? 0.2847 0.1563 0.2903 0.0509  0.0206  0.0204  37  THR A OG1  
366  O  OG1  B THR A 37  ? 0.2942 0.1917 0.2574 0.0706  -0.0175 0.0904  37  THR A OG1  
367  C  CG2  A THR A 37  ? 0.2301 0.2388 0.0940 -0.0038 0.0148  0.0197  37  THR A CG2  
368  C  CG2  B THR A 37  ? 0.1931 0.1897 0.1509 0.0126  0.0010  0.0076  37  THR A CG2  
369  N  N    . ALA A 38  ? 0.2621 0.1281 0.1023 0.0436  0.0187  0.0262  38  ALA A N    
370  C  CA   . ALA A 38  ? 0.2563 0.1132 0.0856 0.0357  0.0454  0.0346  38  ALA A CA   
371  C  C    . ALA A 38  ? 0.2578 0.1466 0.1553 0.0331  0.0640  0.0390  38  ALA A C    
372  O  O    . ALA A 38  ? 0.3382 0.1667 0.2133 0.0388  0.1048  0.0339  38  ALA A O    
373  C  CB   . ALA A 38  ? 0.2276 0.1136 0.1123 0.0214  0.0244  0.0104  38  ALA A CB   
374  N  N    . LYS A 39  ? 0.2479 0.1666 0.1093 0.0498  0.0176  -0.0020 39  LYS A N    
375  C  CA   . LYS A 39  ? 0.2745 0.2195 0.0926 0.0662  0.0034  0.0057  39  LYS A CA   
376  C  C    . LYS A 39  ? 0.2145 0.1809 0.1076 0.0456  0.0309  0.0098  39  LYS A C    
377  O  O    . LYS A 39  ? 0.1990 0.1736 0.0915 0.0425  0.0093  0.0115  39  LYS A O    
378  C  CB   . LYS A 39  ? 0.2856 0.2157 0.1590 0.0570  -0.0218 -0.0063 39  LYS A CB   
379  C  CG   . LYS A 39  ? 0.2930 0.2617 0.1965 0.0504  0.0109  0.0087  39  LYS A CG   
380  C  CD   . LYS A 39  ? 0.2294 0.2319 0.2685 0.0715  -0.0135 0.0366  39  LYS A CD   
381  C  CE   . LYS A 39  ? 0.3253 0.2973 0.2827 0.0263  -0.0119 0.0135  39  LYS A CE   
382  N  NZ   . LYS A 39  ? 0.2479 0.3215 0.2768 0.0425  0.0293  0.1092  39  LYS A NZ   
383  N  N    . TYR A 40  ? 0.2797 0.1851 0.1027 0.0182  0.0335  0.0494  40  TYR A N    
384  C  CA   . TYR A 40  ? 0.2355 0.1881 0.1044 0.0052  0.0542  0.0185  40  TYR A CA   
385  C  C    . TYR A 40  ? 0.2120 0.2078 0.1036 -0.0030 0.0372  0.0219  40  TYR A C    
386  O  O    . TYR A 40  ? 0.2328 0.2721 0.1003 0.0500  0.0296  -0.0087 40  TYR A O    
387  C  CB   . TYR A 40  ? 0.2592 0.2407 0.1432 -0.0373 0.0714  0.0296  40  TYR A CB   
388  C  CG   . TYR A 40  ? 0.2791 0.2660 0.1351 -0.0463 0.0527  0.0296  40  TYR A CG   
389  C  CD1  . TYR A 40  ? 0.2529 0.2897 0.1719 -0.0329 0.0577  -0.0120 40  TYR A CD1  
390  C  CD2  . TYR A 40  ? 0.2743 0.3828 0.1884 -0.0107 0.0515  -0.0043 40  TYR A CD2  
391  C  CE1  . TYR A 40  ? 0.2542 0.3494 0.1608 -0.0183 0.0562  -0.0065 40  TYR A CE1  
392  C  CE2  . TYR A 40  ? 0.2439 0.4219 0.1610 -0.0153 0.0441  -0.0059 40  TYR A CE2  
393  C  CZ   . TYR A 40  ? 0.2569 0.4248 0.2079 -0.0126 0.0649  0.0185  40  TYR A CZ   
394  O  OH   . TYR A 40  ? 0.2547 0.4355 0.3075 0.0104  0.0658  -0.0148 40  TYR A OH   
395  N  N    . ASP A 41  ? 0.1838 0.1745 0.1091 0.0167  0.0335  -0.0076 41  ASP A N    
396  C  CA   . ASP A 41  ? 0.2201 0.1908 0.1120 0.0114  0.0299  -0.0258 41  ASP A CA   
397  C  C    . ASP A 41  ? 0.2281 0.2285 0.1441 0.0205  0.0474  -0.0377 41  ASP A C    
398  O  O    . ASP A 41  ? 0.1975 0.2330 0.1387 0.0294  0.0272  -0.0103 41  ASP A O    
399  C  CB   . ASP A 41  ? 0.2233 0.1702 0.1570 0.0030  0.0074  -0.0142 41  ASP A CB   
400  C  CG   . ASP A 41  ? 0.2364 0.2064 0.2178 -0.0203 -0.0038 -0.0252 41  ASP A CG   
401  O  OD1  . ASP A 41  ? 0.2619 0.2201 0.2141 0.0065  -0.0013 -0.0790 41  ASP A OD1  
402  O  OD2  . ASP A 41  ? 0.2827 0.2291 0.2427 -0.0913 -0.0392 0.0087  41  ASP A OD2  
403  N  N    . PRO A 42  ? 0.2262 0.2770 0.1680 0.0487  0.0441  -0.0242 42  PRO A N    
404  C  CA   . PRO A 42  ? 0.2481 0.2888 0.2247 0.0410  0.0485  -0.0068 42  PRO A CA   
405  C  C    . PRO A 42  ? 0.2291 0.2621 0.2202 0.0745  0.0498  -0.0184 42  PRO A C    
406  O  O    . PRO A 42  ? 0.2266 0.4011 0.2962 0.0684  0.0294  0.0034  42  PRO A O    
407  C  CB   . PRO A 42  ? 0.2569 0.3418 0.2203 0.0296  0.0640  -0.0108 42  PRO A CB   
408  C  CG   . PRO A 42  ? 0.2745 0.3231 0.2300 0.0355  0.0636  -0.0215 42  PRO A CG   
409  C  CD   . PRO A 42  ? 0.2515 0.2660 0.1738 0.0548  0.0586  0.0098  42  PRO A CD   
410  N  N    . SER A 43  ? 0.2601 0.2576 0.2003 0.0621  0.0285  -0.0273 43  SER A N    
411  C  CA   . SER A 43  ? 0.2759 0.2594 0.2328 0.0548  0.0013  -0.0194 43  SER A CA   
412  C  C    . SER A 43  ? 0.2942 0.2452 0.2029 0.0566  0.0027  -0.0131 43  SER A C    
413  O  O    . SER A 43  ? 0.3587 0.2276 0.2515 0.0579  0.0307  0.0015  43  SER A O    
414  C  CB   . SER A 43  ? 0.2705 0.2750 0.2253 0.0351  0.0043  -0.0218 43  SER A CB   
415  O  OG   . SER A 43  ? 0.2793 0.2386 0.3183 -0.0184 -0.0439 -0.0603 43  SER A OG   
416  N  N    . LEU A 44  ? 0.3032 0.2461 0.1708 0.0447  -0.0063 -0.0126 44  LEU A N    
417  C  CA   . LEU A 44  ? 0.2357 0.2240 0.1757 0.0307  -0.0054 -0.0027 44  LEU A CA   
418  C  C    . LEU A 44  ? 0.2249 0.2440 0.2154 -0.0049 -0.0082 -0.0017 44  LEU A C    
419  O  O    . LEU A 44  ? 0.2285 0.3303 0.2833 0.0017  0.0148  0.0948  44  LEU A O    
420  C  CB   . LEU A 44  ? 0.2215 0.2064 0.1475 0.0048  0.0143  -0.0221 44  LEU A CB   
421  C  CG   . LEU A 44  ? 0.1746 0.2208 0.1213 0.0141  -0.0126 0.0093  44  LEU A CG   
422  C  CD1  . LEU A 44  ? 0.2345 0.1908 0.1522 -0.0054 0.0291  -0.0305 44  LEU A CD1  
423  C  CD2  . LEU A 44  ? 0.2741 0.1396 0.2109 -0.0281 0.0098  -0.0006 44  LEU A CD2  
424  N  N    . LYS A 45  ? 0.2221 0.2181 0.2205 0.0196  -0.0054 0.0010  45  LYS A N    
425  C  CA   . LYS A 45  ? 0.2181 0.2021 0.2342 0.0131  -0.0165 -0.0208 45  LYS A CA   
426  C  C    . LYS A 45  ? 0.1856 0.2123 0.2048 0.0377  0.0099  -0.0175 45  LYS A C    
427  O  O    . LYS A 45  ? 0.1786 0.1983 0.2145 0.0147  0.0126  -0.0478 45  LYS A O    
428  C  CB   . LYS A 45  ? 0.2309 0.2003 0.2357 0.0507  0.0000  -0.0176 45  LYS A CB   
429  C  CG   . LYS A 45  ? 0.2610 0.2396 0.2982 0.0285  -0.0049 -0.0243 45  LYS A CG   
430  C  CD   . LYS A 45  ? 0.3136 0.2858 0.3393 0.0013  -0.0076 -0.0186 45  LYS A CD   
431  C  CE   . LYS A 45  ? 0.4047 0.3657 0.3799 -0.0125 -0.0073 -0.0229 45  LYS A CE   
432  N  NZ   . LYS A 45  ? 0.4494 0.5077 0.4757 -0.0085 0.0417  -0.0215 45  LYS A NZ   
433  N  N    . PRO A 46  ? 0.1493 0.2273 0.2154 -0.0052 0.0291  -0.0104 46  PRO A N    
434  C  CA   . PRO A 46  ? 0.1811 0.1886 0.2222 -0.0065 -0.0065 -0.0007 46  PRO A CA   
435  C  C    . PRO A 46  ? 0.1515 0.1197 0.2111 0.0093  0.0333  0.0015  46  PRO A C    
436  O  O    . PRO A 46  ? 0.1337 0.1676 0.2515 -0.0093 0.0081  0.0107  46  PRO A O    
437  C  CB   . PRO A 46  ? 0.1597 0.2009 0.2323 -0.0165 0.0088  0.0131  46  PRO A CB   
438  C  CG   . PRO A 46  ? 0.1818 0.2928 0.2766 -0.0020 0.0005  -0.0137 46  PRO A CG   
439  C  CD   . PRO A 46  ? 0.1719 0.2314 0.2438 0.0364  0.0109  -0.0173 46  PRO A CD   
440  N  N    . LEU A 47  ? 0.1587 0.1580 0.2445 -0.0007 -0.0074 0.0142  47  LEU A N    
441  C  CA   . LEU A 47  ? 0.0982 0.1640 0.2262 -0.0156 0.0098  0.0126  47  LEU A CA   
442  C  C    . LEU A 47  ? 0.1274 0.1832 0.2486 -0.0206 -0.0006 0.0423  47  LEU A C    
443  O  O    . LEU A 47  ? 0.1562 0.2179 0.3585 -0.0658 -0.0516 0.0869  47  LEU A O    
444  C  CB   . LEU A 47  ? 0.1633 0.1942 0.2763 0.0373  -0.0136 -0.0010 47  LEU A CB   
445  C  CG   . LEU A 47  ? 0.1574 0.2091 0.2757 -0.0131 -0.0181 -0.0450 47  LEU A CG   
446  C  CD1  . LEU A 47  ? 0.1280 0.2312 0.3623 -0.0430 -0.0294 -0.0458 47  LEU A CD1  
447  C  CD2  . LEU A 47  ? 0.1633 0.2181 0.3167 0.0207  0.0250  -0.0307 47  LEU A CD2  
448  N  N    . SER A 48  ? 0.1089 0.1674 0.1974 -0.0258 -0.0038 0.0368  48  SER A N    
449  C  CA   . SER A 48  ? 0.1217 0.1484 0.2143 -0.0118 0.0048  0.0219  48  SER A CA   
450  C  C    . SER A 48  ? 0.1155 0.1552 0.2078 -0.0200 -0.0041 0.0041  48  SER A C    
451  O  O    . SER A 48  ? 0.1237 0.1362 0.1912 -0.0417 -0.0038 -0.0098 48  SER A O    
452  C  CB   . SER A 48  ? 0.1314 0.1553 0.2360 -0.0019 0.0043  0.0146  48  SER A CB   
453  O  OG   . SER A 48  ? 0.1454 0.1849 0.2434 0.0225  0.0102  0.0275  48  SER A OG   
454  N  N    . VAL A 49  ? 0.1553 0.1405 0.1913 -0.0533 -0.0006 0.0035  49  VAL A N    
455  C  CA   . VAL A 49  ? 0.1630 0.1401 0.2254 -0.0640 -0.0164 -0.0046 49  VAL A CA   
456  C  C    . VAL A 49  ? 0.1696 0.1579 0.2440 -0.0562 -0.0204 -0.0026 49  VAL A C    
457  O  O    . VAL A 49  ? 0.2095 0.2795 0.2583 -0.0966 -0.0544 0.0086  49  VAL A O    
458  C  CB   . VAL A 49  ? 0.2165 0.1633 0.2136 -0.0732 0.0120  -0.0076 49  VAL A CB   
459  C  CG1  . VAL A 49  ? 0.2915 0.1879 0.2587 -0.0702 0.0423  -0.0252 49  VAL A CG1  
460  C  CG2  . VAL A 49  ? 0.2172 0.1675 0.2784 -0.0520 -0.0043 -0.0288 49  VAL A CG2  
461  N  N    . SER A 50  ? 0.1383 0.1852 0.2253 -0.0579 -0.0463 -0.0115 50  SER A N    
462  C  CA   . SER A 50  ? 0.1822 0.2011 0.2675 -0.0211 -0.0430 0.0043  50  SER A CA   
463  C  C    . SER A 50  ? 0.1312 0.1949 0.2533 -0.0142 -0.0680 0.0126  50  SER A C    
464  O  O    . SER A 50  ? 0.1932 0.1662 0.2603 -0.0390 -0.0588 0.0219  50  SER A O    
465  C  CB   . SER A 50  ? 0.1768 0.2500 0.2994 -0.0030 -0.0487 0.0192  50  SER A CB   
466  O  OG   . SER A 50  ? 0.2172 0.3361 0.3400 0.0132  -0.0164 -0.0397 50  SER A OG   
467  N  N    . TYR A 51  ? 0.1714 0.1569 0.2307 -0.0285 -0.0777 0.0119  51  TYR A N    
468  C  CA   . TYR A 51  ? 0.1831 0.1552 0.2167 -0.0272 -0.0737 0.0275  51  TYR A CA   
469  C  C    . TYR A 51  ? 0.1922 0.1676 0.2442 -0.0003 -0.0621 0.0335  51  TYR A C    
470  O  O    . TYR A 51  ? 0.1985 0.2161 0.2350 -0.0049 -0.0917 0.0353  51  TYR A O    
471  C  CB   . TYR A 51  ? 0.1719 0.1592 0.1764 -0.0377 -0.0562 0.0085  51  TYR A CB   
472  C  CG   . TYR A 51  ? 0.1590 0.1238 0.1357 -0.0286 -0.0553 0.0091  51  TYR A CG   
473  C  CD1  . TYR A 51  ? 0.1826 0.1057 0.1951 -0.0142 -0.0531 0.0093  51  TYR A CD1  
474  C  CD2  . TYR A 51  ? 0.1739 0.1141 0.1308 -0.0208 -0.0423 0.0082  51  TYR A CD2  
475  C  CE1  . TYR A 51  ? 0.1687 0.1019 0.1380 -0.0452 -0.0461 0.0196  51  TYR A CE1  
476  C  CE2  . TYR A 51  ? 0.1583 0.0935 0.1432 -0.0209 -0.0421 0.0065  51  TYR A CE2  
477  C  CZ   . TYR A 51  ? 0.1479 0.0890 0.1409 -0.0251 -0.0414 0.0186  51  TYR A CZ   
478  O  OH   . TYR A 51  ? 0.1466 0.0906 0.1547 -0.0236 -0.0346 0.0043  51  TYR A OH   
479  N  N    A ASP A 52  ? 0.1788 0.1865 0.2630 -0.0222 -0.0595 0.0164  52  ASP A N    
480  N  N    B ASP A 52  ? 0.2029 0.2019 0.2043 0.0015  -0.0780 0.0837  52  ASP A N    
481  C  CA   A ASP A 52  ? 0.2093 0.2026 0.2619 0.0068  -0.0359 0.0218  52  ASP A CA   
482  C  CA   B ASP A 52  ? 0.2233 0.2305 0.2460 0.0005  -0.0553 0.0513  52  ASP A CA   
483  C  C    A ASP A 52  ? 0.1906 0.1929 0.2761 0.0186  -0.0496 0.0324  52  ASP A C    
484  C  C    B ASP A 52  ? 0.2350 0.2509 0.2678 0.0065  -0.0665 0.0549  52  ASP A C    
485  O  O    A ASP A 52  ? 0.1574 0.1734 0.2657 0.0054  -0.0538 0.0317  52  ASP A O    
486  O  O    B ASP A 52  ? 0.1825 0.3023 0.2869 0.0232  -0.0414 0.0599  52  ASP A O    
487  C  CB   A ASP A 52  ? 0.2113 0.2178 0.2680 0.0142  -0.0262 0.0188  52  ASP A CB   
488  C  CB   B ASP A 52  ? 0.2289 0.2624 0.2660 0.0059  -0.0564 0.0461  52  ASP A CB   
489  C  CG   A ASP A 52  ? 0.2700 0.2899 0.3118 0.0010  -0.0203 0.0006  52  ASP A CG   
490  C  CG   B ASP A 52  ? 0.2874 0.2969 0.3395 0.0370  -0.0428 0.0474  52  ASP A CG   
491  O  OD1  A ASP A 52  ? 0.3328 0.3438 0.3425 0.0118  0.0000  0.0412  52  ASP A OD1  
492  O  OD1  B ASP A 52  ? 0.3337 0.3495 0.3574 0.0702  -0.0948 0.0276  52  ASP A OD1  
493  O  OD2  A ASP A 52  ? 0.3889 0.3797 0.3957 0.0254  -0.0284 0.0304  52  ASP A OD2  
494  O  OD2  B ASP A 52  ? 0.4435 0.3858 0.4445 0.0505  0.0210  -0.0099 52  ASP A OD2  
495  N  N    . GLN A 53  ? 0.2231 0.2075 0.3118 -0.0006 -0.0509 0.0649  53  GLN A N    
496  C  CA   . GLN A 53  ? 0.2572 0.1967 0.2861 -0.0104 -0.0472 0.0255  53  GLN A CA   
497  C  C    . GLN A 53  ? 0.2576 0.1795 0.2407 -0.0063 -0.0560 0.0280  53  GLN A C    
498  O  O    . GLN A 53  ? 0.2366 0.1750 0.2725 -0.0307 -0.0706 0.0362  53  GLN A O    
499  C  CB   . GLN A 53  ? 0.2716 0.2280 0.3461 -0.0085 -0.0364 0.0348  53  GLN A CB   
500  C  CG   . GLN A 53  ? 0.3564 0.3790 0.4219 -0.0065 0.0081  0.0164  53  GLN A CG   
501  C  CD   . GLN A 53  ? 0.4296 0.4718 0.4309 -0.0005 -0.0152 0.0263  53  GLN A CD   
502  O  OE1  . GLN A 53  ? 0.4384 0.4808 0.5205 0.0242  0.0181  0.0441  53  GLN A OE1  
503  N  NE2  . GLN A 53  ? 0.4700 0.4787 0.4406 0.0073  -0.0263 0.0599  53  GLN A NE2  
504  N  N    . ALA A 54  ? 0.2707 0.1337 0.2391 -0.0208 -0.0603 -0.0038 54  ALA A N    
505  C  CA   . ALA A 54  ? 0.2479 0.1362 0.1969 -0.0132 -0.0593 -0.0219 54  ALA A CA   
506  C  C    . ALA A 54  ? 0.2703 0.1357 0.1838 -0.0060 -0.0644 -0.0305 54  ALA A C    
507  O  O    . ALA A 54  ? 0.3208 0.2424 0.2469 -0.0408 -0.0702 -0.0575 54  ALA A O    
508  C  CB   . ALA A 54  ? 0.2822 0.1211 0.2369 -0.0120 -0.0351 -0.0273 54  ALA A CB   
509  N  N    A THR A 55  ? 0.2278 0.0888 0.1472 0.0046  -0.0706 0.0013  55  THR A N    
510  N  N    B THR A 55  ? 0.2353 0.1055 0.1559 0.0093  -0.0636 -0.0077 55  THR A N    
511  C  CA   A THR A 55  ? 0.2187 0.1048 0.1314 0.0405  -0.0794 0.0071  55  THR A CA   
512  C  CA   B THR A 55  ? 0.2271 0.1030 0.1418 0.0204  -0.0524 0.0087  55  THR A CA   
513  C  C    A THR A 55  ? 0.1763 0.1046 0.0899 0.0156  -0.0377 -0.0148 55  THR A C    
514  C  C    B THR A 55  ? 0.2093 0.0755 0.0803 0.0109  -0.0533 0.0394  55  THR A C    
515  O  O    A THR A 55  ? 0.1867 0.0847 0.1252 0.0137  -0.0575 0.0142  55  THR A O    
516  O  O    B THR A 55  ? 0.2660 0.0548 0.0949 0.0005  -0.0496 0.0041  55  THR A O    
517  C  CB   A THR A 55  ? 0.2560 0.1261 0.1753 0.0012  -0.0590 0.0151  55  THR A CB   
518  C  CB   B THR A 55  ? 0.2398 0.1466 0.1631 0.0205  -0.0322 0.0031  55  THR A CB   
519  O  OG1  A THR A 55  ? 0.3298 0.0463 0.2111 0.0187  -0.0794 -0.0054 55  THR A OG1  
520  O  OG1  B THR A 55  ? 0.2881 0.2791 0.3337 -0.0031 -0.0284 0.0277  55  THR A OG1  
521  C  CG2  A THR A 55  ? 0.2520 0.0906 0.1412 0.0143  -0.0776 0.0296  55  THR A CG2  
522  C  CG2  B THR A 55  ? 0.2127 0.0897 0.0996 -0.0140 -0.0615 0.0103  55  THR A CG2  
523  N  N    A SER A 56  ? 0.1362 0.0662 0.0951 0.0156  -0.0093 -0.0120 56  SER A N    
524  N  N    B SER A 56  ? 0.1601 0.0881 0.0856 0.0043  -0.0261 0.0114  56  SER A N    
525  C  CA   A SER A 56  ? 0.1190 0.0860 0.0876 -0.0091 -0.0082 0.0041  56  SER A CA   
526  C  CA   B SER A 56  ? 0.1430 0.0764 0.0838 -0.0017 -0.0178 0.0063  56  SER A CA   
527  C  C    A SER A 56  ? 0.1185 0.0678 0.0658 0.0015  -0.0185 0.0175  56  SER A C    
528  C  C    B SER A 56  ? 0.1465 0.0908 0.0847 0.0031  -0.0194 0.0275  56  SER A C    
529  O  O    A SER A 56  ? 0.1208 0.0764 0.0832 0.0148  -0.0296 0.0164  56  SER A O    
530  O  O    B SER A 56  ? 0.1641 0.0847 0.0967 0.0203  -0.0386 0.0024  56  SER A O    
531  C  CB   A SER A 56  ? 0.1271 0.0617 0.0864 0.0115  -0.0161 0.0198  56  SER A CB   
532  C  CB   B SER A 56  ? 0.1409 0.0908 0.0818 0.0027  -0.0195 0.0143  56  SER A CB   
533  O  OG   A SER A 56  ? 0.1091 0.0676 0.0958 -0.0164 -0.0351 0.0096  56  SER A OG   
534  O  OG   B SER A 56  ? 0.1429 0.0730 0.1105 -0.0052 -0.0339 0.0156  56  SER A OG   
535  N  N    A LEU A 57  ? 0.1118 0.0509 0.0885 -0.0015 -0.0103 0.0096  57  LEU A N    
536  N  N    B LEU A 57  ? 0.1498 0.0985 0.0868 0.0015  -0.0124 0.0189  57  LEU A N    
537  C  CA   A LEU A 57  ? 0.1089 0.0534 0.0863 0.0043  -0.0174 0.0092  57  LEU A CA   
538  C  CA   B LEU A 57  ? 0.1694 0.0739 0.0881 0.0037  0.0043  0.0408  57  LEU A CA   
539  C  C    A LEU A 57  ? 0.1102 0.0428 0.0886 -0.0218 -0.0217 0.0142  57  LEU A C    
540  C  C    B LEU A 57  ? 0.1504 0.0922 0.1039 0.0115  0.0102  0.0244  57  LEU A C    
541  O  O    A LEU A 57  ? 0.1246 0.0863 0.0669 0.0068  -0.0131 0.0318  57  LEU A O    
542  O  O    B LEU A 57  ? 0.1660 0.1041 0.0800 -0.0063 0.0104  0.0454  57  LEU A O    
543  C  CB   A LEU A 57  ? 0.1574 0.0581 0.1143 -0.0087 -0.0043 0.0166  57  LEU A CB   
544  C  CB   B LEU A 57  ? 0.1729 0.0744 0.0882 0.0272  0.0185  0.0159  57  LEU A CB   
545  C  CG   A LEU A 57  ? 0.1865 0.0922 0.1563 0.0031  -0.0320 0.0049  57  LEU A CG   
546  C  CG   B LEU A 57  ? 0.2073 0.1154 0.1254 0.0208  0.0015  0.0003  57  LEU A CG   
547  C  CD1  A LEU A 57  ? 0.1981 0.1057 0.1852 -0.0197 -0.0249 -0.0120 57  LEU A CD1  
548  C  CD1  B LEU A 57  ? 0.2057 0.1014 0.1599 0.0187  0.0176  -0.0096 57  LEU A CD1  
549  C  CD2  A LEU A 57  ? 0.3050 0.1204 0.1851 0.0421  -0.0939 0.0274  57  LEU A CD2  
550  C  CD2  B LEU A 57  ? 0.2748 0.1054 0.2224 0.0533  -0.0344 0.0410  57  LEU A CD2  
551  N  N    A ARG A 58  ? 0.1028 0.0581 0.0879 -0.0082 -0.0104 0.0362  58  ARG A N    
552  N  N    B ARG A 58  ? 0.1597 0.1066 0.0798 0.0038  -0.0065 0.0342  58  ARG A N    
553  C  CA   A ARG A 58  ? 0.0979 0.0600 0.0730 -0.0098 -0.0225 0.0164  58  ARG A CA   
554  C  CA   B ARG A 58  ? 0.1576 0.0744 0.0904 0.0068  0.0077  0.0142  58  ARG A CA   
555  C  C    A ARG A 58  ? 0.0750 0.0563 0.0697 -0.0241 0.0031  0.0153  58  ARG A C    
556  C  C    B ARG A 58  ? 0.1307 0.0933 0.0455 -0.0031 0.0086  0.0238  58  ARG A C    
557  O  O    A ARG A 58  ? 0.0969 0.0739 0.0790 -0.0081 -0.0074 0.0146  58  ARG A O    
558  O  O    B ARG A 58  ? 0.1529 0.0863 0.0777 0.0288  0.0006  0.0164  58  ARG A O    
559  C  CB   A ARG A 58  ? 0.1179 0.0547 0.1049 0.0006  -0.0208 0.0222  58  ARG A CB   
560  C  CB   B ARG A 58  ? 0.1333 0.0728 0.1283 0.0060  0.0093  0.0024  58  ARG A CB   
561  C  CG   A ARG A 58  ? 0.1459 0.0688 0.0870 -0.0329 -0.0017 0.0211  58  ARG A CG   
562  C  CG   B ARG A 58  ? 0.2019 0.0930 0.1552 -0.0189 0.0247  0.0017  58  ARG A CG   
563  C  CD   A ARG A 58  ? 0.1551 0.0922 0.1281 -0.0175 0.0020  0.0515  58  ARG A CD   
564  C  CD   B ARG A 58  ? 0.1676 0.1267 0.1732 -0.0031 0.0302  0.0120  58  ARG A CD   
565  N  NE   A ARG A 58  ? 0.1366 0.0933 0.0890 -0.0017 -0.0074 0.0351  58  ARG A NE   
566  N  NE   B ARG A 58  ? 0.1716 0.1398 0.2175 -0.0619 0.0436  -0.0005 58  ARG A NE   
567  C  CZ   A ARG A 58  ? 0.0964 0.1678 0.0555 -0.0443 0.0000  0.0588  58  ARG A CZ   
568  C  CZ   B ARG A 58  ? 0.1714 0.0753 0.1878 -0.0148 0.0060  0.0401  58  ARG A CZ   
569  N  NH1  A ARG A 58  ? 0.1324 0.1093 0.1279 -0.0361 0.0153  0.0308  58  ARG A NH1  
570  N  NH1  B ARG A 58  ? 0.2174 0.1359 0.1845 0.0375  0.0024  0.0286  58  ARG A NH1  
571  N  NH2  A ARG A 58  ? 0.1321 0.0529 0.0939 -0.0273 0.0230  0.0236  58  ARG A NH2  
572  N  NH2  B ARG A 58  ? 0.2475 0.1048 0.1915 0.0077  0.0504  -0.0438 58  ARG A NH2  
573  N  N    A ILE A 59  ? 0.0809 0.0693 0.0563 -0.0140 -0.0063 0.0148  59  ILE A N    
574  N  N    B ILE A 59  ? 0.1585 0.0642 0.0705 -0.0015 0.0143  0.0249  59  ILE A N    
575  C  CA   A ILE A 59  ? 0.0865 0.0746 0.0596 -0.0020 -0.0159 -0.0038 59  ILE A CA   
576  C  CA   B ILE A 59  ? 0.1305 0.0545 0.0658 0.0082  -0.0164 0.0283  59  ILE A CA   
577  C  C    A ILE A 59  ? 0.0793 0.0624 0.0702 0.0126  -0.0081 0.0152  59  ILE A C    
578  C  C    B ILE A 59  ? 0.1488 0.0635 0.0978 0.0010  -0.0035 0.0277  59  ILE A C    
579  O  O    A ILE A 59  ? 0.1026 0.1447 0.0474 0.0186  -0.0034 0.0230  59  ILE A O    
580  O  O    B ILE A 59  ? 0.1520 0.0985 0.0741 0.0046  -0.0034 0.0272  59  ILE A O    
581  C  CB   A ILE A 59  ? 0.0815 0.0674 0.0969 -0.0219 -0.0193 0.0114  59  ILE A CB   
582  C  CB   B ILE A 59  ? 0.1448 0.0903 0.0723 -0.0096 -0.0110 0.0320  59  ILE A CB   
583  C  CG1  A ILE A 59  ? 0.0908 0.1039 0.0640 -0.0038 -0.0229 -0.0186 59  ILE A CG1  
584  C  CG1  B ILE A 59  ? 0.1757 0.0657 0.0656 0.0141  -0.0255 0.0019  59  ILE A CG1  
585  C  CG2  A ILE A 59  ? 0.1098 0.0773 0.0502 -0.0104 -0.0368 0.0060  59  ILE A CG2  
586  C  CG2  B ILE A 59  ? 0.1190 0.1075 0.1018 -0.0174 -0.0220 0.0284  59  ILE A CG2  
587  C  CD1  A ILE A 59  ? 0.1109 0.0489 0.0816 -0.0199 0.0013  -0.0104 59  ILE A CD1  
588  C  CD1  B ILE A 59  ? 0.1585 0.1134 0.1111 0.0031  0.0110  0.0118  59  ILE A CD1  
589  N  N    A LEU A 60  ? 0.0915 0.0574 0.0741 -0.0065 -0.0020 0.0136  60  LEU A N    
590  N  N    B LEU A 60  ? 0.1349 0.0750 0.0507 -0.0115 -0.0073 0.0057  60  LEU A N    
591  C  CA   A LEU A 60  ? 0.0777 0.0437 0.0660 0.0052  -0.0071 0.0218  60  LEU A CA   
592  C  CA   B LEU A 60  ? 0.1445 0.0894 0.0807 -0.0043 -0.0153 0.0082  60  LEU A CA   
593  C  C    A LEU A 60  ? 0.0730 0.0423 0.0784 -0.0092 -0.0107 0.0228  60  LEU A C    
594  C  C    B LEU A 60  ? 0.1365 0.0483 0.0662 0.0010  0.0093  0.0081  60  LEU A C    
595  O  O    A LEU A 60  ? 0.0599 0.0362 0.0789 0.0104  -0.0035 0.0189  60  LEU A O    
596  O  O    B LEU A 60  ? 0.1531 0.0870 0.0563 0.0337  0.0037  0.0274  60  LEU A O    
597  C  CB   A LEU A 60  ? 0.0791 0.0547 0.0667 -0.0027 -0.0015 0.0031  60  LEU A CB   
598  C  CB   B LEU A 60  ? 0.1570 0.0942 0.1319 -0.0247 -0.0125 0.0129  60  LEU A CB   
599  C  CG   A LEU A 60  ? 0.0820 0.0377 0.0996 0.0056  -0.0147 0.0273  60  LEU A CG   
600  C  CG   B LEU A 60  ? 0.1895 0.1064 0.1001 -0.0262 -0.0227 0.0119  60  LEU A CG   
601  C  CD1  A LEU A 60  ? 0.0952 0.0595 0.1014 -0.0160 -0.0121 0.0333  60  LEU A CD1  
602  C  CD1  B LEU A 60  ? 0.2037 0.1163 0.1568 -0.0348 -0.0164 -0.0010 60  LEU A CD1  
603  C  CD2  A LEU A 60  ? 0.0899 0.0306 0.1215 -0.0126 -0.0114 0.0087  60  LEU A CD2  
604  C  CD2  B LEU A 60  ? 0.1592 0.1127 0.1723 -0.0283 -0.0205 0.0006  60  LEU A CD2  
605  N  N    A ASN A 61  ? 0.0865 0.0410 0.0421 0.0007  -0.0081 0.0077  61  ASN A N    
606  N  N    B ASN A 61  ? 0.1347 0.0872 0.0678 -0.0173 0.0030  0.0059  61  ASN A N    
607  C  CA   A ASN A 61  ? 0.0908 0.0676 0.0744 0.0159  -0.0007 0.0020  61  ASN A CA   
608  C  CA   B ASN A 61  ? 0.1181 0.0666 0.0727 -0.0135 0.0104  0.0253  61  ASN A CA   
609  C  C    A ASN A 61  ? 0.0944 0.0564 0.0533 0.0118  0.0049  -0.0013 61  ASN A C    
610  C  C    B ASN A 61  ? 0.1359 0.0651 0.1014 -0.0198 0.0120  0.0020  61  ASN A C    
611  O  O    A ASN A 61  ? 0.0775 0.0644 0.0908 0.0043  -0.0131 0.0377  61  ASN A O    
612  O  O    B ASN A 61  ? 0.1260 0.0843 0.0861 -0.0120 0.0043  0.0250  61  ASN A O    
613  C  CB   A ASN A 61  ? 0.0953 0.0696 0.0671 0.0015  0.0120  -0.0146 61  ASN A CB   
614  C  CB   B ASN A 61  ? 0.1052 0.0739 0.0881 -0.0130 0.0240  0.0081  61  ASN A CB   
615  C  CG   A ASN A 61  ? 0.0992 0.0377 0.0737 0.0156  -0.0082 0.0153  61  ASN A CG   
616  C  CG   B ASN A 61  ? 0.1270 0.0899 0.0809 -0.0203 0.0188  -0.0062 61  ASN A CG   
617  O  OD1  A ASN A 61  ? 0.0865 0.0516 0.0890 -0.0003 0.0070  -0.0063 61  ASN A OD1  
618  O  OD1  B ASN A 61  ? 0.1188 0.0933 0.1215 -0.0027 0.0063  0.0003  61  ASN A OD1  
619  N  ND2  A ASN A 61  ? 0.1041 0.0481 0.0696 -0.0074 0.0048  -0.0019 61  ASN A ND2  
620  N  ND2  B ASN A 61  ? 0.1281 0.1005 0.0920 -0.0142 0.0109  -0.0259 61  ASN A ND2  
621  N  N    A ASN A 62  ? 0.0938 0.0420 0.0656 0.0115  0.0086  0.0031  62  ASN A N    
622  N  N    B ASN A 62  ? 0.1308 0.0750 0.0755 -0.0154 0.0164  0.0266  62  ASN A N    
623  C  CA   A ASN A 62  ? 0.0992 0.0463 0.0942 0.0048  -0.0088 0.0152  62  ASN A CA   
624  C  CA   B ASN A 62  ? 0.1340 0.0644 0.1096 -0.0307 0.0027  0.0126  62  ASN A CA   
625  C  C    A ASN A 62  ? 0.1049 0.0727 0.0890 -0.0017 -0.0130 0.0093  62  ASN A C    
626  C  C    B ASN A 62  ? 0.1565 0.0940 0.0863 -0.0333 0.0333  0.0229  62  ASN A C    
627  O  O    A ASN A 62  ? 0.1195 0.0829 0.1500 -0.0109 -0.0043 0.0054  62  ASN A O    
628  O  O    B ASN A 62  ? 0.1450 0.0802 0.1364 -0.0254 0.0017  -0.0062 62  ASN A O    
629  C  CB   A ASN A 62  ? 0.1215 0.0838 0.1017 -0.0041 -0.0141 -0.0082 62  ASN A CB   
630  C  CB   B ASN A 62  ? 0.1504 0.0806 0.1254 -0.0353 0.0063  0.0175  62  ASN A CB   
631  C  CG   A ASN A 62  ? 0.0961 0.1005 0.0739 -0.0208 -0.0282 -0.0076 62  ASN A CG   
632  C  CG   B ASN A 62  ? 0.1202 0.1037 0.0642 -0.0322 -0.0241 -0.0151 62  ASN A CG   
633  O  OD1  A ASN A 62  ? 0.1008 0.0850 0.1037 0.0054  -0.0062 -0.0017 62  ASN A OD1  
634  O  OD1  B ASN A 62  ? 0.0976 0.0879 0.1143 -0.0219 0.0031  0.0185  62  ASN A OD1  
635  N  ND2  A ASN A 62  ? 0.2319 0.1212 0.1120 0.0027  0.0505  0.0013  62  ASN A ND2  
636  N  ND2  B ASN A 62  ? 0.1752 0.0715 0.1502 -0.0259 -0.0091 -0.0104 62  ASN A ND2  
637  N  N    A GLY A 63  ? 0.1018 0.0815 0.0741 0.0049  0.0034  0.0195  63  GLY A N    
638  N  N    B GLY A 63  ? 0.1435 0.0603 0.1190 -0.0353 0.0175  -0.0062 63  GLY A N    
639  C  CA   A GLY A 63  ? 0.1280 0.0872 0.0546 0.0142  0.0015  0.0417  63  GLY A CA   
640  C  CA   B GLY A 63  ? 0.1579 0.0961 0.1137 -0.0340 0.0086  -0.0059 63  GLY A CA   
641  C  C    A GLY A 63  ? 0.1518 0.0878 0.1163 -0.0148 0.0049  0.0031  63  GLY A C    
642  C  C    B GLY A 63  ? 0.1985 0.0969 0.1445 -0.0515 0.0178  -0.0104 63  GLY A C    
643  O  O    A GLY A 63  ? 0.1453 0.1014 0.0863 0.0096  -0.0118 0.0463  63  GLY A O    
644  O  O    B GLY A 63  ? 0.1884 0.1299 0.0987 -0.0485 0.0207  0.0015  63  GLY A O    
645  N  N    . HIS A 64  ? 0.2069 0.1036 0.1256 -0.0504 0.0417  -0.0087 64  HIS A N    
646  C  CA   . HIS A 64  ? 0.1928 0.1066 0.1107 -0.0421 0.0273  0.0081  64  HIS A CA   
647  C  C    . HIS A 64  ? 0.1770 0.0845 0.1483 -0.0463 0.0340  0.0153  64  HIS A C    
648  O  O    . HIS A 64  ? 0.1831 0.1826 0.2894 -0.0329 -0.0003 0.0986  64  HIS A O    
649  C  CB   . HIS A 64  ? 0.1836 0.1574 0.1127 -0.0518 0.0210  0.0048  64  HIS A CB   
650  C  CG   . HIS A 64  ? 0.2195 0.1507 0.1432 -0.0527 0.0299  -0.0231 64  HIS A CG   
651  N  ND1  . HIS A 64  ? 0.1956 0.2228 0.1897 -0.0592 0.0604  -0.0678 64  HIS A ND1  
652  C  CD2  . HIS A 64  ? 0.2930 0.1484 0.1720 -0.0846 0.0445  -0.0199 64  HIS A CD2  
653  C  CE1  . HIS A 64  ? 0.2123 0.2456 0.2342 -0.0873 0.0478  -0.0252 64  HIS A CE1  
654  N  NE2  . HIS A 64  ? 0.2339 0.2348 0.2327 -0.0847 0.0689  -0.0553 64  HIS A NE2  
655  N  N    . ALA A 65  ? 0.2060 0.0816 0.0976 -0.0604 0.0076  0.0077  65  ALA A N    
656  C  CA   . ALA A 65  ? 0.2213 0.0703 0.0912 -0.0505 -0.0013 0.0162  65  ALA A CA   
657  C  C    . ALA A 65  ? 0.2420 0.0797 0.0612 -0.0513 0.0017  0.0065  65  ALA A C    
658  O  O    . ALA A 65  ? 0.2576 0.1005 0.0935 -0.0627 0.0198  0.0165  65  ALA A O    
659  C  CB   . ALA A 65  ? 0.2052 0.1314 0.0922 -0.0274 -0.0054 0.0057  65  ALA A CB   
660  N  N    . PHE A 66  ? 0.2373 0.0555 0.0703 -0.0388 0.0031  0.0129  66  PHE A N    
661  C  CA   . PHE A 66  ? 0.2497 0.0648 0.0714 -0.0263 0.0013  0.0220  66  PHE A CA   
662  C  C    . PHE A 66  ? 0.2472 0.0730 0.0500 -0.0329 -0.0181 0.0098  66  PHE A C    
663  O  O    . PHE A 66  ? 0.2849 0.0526 0.0482 -0.0193 0.0031  0.0049  66  PHE A O    
664  C  CB   . PHE A 66  ? 0.2522 0.0802 0.0577 -0.0222 -0.0077 0.0154  66  PHE A CB   
665  C  CG   . PHE A 66  ? 0.2897 0.0660 0.0477 -0.0121 -0.0071 -0.0121 66  PHE A CG   
666  C  CD1  . PHE A 66  ? 0.2515 0.0881 0.0746 -0.0236 -0.0230 -0.0073 66  PHE A CD1  
667  C  CD2  . PHE A 66  ? 0.2217 0.0987 0.0543 -0.0086 -0.0054 -0.0208 66  PHE A CD2  
668  C  CE1  . PHE A 66  ? 0.2578 0.1283 0.0696 -0.0049 -0.0249 -0.0172 66  PHE A CE1  
669  C  CE2  . PHE A 66  ? 0.2463 0.0651 0.0870 -0.0093 -0.0205 -0.0119 66  PHE A CE2  
670  C  CZ   . PHE A 66  ? 0.2612 0.0763 0.0953 -0.0350 -0.0355 -0.0120 66  PHE A CZ   
671  N  N    . ASN A 67  ? 0.2675 0.0768 0.0675 -0.0208 -0.0099 0.0315  67  ASN A N    
672  C  CA   . ASN A 67  ? 0.2734 0.0702 0.0714 -0.0238 -0.0049 -0.0086 67  ASN A CA   
673  C  C    . ASN A 67  ? 0.2605 0.0483 0.0802 0.0046  -0.0346 0.0193  67  ASN A C    
674  O  O    . ASN A 67  ? 0.2960 0.0863 0.0811 0.0054  -0.0087 0.0269  67  ASN A O    
675  C  CB   . ASN A 67  ? 0.3075 0.0888 0.0768 -0.0449 0.0074  0.0071  67  ASN A CB   
676  C  CG   . ASN A 67  ? 0.2772 0.1249 0.1610 -0.0549 0.0071  -0.0233 67  ASN A CG   
677  O  OD1  . ASN A 67  ? 0.2849 0.1027 0.1261 -0.0864 0.0000  0.0220  67  ASN A OD1  
678  N  ND2  . ASN A 67  ? 0.2694 0.1473 0.2459 -0.0505 -0.0031 -0.0250 67  ASN A ND2  
679  N  N    A VAL A 68  ? 0.2409 0.0433 0.0718 0.0153  -0.0175 0.0263  68  VAL A N    
680  N  N    B VAL A 68  ? 0.2937 0.0335 0.0403 0.0130  -0.0219 -0.0109 68  VAL A N    
681  C  CA   A VAL A 68  ? 0.1553 0.0687 0.0847 -0.0178 0.0043  0.0184  68  VAL A CA   
682  C  CA   B VAL A 68  ? 0.2915 0.0568 0.0307 0.0672  -0.0297 -0.0021 68  VAL A CA   
683  C  C    A VAL A 68  ? 0.2301 0.0447 0.0687 0.0063  -0.0048 0.0092  68  VAL A C    
684  C  C    B VAL A 68  ? 0.2929 0.0337 0.0258 0.0467  -0.0054 -0.0007 68  VAL A C    
685  O  O    A VAL A 68  ? 0.2953 0.0393 0.0571 0.0524  -0.0439 0.0010  68  VAL A O    
686  O  O    B VAL A 68  ? 0.1998 0.0520 0.0764 0.0216  -0.0177 -0.0020 68  VAL A O    
687  C  CB   A VAL A 68  ? 0.1685 0.0674 0.1159 -0.0041 0.0120  0.0172  68  VAL A CB   
688  C  CB   B VAL A 68  ? 0.2845 0.1163 0.0615 0.0434  -0.0252 0.0000  68  VAL A CB   
689  C  CG1  A VAL A 68  ? 0.1097 0.0894 0.1256 -0.0489 -0.0104 0.0288  68  VAL A CG1  
690  C  CG1  B VAL A 68  ? 0.2648 0.1362 0.0807 0.0706  -0.0410 -0.0126 68  VAL A CG1  
691  C  CG2  A VAL A 68  ? 0.1990 0.0626 0.1179 -0.0483 0.0463  -0.0098 68  VAL A CG2  
692  C  CG2  B VAL A 68  ? 0.3000 0.1172 0.0581 0.0487  -0.0324 0.0093  68  VAL A CG2  
693  N  N    A GLU A 69  ? 0.0922 0.0398 0.0834 -0.0181 -0.0176 0.0137  69  GLU A N    
694  N  N    B GLU A 69  ? 0.2680 0.0608 0.0538 0.0465  -0.0013 0.0272  69  GLU A N    
695  C  CA   A GLU A 69  ? 0.1012 0.0703 0.0687 -0.0164 -0.0171 0.0156  69  GLU A CA   
696  C  CA   B GLU A 69  ? 0.2248 0.0807 0.0978 0.0379  0.0035  0.0447  69  GLU A CA   
697  C  C    A GLU A 69  ? 0.0715 0.0527 0.0529 -0.0104 0.0087  0.0214  69  GLU A C    
698  C  C    B GLU A 69  ? 0.1935 0.0983 0.0697 0.0249  -0.0239 0.0177  69  GLU A C    
699  O  O    A GLU A 69  ? 0.0869 0.0529 0.0921 -0.0065 -0.0109 0.0041  69  GLU A O    
700  O  O    B GLU A 69  ? 0.2813 0.1028 0.0741 0.0881  -0.0522 0.0183  69  GLU A O    
701  C  CB   A GLU A 69  ? 0.0476 0.0520 0.0868 -0.0161 -0.0291 0.0076  69  GLU A CB   
702  C  CB   B GLU A 69  ? 0.2361 0.1163 0.1619 0.0394  0.0439  0.0599  69  GLU A CB   
703  C  CG   A GLU A 69  ? 0.0763 0.0456 0.0706 -0.0023 -0.0006 0.0000  69  GLU A CG   
704  C  CG   B GLU A 69  ? 0.2366 0.1617 0.2461 0.0110  0.0159  0.0242  69  GLU A CG   
705  C  CD   A GLU A 69  ? 0.0890 0.0471 0.1124 -0.0015 -0.0006 0.0285  69  GLU A CD   
706  C  CD   B GLU A 69  ? 0.2928 0.2045 0.2416 0.0102  0.0043  0.0502  69  GLU A CD   
707  O  OE1  A GLU A 69  ? 0.1118 0.0782 0.0913 -0.0162 -0.0035 0.0091  69  GLU A OE1  
708  O  OE1  B GLU A 69  ? 0.3885 0.2912 0.3948 0.0524  -0.0258 0.0516  69  GLU A OE1  
709  O  OE2  A GLU A 69  ? 0.1150 0.0723 0.0958 -0.0088 -0.0043 0.0108  69  GLU A OE2  
710  O  OE2  B GLU A 69  ? 0.2890 0.2169 0.3203 0.0665  0.0675  0.0719  69  GLU A OE2  
711  N  N    A PHE A 70  ? 0.0900 0.0676 0.0645 -0.0010 -0.0062 0.0214  70  PHE A N    
712  N  N    B PHE A 70  ? 0.1520 0.0667 0.0733 -0.0093 -0.0076 0.0015  70  PHE A N    
713  C  CA   A PHE A 70  ? 0.0861 0.0318 0.0736 -0.0120 -0.0063 0.0142  70  PHE A CA   
714  C  CA   B PHE A 70  ? 0.1391 0.0879 0.0815 0.0082  -0.0175 0.0303  70  PHE A CA   
715  C  C    A PHE A 70  ? 0.0838 0.0658 0.0922 -0.0052 0.0003  0.0318  70  PHE A C    
716  C  C    B PHE A 70  ? 0.1344 0.0657 0.0748 -0.0027 -0.0098 0.0305  70  PHE A C    
717  O  O    A PHE A 70  ? 0.0935 0.0588 0.1045 -0.0012 -0.0052 0.0306  70  PHE A O    
718  O  O    B PHE A 70  ? 0.1267 0.0658 0.1089 -0.0217 -0.0209 0.0131  70  PHE A O    
719  C  CB   A PHE A 70  ? 0.0935 0.0467 0.0811 -0.0065 0.0137  0.0175  70  PHE A CB   
720  C  CB   B PHE A 70  ? 0.1026 0.0710 0.0951 0.0076  -0.0080 0.0063  70  PHE A CB   
721  C  CG   A PHE A 70  ? 0.0571 0.0476 0.0897 0.0087  0.0057  0.0085  70  PHE A CG   
722  C  CG   B PHE A 70  ? 0.1315 0.0741 0.0785 0.0306  -0.0040 0.0219  70  PHE A CG   
723  C  CD1  A PHE A 70  ? 0.0744 0.0563 0.0948 0.0103  0.0156  0.0065  70  PHE A CD1  
724  C  CD1  B PHE A 70  ? 0.1062 0.0599 0.1145 0.0147  -0.0252 0.0287  70  PHE A CD1  
725  C  CD2  A PHE A 70  ? 0.0807 0.0571 0.0921 0.0071  0.0000  -0.0097 70  PHE A CD2  
726  C  CD2  B PHE A 70  ? 0.1127 0.0833 0.1271 0.0244  -0.0353 0.0373  70  PHE A CD2  
727  C  CE1  A PHE A 70  ? 0.0709 0.0736 0.1114 0.0228  0.0118  0.0414  70  PHE A CE1  
728  C  CE1  B PHE A 70  ? 0.1229 0.0829 0.1023 0.0024  -0.0185 0.0193  70  PHE A CE1  
729  C  CE2  A PHE A 70  ? 0.0736 0.0753 0.1076 0.0109  -0.0012 0.0086  70  PHE A CE2  
730  C  CE2  B PHE A 70  ? 0.0906 0.0996 0.1145 0.0148  0.0070  0.0264  70  PHE A CE2  
731  C  CZ   A PHE A 70  ? 0.0881 0.0737 0.1274 0.0054  0.0175  -0.0013 70  PHE A CZ   
732  C  CZ   B PHE A 70  ? 0.1125 0.0818 0.1109 -0.0109 0.0065  0.0097  70  PHE A CZ   
733  N  N    A ASP A 71  ? 0.1263 0.0653 0.1199 0.0147  -0.0230 0.0237  71  ASP A N    
734  N  N    B ASP A 71  ? 0.1331 0.0754 0.1222 -0.0049 -0.0195 0.0211  71  ASP A N    
735  C  CA   A ASP A 71  ? 0.1606 0.0651 0.1500 0.0160  -0.0060 0.0333  71  ASP A CA   
736  C  CA   B ASP A 71  ? 0.1569 0.0662 0.1535 0.0060  -0.0137 0.0304  71  ASP A CA   
737  C  C    A ASP A 71  ? 0.1755 0.0442 0.1899 0.0156  -0.0103 0.0054  71  ASP A C    
738  C  C    B ASP A 71  ? 0.1784 0.0349 0.1789 0.0038  -0.0186 0.0205  71  ASP A C    
739  O  O    A ASP A 71  ? 0.2432 0.1107 0.1906 -0.0017 -0.0129 -0.0020 71  ASP A O    
740  O  O    B ASP A 71  ? 0.1967 0.1295 0.1508 0.0040  -0.0207 0.0241  71  ASP A O    
741  C  CB   A ASP A 71  ? 0.1807 0.0581 0.1572 0.0236  -0.0160 0.0560  71  ASP A CB   
742  C  CB   B ASP A 71  ? 0.1473 0.0794 0.1710 0.0114  -0.0182 0.0288  71  ASP A CB   
743  C  CG   A ASP A 71  ? 0.1944 0.0854 0.1992 0.0375  -0.0324 0.0226  71  ASP A CG   
744  C  CG   B ASP A 71  ? 0.2156 0.1096 0.1213 0.0381  -0.0331 0.0645  71  ASP A CG   
745  O  OD1  A ASP A 71  ? 0.2933 0.0701 0.2163 0.0222  -0.0250 0.0436  71  ASP A OD1  
746  O  OD1  B ASP A 71  ? 0.2425 0.0702 0.1350 0.0860  0.0100  0.0381  71  ASP A OD1  
747  O  OD2  A ASP A 71  ? 0.2497 0.1574 0.3104 0.0619  -0.0581 0.0065  71  ASP A OD2  
748  O  OD2  B ASP A 71  ? 0.3239 0.1190 0.2502 0.0236  -0.1084 0.0529  71  ASP A OD2  
749  N  N    . ASP A 72  ? 0.2010 0.0546 0.1823 0.0130  -0.0215 0.0093  72  ASP A N    
750  C  CA   . ASP A 72  ? 0.1924 0.0306 0.1926 -0.0035 0.0163  -0.0052 72  ASP A CA   
751  C  C    . ASP A 72  ? 0.2536 0.0606 0.1985 -0.0087 0.0346  0.0137  72  ASP A C    
752  O  O    . ASP A 72  ? 0.2962 0.0863 0.1799 -0.0137 0.0408  -0.0135 72  ASP A O    
753  C  CB   . ASP A 72  ? 0.2451 0.0703 0.1389 -0.0120 0.0012  0.0054  72  ASP A CB   
754  C  CG   . ASP A 72  ? 0.2255 0.1017 0.1283 0.0027  -0.0030 -0.0027 72  ASP A CG   
755  O  OD1  . ASP A 72  ? 0.2236 0.1420 0.1410 -0.0357 -0.0242 0.0310  72  ASP A OD1  
756  O  OD2  . ASP A 72  ? 0.2384 0.1392 0.1298 -0.0148 -0.0222 0.0043  72  ASP A OD2  
757  N  N    . SER A 73  ? 0.2481 0.0951 0.2287 -0.0035 0.0208  0.0104  73  SER A N    
758  C  CA   . SER A 73  ? 0.2682 0.1032 0.2565 -0.0037 0.0274  0.0043  73  SER A CA   
759  C  C    . SER A 73  ? 0.2583 0.1299 0.2387 -0.0093 0.0324  -0.0148 73  SER A C    
760  O  O    . SER A 73  ? 0.2802 0.1102 0.2380 0.0093  0.0007  0.0082  73  SER A O    
761  C  CB   . SER A 73  ? 0.3023 0.0733 0.2811 -0.0099 0.0177  0.0399  73  SER A CB   
762  O  OG   . SER A 73  ? 0.3240 0.0658 0.2404 0.0275  0.0373  0.0546  73  SER A OG   
763  N  N    . GLN A 74  ? 0.2179 0.0349 0.2373 0.0030  0.0260  -0.0015 74  GLN A N    
764  C  CA   . GLN A 74  ? 0.2317 0.0913 0.2463 -0.0129 0.0071  0.0232  74  GLN A CA   
765  C  C    . GLN A 74  ? 0.2317 0.1240 0.2418 0.0104  0.0146  -0.0020 74  GLN A C    
766  O  O    . GLN A 74  ? 0.2169 0.0790 0.2245 -0.0120 0.0177  -0.0496 74  GLN A O    
767  C  CB   . GLN A 74  ? 0.1887 0.0915 0.2407 0.0115  0.0051  0.0219  74  GLN A CB   
768  C  CG   . GLN A 74  ? 0.2280 0.1296 0.2352 0.0081  0.0060  0.0825  74  GLN A CG   
769  C  CD   . GLN A 74  ? 0.2639 0.1712 0.2612 -0.0057 -0.0153 0.0142  74  GLN A CD   
770  O  OE1  . GLN A 74  ? 0.3188 0.3858 0.3549 0.0049  0.0171  0.0306  74  GLN A OE1  
771  N  NE2  . GLN A 74  ? 0.3402 0.2626 0.2657 -0.0175 0.0087  0.0093  74  GLN A NE2  
772  N  N    A ASP A 75  ? 0.2662 0.1849 0.2759 -0.0161 0.0132  -0.0104 75  ASP A N    
773  N  N    B ASP A 75  ? 0.1993 0.0940 0.2011 0.0074  -0.0329 0.0166  75  ASP A N    
774  C  CA   A ASP A 75  ? 0.2628 0.2045 0.2657 -0.0068 -0.0041 0.0020  75  ASP A CA   
775  C  CA   B ASP A 75  ? 0.1933 0.0511 0.1752 0.0038  -0.0399 0.0040  75  ASP A CA   
776  C  C    A ASP A 75  ? 0.2502 0.2240 0.2560 0.0012  -0.0049 0.0076  75  ASP A C    
777  C  C    B ASP A 75  ? 0.2120 0.1276 0.2239 -0.0046 -0.0575 -0.0006 75  ASP A C    
778  O  O    A ASP A 75  ? 0.2439 0.1732 0.1870 -0.0038 0.0294  0.0586  75  ASP A O    
779  O  O    B ASP A 75  ? 0.2574 0.2037 0.2422 0.0384  -0.0821 0.0197  75  ASP A O    
780  C  CB   A ASP A 75  ? 0.2793 0.2639 0.2870 -0.0003 0.0051  -0.0065 75  ASP A CB   
781  C  CB   B ASP A 75  ? 0.1841 0.0536 0.1972 0.0057  -0.0309 0.0115  75  ASP A CB   
782  C  CG   A ASP A 75  ? 0.3576 0.3147 0.3215 0.0010  -0.0065 0.0109  75  ASP A CG   
783  C  CG   B ASP A 75  ? 0.1689 0.1224 0.2095 0.0274  -0.0024 0.0208  75  ASP A CG   
784  O  OD1  A ASP A 75  ? 0.3948 0.3325 0.4318 0.0241  -0.0030 0.0153  75  ASP A OD1  
785  O  OD1  B ASP A 75  ? 0.1280 0.1604 0.2635 -0.0156 -0.0136 0.0842  75  ASP A OD1  
786  O  OD2  A ASP A 75  ? 0.4499 0.4092 0.3919 0.0010  0.0098  -0.0353 75  ASP A OD2  
787  O  OD2  B ASP A 75  ? 0.2434 0.1762 0.2488 0.0263  0.0529  0.0071  75  ASP A OD2  
788  N  N    A LYS A 76  ? 0.2495 0.1878 0.2506 -0.0184 -0.0291 0.0222  76  LYS A N    
789  N  N    B LYS A 76  ? 0.2120 0.0820 0.1800 -0.0041 -0.0658 0.0401  76  LYS A N    
790  C  CA   A LYS A 76  ? 0.2587 0.1820 0.2581 0.0000  -0.0230 0.0197  76  LYS A CA   
791  C  CA   B LYS A 76  ? 0.2059 0.0696 0.1867 -0.0088 -0.0463 0.0043  76  LYS A CA   
792  C  C    A LYS A 76  ? 0.2639 0.1658 0.2976 -0.0006 -0.0182 0.0260  76  LYS A C    
793  C  C    B LYS A 76  ? 0.1500 0.0845 0.1676 -0.0177 -0.0627 -0.0031 76  LYS A C    
794  O  O    A LYS A 76  ? 0.3239 0.2141 0.3312 0.0195  -0.0109 0.0124  76  LYS A O    
795  O  O    B LYS A 76  ? 0.1703 0.1040 0.1556 -0.0177 -0.0351 -0.0071 76  LYS A O    
796  C  CB   A LYS A 76  ? 0.2497 0.1924 0.2642 -0.0048 -0.0324 0.0368  76  LYS A CB   
797  C  CB   B LYS A 76  ? 0.1935 0.0754 0.1856 -0.0273 -0.0370 0.0070  76  LYS A CB   
798  C  CG   A LYS A 76  ? 0.2644 0.1886 0.2486 0.0087  -0.0351 0.0197  76  LYS A CG   
799  C  CG   B LYS A 76  ? 0.2716 0.1865 0.1671 -0.0176 -0.0291 0.0102  76  LYS A CG   
800  C  CD   A LYS A 76  ? 0.2612 0.1818 0.2517 -0.0241 -0.0142 0.0228  76  LYS A CD   
801  C  CD   B LYS A 76  ? 0.2705 0.1380 0.1883 0.0046  -0.0482 -0.0019 76  LYS A CD   
802  C  CE   A LYS A 76  ? 0.2885 0.1793 0.2407 0.0272  -0.0588 0.0005  76  LYS A CE   
803  C  CE   B LYS A 76  ? 0.3305 0.1931 0.1847 -0.0114 -0.0109 0.0463  76  LYS A CE   
804  N  NZ   A LYS A 76  ? 0.3210 0.1732 0.2161 -0.0115 -0.0832 -0.0020 76  LYS A NZ   
805  N  NZ   B LYS A 76  ? 0.4120 0.2064 0.1714 -0.0324 -0.0350 0.0175  76  LYS A NZ   
806  N  N    A ALA A 77  ? 0.2202 0.1502 0.2626 0.0027  -0.0394 0.0121  77  ALA A N    
807  N  N    B ALA A 77  ? 0.1423 0.1057 0.1728 0.0043  -0.0471 0.0110  77  ALA A N    
808  C  CA   A ALA A 77  ? 0.2008 0.1529 0.2213 -0.0048 -0.0603 0.0102  77  ALA A CA   
809  C  CA   B ALA A 77  ? 0.1748 0.0957 0.1772 0.0108  -0.0631 0.0005  77  ALA A CA   
810  C  C    A ALA A 77  ? 0.1617 0.1263 0.2088 -0.0208 -0.0687 0.0160  77  ALA A C    
811  C  C    B ALA A 77  ? 0.1535 0.0930 0.1836 0.0000  -0.0577 -0.0017 77  ALA A C    
812  O  O    A ALA A 77  ? 0.1610 0.1689 0.2287 -0.0307 -0.0630 0.0724  77  ALA A O    
813  O  O    B ALA A 77  ? 0.1418 0.1268 0.1658 0.0324  -0.0439 -0.0228 77  ALA A O    
814  C  CB   A ALA A 77  ? 0.1937 0.1520 0.2061 -0.0238 -0.0465 -0.0113 77  ALA A CB   
815  C  CB   B ALA A 77  ? 0.2026 0.1136 0.1368 -0.0285 -0.0719 0.0043  77  ALA A CB   
816  N  N    . VAL A 78  ? 0.1558 0.1048 0.1923 0.0000  -0.0670 0.0120  78  VAL A N    
817  C  CA   . VAL A 78  ? 0.1901 0.0877 0.1883 -0.0098 -0.0604 0.0005  78  VAL A CA   
818  C  C    . VAL A 78  ? 0.1344 0.0881 0.1780 -0.0098 -0.0275 0.0031  78  VAL A C    
819  O  O    . VAL A 78  ? 0.1488 0.1184 0.2195 -0.0241 -0.0625 0.0210  78  VAL A O    
820  C  CB   . VAL A 78  ? 0.2560 0.0917 0.2129 -0.0103 -0.0601 0.0060  78  VAL A CB   
821  C  CG1  . VAL A 78  ? 0.2409 0.1630 0.2440 -0.0211 0.0379  -0.0443 78  VAL A CG1  
822  C  CG2  . VAL A 78  ? 0.3456 0.0816 0.2802 0.0024  -0.0397 0.0326  78  VAL A CG2  
823  N  N    . LEU A 79  ? 0.1154 0.0915 0.1535 -0.0120 -0.0285 -0.0131 79  LEU A N    
824  C  CA   . LEU A 79  ? 0.1125 0.1163 0.1568 -0.0076 -0.0161 -0.0052 79  LEU A CA   
825  C  C    . LEU A 79  ? 0.1430 0.0863 0.1276 -0.0109 -0.0175 -0.0230 79  LEU A C    
826  O  O    . LEU A 79  ? 0.1418 0.1136 0.1493 -0.0167 0.0091  -0.0207 79  LEU A O    
827  C  CB   . LEU A 79  ? 0.1389 0.1161 0.1470 -0.0120 -0.0146 -0.0057 79  LEU A CB   
828  C  CG   . LEU A 79  ? 0.1576 0.1114 0.1409 -0.0005 -0.0093 0.0104  79  LEU A CG   
829  C  CD1  . LEU A 79  ? 0.1603 0.1436 0.2917 -0.0281 0.0062  0.0750  79  LEU A CD1  
830  C  CD2  . LEU A 79  ? 0.1358 0.1283 0.1531 0.0377  -0.0027 0.0027  79  LEU A CD2  
831  N  N    . LYS A 80  ? 0.1342 0.1176 0.1396 -0.0152 0.0193  -0.0126 80  LYS A N    
832  C  CA   . LYS A 80  ? 0.1464 0.1154 0.1732 -0.0216 0.0098  -0.0129 80  LYS A CA   
833  C  C    . LYS A 80  ? 0.1349 0.1303 0.1696 0.0031  0.0166  -0.0208 80  LYS A C    
834  O  O    . LYS A 80  ? 0.1177 0.1216 0.1983 -0.0076 -0.0073 -0.0031 80  LYS A O    
835  C  CB   . LYS A 80  ? 0.1883 0.1342 0.1694 0.0153  -0.0091 0.0076  80  LYS A CB   
836  C  CG   . LYS A 80  ? 0.1687 0.1199 0.2381 0.0252  0.0135  0.0219  80  LYS A CG   
837  C  CD   . LYS A 80  ? 0.2014 0.2055 0.2705 0.0288  0.0098  -0.0065 80  LYS A CD   
838  C  CE   . LYS A 80  ? 0.2397 0.2346 0.3680 0.0671  0.0210  0.0196  80  LYS A CE   
839  N  NZ   . LYS A 80  ? 0.3770 0.4032 0.4061 0.0601  0.0465  0.0068  80  LYS A NZ   
840  N  N    . GLY A 81  ? 0.1335 0.1220 0.1965 0.0026  0.0082  -0.0026 81  GLY A N    
841  C  CA   . GLY A 81  ? 0.1509 0.1421 0.2000 0.0027  0.0359  0.0091  81  GLY A CA   
842  C  C    . GLY A 81  ? 0.1475 0.1274 0.1972 0.0253  0.0423  0.0175  81  GLY A C    
843  O  O    . GLY A 81  ? 0.1378 0.1279 0.1789 -0.0162 0.0240  -0.0197 81  GLY A O    
844  N  N    . GLY A 82  ? 0.1371 0.1662 0.2879 -0.0054 0.0410  0.0346  82  GLY A N    
845  C  CA   . GLY A 82  ? 0.1500 0.1506 0.2721 0.0135  0.0154  0.0211  82  GLY A CA   
846  C  C    . GLY A 82  ? 0.1895 0.1658 0.2125 0.0333  0.0482  0.0243  82  GLY A C    
847  O  O    . GLY A 82  ? 0.2254 0.2333 0.2140 0.0586  0.0527  0.0350  82  GLY A O    
848  N  N    . PRO A 83  ? 0.1570 0.1286 0.2154 0.0237  0.0210  0.0080  83  PRO A N    
849  C  CA   . PRO A 83  ? 0.1856 0.1161 0.1798 0.0362  0.0183  0.0085  83  PRO A CA   
850  C  C    . PRO A 83  ? 0.1754 0.1502 0.1493 0.0353  -0.0052 -0.0194 83  PRO A C    
851  O  O    . PRO A 83  ? 0.1948 0.1710 0.1599 0.0249  -0.0164 -0.0024 83  PRO A O    
852  C  CB   . PRO A 83  ? 0.1650 0.1330 0.1671 0.0286  -0.0003 -0.0164 83  PRO A CB   
853  C  CG   . PRO A 83  ? 0.1526 0.1067 0.1755 0.0417  0.0108  0.0085  83  PRO A CG   
854  C  CD   . PRO A 83  ? 0.1619 0.0953 0.2161 0.0298  0.0421  -0.0098 83  PRO A CD   
855  N  N    . LEU A 84  ? 0.1407 0.1032 0.1393 0.0119  0.0162  -0.0161 84  LEU A N    
856  C  CA   . LEU A 84  ? 0.1633 0.1096 0.1459 0.0324  -0.0048 -0.0410 84  LEU A CA   
857  C  C    . LEU A 84  ? 0.1639 0.1071 0.1743 0.0472  -0.0062 -0.0487 84  LEU A C    
858  O  O    . LEU A 84  ? 0.1901 0.1439 0.2102 0.0427  0.0414  -0.0706 84  LEU A O    
859  C  CB   . LEU A 84  ? 0.1374 0.0865 0.1471 0.0230  0.0214  -0.0193 84  LEU A CB   
860  C  CG   . LEU A 84  ? 0.1084 0.0714 0.1448 0.0114  0.0261  -0.0142 84  LEU A CG   
861  C  CD1  . LEU A 84  ? 0.1414 0.1120 0.1290 0.0296  -0.0003 -0.0324 84  LEU A CD1  
862  C  CD2  . LEU A 84  ? 0.1333 0.0845 0.1674 0.0108  0.0253  -0.0178 84  LEU A CD2  
863  N  N    A ASP A 85  ? 0.1793 0.1351 0.1799 0.0013  -0.0232 -0.0612 85  ASP A N    
864  N  N    B ASP A 85  ? 0.1870 0.1134 0.1694 0.0430  -0.0085 -0.0353 85  ASP A N    
865  C  CA   A ASP A 85  ? 0.1748 0.1332 0.1789 0.0068  -0.0164 -0.0790 85  ASP A CA   
866  C  CA   B ASP A 85  ? 0.1890 0.1472 0.1861 0.0162  -0.0203 -0.0207 85  ASP A CA   
867  C  C    A ASP A 85  ? 0.1382 0.0965 0.2107 0.0107  -0.0324 -0.0386 85  ASP A C    
868  C  C    B ASP A 85  ? 0.2007 0.1330 0.2148 -0.0182 -0.0148 -0.0230 85  ASP A C    
869  O  O    A ASP A 85  ? 0.2020 0.1550 0.1428 0.0023  0.0076  -0.0626 85  ASP A O    
870  O  O    B ASP A 85  ? 0.2301 0.2303 0.2531 -0.0109 0.0163  -0.0394 85  ASP A O    
871  C  CB   A ASP A 85  ? 0.1931 0.1541 0.2129 0.0110  -0.0195 -0.0617 85  ASP A CB   
872  C  CB   B ASP A 85  ? 0.2147 0.0781 0.1876 0.0496  -0.0297 -0.0177 85  ASP A CB   
873  C  CG   A ASP A 85  ? 0.2384 0.1721 0.2425 -0.0109 -0.0062 -0.0104 85  ASP A CG   
874  C  CG   B ASP A 85  ? 0.1996 0.2021 0.2240 0.0031  0.0107  0.0193  85  ASP A CG   
875  O  OD1  A ASP A 85  ? 0.2933 0.3413 0.3161 -0.0181 -0.0474 -0.0299 85  ASP A OD1  
876  O  OD1  B ASP A 85  ? 0.2012 0.2418 0.1554 -0.0287 -0.0104 0.0326  85  ASP A OD1  
877  O  OD2  A ASP A 85  ? 0.3761 0.3486 0.3490 -0.0153 -0.0878 -0.0177 85  ASP A OD2  
878  O  OD2  B ASP A 85  ? 0.2500 0.2673 0.2773 0.0026  -0.0526 0.0109  85  ASP A OD2  
879  N  N    A GLY A 86  ? 0.1845 0.0860 0.2096 0.0364  0.0000  -0.0250 86  GLY A N    
880  N  N    B GLY A 86  ? 0.1872 0.1653 0.2122 -0.0419 0.0077  -0.0154 86  GLY A N    
881  C  CA   A GLY A 86  ? 0.1752 0.0744 0.1924 0.0483  -0.0024 -0.0085 86  GLY A CA   
882  C  CA   B GLY A 86  ? 0.2075 0.1136 0.1772 -0.0362 0.0185  -0.0148 86  GLY A CA   
883  C  C    A GLY A 86  ? 0.1897 0.0768 0.1991 0.0299  0.0104  -0.0137 86  GLY A C    
884  C  C    B GLY A 86  ? 0.1791 0.1368 0.1800 -0.0074 0.0037  -0.0167 86  GLY A C    
885  O  O    A GLY A 86  ? 0.1484 0.1283 0.2008 -0.0110 0.0258  0.0093  86  GLY A O    
886  O  O    B GLY A 86  ? 0.1958 0.1441 0.2183 0.0124  0.0357  -0.0260 86  GLY A O    
887  N  N    A THR A 87  ? 0.1741 0.0660 0.1935 0.0324  -0.0038 -0.0329 87  THR A N    
888  N  N    B THR A 87  ? 0.1680 0.0861 0.1809 -0.0035 0.0244  -0.0170 87  THR A N    
889  C  CA   A THR A 87  ? 0.1608 0.0759 0.1881 0.0087  0.0041  -0.0197 87  THR A CA   
890  C  CA   B THR A 87  ? 0.1407 0.0920 0.1620 0.0092  0.0142  -0.0076 87  THR A CA   
891  C  C    A THR A 87  ? 0.1224 0.0728 0.1641 0.0197  0.0043  -0.0109 87  THR A C    
892  C  C    B THR A 87  ? 0.1186 0.0851 0.1678 0.0152  0.0030  -0.0282 87  THR A C    
893  O  O    A THR A 87  ? 0.1199 0.0829 0.1365 0.0046  0.0225  0.0010  87  THR A O    
894  O  O    B THR A 87  ? 0.1542 0.0555 0.1850 0.0275  -0.0182 -0.0186 87  THR A O    
895  C  CB   A THR A 87  ? 0.1615 0.1454 0.2142 0.0359  0.0013  -0.0291 87  THR A CB   
896  C  CB   B THR A 87  ? 0.1075 0.1132 0.1756 0.0026  0.0087  -0.0237 87  THR A CB   
897  O  OG1  A THR A 87  ? 0.1815 0.1953 0.2982 0.0544  0.0082  -0.0430 87  THR A OG1  
898  O  OG1  B THR A 87  ? 0.1432 0.0554 0.1668 0.0060  0.0041  0.0038  87  THR A OG1  
899  C  CG2  A THR A 87  ? 0.1823 0.1473 0.2551 0.0262  -0.0304 -0.0205 87  THR A CG2  
900  C  CG2  B THR A 87  ? 0.1432 0.1230 0.1605 0.0115  0.0401  0.0198  87  THR A CG2  
901  N  N    . TYR A 88  ? 0.1066 0.0733 0.1545 0.0071  -0.0159 -0.0177 88  TYR A N    
902  C  CA   . TYR A 88  ? 0.1107 0.0768 0.1161 0.0000  -0.0088 -0.0342 88  TYR A CA   
903  C  C    . TYR A 88  ? 0.1143 0.0829 0.1371 0.0093  -0.0241 -0.0164 88  TYR A C    
904  O  O    . TYR A 88  ? 0.1428 0.1457 0.1872 -0.0430 -0.0595 0.0252  88  TYR A O    
905  C  CB   . TYR A 88  ? 0.1075 0.0458 0.1498 0.0104  0.0019  -0.0197 88  TYR A CB   
906  C  CG   . TYR A 88  ? 0.1177 0.0504 0.1134 0.0017  0.0074  -0.0249 88  TYR A CG   
907  C  CD1  . TYR A 88  ? 0.1082 0.0861 0.1249 0.0186  -0.0007 0.0035  88  TYR A CD1  
908  C  CD2  . TYR A 88  ? 0.1161 0.0353 0.1145 0.0200  0.0074  -0.0082 88  TYR A CD2  
909  C  CE1  . TYR A 88  ? 0.1249 0.0926 0.1237 0.0249  0.0087  -0.0229 88  TYR A CE1  
910  C  CE2  . TYR A 88  ? 0.1105 0.0480 0.1084 0.0062  0.0062  -0.0076 88  TYR A CE2  
911  C  CZ   . TYR A 88  ? 0.1055 0.0450 0.1261 0.0099  -0.0068 -0.0178 88  TYR A CZ   
912  O  OH   . TYR A 88  ? 0.1230 0.0569 0.1136 0.0065  -0.0104 -0.0119 88  TYR A OH   
913  N  N    . ARG A 89  ? 0.1057 0.0645 0.1251 0.0181  -0.0162 -0.0262 89  ARG A N    
914  C  CA   . ARG A 89  ? 0.1599 0.0548 0.1262 0.0164  -0.0210 0.0057  89  ARG A CA   
915  C  C    . ARG A 89  ? 0.1362 0.0471 0.0988 -0.0023 -0.0209 0.0176  89  ARG A C    
916  O  O    . ARG A 89  ? 0.1326 0.0458 0.0881 -0.0020 -0.0219 0.0030  89  ARG A O    
917  C  CB   . ARG A 89  ? 0.1940 0.0465 0.1543 0.0005  -0.0305 0.0131  89  ARG A CB   
918  C  CG   . ARG A 89  ? 0.2177 0.0759 0.1217 -0.0093 -0.0255 -0.0080 89  ARG A CG   
919  C  CD   . ARG A 89  ? 0.2221 0.0809 0.1660 0.0120  -0.0062 0.0065  89  ARG A CD   
920  N  NE   . ARG A 89  ? 0.2449 0.0872 0.1551 0.0057  -0.0070 0.0379  89  ARG A NE   
921  C  CZ   . ARG A 89  ? 0.1975 0.0696 0.1454 -0.0098 0.0035  0.0046  89  ARG A CZ   
922  N  NH1  . ARG A 89  ? 0.2132 0.1125 0.1985 0.0177  0.0276  0.0428  89  ARG A NH1  
923  N  NH2  . ARG A 89  ? 0.2515 0.0757 0.1729 0.0208  -0.0006 0.0219  89  ARG A NH2  
924  N  N    A LEU A 90  ? 0.1062 0.0385 0.0886 -0.0065 -0.0164 0.0162  90  LEU A N    
925  N  N    B LEU A 90  ? 0.1316 0.0599 0.0931 0.0060  -0.0423 0.0027  90  LEU A N    
926  C  CA   A LEU A 90  ? 0.1152 0.0516 0.0803 -0.0121 -0.0063 0.0115  90  LEU A CA   
927  C  CA   B LEU A 90  ? 0.1224 0.0450 0.0829 -0.0131 -0.0238 0.0003  90  LEU A CA   
928  C  C    A LEU A 90  ? 0.1017 0.0676 0.0791 0.0154  -0.0038 -0.0013 90  LEU A C    
929  C  C    B LEU A 90  ? 0.1299 0.0342 0.0864 -0.0141 -0.0274 -0.0060 90  LEU A C    
930  O  O    A LEU A 90  ? 0.1082 0.0476 0.0791 0.0170  0.0041  0.0131  90  LEU A O    
931  O  O    B LEU A 90  ? 0.1601 0.0861 0.0913 0.0241  -0.0228 0.0317  90  LEU A O    
932  C  CB   A LEU A 90  ? 0.1123 0.0493 0.0688 0.0065  -0.0060 -0.0010 90  LEU A CB   
933  C  CB   B LEU A 90  ? 0.1036 0.0876 0.0645 -0.0006 -0.0236 -0.0003 90  LEU A CB   
934  C  CG   A LEU A 90  ? 0.1134 0.0732 0.0777 -0.0081 0.0030  -0.0068 90  LEU A CG   
935  C  CG   B LEU A 90  ? 0.0870 0.0485 0.0863 -0.0178 -0.0255 0.0043  90  LEU A CG   
936  C  CD1  A LEU A 90  ? 0.0847 0.0626 0.1107 -0.0071 -0.0097 -0.0423 90  LEU A CD1  
937  C  CD1  B LEU A 90  ? 0.1344 0.0495 0.1123 0.0421  0.0115  0.0302  90  LEU A CD1  
938  C  CD2  A LEU A 90  ? 0.0894 0.1014 0.1181 -0.0153 -0.0232 -0.0531 90  LEU A CD2  
939  C  CD2  B LEU A 90  ? 0.1032 0.0692 0.1114 0.0109  -0.0430 -0.0076 90  LEU A CD2  
940  N  N    A ILE A 91  ? 0.1091 0.0436 0.0615 0.0030  0.0000  0.0126  91  ILE A N    
941  N  N    B ILE A 91  ? 0.1276 0.0361 0.0845 0.0006  -0.0253 0.0114  91  ILE A N    
942  C  CA   A ILE A 91  ? 0.0994 0.0412 0.0636 0.0023  -0.0098 -0.0035 91  ILE A CA   
943  C  CA   B ILE A 91  ? 0.1199 0.0379 0.0836 -0.0024 -0.0140 0.0192  91  ILE A CA   
944  C  C    A ILE A 91  ? 0.1029 0.0264 0.0713 -0.0007 -0.0095 0.0069  91  ILE A C    
945  C  C    B ILE A 91  ? 0.1340 0.0414 0.0861 0.0049  -0.0199 0.0282  91  ILE A C    
946  O  O    A ILE A 91  ? 0.1268 0.0256 0.0662 -0.0031 0.0041  0.0023  91  ILE A O    
947  O  O    B ILE A 91  ? 0.1411 0.0561 0.0881 -0.0060 -0.0248 0.0175  91  ILE A O    
948  C  CB   A ILE A 91  ? 0.1039 0.0498 0.0608 0.0038  -0.0193 0.0026  91  ILE A CB   
949  C  CB   B ILE A 91  ? 0.1208 0.0283 0.0908 -0.0065 -0.0093 0.0062  91  ILE A CB   
950  C  CG1  A ILE A 91  ? 0.0912 0.0480 0.0764 0.0010  -0.0093 -0.0049 91  ILE A CG1  
951  C  CG1  B ILE A 91  ? 0.1064 0.0900 0.1089 -0.0068 0.0054  0.0087  91  ILE A CG1  
952  C  CG2  A ILE A 91  ? 0.0915 0.0326 0.1111 -0.0046 -0.0087 -0.0236 91  ILE A CG2  
953  C  CG2  B ILE A 91  ? 0.1215 0.0688 0.0802 -0.0082 -0.0199 0.0284  91  ILE A CG2  
954  C  CD1  A ILE A 91  ? 0.0900 0.0991 0.0949 -0.0164 -0.0013 0.0082  91  ILE A CD1  
955  C  CD1  B ILE A 91  ? 0.1177 0.0888 0.1500 -0.0063 0.0054  -0.0280 91  ILE A CD1  
956  N  N    A GLN A 92  ? 0.1161 0.0459 0.0784 0.0060  -0.0054 0.0005  92  GLN A N    
957  N  N    B GLN A 92  ? 0.1225 0.0423 0.0551 -0.0060 -0.0260 0.0186  92  GLN A N    
958  C  CA   A GLN A 92  ? 0.1221 0.0471 0.0486 0.0091  -0.0015 -0.0051 92  GLN A CA   
959  C  CA   B GLN A 92  ? 0.1265 0.0292 0.0644 -0.0013 -0.0092 0.0057  92  GLN A CA   
960  C  C    A GLN A 92  ? 0.1215 0.0410 0.0449 0.0120  -0.0065 -0.0059 92  GLN A C    
961  C  C    B GLN A 92  ? 0.1520 0.0439 0.0633 -0.0065 -0.0174 0.0220  92  GLN A C    
962  O  O    A GLN A 92  ? 0.1134 0.0300 0.0684 0.0035  -0.0119 -0.0054 92  GLN A O    
963  O  O    B GLN A 92  ? 0.1277 0.0403 0.0662 -0.0148 -0.0048 0.0077  92  GLN A O    
964  C  CB   A GLN A 92  ? 0.1143 0.0271 0.1114 0.0063  -0.0251 0.0082  92  GLN A CB   
965  C  CB   B GLN A 92  ? 0.1369 0.0421 0.0806 0.0035  0.0087  0.0181  92  GLN A CB   
966  C  CG   A GLN A 92  ? 0.0922 0.0554 0.1055 0.0110  -0.0328 -0.0113 92  GLN A CG   
967  C  CG   B GLN A 92  ? 0.1393 0.0561 0.1005 0.0115  -0.0236 0.0043  92  GLN A CG   
968  C  CD   A GLN A 92  ? 0.1215 0.0500 0.0781 0.0193  0.0085  -0.0023 92  GLN A CD   
969  C  CD   B GLN A 92  ? 0.1430 0.0684 0.0868 -0.0023 0.0099  0.0242  92  GLN A CD   
970  O  OE1  A GLN A 92  ? 0.1642 0.0309 0.0888 -0.0035 0.0023  -0.0010 92  GLN A OE1  
971  O  OE1  B GLN A 92  ? 0.1513 0.0370 0.1186 0.0104  -0.0120 0.0196  92  GLN A OE1  
972  N  NE2  A GLN A 92  ? 0.1351 0.0572 0.1856 -0.0024 0.0080  0.0174  92  GLN A NE2  
973  N  NE2  B GLN A 92  ? 0.1333 0.1128 0.1538 0.0007  0.0421  -0.0151 92  GLN A NE2  
974  N  N    A PHE A 93  ? 0.1624 0.0388 0.0468 0.0087  -0.0119 0.0040  93  PHE A N    
975  N  N    B PHE A 93  ? 0.2064 0.0459 0.0539 -0.0115 -0.0324 0.0233  93  PHE A N    
976  C  CA   A PHE A 93  ? 0.1886 0.0353 0.0474 -0.0127 -0.0167 0.0148  93  PHE A CA   
977  C  CA   B PHE A 93  ? 0.1711 0.0351 0.0557 0.0049  -0.0216 0.0153  93  PHE A CA   
978  C  C    A PHE A 93  ? 0.1850 0.0318 0.0476 -0.0130 -0.0357 0.0043  93  PHE A C    
979  C  C    B PHE A 93  ? 0.1668 0.0590 0.0447 -0.0003 -0.0329 0.0171  93  PHE A C    
980  O  O    A PHE A 93  ? 0.2233 0.0410 0.0370 -0.0030 -0.0307 0.0006  93  PHE A O    
981  O  O    B PHE A 93  ? 0.1813 0.0362 0.0868 -0.0035 -0.0186 0.0167  93  PHE A O    
982  C  CB   A PHE A 93  ? 0.1678 0.0414 0.0511 0.0281  -0.0198 -0.0027 93  PHE A CB   
983  C  CB   B PHE A 93  ? 0.1404 0.0495 0.0642 -0.0071 -0.0164 0.0073  93  PHE A CB   
984  C  CG   A PHE A 93  ? 0.1791 0.0306 0.0392 0.0076  -0.0198 0.0046  93  PHE A CG   
985  C  CG   B PHE A 93  ? 0.1107 0.0379 0.0873 -0.0186 0.0057  -0.0048 93  PHE A CG   
986  C  CD1  A PHE A 93  ? 0.1216 0.0315 0.0617 0.0051  -0.0031 0.0143  93  PHE A CD1  
987  C  CD1  B PHE A 93  ? 0.0953 0.0450 0.0703 0.0000  0.0164  0.0129  93  PHE A CD1  
988  C  CD2  A PHE A 93  ? 0.1572 0.0349 0.0710 -0.0037 -0.0263 0.0118  93  PHE A CD2  
989  C  CD2  B PHE A 93  ? 0.0882 0.0545 0.0737 -0.0035 -0.0010 0.0183  93  PHE A CD2  
990  C  CE1  A PHE A 93  ? 0.1577 0.0467 0.0703 0.0178  -0.0265 0.0093  93  PHE A CE1  
991  C  CE1  B PHE A 93  ? 0.1066 0.0579 0.0562 -0.0093 0.0131  -0.0103 93  PHE A CE1  
992  C  CE2  A PHE A 93  ? 0.1615 0.0516 0.0318 -0.0185 -0.0065 0.0000  93  PHE A CE2  
993  C  CE2  B PHE A 93  ? 0.0872 0.0551 0.0649 -0.0041 0.0077  0.0143  93  PHE A CE2  
994  C  CZ   A PHE A 93  ? 0.1464 0.0590 0.0370 -0.0297 -0.0040 0.0017  93  PHE A CZ   
995  C  CZ   B PHE A 93  ? 0.0827 0.0383 0.0688 -0.0177 0.0013  0.0119  93  PHE A CZ   
996  N  N    . HIS A 94  ? 0.1921 0.0414 0.0493 -0.0057 -0.0167 0.0003  94  HIS A N    
997  C  CA   . HIS A 94  ? 0.1825 0.0428 0.0388 -0.0081 -0.0160 -0.0003 94  HIS A CA   
998  C  C    . HIS A 94  ? 0.1615 0.0414 0.0432 -0.0181 -0.0115 -0.0076 94  HIS A C    
999  O  O    . HIS A 94  ? 0.1650 0.0362 0.0640 0.0010  -0.0153 0.0000  94  HIS A O    
1000 C  CB   . HIS A 94  ? 0.1834 0.0424 0.0662 -0.0076 -0.0005 0.0182  94  HIS A CB   
1001 C  CG   . HIS A 94  ? 0.1617 0.0439 0.0319 -0.0046 0.0000  0.0085  94  HIS A CG   
1002 N  ND1  . HIS A 94  ? 0.1680 0.0412 0.0491 -0.0104 -0.0057 0.0003  94  HIS A ND1  
1003 C  CD2  . HIS A 94  ? 0.1490 0.0615 0.0357 -0.0230 -0.0115 -0.0148 94  HIS A CD2  
1004 C  CE1  . HIS A 94  ? 0.1395 0.0285 0.0697 -0.0062 -0.0071 0.0115  94  HIS A CE1  
1005 N  NE2  . HIS A 94  ? 0.1228 0.0459 0.0577 -0.0108 -0.0030 0.0108  94  HIS A NE2  
1006 N  N    . PHE A 95  ? 0.1696 0.0458 0.0450 -0.0198 0.0027  0.0046  95  PHE A N    
1007 C  CA   . PHE A 95  ? 0.1509 0.0349 0.0401 -0.0099 0.0010  0.0110  95  PHE A CA   
1008 C  C    . PHE A 95  ? 0.1468 0.0384 0.0525 -0.0073 0.0020  -0.0082 95  PHE A C    
1009 O  O    . PHE A 95  ? 0.1454 0.0529 0.0806 -0.0148 0.0015  0.0082  95  PHE A O    
1010 C  CB   . PHE A 95  ? 0.1606 0.0491 0.0574 -0.0013 -0.0230 -0.0015 95  PHE A CB   
1011 C  CG   . PHE A 95  ? 0.1703 0.0271 0.0633 -0.0086 -0.0247 -0.0051 95  PHE A CG   
1012 C  CD1  . PHE A 95  ? 0.1572 0.0482 0.0687 -0.0230 -0.0250 -0.0051 95  PHE A CD1  
1013 C  CD2  . PHE A 95  ? 0.1468 0.0644 0.0833 0.0013  -0.0203 0.0007  95  PHE A CD2  
1014 C  CE1  . PHE A 95  ? 0.1723 0.0688 0.0845 -0.0152 -0.0126 -0.0320 95  PHE A CE1  
1015 C  CE2  . PHE A 95  ? 0.1972 0.0499 0.0633 -0.0073 -0.0189 -0.0041 95  PHE A CE2  
1016 C  CZ   . PHE A 95  ? 0.1671 0.0553 0.0865 0.0151  -0.0392 -0.0241 95  PHE A CZ   
1017 N  N    . HIS A 96  ? 0.1305 0.0361 0.0581 -0.0060 -0.0046 0.0035  96  HIS A N    
1018 C  CA   . HIS A 96  ? 0.1301 0.0318 0.0639 -0.0154 0.0115  0.0017  96  HIS A CA   
1019 C  C    . HIS A 96  ? 0.1340 0.0429 0.0509 -0.0210 0.0038  0.0003  96  HIS A C    
1020 O  O    . HIS A 96  ? 0.1389 0.0367 0.0621 -0.0074 0.0035  -0.0074 96  HIS A O    
1021 C  CB   . HIS A 96  ? 0.1295 0.0363 0.0678 -0.0035 0.0098  -0.0113 96  HIS A CB   
1022 C  CG   . HIS A 96  ? 0.1145 0.0379 0.0665 -0.0148 0.0059  -0.0077 96  HIS A CG   
1023 N  ND1  . HIS A 96  ? 0.1206 0.0359 0.0926 -0.0027 -0.0035 -0.0164 96  HIS A ND1  
1024 C  CD2  . HIS A 96  ? 0.1103 0.0291 0.0734 -0.0113 0.0000  -0.0103 96  HIS A CD2  
1025 C  CE1  . HIS A 96  ? 0.1001 0.0348 0.1100 -0.0073 0.0065  -0.0076 96  HIS A CE1  
1026 N  NE2  . HIS A 96  ? 0.1254 0.0342 0.0608 -0.0091 0.0099  -0.0103 96  HIS A NE2  
1027 N  N    . TRP A 97  ? 0.1265 0.0361 0.0563 -0.0183 0.0154  -0.0041 97  TRP A N    
1028 C  CA   . TRP A 97  ? 0.1292 0.0572 0.0712 -0.0188 0.0071  -0.0104 97  TRP A CA   
1029 C  C    . TRP A 97  ? 0.1286 0.0430 0.0671 -0.0129 0.0153  -0.0124 97  TRP A C    
1030 O  O    . TRP A 97  ? 0.1277 0.0402 0.0924 -0.0109 0.0167  -0.0118 97  TRP A O    
1031 C  CB   . TRP A 97  ? 0.1486 0.0353 0.0696 -0.0086 0.0046  -0.0131 97  TRP A CB   
1032 C  CG   . TRP A 97  ? 0.1705 0.0318 0.0548 -0.0125 -0.0012 -0.0020 97  TRP A CG   
1033 C  CD1  . TRP A 97  ? 0.1809 0.0430 0.0667 -0.0206 0.0109  -0.0098 97  TRP A CD1  
1034 C  CD2  . TRP A 97  ? 0.1849 0.0535 0.0622 -0.0364 0.0030  -0.0104 97  TRP A CD2  
1035 N  NE1  . TRP A 97  ? 0.2046 0.0561 0.0680 -0.0243 0.0240  -0.0148 97  TRP A NE1  
1036 C  CE2  . TRP A 97  ? 0.2007 0.0530 0.0631 -0.0272 0.0208  -0.0120 97  TRP A CE2  
1037 C  CE3  . TRP A 97  ? 0.1802 0.0547 0.0509 -0.0065 -0.0068 -0.0068 97  TRP A CE3  
1038 C  CZ2  . TRP A 97  ? 0.1939 0.0644 0.0732 -0.0292 0.0216  -0.0054 97  TRP A CZ2  
1039 C  CZ3  . TRP A 97  ? 0.1881 0.0565 0.0543 -0.0208 0.0000  -0.0070 97  TRP A CZ3  
1040 C  CH2  . TRP A 97  ? 0.2391 0.0570 0.0526 -0.0337 0.0006  0.0006  97  TRP A CH2  
1041 N  N    . GLY A 98  ? 0.1303 0.0450 0.0730 -0.0194 0.0098  -0.0109 98  GLY A N    
1042 C  CA   . GLY A 98  ? 0.1272 0.0465 0.0773 -0.0092 0.0159  -0.0088 98  GLY A CA   
1043 C  C    . GLY A 98  ? 0.1538 0.0604 0.0851 -0.0305 0.0206  -0.0153 98  GLY A C    
1044 O  O    . GLY A 98  ? 0.1789 0.0500 0.0838 -0.0185 0.0173  -0.0208 98  GLY A O    
1045 N  N    . SER A 99  ? 0.1425 0.0627 0.0917 -0.0031 0.0098  -0.0306 99  SER A N    
1046 C  CA   . SER A 99  ? 0.1550 0.0800 0.0994 -0.0126 0.0222  -0.0403 99  SER A CA   
1047 C  C    . SER A 99  ? 0.1676 0.0577 0.1322 -0.0110 0.0231  -0.0403 99  SER A C    
1048 O  O    . SER A 99  ? 0.2075 0.0754 0.1328 -0.0175 0.0052  -0.0416 99  SER A O    
1049 C  CB   . SER A 99  ? 0.1912 0.0709 0.1333 -0.0175 0.0419  -0.0395 99  SER A CB   
1050 O  OG   . SER A 99  ? 0.1462 0.0755 0.1766 0.0063  0.0342  -0.0305 99  SER A OG   
1051 N  N    . LEU A 100 ? 0.1484 0.0669 0.1489 -0.0076 0.0254  -0.0408 100 LEU A N    
1052 C  CA   . LEU A 100 ? 0.1653 0.0423 0.1687 -0.0003 0.0103  -0.0230 100 LEU A CA   
1053 C  C    . LEU A 100 ? 0.1495 0.0447 0.1224 -0.0057 0.0151  -0.0233 100 LEU A C    
1054 O  O    . LEU A 100 ? 0.1554 0.0563 0.1395 -0.0217 0.0148  -0.0219 100 LEU A O    
1055 C  CB   . LEU A 100 ? 0.2346 0.1511 0.2202 0.0309  0.0351  0.0132  100 LEU A CB   
1056 C  CG   . LEU A 100 ? 0.2384 0.2000 0.2858 0.0509  0.0153  0.0160  100 LEU A CG   
1057 C  CD1  . LEU A 100 ? 0.2269 0.3361 0.3512 0.0678  -0.0027 0.0131  100 LEU A CD1  
1058 C  CD2  . LEU A 100 ? 0.3386 0.2391 0.3061 0.0753  0.0922  -0.0776 100 LEU A CD2  
1059 N  N    . ASP A 101 ? 0.1484 0.0348 0.1613 -0.0043 0.0006  -0.0198 101 ASP A N    
1060 C  CA   . ASP A 101 ? 0.1585 0.0467 0.1229 -0.0104 0.0024  -0.0043 101 ASP A CA   
1061 C  C    . ASP A 101 ? 0.1383 0.0324 0.1468 -0.0068 0.0006  0.0024  101 ASP A C    
1062 O  O    . ASP A 101 ? 0.1823 0.0608 0.1283 0.0119  0.0142  0.0154  101 ASP A O    
1063 C  CB   . ASP A 101 ? 0.1685 0.0609 0.1323 -0.0244 -0.0035 0.0155  101 ASP A CB   
1064 C  CG   . ASP A 101 ? 0.1993 0.0746 0.1620 -0.0208 -0.0219 0.0185  101 ASP A CG   
1065 O  OD1  . ASP A 101 ? 0.2138 0.0917 0.1208 -0.0299 -0.0017 0.0054  101 ASP A OD1  
1066 O  OD2  . ASP A 101 ? 0.2906 0.1827 0.2219 -0.1026 -0.0935 0.0597  101 ASP A OD2  
1067 N  N    . GLY A 102 ? 0.1608 0.0366 0.1371 -0.0024 0.0129  0.0096  102 GLY A N    
1068 C  CA   . GLY A 102 ? 0.1518 0.0626 0.1367 -0.0019 0.0126  0.0188  102 GLY A CA   
1069 C  C    . GLY A 102 ? 0.1304 0.0534 0.1152 -0.0006 0.0068  0.0241  102 GLY A C    
1070 O  O    . GLY A 102 ? 0.1851 0.0579 0.1315 -0.0005 0.0140  0.0286  102 GLY A O    
1071 N  N    . GLN A 103 ? 0.1297 0.0545 0.1046 -0.0104 0.0059  -0.0046 103 GLN A N    
1072 C  CA   . GLN A 103 ? 0.1340 0.0615 0.0985 0.0076  0.0034  0.0038  103 GLN A CA   
1073 C  C    . GLN A 103 ? 0.1172 0.0608 0.0701 -0.0098 0.0186  -0.0109 103 GLN A C    
1074 O  O    . GLN A 103 ? 0.1444 0.0344 0.0970 -0.0071 0.0126  -0.0115 103 GLN A O    
1075 C  CB   . GLN A 103 ? 0.1483 0.0571 0.1061 -0.0003 0.0126  0.0000  103 GLN A CB   
1076 C  CG   . GLN A 103 ? 0.1480 0.0727 0.1310 0.0186  0.0294  0.0030  103 GLN A CG   
1077 C  CD   . GLN A 103 ? 0.1707 0.1120 0.1685 0.0421  0.0397  0.0467  103 GLN A CD   
1078 O  OE1  . GLN A 103 ? 0.2488 0.2165 0.2194 0.1263  0.1395  0.1263  103 GLN A OE1  
1079 N  NE2  . GLN A 103 ? 0.1827 0.1032 0.1904 0.0375  0.0395  0.0098  103 GLN A NE2  
1080 N  N    . GLY A 104 ? 0.1199 0.0530 0.0645 -0.0006 0.0038  -0.0062 104 GLY A N    
1081 C  CA   . GLY A 104 ? 0.1247 0.0520 0.0605 -0.0063 0.0110  0.0043  104 GLY A CA   
1082 C  C    . GLY A 104 ? 0.1163 0.0473 0.0615 -0.0010 -0.0063 0.0038  104 GLY A C    
1083 O  O    . GLY A 104 ? 0.1258 0.0460 0.0748 -0.0085 0.0146  0.0027  104 GLY A O    
1084 N  N    . SER A 105 ? 0.1019 0.0401 0.0626 -0.0015 0.0019  -0.0040 105 SER A N    
1085 C  CA   . SER A 105 ? 0.0992 0.0406 0.0706 -0.0068 0.0005  0.0057  105 SER A CA   
1086 C  C    . SER A 105 ? 0.0994 0.0397 0.0676 -0.0092 0.0137  0.0059  105 SER A C    
1087 O  O    . SER A 105 ? 0.1085 0.0379 0.0861 0.0000  -0.0098 -0.0068 105 SER A O    
1088 C  CB   . SER A 105 ? 0.0920 0.0464 0.0689 -0.0099 -0.0043 -0.0017 105 SER A CB   
1089 O  OG   . SER A 105 ? 0.1105 0.0345 0.0721 0.0000  -0.0030 0.0027  105 SER A OG   
1090 N  N    . GLU A 106 ? 0.0899 0.0358 0.0579 0.0040  -0.0024 -0.0049 106 GLU A N    
1091 C  CA   . GLU A 106 ? 0.0976 0.0447 0.0635 -0.0093 -0.0006 -0.0046 106 GLU A CA   
1092 C  C    . GLU A 106 ? 0.0944 0.0275 0.0843 0.0010  -0.0124 0.0003  106 GLU A C    
1093 O  O    . GLU A 106 ? 0.0924 0.0389 0.0797 0.0000  -0.0080 -0.0026 106 GLU A O    
1094 C  CB   . GLU A 106 ? 0.1046 0.0292 0.0723 -0.0098 0.0034  0.0010  106 GLU A CB   
1095 C  CG   . GLU A 106 ? 0.1385 0.0493 0.0851 -0.0121 0.0294  -0.0060 106 GLU A CG   
1096 C  CD   . GLU A 106 ? 0.1008 0.0476 0.0730 -0.0054 0.0081  -0.0156 106 GLU A CD   
1097 O  OE1  . GLU A 106 ? 0.0888 0.0446 0.0818 -0.0147 0.0080  -0.0085 106 GLU A OE1  
1098 O  OE2  . GLU A 106 ? 0.1017 0.0563 0.0969 -0.0017 0.0051  -0.0136 106 GLU A OE2  
1099 N  N    . HIS A 107 ? 0.0942 0.0342 0.0581 -0.0003 -0.0076 0.0130  107 HIS A N    
1100 C  CA   . HIS A 107 ? 0.0887 0.0256 0.0764 -0.0041 -0.0125 0.0000  107 HIS A CA   
1101 C  C    . HIS A 107 ? 0.0794 0.0662 0.0563 0.0035  0.0015  0.0057  107 HIS A C    
1102 O  O    . HIS A 107 ? 0.0940 0.0454 0.0700 -0.0034 -0.0031 0.0052  107 HIS A O    
1103 C  CB   . HIS A 107 ? 0.0969 0.0392 0.0561 -0.0054 -0.0060 -0.0104 107 HIS A CB   
1104 C  CG   . HIS A 107 ? 0.0807 0.0430 0.0635 0.0068  -0.0071 -0.0087 107 HIS A CG   
1105 N  ND1  . HIS A 107 ? 0.0926 0.0319 0.0693 0.0031  -0.0107 0.0059  107 HIS A ND1  
1106 C  CD2  . HIS A 107 ? 0.0832 0.0441 0.0660 0.0166  -0.0020 0.0020  107 HIS A CD2  
1107 C  CE1  . HIS A 107 ? 0.1054 0.0309 0.0676 0.0142  0.0015  0.0024  107 HIS A CE1  
1108 N  NE2  . HIS A 107 ? 0.0859 0.0515 0.0649 0.0093  -0.0027 -0.0041 107 HIS A NE2  
1109 N  N    . THR A 108 ? 0.1005 0.0420 0.0696 0.0000  -0.0027 0.0007  108 THR A N    
1110 C  CA   . THR A 108 ? 0.1152 0.0353 0.0759 0.0027  -0.0007 0.0013  108 THR A CA   
1111 C  C    . THR A 108 ? 0.1206 0.0429 0.0685 0.0068  -0.0073 -0.0031 108 THR A C    
1112 O  O    . THR A 108 ? 0.1230 0.0518 0.0784 0.0063  -0.0082 0.0076  108 THR A O    
1113 C  CB   . THR A 108 ? 0.1154 0.0403 0.0841 0.0000  -0.0046 -0.0035 108 THR A CB   
1114 O  OG1  . THR A 108 ? 0.1179 0.0449 0.0890 0.0048  -0.0148 0.0057  108 THR A OG1  
1115 C  CG2  . THR A 108 ? 0.1179 0.0715 0.0920 0.0082  -0.0046 0.0024  108 THR A CG2  
1116 N  N    . VAL A 109 ? 0.1111 0.0419 0.0719 -0.0013 0.0059  0.0005  109 VAL A N    
1117 C  CA   . VAL A 109 ? 0.1263 0.0624 0.0737 -0.0098 -0.0006 0.0104  109 VAL A CA   
1118 C  C    . VAL A 109 ? 0.1278 0.0529 0.0825 0.0000  0.0068  0.0143  109 VAL A C    
1119 O  O    . VAL A 109 ? 0.1430 0.0406 0.0852 -0.0065 0.0099  0.0189  109 VAL A O    
1120 C  CB   . VAL A 109 ? 0.1265 0.0543 0.0833 -0.0026 0.0099  0.0060  109 VAL A CB   
1121 C  CG1  . VAL A 109 ? 0.1466 0.0881 0.1229 0.0015  0.0249  0.0309  109 VAL A CG1  
1122 C  CG2  . VAL A 109 ? 0.1571 0.0534 0.1055 0.0175  -0.0104 0.0285  109 VAL A CG2  
1123 N  N    . ASP A 110 ? 0.1689 0.0450 0.0741 0.0065  0.0073  0.0175  110 ASP A N    
1124 C  CA   . ASP A 110 ? 0.1664 0.0554 0.0912 0.0109  0.0026  0.0230  110 ASP A CA   
1125 C  C    . ASP A 110 ? 0.1716 0.0536 0.0870 0.0076  0.0012  0.0170  110 ASP A C    
1126 O  O    . ASP A 110 ? 0.1985 0.0483 0.0904 0.0137  0.0070  0.0237  110 ASP A O    
1127 C  CB   . ASP A 110 ? 0.1887 0.0940 0.0964 0.0337  0.0175  0.0386  110 ASP A CB   
1128 C  CG   . ASP A 110 ? 0.2231 0.0768 0.1066 0.0253  0.0175  0.0445  110 ASP A CG   
1129 O  OD1  . ASP A 110 ? 0.2238 0.0872 0.1190 0.0288  0.0395  0.0296  110 ASP A OD1  
1130 O  OD2  . ASP A 110 ? 0.2341 0.1206 0.1358 0.0126  0.0258  0.0098  110 ASP A OD2  
1131 N  N    . LYS A 111 ? 0.1414 0.0527 0.0863 0.0155  -0.0153 0.0187  111 LYS A N    
1132 C  CA   . LYS A 111 ? 0.1382 0.0379 0.0979 0.0230  0.0000  0.0238  111 LYS A CA   
1133 C  C    . LYS A 111 ? 0.1561 0.0380 0.0974 0.0203  -0.0005 0.0068  111 LYS A C    
1134 O  O    . LYS A 111 ? 0.1391 0.0775 0.1106 0.0124  0.0006  -0.0052 111 LYS A O    
1135 C  CB   . LYS A 111 ? 0.1752 0.0802 0.1062 0.0198  -0.0167 0.0160  111 LYS A CB   
1136 C  CG   . LYS A 111 ? 0.2086 0.1159 0.1536 0.0847  -0.0253 0.0153  111 LYS A CG   
1137 C  CD   . LYS A 111 ? 0.2247 0.1814 0.1712 0.0182  -0.0577 -0.0403 111 LYS A CD   
1138 C  CE   . LYS A 111 ? 0.2592 0.1893 0.2082 0.0076  -0.0410 -0.0093 111 LYS A CE   
1139 N  NZ   . LYS A 111 ? 0.2637 0.2432 0.2332 0.0054  -0.0588 0.0359  111 LYS A NZ   
1140 N  N    . LYS A 112 ? 0.1459 0.0572 0.0705 0.0071  0.0000  0.0126  112 LYS A N    
1141 C  CA   . LYS A 112 ? 0.1315 0.0458 0.0913 0.0065  0.0041  -0.0074 112 LYS A CA   
1142 C  C    . LYS A 112 ? 0.1161 0.0467 0.0845 -0.0006 -0.0185 0.0076  112 LYS A C    
1143 O  O    . LYS A 112 ? 0.1367 0.0432 0.0775 -0.0010 -0.0049 0.0013  112 LYS A O    
1144 C  CB   . LYS A 112 ? 0.1367 0.0642 0.1021 -0.0194 0.0096  -0.0027 112 LYS A CB   
1145 C  CG   . LYS A 112 ? 0.1215 0.1010 0.1133 -0.0102 0.0152  -0.0192 112 LYS A CG   
1146 C  CD   . LYS A 112 ? 0.1698 0.1222 0.1100 0.0077  -0.0006 0.0017  112 LYS A CD   
1147 C  CE   . LYS A 112 ? 0.1825 0.0974 0.1339 -0.0219 -0.0015 0.0024  112 LYS A CE   
1148 N  NZ   . LYS A 112 ? 0.1701 0.1048 0.1565 -0.0151 -0.0167 0.0230  112 LYS A NZ   
1149 N  N    A LYS A 113 ? 0.1242 0.0309 0.0958 0.0054  0.0012  0.0060  113 LYS A N    
1150 N  N    B LYS A 113 ? 0.1057 0.0491 0.0829 0.0098  -0.0161 -0.0148 113 LYS A N    
1151 C  CA   A LYS A 113 ? 0.1301 0.0406 0.0750 0.0054  0.0005  0.0082  113 LYS A CA   
1152 C  CA   B LYS A 113 ? 0.1346 0.0482 0.0762 0.0103  -0.0098 0.0098  113 LYS A CA   
1153 C  C    A LYS A 113 ? 0.1163 0.0545 0.0766 -0.0082 0.0098  0.0104  113 LYS A C    
1154 C  C    B LYS A 113 ? 0.1019 0.0684 0.0624 0.0087  0.0027  -0.0209 113 LYS A C    
1155 O  O    A LYS A 113 ? 0.1154 0.0304 0.1032 -0.0210 0.0097  0.0000  113 LYS A O    
1156 O  O    B LYS A 113 ? 0.1177 0.0485 0.0727 0.0120  -0.0120 -0.0003 113 LYS A O    
1157 C  CB   A LYS A 113 ? 0.1288 0.0456 0.0574 0.0313  -0.0114 0.0108  113 LYS A CB   
1158 C  CB   B LYS A 113 ? 0.1342 0.0548 0.1032 -0.0071 -0.0103 0.0019  113 LYS A CB   
1159 C  CG   A LYS A 113 ? 0.1194 0.0768 0.0459 -0.0186 0.0035  -0.0023 113 LYS A CG   
1160 C  CG   B LYS A 113 ? 0.1430 0.0715 0.0836 0.0346  -0.0399 -0.0098 113 LYS A CG   
1161 C  CD   A LYS A 113 ? 0.1262 0.0784 0.0604 0.0248  0.0091  -0.0110 113 LYS A CD   
1162 C  CD   B LYS A 113 ? 0.1511 0.0944 0.1046 0.0313  -0.0140 -0.0092 113 LYS A CD   
1163 C  CE   A LYS A 113 ? 0.1272 0.1046 0.1089 0.0074  -0.0052 -0.0333 113 LYS A CE   
1164 C  CE   B LYS A 113 ? 0.1456 0.1287 0.1213 -0.0057 -0.0441 0.0126  113 LYS A CE   
1165 N  NZ   A LYS A 113 ? 0.1499 0.1000 0.1319 0.0296  -0.0244 -0.0118 113 LYS A NZ   
1166 N  NZ   B LYS A 113 ? 0.2070 0.1577 0.1708 0.0208  -0.0155 -0.0274 113 LYS A NZ   
1167 N  N    . TYR A 114 ? 0.1154 0.0255 0.0847 0.0008  -0.0143 -0.0033 114 TYR A N    
1168 C  CA   . TYR A 114 ? 0.1197 0.0306 0.0881 -0.0087 -0.0035 0.0162  114 TYR A CA   
1169 C  C    . TYR A 114 ? 0.1127 0.0280 0.0813 -0.0152 -0.0086 -0.0002 114 TYR A C    
1170 O  O    . TYR A 114 ? 0.1118 0.0432 0.0878 -0.0065 -0.0052 -0.0057 114 TYR A O    
1171 C  CB   . TYR A 114 ? 0.1052 0.0473 0.0789 0.0012  -0.0034 0.0046  114 TYR A CB   
1172 C  CG   . TYR A 114 ? 0.1342 0.0342 0.0685 0.0054  -0.0087 0.0052  114 TYR A CG   
1173 C  CD1  . TYR A 114 ? 0.1565 0.0376 0.1005 -0.0006 -0.0020 0.0152  114 TYR A CD1  
1174 C  CD2  . TYR A 114 ? 0.1036 0.0486 0.1102 -0.0103 -0.0068 0.0148  114 TYR A CD2  
1175 C  CE1  . TYR A 114 ? 0.1832 0.0696 0.0806 0.0131  0.0185  0.0104  114 TYR A CE1  
1176 C  CE2  . TYR A 114 ? 0.1161 0.0653 0.1533 -0.0109 0.0136  0.0175  114 TYR A CE2  
1177 C  CZ   . TYR A 114 ? 0.1565 0.0723 0.1332 -0.0080 0.0375  0.0109  114 TYR A CZ   
1178 O  OH   . TYR A 114 ? 0.2256 0.1402 0.1572 0.0135  0.0917  0.0013  114 TYR A OH   
1179 N  N    . ALA A 115 ? 0.1188 0.0306 0.0967 -0.0165 -0.0097 0.0031  115 ALA A N    
1180 C  CA   . ALA A 115 ? 0.1353 0.0313 0.0757 -0.0020 0.0041  0.0043  115 ALA A CA   
1181 C  C    . ALA A 115 ? 0.1312 0.0362 0.0719 0.0000  0.0074  -0.0006 115 ALA A C    
1182 O  O    . ALA A 115 ? 0.1287 0.0388 0.0895 -0.0082 0.0065  -0.0070 115 ALA A O    
1183 C  CB   . ALA A 115 ? 0.1324 0.0494 0.1125 -0.0226 -0.0098 -0.0114 115 ALA A CB   
1184 N  N    . ALA A 116 ? 0.1324 0.0446 0.0640 -0.0114 0.0103  0.0088  116 ALA A N    
1185 C  CA   . ALA A 116 ? 0.1421 0.0323 0.0644 -0.0094 0.0125  0.0142  116 ALA A CA   
1186 C  C    . ALA A 116 ? 0.1129 0.0468 0.0586 -0.0038 -0.0057 0.0065  116 ALA A C    
1187 O  O    . ALA A 116 ? 0.1277 0.0339 0.0658 -0.0043 0.0000  0.0041  116 ALA A O    
1188 C  CB   . ALA A 116 ? 0.1506 0.0415 0.0721 -0.0114 -0.0010 -0.0006 116 ALA A CB   
1189 N  N    . GLU A 117 ? 0.1267 0.0288 0.0676 -0.0074 0.0043  0.0040  117 GLU A N    
1190 C  CA   . GLU A 117 ? 0.1107 0.0279 0.0555 -0.0035 -0.0085 -0.0038 117 GLU A CA   
1191 C  C    . GLU A 117 ? 0.1396 0.0377 0.0421 -0.0164 -0.0126 0.0043  117 GLU A C    
1192 O  O    . GLU A 117 ? 0.1270 0.0386 0.0768 0.0000  -0.0012 0.0153  117 GLU A O    
1193 C  CB   . GLU A 117 ? 0.1224 0.0287 0.0617 0.0076  0.0015  0.0026  117 GLU A CB   
1194 C  CG   . GLU A 117 ? 0.1142 0.0386 0.0719 0.0040  -0.0038 0.0040  117 GLU A CG   
1195 C  CD   . GLU A 117 ? 0.0940 0.0357 0.0520 -0.0097 -0.0086 0.0015  117 GLU A CD   
1196 O  OE1  . GLU A 117 ? 0.1012 0.0389 0.0750 0.0031  -0.0065 0.0052  117 GLU A OE1  
1197 O  OE2  . GLU A 117 ? 0.1206 0.0394 0.0572 -0.0031 -0.0124 0.0027  117 GLU A OE2  
1198 N  N    . LEU A 118 ? 0.1150 0.0344 0.0588 -0.0092 -0.0171 -0.0013 118 LEU A N    
1199 C  CA   . LEU A 118 ? 0.1173 0.0406 0.0502 0.0027  -0.0109 -0.0010 118 LEU A CA   
1200 C  C    . LEU A 118 ? 0.1177 0.0318 0.0623 -0.0010 -0.0186 0.0038  118 LEU A C    
1201 O  O    . LEU A 118 ? 0.1303 0.0297 0.0527 -0.0076 -0.0099 0.0006  118 LEU A O    
1202 C  CB   . LEU A 118 ? 0.1396 0.0335 0.0658 -0.0027 -0.0173 -0.0015 118 LEU A CB   
1203 C  CG   . LEU A 118 ? 0.1427 0.0433 0.0809 0.0054  -0.0295 0.0031  118 LEU A CG   
1204 C  CD1  . LEU A 118 ? 0.1732 0.0485 0.0832 0.0043  -0.0465 0.0211  118 LEU A CD1  
1205 C  CD2  . LEU A 118 ? 0.1551 0.0721 0.1032 0.0023  -0.0299 0.0035  118 LEU A CD2  
1206 N  N    . HIS A 119 ? 0.1274 0.0262 0.0474 0.0007  -0.0043 0.0044  119 HIS A N    
1207 C  CA   . HIS A 119 ? 0.1199 0.0275 0.0471 -0.0096 -0.0087 0.0007  119 HIS A CA   
1208 C  C    . HIS A 119 ? 0.1252 0.0309 0.0500 -0.0225 -0.0265 0.0060  119 HIS A C    
1209 O  O    . HIS A 119 ? 0.1495 0.0306 0.0656 -0.0006 -0.0137 0.0104  119 HIS A O    
1210 C  CB   . HIS A 119 ? 0.1369 0.0263 0.0533 -0.0086 0.0023  0.0026  119 HIS A CB   
1211 C  CG   . HIS A 119 ? 0.0957 0.0397 0.0503 -0.0076 0.0076  -0.0087 119 HIS A CG   
1212 N  ND1  . HIS A 119 ? 0.0974 0.0433 0.0372 -0.0164 0.0126  -0.0006 119 HIS A ND1  
1213 C  CD2  . HIS A 119 ? 0.0912 0.0402 0.0599 -0.0006 0.0019  -0.0005 119 HIS A CD2  
1214 C  CE1  . HIS A 119 ? 0.1237 0.0415 0.0458 0.0020  0.0027  0.0087  119 HIS A CE1  
1215 N  NE2  . HIS A 119 ? 0.0917 0.0326 0.0617 0.0031  0.0020  0.0054  119 HIS A NE2  
1216 N  N    . LEU A 120 ? 0.1243 0.0255 0.0555 0.0014  -0.0136 0.0018  120 LEU A N    
1217 C  CA   . LEU A 120 ? 0.1326 0.0288 0.0750 0.0046  -0.0306 0.0051  120 LEU A CA   
1218 C  C    . LEU A 120 ? 0.1064 0.0258 0.0608 0.0063  -0.0160 -0.0016 120 LEU A C    
1219 O  O    . LEU A 120 ? 0.1073 0.0279 0.0694 -0.0015 -0.0142 -0.0010 120 LEU A O    
1220 C  CB   . LEU A 120 ? 0.1228 0.0306 0.0802 0.0041  -0.0284 0.0027  120 LEU A CB   
1221 C  CG   . LEU A 120 ? 0.1389 0.0538 0.0921 -0.0006 -0.0299 -0.0023 120 LEU A CG   
1222 C  CD1  . LEU A 120 ? 0.1908 0.0836 0.1316 -0.0644 -0.0370 -0.0020 120 LEU A CD1  
1223 C  CD2  . LEU A 120 ? 0.1667 0.0841 0.1188 0.0207  -0.0723 -0.0206 120 LEU A CD2  
1224 N  N    . VAL A 121 ? 0.1296 0.0333 0.0649 -0.0121 -0.0210 0.0065  121 VAL A N    
1225 C  CA   . VAL A 121 ? 0.1298 0.0394 0.0728 0.0005  -0.0104 0.0142  121 VAL A CA   
1226 C  C    . VAL A 121 ? 0.1140 0.0377 0.0640 -0.0057 -0.0068 0.0065  121 VAL A C    
1227 O  O    . VAL A 121 ? 0.1430 0.0332 0.0759 0.0015  -0.0131 0.0065  121 VAL A O    
1228 C  CB   . VAL A 121 ? 0.1435 0.0297 0.0660 -0.0020 -0.0068 0.0085  121 VAL A CB   
1229 C  CG1  . VAL A 121 ? 0.1387 0.0485 0.0827 -0.0092 -0.0031 -0.0019 121 VAL A CG1  
1230 C  CG2  . VAL A 121 ? 0.1351 0.0423 0.0931 -0.0030 0.0165  0.0049  121 VAL A CG2  
1231 N  N    . HIS A 122 ? 0.1116 0.0363 0.0745 -0.0103 -0.0228 0.0081  122 HIS A N    
1232 C  CA   . HIS A 122 ? 0.1172 0.0288 0.0798 0.0098  -0.0188 -0.0037 122 HIS A CA   
1233 C  C    . HIS A 122 ? 0.1251 0.0366 0.0705 0.0043  -0.0071 0.0057  122 HIS A C    
1234 O  O    . HIS A 122 ? 0.1286 0.0349 0.0845 -0.0104 -0.0221 0.0038  122 HIS A O    
1235 C  CB   . HIS A 122 ? 0.1127 0.0379 0.0797 0.0109  -0.0107 0.0098  122 HIS A CB   
1236 C  CG   . HIS A 122 ? 0.1247 0.0388 0.0838 -0.0065 -0.0186 0.0038  122 HIS A CG   
1237 N  ND1  . HIS A 122 ? 0.1102 0.0336 0.1005 0.0003  -0.0109 0.0054  122 HIS A ND1  
1238 C  CD2  . HIS A 122 ? 0.1243 0.0688 0.0895 -0.0015 -0.0093 -0.0023 122 HIS A CD2  
1239 C  CE1  . HIS A 122 ? 0.1062 0.0357 0.0987 -0.0082 -0.0110 0.0091  122 HIS A CE1  
1240 N  NE2  . HIS A 122 ? 0.1163 0.0491 0.1073 -0.0031 -0.0216 -0.0054 122 HIS A NE2  
1241 N  N    . TRP A 123 ? 0.1127 0.0345 0.0881 -0.0007 -0.0140 0.0000  123 TRP A N    
1242 C  CA   . TRP A 123 ? 0.1027 0.0326 0.0960 -0.0027 -0.0153 0.0030  123 TRP A CA   
1243 C  C    . TRP A 123 ? 0.1181 0.0414 0.0809 0.0006  -0.0166 -0.0076 123 TRP A C    
1244 O  O    . TRP A 123 ? 0.1268 0.0476 0.1118 0.0054  -0.0103 -0.0142 123 TRP A O    
1245 C  CB   . TRP A 123 ? 0.1497 0.0359 0.0976 -0.0087 0.0063  -0.0141 123 TRP A CB   
1246 C  CG   . TRP A 123 ? 0.1441 0.0577 0.0926 -0.0142 -0.0071 0.0059  123 TRP A CG   
1247 C  CD1  . TRP A 123 ? 0.1962 0.0525 0.0836 -0.0170 -0.0173 0.0085  123 TRP A CD1  
1248 C  CD2  . TRP A 123 ? 0.1985 0.0306 0.1039 -0.0051 0.0019  0.0115  123 TRP A CD2  
1249 N  NE1  . TRP A 123 ? 0.2397 0.0525 0.1032 -0.0109 -0.0283 -0.0071 123 TRP A NE1  
1250 C  CE2  . TRP A 123 ? 0.2073 0.0563 0.1075 -0.0164 -0.0242 0.0082  123 TRP A CE2  
1251 C  CE3  . TRP A 123 ? 0.2330 0.0351 0.0939 -0.0147 -0.0086 -0.0005 123 TRP A CE3  
1252 C  CZ2  . TRP A 123 ? 0.2273 0.0468 0.1149 -0.0087 -0.0140 0.0027  123 TRP A CZ2  
1253 C  CZ3  . TRP A 123 ? 0.2587 0.0388 0.1019 -0.0189 0.0093  0.0000  123 TRP A CZ3  
1254 C  CH2  . TRP A 123 ? 0.2716 0.0401 0.1097 -0.0065 -0.0140 0.0159  123 TRP A CH2  
1255 N  N    . ASN A 124 ? 0.1057 0.0403 0.1093 0.0091  -0.0118 -0.0071 124 ASN A N    
1256 C  CA   . ASN A 124 ? 0.1164 0.0474 0.1073 0.0065  -0.0068 -0.0115 124 ASN A CA   
1257 C  C    . ASN A 124 ? 0.1432 0.0473 0.0924 0.0227  -0.0178 -0.0228 124 ASN A C    
1258 O  O    . ASN A 124 ? 0.1316 0.0486 0.1100 0.0065  -0.0104 -0.0113 124 ASN A O    
1259 C  CB   . ASN A 124 ? 0.1256 0.0554 0.1058 -0.0038 -0.0162 -0.0092 124 ASN A CB   
1260 C  CG   . ASN A 124 ? 0.1341 0.0464 0.1075 0.0043  0.0060  -0.0186 124 ASN A CG   
1261 O  OD1  . ASN A 124 ? 0.1526 0.0577 0.1213 0.0155  0.0000  -0.0210 124 ASN A OD1  
1262 N  ND2  . ASN A 124 ? 0.1815 0.0748 0.0856 0.0010  -0.0063 -0.0098 124 ASN A ND2  
1263 N  N    . THR A 125 ? 0.1362 0.0547 0.0983 0.0210  -0.0110 -0.0024 125 THR A N    
1264 C  CA   . THR A 125 ? 0.1453 0.0539 0.1307 0.0148  -0.0137 0.0082  125 THR A CA   
1265 C  C    . THR A 125 ? 0.1533 0.0414 0.1601 0.0355  -0.0115 -0.0031 125 THR A C    
1266 O  O    . THR A 125 ? 0.1800 0.0578 0.1594 0.0252  -0.0087 0.0081  125 THR A O    
1267 C  CB   . THR A 125 ? 0.1641 0.0897 0.1844 0.0020  -0.0243 0.0252  125 THR A CB   
1268 O  OG1  . THR A 125 ? 0.1768 0.1026 0.2560 0.0537  0.0253  0.0264  125 THR A OG1  
1269 C  CG2  . THR A 125 ? 0.1630 0.1167 0.2332 0.0037  -0.0675 -0.0186 125 THR A CG2  
1270 N  N    A LYS A 126 ? 0.1462 0.0326 0.0931 0.0076  -0.0252 -0.0221 127 LYS A N    
1271 N  N    B LYS A 126 ? 0.1827 0.0485 0.1106 0.0186  0.0219  -0.0049 127 LYS A N    
1272 C  CA   A LYS A 126 ? 0.1619 0.0468 0.1233 0.0038  -0.0186 -0.0414 127 LYS A CA   
1273 C  CA   B LYS A 126 ? 0.1784 0.0539 0.1260 0.0080  0.0054  -0.0043 127 LYS A CA   
1274 C  C    A LYS A 126 ? 0.1721 0.0565 0.1032 -0.0006 -0.0170 -0.0102 127 LYS A C    
1275 C  C    B LYS A 126 ? 0.1892 0.0741 0.1340 0.0074  -0.0051 -0.0080 127 LYS A C    
1276 O  O    A LYS A 126 ? 0.1960 0.0456 0.0648 -0.0098 -0.0115 0.0015  127 LYS A O    
1277 O  O    B LYS A 126 ? 0.2027 0.1009 0.2026 -0.0114 -0.0206 -0.0199 127 LYS A O    
1278 C  CB   A LYS A 126 ? 0.1509 0.0727 0.0854 -0.0178 -0.0297 -0.0081 127 LYS A CB   
1279 C  CB   B LYS A 126 ? 0.1930 0.0917 0.1465 0.0231  -0.0074 -0.0119 127 LYS A CB   
1280 C  CG   A LYS A 126 ? 0.1098 0.0667 0.1391 -0.0020 -0.0370 -0.0239 127 LYS A CG   
1281 C  CG   B LYS A 126 ? 0.2068 0.1107 0.1574 0.0335  0.0097  0.0059  127 LYS A CG   
1282 C  CD   A LYS A 126 ? 0.1410 0.1554 0.1285 0.0164  0.0007  -0.0167 127 LYS A CD   
1283 C  CD   B LYS A 126 ? 0.2245 0.0939 0.1206 0.0193  0.0000  0.0110  127 LYS A CD   
1284 C  CE   A LYS A 126 ? 0.1404 0.1826 0.1472 0.0092  -0.0225 0.0148  127 LYS A CE   
1285 C  CE   B LYS A 126 ? 0.2949 0.1161 0.1136 -0.0104 -0.0131 0.0049  127 LYS A CE   
1286 N  NZ   A LYS A 126 ? 0.1842 0.1964 0.1396 0.0082  -0.0118 -0.0255 127 LYS A NZ   
1287 N  NZ   B LYS A 126 ? 0.2759 0.1676 0.1708 0.0315  0.0003  0.0177  127 LYS A NZ   
1288 N  N    . TYR A 127 ? 0.1732 0.0335 0.1152 -0.0054 -0.0165 -0.0159 128 TYR A N    
1289 C  CA   . TYR A 127 ? 0.1702 0.0502 0.1100 -0.0119 -0.0166 -0.0035 128 TYR A CA   
1290 C  C    . TYR A 127 ? 0.1669 0.0368 0.1278 -0.0126 -0.0193 -0.0071 128 TYR A C    
1291 O  O    . TYR A 127 ? 0.1678 0.0489 0.1215 -0.0102 -0.0103 -0.0015 128 TYR A O    
1292 C  CB   . TYR A 127 ? 0.1613 0.0456 0.1301 -0.0082 -0.0041 0.0046  128 TYR A CB   
1293 C  CG   . TYR A 127 ? 0.1513 0.0449 0.1199 0.0013  -0.0103 -0.0060 128 TYR A CG   
1294 C  CD1  . TYR A 127 ? 0.1770 0.0612 0.1190 0.0037  -0.0351 -0.0155 128 TYR A CD1  
1295 C  CD2  . TYR A 127 ? 0.1641 0.0678 0.1037 -0.0003 -0.0118 -0.0108 128 TYR A CD2  
1296 C  CE1  . TYR A 127 ? 0.1867 0.0591 0.1332 0.0137  -0.0294 -0.0394 128 TYR A CE1  
1297 C  CE2  . TYR A 127 ? 0.1639 0.0581 0.1179 0.0115  -0.0236 -0.0204 128 TYR A CE2  
1298 C  CZ   . TYR A 127 ? 0.1683 0.0662 0.1344 0.0186  0.0063  -0.0285 128 TYR A CZ   
1299 O  OH   . TYR A 127 ? 0.2459 0.0802 0.1021 0.0189  -0.0254 -0.0317 128 TYR A OH   
1300 N  N    . GLY A 128 ? 0.1595 0.0439 0.1283 -0.0142 -0.0186 0.0087  129 GLY A N    
1301 C  CA   . GLY A 128 ? 0.1887 0.0423 0.1276 -0.0109 -0.0153 0.0135  129 GLY A CA   
1302 C  C    . GLY A 128 ? 0.2041 0.0437 0.1115 -0.0031 -0.0241 0.0034  129 GLY A C    
1303 O  O    . GLY A 128 ? 0.2483 0.0579 0.1149 -0.0093 -0.0419 0.0148  129 GLY A O    
1304 N  N    A ASP A 129 ? 0.1860 0.0640 0.0947 0.0049  -0.0035 0.0035  130 ASP A N    
1305 N  N    B ASP A 129 ? 0.2215 0.0545 0.1021 0.0120  -0.0344 0.0024  130 ASP A N    
1306 C  CA   A ASP A 129 ? 0.1565 0.0605 0.0732 -0.0197 -0.0031 0.0148  130 ASP A CA   
1307 C  CA   B ASP A 129 ? 0.1911 0.0526 0.1118 0.0006  -0.0274 -0.0015 130 ASP A CA   
1308 C  C    A ASP A 129 ? 0.1159 0.0527 0.0581 -0.0160 0.0020  0.0093  130 ASP A C    
1309 C  C    B ASP A 129 ? 0.1650 0.0825 0.1233 0.0098  -0.0247 0.0015  130 ASP A C    
1310 O  O    A ASP A 129 ? 0.1055 0.0456 0.0748 0.0000  -0.0006 0.0065  130 ASP A O    
1311 O  O    B ASP A 129 ? 0.1610 0.0666 0.1204 0.0048  -0.0049 -0.0091 130 ASP A O    
1312 C  CB   A ASP A 129 ? 0.1483 0.0529 0.1093 -0.0148 -0.0012 0.0098  130 ASP A CB   
1313 C  CB   B ASP A 129 ? 0.1782 0.0678 0.1079 0.0322  -0.0305 0.0000  130 ASP A CB   
1314 C  CG   A ASP A 129 ? 0.1253 0.0529 0.0782 -0.0252 -0.0208 0.0098  130 ASP A CG   
1315 C  CG   B ASP A 129 ? 0.1892 0.0518 0.1755 0.0570  -0.0060 -0.0333 130 ASP A CG   
1316 O  OD1  A ASP A 129 ? 0.2626 0.0633 0.1161 -0.0755 -0.0571 0.0183  130 ASP A OD1  
1317 O  OD1  B ASP A 129 ? 0.3149 0.1623 0.2915 0.0136  -0.0500 0.0266  130 ASP A OD1  
1318 O  OD2  A ASP A 129 ? 0.1459 0.0633 0.1061 0.0186  0.0153  0.0176  130 ASP A OD2  
1319 O  OD2  B ASP A 129 ? 0.1728 0.2348 0.3398 0.0043  0.0315  0.0834  130 ASP A OD2  
1320 N  N    A PHE A 130 ? 0.1030 0.0455 0.0653 -0.0186 0.0208  0.0057  131 PHE A N    
1321 N  N    B PHE A 130 ? 0.1545 0.0624 0.1036 0.0020  -0.0171 -0.0013 131 PHE A N    
1322 C  CA   A PHE A 130 ? 0.1181 0.0563 0.0617 -0.0062 0.0034  0.0153  131 PHE A CA   
1323 C  CA   B PHE A 130 ? 0.1412 0.0583 0.0951 -0.0068 -0.0113 0.0043  131 PHE A CA   
1324 C  C    A PHE A 130 ? 0.0953 0.0615 0.0798 -0.0120 0.0227  0.0098  131 PHE A C    
1325 C  C    B PHE A 130 ? 0.1391 0.0385 0.0967 -0.0219 -0.0031 -0.0081 131 PHE A C    
1326 O  O    A PHE A 130 ? 0.0917 0.0676 0.0703 -0.0131 -0.0007 0.0076  131 PHE A O    
1327 O  O    B PHE A 130 ? 0.1362 0.0467 0.0996 -0.0263 -0.0082 -0.0109 131 PHE A O    
1328 C  CB   A PHE A 130 ? 0.0836 0.0499 0.0891 -0.0140 0.0146  -0.0043 131 PHE A CB   
1329 C  CB   B PHE A 130 ? 0.1499 0.0768 0.0930 0.0013  -0.0088 -0.0120 131 PHE A CB   
1330 C  CG   A PHE A 130 ? 0.0852 0.0296 0.0750 0.0076  0.0012  -0.0043 131 PHE A CG   
1331 C  CG   B PHE A 130 ? 0.1136 0.0465 0.1283 -0.0035 0.0070  -0.0024 131 PHE A CG   
1332 C  CD1  A PHE A 130 ? 0.0929 0.0472 0.0833 -0.0164 -0.0087 -0.0037 131 PHE A CD1  
1333 C  CD1  B PHE A 130 ? 0.1168 0.0766 0.1048 0.0038  0.0126  -0.0113 131 PHE A CD1  
1334 C  CD2  A PHE A 130 ? 0.0949 0.0824 0.1161 -0.0074 0.0104  -0.0108 131 PHE A CD2  
1335 C  CD2  B PHE A 130 ? 0.1500 0.0335 0.1513 -0.0146 0.0162  0.0088  131 PHE A CD2  
1336 C  CE1  A PHE A 130 ? 0.0888 0.0685 0.1028 -0.0187 0.0076  0.0046  131 PHE A CE1  
1337 C  CE1  B PHE A 130 ? 0.0815 0.0811 0.1213 -0.0059 -0.0017 -0.0052 131 PHE A CE1  
1338 C  CE2  A PHE A 130 ? 0.1044 0.1005 0.1195 0.0129  0.0250  -0.0186 131 PHE A CE2  
1339 C  CE2  B PHE A 130 ? 0.1030 0.0850 0.1850 -0.0294 -0.0192 0.0031  131 PHE A CE2  
1340 C  CZ   A PHE A 130 ? 0.1045 0.0500 0.1058 -0.0049 -0.0031 0.0048  131 PHE A CZ   
1341 C  CZ   B PHE A 130 ? 0.1084 0.0714 0.1360 -0.0161 -0.0131 0.0027  131 PHE A CZ   
1342 N  N    A GLY A 131 ? 0.1152 0.0581 0.0903 -0.0186 0.0175  0.0068  132 GLY A N    
1343 N  N    B GLY A 131 ? 0.1601 0.0553 0.1204 -0.0126 0.0126  0.0057  132 GLY A N    
1344 C  CA   A GLY A 131 ? 0.1197 0.0715 0.0906 -0.0197 0.0159  0.0166  132 GLY A CA   
1345 C  CA   B GLY A 131 ? 0.1665 0.0811 0.1224 -0.0230 0.0087  0.0052  132 GLY A CA   
1346 C  C    A GLY A 131 ? 0.1434 0.0591 0.1386 -0.0373 0.0118  0.0048  132 GLY A C    
1347 C  C    B GLY A 131 ? 0.1822 0.0728 0.1297 -0.0346 0.0259  0.0065  132 GLY A C    
1348 O  O    A GLY A 131 ? 0.1572 0.0825 0.1048 0.0051  -0.0071 -0.0186 132 GLY A O    
1349 O  O    B GLY A 131 ? 0.2151 0.0571 0.1075 -0.0505 0.0346  -0.0211 132 GLY A O    
1350 N  N    . LYS A 132 ? 0.1978 0.0592 0.1411 -0.0251 0.0140  0.0124  133 LYS A N    
1351 C  CA   . LYS A 132 ? 0.1759 0.0539 0.1254 -0.0263 0.0017  -0.0068 133 LYS A CA   
1352 C  C    . LYS A 132 ? 0.1685 0.0606 0.1125 -0.0200 0.0225  -0.0087 133 LYS A C    
1353 O  O    . LYS A 132 ? 0.1622 0.0624 0.1222 -0.0322 0.0027  -0.0082 133 LYS A O    
1354 C  CB   . LYS A 132 ? 0.1772 0.0696 0.1453 -0.0247 0.0019  -0.0153 133 LYS A CB   
1355 C  CG   . LYS A 132 ? 0.1676 0.0697 0.2199 -0.0295 0.0068  0.0076  133 LYS A CG   
1356 C  CD   . LYS A 132 ? 0.2366 0.1653 0.3826 -0.0006 -0.0057 0.0443  133 LYS A CD   
1357 C  CE   . LYS A 132 ? 0.2327 0.1838 0.3569 -0.0317 -0.0195 0.0000  133 LYS A CE   
1358 N  NZ   . LYS A 132 ? 0.3118 0.3018 0.4374 -0.1076 -0.0406 0.0210  133 LYS A NZ   
1359 N  N    . ALA A 133 ? 0.1635 0.0626 0.0895 -0.0286 -0.0015 -0.0164 134 ALA A N    
1360 C  CA   . ALA A 133 ? 0.1554 0.0608 0.0766 -0.0348 0.0062  -0.0131 134 ALA A CA   
1361 C  C    . ALA A 133 ? 0.1221 0.0626 0.0996 -0.0288 -0.0024 -0.0068 134 ALA A C    
1362 O  O    . ALA A 133 ? 0.1237 0.0791 0.0845 -0.0176 0.0007  -0.0026 134 ALA A O    
1363 C  CB   . ALA A 133 ? 0.1412 0.0715 0.0870 -0.0228 -0.0186 -0.0020 134 ALA A CB   
1364 N  N    . VAL A 134 ? 0.1396 0.0538 0.0926 -0.0174 0.0120  -0.0104 135 VAL A N    
1365 C  CA   . VAL A 134 ? 0.1563 0.0621 0.1030 -0.0288 0.0249  -0.0131 135 VAL A CA   
1366 C  C    . VAL A 134 ? 0.1533 0.0648 0.1105 -0.0204 0.0259  -0.0109 135 VAL A C    
1367 O  O    . VAL A 134 ? 0.1435 0.0750 0.1288 -0.0184 0.0148  -0.0093 135 VAL A O    
1368 C  CB   . VAL A 134 ? 0.1678 0.0606 0.1093 -0.0251 0.0217  -0.0071 135 VAL A CB   
1369 C  CG1  . VAL A 134 ? 0.1804 0.0843 0.1326 -0.0216 0.0071  0.0000  135 VAL A CG1  
1370 C  CG2  . VAL A 134 ? 0.1746 0.0865 0.1234 -0.0197 0.0346  -0.0073 135 VAL A CG2  
1371 N  N    . GLN A 135 ? 0.1483 0.0678 0.1272 -0.0215 0.0199  0.0020  136 GLN A N    
1372 C  CA   . GLN A 135 ? 0.1407 0.0825 0.1301 -0.0273 -0.0034 -0.0153 136 GLN A CA   
1373 C  C    . GLN A 135 ? 0.1499 0.0727 0.1199 -0.0296 -0.0118 -0.0120 136 GLN A C    
1374 O  O    . GLN A 135 ? 0.1590 0.1261 0.1437 -0.0421 -0.0031 -0.0240 136 GLN A O    
1375 C  CB   . GLN A 135 ? 0.1685 0.0969 0.1416 -0.0469 -0.0015 -0.0074 136 GLN A CB   
1376 C  CG   . GLN A 135 ? 0.1808 0.1410 0.1614 -0.0665 0.0153  0.0085  136 GLN A CG   
1377 C  CD   . GLN A 135 ? 0.2208 0.2201 0.2350 -0.0606 0.0104  0.0253  136 GLN A CD   
1378 O  OE1  . GLN A 135 ? 0.2750 0.2705 0.3115 -0.0568 0.0260  0.0838  136 GLN A OE1  
1379 N  NE2  . GLN A 135 ? 0.2425 0.2438 0.3088 -0.0630 -0.0031 0.0284  136 GLN A NE2  
1380 N  N    . GLN A 136 ? 0.1400 0.0705 0.1111 -0.0164 0.0077  -0.0109 137 GLN A N    
1381 C  CA   . GLN A 136 ? 0.1411 0.0741 0.0802 -0.0093 -0.0143 -0.0241 137 GLN A CA   
1382 C  C    . GLN A 136 ? 0.1084 0.0869 0.1084 -0.0110 -0.0088 -0.0226 137 GLN A C    
1383 O  O    . GLN A 136 ? 0.1272 0.0694 0.0847 -0.0020 0.0000  -0.0115 137 GLN A O    
1384 C  CB   . GLN A 136 ? 0.1520 0.0649 0.1118 -0.0057 -0.0186 -0.0203 137 GLN A CB   
1385 C  CG   . GLN A 136 ? 0.2456 0.1146 0.1145 0.0631  0.0189  -0.0098 137 GLN A CG   
1386 C  CD   . GLN A 136 ? 0.1913 0.0983 0.2644 -0.0166 0.0306  0.0370  137 GLN A CD   
1387 O  OE1  . GLN A 136 ? 0.3246 0.1604 0.3068 0.0196  -0.0425 -0.0465 137 GLN A OE1  
1388 N  NE2  . GLN A 136 ? 0.3621 0.1691 0.2601 -0.0421 -0.0727 -0.0362 137 GLN A NE2  
1389 N  N    . PRO A 137 ? 0.1281 0.1017 0.0793 -0.0126 -0.0184 -0.0260 138 PRO A N    
1390 C  CA   . PRO A 137 ? 0.1421 0.1039 0.0775 0.0041  -0.0035 0.0082  138 PRO A CA   
1391 C  C    . PRO A 137 ? 0.1323 0.0987 0.0793 -0.0142 -0.0035 0.0023  138 PRO A C    
1392 O  O    . PRO A 137 ? 0.1489 0.0878 0.1699 -0.0031 -0.0019 0.0383  138 PRO A O    
1393 C  CB   . PRO A 137 ? 0.1808 0.1393 0.0882 0.0109  -0.0027 -0.0104 138 PRO A CB   
1394 C  CG   . PRO A 137 ? 0.2734 0.1935 0.0947 -0.0324 -0.0222 -0.0253 138 PRO A CG   
1395 C  CD   . PRO A 137 ? 0.1428 0.1522 0.0951 -0.0331 -0.0175 -0.0276 138 PRO A CD   
1396 N  N    . ASP A 138 ? 0.1254 0.0773 0.0807 -0.0038 -0.0049 0.0010  139 ASP A N    
1397 C  CA   . ASP A 138 ? 0.1295 0.0732 0.0877 -0.0096 0.0038  -0.0124 139 ASP A CA   
1398 C  C    . ASP A 138 ? 0.1115 0.0471 0.0966 -0.0041 -0.0063 -0.0087 139 ASP A C    
1399 O  O    . ASP A 138 ? 0.1253 0.0633 0.0961 -0.0020 -0.0031 -0.0076 139 ASP A O    
1400 C  CB   . ASP A 138 ? 0.1523 0.1106 0.0915 0.0017  0.0038  -0.0060 139 ASP A CB   
1401 C  CG   . ASP A 138 ? 0.1448 0.1091 0.1152 0.0163  0.0027  -0.0243 139 ASP A CG   
1402 O  OD1  . ASP A 138 ? 0.1859 0.0759 0.1125 0.0209  -0.0260 -0.0331 139 ASP A OD1  
1403 O  OD2  . ASP A 138 ? 0.2078 0.1254 0.1314 0.0368  0.0148  -0.0410 139 ASP A OD2  
1404 N  N    . GLY A 139 ? 0.1168 0.0490 0.0877 -0.0017 -0.0030 -0.0166 140 GLY A N    
1405 C  CA   . GLY A 139 ? 0.1279 0.0459 0.0648 -0.0052 -0.0115 0.0013  140 GLY A CA   
1406 C  C    . GLY A 139 ? 0.1249 0.0379 0.0727 0.0020  0.0035  0.0086  140 GLY A C    
1407 O  O    . GLY A 139 ? 0.1172 0.0414 0.0775 0.0000  -0.0046 -0.0017 140 GLY A O    
1408 N  N    . LEU A 140 ? 0.1118 0.0423 0.0757 0.0005  -0.0097 -0.0092 141 LEU A N    
1409 C  CA   . LEU A 140 ? 0.1023 0.0339 0.0784 -0.0062 -0.0163 -0.0035 141 LEU A CA   
1410 C  C    . LEU A 140 ? 0.1058 0.0280 0.0662 0.0057  -0.0043 -0.0013 141 LEU A C    
1411 O  O    . LEU A 140 ? 0.0978 0.0335 0.0825 -0.0043 -0.0035 -0.0005 141 LEU A O    
1412 C  CB   . LEU A 140 ? 0.1005 0.0376 0.0879 0.0015  -0.0130 -0.0071 141 LEU A CB   
1413 C  CG   . LEU A 140 ? 0.1037 0.0486 0.0942 -0.0108 0.0057  -0.0057 141 LEU A CG   
1414 C  CD1  . LEU A 140 ? 0.1111 0.0597 0.1010 0.0087  0.0109  -0.0135 141 LEU A CD1  
1415 C  CD2  . LEU A 140 ? 0.1386 0.0465 0.1170 0.0096  0.0119  0.0068  141 LEU A CD2  
1416 N  N    . ALA A 141 ? 0.1084 0.0274 0.0693 0.0012  -0.0041 0.0006  142 ALA A N    
1417 C  CA   . ALA A 141 ? 0.0944 0.0370 0.0852 -0.0035 -0.0086 -0.0054 142 ALA A CA   
1418 C  C    . ALA A 141 ? 0.1035 0.0414 0.0719 -0.0080 -0.0030 0.0109  142 ALA A C    
1419 O  O    . ALA A 141 ? 0.1203 0.0342 0.0881 -0.0096 -0.0141 0.0071  142 ALA A O    
1420 C  CB   . ALA A 141 ? 0.1252 0.0605 0.0924 -0.0098 -0.0010 -0.0097 142 ALA A CB   
1421 N  N    A VAL A 142 ? 0.0973 0.0359 0.0362 -0.0164 -0.0167 -0.0024 143 VAL A N    
1422 N  N    B VAL A 142 ? 0.0836 0.0275 0.0829 0.0082  -0.0152 0.0054  143 VAL A N    
1423 C  CA   A VAL A 142 ? 0.0746 0.0291 0.0563 0.0043  -0.0003 -0.0054 143 VAL A CA   
1424 C  CA   B VAL A 142 ? 0.0763 0.0322 0.0721 -0.0034 -0.0073 0.0175  143 VAL A CA   
1425 C  C    A VAL A 142 ? 0.0818 0.0288 0.0797 -0.0019 0.0099  0.0062  143 VAL A C    
1426 C  C    B VAL A 142 ? 0.0606 0.0451 0.0599 0.0080  -0.0027 -0.0159 143 VAL A C    
1427 O  O    A VAL A 142 ? 0.0793 0.0392 0.0618 0.0043  0.0077  0.0006  143 VAL A O    
1428 O  O    B VAL A 142 ? 0.0687 0.0529 0.0581 0.0035  -0.0041 -0.0035 143 VAL A O    
1429 C  CB   A VAL A 142 ? 0.0872 0.0520 0.0570 -0.0237 -0.0241 0.0059  143 VAL A CB   
1430 C  CB   B VAL A 142 ? 0.0640 0.0671 0.0821 0.0176  -0.0010 0.0076  143 VAL A CB   
1431 C  CG1  A VAL A 142 ? 0.0498 0.0680 0.1005 0.0049  -0.0120 -0.0250 143 VAL A CG1  
1432 C  CG1  B VAL A 142 ? 0.0897 0.0724 0.0379 -0.0243 -0.0060 0.0104  143 VAL A CG1  
1433 C  CG2  A VAL A 142 ? 0.0617 0.0838 0.1159 -0.0081 -0.0031 -0.0135 143 VAL A CG2  
1434 C  CG2  B VAL A 142 ? 0.0680 0.0885 0.0944 -0.0403 -0.0272 0.0465  143 VAL A CG2  
1435 N  N    A LEU A 143 ? 0.0709 0.0287 0.0543 -0.0071 0.0043  0.0070  144 LEU A N    
1436 N  N    B LEU A 143 ? 0.0657 0.0258 0.0733 -0.0020 0.0042  -0.0045 144 LEU A N    
1437 C  CA   A LEU A 143 ? 0.0606 0.0318 0.0777 -0.0070 -0.0019 0.0156  144 LEU A CA   
1438 C  CA   B LEU A 143 ? 0.0635 0.0491 0.0669 0.0026  0.0153  -0.0096 144 LEU A CA   
1439 C  C    A LEU A 143 ? 0.0572 0.0579 0.0521 -0.0010 0.0003  0.0093  144 LEU A C    
1440 C  C    B LEU A 143 ? 0.0653 0.0392 0.0669 -0.0068 0.0217  -0.0175 144 LEU A C    
1441 O  O    A LEU A 143 ? 0.0687 0.0428 0.0551 -0.0030 0.0186  0.0057  144 LEU A O    
1442 O  O    B LEU A 143 ? 0.0546 0.0383 0.0782 0.0023  0.0034  0.0000  144 LEU A O    
1443 C  CB   A LEU A 143 ? 0.0861 0.0544 0.0542 -0.0043 0.0037  0.0284  144 LEU A CB   
1444 C  CB   B LEU A 143 ? 0.0800 0.0651 0.0750 -0.0060 0.0307  -0.0120 144 LEU A CB   
1445 C  CG   A LEU A 143 ? 0.0579 0.0635 0.1045 -0.0054 0.0125  0.0063  144 LEU A CG   
1446 C  CG   B LEU A 143 ? 0.0900 0.0732 0.0775 -0.0087 0.0313  -0.0251 144 LEU A CG   
1447 C  CD1  A LEU A 143 ? 0.0710 0.1563 0.0951 -0.0096 0.0324  0.0370  144 LEU A CD1  
1448 C  CD1  B LEU A 143 ? 0.0942 0.0683 0.0906 -0.0140 0.0423  -0.0086 144 LEU A CD1  
1449 C  CD2  A LEU A 143 ? 0.0757 0.0994 0.0685 0.0263  0.0186  0.0164  144 LEU A CD2  
1450 C  CD2  B LEU A 143 ? 0.0836 0.1084 0.1256 -0.0161 0.0309  -0.0248 144 LEU A CD2  
1451 N  N    A GLY A 144 ? 0.0736 0.0476 0.0714 0.0085  0.0010  0.0148  145 GLY A N    
1452 N  N    B GLY A 144 ? 0.0552 0.0447 0.0579 -0.0065 0.0000  -0.0091 145 GLY A N    
1453 C  CA   A GLY A 144 ? 0.0678 0.0495 0.0512 0.0113  -0.0087 -0.0043 145 GLY A CA   
1454 C  CA   B GLY A 144 ? 0.0697 0.0367 0.0596 -0.0013 -0.0059 -0.0109 145 GLY A CA   
1455 C  C    A GLY A 144 ? 0.0718 0.0326 0.0712 0.0006  -0.0109 0.0171  145 GLY A C    
1456 C  C    B GLY A 144 ? 0.0701 0.0441 0.0524 -0.0013 0.0098  0.0017  145 GLY A C    
1457 O  O    A GLY A 144 ? 0.0657 0.0428 0.0776 -0.0098 0.0104  -0.0046 145 GLY A O    
1458 O  O    B GLY A 144 ? 0.0706 0.0439 0.0744 -0.0010 -0.0082 -0.0082 145 GLY A O    
1459 N  N    A ILE A 145 ? 0.0759 0.0287 0.0554 0.0038  0.0151  0.0093  146 ILE A N    
1460 N  N    B ILE A 145 ? 0.0606 0.0421 0.0538 -0.0051 -0.0031 -0.0074 146 ILE A N    
1461 C  CA   A ILE A 145 ? 0.0769 0.0301 0.0639 -0.0100 0.0108  0.0080  146 ILE A CA   
1462 C  CA   B ILE A 145 ? 0.0486 0.0335 0.0621 -0.0052 -0.0041 0.0000  146 ILE A CA   
1463 C  C    A ILE A 145 ? 0.0781 0.0432 0.0599 -0.0038 0.0114  0.0136  146 ILE A C    
1464 C  C    B ILE A 145 ? 0.0763 0.0403 0.0603 0.0035  -0.0119 0.0030  146 ILE A C    
1465 O  O    A ILE A 145 ? 0.0583 0.0292 0.1085 0.0017  -0.0013 0.0085  146 ILE A O    
1466 O  O    B ILE A 145 ? 0.0864 0.0314 0.0696 -0.0006 -0.0211 -0.0137 146 ILE A O    
1467 C  CB   A ILE A 145 ? 0.0529 0.0485 0.0694 0.0038  0.0293  0.0034  146 ILE A CB   
1468 C  CB   B ILE A 145 ? 0.0634 0.0266 0.0541 -0.0069 0.0138  -0.0020 146 ILE A CB   
1469 C  CG1  A ILE A 145 ? 0.0721 0.0960 0.0539 0.0335  0.0307  0.0024  146 ILE A CG1  
1470 C  CG1  B ILE A 145 ? 0.0730 0.0543 0.0570 0.0104  0.0285  -0.0046 146 ILE A CG1  
1471 C  CG2  A ILE A 145 ? 0.0626 0.0421 0.1115 -0.0178 0.0219  -0.0205 146 ILE A CG2  
1472 C  CG2  B ILE A 145 ? 0.0476 0.0967 0.0615 -0.0012 -0.0015 0.0233  146 ILE A CG2  
1473 C  CD1  A ILE A 145 ? 0.0755 0.0675 0.0597 0.0258  0.0161  0.0214  146 ILE A CD1  
1474 C  CD1  B ILE A 145 ? 0.0680 0.0313 0.1044 0.0104  -0.0059 -0.0065 146 ILE A CD1  
1475 N  N    . PHE A 146 ? 0.1093 0.0380 0.0667 0.0000  -0.0087 -0.0012 147 PHE A N    
1476 C  CA   . PHE A 146 ? 0.0997 0.0327 0.0748 0.0041  -0.0130 0.0102  147 PHE A CA   
1477 C  C    . PHE A 146 ? 0.0938 0.0359 0.0926 -0.0041 -0.0020 -0.0027 147 PHE A C    
1478 O  O    . PHE A 146 ? 0.1181 0.0450 0.0863 -0.0020 -0.0137 -0.0096 147 PHE A O    
1479 C  CB   . PHE A 146 ? 0.1023 0.0353 0.0784 -0.0046 -0.0126 0.0003  147 PHE A CB   
1480 C  CG   . PHE A 146 ? 0.0809 0.0285 0.0753 0.0006  -0.0077 0.0125  147 PHE A CG   
1481 C  CD1  . PHE A 146 ? 0.1221 0.0372 0.0599 0.0119  -0.0147 0.0035  147 PHE A CD1  
1482 C  CD2  . PHE A 146 ? 0.1000 0.0486 0.0793 -0.0023 -0.0181 0.0102  147 PHE A CD2  
1483 C  CE1  . PHE A 146 ? 0.1028 0.0491 0.0953 0.0054  -0.0236 0.0054  147 PHE A CE1  
1484 C  CE2  . PHE A 146 ? 0.0917 0.0503 0.0915 -0.0043 0.0137  0.0109  147 PHE A CE2  
1485 C  CZ   . PHE A 146 ? 0.1324 0.0327 0.0645 0.0130  -0.0130 -0.0013 147 PHE A CZ   
1486 N  N    . LEU A 147 ? 0.1026 0.0380 0.0860 -0.0043 -0.0017 0.0097  148 LEU A N    
1487 C  CA   . LEU A 147 ? 0.1163 0.0397 0.0721 -0.0071 -0.0296 -0.0087 148 LEU A CA   
1488 C  C    . LEU A 147 ? 0.1098 0.0392 0.0791 0.0037  -0.0200 0.0012  148 LEU A C    
1489 O  O    . LEU A 147 ? 0.1159 0.0401 0.0904 -0.0043 -0.0076 0.0098  148 LEU A O    
1490 C  CB   . LEU A 147 ? 0.1367 0.0518 0.0766 -0.0088 -0.0232 0.0031  148 LEU A CB   
1491 C  CG   . LEU A 147 ? 0.1648 0.0402 0.1040 -0.0121 -0.0401 -0.0087 148 LEU A CG   
1492 C  CD1  . LEU A 147 ? 0.1957 0.0379 0.0930 -0.0070 -0.0427 -0.0041 148 LEU A CD1  
1493 C  CD2  . LEU A 147 ? 0.1987 0.0622 0.0631 -0.0181 -0.0187 0.0040  148 LEU A CD2  
1494 N  N    . LYS A 148 ? 0.1127 0.0314 0.1062 -0.0093 -0.0192 -0.0051 149 LYS A N    
1495 C  CA   . LYS A 148 ? 0.1452 0.0359 0.0924 -0.0003 -0.0110 -0.0017 149 LYS A CA   
1496 C  C    . LYS A 148 ? 0.1283 0.0428 0.1161 0.0074  -0.0060 0.0063  149 LYS A C    
1497 O  O    . LYS A 148 ? 0.1620 0.0518 0.1054 0.0186  -0.0310 -0.0059 149 LYS A O    
1498 C  CB   . LYS A 148 ? 0.1576 0.0662 0.0895 -0.0153 -0.0302 0.0006  149 LYS A CB   
1499 C  CG   . LYS A 148 ? 0.1639 0.0870 0.1356 -0.0337 0.0034  0.0285  149 LYS A CG   
1500 C  CD   . LYS A 148 ? 0.1834 0.1377 0.2220 -0.0120 0.0043  0.0296  149 LYS A CD   
1501 C  CE   . LYS A 148 ? 0.2666 0.2867 0.2610 -0.0557 0.0467  0.0582  149 LYS A CE   
1502 N  NZ   . LYS A 148 ? 0.3443 0.3722 0.3018 -0.1298 0.0570  0.0979  149 LYS A NZ   
1503 N  N    . VAL A 149 ? 0.1454 0.0520 0.1120 0.0091  -0.0344 -0.0038 150 VAL A N    
1504 C  CA   . VAL A 149 ? 0.1391 0.0467 0.1039 -0.0013 -0.0237 -0.0102 150 VAL A CA   
1505 C  C    . VAL A 149 ? 0.1659 0.0502 0.1098 -0.0003 -0.0187 0.0003  150 VAL A C    
1506 O  O    . VAL A 149 ? 0.1796 0.0653 0.1277 -0.0097 -0.0344 0.0060  150 VAL A O    
1507 C  CB   . VAL A 149 ? 0.1680 0.0553 0.1082 0.0060  -0.0227 -0.0065 150 VAL A CB   
1508 C  CG1  . VAL A 149 ? 0.1748 0.1127 0.1328 0.0000  -0.0215 -0.0359 150 VAL A CG1  
1509 C  CG2  . VAL A 149 ? 0.1474 0.0933 0.1581 -0.0060 -0.0024 0.0097  150 VAL A CG2  
1510 N  N    . GLY A 150 ? 0.1423 0.0649 0.1252 -0.0120 -0.0401 0.0130  151 GLY A N    
1511 C  CA   . GLY A 150 ? 0.1732 0.0802 0.1222 -0.0270 -0.0339 0.0108  151 GLY A CA   
1512 C  C    . GLY A 150 ? 0.1739 0.0626 0.1337 -0.0397 -0.0359 0.0186  151 GLY A C    
1513 O  O    . GLY A 150 ? 0.1974 0.0718 0.1254 -0.0296 -0.0305 0.0013  151 GLY A O    
1514 N  N    A SER A 151 ? 0.1703 0.1057 0.1249 -0.0181 -0.0370 0.0024  152 SER A N    
1515 N  N    B SER A 151 ? 0.1640 0.0888 0.1307 -0.0276 -0.0399 -0.0082 152 SER A N    
1516 C  CA   A SER A 151 ? 0.1845 0.0913 0.1502 -0.0110 -0.0342 -0.0093 152 SER A CA   
1517 C  CA   B SER A 151 ? 0.1732 0.0617 0.1456 -0.0280 -0.0408 -0.0197 152 SER A CA   
1518 C  C    A SER A 151 ? 0.1933 0.0775 0.1392 -0.0115 -0.0359 -0.0171 152 SER A C    
1519 C  C    B SER A 151 ? 0.1894 0.0631 0.1349 -0.0120 -0.0419 -0.0167 152 SER A C    
1520 O  O    A SER A 151 ? 0.1771 0.0978 0.1326 -0.0129 -0.0355 -0.0333 152 SER A O    
1521 O  O    B SER A 151 ? 0.1809 0.0577 0.1222 -0.0187 -0.0241 -0.0109 152 SER A O    
1522 C  CB   A SER A 151 ? 0.2025 0.1369 0.1822 -0.0225 -0.0326 -0.0071 152 SER A CB   
1523 C  CB   B SER A 151 ? 0.2039 0.0958 0.1917 -0.0228 -0.0348 -0.0208 152 SER A CB   
1524 O  OG   A SER A 151 ? 0.2285 0.1823 0.2479 -0.0098 -0.0346 -0.0388 152 SER A OG   
1525 O  OG   B SER A 151 ? 0.1915 0.1673 0.2393 -0.0177 -0.0219 0.0494  152 SER A OG   
1526 N  N    . ALA A 152 ? 0.1867 0.0876 0.1301 -0.0062 -0.0516 -0.0242 153 ALA A N    
1527 C  CA   . ALA A 152 ? 0.1993 0.0644 0.1407 0.0046  -0.0375 -0.0166 153 ALA A CA   
1528 C  C    . ALA A 152 ? 0.2213 0.1023 0.1247 0.0156  -0.0447 -0.0010 153 ALA A C    
1529 O  O    . ALA A 152 ? 0.2400 0.0794 0.1750 0.0046  -0.0425 -0.0208 153 ALA A O    
1530 C  CB   . ALA A 152 ? 0.2520 0.1252 0.1084 0.0243  -0.0441 -0.0274 153 ALA A CB   
1531 N  N    . LYS A 153 ? 0.2127 0.0640 0.1333 0.0013  -0.0467 -0.0031 154 LYS A N    
1532 C  CA   . LYS A 153 ? 0.2236 0.0705 0.1369 0.0231  -0.0434 -0.0114 154 LYS A CA   
1533 C  C    . LYS A 153 ? 0.2183 0.0658 0.1306 0.0254  -0.0485 -0.0183 154 LYS A C    
1534 O  O    . LYS A 153 ? 0.2269 0.0719 0.1168 0.0104  -0.0675 -0.0125 154 LYS A O    
1535 C  CB   . LYS A 153 ? 0.2477 0.0671 0.1306 0.0057  -0.0715 0.0012  154 LYS A CB   
1536 C  CG   . LYS A 153 ? 0.3199 0.0586 0.1720 0.0154  -0.0859 -0.0051 154 LYS A CG   
1537 C  CD   . LYS A 153 ? 0.3152 0.0468 0.1687 0.0248  -0.0753 -0.0461 154 LYS A CD   
1538 C  CE   . LYS A 153 ? 0.4192 0.1190 0.1430 0.0542  -0.0662 -0.0456 154 LYS A CE   
1539 N  NZ   . LYS A 153 ? 0.4056 0.0956 0.2220 0.0253  -0.0274 -0.0820 154 LYS A NZ   
1540 N  N    A PRO A 154 ? 0.2181 0.0554 0.1423 0.0120  -0.0533 -0.0097 155 PRO A N    
1541 N  N    B PRO A 154 ? 0.2193 0.1177 0.1455 0.0182  -0.0401 -0.0030 155 PRO A N    
1542 C  CA   A PRO A 154 ? 0.1660 0.0931 0.1351 0.0043  -0.0197 -0.0073 155 PRO A CA   
1543 C  CA   B PRO A 154 ? 0.1739 0.1123 0.1154 -0.0031 -0.0344 -0.0209 155 PRO A CA   
1544 C  C    A PRO A 154 ? 0.1184 0.0969 0.1155 0.0027  -0.0137 0.0082  155 PRO A C    
1545 C  C    B PRO A 154 ? 0.1395 0.1301 0.1005 0.0010  -0.0370 0.0000  155 PRO A C    
1546 O  O    A PRO A 154 ? 0.1039 0.1286 0.1305 0.0197  -0.0208 0.0120  155 PRO A O    
1547 O  O    B PRO A 154 ? 0.1477 0.1378 0.0933 0.0057  -0.0219 -0.0080 155 PRO A O    
1548 C  CB   A PRO A 154 ? 0.1306 0.1046 0.1861 -0.0276 0.0074  0.0173  155 PRO A CB   
1549 C  CB   B PRO A 154 ? 0.2027 0.1272 0.1000 0.0054  -0.0152 0.0076  155 PRO A CB   
1550 C  CG   A PRO A 154 ? 0.1863 0.1299 0.1507 -0.0049 -0.0142 0.0155  155 PRO A CG   
1551 C  CG   B PRO A 154 ? 0.1881 0.1398 0.1790 0.0280  -0.0310 0.0098  155 PRO A CG   
1552 C  CD   A PRO A 154 ? 0.2375 0.0996 0.1203 0.0210  -0.0305 -0.0272 155 PRO A CD   
1553 C  CD   B PRO A 154 ? 0.2290 0.1544 0.1626 0.0093  -0.0414 -0.0065 155 PRO A CD   
1554 N  N    A GLY A 155 ? 0.0915 0.0741 0.1062 -0.0013 -0.0003 -0.0012 156 GLY A N    
1555 N  N    B GLY A 155 ? 0.1233 0.0645 0.1127 0.0015  -0.0104 -0.0010 156 GLY A N    
1556 C  CA   A GLY A 155 ? 0.1109 0.0847 0.1339 -0.0070 0.0131  -0.0010 156 GLY A CA   
1557 C  CA   B GLY A 155 ? 0.1313 0.0614 0.1483 0.0060  -0.0060 0.0082  156 GLY A CA   
1558 C  C    A GLY A 155 ? 0.0850 0.0807 0.1199 -0.0037 0.0137  0.0104  156 GLY A C    
1559 C  C    B GLY A 155 ? 0.1233 0.0780 0.1405 -0.0098 -0.0091 -0.0031 156 GLY A C    
1560 O  O    A GLY A 155 ? 0.0908 0.0753 0.2206 -0.0006 0.0351  0.0154  156 GLY A O    
1561 O  O    B GLY A 155 ? 0.1203 0.0940 0.1791 -0.0015 0.0015  0.0434  156 GLY A O    
1562 N  N    A LEU A 156 ? 0.0832 0.0651 0.1003 -0.0087 0.0104  0.0017  157 LEU A N    
1563 N  N    B LEU A 156 ? 0.1188 0.0671 0.0922 -0.0085 -0.0215 0.0027  157 LEU A N    
1564 C  CA   A LEU A 156 ? 0.0863 0.0627 0.0886 -0.0065 -0.0010 -0.0054 157 LEU A CA   
1565 C  CA   B LEU A 156 ? 0.1316 0.0597 0.0992 -0.0006 -0.0115 -0.0074 157 LEU A CA   
1566 C  C    A LEU A 156 ? 0.0917 0.0420 0.0939 -0.0076 -0.0074 -0.0153 157 LEU A C    
1567 C  C    B LEU A 156 ? 0.1263 0.0763 0.1134 -0.0019 -0.0087 -0.0037 157 LEU A C    
1568 O  O    A LEU A 156 ? 0.1055 0.0687 0.0714 -0.0143 -0.0096 0.0087  157 LEU A O    
1569 O  O    B LEU A 156 ? 0.1037 0.0938 0.0864 -0.0104 -0.0109 0.0017  157 LEU A O    
1570 C  CB   A LEU A 156 ? 0.0915 0.0714 0.1193 -0.0046 0.0031  -0.0024 157 LEU A CB   
1571 C  CB   B LEU A 156 ? 0.1321 0.0917 0.0603 -0.0087 0.0007  -0.0175 157 LEU A CB   
1572 C  CG   A LEU A 156 ? 0.0861 0.1014 0.1046 0.0031  0.0000  -0.0059 157 LEU A CG   
1573 C  CG   B LEU A 156 ? 0.1154 0.1100 0.0811 -0.0197 -0.0171 0.0087  157 LEU A CG   
1574 C  CD1  A LEU A 156 ? 0.1221 0.1224 0.0987 -0.0298 0.0118  -0.0207 157 LEU A CD1  
1575 C  CD1  B LEU A 156 ? 0.1199 0.0931 0.0996 -0.0215 -0.0272 -0.0226 157 LEU A CD1  
1576 C  CD2  A LEU A 156 ? 0.0784 0.1014 0.1172 0.0006  -0.0331 -0.0228 157 LEU A CD2  
1577 C  CD2  B LEU A 156 ? 0.1075 0.0838 0.1249 0.0091  -0.0052 -0.0098 157 LEU A CD2  
1578 N  N    A GLN A 157 ? 0.0949 0.0724 0.0870 -0.0160 -0.0175 -0.0120 158 GLN A N    
1579 N  N    B GLN A 157 ? 0.1289 0.0872 0.0920 -0.0153 -0.0085 -0.0148 158 GLN A N    
1580 C  CA   A GLN A 157 ? 0.0877 0.0503 0.1005 -0.0003 -0.0082 -0.0051 158 GLN A CA   
1581 C  CA   B GLN A 157 ? 0.1136 0.0881 0.0797 -0.0131 -0.0077 -0.0293 158 GLN A CA   
1582 C  C    A GLN A 157 ? 0.0820 0.0590 0.1044 -0.0082 -0.0251 -0.0324 158 GLN A C    
1583 C  C    B GLN A 157 ? 0.1181 0.0908 0.0721 -0.0006 0.0024  -0.0184 158 GLN A C    
1584 O  O    A GLN A 157 ? 0.0705 0.0891 0.0912 -0.0048 -0.0086 -0.0281 158 GLN A O    
1585 O  O    B GLN A 157 ? 0.1023 0.1208 0.0859 -0.0142 -0.0087 -0.0077 158 GLN A O    
1586 C  CB   A GLN A 157 ? 0.0882 0.0897 0.1217 -0.0208 -0.0070 -0.0264 158 GLN A CB   
1587 C  CB   B GLN A 157 ? 0.1216 0.1064 0.1164 -0.0137 -0.0080 -0.0176 158 GLN A CB   
1588 C  CG   A GLN A 157 ? 0.1277 0.1213 0.0960 -0.0006 -0.0030 -0.0132 158 GLN A CG   
1589 C  CG   B GLN A 157 ? 0.1230 0.0753 0.1158 -0.0335 -0.0005 -0.0271 158 GLN A CG   
1590 C  CD   A GLN A 157 ? 0.1224 0.0732 0.0748 0.0000  -0.0020 0.0152  158 GLN A CD   
1591 C  CD   B GLN A 157 ? 0.1155 0.0410 0.0881 -0.0153 -0.0178 -0.0198 158 GLN A CD   
1592 O  OE1  A GLN A 157 ? 0.1195 0.0886 0.1010 -0.0059 0.0082  -0.0043 158 GLN A OE1  
1593 O  OE1  B GLN A 157 ? 0.1601 0.1420 0.1039 -0.0335 0.0007  -0.0188 158 GLN A OE1  
1594 N  NE2  A GLN A 157 ? 0.1448 0.1240 0.1132 -0.0419 -0.0161 -0.0728 158 GLN A NE2  
1595 N  NE2  B GLN A 157 ? 0.1107 0.0764 0.0744 0.0023  0.0194  -0.0121 158 GLN A NE2  
1596 N  N    A LYS A 158 ? 0.0712 0.0854 0.0992 -0.0059 -0.0031 0.0118  159 LYS A N    
1597 N  N    B LYS A 158 ? 0.1344 0.1152 0.0538 -0.0007 -0.0030 -0.0043 159 LYS A N    
1598 C  CA   A LYS A 158 ? 0.1276 0.0881 0.1079 -0.0181 -0.0184 -0.0027 159 LYS A CA   
1599 C  CA   B LYS A 158 ? 0.1353 0.0909 0.0922 0.0081  -0.0060 0.0176  159 LYS A CA   
1600 C  C    A LYS A 158 ? 0.1247 0.0538 0.1102 -0.0007 -0.0057 0.0013  159 LYS A C    
1601 C  C    B LYS A 158 ? 0.1283 0.1067 0.0599 -0.0065 -0.0087 0.0027  159 LYS A C    
1602 O  O    A LYS A 158 ? 0.1447 0.1115 0.1014 -0.0146 -0.0010 -0.0143 159 LYS A O    
1603 O  O    B LYS A 158 ? 0.1581 0.1242 0.0793 -0.0113 -0.0230 0.0098  159 LYS A O    
1604 C  CB   A LYS A 158 ? 0.0976 0.1407 0.1224 -0.0110 -0.0340 0.0266  159 LYS A CB   
1605 C  CB   B LYS A 158 ? 0.1823 0.0836 0.1102 0.0216  0.0065  0.0401  159 LYS A CB   
1606 C  CG   A LYS A 158 ? 0.2036 0.1493 0.1655 -0.0052 -0.0248 0.0046  159 LYS A CG   
1607 C  CG   B LYS A 158 ? 0.2637 0.1416 0.1972 0.0472  -0.0132 0.0403  159 LYS A CG   
1608 C  CD   A LYS A 158 ? 0.2224 0.1486 0.2170 -0.0019 -0.0342 -0.0065 159 LYS A CD   
1609 C  CD   B LYS A 158 ? 0.3147 0.2612 0.2574 0.0254  -0.0024 -0.0337 159 LYS A CD   
1610 C  CE   A LYS A 158 ? 0.2307 0.2339 0.1768 -0.0216 -0.0359 0.0188  159 LYS A CE   
1611 C  CE   B LYS A 158 ? 0.2876 0.2319 0.2615 0.0114  -0.0071 -0.0328 159 LYS A CE   
1612 N  NZ   A LYS A 158 ? 0.3296 0.1107 0.1942 -0.0361 -0.0430 -0.0076 159 LYS A NZ   
1613 N  NZ   B LYS A 158 ? 0.3298 0.3242 0.2919 -0.0373 -0.0324 -0.0232 159 LYS A NZ   
1614 N  N    A VAL A 159 ? 0.1091 0.0709 0.0721 -0.0205 -0.0031 -0.0115 160 VAL A N    
1615 N  N    B VAL A 159 ? 0.1211 0.0948 0.0705 -0.0104 -0.0017 0.0173  160 VAL A N    
1616 C  CA   A VAL A 159 ? 0.1070 0.0658 0.0957 -0.0096 0.0020  0.0043  160 VAL A CA   
1617 C  CA   B VAL A 159 ? 0.1208 0.0789 0.0793 0.0027  -0.0131 -0.0049 160 VAL A CA   
1618 C  C    A VAL A 159 ? 0.0838 0.0869 0.0825 -0.0035 -0.0007 -0.0010 160 VAL A C    
1619 C  C    B VAL A 159 ? 0.1128 0.0590 0.0838 -0.0114 -0.0057 -0.0148 160 VAL A C    
1620 O  O    A VAL A 159 ? 0.1109 0.0803 0.0930 -0.0159 0.0035  -0.0041 160 VAL A O    
1621 O  O    B VAL A 159 ? 0.1323 0.0719 0.1045 -0.0003 -0.0241 -0.0166 160 VAL A O    
1622 C  CB   A VAL A 159 ? 0.1159 0.0504 0.1129 -0.0198 0.0006  -0.0226 160 VAL A CB   
1623 C  CB   B VAL A 159 ? 0.1124 0.0809 0.0988 0.0054  0.0023  0.0071  160 VAL A CB   
1624 C  CG1  A VAL A 159 ? 0.1145 0.0636 0.1290 0.0147  0.0073  -0.0040 160 VAL A CG1  
1625 C  CG1  B VAL A 159 ? 0.1337 0.1439 0.0933 0.0003  -0.0362 -0.0006 160 VAL A CG1  
1626 C  CG2  A VAL A 159 ? 0.1161 0.0764 0.1280 0.0013  0.0199  -0.0197 160 VAL A CG2  
1627 C  CG2  B VAL A 159 ? 0.1254 0.1317 0.0669 0.0322  -0.0207 -0.0124 160 VAL A CG2  
1628 N  N    A VAL A 160 ? 0.0790 0.0604 0.1023 -0.0126 -0.0003 -0.0137 161 VAL A N    
1629 N  N    B VAL A 160 ? 0.1225 0.0718 0.0624 0.0043  -0.0041 0.0000  161 VAL A N    
1630 C  CA   A VAL A 160 ? 0.1010 0.0865 0.1233 0.0082  -0.0087 -0.0104 161 VAL A CA   
1631 C  CA   B VAL A 160 ? 0.1353 0.0653 0.0845 0.0043  -0.0071 0.0015  161 VAL A CA   
1632 C  C    A VAL A 160 ? 0.1046 0.0709 0.0967 -0.0003 -0.0030 -0.0302 161 VAL A C    
1633 C  C    B VAL A 160 ? 0.1357 0.0579 0.0960 -0.0035 -0.0219 0.0000  161 VAL A C    
1634 O  O    A VAL A 160 ? 0.0935 0.0952 0.1304 -0.0015 -0.0046 -0.0318 161 VAL A O    
1635 O  O    B VAL A 160 ? 0.1256 0.0888 0.1048 -0.0221 -0.0126 -0.0107 161 VAL A O    
1636 C  CB   A VAL A 160 ? 0.1362 0.0908 0.1045 0.0070  -0.0172 -0.0280 161 VAL A CB   
1637 C  CB   B VAL A 160 ? 0.1922 0.0714 0.1572 0.0252  0.0037  0.0136  161 VAL A CB   
1638 C  CG1  A VAL A 160 ? 0.1468 0.0976 0.1649 -0.0012 -0.0057 -0.0206 161 VAL A CG1  
1639 C  CG1  B VAL A 160 ? 0.1400 0.1172 0.1877 -0.0027 0.0166  -0.0003 161 VAL A CG1  
1640 C  CG2  A VAL A 160 ? 0.1344 0.0362 0.1407 0.0076  -0.0274 0.0048  161 VAL A CG2  
1641 C  CG2  B VAL A 160 ? 0.2301 0.1754 0.1508 0.0425  0.0414  0.0315  161 VAL A CG2  
1642 N  N    A ASP A 161 ? 0.1073 0.1018 0.0960 -0.0200 -0.0093 -0.0189 162 ASP A N    
1643 N  N    B ASP A 161 ? 0.1470 0.0888 0.0750 -0.0187 -0.0185 -0.0043 162 ASP A N    
1644 C  CA   A ASP A 161 ? 0.1154 0.1328 0.0723 -0.0153 -0.0171 -0.0403 162 ASP A CA   
1645 C  CA   B ASP A 161 ? 0.1401 0.1188 0.1061 -0.0208 -0.0368 -0.0263 162 ASP A CA   
1646 C  C    A ASP A 161 ? 0.1538 0.1563 0.0556 -0.0048 -0.0233 -0.0200 162 ASP A C    
1647 C  C    B ASP A 161 ? 0.1392 0.1482 0.1197 -0.0210 -0.0281 0.0000  162 ASP A C    
1648 O  O    A ASP A 161 ? 0.2102 0.2070 0.0845 -0.0225 -0.0003 -0.0200 162 ASP A O    
1649 O  O    B ASP A 161 ? 0.1748 0.1646 0.1797 -0.0284 -0.0037 -0.0065 162 ASP A O    
1650 C  CB   A ASP A 161 ? 0.1414 0.1739 0.0845 -0.0185 -0.0088 -0.0357 162 ASP A CB   
1651 C  CB   B ASP A 161 ? 0.1438 0.1301 0.1436 -0.0262 -0.0270 -0.0252 162 ASP A CB   
1652 C  CG   A ASP A 161 ? 0.1369 0.1947 0.1215 -0.0240 -0.0137 -0.0130 162 ASP A CG   
1653 C  CG   B ASP A 161 ? 0.1490 0.1085 0.1149 -0.0197 -0.0120 0.0120  162 ASP A CG   
1654 O  OD1  A ASP A 161 ? 0.1709 0.1456 0.2229 -0.0467 -0.0143 -0.0040 162 ASP A OD1  
1655 O  OD1  B ASP A 161 ? 0.1836 0.1641 0.1332 -0.0439 -0.0226 -0.0357 162 ASP A OD1  
1656 O  OD2  A ASP A 161 ? 0.1298 0.2723 0.1642 -0.0513 -0.0359 -0.0494 162 ASP A OD2  
1657 O  OD2  B ASP A 161 ? 0.1664 0.1330 0.1527 -0.0394 -0.0344 -0.0549 162 ASP A OD2  
1658 N  N    A VAL A 162 ? 0.1136 0.0944 0.0838 -0.0049 -0.0048 -0.0093 163 VAL A N    
1659 N  N    B VAL A 162 ? 0.1332 0.1301 0.0958 -0.0182 -0.0263 0.0088  163 VAL A N    
1660 C  CA   A VAL A 162 ? 0.1023 0.0992 0.0741 0.0059  -0.0115 0.0087  163 VAL A CA   
1661 C  CA   B VAL A 162 ? 0.1545 0.1360 0.1053 -0.0082 -0.0296 0.0303  163 VAL A CA   
1662 C  C    A VAL A 162 ? 0.0974 0.0809 0.1111 -0.0126 -0.0065 0.0026  163 VAL A C    
1663 C  C    B VAL A 162 ? 0.1401 0.0985 0.0895 -0.0024 -0.0181 0.0000  163 VAL A C    
1664 O  O    A VAL A 162 ? 0.1240 0.0809 0.0987 -0.0070 -0.0048 0.0065  163 VAL A O    
1665 O  O    B VAL A 162 ? 0.1586 0.1084 0.1155 -0.0280 0.0120  0.0135  163 VAL A O    
1666 C  CB   A VAL A 162 ? 0.0983 0.1088 0.1493 0.0017  0.0148  -0.0052 163 VAL A CB   
1667 C  CB   B VAL A 162 ? 0.1583 0.0974 0.1985 0.0225  -0.0355 0.0504  163 VAL A CB   
1668 C  CG1  A VAL A 162 ? 0.1445 0.0639 0.1143 -0.0200 -0.0152 -0.0098 163 VAL A CG1  
1669 C  CG1  B VAL A 162 ? 0.1658 0.0930 0.1648 -0.0104 0.0006  0.0313  163 VAL A CG1  
1670 C  CG2  A VAL A 162 ? 0.1335 0.1484 0.1143 0.0035  -0.0118 0.0359  163 VAL A CG2  
1671 C  CG2  B VAL A 162 ? 0.1957 0.1893 0.1849 -0.0164 0.0005  0.0126  163 VAL A CG2  
1672 N  N    A LEU A 163 ? 0.1107 0.0807 0.1039 -0.0006 -0.0163 0.0115  164 LEU A N    
1673 N  N    B LEU A 163 ? 0.1378 0.1005 0.0956 -0.0232 -0.0141 0.0222  164 LEU A N    
1674 C  CA   A LEU A 163 ? 0.1154 0.0915 0.0870 -0.0052 -0.0076 0.0043  164 LEU A CA   
1675 C  CA   B LEU A 163 ? 0.1447 0.0812 0.0922 -0.0057 -0.0252 0.0034  164 LEU A CA   
1676 C  C    A LEU A 163 ? 0.1292 0.0856 0.0845 0.0035  -0.0137 -0.0026 164 LEU A C    
1677 C  C    B LEU A 163 ? 0.1531 0.0952 0.0915 -0.0241 -0.0185 -0.0051 164 LEU A C    
1678 O  O    A LEU A 163 ? 0.1053 0.0935 0.0931 0.0043  -0.0194 0.0114  164 LEU A O    
1679 O  O    B LEU A 163 ? 0.1590 0.1008 0.0908 -0.0019 -0.0386 0.0177  164 LEU A O    
1680 C  CB   A LEU A 163 ? 0.0967 0.0793 0.1111 0.0052  0.0041  0.0017  164 LEU A CB   
1681 C  CB   B LEU A 163 ? 0.1231 0.0816 0.0931 0.0026  -0.0065 0.0153  164 LEU A CB   
1682 C  CG   A LEU A 163 ? 0.1155 0.0718 0.0732 0.0005  -0.0065 0.0052  164 LEU A CG   
1683 C  CG   B LEU A 163 ? 0.1037 0.0856 0.0978 -0.0003 -0.0027 0.0017  164 LEU A CG   
1684 C  CD1  A LEU A 163 ? 0.1111 0.0666 0.1254 -0.0023 -0.0051 0.0040  164 LEU A CD1  
1685 C  CD1  B LEU A 163 ? 0.1660 0.0930 0.0969 0.0065  -0.0131 0.0390  164 LEU A CD1  
1686 C  CD2  A LEU A 163 ? 0.1039 0.1005 0.1190 -0.0104 -0.0048 0.0020  164 LEU A CD2  
1687 C  CD2  B LEU A 163 ? 0.1773 0.0906 0.0780 -0.0154 -0.0099 -0.0054 164 LEU A CD2  
1688 N  N    A ASP A 164 ? 0.1362 0.0982 0.0865 -0.0092 -0.0148 -0.0185 165 ASP A N    
1689 N  N    B ASP A 164 ? 0.1928 0.0992 0.0951 -0.0277 -0.0198 -0.0097 165 ASP A N    
1690 C  CA   A ASP A 164 ? 0.1544 0.1356 0.1014 -0.0137 -0.0076 -0.0148 165 ASP A CA   
1691 C  CA   B ASP A 164 ? 0.1892 0.1037 0.1371 -0.0156 0.0030  -0.0273 165 ASP A CA   
1692 C  C    A ASP A 164 ? 0.1466 0.1328 0.0633 -0.0216 0.0027  -0.0076 165 ASP A C    
1693 C  C    B ASP A 164 ? 0.1926 0.1305 0.0951 -0.0059 -0.0173 -0.0034 165 ASP A C    
1694 O  O    A ASP A 164 ? 0.2057 0.1495 0.1061 -0.0186 0.0118  -0.0272 165 ASP A O    
1695 O  O    B ASP A 164 ? 0.2249 0.1640 0.1723 -0.0153 0.0263  -0.0041 165 ASP A O    
1696 C  CB   A ASP A 164 ? 0.1694 0.1597 0.1107 -0.0041 0.0054  -0.0263 165 ASP A CB   
1697 C  CB   B ASP A 164 ? 0.2276 0.1018 0.1657 -0.0104 -0.0109 -0.0259 165 ASP A CB   
1698 C  CG   A ASP A 164 ? 0.2299 0.2869 0.1820 0.0031  -0.0043 0.0097  165 ASP A CG   
1699 C  CG   B ASP A 164 ? 0.2290 0.1826 0.1650 -0.0208 -0.0071 -0.0155 165 ASP A CG   
1700 O  OD1  A ASP A 164 ? 0.3048 0.2994 0.2222 0.0454  -0.0243 0.0416  165 ASP A OD1  
1701 O  OD1  B ASP A 164 ? 0.2039 0.3131 0.1421 -0.0043 -0.0348 -0.0350 165 ASP A OD1  
1702 O  OD2  A ASP A 164 ? 0.2657 0.3413 0.1969 0.0228  -0.0549 0.0013  165 ASP A OD2  
1703 O  OD2  B ASP A 164 ? 0.2978 0.3377 0.2224 -0.0241 0.0335  0.0104  165 ASP A OD2  
1704 N  N    A SER A 165 ? 0.1346 0.1601 0.0649 -0.0231 -0.0152 0.0126  166 SER A N    
1705 N  N    B SER A 165 ? 0.1771 0.1154 0.0982 -0.0261 -0.0065 0.0114  166 SER A N    
1706 C  CA   A SER A 165 ? 0.1312 0.1233 0.0906 0.0049  0.0000  0.0252  166 SER A CA   
1707 C  CA   B SER A 165 ? 0.1646 0.1286 0.1001 -0.0222 0.0054  0.0225  166 SER A CA   
1708 C  C    A SER A 165 ? 0.1179 0.1150 0.0703 -0.0006 -0.0167 0.0192  166 SER A C    
1709 C  C    B SER A 165 ? 0.1674 0.0952 0.0913 -0.0164 0.0052  0.0126  166 SER A C    
1710 O  O    A SER A 165 ? 0.1337 0.0996 0.0820 -0.0196 -0.0197 0.0307  166 SER A O    
1711 O  O    B SER A 165 ? 0.1637 0.1061 0.1199 -0.0030 0.0068  0.0236  166 SER A O    
1712 C  CB   A SER A 165 ? 0.1513 0.1639 0.1136 -0.0057 0.0148  0.0151  166 SER A CB   
1713 C  CB   B SER A 165 ? 0.1666 0.1394 0.1268 -0.0091 -0.0081 0.0086  166 SER A CB   
1714 O  OG   A SER A 165 ? 0.1506 0.1335 0.1452 0.0000  -0.0373 0.0052  166 SER A OG   
1715 O  OG   B SER A 165 ? 0.1899 0.1299 0.1276 -0.0065 -0.0120 0.0186  166 SER A OG   
1716 N  N    A ILE A 166 ? 0.1057 0.0888 0.0764 0.0063  0.0006  0.0170  167 ILE A N    
1717 N  N    B ILE A 166 ? 0.1481 0.1152 0.0784 0.0013  -0.0071 0.0120  167 ILE A N    
1718 C  CA   A ILE A 166 ? 0.0909 0.0863 0.0732 0.0071  0.0006  0.0185  167 ILE A CA   
1719 C  CA   B ILE A 166 ? 0.1500 0.0890 0.0973 -0.0038 -0.0087 0.0027  167 ILE A CA   
1720 C  C    A ILE A 166 ? 0.0861 0.0820 0.0559 0.0098  0.0131  0.0020  167 ILE A C    
1721 C  C    B ILE A 166 ? 0.1599 0.0800 0.0965 0.0006  -0.0130 0.0164  167 ILE A C    
1722 O  O    A ILE A 166 ? 0.1000 0.0645 0.0582 0.0087  0.0038  0.0174  167 ILE A O    
1723 O  O    B ILE A 166 ? 0.1437 0.0856 0.0956 0.0135  -0.0156 0.0031  167 ILE A O    
1724 C  CB   A ILE A 166 ? 0.1032 0.0562 0.0886 -0.0148 -0.0184 0.0085  167 ILE A CB   
1725 C  CB   B ILE A 166 ? 0.1432 0.0784 0.0854 -0.0010 -0.0027 0.0080  167 ILE A CB   
1726 C  CG1  A ILE A 166 ? 0.0680 0.0811 0.0741 0.0136  -0.0010 0.0051  167 ILE A CG1  
1727 C  CG1  B ILE A 166 ? 0.1448 0.0766 0.0705 0.0015  -0.0109 -0.0073 167 ILE A CG1  
1728 C  CG2  A ILE A 166 ? 0.0994 0.0983 0.1082 0.0353  -0.0214 0.0052  167 ILE A CG2  
1729 C  CG2  B ILE A 166 ? 0.1669 0.0985 0.1067 0.0087  -0.0082 -0.0504 167 ILE A CG2  
1730 C  CD1  A ILE A 166 ? 0.1030 0.1044 0.0811 0.0006  -0.0051 -0.0027 167 ILE A CD1  
1731 C  CD1  B ILE A 166 ? 0.1418 0.0775 0.0926 -0.0006 0.0131  0.0000  167 ILE A CD1  
1732 N  N    A LYS A 167 ? 0.1046 0.0895 0.0556 0.0000  -0.0010 0.0065  168 LYS A N    
1733 N  N    B LYS A 167 ? 0.1737 0.1132 0.0935 0.0110  0.0000  -0.0114 168 LYS A N    
1734 C  CA   A LYS A 167 ? 0.0967 0.0807 0.0669 0.0108  0.0147  -0.0027 168 LYS A CA   
1735 C  CA   B LYS A 167 ? 0.1696 0.1360 0.0966 0.0124  0.0015  -0.0118 168 LYS A CA   
1736 C  C    A LYS A 167 ? 0.0924 0.0886 0.0578 0.0114  0.0184  0.0119  168 LYS A C    
1737 C  C    B LYS A 167 ? 0.1660 0.1197 0.0527 0.0125  0.0266  -0.0186 168 LYS A C    
1738 O  O    A LYS A 167 ? 0.1091 0.0671 0.0545 0.0093  0.0048  0.0098  168 LYS A O    
1739 O  O    B LYS A 167 ? 0.1475 0.1026 0.0940 0.0003  0.0114  -0.0147 168 LYS A O    
1740 C  CB   A LYS A 167 ? 0.1161 0.0926 0.0806 -0.0054 -0.0192 -0.0280 168 LYS A CB   
1741 C  CB   B LYS A 167 ? 0.1924 0.1158 0.0881 0.0238  0.0037  -0.0366 168 LYS A CB   
1742 C  CG   A LYS A 167 ? 0.1532 0.0915 0.1045 0.0070  -0.0211 0.0062  168 LYS A CG   
1743 C  CG   B LYS A 167 ? 0.1804 0.1511 0.0926 0.0208  -0.0237 -0.0208 168 LYS A CG   
1744 C  CD   A LYS A 167 ? 0.1865 0.1100 0.1913 0.0142  -0.0130 -0.0304 168 LYS A CD   
1745 C  CD   B LYS A 167 ? 0.2127 0.1518 0.1572 0.0187  -0.0170 -0.0423 168 LYS A CD   
1746 C  CE   A LYS A 167 ? 0.2824 0.1613 0.2294 0.0162  -0.0081 -0.0423 168 LYS A CE   
1747 C  CE   B LYS A 167 ? 0.2630 0.2210 0.1784 0.0214  -0.0065 -0.0194 168 LYS A CE   
1748 N  NZ   A LYS A 167 ? 0.2594 0.1635 0.2167 -0.0209 0.0183  -0.1045 168 LYS A NZ   
1749 N  NZ   B LYS A 167 ? 0.3461 0.2901 0.1926 0.0198  -0.0119 -0.0518 168 LYS A NZ   
1750 N  N    A THR A 168 ? 0.1009 0.0624 0.0773 0.0161  0.0175  0.0093  169 THR A N    
1751 N  N    B THR A 168 ? 0.1617 0.1247 0.0881 -0.0140 0.0252  -0.0035 169 THR A N    
1752 C  CA   A THR A 168 ? 0.1021 0.0845 0.0827 0.0046  0.0184  0.0091  169 THR A CA   
1753 C  CA   B THR A 168 ? 0.1665 0.1283 0.0922 -0.0003 0.0086  0.0081  169 THR A CA   
1754 C  C    A THR A 168 ? 0.0992 0.0741 0.0635 -0.0027 0.0185  0.0148  169 THR A C    
1755 C  C    B THR A 168 ? 0.1504 0.1114 0.0917 -0.0049 0.0148  0.0215  169 THR A C    
1756 O  O    A THR A 168 ? 0.0895 0.0665 0.0904 0.0043  0.0176  0.0115  169 THR A O    
1757 O  O    B THR A 168 ? 0.1489 0.0870 0.1145 -0.0208 0.0118  0.0071  169 THR A O    
1758 C  CB   A THR A 168 ? 0.1049 0.0886 0.1118 0.0251  0.0153  0.0086  169 THR A CB   
1759 C  CB   B THR A 168 ? 0.1691 0.1176 0.1049 0.0065  0.0423  0.0015  169 THR A CB   
1760 O  OG1  A THR A 168 ? 0.1262 0.0881 0.0895 0.0221  0.0068  0.0059  169 THR A OG1  
1761 O  OG1  B THR A 168 ? 0.2145 0.1369 0.1136 0.0313  0.0136  -0.0043 169 THR A OG1  
1762 C  CG2  A THR A 168 ? 0.1216 0.0944 0.0988 0.0163  0.0359  0.0129  169 THR A CG2  
1763 C  CG2  B THR A 168 ? 0.2298 0.1184 0.1181 0.0305  0.0054  -0.0200 169 THR A CG2  
1764 N  N    A LYS A 169 ? 0.1120 0.0818 0.0863 -0.0027 -0.0013 0.0120  170 LYS A N    
1765 N  N    B LYS A 169 ? 0.1517 0.0976 0.1084 -0.0052 0.0076  -0.0037 170 LYS A N    
1766 C  CA   A LYS A 169 ? 0.0856 0.0827 0.0903 0.0054  0.0031  0.0165  170 LYS A CA   
1767 C  CA   B LYS A 169 ? 0.1493 0.1146 0.1032 -0.0148 0.0086  0.0020  170 LYS A CA   
1768 C  C    A LYS A 169 ? 0.1125 0.0775 0.0757 0.0000  -0.0054 0.0071  170 LYS A C    
1769 C  C    B LYS A 169 ? 0.1614 0.0985 0.1206 -0.0031 0.0182  0.0006  170 LYS A C    
1770 O  O    A LYS A 169 ? 0.1136 0.1109 0.0755 0.0063  0.0239  0.0271  170 LYS A O    
1771 O  O    B LYS A 169 ? 0.1793 0.1274 0.1432 0.0038  0.0577  0.0040  170 LYS A O    
1772 C  CB   A LYS A 169 ? 0.0926 0.0784 0.0949 -0.0043 -0.0003 0.0013  170 LYS A CB   
1773 C  CB   B LYS A 169 ? 0.1628 0.1168 0.0917 -0.0065 0.0048  -0.0097 170 LYS A CB   
1774 C  CG   A LYS A 169 ? 0.1233 0.1109 0.0982 0.0024  -0.0096 0.0153  170 LYS A CG   
1775 C  CG   B LYS A 169 ? 0.1508 0.1369 0.1376 -0.0210 -0.0043 0.0043  170 LYS A CG   
1776 C  CD   A LYS A 169 ? 0.1346 0.1335 0.1100 -0.0017 -0.0057 0.0399  170 LYS A CD   
1777 C  CD   B LYS A 169 ? 0.1373 0.1513 0.1524 -0.0254 -0.0148 -0.0197 170 LYS A CD   
1778 C  CE   A LYS A 169 ? 0.1429 0.2675 0.1692 -0.0126 -0.0119 0.0031  170 LYS A CE   
1779 C  CE   B LYS A 169 ? 0.2583 0.2303 0.2412 -0.0252 0.0260  0.0344  170 LYS A CE   
1780 N  NZ   A LYS A 169 ? 0.2073 0.2960 0.2605 0.0264  -0.0516 0.0207  170 LYS A NZ   
1781 N  NZ   B LYS A 169 ? 0.2014 0.3533 0.3425 -0.0395 0.0119  0.0012  170 LYS A NZ   
1782 N  N    A GLY A 170 ? 0.1001 0.0658 0.1048 -0.0012 0.0087  0.0102  171 GLY A N    
1783 N  N    B GLY A 170 ? 0.1243 0.0876 0.1040 -0.0098 0.0219  0.0194  171 GLY A N    
1784 C  CA   A GLY A 170 ? 0.1088 0.0572 0.1107 -0.0054 -0.0040 0.0176  171 GLY A CA   
1785 C  CA   B GLY A 170 ? 0.1556 0.0732 0.1289 -0.0266 0.0187  0.0068  171 GLY A CA   
1786 C  C    A GLY A 170 ? 0.1030 0.1005 0.1286 0.0006  -0.0027 0.0515  171 GLY A C    
1787 C  C    B GLY A 170 ? 0.1453 0.0474 0.1459 -0.0135 0.0120  0.0164  171 GLY A C    
1788 O  O    A GLY A 170 ? 0.1597 0.0771 0.1836 -0.0248 -0.0176 0.0606  171 GLY A O    
1789 O  O    B GLY A 170 ? 0.2217 0.0860 0.1626 -0.0250 0.0071  0.0480  171 GLY A O    
1790 N  N    A LYS A 171 ? 0.1076 0.0599 0.0864 0.0126  0.0005  0.0296  172 LYS A N    
1791 N  N    B LYS A 171 ? 0.1425 0.0631 0.1150 -0.0038 0.0024  0.0177  172 LYS A N    
1792 C  CA   A LYS A 171 ? 0.1055 0.0827 0.0847 -0.0034 0.0063  0.0335  172 LYS A CA   
1793 C  CA   B LYS A 171 ? 0.1572 0.0890 0.0974 -0.0023 0.0115  0.0175  172 LYS A CA   
1794 C  C    A LYS A 171 ? 0.0821 0.0728 0.0768 -0.0082 -0.0005 0.0293  172 LYS A C    
1795 C  C    B LYS A 171 ? 0.1580 0.0802 0.0789 -0.0126 0.0152  0.0195  172 LYS A C    
1796 O  O    A LYS A 171 ? 0.0935 0.0872 0.0564 0.0103  0.0017  0.0375  172 LYS A O    
1797 O  O    B LYS A 171 ? 0.1780 0.0881 0.1044 0.0131  0.0186  0.0296  172 LYS A O    
1798 C  CB   A LYS A 171 ? 0.1199 0.1057 0.0640 0.0046  0.0013  0.0124  172 LYS A CB   
1799 C  CB   B LYS A 171 ? 0.1556 0.1014 0.1128 -0.0082 0.0272  -0.0137 172 LYS A CB   
1800 C  CG   A LYS A 171 ? 0.1242 0.1044 0.1285 0.0024  0.0088  0.0219  172 LYS A CG   
1801 C  CG   B LYS A 171 ? 0.2143 0.1520 0.1738 0.0320  0.0052  -0.0215 172 LYS A CG   
1802 C  CD   A LYS A 171 ? 0.1709 0.1444 0.1279 0.0017  -0.0017 0.0096  172 LYS A CD   
1803 C  CD   B LYS A 171 ? 0.2203 0.1793 0.1515 -0.0065 0.0285  -0.0049 172 LYS A CD   
1804 C  CE   A LYS A 171 ? 0.2106 0.1935 0.1238 0.0344  0.0232  0.0135  172 LYS A CE   
1805 C  CE   B LYS A 171 ? 0.2642 0.1935 0.2114 -0.0388 -0.0156 0.0172  172 LYS A CE   
1806 N  NZ   A LYS A 171 ? 0.3249 0.2167 0.0829 -0.0296 0.0648  -0.0049 172 LYS A NZ   
1807 N  NZ   B LYS A 171 ? 0.3197 0.3377 0.2578 -0.0051 0.0544  0.0024  172 LYS A NZ   
1808 N  N    A SER A 172 ? 0.1145 0.1136 0.0385 0.0142  0.0164  0.0292  173 SER A N    
1809 N  N    B SER A 172 ? 0.1355 0.0847 0.0947 -0.0166 0.0097  0.0283  173 SER A N    
1810 C  CA   A SER A 172 ? 0.1150 0.0991 0.0782 0.0092  0.0030  0.0140  173 SER A CA   
1811 C  CA   B SER A 172 ? 0.1540 0.0859 0.0502 -0.0115 0.0099  0.0260  173 SER A CA   
1812 C  C    A SER A 172 ? 0.1220 0.1312 0.0446 0.0015  0.0108  0.0220  173 SER A C    
1813 C  C    B SER A 172 ? 0.1653 0.0872 0.0891 -0.0197 -0.0031 0.0186  173 SER A C    
1814 O  O    A SER A 172 ? 0.1547 0.1242 0.0642 0.0187  0.0000  0.0109  173 SER A O    
1815 O  O    B SER A 172 ? 0.2089 0.1529 0.0766 0.0046  0.0239  0.0275  173 SER A O    
1816 C  CB   A SER A 172 ? 0.1150 0.1114 0.0737 0.0218  -0.0251 0.0054  173 SER A CB   
1817 C  CB   B SER A 172 ? 0.1913 0.0949 0.0852 -0.0261 0.0068  0.0031  173 SER A CB   
1818 O  OG   A SER A 172 ? 0.1798 0.0870 0.1545 0.0403  -0.0176 0.0294  173 SER A OG   
1819 O  OG   B SER A 172 ? 0.2380 0.0915 0.1263 0.0126  0.0375  0.0342  173 SER A OG   
1820 N  N    A ALA A 173 ? 0.1344 0.1118 0.0538 0.0096  -0.0099 0.0121  174 ALA A N    
1821 N  N    B ALA A 173 ? 0.1953 0.0904 0.0683 -0.0093 0.0120  0.0137  174 ALA A N    
1822 C  CA   A ALA A 173 ? 0.1253 0.1133 0.0803 0.0126  -0.0142 0.0326  174 ALA A CA   
1823 C  CA   B ALA A 173 ? 0.1628 0.1234 0.1145 0.0166  0.0115  0.0264  174 ALA A CA   
1824 C  C    A ALA A 173 ? 0.0710 0.1287 0.0935 -0.0104 -0.0156 0.0197  174 ALA A C    
1825 C  C    B ALA A 173 ? 0.1486 0.1041 0.0870 0.0219  0.0167  0.0436  174 ALA A C    
1826 O  O    A ALA A 173 ? 0.1181 0.0852 0.0450 -0.0093 -0.0065 0.0137  174 ALA A O    
1827 O  O    B ALA A 173 ? 0.1775 0.1055 0.0732 0.0107  0.0155  0.0348  174 ALA A O    
1828 C  CB   A ALA A 173 ? 0.1369 0.1635 0.1252 0.0088  -0.0255 -0.0274 174 ALA A CB   
1829 C  CB   B ALA A 173 ? 0.1412 0.1675 0.1197 0.0015  0.0093  0.0104  174 ALA A CB   
1830 N  N    A ASP A 174 ? 0.1268 0.1021 0.0741 -0.0017 -0.0175 0.0346  175 ASP A N    
1831 N  N    B ASP A 174 ? 0.1606 0.1193 0.0759 0.0152  0.0142  0.0474  175 ASP A N    
1832 C  CA   A ASP A 174 ? 0.1181 0.1014 0.0732 0.0148  -0.0164 0.0377  175 ASP A CA   
1833 C  CA   B ASP A 174 ? 0.1787 0.0863 0.1030 0.0239  -0.0046 0.0390  175 ASP A CA   
1834 C  C    A ASP A 174 ? 0.1037 0.0811 0.1066 0.0003  -0.0048 0.0121  175 ASP A C    
1835 C  C    B ASP A 174 ? 0.1568 0.1010 0.1046 0.0120  -0.0174 -0.0076 175 ASP A C    
1836 O  O    A ASP A 174 ? 0.1265 0.1005 0.0960 -0.0098 0.0007  -0.0175 175 ASP A O    
1837 O  O    B ASP A 174 ? 0.1777 0.1238 0.1014 0.0167  -0.0178 -0.0230 175 ASP A O    
1838 C  CB   A ASP A 174 ? 0.1657 0.0879 0.1693 0.0252  -0.0077 0.0331  175 ASP A CB   
1839 C  CB   B ASP A 174 ? 0.1847 0.1097 0.1572 0.0208  -0.0103 0.0186  175 ASP A CB   
1840 C  CG   A ASP A 174 ? 0.2063 0.1551 0.1770 -0.0548 -0.0531 0.0318  175 ASP A CG   
1841 C  CG   B ASP A 174 ? 0.1543 0.1743 0.1637 0.0414  -0.0020 0.0063  175 ASP A CG   
1842 O  OD1  A ASP A 174 ? 0.2802 0.2468 0.2265 -0.0925 -0.0700 0.0366  175 ASP A OD1  
1843 O  OD1  B ASP A 174 ? 0.3709 0.2502 0.3768 -0.0361 -0.0186 0.0013  175 ASP A OD1  
1844 O  OD2  A ASP A 174 ? 0.1820 0.1870 0.1644 -0.0399 -0.0258 0.0714  175 ASP A OD2  
1845 O  OD2  B ASP A 174 ? 0.3785 0.4122 0.3330 0.0160  0.0233  -0.0198 175 ASP A OD2  
1846 N  N    A PHE A 175 ? 0.1035 0.0737 0.0797 0.0120  -0.0038 0.0108  176 PHE A N    
1847 N  N    B PHE A 175 ? 0.1583 0.0952 0.0797 0.0156  -0.0098 0.0088  176 PHE A N    
1848 C  CA   A PHE A 175 ? 0.0969 0.0920 0.0969 0.0013  -0.0093 0.0088  176 PHE A CA   
1849 C  CA   B PHE A 175 ? 0.1613 0.1127 0.0985 0.0115  -0.0262 0.0131  176 PHE A CA   
1850 C  C    A PHE A 175 ? 0.0992 0.0678 0.1129 0.0152  -0.0175 0.0194  176 PHE A C    
1851 C  C    B PHE A 175 ? 0.1463 0.0940 0.0951 0.0027  -0.0188 0.0337  176 PHE A C    
1852 O  O    A PHE A 175 ? 0.1120 0.1184 0.1064 0.0140  -0.0417 -0.0073 176 PHE A O    
1853 O  O    B PHE A 175 ? 0.1518 0.1344 0.0970 0.0107  -0.0471 0.0120  176 PHE A O    
1854 C  CB   A PHE A 175 ? 0.1084 0.0929 0.1322 -0.0065 -0.0043 0.0068  176 PHE A CB   
1855 C  CB   B PHE A 175 ? 0.1879 0.0890 0.0983 0.0074  -0.0262 0.0366  176 PHE A CB   
1856 C  CG   A PHE A 175 ? 0.0942 0.0565 0.0797 0.0076  -0.0137 0.0038  176 PHE A CG   
1857 C  CG   B PHE A 175 ? 0.1369 0.0957 0.1176 0.0137  -0.0170 0.0104  176 PHE A CG   
1858 C  CD1  A PHE A 175 ? 0.1906 0.0843 0.1179 -0.0218 0.0006  0.0227  176 PHE A CD1  
1859 C  CD1  B PHE A 175 ? 0.2066 0.0603 0.1517 -0.0259 -0.0038 0.0463  176 PHE A CD1  
1860 C  CD2  A PHE A 175 ? 0.1536 0.0741 0.1249 -0.0184 -0.0395 0.0088  176 PHE A CD2  
1861 C  CD2  B PHE A 175 ? 0.1500 0.1061 0.1129 0.0377  -0.0337 0.0410  176 PHE A CD2  
1862 C  CE1  A PHE A 175 ? 0.1919 0.0617 0.1447 0.0037  -0.0086 0.0207  176 PHE A CE1  
1863 C  CE1  B PHE A 175 ? 0.1838 0.0748 0.1459 -0.0071 0.0140  0.0060  176 PHE A CE1  
1864 C  CE2  A PHE A 175 ? 0.1116 0.0913 0.1365 0.0115  -0.0153 0.0209  176 PHE A CE2  
1865 C  CE2  B PHE A 175 ? 0.1348 0.1048 0.1106 0.0230  -0.0171 0.0248  176 PHE A CE2  
1866 C  CZ   A PHE A 175 ? 0.1233 0.0597 0.1506 -0.0005 -0.0241 -0.0035 176 PHE A CZ   
1867 C  CZ   B PHE A 175 ? 0.1946 0.0508 0.1409 -0.0097 -0.0351 0.0274  176 PHE A CZ   
1868 N  N    A THR A 176 ? 0.1276 0.0956 0.0750 0.0248  -0.0148 0.0035  177 THR A N    
1869 N  N    B THR A 176 ? 0.1362 0.1163 0.0807 0.0005  -0.0333 0.0281  177 THR A N    
1870 C  CA   A THR A 176 ? 0.1062 0.0702 0.0924 0.0104  -0.0164 0.0076  177 THR A CA   
1871 C  CA   B THR A 176 ? 0.1612 0.0922 0.0978 -0.0038 -0.0337 0.0286  177 THR A CA   
1872 C  C    A THR A 176 ? 0.1154 0.0724 0.0870 0.0181  -0.0197 0.0307  177 THR A C    
1873 C  C    B THR A 176 ? 0.1527 0.0832 0.0926 -0.0063 -0.0430 0.0296  177 THR A C    
1874 O  O    A THR A 176 ? 0.1536 0.0624 0.1014 -0.0098 -0.0199 0.0131  177 THR A O    
1875 O  O    B THR A 176 ? 0.1486 0.0591 0.1089 -0.0119 -0.0386 0.0227  177 THR A O    
1876 C  CB   A THR A 176 ? 0.0978 0.1314 0.0809 0.0163  -0.0087 0.0417  177 THR A CB   
1877 C  CB   B THR A 176 ? 0.1441 0.0942 0.1089 -0.0023 -0.0331 0.0214  177 THR A CB   
1878 O  OG1  A THR A 176 ? 0.2100 0.1367 0.0933 0.0324  -0.0331 0.0372  177 THR A OG1  
1879 O  OG1  B THR A 176 ? 0.1835 0.1428 0.1159 0.0130  -0.0428 0.0421  177 THR A OG1  
1880 C  CG2  A THR A 176 ? 0.1154 0.1983 0.2330 -0.0148 -0.0151 0.0658  177 THR A CG2  
1881 C  CG2  B THR A 176 ? 0.1735 0.1394 0.2136 -0.0282 -0.0443 0.0930  177 THR A CG2  
1882 N  N    A ASN A 177 ? 0.1026 0.0748 0.0797 -0.0020 -0.0181 0.0315  178 ASN A N    
1883 N  N    B ASN A 177 ? 0.1185 0.0748 0.1008 -0.0074 -0.0386 0.0160  178 ASN A N    
1884 C  CA   A ASN A 177 ? 0.0994 0.0933 0.0881 0.0049  -0.0143 0.0272  178 ASN A CA   
1885 C  CA   B ASN A 177 ? 0.1382 0.0897 0.0969 -0.0082 -0.0274 0.0107  178 ASN A CA   
1886 C  C    A ASN A 177 ? 0.0829 0.0873 0.0969 0.0164  -0.0296 0.0093  178 ASN A C    
1887 C  C    B ASN A 177 ? 0.1321 0.0825 0.1134 -0.0174 -0.0276 0.0189  178 ASN A C    
1888 O  O    A ASN A 177 ? 0.1039 0.1495 0.1744 -0.0175 -0.0183 0.0825  178 ASN A O    
1889 O  O    B ASN A 177 ? 0.1435 0.1211 0.1486 -0.0141 -0.0262 0.0749  178 ASN A O    
1890 C  CB   A ASN A 177 ? 0.0926 0.1242 0.1290 0.0135  -0.0272 0.0467  178 ASN A CB   
1891 C  CB   B ASN A 177 ? 0.1199 0.1014 0.1545 0.0109  -0.0304 0.0183  178 ASN A CB   
1892 C  CG   A ASN A 177 ? 0.1203 0.1195 0.1185 -0.0043 -0.0384 0.0137  178 ASN A CG   
1893 C  CG   B ASN A 177 ? 0.1261 0.0517 0.1659 0.0243  -0.0241 0.0164  178 ASN A CG   
1894 O  OD1  A ASN A 177 ? 0.1075 0.1495 0.1991 0.0373  0.0322  0.0120  178 ASN A OD1  
1895 O  OD1  B ASN A 177 ? 0.1188 0.0841 0.1703 0.0148  -0.0098 0.0305  178 ASN A OD1  
1896 N  ND2  A ASN A 177 ? 0.1073 0.1626 0.1222 -0.0010 -0.0195 0.0740  178 ASN A ND2  
1897 N  ND2  B ASN A 177 ? 0.1344 0.1075 0.0829 -0.0027 -0.0375 0.0344  178 ASN A ND2  
1898 N  N    A PHE A 178 ? 0.1145 0.0705 0.0940 -0.0038 -0.0242 0.0189  179 PHE A N    
1899 N  N    B PHE A 178 ? 0.1303 0.0904 0.0753 -0.0097 -0.0087 0.0287  179 PHE A N    
1900 C  CA   A PHE A 178 ? 0.0935 0.0511 0.0825 -0.0020 -0.0088 0.0243  179 PHE A CA   
1901 C  CA   B PHE A 178 ? 0.1297 0.0949 0.0748 0.0003  -0.0126 0.0186  179 PHE A CA   
1902 C  C    A PHE A 178 ? 0.1039 0.0631 0.0868 -0.0080 -0.0153 0.0046  179 PHE A C    
1903 C  C    B PHE A 178 ? 0.1190 0.0888 0.0626 0.0006  -0.0243 0.0395  179 PHE A C    
1904 O  O    A PHE A 178 ? 0.1414 0.0658 0.0764 -0.0024 -0.0194 0.0040  179 PHE A O    
1905 O  O    B PHE A 178 ? 0.1653 0.1080 0.0915 -0.0114 -0.0153 0.0185  179 PHE A O    
1906 C  CB   A PHE A 178 ? 0.0991 0.0719 0.0798 -0.0027 -0.0186 0.0060  179 PHE A CB   
1907 C  CB   B PHE A 178 ? 0.1278 0.0815 0.0917 0.0041  -0.0030 0.0263  179 PHE A CB   
1908 C  CG   A PHE A 178 ? 0.0940 0.0538 0.0915 -0.0199 -0.0142 0.0229  179 PHE A CG   
1909 C  CG   B PHE A 178 ? 0.1278 0.0526 0.1127 -0.0109 -0.0088 0.0335  179 PHE A CG   
1910 C  CD1  A PHE A 178 ? 0.1190 0.0922 0.1102 -0.0027 -0.0357 0.0081  179 PHE A CD1  
1911 C  CD1  B PHE A 178 ? 0.1495 0.0861 0.0915 -0.0098 -0.0208 0.0216  179 PHE A CD1  
1912 C  CD2  A PHE A 178 ? 0.0536 0.0829 0.0944 -0.0230 -0.0048 0.0221  179 PHE A CD2  
1913 C  CD2  B PHE A 178 ? 0.1057 0.0617 0.0922 -0.0046 0.0043  0.0252  179 PHE A CD2  
1914 C  CE1  A PHE A 178 ? 0.1649 0.0499 0.0938 0.0137  -0.0307 -0.0003 179 PHE A CE1  
1915 C  CE1  B PHE A 178 ? 0.1324 0.0992 0.1427 -0.0040 -0.0031 0.0392  179 PHE A CE1  
1916 C  CE2  A PHE A 178 ? 0.0947 0.0590 0.0845 -0.0181 -0.0130 0.0188  179 PHE A CE2  
1917 C  CE2  B PHE A 178 ? 0.0983 0.0886 0.1129 0.0085  -0.0209 0.0126  179 PHE A CE2  
1918 C  CZ   A PHE A 178 ? 0.0886 0.0472 0.1107 -0.0129 -0.0147 0.0193  179 PHE A CZ   
1919 C  CZ   B PHE A 178 ? 0.1448 0.1328 0.0956 0.0062  -0.0087 0.0326  179 PHE A CZ   
1920 N  N    A ASP A 179 ? 0.0942 0.0737 0.0864 -0.0031 -0.0109 0.0060  180 ASP A N    
1921 N  N    B ASP A 179 ? 0.1324 0.0897 0.0733 0.0109  -0.0209 0.0125  180 ASP A N    
1922 C  CA   A ASP A 179 ? 0.1247 0.1064 0.0852 0.0082  0.0010  0.0052  180 ASP A CA   
1923 C  CA   B ASP A 179 ? 0.1425 0.0961 0.0960 0.0156  -0.0119 0.0260  180 ASP A CA   
1924 C  C    A ASP A 179 ? 0.1125 0.0838 0.0960 0.0098  0.0137  0.0006  180 ASP A C    
1925 C  C    B ASP A 179 ? 0.1429 0.0926 0.0696 0.0103  -0.0175 0.0024  180 ASP A C    
1926 O  O    A ASP A 179 ? 0.1208 0.0710 0.0938 0.0037  0.0093  -0.0063 180 ASP A O    
1927 O  O    B ASP A 179 ? 0.1208 0.0827 0.0856 0.0087  -0.0020 0.0120  180 ASP A O    
1928 C  CB   A ASP A 179 ? 0.1057 0.1480 0.0899 0.0214  0.0063  0.0109  180 ASP A CB   
1929 C  CB   B ASP A 179 ? 0.1542 0.1335 0.1391 0.0125  -0.0037 0.0252  180 ASP A CB   
1930 C  CG   A ASP A 179 ? 0.1317 0.1644 0.1498 0.0081  -0.0054 0.0131  180 ASP A CG   
1931 C  CG   B ASP A 179 ? 0.1556 0.1500 0.1188 0.0307  -0.0017 0.0007  180 ASP A CG   
1932 O  OD1  A ASP A 179 ? 0.1143 0.1274 0.1233 0.0441  0.0125  0.0007  180 ASP A OD1  
1933 O  OD1  B ASP A 179 ? 0.1583 0.1102 0.1181 0.0472  -0.0006 -0.0063 180 ASP A OD1  
1934 O  OD2  A ASP A 179 ? 0.2078 0.2348 0.1725 0.0741  -0.0718 -0.0088 180 ASP A OD2  
1935 O  OD2  B ASP A 179 ? 0.2389 0.2558 0.2624 0.0109  -0.0277 -0.0251 180 ASP A OD2  
1936 N  N    A PRO A 180 ? 0.1358 0.0624 0.1008 0.0164  -0.0082 0.0151  181 PRO A N    
1937 N  N    B PRO A 180 ? 0.1385 0.0687 0.0974 0.0086  -0.0401 0.0027  181 PRO A N    
1938 C  CA   A PRO A 180 ? 0.1599 0.0885 0.1093 0.0196  -0.0280 0.0093  181 PRO A CA   
1939 C  CA   B PRO A 180 ? 0.1726 0.0825 0.1057 0.0253  -0.0524 0.0162  181 PRO A CA   
1940 C  C    A PRO A 180 ? 0.1924 0.0935 0.0976 0.0142  -0.0353 -0.0024 181 PRO A C    
1941 C  C    B PRO A 180 ? 0.1917 0.0969 0.1057 0.0052  -0.0515 0.0023  181 PRO A C    
1942 O  O    A PRO A 180 ? 0.1869 0.0856 0.0961 0.0153  -0.0688 -0.0043 181 PRO A O    
1943 O  O    B PRO A 180 ? 0.2003 0.0684 0.1127 -0.0041 -0.0392 0.0052  181 PRO A O    
1944 C  CB   A PRO A 180 ? 0.1468 0.1073 0.1249 0.0164  -0.0260 0.0175  181 PRO A CB   
1945 C  CB   B PRO A 180 ? 0.1725 0.1118 0.1064 0.0131  -0.0452 0.0186  181 PRO A CB   
1946 C  CG   A PRO A 180 ? 0.1225 0.1071 0.0935 -0.0017 -0.0143 0.0104  181 PRO A CG   
1947 C  CG   B PRO A 180 ? 0.1515 0.1186 0.1041 0.0000  -0.0285 -0.0115 181 PRO A CG   
1948 C  CD   A PRO A 180 ? 0.1317 0.0551 0.0952 0.0096  -0.0124 0.0263  181 PRO A CD   
1949 C  CD   B PRO A 180 ? 0.1181 0.0926 0.0818 0.0077  -0.0239 -0.0131 181 PRO A CD   
1950 N  N    . ARG A 181 ? 0.1935 0.0894 0.1091 0.0222  -0.0568 0.0252  182 ARG A N    
1951 C  CA   . ARG A 181 ? 0.1894 0.0926 0.1125 0.0024  -0.0531 0.0103  182 ARG A CA   
1952 C  C    . ARG A 181 ? 0.1976 0.0929 0.1454 0.0027  -0.0948 0.0013  182 ARG A C    
1953 O  O    . ARG A 181 ? 0.2292 0.1075 0.1639 -0.0057 -0.0737 0.0238  182 ARG A O    
1954 C  CB   . ARG A 181 ? 0.2125 0.0987 0.1565 0.0043  -0.0474 -0.0017 182 ARG A CB   
1955 C  CG   . ARG A 181 ? 0.2078 0.1142 0.1752 -0.0131 0.0020  0.0093  182 ARG A CG   
1956 C  CD   . ARG A 181 ? 0.1676 0.1680 0.2520 0.0118  -0.0054 0.0214  182 ARG A CD   
1957 N  NE   . ARG A 181 ? 0.2025 0.1356 0.2669 0.0093  -0.0233 0.0732  182 ARG A NE   
1958 C  CZ   . ARG A 181 ? 0.2090 0.2350 0.2741 0.0052  0.0020  0.0790  182 ARG A CZ   
1959 N  NH1  . ARG A 181 ? 0.2490 0.2980 0.3772 0.0483  -0.0006 0.0798  182 ARG A NH1  
1960 N  NH2  . ARG A 181 ? 0.1696 0.3312 0.3194 0.0340  -0.0031 0.1071  182 ARG A NH2  
1961 N  N    . GLY A 182 ? 0.2359 0.0947 0.1186 0.0196  -0.0979 -0.0065 183 GLY A N    
1962 C  CA   . GLY A 182 ? 0.2409 0.0833 0.1479 -0.0031 -0.0944 0.0020  183 GLY A CA   
1963 C  C    . GLY A 182 ? 0.2484 0.0714 0.1522 0.0163  -0.0763 0.0017  183 GLY A C    
1964 O  O    . GLY A 182 ? 0.3073 0.0973 0.1838 0.0184  -0.1089 0.0031  183 GLY A O    
1965 N  N    A LEU A 183 ? 0.2048 0.0793 0.0800 -0.0024 -0.0280 -0.0108 184 LEU A N    
1966 N  N    B LEU A 183 ? 0.1978 0.0712 0.0793 0.0131  -0.0472 0.0107  184 LEU A N    
1967 C  CA   A LEU A 183 ? 0.1421 0.0684 0.0924 0.0181  0.0118  0.0010  184 LEU A CA   
1968 C  CA   B LEU A 183 ? 0.1597 0.0599 0.0930 -0.0071 -0.0236 0.0000  184 LEU A CA   
1969 C  C    A LEU A 183 ? 0.1233 0.0709 0.0587 0.0131  0.0068  -0.0010 184 LEU A C    
1970 C  C    B LEU A 183 ? 0.1418 0.0709 0.0847 0.0000  0.0074  -0.0054 184 LEU A C    
1971 O  O    A LEU A 183 ? 0.1073 0.1045 0.0850 0.0548  0.0324  0.0317  184 LEU A O    
1972 O  O    B LEU A 183 ? 0.1168 0.0966 0.0838 0.0294  0.0104  0.0135  184 LEU A O    
1973 C  CB   A LEU A 183 ? 0.1045 0.0836 0.0739 0.0230  -0.0041 0.0222  184 LEU A CB   
1974 C  CB   B LEU A 183 ? 0.1635 0.0538 0.0935 -0.0136 -0.0141 0.0099  184 LEU A CB   
1975 C  CG   A LEU A 183 ? 0.0834 0.0969 0.0958 -0.0318 0.0217  0.0188  184 LEU A CG   
1976 C  CG   B LEU A 183 ? 0.1089 0.0985 0.0675 0.0062  -0.0283 0.0362  184 LEU A CG   
1977 C  CD1  A LEU A 183 ? 0.0935 0.1746 0.0750 -0.0351 0.0164  0.0520  184 LEU A CD1  
1978 C  CD1  B LEU A 183 ? 0.1233 0.1447 0.0876 -0.0063 0.0216  0.0697  184 LEU A CD1  
1979 C  CD2  A LEU A 183 ? 0.1215 0.1133 0.0827 0.0423  -0.0091 -0.0087 184 LEU A CD2  
1980 C  CD2  B LEU A 183 ? 0.1268 0.1305 0.1516 0.0186  -0.0097 -0.0324 184 LEU A CD2  
1981 N  N    A LEU A 184 ? 0.0908 0.0615 0.1102 0.0265  0.0186  0.0082  185 LEU A N    
1982 N  N    B LEU A 184 ? 0.1109 0.0922 0.0906 0.0068  -0.0153 0.0178  185 LEU A N    
1983 C  CA   A LEU A 184 ? 0.0829 0.0948 0.0912 0.0104  0.0071  0.0041  185 LEU A CA   
1984 C  CA   B LEU A 184 ? 0.1179 0.0881 0.1057 0.0024  -0.0229 -0.0140 185 LEU A CA   
1985 C  C    A LEU A 184 ? 0.1073 0.0757 0.0970 -0.0010 0.0017  0.0031  185 LEU A C    
1986 C  C    B LEU A 184 ? 0.1299 0.0836 0.1252 -0.0136 -0.0288 0.0063  185 LEU A C    
1987 O  O    A LEU A 184 ? 0.1411 0.0832 0.1066 -0.0085 -0.0174 0.0087  185 LEU A O    
1988 O  O    B LEU A 184 ? 0.1287 0.0829 0.1453 -0.0020 -0.0414 -0.0046 185 LEU A O    
1989 C  CB   A LEU A 184 ? 0.0773 0.0511 0.0992 0.0082  -0.0013 -0.0160 185 LEU A CB   
1990 C  CB   B LEU A 184 ? 0.1234 0.0958 0.1107 -0.0082 -0.0107 0.0017  185 LEU A CB   
1991 C  CG   A LEU A 184 ? 0.0948 0.0685 0.1032 0.0229  -0.0458 0.0184  185 LEU A CG   
1992 C  CG   B LEU A 184 ? 0.0924 0.1125 0.1344 -0.0137 0.0031  -0.0027 185 LEU A CG   
1993 C  CD1  A LEU A 184 ? 0.1251 0.0852 0.1208 0.0199  -0.0476 -0.0137 185 LEU A CD1  
1994 C  CD1  B LEU A 184 ? 0.1238 0.1319 0.1233 -0.0285 -0.0241 0.0091  185 LEU A CD1  
1995 C  CD2  A LEU A 184 ? 0.0802 0.0556 0.0834 -0.0065 -0.0178 0.0081  185 LEU A CD2  
1996 C  CD2  B LEU A 184 ? 0.1217 0.1407 0.0947 0.0109  -0.0450 -0.0230 185 LEU A CD2  
1997 N  N    A PRO A 185 ? 0.1341 0.0744 0.1511 -0.0177 -0.0401 0.0241  186 PRO A N    
1998 N  N    B PRO A 185 ? 0.1242 0.0881 0.1522 -0.0231 -0.0505 0.0209  186 PRO A N    
1999 C  CA   A PRO A 185 ? 0.1039 0.0958 0.1561 0.0007  -0.0263 0.0175  186 PRO A CA   
2000 C  CA   B PRO A 185 ? 0.0969 0.0829 0.1412 0.0175  -0.0225 0.0203  186 PRO A CA   
2001 C  C    A PRO A 185 ? 0.0978 0.0719 0.1391 -0.0310 -0.0197 0.0000  186 PRO A C    
2002 C  C    B PRO A 185 ? 0.0788 0.0705 0.1493 0.0204  -0.0098 0.0041  186 PRO A C    
2003 O  O    A PRO A 185 ? 0.0926 0.0706 0.1613 -0.0035 -0.0215 0.0176  186 PRO A O    
2004 O  O    B PRO A 185 ? 0.0825 0.0705 0.1057 0.0160  -0.0080 0.0041  186 PRO A O    
2005 C  CB   A PRO A 185 ? 0.1057 0.0903 0.1682 0.0054  -0.0318 0.0253  186 PRO A CB   
2006 C  CB   B PRO A 185 ? 0.1161 0.0727 0.1299 -0.0098 -0.0230 0.0091  186 PRO A CB   
2007 C  CG   A PRO A 185 ? 0.1055 0.0859 0.1324 -0.0054 0.0020  -0.0057 186 PRO A CG   
2008 C  CG   B PRO A 185 ? 0.1158 0.0793 0.1064 0.0142  -0.0304 0.0307  186 PRO A CG   
2009 C  CD   A PRO A 185 ? 0.1030 0.0829 0.0836 0.0132  -0.0038 -0.0038 186 PRO A CD   
2010 C  CD   B PRO A 185 ? 0.0978 0.1100 0.0992 -0.0012 -0.0203 0.0208  186 PRO A CD   
2011 N  N    A GLU A 186 ? 0.1008 0.0890 0.1744 -0.0148 -0.0151 0.0046  187 GLU A N    
2012 N  N    B GLU A 186 ? 0.0949 0.0750 0.1481 0.0074  0.0135  0.0017  187 GLU A N    
2013 C  CA   A GLU A 186 ? 0.1010 0.0996 0.1940 -0.0162 -0.0146 0.0046  187 GLU A CA   
2014 C  CA   B GLU A 186 ? 0.0784 0.0827 0.1833 0.0000  0.0108  0.0085  187 GLU A CA   
2015 C  C    A GLU A 186 ? 0.0933 0.0939 0.2348 0.0027  -0.0208 -0.0031 187 GLU A C    
2016 C  C    B GLU A 186 ? 0.0859 0.1115 0.2406 -0.0065 -0.0024 0.0006  187 GLU A C    
2017 O  O    A GLU A 186 ? 0.1066 0.1432 0.2781 0.0151  -0.0195 0.0170  187 GLU A O    
2018 O  O    B GLU A 186 ? 0.1075 0.1238 0.2096 0.0308  -0.0092 0.0031  187 GLU A O    
2019 C  CB   A GLU A 186 ? 0.1010 0.1215 0.1495 -0.0070 -0.0236 -0.0010 187 GLU A CB   
2020 C  CB   B GLU A 186 ? 0.0630 0.1319 0.1678 -0.0142 0.0062  0.0000  187 GLU A CB   
2021 C  CG   A GLU A 186 ? 0.1401 0.1263 0.2105 -0.0108 -0.0315 -0.0065 187 GLU A CG   
2022 C  CG   B GLU A 186 ? 0.1570 0.0961 0.2075 -0.0329 -0.0060 -0.0260 187 GLU A CG   
2023 C  CD   A GLU A 186 ? 0.1834 0.1619 0.2307 -0.0203 0.0173  0.0185  187 GLU A CD   
2024 C  CD   B GLU A 186 ? 0.1315 0.1294 0.2332 -0.0390 -0.0188 -0.0118 187 GLU A CD   
2025 O  OE1  A GLU A 186 ? 0.1685 0.1380 0.2678 -0.0074 0.0274  0.0013  187 GLU A OE1  
2026 O  OE1  B GLU A 186 ? 0.1639 0.1382 0.2098 -0.0430 0.0284  0.0087  187 GLU A OE1  
2027 O  OE2  A GLU A 186 ? 0.2228 0.1689 0.2115 0.0303  0.0233  0.0538  187 GLU A OE2  
2028 O  OE2  B GLU A 186 ? 0.2048 0.1711 0.2881 -0.0350 -0.0337 -0.0284 187 GLU A OE2  
2029 N  N    . SER A 187 ? 0.0863 0.1075 0.2465 -0.0096 -0.0093 0.0137  188 SER A N    
2030 C  CA   . SER A 187 ? 0.0895 0.1136 0.2292 -0.0059 -0.0125 0.0063  188 SER A CA   
2031 C  C    . SER A 187 ? 0.0820 0.1052 0.2120 -0.0062 -0.0017 0.0220  188 SER A C    
2032 O  O    . SER A 187 ? 0.0994 0.1276 0.2073 -0.0194 -0.0054 0.0003  188 SER A O    
2033 C  CB   . SER A 187 ? 0.1127 0.1498 0.2240 -0.0225 0.0038  0.0188  188 SER A CB   
2034 O  OG   . SER A 187 ? 0.1238 0.1535 0.2199 -0.0266 -0.0031 0.0250  188 SER A OG   
2035 N  N    . LEU A 188 ? 0.0863 0.1046 0.2091 -0.0023 0.0038  0.0104  189 LEU A N    
2036 C  CA   . LEU A 188 ? 0.0894 0.1163 0.2039 -0.0024 0.0071  0.0043  189 LEU A CA   
2037 C  C    . LEU A 188 ? 0.1010 0.1179 0.1784 0.0035  -0.0074 -0.0217 189 LEU A C    
2038 O  O    . LEU A 188 ? 0.1204 0.1331 0.2003 -0.0174 -0.0131 -0.0454 189 LEU A O    
2039 C  CB   . LEU A 188 ? 0.1132 0.1217 0.2587 -0.0232 0.0017  0.0142  189 LEU A CB   
2040 C  CG   . LEU A 188 ? 0.1304 0.1100 0.2906 0.0052  -0.0076 0.0366  189 LEU A CG   
2041 C  CD1  . LEU A 188 ? 0.1653 0.1436 0.3776 -0.0252 -0.0120 0.0498  189 LEU A CD1  
2042 C  CD2  . LEU A 188 ? 0.1292 0.2542 0.2100 0.0199  -0.0337 0.0727  189 LEU A CD2  
2043 N  N    . ASP A 189 ? 0.1001 0.1089 0.1613 -0.0017 0.0151  -0.0160 190 ASP A N    
2044 C  CA   . ASP A 189 ? 0.1039 0.1368 0.1509 -0.0324 0.0131  -0.0141 190 ASP A CA   
2045 C  C    . ASP A 189 ? 0.0886 0.0872 0.1263 -0.0236 0.0124  0.0012  190 ASP A C    
2046 O  O    . ASP A 189 ? 0.0906 0.0890 0.1195 -0.0121 0.0027  -0.0065 190 ASP A O    
2047 C  CB   . ASP A 189 ? 0.1393 0.1660 0.1565 -0.0652 0.0193  0.0243  190 ASP A CB   
2048 C  CG   . ASP A 189 ? 0.1949 0.2337 0.2050 -0.0970 0.0034  0.0412  190 ASP A CG   
2049 O  OD1  . ASP A 189 ? 0.1278 0.4086 0.3106 -0.0394 0.0842  0.0024  190 ASP A OD1  
2050 O  OD2  . ASP A 189 ? 0.2129 0.4027 0.2694 -0.0966 -0.0357 0.0807  190 ASP A OD2  
2051 N  N    . TYR A 190 ? 0.1021 0.0996 0.1150 -0.0076 0.0186  -0.0087 191 TYR A N    
2052 C  CA   . TYR A 190 ? 0.0933 0.0888 0.0985 -0.0147 0.0120  0.0040  191 TYR A CA   
2053 C  C    . TYR A 190 ? 0.1010 0.0745 0.0829 -0.0120 0.0131  0.0006  191 TYR A C    
2054 O  O    . TYR A 190 ? 0.1305 0.0951 0.0861 -0.0096 0.0243  -0.0060 191 TYR A O    
2055 C  CB   . TYR A 190 ? 0.1027 0.1030 0.0794 -0.0121 -0.0054 0.0015  191 TYR A CB   
2056 C  CG   . TYR A 190 ? 0.1082 0.0861 0.0944 -0.0161 0.0132  0.0065  191 TYR A CG   
2057 C  CD1  . TYR A 190 ? 0.0983 0.0958 0.1195 -0.0205 0.0015  -0.0006 191 TYR A CD1  
2058 C  CD2  . TYR A 190 ? 0.1202 0.0966 0.1085 -0.0178 0.0013  0.0108  191 TYR A CD2  
2059 C  CE1  . TYR A 190 ? 0.1224 0.0951 0.1120 -0.0315 -0.0035 -0.0071 191 TYR A CE1  
2060 C  CE2  . TYR A 190 ? 0.1150 0.1062 0.1517 -0.0013 0.0060  0.0062  191 TYR A CE2  
2061 C  CZ   . TYR A 190 ? 0.1278 0.0906 0.1146 -0.0098 0.0017  -0.0086 191 TYR A CZ   
2062 O  OH   . TYR A 190 ? 0.1824 0.1071 0.1247 0.0059  -0.0051 -0.0162 191 TYR A OH   
2063 N  N    . TRP A 191 ? 0.1012 0.0705 0.0705 -0.0082 0.0054  -0.0003 192 TRP A N    
2064 C  CA   . TRP A 191 ? 0.1084 0.0642 0.0788 0.0000  0.0221  0.0065  192 TRP A CA   
2065 C  C    . TRP A 191 ? 0.1079 0.0687 0.0562 -0.0003 0.0186  0.0068  192 TRP A C    
2066 O  O    . TRP A 191 ? 0.1242 0.0739 0.0680 -0.0284 0.0057  -0.0065 192 TRP A O    
2067 C  CB   . TRP A 191 ? 0.0969 0.0820 0.0775 -0.0187 0.0115  -0.0027 192 TRP A CB   
2068 C  CG   . TRP A 191 ? 0.1143 0.0715 0.0750 0.0006  0.0076  0.0093  192 TRP A CG   
2069 C  CD1  . TRP A 191 ? 0.1353 0.0868 0.1134 -0.0013 0.0109  -0.0130 192 TRP A CD1  
2070 C  CD2  . TRP A 191 ? 0.1093 0.0627 0.1152 -0.0019 0.0034  0.0030  192 TRP A CD2  
2071 N  NE1  . TRP A 191 ? 0.1667 0.0710 0.1155 0.0019  -0.0080 0.0198  192 TRP A NE1  
2072 C  CE2  . TRP A 191 ? 0.1391 0.0746 0.1128 -0.0038 -0.0041 -0.0012 192 TRP A CE2  
2073 C  CE3  . TRP A 191 ? 0.1084 0.0759 0.0987 0.0006  0.0034  -0.0038 192 TRP A CE3  
2074 C  CZ2  . TRP A 191 ? 0.1430 0.0635 0.1541 -0.0160 -0.0171 0.0155  192 TRP A CZ2  
2075 C  CZ3  . TRP A 191 ? 0.1076 0.0900 0.1249 0.0003  0.0000  -0.0131 192 TRP A CZ3  
2076 C  CH2  . TRP A 191 ? 0.1398 0.0768 0.1541 0.0071  -0.0170 -0.0296 192 TRP A CH2  
2077 N  N    . THR A 192 ? 0.1082 0.0627 0.0565 -0.0115 0.0006  -0.0005 193 THR A N    
2078 C  CA   . THR A 192 ? 0.1062 0.0642 0.0588 0.0020  0.0054  -0.0049 193 THR A CA   
2079 C  C    . THR A 192 ? 0.1053 0.0617 0.0657 0.0006  0.0034  -0.0020 193 THR A C    
2080 O  O    . THR A 192 ? 0.1159 0.0890 0.0687 -0.0098 0.0091  0.0054  193 THR A O    
2081 C  CB   . THR A 192 ? 0.0922 0.0635 0.0676 -0.0093 0.0076  -0.0065 193 THR A CB   
2082 O  OG1  . THR A 192 ? 0.1084 0.0642 0.0791 0.0057  0.0065  -0.0063 193 THR A OG1  
2083 C  CG2  . THR A 192 ? 0.1367 0.0764 0.0939 0.0126  0.0176  -0.0015 193 THR A CG2  
2084 N  N    . TYR A 193 ? 0.0969 0.0556 0.0612 0.0010  -0.0087 -0.0007 194 TYR A N    
2085 C  CA   . TYR A 193 ? 0.1096 0.0683 0.0689 -0.0027 -0.0013 -0.0110 194 TYR A CA   
2086 C  C    . TYR A 193 ? 0.0969 0.0605 0.0623 0.0052  0.0023  -0.0057 194 TYR A C    
2087 O  O    . TYR A 193 ? 0.1005 0.0642 0.0579 0.0037  -0.0060 0.0027  194 TYR A O    
2088 C  CB   . TYR A 193 ? 0.1088 0.0642 0.0640 0.0049  -0.0098 -0.0035 194 TYR A CB   
2089 C  CG   . TYR A 193 ? 0.0931 0.0509 0.0727 -0.0076 -0.0165 0.0038  194 TYR A CG   
2090 C  CD1  . TYR A 193 ? 0.1003 0.0536 0.0811 0.0108  -0.0054 0.0096  194 TYR A CD1  
2091 C  CD2  . TYR A 193 ? 0.1190 0.0430 0.0845 0.0119  -0.0181 -0.0074 194 TYR A CD2  
2092 C  CE1  . TYR A 193 ? 0.1009 0.0429 0.0746 -0.0020 -0.0209 0.0010  194 TYR A CE1  
2093 C  CE2  . TYR A 193 ? 0.0785 0.0572 0.0956 0.0046  -0.0131 -0.0071 194 TYR A CE2  
2094 C  CZ   . TYR A 193 ? 0.0987 0.0359 0.0773 0.0137  -0.0217 -0.0043 194 TYR A CZ   
2095 O  OH   . TYR A 193 ? 0.0903 0.0527 0.0798 0.0054  -0.0043 -0.0082 194 TYR A OH   
2096 N  N    . PRO A 194 ? 0.1041 0.0697 0.0554 -0.0006 -0.0115 -0.0093 195 PRO A N    
2097 C  CA   . PRO A 194 ? 0.1062 0.0486 0.0793 0.0041  -0.0060 -0.0137 195 PRO A CA   
2098 C  C    . PRO A 194 ? 0.0926 0.0534 0.0746 -0.0057 -0.0204 -0.0041 195 PRO A C    
2099 O  O    . PRO A 194 ? 0.1032 0.0750 0.0688 0.0161  -0.0147 -0.0093 195 PRO A O    
2100 C  CB   . PRO A 194 ? 0.1142 0.0802 0.0802 0.0071  -0.0020 -0.0177 195 PRO A CB   
2101 C  CG   . PRO A 194 ? 0.1206 0.0976 0.0854 -0.0015 0.0015  -0.0232 195 PRO A CG   
2102 C  CD   . PRO A 194 ? 0.1256 0.0908 0.0676 -0.0115 -0.0012 -0.0151 195 PRO A CD   
2103 N  N    . GLY A 195 ? 0.0827 0.0456 0.0845 0.0215  -0.0131 -0.0129 196 GLY A N    
2104 C  CA   . GLY A 195 ? 0.0958 0.0421 0.0935 -0.0038 -0.0151 -0.0147 196 GLY A CA   
2105 C  C    . GLY A 195 ? 0.0949 0.0379 0.0784 0.0017  -0.0162 -0.0120 196 GLY A C    
2106 O  O    . GLY A 195 ? 0.1026 0.0476 0.0721 -0.0030 -0.0087 -0.0118 196 GLY A O    
2107 N  N    . SER A 196 ? 0.0876 0.0406 0.0890 -0.0052 -0.0088 -0.0080 197 SER A N    
2108 C  CA   . SER A 196 ? 0.0949 0.0423 0.0856 -0.0054 0.0082  -0.0114 197 SER A CA   
2109 C  C    . SER A 196 ? 0.0766 0.0315 0.0829 0.0010  -0.0027 -0.0073 197 SER A C    
2110 O  O    . SER A 196 ? 0.0816 0.0476 0.0757 0.0000  -0.0035 -0.0049 197 SER A O    
2111 C  CB   . SER A 196 ? 0.0854 0.0588 0.1026 -0.0102 -0.0006 -0.0131 197 SER A CB   
2112 O  OG   . SER A 196 ? 0.0824 0.0437 0.1039 0.0040  -0.0065 -0.0104 197 SER A OG   
2113 N  N    . LEU A 197 ? 0.0829 0.0402 0.0832 -0.0068 -0.0010 -0.0043 198 LEU A N    
2114 C  CA   . LEU A 197 ? 0.1005 0.0458 0.0689 -0.0051 0.0007  -0.0137 198 LEU A CA   
2115 C  C    . LEU A 197 ? 0.0827 0.0563 0.0850 -0.0035 0.0065  -0.0109 198 LEU A C    
2116 O  O    . LEU A 197 ? 0.0909 0.0491 0.0994 -0.0035 0.0059  -0.0148 198 LEU A O    
2117 C  CB   . LEU A 197 ? 0.1023 0.0476 0.0958 -0.0109 0.0148  -0.0167 198 LEU A CB   
2118 C  CG   . LEU A 197 ? 0.1527 0.1664 0.2466 0.0509  0.0568  0.0988  198 LEU A CG   
2119 C  CD1  . LEU A 197 ? 0.1562 0.1102 0.2488 0.0359  0.0727  0.0728  198 LEU A CD1  
2120 C  CD2  . LEU A 197 ? 0.2333 0.1903 0.2725 0.0627  0.0855  0.0925  198 LEU A CD2  
2121 N  N    . THR A 198 ? 0.0790 0.0502 0.0838 -0.0098 -0.0151 -0.0120 199 THR A N    
2122 C  CA   . THR A 198 ? 0.0825 0.0527 0.0926 0.0099  -0.0038 -0.0093 199 THR A CA   
2123 C  C    . THR A 198 ? 0.0816 0.0653 0.1039 -0.0131 0.0046  -0.0208 199 THR A C    
2124 O  O    . THR A 198 ? 0.0800 0.0572 0.1206 0.0041  0.0142  -0.0115 199 THR A O    
2125 C  CB   . THR A 198 ? 0.0949 0.0377 0.0900 -0.0108 -0.0082 -0.0087 199 THR A CB   
2126 O  OG1  . THR A 198 ? 0.0913 0.0502 0.0741 -0.0006 0.0104  -0.0006 199 THR A OG1  
2127 C  CG2  . THR A 198 ? 0.0718 0.0684 0.0816 -0.0043 0.0096  -0.0187 199 THR A CG2  
2128 N  N    . THR A 199 ? 0.0969 0.0595 0.1134 -0.0019 0.0241  -0.0230 200 THR A N    
2129 C  CA   . THR A 199 ? 0.1070 0.0715 0.1170 -0.0085 0.0258  -0.0181 200 THR A CA   
2130 C  C    . THR A 199 ? 0.0985 0.0741 0.1146 -0.0181 0.0147  -0.0046 200 THR A C    
2131 O  O    . THR A 199 ? 0.1071 0.0627 0.1265 -0.0142 0.0231  -0.0310 200 THR A O    
2132 C  CB   . THR A 199 ? 0.1093 0.0958 0.0940 -0.0276 0.0130  -0.0120 200 THR A CB   
2133 O  OG1  . THR A 199 ? 0.2014 0.0772 0.1286 0.0196  -0.0043 -0.0082 200 THR A OG1  
2134 C  CG2  . THR A 199 ? 0.1310 0.0825 0.1170 -0.0247 0.0038  -0.0159 200 THR A CG2  
2135 N  N    . PRO A 200 ? 0.1023 0.0721 0.1272 -0.0088 0.0296  -0.0200 201 PRO A N    
2136 C  CA   . PRO A 200 ? 0.1100 0.0935 0.1242 -0.0249 0.0192  -0.0141 201 PRO A CA   
2137 C  C    . PRO A 200 ? 0.1163 0.0838 0.1391 -0.0263 0.0195  -0.0227 201 PRO A C    
2138 O  O    . PRO A 200 ? 0.1565 0.0940 0.1380 -0.0153 0.0153  -0.0130 201 PRO A O    
2139 C  CB   . PRO A 200 ? 0.1082 0.1170 0.1545 -0.0240 0.0175  -0.0210 201 PRO A CB   
2140 C  CG   . PRO A 200 ? 0.1172 0.0987 0.1617 -0.0130 0.0225  -0.0333 201 PRO A CG   
2141 C  CD   . PRO A 200 ? 0.1149 0.1005 0.1411 -0.0109 0.0253  -0.0372 201 PRO A CD   
2142 N  N    . PRO A 201 ? 0.1116 0.0854 0.1315 -0.0204 0.0120  0.0003  202 PRO A N    
2143 C  CA   . PRO A 201 ? 0.1350 0.0879 0.1389 -0.0309 0.0197  -0.0076 202 PRO A CA   
2144 C  C    . PRO A 201 ? 0.1152 0.0606 0.1328 -0.0102 0.0063  -0.0140 202 PRO A C    
2145 O  O    . PRO A 201 ? 0.1102 0.0834 0.1561 -0.0298 0.0154  -0.0188 202 PRO A O    
2146 C  CB   . PRO A 201 ? 0.1757 0.0777 0.1712 -0.0412 0.0203  0.0013  202 PRO A CB   
2147 C  CG   . PRO A 201 ? 0.2007 0.0732 0.1651 -0.0115 0.0227  -0.0006 202 PRO A CG   
2148 C  CD   . PRO A 201 ? 0.1608 0.0924 0.1324 -0.0093 0.0222  -0.0043 202 PRO A CD   
2149 N  N    . LEU A 202 ? 0.0891 0.0666 0.1197 -0.0195 0.0043  -0.0142 203 LEU A N    
2150 C  CA   . LEU A 202 ? 0.0803 0.0535 0.1242 0.0023  -0.0052 -0.0165 203 LEU A CA   
2151 C  C    . LEU A 202 ? 0.0829 0.0662 0.1107 -0.0156 -0.0015 -0.0093 203 LEU A C    
2152 O  O    . LEU A 202 ? 0.0904 0.0588 0.1159 -0.0015 -0.0046 -0.0197 203 LEU A O    
2153 C  CB   . LEU A 202 ? 0.0762 0.0744 0.1337 -0.0010 0.0076  -0.0162 203 LEU A CB   
2154 C  CG   . LEU A 202 ? 0.0881 0.0745 0.1438 0.0063  0.0007  -0.0292 203 LEU A CG   
2155 C  CD1  . LEU A 202 ? 0.0952 0.0861 0.1971 -0.0103 0.0006  -0.0230 203 LEU A CD1  
2156 C  CD2  . LEU A 202 ? 0.1066 0.0588 0.1613 -0.0121 0.0164  -0.0419 203 LEU A CD2  
2157 N  N    . LEU A 203 ? 0.0913 0.0623 0.1195 0.0000  -0.0031 -0.0104 204 LEU A N    
2158 C  CA   . LEU A 203 ? 0.0969 0.0538 0.1289 -0.0051 -0.0012 -0.0159 204 LEU A CA   
2159 C  C    . LEU A 203 ? 0.0920 0.0354 0.1378 0.0010  -0.0031 -0.0147 204 LEU A C    
2160 O  O    . LEU A 203 ? 0.0976 0.0520 0.1088 -0.0141 -0.0038 -0.0175 204 LEU A O    
2161 C  CB   . LEU A 203 ? 0.1281 0.0490 0.1414 -0.0115 0.0140  -0.0085 204 LEU A CB   
2162 C  CG   . LEU A 203 ? 0.1386 0.0755 0.1678 0.0093  0.0414  0.0302  204 LEU A CG   
2163 C  CD1  . LEU A 203 ? 0.1596 0.0710 0.2141 0.0125  0.0546  0.0383  204 LEU A CD1  
2164 C  CD2  . LEU A 203 ? 0.1288 0.1396 0.3014 -0.0540 0.0093  0.0161  204 LEU A CD2  
2165 N  N    . GLU A 204 ? 0.0906 0.0548 0.1106 -0.0217 -0.0024 -0.0285 205 GLU A N    
2166 C  CA   . GLU A 204 ? 0.1054 0.0554 0.1026 -0.0062 -0.0233 -0.0307 205 GLU A CA   
2167 C  C    . GLU A 204 ? 0.0926 0.0525 0.1012 -0.0115 -0.0236 -0.0142 205 GLU A C    
2168 O  O    . GLU A 204 ? 0.1204 0.0904 0.1136 0.0046  -0.0137 -0.0357 205 GLU A O    
2169 C  CB   . GLU A 204 ? 0.1120 0.0788 0.1163 0.0010  -0.0254 -0.0280 205 GLU A CB   
2170 C  CG   . GLU A 204 ? 0.1041 0.0762 0.1145 -0.0031 -0.0088 -0.0255 205 GLU A CG   
2171 C  CD   . GLU A 204 ? 0.1159 0.0860 0.1295 0.0076  -0.0419 -0.0167 205 GLU A CD   
2172 O  OE1  . GLU A 204 ? 0.1430 0.1168 0.1875 0.0048  -0.0772 -0.0584 205 GLU A OE1  
2173 O  OE2  . GLU A 204 ? 0.1145 0.1009 0.1339 -0.0046 -0.0401 -0.0161 205 GLU A OE2  
2174 N  N    . CYS A 205 ? 0.0897 0.0450 0.1010 -0.0038 -0.0013 -0.0187 206 CYS A N    
2175 C  CA   . CYS A 205 ? 0.1124 0.0271 0.1039 -0.0109 -0.0088 0.0007  206 CYS A CA   
2176 C  C    . CYS A 205 ? 0.0899 0.0351 0.0969 0.0006  -0.0140 -0.0076 206 CYS A C    
2177 O  O    . CYS A 205 ? 0.1111 0.0455 0.1195 -0.0043 -0.0204 -0.0020 206 CYS A O    
2178 C  CB   . CYS A 205 ? 0.1141 0.0561 0.1046 -0.0063 0.0015  -0.0217 206 CYS A CB   
2179 S  SG   . CYS A 205 ? 0.1386 0.0600 0.0985 -0.0038 -0.0017 -0.0013 206 CYS A SG   
2180 N  N    . VAL A 206 ? 0.0917 0.0397 0.0969 0.0060  -0.0161 0.0013  207 VAL A N    
2181 C  CA   . VAL A 206 ? 0.0854 0.0406 0.0926 -0.0031 -0.0099 0.0017  207 VAL A CA   
2182 C  C    . VAL A 206 ? 0.1039 0.0430 0.0879 0.0118  -0.0288 0.0046  207 VAL A C    
2183 O  O    . VAL A 206 ? 0.0933 0.0618 0.1082 -0.0038 -0.0098 0.0093  207 VAL A O    
2184 C  CB   . VAL A 206 ? 0.0985 0.0536 0.0793 0.0113  -0.0030 0.0052  207 VAL A CB   
2185 C  CG1  . VAL A 206 ? 0.0836 0.0529 0.0942 -0.0119 -0.0082 -0.0195 207 VAL A CG1  
2186 C  CG2  . VAL A 206 ? 0.1111 0.0588 0.1008 -0.0006 0.0073  0.0005  207 VAL A CG2  
2187 N  N    . THR A 207 ? 0.1014 0.0315 0.0755 0.0098  -0.0109 -0.0035 208 THR A N    
2188 C  CA   . THR A 207 ? 0.1021 0.0533 0.0604 0.0020  -0.0019 0.0114  208 THR A CA   
2189 C  C    . THR A 207 ? 0.0921 0.0527 0.0482 -0.0051 -0.0051 0.0052  208 THR A C    
2190 O  O    . THR A 207 ? 0.0952 0.0415 0.0755 -0.0051 -0.0115 -0.0027 208 THR A O    
2191 C  CB   . THR A 207 ? 0.0895 0.0493 0.0802 -0.0027 -0.0102 0.0046  208 THR A CB   
2192 O  OG1  . THR A 207 ? 0.1172 0.0502 0.0942 0.0057  -0.0031 -0.0175 208 THR A OG1  
2193 C  CG2  . THR A 207 ? 0.1290 0.0700 0.0958 0.0088  0.0038  -0.0006 208 THR A CG2  
2194 N  N    . TRP A 208 ? 0.0899 0.0412 0.0547 0.0000  -0.0109 0.0043  209 TRP A N    
2195 C  CA   . TRP A 208 ? 0.0815 0.0388 0.0719 0.0005  -0.0131 0.0051  209 TRP A CA   
2196 C  C    . TRP A 208 ? 0.0904 0.0305 0.0658 0.0031  -0.0054 -0.0054 209 TRP A C    
2197 O  O    . TRP A 208 ? 0.0965 0.0559 0.0552 -0.0074 0.0063  0.0035  209 TRP A O    
2198 C  CB   . TRP A 208 ? 0.0802 0.0414 0.0706 -0.0003 -0.0142 0.0031  209 TRP A CB   
2199 C  CG   . TRP A 208 ? 0.0794 0.0270 0.0820 -0.0052 -0.0070 -0.0073 209 TRP A CG   
2200 C  CD1  . TRP A 208 ? 0.1163 0.0511 0.0626 0.0121  -0.0065 -0.0118 209 TRP A CD1  
2201 C  CD2  . TRP A 208 ? 0.0687 0.0451 0.0764 0.0010  -0.0164 -0.0035 209 TRP A CD2  
2202 N  NE1  . TRP A 208 ? 0.0782 0.0533 0.0890 -0.0065 -0.0031 -0.0024 209 TRP A NE1  
2203 C  CE2  . TRP A 208 ? 0.0878 0.0322 0.0882 0.0091  -0.0113 -0.0027 209 TRP A CE2  
2204 C  CE3  . TRP A 208 ? 0.0820 0.0394 0.0644 0.0024  -0.0007 0.0098  209 TRP A CE3  
2205 C  CZ2  . TRP A 208 ? 0.1032 0.0402 0.0834 0.0193  0.0220  -0.0080 209 TRP A CZ2  
2206 C  CZ3  . TRP A 208 ? 0.0863 0.0527 0.0854 -0.0024 -0.0087 0.0077  209 TRP A CZ3  
2207 C  CH2  . TRP A 208 ? 0.1075 0.0456 0.0926 0.0153  0.0034  -0.0093 209 TRP A CH2  
2208 N  N    . ILE A 209 ? 0.0847 0.0406 0.0608 -0.0035 0.0031  -0.0006 210 ILE A N    
2209 C  CA   . ILE A 209 ? 0.0781 0.0476 0.0719 -0.0054 -0.0131 0.0015  210 ILE A CA   
2210 C  C    . ILE A 209 ? 0.0890 0.0546 0.0606 -0.0038 -0.0038 0.0010  210 ILE A C    
2211 O  O    . ILE A 209 ? 0.1136 0.0429 0.0687 -0.0046 -0.0070 0.0010  210 ILE A O    
2212 C  CB   . ILE A 209 ? 0.0845 0.0521 0.0847 0.0003  0.0005  -0.0057 210 ILE A CB   
2213 C  CG1  . ILE A 209 ? 0.1127 0.0562 0.0942 0.0126  -0.0041 -0.0143 210 ILE A CG1  
2214 C  CG2  . ILE A 209 ? 0.0818 0.0694 0.1224 0.0012  -0.0076 -0.0049 210 ILE A CG2  
2215 C  CD1  . ILE A 209 ? 0.1145 0.0481 0.1910 0.0261  -0.0031 -0.0135 210 ILE A CD1  
2216 N  N    . VAL A 210 ? 0.0947 0.0464 0.0608 -0.0054 -0.0005 -0.0024 211 VAL A N    
2217 C  CA   . VAL A 210 ? 0.0860 0.0500 0.0613 -0.0074 -0.0027 0.0082  211 VAL A CA   
2218 C  C    . VAL A 210 ? 0.0881 0.0441 0.0791 0.0060  -0.0027 0.0006  211 VAL A C    
2219 O  O    . VAL A 210 ? 0.1032 0.0573 0.0727 -0.0164 -0.0031 0.0015  211 VAL A O    
2220 C  CB   . VAL A 210 ? 0.0969 0.0590 0.0674 -0.0043 -0.0076 0.0038  211 VAL A CB   
2221 C  CG1  . VAL A 210 ? 0.1115 0.0464 0.0960 0.0082  -0.0107 -0.0040 211 VAL A CG1  
2222 C  CG2  . VAL A 210 ? 0.0994 0.0662 0.0926 -0.0063 0.0017  -0.0013 211 VAL A CG2  
2223 N  N    . LEU A 211 ? 0.0864 0.0596 0.0755 -0.0065 -0.0037 0.0037  212 LEU A N    
2224 C  CA   . LEU A 211 ? 0.0763 0.0694 0.0818 -0.0073 -0.0020 -0.0068 212 LEU A CA   
2225 C  C    . LEU A 211 ? 0.0860 0.0631 0.0948 -0.0131 -0.0124 0.0026  212 LEU A C    
2226 O  O    . LEU A 211 ? 0.1023 0.0674 0.0895 -0.0099 -0.0065 0.0082  212 LEU A O    
2227 C  CB   . LEU A 211 ? 0.0956 0.0609 0.1076 -0.0065 -0.0148 0.0087  212 LEU A CB   
2228 C  CG   . LEU A 211 ? 0.0872 0.0885 0.1114 -0.0007 -0.0183 0.0031  212 LEU A CG   
2229 C  CD1  . LEU A 211 ? 0.1265 0.1188 0.1313 -0.0183 -0.0416 0.0131  212 LEU A CD1  
2230 C  CD2  . LEU A 211 ? 0.1064 0.0969 0.1356 0.0194  -0.0043 0.0019  212 LEU A CD2  
2231 N  N    . LYS A 212 ? 0.0996 0.0806 0.0969 -0.0164 -0.0035 -0.0006 213 LYS A N    
2232 C  CA   . LYS A 212 ? 0.1289 0.0653 0.0958 -0.0113 -0.0041 0.0109  213 LYS A CA   
2233 C  C    . LYS A 212 ? 0.1040 0.0653 0.0994 -0.0194 0.0124  0.0186  213 LYS A C    
2234 O  O    . LYS A 212 ? 0.1142 0.0768 0.1419 -0.0086 -0.0283 0.0186  213 LYS A O    
2235 C  CB   . LYS A 212 ? 0.1405 0.1186 0.0988 -0.0456 0.0164  0.0170  213 LYS A CB   
2236 C  CG   . LYS A 212 ? 0.1705 0.1387 0.1395 -0.0373 -0.0109 0.0443  213 LYS A CG   
2237 C  CD   . LYS A 212 ? 0.2818 0.1676 0.1581 -0.0728 -0.0006 0.0318  213 LYS A CD   
2238 C  CE   . LYS A 212 ? 0.3310 0.2461 0.2276 -0.0500 0.0228  0.0979  213 LYS A CE   
2239 N  NZ   . LYS A 212 ? 0.4070 0.3646 0.2666 -0.0811 0.0285  0.0604  213 LYS A NZ   
2240 N  N    . GLU A 213 ? 0.1057 0.0599 0.0958 -0.0041 -0.0054 0.0000  214 GLU A N    
2241 C  CA   . GLU A 213 ? 0.1070 0.0617 0.1186 -0.0103 -0.0057 0.0120  214 GLU A CA   
2242 C  C    . GLU A 213 ? 0.0966 0.0574 0.0939 -0.0098 -0.0098 0.0038  214 GLU A C    
2243 O  O    . GLU A 213 ? 0.0987 0.0572 0.1111 -0.0087 -0.0204 0.0060  214 GLU A O    
2244 C  CB   . GLU A 213 ? 0.1048 0.0821 0.1263 -0.0126 -0.0062 0.0110  214 GLU A CB   
2245 C  CG   . GLU A 213 ? 0.1382 0.1114 0.1443 -0.0315 -0.0320 0.0109  214 GLU A CG   
2246 C  CD   . GLU A 213 ? 0.1603 0.1444 0.1994 -0.0320 -0.0295 -0.0238 214 GLU A CD   
2247 O  OE1  . GLU A 213 ? 0.1358 0.0976 0.2861 -0.0280 -0.0745 0.0241  214 GLU A OE1  
2248 O  OE2  . GLU A 213 ? 0.2908 0.1865 0.3316 -0.0377 -0.0394 -0.0232 214 GLU A OE2  
2249 N  N    . PRO A 214 ? 0.1075 0.0605 0.0913 -0.0073 -0.0108 0.0034  215 PRO A N    
2250 C  CA   . PRO A 214 ? 0.1019 0.0623 0.1057 -0.0046 -0.0126 0.0015  215 PRO A CA   
2251 C  C    . PRO A 214 ? 0.1120 0.0667 0.1019 -0.0175 -0.0211 -0.0130 215 PRO A C    
2252 O  O    . PRO A 214 ? 0.1383 0.1018 0.1137 -0.0368 -0.0346 0.0104  215 PRO A O    
2253 C  CB   . PRO A 214 ? 0.1111 0.0581 0.1039 -0.0065 -0.0107 0.0019  215 PRO A CB   
2254 C  CG   . PRO A 214 ? 0.1773 0.1106 0.1685 -0.0241 -0.0142 -0.0065 215 PRO A CG   
2255 C  CD   . PRO A 214 ? 0.1319 0.0526 0.1233 -0.0062 0.0080  0.0184  215 PRO A CD   
2256 N  N    . ILE A 215 ? 0.1234 0.0512 0.0966 -0.0017 -0.0239 -0.0007 216 ILE A N    
2257 C  CA   . ILE A 215 ? 0.1249 0.0621 0.0920 0.0017  -0.0293 -0.0153 216 ILE A CA   
2258 C  C    . ILE A 215 ? 0.1158 0.0554 0.0949 -0.0086 -0.0239 -0.0119 216 ILE A C    
2259 O  O    . ILE A 215 ? 0.1143 0.0588 0.1342 0.0000  -0.0225 -0.0209 216 ILE A O    
2260 C  CB   . ILE A 215 ? 0.1484 0.0621 0.1136 0.0086  -0.0294 -0.0208 216 ILE A CB   
2261 C  CG1  . ILE A 215 ? 0.2222 0.0596 0.0820 0.0088  -0.0394 0.0017  216 ILE A CG1  
2262 C  CG2  . ILE A 215 ? 0.1930 0.0789 0.1237 0.0331  -0.0386 -0.0087 216 ILE A CG2  
2263 C  CD1  . ILE A 215 ? 0.2167 0.0895 0.1323 -0.0037 -0.0450 0.0024  216 ILE A CD1  
2264 N  N    A SER A 216 ? 0.0951 0.0662 0.1170 0.0197  -0.0364 0.0006  217 SER A N    
2265 N  N    B SER A 216 ? 0.1391 0.0721 0.1262 -0.0017 -0.0337 -0.0244 217 SER A N    
2266 C  CA   A SER A 216 ? 0.1368 0.0696 0.1019 -0.0023 -0.0261 -0.0184 217 SER A CA   
2267 C  CA   B SER A 216 ? 0.1517 0.0669 0.1098 -0.0093 -0.0265 -0.0228 217 SER A CA   
2268 C  C    A SER A 216 ? 0.1475 0.0493 0.1213 -0.0006 -0.0370 -0.0181 217 SER A C    
2269 C  C    B SER A 216 ? 0.1509 0.0502 0.1265 -0.0126 -0.0394 -0.0232 217 SER A C    
2270 O  O    A SER A 216 ? 0.1249 0.0797 0.1314 0.0104  -0.0328 -0.0126 217 SER A O    
2271 O  O    B SER A 216 ? 0.1624 0.0658 0.1199 -0.0087 -0.0390 0.0120  217 SER A O    
2272 C  CB   A SER A 216 ? 0.2109 0.0642 0.1299 -0.0093 0.0082  -0.0092 217 SER A CB   
2273 C  CB   B SER A 216 ? 0.2158 0.0906 0.1493 -0.0218 -0.0092 -0.0263 217 SER A CB   
2274 O  OG   A SER A 216 ? 0.1641 0.0807 0.1154 -0.0331 -0.0322 0.0046  217 SER A OG   
2275 O  OG   B SER A 216 ? 0.2691 0.1559 0.1689 -0.0087 -0.0048 -0.0329 217 SER A OG   
2276 N  N    . VAL A 217 ? 0.1423 0.0579 0.0974 -0.0086 -0.0419 -0.0060 218 VAL A N    
2277 C  CA   . VAL A 217 ? 0.1714 0.0518 0.0983 0.0013  -0.0333 -0.0031 218 VAL A CA   
2278 C  C    . VAL A 217 ? 0.1583 0.0542 0.0952 -0.0175 -0.0317 -0.0129 218 VAL A C    
2279 O  O    . VAL A 217 ? 0.1718 0.0441 0.1018 -0.0137 -0.0307 -0.0059 218 VAL A O    
2280 C  CB   . VAL A 217 ? 0.1845 0.0447 0.1224 -0.0076 -0.0370 -0.0065 218 VAL A CB   
2281 C  CG1  . VAL A 217 ? 0.1962 0.0545 0.1233 -0.0132 -0.0220 -0.0203 218 VAL A CG1  
2282 C  CG2  . VAL A 217 ? 0.1515 0.0553 0.1632 -0.0057 -0.0296 -0.0107 218 VAL A CG2  
2283 N  N    . SER A 218 ? 0.1867 0.0437 0.1093 -0.0131 -0.0266 -0.0088 219 SER A N    
2284 C  CA   . SER A 218 ? 0.1852 0.0485 0.1093 -0.0020 -0.0195 -0.0062 219 SER A CA   
2285 C  C    . SER A 218 ? 0.1996 0.0335 0.1170 -0.0020 -0.0249 -0.0171 219 SER A C    
2286 O  O    . SER A 218 ? 0.1789 0.0499 0.1267 -0.0086 -0.0176 -0.0081 219 SER A O    
2287 C  CB   . SER A 218 ? 0.2193 0.0525 0.1005 0.0035  -0.0273 -0.0217 219 SER A CB   
2288 O  OG   . SER A 218 ? 0.2348 0.0648 0.1082 -0.0199 -0.0326 0.0019  219 SER A OG   
2289 N  N    A SER A 219 ? 0.1676 0.0279 0.1267 -0.0129 -0.0219 -0.0096 220 SER A N    
2290 N  N    B SER A 219 ? 0.1616 0.0270 0.1344 -0.0151 -0.0173 0.0016  220 SER A N    
2291 C  CA   A SER A 219 ? 0.2035 0.0746 0.1456 -0.0063 -0.0280 -0.0026 220 SER A CA   
2292 C  CA   B SER A 219 ? 0.2000 0.0834 0.1588 -0.0140 -0.0204 0.0115  220 SER A CA   
2293 C  C    A SER A 219 ? 0.2120 0.0524 0.1599 -0.0030 -0.0091 -0.0115 220 SER A C    
2294 C  C    B SER A 219 ? 0.1946 0.0474 0.1730 -0.0142 0.0027  -0.0037 220 SER A C    
2295 O  O    A SER A 219 ? 0.2032 0.0983 0.1612 0.0126  -0.0024 -0.0074 220 SER A O    
2296 O  O    B SER A 219 ? 0.1883 0.0563 0.2071 -0.0027 0.0171  -0.0015 220 SER A O    
2297 C  CB   A SER A 219 ? 0.2138 0.0921 0.1615 0.0041  -0.0131 -0.0030 220 SER A CB   
2298 C  CB   B SER A 219 ? 0.1863 0.0881 0.1565 -0.0291 -0.0006 0.0247  220 SER A CB   
2299 O  OG   A SER A 219 ? 0.2405 0.0383 0.1344 0.0119  -0.0186 -0.0373 220 SER A OG   
2300 O  OG   B SER A 219 ? 0.2263 0.0868 0.2010 0.0131  -0.0137 -0.0043 220 SER A OG   
2301 N  N    . GLU A 220 ? 0.2025 0.0630 0.1331 -0.0248 0.0005  -0.0098 221 GLU A N    
2302 C  CA   . GLU A 220 ? 0.2493 0.0712 0.1371 -0.0040 -0.0070 -0.0219 221 GLU A CA   
2303 C  C    . GLU A 220 ? 0.2438 0.0689 0.1184 0.0088  -0.0060 0.0006  221 GLU A C    
2304 O  O    . GLU A 220 ? 0.2732 0.0771 0.1221 0.0054  0.0204  -0.0071 221 GLU A O    
2305 C  CB   . GLU A 220 ? 0.2973 0.0951 0.1188 -0.0273 -0.0135 -0.0270 221 GLU A CB   
2306 C  CG   . GLU A 220 ? 0.3240 0.1335 0.1807 -0.0181 -0.0366 -0.0505 221 GLU A CG   
2307 C  CD   . GLU A 220 ? 0.3982 0.2217 0.2637 -0.0379 0.0107  -0.0225 221 GLU A CD   
2308 O  OE1  . GLU A 220 ? 0.2529 0.1387 0.2504 -0.0487 -0.0124 -0.0546 221 GLU A OE1  
2309 O  OE2  . GLU A 220 ? 0.5054 0.3212 0.4239 -0.0877 0.0425  -0.0825 221 GLU A OE2  
2310 N  N    . GLN A 221 ? 0.2199 0.0517 0.1158 -0.0197 -0.0164 -0.0071 222 GLN A N    
2311 C  CA   . GLN A 221 ? 0.2118 0.0595 0.1123 -0.0124 -0.0132 -0.0023 222 GLN A CA   
2312 C  C    . GLN A 221 ? 0.2026 0.0503 0.1340 -0.0013 -0.0051 0.0107  222 GLN A C    
2313 O  O    . GLN A 221 ? 0.2167 0.0702 0.1199 -0.0244 -0.0059 0.0054  222 GLN A O    
2314 C  CB   . GLN A 221 ? 0.2284 0.0483 0.0967 -0.0155 -0.0219 -0.0082 222 GLN A CB   
2315 C  CG   . GLN A 221 ? 0.2113 0.0560 0.0997 -0.0274 -0.0425 0.0076  222 GLN A CG   
2316 C  CD   . GLN A 221 ? 0.1913 0.0618 0.1053 -0.0080 -0.0351 -0.0068 222 GLN A CD   
2317 O  OE1  . GLN A 221 ? 0.2057 0.0511 0.1163 0.0049  -0.0317 -0.0065 222 GLN A OE1  
2318 N  NE2  . GLN A 221 ? 0.2312 0.0579 0.1215 -0.0024 -0.0520 0.0013  222 GLN A NE2  
2319 N  N    . VAL A 222 ? 0.2035 0.0656 0.1145 -0.0361 -0.0195 0.0156  223 VAL A N    
2320 C  CA   . VAL A 222 ? 0.2080 0.0750 0.1346 -0.0241 -0.0065 0.0335  223 VAL A CA   
2321 C  C    . VAL A 222 ? 0.1976 0.0640 0.1270 -0.0076 -0.0065 0.0244  223 VAL A C    
2322 O  O    . VAL A 222 ? 0.1992 0.0863 0.1429 -0.0171 0.0054  0.0205  223 VAL A O    
2323 C  CB   . VAL A 222 ? 0.2296 0.1098 0.1653 -0.0107 -0.0280 0.0425  223 VAL A CB   
2324 C  CG1  . VAL A 222 ? 0.2075 0.1696 0.2181 -0.0329 -0.0461 0.0394  223 VAL A CG1  
2325 C  CG2  . VAL A 222 ? 0.2195 0.1383 0.1753 -0.0096 -0.0447 0.0102  223 VAL A CG2  
2326 N  N    . LEU A 223 ? 0.2046 0.0917 0.1475 -0.0198 -0.0038 0.0175  224 LEU A N    
2327 C  CA   . LEU A 223 ? 0.2138 0.0860 0.1967 -0.0184 0.0043  -0.0077 224 LEU A CA   
2328 C  C    . LEU A 223 ? 0.2348 0.1005 0.1492 -0.0170 -0.0081 -0.0295 224 LEU A C    
2329 O  O    . LEU A 223 ? 0.2333 0.1346 0.1657 -0.0160 0.0265  -0.0164 224 LEU A O    
2330 C  CB   . LEU A 223 ? 0.2389 0.1145 0.2355 -0.0273 0.0082  -0.0383 224 LEU A CB   
2331 C  CG   . LEU A 223 ? 0.3016 0.1348 0.2203 -0.0258 0.0379  -0.0035 224 LEU A CG   
2332 C  CD1  . LEU A 223 ? 0.3533 0.1574 0.3361 -0.0131 0.0186  -0.0281 224 LEU A CD1  
2333 C  CD2  . LEU A 223 ? 0.2896 0.1438 0.3203 0.0020  0.0522  -0.0218 224 LEU A CD2  
2334 N  N    . LYS A 224 ? 0.2260 0.0978 0.1287 -0.0259 0.0000  -0.0104 225 LYS A N    
2335 C  CA   . LYS A 224 ? 0.2409 0.1308 0.1237 -0.0137 0.0093  -0.0043 225 LYS A CA   
2336 C  C    . LYS A 224 ? 0.2382 0.0775 0.1109 -0.0030 -0.0099 0.0073  225 LYS A C    
2337 O  O    . LYS A 224 ? 0.2655 0.1137 0.0994 -0.0361 0.0142  0.0093  225 LYS A O    
2338 C  CB   . LYS A 224 ? 0.2770 0.1707 0.1535 -0.0113 -0.0020 0.0291  225 LYS A CB   
2339 C  CG   . LYS A 224 ? 0.2633 0.2002 0.2057 -0.0219 -0.0265 0.0104  225 LYS A CG   
2340 C  CD   . LYS A 224 ? 0.3424 0.1565 0.2291 -0.0222 -0.0366 -0.0271 225 LYS A CD   
2341 C  CE   . LYS A 224 ? 0.3603 0.2030 0.2346 -0.0109 -0.0182 -0.0546 225 LYS A CE   
2342 N  NZ   . LYS A 224 ? 0.3889 0.2027 0.3479 -0.0109 -0.0372 -0.0661 225 LYS A NZ   
2343 N  N    . PHE A 225 ? 0.2201 0.0701 0.0909 -0.0054 0.0152  0.0085  226 PHE A N    
2344 C  CA   . PHE A 225 ? 0.2175 0.0702 0.1032 -0.0219 0.0197  0.0131  226 PHE A CA   
2345 C  C    . PHE A 225 ? 0.2312 0.0591 0.0854 -0.0208 0.0186  0.0007  226 PHE A C    
2346 O  O    . PHE A 225 ? 0.2381 0.0785 0.0838 -0.0361 0.0285  -0.0230 226 PHE A O    
2347 C  CB   . PHE A 225 ? 0.1987 0.0714 0.1026 -0.0162 0.0244  0.0125  226 PHE A CB   
2348 C  CG   . PHE A 225 ? 0.2240 0.0543 0.1102 -0.0399 0.0164  -0.0205 226 PHE A CG   
2349 C  CD1  . PHE A 225 ? 0.2587 0.1173 0.1296 0.0215  0.0269  -0.0040 226 PHE A CD1  
2350 C  CD2  . PHE A 225 ? 0.2179 0.1448 0.1483 -0.0342 -0.0031 -0.0443 226 PHE A CD2  
2351 C  CE1  . PHE A 225 ? 0.2888 0.1224 0.1409 0.0353  0.0167  0.0162  226 PHE A CE1  
2352 C  CE2  . PHE A 225 ? 0.2301 0.1520 0.1683 -0.0362 0.0081  -0.0803 226 PHE A CE2  
2353 C  CZ   . PHE A 225 ? 0.2466 0.0829 0.1917 -0.0104 -0.0051 -0.0692 226 PHE A CZ   
2354 N  N    . ARG A 226 ? 0.1935 0.0671 0.0909 -0.0156 0.0176  -0.0088 227 ARG A N    
2355 C  CA   . ARG A 226 ? 0.2050 0.0847 0.0961 -0.0244 0.0148  -0.0142 227 ARG A CA   
2356 C  C    . ARG A 226 ? 0.2276 0.0657 0.1313 -0.0238 0.0296  -0.0174 227 ARG A C    
2357 O  O    . ARG A 226 ? 0.2375 0.0996 0.1125 -0.0164 0.0318  -0.0048 227 ARG A O    
2358 C  CB   . ARG A 226 ? 0.2258 0.0714 0.1032 -0.0236 0.0125  0.0024  227 ARG A CB   
2359 C  CG   . ARG A 226 ? 0.2021 0.0863 0.1073 -0.0208 0.0119  -0.0052 227 ARG A CG   
2360 C  CD   . ARG A 226 ? 0.2545 0.0824 0.1346 -0.0249 0.0126  0.0098  227 ARG A CD   
2361 N  NE   . ARG A 226 ? 0.2278 0.0658 0.1005 -0.0491 -0.0085 -0.0088 227 ARG A NE   
2362 C  CZ   . ARG A 226 ? 0.2504 0.0948 0.0956 -0.0502 -0.0147 -0.0142 227 ARG A CZ   
2363 N  NH1  . ARG A 226 ? 0.2721 0.1333 0.1562 -0.0535 0.0015  -0.0269 227 ARG A NH1  
2364 N  NH2  . ARG A 226 ? 0.2709 0.0820 0.0969 -0.0812 -0.0120 -0.0165 227 ARG A NH2  
2365 N  N    . LYS A 227 ? 0.1973 0.0865 0.0935 -0.0219 0.0161  -0.0187 228 LYS A N    
2366 C  CA   . LYS A 227 ? 0.2490 0.1048 0.1096 -0.0381 0.0357  -0.0357 228 LYS A CA   
2367 C  C    . LYS A 227 ? 0.2583 0.1080 0.0712 -0.0388 0.0315  -0.0113 228 LYS A C    
2368 O  O    . LYS A 227 ? 0.3070 0.1170 0.0917 -0.0553 0.0359  -0.0302 228 LYS A O    
2369 C  CB   . LYS A 227 ? 0.2617 0.1188 0.1003 -0.0447 0.0046  -0.0326 228 LYS A CB   
2370 C  CG   . LYS A 227 ? 0.2818 0.1605 0.1429 -0.0544 0.0164  -0.0322 228 LYS A CG   
2371 C  CD   . LYS A 227 ? 0.3147 0.2041 0.2389 -0.0803 0.0005  -0.0388 228 LYS A CD   
2372 C  CE   . LYS A 227 ? 0.3528 0.3662 0.2851 -0.0614 -0.0193 -0.0377 228 LYS A CE   
2373 N  NZ   . LYS A 227 ? 0.4571 0.4627 0.3445 -0.0197 -0.0522 -0.0666 228 LYS A NZ   
2374 N  N    A LEU A 228 ? 0.2596 0.0773 0.0685 -0.0436 0.0313  -0.0098 229 LEU A N    
2375 N  N    B LEU A 228 ? 0.2184 0.0631 0.0471 -0.0364 0.0229  -0.0166 229 LEU A N    
2376 C  CA   A LEU A 228 ? 0.2368 0.0640 0.0926 -0.0253 0.0188  -0.0068 229 LEU A CA   
2377 C  CA   B LEU A 228 ? 0.1865 0.0829 0.0590 -0.0252 0.0131  -0.0131 229 LEU A CA   
2378 C  C    A LEU A 228 ? 0.2316 0.1062 0.0872 -0.0228 0.0197  -0.0173 229 LEU A C    
2379 C  C    B LEU A 228 ? 0.1538 0.0870 0.0420 -0.0392 -0.0068 -0.0219 229 LEU A C    
2380 O  O    A LEU A 228 ? 0.2283 0.0992 0.1062 -0.0379 0.0366  -0.0225 229 LEU A O    
2381 O  O    B LEU A 228 ? 0.1533 0.0653 0.0653 -0.0003 0.0137  0.0010  229 LEU A O    
2382 C  CB   A LEU A 228 ? 0.2424 0.1252 0.0660 -0.0177 0.0244  -0.0215 229 LEU A CB   
2383 C  CB   B LEU A 228 ? 0.1831 0.0603 0.0411 -0.0282 0.0251  -0.0170 229 LEU A CB   
2384 C  CG   A LEU A 228 ? 0.2370 0.1048 0.1120 -0.0399 0.0114  -0.0151 229 LEU A CG   
2385 C  CG   B LEU A 228 ? 0.1906 0.0458 0.0728 -0.0099 0.0142  0.0017  229 LEU A CG   
2386 C  CD1  A LEU A 228 ? 0.2432 0.1035 0.1392 -0.0034 0.0277  -0.0344 229 LEU A CD1  
2387 C  CD1  B LEU A 228 ? 0.2078 0.0931 0.0572 -0.0120 0.0403  -0.0216 229 LEU A CD1  
2388 C  CD2  A LEU A 228 ? 0.1933 0.1454 0.1486 0.0082  -0.0142 0.0218  229 LEU A CD2  
2389 C  CD2  B LEU A 228 ? 0.2181 0.0723 0.0653 -0.0348 -0.0241 0.0141  229 LEU A CD2  
2390 N  N    A ASN A 229 ? 0.1996 0.1003 0.0856 -0.0109 0.0063  -0.0020 230 ASN A N    
2391 N  N    B ASN A 229 ? 0.1418 0.0674 0.0660 -0.0148 0.0030  0.0024  230 ASN A N    
2392 C  CA   A ASN A 229 ? 0.1893 0.0878 0.0748 -0.0454 0.0080  0.0027  230 ASN A CA   
2393 C  CA   B ASN A 229 ? 0.1286 0.0660 0.0590 -0.0038 -0.0005 0.0054  230 ASN A CA   
2394 C  C    A ASN A 229 ? 0.1650 0.0718 0.0953 -0.0318 0.0148  0.0098  230 ASN A C    
2395 C  C    B ASN A 229 ? 0.1128 0.0572 0.0942 0.0096  0.0038  0.0175  230 ASN A C    
2396 O  O    A ASN A 229 ? 0.1371 0.1028 0.0685 0.0013  -0.0124 0.0148  230 ASN A O    
2397 O  O    B ASN A 229 ? 0.1154 0.0719 0.0608 0.0003  -0.0241 0.0153  230 ASN A O    
2398 C  CB   A ASN A 229 ? 0.1999 0.1134 0.0662 -0.0103 0.0003  0.0005  230 ASN A CB   
2399 C  CB   B ASN A 229 ? 0.1310 0.0793 0.0621 -0.0177 -0.0051 0.0031  230 ASN A CB   
2400 C  CG   A ASN A 229 ? 0.2493 0.1299 0.0671 -0.0397 0.0243  -0.0207 230 ASN A CG   
2401 C  CG   B ASN A 229 ? 0.2352 0.1310 0.0773 0.0000  -0.0038 -0.0280 230 ASN A CG   
2402 O  OD1  A ASN A 229 ? 0.3355 0.1262 0.1773 -0.0538 0.0000  -0.0057 230 ASN A OD1  
2403 O  OD1  B ASN A 229 ? 0.2334 0.0987 0.0845 -0.0518 0.0176  -0.0281 230 ASN A OD1  
2404 N  ND2  A ASN A 229 ? 0.2935 0.0843 0.0483 -0.0644 0.0589  -0.0350 230 ASN A ND2  
2405 N  ND2  B ASN A 229 ? 0.1993 0.1441 0.1177 0.0019  0.0024  0.0005  230 ASN A ND2  
2406 N  N    A PHE A 230 ? 0.1763 0.1155 0.0658 -0.0662 0.0216  -0.0151 231 PHE A N    
2407 N  N    B PHE A 230 ? 0.1194 0.0829 0.0879 0.0006  0.0057  -0.0108 231 PHE A N    
2408 C  CA   A PHE A 230 ? 0.1793 0.1206 0.1012 -0.0666 0.0305  -0.0225 231 PHE A CA   
2409 C  CA   B PHE A 230 ? 0.1058 0.0554 0.0988 0.0020  -0.0082 0.0155  231 PHE A CA   
2410 C  C    A PHE A 230 ? 0.1996 0.1353 0.0895 -0.0718 0.0419  -0.0263 231 PHE A C    
2411 C  C    B PHE A 230 ? 0.1349 0.0843 0.1000 -0.0250 -0.0068 0.0038  231 PHE A C    
2412 O  O    A PHE A 230 ? 0.2346 0.1242 0.0983 -0.0922 0.0644  -0.0482 231 PHE A O    
2413 O  O    B PHE A 230 ? 0.1657 0.1215 0.1132 -0.0392 -0.0038 0.0126  231 PHE A O    
2414 C  CB   A PHE A 230 ? 0.2014 0.1213 0.0856 -0.0610 0.0286  -0.0282 231 PHE A CB   
2415 C  CB   B PHE A 230 ? 0.1044 0.0626 0.1384 0.0291  0.0043  0.0142  231 PHE A CB   
2416 C  CG   A PHE A 230 ? 0.2019 0.1351 0.0944 -0.0768 0.0529  0.0102  231 PHE A CG   
2417 C  CG   B PHE A 230 ? 0.1238 0.0640 0.1023 0.0164  -0.0320 0.0251  231 PHE A CG   
2418 C  CD1  A PHE A 230 ? 0.2077 0.1507 0.0635 -0.0828 0.0386  -0.0551 231 PHE A CD1  
2419 C  CD1  B PHE A 230 ? 0.1064 0.1028 0.0947 0.0096  0.0031  0.0236  231 PHE A CD1  
2420 C  CD2  A PHE A 230 ? 0.2143 0.1305 0.1154 -0.0737 0.0328  -0.0147 231 PHE A CD2  
2421 C  CD2  B PHE A 230 ? 0.1332 0.1190 0.0746 0.0603  0.0034  0.0043  231 PHE A CD2  
2422 C  CE1  A PHE A 230 ? 0.2061 0.1283 0.0498 -0.0755 0.0439  -0.0423 231 PHE A CE1  
2423 C  CE1  B PHE A 230 ? 0.1664 0.0870 0.1199 0.0296  -0.0107 -0.0024 231 PHE A CE1  
2424 C  CE2  A PHE A 230 ? 0.2086 0.1215 0.0983 -0.0847 0.0186  -0.0175 231 PHE A CE2  
2425 C  CE2  B PHE A 230 ? 0.1313 0.0591 0.1304 0.0276  -0.0046 -0.0054 231 PHE A CE2  
2426 C  CZ   A PHE A 230 ? 0.2036 0.1380 0.0741 -0.0921 0.0401  -0.0593 231 PHE A CZ   
2427 C  CZ   B PHE A 230 ? 0.1412 0.1247 0.0951 -0.0060 -0.0220 0.0140  231 PHE A CZ   
2428 N  N    A ASN A 231 ? 0.2073 0.0926 0.0881 -0.0645 0.0527  -0.0270 232 ASN A N    
2429 N  N    B ASN A 231 ? 0.1208 0.1084 0.0951 -0.0120 -0.0086 0.0233  232 ASN A N    
2430 C  CA   A ASN A 231 ? 0.1879 0.1109 0.1048 -0.0381 0.0476  -0.0040 232 ASN A CA   
2431 C  CA   B ASN A 231 ? 0.1295 0.0964 0.1003 0.0093  -0.0218 0.0315  232 ASN A CA   
2432 C  C    A ASN A 231 ? 0.2170 0.1091 0.1010 -0.0215 0.0423  -0.0148 232 ASN A C    
2433 C  C    B ASN A 231 ? 0.0958 0.1204 0.0942 0.0115  -0.0027 0.0258  232 ASN A C    
2434 O  O    A ASN A 231 ? 0.1985 0.0897 0.0978 -0.0019 0.0439  -0.0082 232 ASN A O    
2435 O  O    B ASN A 231 ? 0.1066 0.1190 0.1231 0.0549  -0.0096 0.0082  232 ASN A O    
2436 C  CB   A ASN A 231 ? 0.2097 0.1263 0.0617 -0.0219 0.0403  -0.0065 232 ASN A CB   
2437 C  CB   B ASN A 231 ? 0.1304 0.1109 0.0816 0.0282  0.0015  0.0353  232 ASN A CB   
2438 C  CG   A ASN A 231 ? 0.2206 0.0935 0.1100 -0.0108 0.0423  -0.0188 232 ASN A CG   
2439 C  CG   B ASN A 231 ? 0.1274 0.0877 0.1120 0.0417  0.0115  -0.0040 232 ASN A CG   
2440 O  OD1  A ASN A 231 ? 0.1826 0.0847 0.1133 -0.0126 0.0450  -0.0062 232 ASN A OD1  
2441 O  OD1  B ASN A 231 ? 0.1544 0.1005 0.1067 0.0423  0.0274  0.0252  232 ASN A OD1  
2442 N  ND2  A ASN A 231 ? 0.2075 0.1096 0.1262 -0.0006 0.0322  -0.0126 232 ASN A ND2  
2443 N  ND2  B ASN A 231 ? 0.1321 0.1777 0.0957 0.0684  0.0185  0.0170  232 ASN A ND2  
2444 N  N    A GLY A 232 ? 0.2208 0.0964 0.1247 -0.0220 0.0688  0.0006  233 GLY A N    
2445 N  N    B GLY A 232 ? 0.1127 0.0965 0.1039 0.0348  -0.0109 0.0361  233 GLY A N    
2446 C  CA   A GLY A 232 ? 0.2500 0.1316 0.1368 -0.0270 0.0533  -0.0063 233 GLY A CA   
2447 C  CA   B GLY A 232 ? 0.1039 0.1028 0.1271 0.0373  0.0104  0.0221  233 GLY A CA   
2448 C  C    A GLY A 232 ? 0.2879 0.1344 0.1579 -0.0241 0.0732  0.0054  233 GLY A C    
2449 C  C    B GLY A 232 ? 0.1312 0.1005 0.1446 0.0619  -0.0248 0.0379  233 GLY A C    
2450 O  O    A GLY A 232 ? 0.3571 0.1330 0.1906 -0.0196 0.1181  0.0000  233 GLY A O    
2451 O  O    B GLY A 232 ? 0.1714 0.1438 0.1215 0.1080  0.0438  0.0493  233 GLY A O    
2452 N  N    A GLU A 233 ? 0.2874 0.1745 0.1531 -0.0305 0.0425  -0.0164 234 GLU A N    
2453 N  N    B GLU A 233 ? 0.1403 0.0947 0.1190 0.0255  -0.0131 0.0126  234 GLU A N    
2454 C  CA   A GLU A 233 ? 0.2779 0.1845 0.1535 -0.0329 0.0502  -0.0239 234 GLU A CA   
2455 C  CA   B GLU A 233 ? 0.1550 0.1093 0.1128 0.0351  -0.0175 0.0142  234 GLU A CA   
2456 C  C    A GLU A 233 ? 0.2883 0.1804 0.1875 -0.0302 0.0346  -0.0220 234 GLU A C    
2457 C  C    B GLU A 233 ? 0.1976 0.1351 0.1062 0.0284  -0.0104 0.0414  234 GLU A C    
2458 O  O    A GLU A 233 ? 0.3296 0.2197 0.1483 -0.0549 0.1066  -0.0261 234 GLU A O    
2459 O  O    B GLU A 233 ? 0.1620 0.1423 0.1665 0.0434  0.0060  0.0370  234 GLU A O    
2460 C  CB   A GLU A 233 ? 0.2526 0.1859 0.1473 -0.0315 0.0185  -0.0236 234 GLU A CB   
2461 C  CB   B GLU A 233 ? 0.1739 0.1387 0.1014 0.0148  -0.0205 0.0308  234 GLU A CB   
2462 C  CG   A GLU A 233 ? 0.2635 0.1999 0.1610 -0.0458 0.0262  -0.0103 234 GLU A CG   
2463 C  CG   B GLU A 233 ? 0.1955 0.1313 0.1026 -0.0219 0.0027  0.0126  234 GLU A CG   
2464 C  CD   A GLU A 233 ? 0.2490 0.2328 0.1565 -0.0173 0.0715  -0.0076 234 GLU A CD   
2465 C  CD   B GLU A 233 ? 0.2118 0.2157 0.1678 0.0329  -0.0057 -0.0147 234 GLU A CD   
2466 O  OE1  A GLU A 233 ? 0.3154 0.1491 0.1888 -0.0395 0.0617  0.0592  234 GLU A OE1  
2467 O  OE1  B GLU A 233 ? 0.3064 0.3716 0.3208 0.0851  0.0219  -0.0469 234 GLU A OE1  
2468 O  OE2  A GLU A 233 ? 0.3217 0.2797 0.1161 0.0186  0.0135  0.0151  234 GLU A OE2  
2469 O  OE2  B GLU A 233 ? 0.2339 0.2082 0.1407 -0.0059 0.0216  0.0010  234 GLU A OE2  
2470 N  N    A GLY A 234 ? 0.2694 0.1446 0.1536 -0.0068 0.0260  -0.0252 235 GLY A N    
2471 N  N    B GLY A 234 ? 0.2339 0.2060 0.1827 0.0211  0.0038  -0.0076 235 GLY A N    
2472 C  CA   A GLY A 234 ? 0.2249 0.1588 0.1497 0.0241  0.0097  0.0098  235 GLY A CA   
2473 C  CA   B GLY A 234 ? 0.2312 0.2102 0.1856 0.0041  -0.0013 -0.0175 235 GLY A CA   
2474 C  C    A GLY A 234 ? 0.2102 0.1277 0.1276 0.0220  -0.0185 0.0441  235 GLY A C    
2475 C  C    B GLY A 234 ? 0.2554 0.2587 0.2064 -0.0076 -0.0019 -0.0015 235 GLY A C    
2476 O  O    A GLY A 234 ? 0.2079 0.2043 0.1434 0.0071  0.0120  -0.0024 235 GLY A O    
2477 O  O    B GLY A 234 ? 0.2948 0.2628 0.2098 -0.0337 0.0188  -0.0068 235 GLY A O    
2478 N  N    A GLU A 235 ? 0.1462 0.1409 0.1623 0.0355  0.0093  0.0351  236 GLU A N    
2479 N  N    B GLU A 235 ? 0.2432 0.2549 0.2055 -0.0181 0.0115  -0.0027 236 GLU A N    
2480 C  CA   A GLU A 235 ? 0.1541 0.0832 0.1278 0.0535  -0.0038 0.0428  236 GLU A CA   
2481 C  CA   B GLU A 235 ? 0.2393 0.2185 0.2050 -0.0107 0.0186  -0.0153 236 GLU A CA   
2482 C  C    A GLU A 235 ? 0.1696 0.1398 0.1604 0.0015  0.0118  0.0456  236 GLU A C    
2483 C  C    B GLU A 235 ? 0.2061 0.2305 0.1723 -0.0093 0.0399  -0.0059 236 GLU A C    
2484 O  O    A GLU A 235 ? 0.1599 0.1150 0.1612 0.0196  0.0041  0.0186  236 GLU A O    
2485 O  O    B GLU A 235 ? 0.2671 0.2321 0.1899 -0.0082 0.0397  -0.0219 236 GLU A O    
2486 C  CB   A GLU A 235 ? 0.1455 0.0965 0.1610 0.0766  0.0087  0.0313  236 GLU A CB   
2487 C  CB   B GLU A 235 ? 0.2463 0.2373 0.2014 -0.0219 0.0368  -0.0080 236 GLU A CB   
2488 C  CG   A GLU A 235 ? 0.1624 0.1351 0.1331 0.0368  0.0230  0.0098  236 GLU A CG   
2489 C  CG   B GLU A 235 ? 0.2854 0.1448 0.2273 0.0068  0.0375  -0.0200 236 GLU A CG   
2490 C  CD   A GLU A 235 ? 0.1644 0.1322 0.1526 0.0214  0.0148  0.0432  236 GLU A CD   
2491 C  CD   B GLU A 235 ? 0.2603 0.1829 0.2409 -0.0355 0.0294  -0.0098 236 GLU A CD   
2492 O  OE1  A GLU A 235 ? 0.1583 0.1520 0.1217 -0.0096 0.0143  -0.0024 236 GLU A OE1  
2493 O  OE1  B GLU A 235 ? 0.2120 0.2300 0.3113 -0.0065 0.0294  0.0498  236 GLU A OE1  
2494 O  OE2  A GLU A 235 ? 0.2910 0.2133 0.2224 -0.0436 0.0313  0.0012  236 GLU A OE2  
2495 O  OE2  B GLU A 235 ? 0.2858 0.2100 0.3258 -0.0297 0.0410  0.0329  236 GLU A OE2  
2496 N  N    A PRO A 236 ? 0.1624 0.0860 0.1105 0.0450  0.0070  0.0640  237 PRO A N    
2497 N  N    B PRO A 236 ? 0.1985 0.2626 0.1380 -0.0320 0.0318  -0.0041 237 PRO A N    
2498 C  CA   A PRO A 236 ? 0.1504 0.1152 0.1462 0.0353  0.0226  0.0326  237 PRO A CA   
2499 C  CA   B PRO A 236 ? 0.1994 0.2384 0.1662 -0.0093 0.0342  -0.0049 237 PRO A CA   
2500 C  C    A PRO A 236 ? 0.1587 0.1057 0.1172 0.0135  0.0206  0.0142  237 PRO A C    
2501 C  C    B PRO A 236 ? 0.2037 0.1926 0.1389 -0.0298 0.0392  -0.0342 237 PRO A C    
2502 O  O    A PRO A 236 ? 0.2759 0.1124 0.0931 -0.0593 0.1208  -0.0549 237 PRO A O    
2503 O  O    B PRO A 236 ? 0.2290 0.1619 0.1962 0.0364  -0.0137 0.0395  237 PRO A O    
2504 C  CB   A PRO A 236 ? 0.1116 0.0996 0.1650 0.0439  0.0351  0.0846  237 PRO A CB   
2505 C  CB   B PRO A 236 ? 0.1890 0.2876 0.1531 -0.0527 0.0379  -0.0097 237 PRO A CB   
2506 C  CG   A PRO A 236 ? 0.2141 0.1298 0.1972 0.0203  -0.0148 0.0502  237 PRO A CG   
2507 C  CG   B PRO A 236 ? 0.1263 0.3046 0.1675 -0.0178 0.0031  0.0120  237 PRO A CG   
2508 C  CD   A PRO A 236 ? 0.1851 0.1159 0.1822 0.0548  0.0137  0.0386  237 PRO A CD   
2509 C  CD   B PRO A 236 ? 0.2215 0.2581 0.1547 -0.0296 0.0010  0.0052  237 PRO A CD   
2510 N  N    A GLU A 237 ? 0.1414 0.1123 0.0899 0.0272  0.0132  -0.0205 238 GLU A N    
2511 N  N    B GLU A 237 ? 0.1960 0.1432 0.1048 0.0222  0.0362  -0.0054 238 GLU A N    
2512 C  CA   A GLU A 237 ? 0.1382 0.1096 0.1098 0.0239  0.0163  -0.0031 238 GLU A CA   
2513 C  CA   B GLU A 237 ? 0.1696 0.1412 0.1143 -0.0031 0.0206  -0.0152 238 GLU A CA   
2514 C  C    A GLU A 237 ? 0.1278 0.0897 0.1057 0.0189  0.0108  -0.0040 238 GLU A C    
2515 C  C    B GLU A 237 ? 0.1669 0.1137 0.1136 0.0151  0.0283  0.0019  238 GLU A C    
2516 O  O    A GLU A 237 ? 0.1356 0.0969 0.1097 0.0359  0.0171  -0.0137 238 GLU A O    
2517 O  O    B GLU A 237 ? 0.1699 0.0908 0.1197 0.0108  0.0015  -0.0015 238 GLU A O    
2518 C  CB   A GLU A 237 ? 0.1295 0.1193 0.1277 0.0193  0.0120  -0.0379 238 GLU A CB   
2519 C  CB   B GLU A 237 ? 0.1738 0.1181 0.1297 -0.0041 0.0077  -0.0286 238 GLU A CB   
2520 C  CG   A GLU A 237 ? 0.1637 0.1137 0.1243 0.0318  0.0071  -0.0364 238 GLU A CG   
2521 C  CG   B GLU A 237 ? 0.1890 0.1048 0.1256 0.0006  0.0074  -0.0288 238 GLU A CG   
2522 C  CD   A GLU A 237 ? 0.1750 0.1141 0.1459 -0.0049 0.0297  -0.0540 238 GLU A CD   
2523 C  CD   B GLU A 237 ? 0.1856 0.1249 0.1393 -0.0176 -0.0026 -0.0555 238 GLU A CD   
2524 O  OE1  A GLU A 237 ? 0.2323 0.1386 0.2116 0.0054  -0.0196 -0.0342 238 GLU A OE1  
2525 O  OE1  B GLU A 237 ? 0.2303 0.1723 0.2106 0.0151  -0.0027 -0.0762 238 GLU A OE1  
2526 O  OE2  A GLU A 237 ? 0.1678 0.1243 0.1116 -0.0146 0.0077  -0.0630 238 GLU A OE2  
2527 O  OE2  B GLU A 237 ? 0.1966 0.1403 0.1791 -0.0249 0.0068  -0.0700 238 GLU A OE2  
2528 N  N    A GLU A 238 ? 0.0784 0.0745 0.1021 0.0240  0.0065  -0.0071 239 GLU A N    
2529 N  N    B GLU A 238 ? 0.1331 0.0834 0.1084 0.0076  0.0219  -0.0114 239 GLU A N    
2530 C  CA   A GLU A 238 ? 0.0938 0.0836 0.1037 0.0126  0.0085  -0.0041 239 GLU A CA   
2531 C  CA   B GLU A 238 ? 0.1217 0.1064 0.1242 -0.0071 0.0193  -0.0081 239 GLU A CA   
2532 C  C    A GLU A 238 ? 0.0922 0.0933 0.1030 0.0062  0.0104  0.0015  239 GLU A C    
2533 C  C    B GLU A 238 ? 0.1071 0.1080 0.0978 0.0023  0.0057  -0.0215 239 GLU A C    
2534 O  O    A GLU A 238 ? 0.1102 0.0744 0.1299 0.0263  0.0156  0.0049  239 GLU A O    
2535 O  O    B GLU A 238 ? 0.1150 0.1206 0.1021 0.0024  0.0057  0.0197  239 GLU A O    
2536 C  CB   A GLU A 238 ? 0.1093 0.0929 0.1272 0.0093  0.0062  0.0208  239 GLU A CB   
2537 C  CB   B GLU A 238 ? 0.1294 0.1116 0.1265 -0.0048 0.0306  -0.0126 239 GLU A CB   
2538 C  CG   A GLU A 238 ? 0.1941 0.1551 0.1994 -0.0024 0.0196  -0.0076 239 GLU A CG   
2539 C  CG   B GLU A 238 ? 0.1559 0.1265 0.1621 0.0003  -0.0043 0.0093  239 GLU A CG   
2540 C  CD   A GLU A 238 ? 0.2012 0.1978 0.2069 -0.0030 0.0060  -0.0208 239 GLU A CD   
2541 C  CD   B GLU A 238 ? 0.1630 0.1513 0.1366 -0.0119 -0.0120 -0.0010 239 GLU A CD   
2542 O  OE1  A GLU A 238 ? 0.2648 0.2034 0.1829 -0.0298 0.0175  -0.0241 239 GLU A OE1  
2543 O  OE1  B GLU A 238 ? 0.1466 0.1421 0.1804 0.0277  0.0046  -0.0197 239 GLU A OE1  
2544 O  OE2  A GLU A 238 ? 0.2278 0.2601 0.3142 -0.0741 -0.0425 -0.0175 239 GLU A OE2  
2545 O  OE2  B GLU A 238 ? 0.1709 0.1347 0.1447 -0.0357 0.0109  -0.0109 239 GLU A OE2  
2546 N  N    A LEU A 239 ? 0.0852 0.0712 0.0965 0.0120  0.0017  -0.0073 240 LEU A N    
2547 N  N    B LEU A 239 ? 0.0958 0.1172 0.1019 0.0120  0.0107  0.0006  240 LEU A N    
2548 C  CA   A LEU A 239 ? 0.0701 0.0820 0.0723 0.0148  0.0081  0.0024  240 LEU A CA   
2549 C  CA   B LEU A 239 ? 0.1150 0.1142 0.0960 0.0087  -0.0048 -0.0065 240 LEU A CA   
2550 C  C    A LEU A 239 ? 0.0947 0.0401 0.0494 -0.0003 -0.0035 0.0081  240 LEU A C    
2551 C  C    B LEU A 239 ? 0.0821 0.1075 0.0800 0.0038  0.0175  0.0052  240 LEU A C    
2552 O  O    A LEU A 239 ? 0.0908 0.0745 0.0480 0.0233  0.0017  -0.0049 240 LEU A O    
2553 O  O    B LEU A 239 ? 0.1057 0.1233 0.0913 0.0131  -0.0185 -0.0059 240 LEU A O    
2554 C  CB   A LEU A 239 ? 0.0967 0.0657 0.0815 0.0046  -0.0017 -0.0024 240 LEU A CB   
2555 C  CB   B LEU A 239 ? 0.1140 0.1127 0.1225 0.0271  0.0041  -0.0181 240 LEU A CB   
2556 C  CG   A LEU A 239 ? 0.1177 0.0562 0.1750 -0.0010 -0.0019 -0.0170 240 LEU A CG   
2557 C  CG   B LEU A 239 ? 0.1605 0.0836 0.1544 -0.0217 0.0062  0.0024  240 LEU A CG   
2558 C  CD1  A LEU A 239 ? 0.1653 0.1303 0.2500 0.0017  -0.0208 0.0046  240 LEU A CD1  
2559 C  CD1  B LEU A 239 ? 0.2125 0.1647 0.1861 0.0000  -0.0205 -0.0225 240 LEU A CD1  
2560 C  CD2  A LEU A 239 ? 0.1493 0.0653 0.0508 0.0317  -0.0153 -0.0274 240 LEU A CD2  
2561 C  CD2  B LEU A 239 ? 0.1698 0.0841 0.1435 0.0027  0.0165  -0.0428 240 LEU A CD2  
2562 N  N    A MET A 240 ? 0.0832 0.0644 0.0624 0.0226  -0.0006 -0.0057 241 MET A N    
2563 N  N    B MET A 240 ? 0.1035 0.0899 0.0870 -0.0054 0.0153  -0.0142 241 MET A N    
2564 C  CA   A MET A 240 ? 0.0842 0.0459 0.0648 0.0054  -0.0013 -0.0049 241 MET A CA   
2565 C  CA   B MET A 240 ? 0.1150 0.1005 0.0644 -0.0162 0.0252  -0.0104 241 MET A CA   
2566 C  C    A MET A 240 ? 0.0618 0.0750 0.0562 -0.0040 -0.0046 -0.0220 241 MET A C    
2567 C  C    B MET A 240 ? 0.1342 0.1037 0.0741 -0.0317 0.0243  -0.0309 241 MET A C    
2568 O  O    A MET A 240 ? 0.0942 0.0658 0.0680 0.0110  0.0049  -0.0154 241 MET A O    
2569 O  O    B MET A 240 ? 0.1128 0.0996 0.0996 -0.0031 0.0295  -0.0102 241 MET A O    
2570 C  CB   A MET A 240 ? 0.0851 0.0687 0.0737 -0.0120 0.0081  0.0031  241 MET A CB   
2571 C  CB   B MET A 240 ? 0.1124 0.1105 0.0809 -0.0071 0.0260  -0.0087 241 MET A CB   
2572 C  CG   A MET A 240 ? 0.0820 0.0746 0.0794 0.0251  0.0019  0.0048  241 MET A CG   
2573 C  CG   B MET A 240 ? 0.1089 0.0613 0.0951 -0.0073 0.0093  -0.0136 241 MET A CG   
2574 S  SD   A MET A 240 ? 0.1091 0.0481 0.0942 0.0109  0.0031  0.0091  241 MET A SD   
2575 S  SD   B MET A 240 ? 0.1401 0.0924 0.1177 -0.0153 0.0260  0.0007  241 MET A SD   
2576 C  CE   A MET A 240 ? 0.0913 0.0680 0.0802 0.0093  0.0208  0.0195  241 MET A CE   
2577 C  CE   B MET A 240 ? 0.1324 0.0649 0.1279 -0.0273 0.0226  0.0091  241 MET A CE   
2578 N  N    A VAL A 241 ? 0.0784 0.0464 0.0764 -0.0203 0.0098  -0.0102 242 VAL A N    
2579 N  N    B VAL A 241 ? 0.1502 0.0996 0.0642 -0.0062 0.0114  -0.0322 242 VAL A N    
2580 C  CA   A VAL A 241 ? 0.1106 0.0538 0.0644 0.0035  0.0308  -0.0097 242 VAL A CA   
2581 C  CA   B VAL A 241 ? 0.1337 0.0791 0.0755 -0.0184 0.0364  -0.0199 242 VAL A CA   
2582 C  C    A VAL A 241 ? 0.1484 0.0511 0.0656 0.0003  0.0153  -0.0109 242 VAL A C    
2583 C  C    B VAL A 241 ? 0.1666 0.0648 0.0845 -0.0183 0.0183  -0.0329 242 VAL A C    
2584 O  O    A VAL A 241 ? 0.1402 0.0635 0.0712 -0.0073 0.0148  -0.0082 242 VAL A O    
2585 O  O    B VAL A 241 ? 0.1592 0.0696 0.1010 -0.0266 0.0313  -0.0252 242 VAL A O    
2586 C  CB   A VAL A 241 ? 0.1114 0.0599 0.0721 0.0143  0.0310  0.0092  242 VAL A CB   
2587 C  CB   B VAL A 241 ? 0.1265 0.0676 0.0603 0.0052  0.0000  -0.0269 242 VAL A CB   
2588 C  CG1  A VAL A 241 ? 0.1339 0.0562 0.1005 -0.0177 -0.0364 -0.0324 242 VAL A CG1  
2589 C  CG1  B VAL A 241 ? 0.1186 0.1314 0.0942 0.0182  0.0333  0.0003  242 VAL A CG1  
2590 C  CG2  A VAL A 241 ? 0.1437 0.0319 0.0924 0.0059  -0.0178 -0.0210 242 VAL A CG2  
2591 C  CG2  B VAL A 241 ? 0.1040 0.0987 0.1301 0.0342  0.0225  -0.0065 242 VAL A CG2  
2592 N  N    . ASP A 242 ? 0.1569 0.0515 0.0881 -0.0161 0.0242  -0.0225 243 ASP A N    
2593 C  CA   . ASP A 242 ? 0.1495 0.0573 0.0836 -0.0098 0.0320  -0.0326 243 ASP A CA   
2594 C  C    . ASP A 242 ? 0.1623 0.0694 0.0845 -0.0302 0.0370  -0.0151 243 ASP A C    
2595 O  O    . ASP A 242 ? 0.1493 0.0730 0.1407 -0.0254 0.0288  -0.0318 243 ASP A O    
2596 C  CB   . ASP A 242 ? 0.1595 0.0757 0.0847 -0.0107 0.0285  -0.0184 243 ASP A CB   
2597 C  CG   . ASP A 242 ? 0.1323 0.0685 0.1158 -0.0163 0.0216  -0.0222 243 ASP A CG   
2598 O  OD1  . ASP A 242 ? 0.1400 0.0529 0.1155 -0.0038 0.0114  -0.0189 243 ASP A OD1  
2599 O  OD2  . ASP A 242 ? 0.1712 0.0714 0.1516 -0.0054 0.0340  -0.0366 243 ASP A OD2  
2600 N  N    . ASN A 243 ? 0.1350 0.0538 0.0878 -0.0218 0.0208  -0.0315 244 ASN A N    
2601 C  CA   . ASN A 243 ? 0.1331 0.0568 0.0992 -0.0252 0.0317  -0.0239 244 ASN A CA   
2602 C  C    . ASN A 243 ? 0.1202 0.0463 0.0856 -0.0294 0.0216  -0.0060 244 ASN A C    
2603 O  O    . ASN A 243 ? 0.1592 0.0612 0.0757 -0.0052 0.0258  -0.0065 244 ASN A O    
2604 C  CB   . ASN A 243 ? 0.1553 0.0635 0.0666 -0.0259 0.0307  -0.0097 244 ASN A CB   
2605 C  CG   . ASN A 243 ? 0.1577 0.0644 0.0886 -0.0445 0.0317  -0.0119 244 ASN A CG   
2606 O  OD1  . ASN A 243 ? 0.1624 0.0588 0.1012 -0.0283 0.0252  -0.0013 244 ASN A OD1  
2607 N  ND2  . ASN A 243 ? 0.1885 0.1356 0.1595 -0.0688 -0.0210 0.0799  244 ASN A ND2  
2608 N  N    . TRP A 244 ? 0.1215 0.0388 0.0899 -0.0031 0.0275  -0.0146 245 TRP A N    
2609 C  CA   . TRP A 244 ? 0.1190 0.0464 0.0876 -0.0082 0.0137  -0.0197 245 TRP A CA   
2610 C  C    . TRP A 244 ? 0.1145 0.0518 0.0824 -0.0035 0.0176  -0.0118 245 TRP A C    
2611 O  O    . TRP A 244 ? 0.1170 0.0649 0.1170 -0.0017 0.0154  -0.0295 245 TRP A O    
2612 C  CB   . TRP A 244 ? 0.0992 0.0463 0.0908 -0.0057 0.0146  -0.0208 245 TRP A CB   
2613 C  CG   . TRP A 244 ? 0.1057 0.0606 0.0869 -0.0099 0.0088  -0.0110 245 TRP A CG   
2614 C  CD1  . TRP A 244 ? 0.1233 0.0508 0.0836 -0.0038 0.0184  -0.0031 245 TRP A CD1  
2615 C  CD2  . TRP A 244 ? 0.1084 0.0552 0.0772 -0.0054 0.0043  -0.0214 245 TRP A CD2  
2616 N  NE1  . TRP A 244 ? 0.1259 0.0502 0.0947 -0.0074 0.0243  -0.0148 245 TRP A NE1  
2617 C  CE2  . TRP A 244 ? 0.1019 0.0491 0.1089 0.0000  0.0221  -0.0027 245 TRP A CE2  
2618 C  CE3  . TRP A 244 ? 0.1084 0.0556 0.1152 0.0003  0.0129  -0.0205 245 TRP A CE3  
2619 C  CZ2  . TRP A 244 ? 0.1412 0.0538 0.1107 -0.0015 0.0147  -0.0263 245 TRP A CZ2  
2620 C  CZ3  . TRP A 244 ? 0.1317 0.0789 0.1123 -0.0031 0.0024  0.0015  245 TRP A CZ3  
2621 C  CH2  . TRP A 244 ? 0.1412 0.0574 0.1340 0.0137  0.0186  0.0143  245 TRP A CH2  
2622 N  N    . ARG A 245 ? 0.0957 0.0527 0.0870 0.0010  0.0093  -0.0229 246 ARG A N    
2623 C  CA   . ARG A 245 ? 0.0922 0.0485 0.1143 0.0031  0.0197  -0.0192 246 ARG A CA   
2624 C  C    . ARG A 245 ? 0.1014 0.0499 0.0847 -0.0057 0.0017  -0.0280 246 ARG A C    
2625 O  O    . ARG A 245 ? 0.0832 0.0732 0.1012 -0.0003 -0.0054 -0.0109 246 ARG A O    
2626 C  CB   . ARG A 245 ? 0.0788 0.0759 0.0951 -0.0063 0.0104  -0.0164 246 ARG A CB   
2627 C  CG   . ARG A 245 ? 0.0730 0.0697 0.1179 0.0007  0.0107  -0.0203 246 ARG A CG   
2628 C  CD   . ARG A 245 ? 0.0834 0.0666 0.1260 -0.0141 0.0205  -0.0197 246 ARG A CD   
2629 N  NE   . ARG A 245 ? 0.0847 0.0604 0.1376 -0.0082 -0.0087 -0.0171 246 ARG A NE   
2630 C  CZ   . ARG A 245 ? 0.1005 0.0564 0.1145 -0.0142 0.0076  -0.0196 246 ARG A CZ   
2631 N  NH1  . ARG A 245 ? 0.0992 0.0737 0.1240 -0.0304 -0.0006 -0.0252 246 ARG A NH1  
2632 N  NH2  . ARG A 245 ? 0.1155 0.0771 0.1605 -0.0247 0.0059  -0.0313 246 ARG A NH2  
2633 N  N    A PRO A 246 ? 0.0958 0.0608 0.1120 0.0187  -0.0017 -0.0006 247 PRO A N    
2634 N  N    B PRO A 246 ? 0.0976 0.0518 0.1003 0.0017  0.0118  -0.0082 247 PRO A N    
2635 C  CA   A PRO A 246 ? 0.1058 0.0379 0.0915 0.0247  0.0026  -0.0173 247 PRO A CA   
2636 C  CA   B PRO A 246 ? 0.1000 0.0579 0.0992 -0.0043 0.0006  -0.0035 247 PRO A CA   
2637 C  C    A PRO A 246 ? 0.1014 0.0403 0.1093 0.0186  -0.0142 -0.0030 247 PRO A C    
2638 C  C    B PRO A 246 ? 0.0978 0.0614 0.1001 0.0060  -0.0194 -0.0038 247 PRO A C    
2639 O  O    A PRO A 246 ? 0.1181 0.0563 0.0996 0.0132  -0.0171 0.0006  247 PRO A O    
2640 O  O    B PRO A 246 ? 0.1145 0.0609 0.1000 0.0071  -0.0129 -0.0049 247 PRO A O    
2641 C  CB   A PRO A 246 ? 0.1286 0.0332 0.1398 0.0285  0.0024  0.0003  247 PRO A CB   
2642 C  CB   B PRO A 246 ? 0.1070 0.0938 0.0894 -0.0120 -0.0093 -0.0171 247 PRO A CB   
2643 C  CG   A PRO A 246 ? 0.1283 0.0705 0.1093 0.0364  -0.0034 -0.0054 247 PRO A CG   
2644 C  CG   B PRO A 246 ? 0.1353 0.1190 0.1450 0.0113  0.0026  0.0006  247 PRO A CG   
2645 C  CD   A PRO A 246 ? 0.0992 0.0520 0.1483 0.0261  -0.0051 -0.0425 247 PRO A CD   
2646 C  CD   B PRO A 246 ? 0.1263 0.0873 0.1079 0.0027  0.0087  -0.0386 247 PRO A CD   
2647 N  N    . ALA A 247 ? 0.1247 0.0520 0.1159 0.0046  0.0013  0.0015  248 ALA A N    
2648 C  CA   . ALA A 247 ? 0.1252 0.0491 0.1093 0.0159  -0.0096 -0.0043 248 ALA A CA   
2649 C  C    . ALA A 247 ? 0.1229 0.0680 0.1035 0.0171  -0.0085 0.0104  248 ALA A C    
2650 O  O    . ALA A 247 ? 0.1102 0.0863 0.1231 0.0273  -0.0226 0.0000  248 ALA A O    
2651 C  CB   . ALA A 247 ? 0.1502 0.0897 0.1208 0.0006  0.0233  0.0074  248 ALA A CB   
2652 N  N    . GLN A 248 ? 0.1049 0.0658 0.1062 0.0148  -0.0148 0.0088  249 GLN A N    
2653 C  CA   . GLN A 248 ? 0.0926 0.0676 0.1253 0.0126  -0.0219 0.0017  249 GLN A CA   
2654 C  C    . GLN A 248 ? 0.1116 0.0899 0.1249 0.0370  -0.0403 0.0109  249 GLN A C    
2655 O  O    . GLN A 248 ? 0.1208 0.0856 0.1141 0.0154  -0.0132 0.0071  249 GLN A O    
2656 C  CB   . GLN A 248 ? 0.0973 0.0800 0.1295 -0.0024 -0.0285 -0.0006 249 GLN A CB   
2657 C  CG   . GLN A 248 ? 0.1290 0.0674 0.1225 -0.0046 -0.0242 0.0060  249 GLN A CG   
2658 C  CD   . GLN A 248 ? 0.1163 0.1080 0.1427 -0.0027 -0.0007 0.0080  249 GLN A CD   
2659 O  OE1  . GLN A 248 ? 0.1252 0.1689 0.1759 -0.0344 0.0007  -0.0452 249 GLN A OE1  
2660 N  NE2  . GLN A 248 ? 0.1420 0.1093 0.1342 -0.0153 0.0027  -0.0082 249 GLN A NE2  
2661 N  N    . PRO A 249 ? 0.1217 0.1398 0.1237 0.0384  -0.0295 -0.0054 250 PRO A N    
2662 C  CA   . PRO A 249 ? 0.1495 0.1331 0.1448 0.0478  -0.0482 -0.0024 250 PRO A CA   
2663 C  C    . PRO A 249 ? 0.1520 0.1120 0.0935 0.0231  -0.0375 -0.0024 250 PRO A C    
2664 O  O    . PRO A 249 ? 0.1401 0.1041 0.1374 0.0320  -0.0395 0.0187  250 PRO A O    
2665 C  CB   . PRO A 249 ? 0.1586 0.2098 0.1383 0.0785  -0.0566 -0.0198 250 PRO A CB   
2666 C  CG   . PRO A 249 ? 0.1572 0.2319 0.1689 0.0038  -0.0625 -0.0271 250 PRO A CG   
2667 C  CD   . PRO A 249 ? 0.1481 0.1726 0.1525 0.0438  -0.0683 -0.0219 250 PRO A CD   
2668 N  N    . LEU A 250 ? 0.1850 0.0832 0.1088 0.0417  -0.0147 0.0092  251 LEU A N    
2669 C  CA   . LEU A 250 ? 0.1639 0.0791 0.1089 0.0175  -0.0401 -0.0010 251 LEU A CA   
2670 C  C    . LEU A 250 ? 0.1495 0.0908 0.1146 0.0370  -0.0285 0.0241  251 LEU A C    
2671 O  O    . LEU A 250 ? 0.1617 0.0854 0.1124 0.0125  -0.0526 -0.0003 251 LEU A O    
2672 C  CB   . LEU A 250 ? 0.2000 0.0860 0.1176 -0.0030 -0.0148 0.0119  251 LEU A CB   
2673 C  CG   . LEU A 250 ? 0.2084 0.1021 0.1283 -0.0255 0.0104  -0.0073 251 LEU A CG   
2674 C  CD1  . LEU A 250 ? 0.1533 0.1693 0.1376 -0.0063 -0.0298 -0.0394 251 LEU A CD1  
2675 C  CD2  . LEU A 250 ? 0.2352 0.1367 0.1642 -0.0148 0.0071  0.0031  251 LEU A CD2  
2676 N  N    . LYS A 251 ? 0.2091 0.1009 0.1170 0.0467  -0.0546 0.0012  252 LYS A N    
2677 C  CA   . LYS A 251 ? 0.1902 0.1358 0.1066 0.0392  -0.0509 -0.0065 252 LYS A CA   
2678 C  C    . LYS A 251 ? 0.1835 0.1297 0.1556 0.0175  -0.0498 -0.0076 252 LYS A C    
2679 O  O    . LYS A 251 ? 0.2409 0.1459 0.1532 0.0227  -0.0307 -0.0026 252 LYS A O    
2680 C  CB   . LYS A 251 ? 0.1893 0.1531 0.1280 -0.0048 -0.0732 -0.0093 252 LYS A CB   
2681 C  CG   . LYS A 251 ? 0.2472 0.1701 0.1863 0.0491  -0.0096 -0.0087 252 LYS A CG   
2682 C  CD   . LYS A 251 ? 0.2470 0.1845 0.1962 0.0383  -0.0344 -0.0027 252 LYS A CD   
2683 C  CE   . LYS A 251 ? 0.2088 0.2269 0.3472 0.0662  -0.0019 0.0447  252 LYS A CE   
2684 N  NZ   . LYS A 251 ? 0.2504 0.2700 0.3970 0.0194  -0.0076 0.0544  252 LYS A NZ   
2685 N  N    . ASN A 252 ? 0.2206 0.1231 0.0915 0.0087  -0.0381 -0.0308 253 ASN A N    
2686 C  CA   . ASN A 252 ? 0.2165 0.2377 0.1493 0.0292  -0.0527 -0.0496 253 ASN A CA   
2687 C  C    . ASN A 252 ? 0.2402 0.1899 0.1620 0.0653  -0.0295 -0.0469 253 ASN A C    
2688 O  O    . ASN A 252 ? 0.2610 0.2287 0.2082 0.0461  -0.0274 -0.0408 253 ASN A O    
2689 C  CB   . ASN A 252 ? 0.2669 0.2633 0.1994 0.0197  -0.0294 -0.0658 253 ASN A CB   
2690 C  CG   . ASN A 252 ? 0.3456 0.2556 0.2161 0.0085  -0.0109 -0.0428 253 ASN A CG   
2691 O  OD1  . ASN A 252 ? 0.4860 0.4690 0.2953 -0.0262 0.0535  -0.0135 253 ASN A OD1  
2692 N  ND2  . ASN A 252 ? 0.3325 0.2716 0.2813 -0.0494 -0.0181 -0.0702 253 ASN A ND2  
2693 N  N    . ARG A 253 ? 0.2017 0.2389 0.0888 0.0662  -0.0199 0.0087  254 ARG A N    
2694 C  CA   . ARG A 253 ? 0.1605 0.1316 0.1030 0.0445  -0.0247 -0.0070 254 ARG A CA   
2695 C  C    . ARG A 253 ? 0.1960 0.1021 0.0966 0.0326  0.0020  -0.0175 254 ARG A C    
2696 O  O    . ARG A 253 ? 0.2335 0.1696 0.2369 0.0579  0.0825  0.0588  254 ARG A O    
2697 C  CB   . ARG A 253 ? 0.1617 0.1023 0.0599 0.0296  -0.0208 -0.0077 254 ARG A CB   
2698 C  CG   . ARG A 253 ? 0.1614 0.0755 0.0913 0.0175  -0.0086 -0.0104 254 ARG A CG   
2699 C  CD   . ARG A 253 ? 0.1522 0.0759 0.0881 0.0140  -0.0172 -0.0041 254 ARG A CD   
2700 N  NE   . ARG A 253 ? 0.1306 0.0759 0.0820 0.0163  -0.0353 0.0059  254 ARG A NE   
2701 C  CZ   . ARG A 253 ? 0.1136 0.0741 0.0630 -0.0098 -0.0285 0.0143  254 ARG A CZ   
2702 N  NH1  . ARG A 253 ? 0.1080 0.0642 0.0736 0.0063  -0.0124 -0.0060 254 ARG A NH1  
2703 N  NH2  . ARG A 253 ? 0.1295 0.0615 0.0843 0.0275  -0.0318 -0.0038 254 ARG A NH2  
2704 N  N    A GLN A 254 ? 0.1685 0.1115 0.0987 0.0221  -0.0119 -0.0372 255 GLN A N    
2705 N  N    B GLN A 254 ? 0.1739 0.1197 0.1040 0.0175  -0.0183 -0.0255 255 GLN A N    
2706 C  CA   A GLN A 254 ? 0.1757 0.1308 0.0913 0.0137  0.0031  -0.0228 255 GLN A CA   
2707 C  CA   B GLN A 254 ? 0.1762 0.1500 0.0976 0.0164  -0.0041 -0.0197 255 GLN A CA   
2708 C  C    A GLN A 254 ? 0.1457 0.1037 0.0834 0.0087  -0.0017 0.0010  255 GLN A C    
2709 C  C    B GLN A 254 ? 0.1626 0.1215 0.1142 -0.0026 -0.0281 -0.0126 255 GLN A C    
2710 O  O    A GLN A 254 ? 0.1757 0.0639 0.1145 -0.0020 0.0104  0.0031  255 GLN A O    
2711 O  O    B GLN A 254 ? 0.1850 0.1261 0.1605 0.0155  -0.0412 -0.0208 255 GLN A O    
2712 C  CB   A GLN A 254 ? 0.1914 0.1933 0.1215 0.0200  -0.0023 -0.0467 255 GLN A CB   
2713 C  CB   B GLN A 254 ? 0.2027 0.1942 0.0948 0.0218  -0.0182 -0.0126 255 GLN A CB   
2714 C  CG   A GLN A 254 ? 0.2926 0.2980 0.1441 0.0000  0.0469  -0.0546 255 GLN A CG   
2715 C  CG   B GLN A 254 ? 0.2379 0.3043 0.1965 0.0059  0.0228  -0.0384 255 GLN A CG   
2716 C  CD   A GLN A 254 ? 0.3734 0.3758 0.2991 0.0126  0.0020  -0.0172 255 GLN A CD   
2717 C  CD   B GLN A 254 ? 0.2581 0.2646 0.3023 0.0392  0.0286  0.0247  255 GLN A CD   
2718 O  OE1  A GLN A 254 ? 0.4685 0.4754 0.4517 -0.0281 0.0103  -0.0151 255 GLN A OE1  
2719 O  OE1  B GLN A 254 ? 0.3003 0.4250 0.3634 0.0262  0.0214  0.0065  255 GLN A OE1  
2720 N  NE2  A GLN A 254 ? 0.3740 0.4077 0.4119 0.0082  -0.0170 -0.0199 255 GLN A NE2  
2721 N  NE2  B GLN A 254 ? 0.2709 0.2520 0.1556 -0.0076 0.0048  0.0471  255 GLN A NE2  
2722 N  N    . ILE A 255 ? 0.1565 0.0890 0.0940 0.0070  -0.0076 0.0020  256 ILE A N    
2723 C  CA   . ILE A 255 ? 0.1425 0.0935 0.0710 -0.0074 -0.0065 0.0141  256 ILE A CA   
2724 C  C    . ILE A 255 ? 0.1553 0.0895 0.0820 0.0142  -0.0068 0.0027  256 ILE A C    
2725 O  O    . ILE A 255 ? 0.1838 0.1084 0.0825 0.0148  0.0163  0.0372  256 ILE A O    
2726 C  CB   . ILE A 255 ? 0.1493 0.0614 0.0827 -0.0024 -0.0137 0.0019  256 ILE A CB   
2727 C  CG1  . ILE A 255 ? 0.1450 0.0851 0.1014 -0.0037 -0.0020 0.0006  256 ILE A CG1  
2728 C  CG2  . ILE A 255 ? 0.1556 0.1091 0.0987 0.0027  -0.0093 -0.0010 256 ILE A CG2  
2729 C  CD1  . ILE A 255 ? 0.1682 0.1075 0.1167 0.0027  0.0082  -0.0322 256 ILE A CD1  
2730 N  N    . LYS A 256 ? 0.1429 0.1026 0.0626 -0.0076 0.0054  0.0165  257 LYS A N    
2731 C  CA   . LYS A 256 ? 0.1574 0.1019 0.0750 0.0065  0.0183  0.0115  257 LYS A CA   
2732 C  C    . LYS A 256 ? 0.1455 0.1055 0.0931 -0.0135 -0.0104 -0.0063 257 LYS A C    
2733 O  O    . LYS A 256 ? 0.1775 0.1676 0.0581 -0.0516 0.0076  0.0059  257 LYS A O    
2734 C  CB   . LYS A 256 ? 0.1316 0.1204 0.0994 -0.0020 0.0087  -0.0099 257 LYS A CB   
2735 C  CG   . LYS A 256 ? 0.2281 0.1359 0.1577 -0.0120 0.0274  -0.0423 257 LYS A CG   
2736 C  CD   . LYS A 256 ? 0.2567 0.1886 0.2095 0.0129  -0.0063 -0.0104 257 LYS A CD   
2737 C  CE   . LYS A 256 ? 0.2770 0.2258 0.2461 -0.0439 -0.0020 -0.0798 257 LYS A CE   
2738 N  NZ   . LYS A 256 ? 0.2836 0.2542 0.3497 -0.0070 0.0015  -0.1010 257 LYS A NZ   
2739 N  N    . ALA A 257 ? 0.1429 0.1276 0.0766 -0.0104 0.0263  -0.0006 258 ALA A N    
2740 C  CA   . ALA A 257 ? 0.1459 0.1140 0.0992 -0.0142 0.0130  0.0043  258 ALA A CA   
2741 C  C    . ALA A 257 ? 0.1365 0.1035 0.1114 -0.0164 0.0230  -0.0027 258 ALA A C    
2742 O  O    . ALA A 257 ? 0.1818 0.1425 0.0922 -0.0104 0.0408  -0.0172 258 ALA A O    
2743 C  CB   . ALA A 257 ? 0.1800 0.1120 0.1208 -0.0131 0.0326  0.0129  258 ALA A CB   
2744 N  N    . SER A 258 ? 0.1373 0.1136 0.0969 -0.0046 0.0208  -0.0049 259 SER A N    
2745 C  CA   . SER A 258 ? 0.1543 0.1297 0.1143 -0.0003 0.0260  -0.0186 259 SER A CA   
2746 C  C    . SER A 258 ? 0.1457 0.1565 0.1353 -0.0187 0.0383  -0.0041 259 SER A C    
2747 O  O    . SER A 258 ? 0.1542 0.2468 0.1781 0.0192  0.0511  0.0020  259 SER A O    
2748 C  CB   . SER A 258 ? 0.1662 0.1186 0.1368 -0.0017 0.0052  -0.0097 259 SER A CB   
2749 O  OG   . SER A 258 ? 0.1278 0.1429 0.1109 -0.0098 0.0284  -0.0099 259 SER A OG   
2750 N  N    . PHE A 259 ? 0.1445 0.1668 0.1644 -0.0394 0.0483  -0.0005 260 PHE A N    
2751 C  CA   . PHE A 259 ? 0.1818 0.1789 0.1754 -0.0443 0.0480  0.0160  260 PHE A CA   
2752 C  C    . PHE A 259 ? 0.2190 0.2345 0.1989 -0.0693 0.0709  0.0487  260 PHE A C    
2753 O  O    . PHE A 259 ? 0.2969 0.1825 0.2032 -0.0509 0.0193  0.0732  260 PHE A O    
2754 C  CB   . PHE A 259 ? 0.1777 0.1762 0.1730 -0.0458 0.0259  0.0074  260 PHE A CB   
2755 C  CG   . PHE A 259 ? 0.1773 0.1482 0.1867 -0.0373 0.0225  0.0049  260 PHE A CG   
2756 C  CD1  . PHE A 259 ? 0.1820 0.1102 0.1357 -0.0405 -0.0104 -0.0059 260 PHE A CD1  
2757 C  CD2  . PHE A 259 ? 0.2623 0.1378 0.2412 -0.0386 0.0254  0.0322  260 PHE A CD2  
2758 C  CE1  . PHE A 259 ? 0.1477 0.1752 0.2132 -0.0159 0.0162  -0.0152 260 PHE A CE1  
2759 C  CE2  . PHE A 259 ? 0.2242 0.1818 0.2639 -0.0249 0.0006  0.0226  260 PHE A CE2  
2760 C  CZ   . PHE A 259 ? 0.2177 0.1497 0.2285 -0.0005 0.0024  -0.0115 260 PHE A CZ   
2761 N  N    . LYS A 260 ? 0.3134 0.2964 0.2781 -0.0881 0.0653  0.0688  261 LYS A N    
2762 C  CA   . LYS A 260 ? 0.3944 0.3671 0.3461 -0.0340 0.0417  0.0458  261 LYS A CA   
2763 C  C    . LYS A 260 ? 0.4494 0.4535 0.4395 -0.0206 0.0249  0.0221  261 LYS A C    
2764 O  O    . LYS A 260 ? 0.5054 0.5108 0.4695 -0.0049 0.0406  0.0137  261 LYS A O    
2765 C  CB   . LYS A 260 ? 0.4201 0.3693 0.3756 -0.0406 0.0419  0.0527  261 LYS A CB   
2766 C  CG   . LYS A 260 ? 0.4287 0.4063 0.4199 -0.0303 0.0362  0.0152  261 LYS A CG   
2767 C  CD   . LYS A 260 ? 0.4485 0.4081 0.4347 -0.0241 0.0177  0.0125  261 LYS A CD   
2768 C  CE   . LYS A 260 ? 0.4645 0.4341 0.4607 -0.0006 0.0063  0.0109  261 LYS A CE   
2769 N  NZ   . LYS A 260 ? 0.5210 0.4603 0.5018 0.0010  0.0211  -0.0129 261 LYS A NZ   
2770 O  OXT  . LYS A 260 ? 0.5041 0.5421 0.5385 -0.0063 0.0252  0.0031  261 LYS A OXT  
2771 ZN ZN   . ZN  B .   ? 0.1136 0.0327 0.0582 -0.0110 0.0017  -0.0020 262 ZN  A ZN   
2772 N  N1   . E50 C .   ? 0.2752 0.2476 0.3567 -0.0719 0.0634  0.0006  263 E50 A N1   
2773 C  C2   . E50 C .   ? 0.2664 0.2206 0.2693 -0.0529 0.0776  0.0185  263 E50 A C2   
2774 N  N3   . E50 C .   ? 0.2854 0.2036 0.2741 -0.0631 0.0908  -0.0109 263 E50 A N3   
2775 C  C4   . E50 C .   ? 0.2833 0.2172 0.3012 -0.0846 -0.0196 -0.0140 263 E50 A C4   
2776 C  C5   . E50 C .   ? 0.2967 0.2258 0.3224 -0.0608 0.0392  0.0203  263 E50 A C5   
2777 C  C6   . E50 C .   ? 0.3240 0.2881 0.3407 -0.0483 0.0104  -0.0259 263 E50 A C6   
2778 S  S7   . E50 C .   ? 0.3336 0.2599 0.2068 -0.0505 0.0675  0.0146  263 E50 A S7   
2779 C  C8   . E50 C .   ? 0.1980 0.1611 0.1714 -0.0152 0.0253  0.0017  263 E50 A C8   
2780 C  C9   . E50 C .   ? 0.2272 0.1276 0.1606 -0.0263 0.0174  0.0410  263 E50 A C9   
2781 O  O10  . E50 C .   ? 0.2330 0.2289 0.2122 -0.0164 0.0171  0.0819  263 E50 A O10  
2782 C  C11  . E50 C .   ? 0.3393 0.2393 0.3404 -0.0577 0.0307  0.0251  263 E50 A C11  
2783 C  C12  . E50 C .   ? 0.2479 0.2560 0.2903 -0.0027 0.0335  0.0328  263 E50 A C12  
2784 C  C13  . E50 C .   ? 0.2267 0.0811 0.1563 -0.0109 0.0273  0.0146  263 E50 A C13  
2785 C  C14  . E50 C .   ? 0.1875 0.0588 0.1350 -0.0379 -0.0060 0.0233  263 E50 A C14  
2786 C  C15  . E50 C .   ? 0.1172 0.0693 0.1136 -0.0074 0.0013  0.0000  263 E50 A C15  
2787 C  C16  . E50 C .   ? 0.1744 0.0437 0.1556 -0.0071 -0.0020 -0.0253 263 E50 A C16  
2788 C  C17  . E50 C .   ? 0.1680 0.0474 0.1793 -0.0274 -0.0003 0.0315  263 E50 A C17  
2789 C  C18  . E50 C .   ? 0.1772 0.1140 0.1687 -0.0093 0.0005  0.0566  263 E50 A C18  
2790 S  S19  . E50 C .   ? 0.1342 0.0494 0.1028 -0.0129 -0.0035 -0.0093 263 E50 A S19  
2791 O  O20  . E50 C .   ? 0.1154 0.0642 0.1001 0.0031  -0.0137 -0.0297 263 E50 A O20  
2792 CL CL21 . E50 C .   ? 0.1590 0.0615 0.1728 -0.0013 0.0085  -0.0146 263 E50 A CL21 
2793 O  O22  . E50 C .   ? 0.1150 0.0569 0.1093 -0.0070 -0.0070 -0.0054 263 E50 A O22  
2794 N  N23  . E50 C .   ? 0.1163 0.0432 0.0829 -0.0230 -0.0027 -0.0088 263 E50 A N23  
2795 N  N1   . BCN D .   ? 0.2933 0.2193 0.2935 -0.0491 0.0082  -0.0080 264 BCN A N1   
2796 C  C1   . BCN D .   ? 0.2549 0.2998 0.2167 -0.0623 -0.0131 0.0313  264 BCN A C1   
2797 C  C2   . BCN D .   ? 0.2736 0.2560 0.2477 -0.0746 0.0024  0.0388  264 BCN A C2   
2798 O  O21  . BCN D .   ? 0.3607 0.2910 0.2809 -0.0920 0.0250  0.0333  264 BCN A O21  
2799 O  O22  . BCN D .   ? 0.3032 0.2874 0.2964 -0.0762 -0.0081 0.0489  264 BCN A O22  
2800 C  C3   . BCN D .   ? 0.1899 0.1046 0.1971 -0.0206 0.0469  0.0097  264 BCN A C3   
2801 C  C4   . BCN D .   ? 0.3973 0.3111 0.3273 -0.0471 -0.0252 0.0043  264 BCN A C4   
2802 O  O4   . BCN D .   ? 0.4156 0.2260 0.3115 -0.1207 -0.0040 0.0328  264 BCN A O4   
2803 C  C5   . BCN D .   ? 0.1967 0.1283 0.2231 -0.0038 0.0087  0.0220  264 BCN A C5   
2804 C  C6   . BCN D .   ? 0.4059 0.3104 0.3614 -0.0054 0.0280  -0.0120 264 BCN A C6   
2805 O  O6   . BCN D .   ? 0.3176 0.2179 0.3458 -0.0085 0.0678  -0.0063 264 BCN A O6   
2806 S  S    . DMS E .   ? 0.2450 0.1659 0.2328 -0.0241 0.0307  -0.0176 265 DMS A S    
2807 O  O    . DMS E .   ? 0.2966 0.2233 0.3691 -0.0118 0.0447  -0.0099 265 DMS A O    
2808 C  C1   . DMS E .   ? 0.2989 0.1224 0.2263 -0.0076 0.0737  -0.0723 265 DMS A C1   
2809 C  C2   . DMS E .   ? 0.2109 0.2319 0.2412 0.0041  0.0283  -0.1017 265 DMS A C2   
2810 S  S    . DMS F .   ? 0.3673 0.1418 0.1696 -0.0417 -0.0063 0.0198  266 DMS A S    
2811 O  O    . DMS F .   ? 0.3179 0.1277 0.2502 -0.0931 -0.0062 0.0194  266 DMS A O    
2812 C  C1   . DMS F .   ? 0.3246 0.3373 0.2157 -0.0656 0.0340  0.0186  266 DMS A C1   
2813 C  C2   . DMS F .   ? 0.4077 0.1184 0.2865 -0.0324 -0.0555 0.0034  266 DMS A C2   
2814 O  O    . HOH G .   ? 0.3494 0.2389 0.3418 -0.0148 -0.0922 -0.0074 126 HOH A O    
2815 O  O    . HOH G .   ? 0.3697 0.4050 0.4516 -0.0771 0.1105  -0.0287 267 HOH A O    
2816 O  O    A HOH G .   ? 0.3937 0.2276 0.4052 -0.0310 -0.0175 0.0478  268 HOH A O    
2817 O  O    B HOH G .   ? 0.3655 0.1642 0.3070 0.0210  0.0236  0.0331  268 HOH A O    
2818 O  O    . HOH G .   ? 0.3021 0.2317 0.3526 -0.0408 0.0082  -0.0988 269 HOH A O    
2819 O  O    . HOH G .   ? 0.3993 0.3222 0.4699 0.0533  0.0847  -0.0307 270 HOH A O    
2820 O  O    . HOH G .   ? 0.5756 0.4871 0.4038 0.0120  -0.0065 -0.1250 271 HOH A O    
2821 O  O    . HOH G .   ? 0.4138 0.3819 0.4683 -0.0881 0.0043  -0.0674 272 HOH A O    
2822 O  O    . HOH G .   ? 0.6226 0.2391 0.3623 0.0373  0.0251  0.0617  273 HOH A O    
2823 O  O    . HOH G .   ? 0.3623 0.5296 0.5238 -0.1124 0.0071  0.1119  274 HOH A O    
2824 O  O    . HOH G .   ? 0.3720 0.3357 0.2876 -0.0082 0.0471  -0.1014 275 HOH A O    
2825 O  O    . HOH G .   ? 0.2161 0.3267 0.5594 -0.1501 -0.0969 -0.0317 276 HOH A O    
2826 O  O    . HOH G .   ? 0.3535 0.5457 0.3521 -0.0159 -0.0006 0.1230  277 HOH A O    
2827 O  O    A HOH G .   ? 0.2193 0.2372 0.2337 0.0749  -0.0560 0.1036  278 HOH A O    
2828 O  O    B HOH G .   ? 0.2910 0.2969 0.2226 0.0346  -0.0276 0.0898  278 HOH A O    
2829 O  O    . HOH G .   ? 0.3402 0.2705 0.3434 -0.0513 -0.0253 -0.0592 279 HOH A O    
2830 O  O    . HOH G .   ? 0.4392 0.3512 0.3210 -0.0974 -0.0706 -0.0825 280 HOH A O    
2831 O  O    . HOH G .   ? 0.2396 0.3122 0.4817 -0.0313 -0.0131 -0.1272 281 HOH A O    
2832 O  O    A HOH G .   ? 0.2917 0.2274 0.3393 -0.0379 -0.1181 -0.0522 282 HOH A O    
2833 O  O    B HOH G .   ? 0.2560 0.1400 0.2256 -0.0621 -0.0649 -0.0076 282 HOH A O    
2834 O  O    . HOH G .   ? 0.4991 0.3470 0.1331 0.0515  0.0566  -0.0635 283 HOH A O    
2835 O  O    . HOH G .   ? 0.4077 0.3955 0.3601 0.0252  -0.0291 0.0007  284 HOH A O    
2836 O  O    . HOH G .   ? 0.4416 0.3528 0.3106 0.0141  0.1274  0.0181  285 HOH A O    
2837 O  O    . HOH G .   ? 0.4837 0.3835 0.5587 -0.0595 0.0372  0.0696  286 HOH A O    
2838 O  O    . HOH G .   ? 0.2102 0.2140 0.2442 -0.0522 -0.0241 0.0046  287 HOH A O    
2839 O  O    . HOH G .   ? 0.2698 0.4004 0.5328 0.0894  -0.0046 0.1067  288 HOH A O    
2840 O  O    . HOH G .   ? 0.3932 0.2773 0.4272 -0.0671 -0.0342 -0.0472 289 HOH A O    
2841 O  O    . HOH G .   ? 0.3492 0.3691 0.5587 0.0366  0.0434  0.0104  290 HOH A O    
2842 O  O    . HOH G .   ? 0.4606 0.3176 0.4905 -0.1233 0.0209  0.0781  291 HOH A O    
2843 O  O    . HOH G .   ? 0.4081 0.4126 0.3167 -0.0262 0.0737  0.0397  292 HOH A O    
2844 O  O    . HOH G .   ? 0.4826 0.4068 0.5684 0.1212  -0.1137 0.0441  293 HOH A O    
2845 O  O    . HOH G .   ? 0.4758 0.4207 0.3332 -0.1206 -0.1026 -0.0060 294 HOH A O    
2846 O  O    A HOH G .   ? 0.2430 0.1088 0.2723 -0.0203 -0.0384 -0.0057 295 HOH A O    
2847 O  O    B HOH G .   ? 0.3158 0.1845 0.2996 -0.0087 0.0505  0.0961  295 HOH A O    
2848 O  O    . HOH G .   ? 0.4916 0.2231 0.4557 0.0186  -0.0401 -0.0421 296 HOH A O    
2849 O  O    . HOH G .   ? 0.3212 0.3014 0.4884 -0.0164 0.0505  0.0181  297 HOH A O    
2850 O  O    . HOH G .   ? 0.5529 0.2590 0.5891 -0.0019 -0.0230 -0.0297 298 HOH A O    
2851 O  O    . HOH G .   ? 0.6790 0.2298 0.5083 -0.0666 0.0010  -0.0151 299 HOH A O    
2852 O  O    . HOH G .   ? 0.4050 0.2615 0.3562 0.0603  0.0087  -0.0443 300 HOH A O    
2853 O  O    . HOH G .   ? 0.5590 0.4438 0.5353 -0.0749 -0.0494 -0.0252 301 HOH A O    
2854 O  O    . HOH G .   ? 0.3170 0.3634 0.4811 0.0071  0.0555  -0.0174 302 HOH A O    
2855 O  O    . HOH G .   ? 0.4156 0.2748 0.4898 0.0702  0.0353  -0.0960 303 HOH A O    
2856 O  O    . HOH G .   ? 0.6323 0.6704 0.6682 0.0272  -0.0233 -0.0054 304 HOH A O    
2857 O  O    . HOH G .   ? 0.5723 0.3086 0.1914 0.0500  -0.0163 0.0186  305 HOH A O    
2858 O  O    A HOH G .   ? 0.4469 0.2978 0.4736 -0.0026 0.0498  -0.0037 306 HOH A O    
2859 O  O    B HOH G .   ? 0.2443 0.2237 0.3865 -0.0557 -0.0225 -0.0625 306 HOH A O    
2860 O  O    . HOH G .   ? 0.4308 0.1962 0.4332 -0.0060 0.0688  0.0142  307 HOH A O    
2861 O  O    . HOH G .   ? 0.4097 0.2791 0.4571 -0.0339 0.0241  0.0188  308 HOH A O    
2862 O  O    . HOH G .   ? 0.3641 0.3740 0.4074 -0.0509 0.0217  -0.0957 309 HOH A O    
2863 O  O    . HOH G .   ? 0.3892 0.2526 0.4922 0.0015  0.0292  0.0639  310 HOH A O    
2864 O  O    . HOH G .   ? 0.4235 0.2759 0.2858 0.0412  0.0568  -0.0834 311 HOH A O    
2865 O  O    A HOH G .   ? 0.2205 0.1522 0.2434 0.0098  -0.0529 -0.0772 312 HOH A O    
2866 O  O    B HOH G .   ? 0.2754 0.1887 0.3005 -0.0405 0.0441  -0.0250 312 HOH A O    
2867 O  O    . HOH G .   ? 0.5763 0.2484 0.3549 0.0355  -0.0207 0.0231  313 HOH A O    
2868 O  O    . HOH G .   ? 0.6157 0.1832 0.5220 -0.0428 -0.0153 -0.0811 314 HOH A O    
2869 O  O    . HOH G .   ? 0.5410 0.3269 0.3707 -0.0658 0.0623  0.0873  315 HOH A O    
2870 O  O    . HOH G .   ? 0.2470 0.2030 0.3068 0.0057  -0.0113 0.0296  316 HOH A O    
2871 O  O    . HOH G .   ? 0.5903 0.4273 0.4162 0.1049  0.1119  -0.0353 317 HOH A O    
2872 O  O    . HOH G .   ? 0.4592 0.3366 0.3946 0.0037  -0.0653 0.0812  318 HOH A O    
2873 O  O    . HOH G .   ? 0.3682 0.3088 0.4214 0.0115  0.0102  -0.0395 319 HOH A O    
2874 O  O    . HOH G .   ? 0.3684 0.2170 0.5062 -0.0410 0.0174  0.1551  320 HOH A O    
2875 O  O    . HOH G .   ? 0.4074 0.4805 0.3948 0.0621  -0.0027 -0.0740 321 HOH A O    
2876 O  O    . HOH G .   ? 0.3781 0.2551 0.4334 0.0088  -0.0099 0.0869  322 HOH A O    
2877 O  O    . HOH G .   ? 0.5120 0.3835 0.3501 -0.0073 0.1045  -0.1080 323 HOH A O    
2878 O  O    . HOH G .   ? 0.4370 0.3553 0.3172 -0.0147 -0.1111 0.0790  324 HOH A O    
2879 O  O    . HOH G .   ? 0.2720 0.2750 0.2535 -0.0390 -0.0384 0.0059  325 HOH A O    
2880 O  O    . HOH G .   ? 0.4474 0.2969 0.4726 0.1216  0.0060  -0.0110 326 HOH A O    
2881 O  O    . HOH G .   ? 0.3853 0.3226 0.4074 0.0129  0.1449  -0.0273 327 HOH A O    
2882 O  O    . HOH G .   ? 0.7069 0.6309 0.2795 -0.0087 0.0299  -0.0549 328 HOH A O    
2883 O  O    . HOH G .   ? 0.3774 0.3282 0.3682 -0.0763 0.0627  -0.0715 329 HOH A O    
2884 O  O    . HOH G .   ? 0.4636 0.2628 0.4840 -0.0478 0.0073  0.0071  330 HOH A O    
2885 O  O    . HOH G .   ? 0.4814 0.3382 0.4198 0.0197  -0.0296 0.0478  331 HOH A O    
2886 O  O    . HOH G .   ? 0.4919 0.3149 0.3294 -0.0634 0.0447  -0.0148 332 HOH A O    
2887 O  O    . HOH G .   ? 0.2549 0.4074 0.4700 -0.0557 0.1261  -0.1391 333 HOH A O    
2888 O  O    . HOH G .   ? 0.5697 0.5799 0.4126 0.0313  -0.0617 0.0379  334 HOH A O    
2889 O  O    . HOH G .   ? 0.5245 0.5572 0.5981 0.0482  0.0478  -0.0020 335 HOH A O    
2890 O  O    . HOH G .   ? 0.3118 0.5371 0.5429 -0.0873 0.1280  0.0741  336 HOH A O    
2891 O  O    . HOH G .   ? 0.4465 0.2691 0.5820 0.0353  -0.0048 0.0483  337 HOH A O    
2892 O  O    . HOH G .   ? 0.5486 0.3916 0.4427 -0.0732 0.0636  0.1474  338 HOH A O    
2893 O  O    . HOH G .   ? 0.4268 0.2709 0.6642 0.0478  -0.0439 -0.0115 339 HOH A O    
2894 O  O    . HOH G .   ? 0.5820 0.5127 0.4898 -0.0377 0.0693  0.0511  340 HOH A O    
2895 O  O    . HOH G .   ? 0.4027 0.3278 0.4438 -0.0974 -0.0337 0.0533  341 HOH A O    
2896 O  O    . HOH G .   ? 0.4904 0.2605 0.6395 -0.0456 0.0649  0.0051  342 HOH A O    
2897 O  O    . HOH G .   ? 0.3357 0.5077 0.6054 0.1937  0.0296  -0.0057 343 HOH A O    
2898 O  O    . HOH G .   ? 0.5996 0.4176 0.5264 -0.0412 0.0696  -0.0586 344 HOH A O    
2899 O  O    . HOH G .   ? 0.4341 0.4808 0.4472 -0.0838 0.0230  -0.0789 345 HOH A O    
2900 O  O    . HOH G .   ? 0.5543 0.3242 0.4751 0.0076  -0.0575 0.0644  346 HOH A O    
2901 O  O    . HOH G .   ? 0.4582 0.3323 0.4833 -0.0493 -0.1299 -0.0049 347 HOH A O    
2902 O  O    . HOH G .   ? 0.3689 0.5730 0.5034 0.0754  -0.1582 0.0966  348 HOH A O    
2903 O  O    . HOH G .   ? 0.4290 0.2910 0.2493 0.0772  0.0232  0.0432  349 HOH A O    
2904 O  O    . HOH G .   ? 0.5388 0.4083 0.2615 0.0438  -0.0264 0.0513  350 HOH A O    
2905 O  O    . HOH G .   ? 0.4489 0.3968 0.2134 -0.0394 0.0732  -0.0610 351 HOH A O    
2906 O  O    . HOH G .   ? 0.3027 0.0847 0.1723 -0.0054 -0.0065 -0.0142 352 HOH A O    
2907 O  O    . HOH G .   ? 0.2382 0.2176 0.2989 0.0869  -0.0342 -0.0957 353 HOH A O    
2908 O  O    . HOH G .   ? 0.2994 0.1163 0.3991 -0.0035 0.0912  -0.0265 354 HOH A O    
2909 O  O    . HOH G .   ? 0.5343 0.3716 0.4013 0.0359  0.0303  -0.0658 355 HOH A O    
2910 O  O    . HOH G .   ? 0.3986 0.2842 0.3152 0.1010  0.0705  0.0930  356 HOH A O    
2911 O  O    . HOH G .   ? 0.1195 0.0476 0.0969 0.0109  -0.0015 -0.0024 357 HOH A O    
2912 O  O    . HOH G .   ? 0.1186 0.0660 0.0992 -0.0186 0.0165  -0.0137 358 HOH A O    
2913 O  O    . HOH G .   ? 0.1145 0.0631 0.0872 -0.0074 0.0068  0.0000  359 HOH A O    
2914 O  O    . HOH G .   ? 0.1084 0.0733 0.0961 0.0194  -0.0085 -0.0041 360 HOH A O    
2915 O  O    . HOH G .   ? 0.1558 0.0617 0.0942 -0.0109 0.0093  -0.0104 361 HOH A O    
2916 O  O    . HOH G .   ? 0.2019 0.0586 0.0546 -0.0197 -0.0037 0.0015  362 HOH A O    
2917 O  O    . HOH G .   ? 0.1233 0.0748 0.1216 0.0098  -0.0167 0.0247  363 HOH A O    
2918 O  O    . HOH G .   ? 0.1195 0.0645 0.1286 0.0109  -0.0208 -0.0063 364 HOH A O    
2919 O  O    . HOH G .   ? 0.1493 0.0615 0.1265 -0.0057 -0.0195 -0.0071 365 HOH A O    
2920 O  O    . HOH G .   ? 0.1369 0.1075 0.1265 -0.0065 -0.0379 0.0147  366 HOH A O    
2921 O  O    . HOH G .   ? 0.1590 0.0527 0.1231 -0.0124 -0.0041 0.0070  367 HOH A O    
2922 O  O    . HOH G .   ? 0.1534 0.0626 0.1008 -0.0137 0.0183  -0.0148 368 HOH A O    
2923 O  O    . HOH G .   ? 0.1416 0.0951 0.1459 0.0164  -0.0041 0.0057  369 HOH A O    
2924 O  O    . HOH G .   ? 0.2093 0.0851 0.1242 -0.0366 -0.0276 0.0082  370 HOH A O    
2925 O  O    . HOH G .   ? 0.0917 0.1084 0.1906 0.0020  -0.0175 -0.0452 371 HOH A O    
2926 O  O    . HOH G .   ? 0.1800 0.0727 0.1197 -0.0098 -0.0010 0.0068  372 HOH A O    
2927 O  O    . HOH G .   ? 0.1412 0.1294 0.1481 0.0197  -0.0178 0.0206  373 HOH A O    
2928 O  O    . HOH G .   ? 0.1488 0.1014 0.1744 -0.0148 0.0175  -0.0027 374 HOH A O    
2929 O  O    . HOH G .   ? 0.1820 0.0816 0.1438 0.0003  -0.0215 0.0034  375 HOH A O    
2930 O  O    . HOH G .   ? 0.1466 0.1781 0.1523 -0.0233 -0.0531 0.0533  376 HOH A O    
2931 O  O    . HOH G .   ? 0.0969 0.1471 0.2246 0.0115  0.0193  -0.0395 377 HOH A O    
2932 O  O    . HOH G .   ? 0.1869 0.0809 0.1279 0.0137  -0.0208 0.0080  378 HOH A O    
2933 O  O    . HOH G .   ? 0.1992 0.0728 0.1653 -0.0229 -0.0060 0.0131  379 HOH A O    
2934 O  O    . HOH G .   ? 0.2305 0.1454 0.2458 0.0076  -0.1304 -0.0463 380 HOH A O    
2935 O  O    . HOH G .   ? 0.2360 0.0730 0.1692 0.0000  -0.0697 0.0043  381 HOH A O    
2936 O  O    . HOH G .   ? 0.3398 0.0820 0.1700 0.0218  0.0174  0.0175  382 HOH A O    
2937 O  O    . HOH G .   ? 0.2892 0.1409 0.3443 0.0171  0.1044  0.0104  383 HOH A O    
2938 O  O    . HOH G .   ? 0.1991 0.1554 0.2308 0.0060  0.0553  0.0469  384 HOH A O    
2939 O  O    A HOH G .   ? 0.1423 0.0949 0.1127 0.0121  -0.0306 0.0136  385 HOH A O    
2940 O  O    B HOH G .   ? 0.1711 0.0960 0.0983 0.0102  -0.0263 0.0043  385 HOH A O    
2941 O  O    . HOH G .   ? 0.2169 0.1158 0.1601 -0.0005 -0.0368 -0.0054 386 HOH A O    
2942 O  O    . HOH G .   ? 0.2017 0.1500 0.1726 0.0282  0.0313  -0.0197 387 HOH A O    
2943 O  O    . HOH G .   ? 0.2474 0.0944 0.1432 -0.0040 -0.0728 -0.0048 388 HOH A O    
2944 O  O    . HOH G .   ? 0.2120 0.1412 0.1592 -0.0057 -0.0625 0.0046  389 HOH A O    
2945 O  O    . HOH G .   ? 0.2919 0.1518 0.2558 0.0423  0.0480  0.0372  390 HOH A O    
2946 O  O    . HOH G .   ? 0.1820 0.2459 0.1213 0.0296  0.0086  -0.0286 391 HOH A O    
2947 O  O    . HOH G .   ? 0.2093 0.1299 0.2163 0.0041  0.0153  0.0333  392 HOH A O    
2948 O  O    . HOH G .   ? 0.2314 0.2134 0.1633 0.0281  0.0494  -0.0230 393 HOH A O    
2949 O  O    . HOH G .   ? 0.1965 0.1193 0.2624 -0.0679 -0.0548 -0.0098 394 HOH A O    
2950 O  O    . HOH G .   ? 0.1234 0.1268 0.3113 -0.0198 0.0024  -0.0020 395 HOH A O    
2951 O  O    . HOH G .   ? 0.3490 0.1199 0.1793 0.0430  -0.0912 -0.0390 396 HOH A O    
2952 O  O    . HOH G .   ? 0.1777 0.1576 0.2402 0.0120  -0.0082 0.0054  397 HOH A O    
2953 O  O    . HOH G .   ? 0.1624 0.1014 0.2951 -0.0483 -0.0644 0.0030  398 HOH A O    
2954 O  O    . HOH G .   ? 0.1423 0.1181 0.2590 -0.0098 0.0092  0.0098  399 HOH A O    
2955 O  O    . HOH G .   ? 0.2793 0.1206 0.2266 -0.0148 -0.0093 -0.0181 400 HOH A O    
2956 O  O    . HOH G .   ? 0.2495 0.1414 0.1956 0.0366  0.0406  0.0812  401 HOH A O    
2957 O  O    . HOH G .   ? 0.1920 0.0802 0.1527 0.0023  -0.0335 0.0115  402 HOH A O    
2958 O  O    . HOH G .   ? 0.1782 0.1745 0.2585 -0.0031 0.0121  -0.0275 403 HOH A O    
2959 O  O    . HOH G .   ? 0.2373 0.1448 0.1732 0.0282  -0.0472 0.0104  404 HOH A O    
2960 O  O    . HOH G .   ? 0.1904 0.1393 0.2199 0.0082  0.0172  -0.0174 405 HOH A O    
2961 O  O    A HOH G .   ? 0.1249 0.1057 0.1003 0.0348  0.0185  0.0370  406 HOH A O    
2962 O  O    B HOH G .   ? 0.3233 0.1368 0.1170 -0.0595 0.0599  0.0118  406 HOH A O    
2963 O  O    . HOH G .   ? 0.1935 0.1061 0.2416 0.0274  -0.0259 -0.0395 407 HOH A O    
2964 O  O    . HOH G .   ? 0.2179 0.2903 0.1980 -0.0003 0.0238  -0.0675 408 HOH A O    
2965 O  O    . HOH G .   ? 0.1876 0.1231 0.1877 0.0046  -0.0296 -0.0233 409 HOH A O    
2966 O  O    . HOH G .   ? 0.2310 0.1427 0.2081 -0.0060 -0.0516 -0.0680 410 HOH A O    
2967 O  O    . HOH G .   ? 0.3366 0.1402 0.1324 0.0040  -0.0241 0.0546  411 HOH A O    
2968 O  O    . HOH G .   ? 0.2721 0.1242 0.1394 0.0017  -0.0242 0.0115  412 HOH A O    
2969 O  O    . HOH G .   ? 0.2982 0.1118 0.2090 0.0135  -0.0430 -0.0114 413 HOH A O    
2970 O  O    . HOH G .   ? 0.2587 0.1506 0.1622 0.0335  -0.0167 0.0478  414 HOH A O    
2971 O  O    . HOH G .   ? 0.3537 0.1229 0.2442 0.0046  -0.1058 0.0399  415 HOH A O    
2972 O  O    . HOH G .   ? 0.1781 0.1256 0.2125 -0.0026 -0.0357 0.0239  416 HOH A O    
2973 O  O    . HOH G .   ? 0.3249 0.1714 0.1680 -0.0749 0.0772  -0.0478 417 HOH A O    
2974 O  O    . HOH G .   ? 0.3077 0.1515 0.1879 -0.0803 -0.0436 -0.0005 418 HOH A O    
2975 O  O    . HOH G .   ? 0.2567 0.1608 0.2436 -0.0675 0.0390  -0.0476 419 HOH A O    
2976 O  O    . HOH G .   ? 0.3208 0.1423 0.2509 -0.0060 -0.0485 -0.0581 420 HOH A O    
2977 O  O    . HOH G .   ? 0.2310 0.1344 0.2063 0.0299  0.0175  -0.0098 421 HOH A O    
2978 O  O    . HOH G .   ? 0.3030 0.3165 0.2838 0.1509  -0.0535 -0.0297 422 HOH A O    
2979 O  O    A HOH G .   ? 0.2370 0.1619 0.1364 -0.0397 -0.0524 0.0113  423 HOH A O    
2980 O  O    B HOH G .   ? 0.1685 0.1534 0.1687 -0.0542 -0.0513 0.0110  423 HOH A O    
2981 O  O    . HOH G .   ? 0.2527 0.1098 0.2075 0.0372  -0.0151 -0.0140 424 HOH A O    
2982 O  O    . HOH G .   ? 0.2518 0.2167 0.2391 -0.0640 -0.0186 -0.0273 425 HOH A O    
2983 O  O    . HOH G .   ? 0.3472 0.1991 0.3533 0.0450  -0.1596 -0.0425 426 HOH A O    
2984 O  O    . HOH G .   ? 0.1854 0.1489 0.2892 0.0403  -0.0200 -0.0027 427 HOH A O    
2985 O  O    . HOH G .   ? 0.3217 0.3666 0.2025 -0.0375 0.0487  0.0197  428 HOH A O    
2986 O  O    A HOH G .   ? 0.2188 0.1529 0.1294 -0.0469 -0.0403 0.0087  429 HOH A O    
2987 O  O    B HOH G .   ? 0.1858 0.1929 0.1396 -0.0535 0.0183  0.0210  429 HOH A O    
2988 O  O    . HOH G .   ? 0.3440 0.3398 0.1145 -0.0005 0.0265  0.0948  430 HOH A O    
2989 O  O    . HOH G .   ? 0.2824 0.1412 0.1374 0.0085  -0.0177 -0.0082 431 HOH A O    
2990 O  O    . HOH G .   ? 0.2870 0.1870 0.2432 -0.0209 -0.0776 -0.0162 432 HOH A O    
2991 O  O    A HOH G .   ? 0.2563 0.2389 0.2269 -0.0263 -0.0737 0.1238  433 HOH A O    
2992 O  O    B HOH G .   ? 0.2292 0.1168 0.1641 0.0178  -0.0522 0.0724  433 HOH A O    
2993 O  O    . HOH G .   ? 0.2134 0.1689 0.3226 0.0027  -0.0388 -0.0099 434 HOH A O    
2994 O  O    . HOH G .   ? 0.3158 0.2296 0.1678 -0.0315 0.0107  0.0417  435 HOH A O    
2995 O  O    . HOH G .   ? 0.2603 0.1809 0.1509 -0.0178 0.0207  0.0102  436 HOH A O    
2996 O  O    . HOH G .   ? 0.2518 0.1133 0.1632 0.0243  -0.0366 -0.0226 437 HOH A O    
2997 O  O    . HOH G .   ? 0.2772 0.1735 0.2117 0.0054  0.0428  -0.0227 438 HOH A O    
2998 O  O    . HOH G .   ? 0.1608 0.1985 0.2412 0.0241  -0.0207 0.0636  439 HOH A O    
2999 O  O    . HOH G .   ? 0.4065 0.1788 0.2908 0.0445  0.0326  0.0410  440 HOH A O    
3000 O  O    . HOH G .   ? 0.2238 0.2064 0.2985 0.0975  -0.0828 -0.0154 441 HOH A O    
3001 O  O    . HOH G .   ? 0.3824 0.1832 0.1748 -0.0253 -0.0137 0.0146  442 HOH A O    
3002 O  O    . HOH G .   ? 0.4147 0.2414 0.2000 -0.0689 0.0610  -0.0560 443 HOH A O    
3003 O  O    . HOH G .   ? 0.3113 0.2364 0.3048 -0.0320 -0.0604 0.1027  444 HOH A O    
3004 O  O    . HOH G .   ? 0.2337 0.2447 0.3930 0.1308  0.1717  0.1040  445 HOH A O    
3005 O  O    . HOH G .   ? 0.1328 0.3106 0.3837 0.0318  -0.0147 0.1158  446 HOH A O    
3006 O  O    . HOH G .   ? 0.1439 0.2217 0.3377 -0.0284 -0.0320 0.0419  447 HOH A O    
3007 O  O    . HOH G .   ? 0.2327 0.1858 0.1818 -0.0454 0.0098  -0.0375 448 HOH A O    
3008 O  O    . HOH G .   ? 0.2556 0.1137 0.2529 -0.0237 -0.0463 -0.0074 449 HOH A O    
3009 O  O    . HOH G .   ? 0.2412 0.2495 0.2585 0.0082  -0.0436 -0.0581 450 HOH A O    
3010 O  O    . HOH G .   ? 0.2569 0.2714 0.2063 0.0373  0.0577  -0.0068 451 HOH A O    
3011 O  O    . HOH G .   ? 0.2326 0.1337 0.2300 0.0156  -0.0511 -0.0252 452 HOH A O    
3012 O  O    . HOH G .   ? 0.3946 0.1814 0.2229 -0.0287 -0.0390 0.0480  453 HOH A O    
3013 O  O    . HOH G .   ? 0.2567 0.1877 0.3154 -0.0688 0.0544  -0.0250 454 HOH A O    
3014 O  O    . HOH G .   ? 0.3276 0.3167 0.2608 0.1348  0.1133  0.0837  455 HOH A O    
3015 O  O    . HOH G .   ? 0.2084 0.2420 0.3526 0.0342  0.0445  0.0687  456 HOH A O    
3016 O  O    . HOH G .   ? 0.3032 0.1800 0.2059 -0.0496 -0.0414 -0.0131 457 HOH A O    
3017 O  O    . HOH G .   ? 0.3783 0.1680 0.2630 0.0184  0.1450  -0.0522 458 HOH A O    
3018 O  O    . HOH G .   ? 0.3623 0.1421 0.1787 0.0049  -0.0399 0.0038  459 HOH A O    
3019 O  O    . HOH G .   ? 0.3740 0.2827 0.1996 -0.1111 -0.0299 -0.0230 460 HOH A O    
3020 O  O    . HOH G .   ? 0.2071 0.2157 0.2166 0.0283  -0.0538 -0.0174 461 HOH A O    
3021 O  O    . HOH G .   ? 0.2711 0.1321 0.2156 0.0074  0.0181  0.0527  462 HOH A O    
3022 O  O    . HOH G .   ? 0.3420 0.4965 0.2360 0.0071  -0.0306 0.0653  463 HOH A O    
3023 O  O    . HOH G .   ? 0.2402 0.3273 0.2996 -0.0772 -0.0450 -0.0216 464 HOH A O    
3024 O  O    . HOH G .   ? 0.5120 0.2653 0.2178 -0.0828 0.0087  0.0077  465 HOH A O    
3025 O  O    . HOH G .   ? 0.2309 0.3643 0.2802 0.0046  0.0706  0.0564  466 HOH A O    
3026 O  O    A HOH G .   ? 0.3102 0.1719 0.2281 0.0575  -0.0346 0.0231  467 HOH A O    
3027 O  O    B HOH G .   ? 0.1836 0.1498 0.1515 0.0538  -0.0292 0.0410  467 HOH A O    
3028 O  O    . HOH G .   ? 0.5568 0.3819 0.1161 -0.0057 -0.0315 0.1110  468 HOH A O    
3029 O  O    . HOH G .   ? 0.2260 0.2797 0.1680 -0.0211 -0.0109 -0.0869 469 HOH A O    
3030 O  O    . HOH G .   ? 0.3472 0.2332 0.1969 0.0175  0.0076  -0.0644 470 HOH A O    
3031 O  O    . HOH G .   ? 0.2029 0.3355 0.2323 0.0417  0.0164  -0.0052 471 HOH A O    
3032 O  O    . HOH G .   ? 0.3488 0.1806 0.3041 0.0869  -0.0544 -0.0208 472 HOH A O    
3033 O  O    . HOH G .   ? 0.1921 0.0579 0.1351 0.0063  -0.0019 -0.0082 473 HOH A O    
3034 O  O    . HOH G .   ? 0.2506 0.2998 0.2892 -0.0540 0.0837  -0.1366 474 HOH A O    
3035 O  O    . HOH G .   ? 0.2075 0.2531 0.5174 -0.0566 -0.0142 -0.0377 475 HOH A O    
3036 O  O    . HOH G .   ? 0.2773 0.1492 0.2978 -0.0126 0.0346  -0.0046 476 HOH A O    
3037 O  O    . HOH G .   ? 0.3612 0.1992 0.1893 0.0187  0.0186  0.0226  477 HOH A O    
3038 O  O    . HOH G .   ? 0.4329 0.2500 0.1597 -0.0819 -0.0604 -0.0104 478 HOH A O    
3039 O  O    A HOH G .   ? 0.2461 0.2675 0.1861 0.0175  -0.0065 0.0806  479 HOH A O    
3040 O  O    B HOH G .   ? 0.2773 0.1482 0.1017 0.0020  -0.0315 -0.0071 479 HOH A O    
3041 O  O    . HOH G .   ? 0.3127 0.1861 0.2752 -0.0397 -0.0728 0.0252  480 HOH A O    
3042 O  O    . HOH G .   ? 0.3305 0.1453 0.4319 0.0102  0.0241  0.0696  481 HOH A O    
3043 O  O    . HOH G .   ? 0.3364 0.2011 0.1637 -0.0619 0.0126  0.0305  482 HOH A O    
3044 O  O    . HOH G .   ? 0.2354 0.2842 0.1951 -0.0315 -0.0076 0.0195  483 HOH A O    
3045 O  O    . HOH G .   ? 0.2994 0.1472 0.3305 -0.0103 0.0197  0.0612  484 HOH A O    
3046 O  O    . HOH G .   ? 0.2734 0.1897 0.3847 -0.0065 0.0043  -0.0939 485 HOH A O    
3047 O  O    . HOH G .   ? 0.3077 0.1831 0.3840 0.1035  0.1023  0.1062  486 HOH A O    
3048 O  O    . HOH G .   ? 0.3305 0.1996 0.3341 -0.0719 0.0878  -0.0601 487 HOH A O    
3049 O  O    . HOH G .   ? 0.3490 0.4246 0.1437 0.0187  -0.0780 -0.0788 488 HOH A O    
3050 O  O    . HOH G .   ? 0.2637 0.2111 0.3847 -0.0326 0.1067  -0.0293 489 HOH A O    
3051 O  O    . HOH G .   ? 0.4104 0.1462 0.2127 -0.0653 -0.1089 -0.0388 490 HOH A O    
3052 O  O    . HOH G .   ? 0.3161 0.1854 0.2556 -0.0026 0.0639  0.0041  491 HOH A O    
3053 O  O    . HOH G .   ? 0.2949 0.1556 0.2563 0.0059  -0.0017 -0.0204 492 HOH A O    
3054 O  O    . HOH G .   ? 0.3722 0.4578 0.1500 0.1063  -0.0775 -0.0204 493 HOH A O    
3055 O  O    . HOH G .   ? 0.4672 0.2454 0.2996 -0.0417 -0.0240 0.0619  494 HOH A O    
3056 O  O    . HOH G .   ? 0.4036 0.2985 0.4101 -0.0317 0.0416  -0.0249 495 HOH A O    
3057 O  O    A HOH G .   ? 0.1262 0.2461 0.3901 0.0120  0.0208  0.0803  496 HOH A O    
3058 O  O    B HOH G .   ? 0.3447 0.2939 0.3535 0.0644  -0.0430 0.0020  496 HOH A O    
3059 O  O    . HOH G .   ? 0.4553 0.2108 0.2881 -0.0636 0.1287  -0.1198 497 HOH A O    
3060 O  O    . HOH G .   ? 0.3226 0.2418 0.2436 0.0160  -0.0557 -0.0175 498 HOH A O    
3061 O  O    . HOH G .   ? 0.2709 0.2089 0.3422 -0.0097 0.1149  0.0537  499 HOH A O    
3062 O  O    . HOH G .   ? 0.5070 0.3418 0.3088 -0.0612 -0.1745 0.0535  500 HOH A O    
3063 O  O    . HOH G .   ? 0.5418 0.3476 0.2296 0.0750  0.0017  -0.0006 501 HOH A O    
3064 O  O    . HOH G .   ? 0.3260 0.1906 0.4115 -0.0296 0.0745  -0.0489 502 HOH A O    
3065 O  O    . HOH G .   ? 0.2178 0.2492 0.3251 -0.0104 0.0480  0.0281  503 HOH A O    
3066 O  O    . HOH G .   ? 0.4467 0.2574 0.2700 -0.0353 -0.0538 -0.0266 504 HOH A O    
3067 O  O    . HOH G .   ? 0.3339 0.3691 0.2691 -0.0284 -0.0262 -0.0243 505 HOH A O    
3068 O  O    . HOH G .   ? 0.5084 0.3980 0.2572 -0.0113 -0.0715 0.0750  506 HOH A O    
3069 O  O    . HOH G .   ? 0.4697 0.1775 0.1958 0.0749  0.0208  0.0174  507 HOH A O    
3070 O  O    . HOH G .   ? 0.2615 0.3115 0.2693 -0.1181 0.0000  0.0240  508 HOH A O    
3071 O  O    . HOH G .   ? 0.6930 0.2777 0.1423 -0.0248 -0.0114 0.1717  509 HOH A O    
3072 O  O    . HOH G .   ? 0.3986 0.2275 0.1805 -0.0086 -0.0160 -0.0553 510 HOH A O    
3073 O  O    . HOH G .   ? 0.5450 0.2897 0.2703 -0.0926 0.0450  -0.0020 511 HOH A O    
3074 O  O    . HOH G .   ? 0.1859 0.2064 0.3941 0.0353  0.0074  0.0043  512 HOH A O    
3075 O  O    . HOH G .   ? 0.1574 0.2120 0.3452 0.0395  0.0504  0.0103  513 HOH A O    
3076 O  O    . HOH G .   ? 0.5472 0.3837 0.3882 -0.0120 0.0164  -0.0527 514 HOH A O    
3077 O  O    . HOH G .   ? 0.4074 0.1987 0.5310 -0.0162 -0.0504 -0.1224 515 HOH A O    
3078 O  O    . HOH G .   ? 0.3853 0.1477 0.2777 0.0206  -0.0262 0.0496  516 HOH A O    
3079 O  O    . HOH G .   ? 0.5127 0.4717 0.2003 -0.0732 0.0026  0.1146  517 HOH A O    
3080 O  O    . HOH G .   ? 0.3571 0.2811 0.3623 -0.0925 -0.0948 0.0908  518 HOH A O    
3081 O  O    . HOH G .   ? 0.2036 0.2177 0.3316 0.0313  0.0313  0.0220  519 HOH A O    
3082 O  O    . HOH G .   ? 0.3073 0.2023 0.4241 0.0604  0.0351  0.0798  520 HOH A O    
3083 O  O    . HOH G .   ? 0.3713 0.2915 0.2768 -0.0003 0.0992  0.0658  521 HOH A O    
3084 O  O    . HOH G .   ? 0.2982 0.2962 0.3208 0.1150  0.0419  0.0504  522 HOH A O    
3085 O  O    . HOH G .   ? 0.4799 0.2230 0.3865 -0.0803 -0.0124 -0.0326 523 HOH A O    
3086 O  O    . HOH G .   ? 0.2263 0.2152 0.3361 -0.0423 -0.0606 0.0242  524 HOH A O    
3087 O  O    A HOH G .   ? 0.1039 0.0730 0.1470 0.0041  -0.0390 0.0096  525 HOH A O    
3088 O  O    B HOH G .   ? 0.1651 0.0926 0.0985 0.0131  -0.0410 0.0265  525 HOH A O    
3089 O  O    . HOH G .   ? 0.2558 0.2221 0.4970 0.0684  -0.0452 -0.0377 526 HOH A O    
3090 O  O    . HOH G .   ? 0.2858 0.2915 0.2739 0.0173  0.0313  0.0317  527 HOH A O    
3091 O  O    . HOH G .   ? 0.2847 0.2508 0.5321 -0.1168 0.0092  -0.0020 528 HOH A O    
3092 O  O    . HOH G .   ? 0.2406 0.1481 0.4568 0.0041  -0.0348 0.0357  529 HOH A O    
3093 O  O    . HOH G .   ? 0.3115 0.3222 0.2587 0.0173  -0.0175 -0.0031 530 HOH A O    
3094 O  O    . HOH G .   ? 0.4183 0.2475 0.4266 -0.0274 -0.0614 0.0098  531 HOH A O    
3095 O  O    . HOH G .   ? 0.2876 0.2057 0.3876 -0.0005 0.0142  -0.0860 532 HOH A O    
3096 O  O    . HOH G .   ? 0.2161 0.2045 0.5687 -0.0074 0.0693  0.0148  533 HOH A O    
3097 O  O    . HOH G .   ? 0.3826 0.3142 0.2870 0.0137  -0.0205 0.0856  534 HOH A O    
3098 O  O    . HOH G .   ? 0.3991 0.3249 0.3055 -0.0507 0.0226  -0.0219 535 HOH A O    
3099 O  O    . HOH G .   ? 0.2851 0.3000 0.2303 -0.0366 0.0030  -0.0689 536 HOH A O    
3100 O  O    A HOH G .   ? 0.2495 0.3975 0.1775 -0.0606 -0.0592 0.0287  537 HOH A O    
3101 O  O    B HOH G .   ? 0.2231 0.2039 0.1234 -0.0052 -0.0564 0.0373  537 HOH A O    
3102 O  O    . HOH G .   ? 0.4138 0.3000 0.4909 0.0161  0.0432  -0.0467 538 HOH A O    
3103 O  O    . HOH G .   ? 0.2716 0.2412 0.4036 -0.1146 -0.0215 -0.1216 539 HOH A O    
3104 O  O    . HOH G .   ? 0.1247 0.5690 0.3043 0.0645  -0.0007 -0.2221 540 HOH A O    
3105 O  O    A HOH G .   ? 0.3407 0.1085 0.1912 -0.0243 -0.0388 0.0175  541 HOH A O    
3106 O  O    B HOH G .   ? 0.2861 0.1929 0.2069 -0.0307 -0.0048 0.0258  541 HOH A O    
3107 O  O    . HOH G .   ? 0.2592 0.5235 0.4571 -0.0208 0.0952  0.1106  542 HOH A O    
3108 O  O    . HOH G .   ? 0.3501 0.5562 0.2027 -0.0416 0.0379  -0.0299 543 HOH A O    
3109 O  O    . HOH G .   ? 0.5059 0.2879 0.5062 -0.1243 0.0015  0.0410  544 HOH A O    
3110 O  O    . HOH G .   ? 0.3679 0.3249 0.4675 -0.0538 0.0357  0.0326  545 HOH A O    
3111 O  O    . HOH G .   ? 0.4668 0.3009 0.3625 -0.0930 -0.0027 -0.0864 546 HOH A O    
3112 O  O    . HOH G .   ? 0.4650 0.2181 0.3057 -0.0912 0.0046  0.0228  547 HOH A O    
3113 O  O    . HOH G .   ? 0.2840 0.3131 0.3792 0.0419  0.0588  0.0274  548 HOH A O    
3114 O  O    . HOH G .   ? 0.2745 0.3134 0.4914 0.1014  0.0881  0.1343  549 HOH A O    
3115 O  O    . HOH G .   ? 0.4912 0.1908 0.2402 0.0533  -0.0233 0.0741  550 HOH A O    
3116 O  O    . HOH G .   ? 0.3804 0.2215 0.4609 -0.0114 0.0917  -0.0395 551 HOH A O    
3117 O  O    A HOH G .   ? 0.1477 0.1439 0.2285 -0.0368 0.0255  0.0098  552 HOH A O    
3118 O  O    B HOH G .   ? 0.1290 0.1613 0.3844 -0.0197 0.0266  -0.0542 552 HOH A O    
3119 O  O    . HOH G .   ? 0.3695 0.2824 0.3625 -0.0153 0.0027  0.0263  553 HOH A O    
3120 O  O    . HOH G .   ? 0.2540 0.3328 0.2560 -0.0156 0.0483  0.0015  554 HOH A O    
3121 O  O    . HOH G .   ? 0.2005 0.2170 0.4273 -0.0546 -0.0653 0.0395  555 HOH A O    
3122 O  O    . HOH G .   ? 0.1808 0.4742 0.3402 -0.0781 0.0294  0.0381  556 HOH A O    
3123 O  O    . HOH G .   ? 0.2901 0.3228 0.3151 0.0785  0.1217  0.0107  557 HOH A O    
3124 O  O    . HOH G .   ? 0.2734 0.2497 0.5295 -0.0913 0.0979  -0.0260 558 HOH A O    
3125 O  O    . HOH G .   ? 0.5515 0.3874 0.2318 -0.0208 -0.0423 0.0063  559 HOH A O    
3126 O  O    . HOH G .   ? 0.2836 0.3930 0.3776 0.0231  0.0274  0.0346  560 HOH A O    
3127 O  O    . HOH G .   ? 0.2381 0.3970 0.5982 -0.0313 -0.0961 0.0920  561 HOH A O    
3128 O  O    . HOH G .   ? 0.6200 0.1371 0.3298 -0.0228 -0.0065 0.0104  562 HOH A O    
3129 O  O    . HOH G .   ? 0.3783 0.2685 0.4038 -0.0317 -0.0974 0.0230  563 HOH A O    
3130 O  O    A HOH G .   ? 0.2551 0.2560 0.2178 -0.0041 0.0255  0.0518  564 HOH A O    
3131 O  O    B HOH G .   ? 0.2212 0.3082 0.2705 0.0098  0.0131  0.1008  564 HOH A O    
3132 O  O    . HOH G .   ? 0.5468 0.3337 0.3709 -0.0803 0.0736  -0.0228 565 HOH A O    
3133 O  O    A HOH G .   ? 0.1908 0.3032 0.1960 0.0518  0.0364  0.0983  566 HOH A O    
3134 O  O    B HOH G .   ? 0.1912 0.1729 0.1840 0.0000  -0.0174 0.0658  566 HOH A O    
3135 O  O    . HOH G .   ? 0.4081 0.3465 0.4997 0.0719  0.0077  -0.0188 567 HOH A O    
3136 O  O    . HOH G .   ? 0.4176 0.3508 0.3941 -0.0346 -0.0309 -0.0215 568 HOH A O    
3137 O  O    . HOH G .   ? 0.5048 0.3637 0.2705 0.0474  0.0427  0.0842  569 HOH A O    
3138 O  O    . HOH G .   ? 0.2345 0.4253 0.5101 0.0627  0.0049  -0.0491 570 HOH A O    
3139 O  O    A HOH G .   ? 0.2244 0.2046 0.2046 0.0549  0.0469  -0.0443 571 HOH A O    
3140 O  O    B HOH G .   ? 0.2763 0.1541 0.1419 -0.0043 0.0174  -0.0399 571 HOH A O    
3141 O  O    . HOH G .   ? 0.4348 0.2084 0.4156 0.0175  0.0052  -0.0542 572 HOH A O    
3142 O  O    . HOH G .   ? 0.3506 0.2788 0.3109 0.0337  -0.0969 0.0549  573 HOH A O    
3143 O  O    . HOH G .   ? 0.2422 0.6316 0.4706 0.0073  0.0119  0.0696  574 HOH A O    
3144 O  O    . HOH G .   ? 0.3759 0.3271 0.2991 -0.0416 0.0776  -0.0449 575 HOH A O    
3145 O  O    . HOH G .   ? 0.4059 0.3109 0.2477 -0.0593 -0.0227 0.1162  576 HOH A O    
3146 O  O    . HOH G .   ? 0.3481 0.6236 0.2793 0.0120  -0.0471 -0.0326 577 HOH A O    
3147 O  O    . HOH G .   ? 0.4232 0.2421 0.4088 0.0634  0.1543  0.0744  578 HOH A O    
3148 O  O    . HOH G .   ? 0.5228 0.4423 0.3192 -0.0916 0.1142  -0.0662 579 HOH A O    
3149 O  O    . HOH G .   ? 0.3476 0.2511 0.4345 0.0908  -0.1230 -0.0877 580 HOH A O    
3150 O  O    . HOH G .   ? 0.3903 0.3833 0.5644 -0.0293 0.0141  0.0194  581 HOH A O    
3151 O  O    . HOH G .   ? 0.5705 0.2398 0.3901 0.0340  0.0575  -0.0472 582 HOH A O    
3152 O  O    . HOH G .   ? 0.4801 0.4999 0.2957 -0.0054 0.0428  -0.1283 583 HOH A O    
3153 O  O    . HOH G .   ? 0.4138 0.2157 0.2193 -0.0812 0.0208  -0.0359 584 HOH A O    
3154 O  O    . HOH G .   ? 0.5400 0.3558 0.2267 -0.0706 0.0176  -0.0601 585 HOH A O    
3155 O  O    . HOH G .   ? 0.5199 0.4616 0.4223 -0.0524 0.0353  0.0476  586 HOH A O    
3156 O  O    . HOH G .   ? 0.3034 0.4212 0.2888 -0.0465 -0.0546 0.0850  587 HOH A O    
3157 O  O    . HOH G .   ? 0.3208 0.4986 0.4538 0.0789  0.0834  -0.0219 588 HOH A O    
3158 O  O    . HOH G .   ? 0.4675 0.3075 0.2337 0.0030  -0.0494 -0.0432 589 HOH A O    
3159 O  O    . HOH G .   ? 0.3826 0.3012 0.2567 0.0148  -0.0247 -0.0700 590 HOH A O    
3160 O  O    . HOH G .   ? 0.3052 0.3589 0.2754 0.0899  0.0405  0.1009  591 HOH A O    
3161 O  O    . HOH G .   ? 0.2691 0.3217 0.3190 -0.0342 -0.0948 0.0414  592 HOH A O    
3162 O  O    . HOH G .   ? 0.2966 0.3158 0.6492 -0.0571 -0.0222 -0.0115 593 HOH A O    
3163 O  O    . HOH G .   ? 0.4388 0.3156 0.2529 -0.0340 0.0381  0.0348  594 HOH A O    
3164 O  O    . HOH G .   ? 0.3296 0.1854 0.3677 -0.1652 -0.0815 0.0584  595 HOH A O    
3165 O  O    . HOH G .   ? 0.5105 0.4000 0.2978 -0.1250 -0.0043 0.1177  596 HOH A O    
3166 O  O    . HOH G .   ? 0.3483 0.3533 0.3165 0.0496  0.0983  0.0013  597 HOH A O    
3167 O  O    . HOH G .   ? 0.3458 0.1825 0.2382 -0.0098 0.0373  -0.0140 598 HOH A O    
3168 O  O    . HOH G .   ? 0.4713 0.5727 0.3889 0.0373  0.0041  0.0684  599 HOH A O    
3169 O  O    . HOH G .   ? 0.4920 0.3898 0.3416 0.0601  -0.0741 0.0684  600 HOH A O    
3170 O  O    . HOH G .   ? 0.4862 0.5174 0.2599 0.1321  -0.0709 0.0041  601 HOH A O    
3171 O  O    . HOH G .   ? 0.4768 0.2342 0.2377 -0.0340 -0.0575 0.0151  602 HOH A O    
3172 O  O    . HOH G .   ? 0.2624 0.2258 0.5356 -0.0195 0.0006  -0.0509 603 HOH A O    
3173 O  O    . HOH G .   ? 0.3686 0.2885 0.3397 0.0155  -0.0649 -0.1728 604 HOH A O    
3174 O  O    . HOH G .   ? 0.4871 0.5105 0.2005 -0.0450 0.0467  0.0520  605 HOH A O    
3175 O  O    . HOH G .   ? 0.4379 0.2921 0.4171 0.0076  -0.1464 0.0666  606 HOH A O    
3176 O  O    . HOH G .   ? 0.4092 0.4550 0.6366 0.0242  -0.0026 0.0091  607 HOH A O    
3177 O  O    . HOH G .   ? 0.4431 0.2854 0.4169 0.0043  -0.1208 0.0399  608 HOH A O    
3178 O  O    . HOH G .   ? 0.4144 0.3176 0.4320 0.0049  0.0236  0.0108  609 HOH A O    
3179 O  O    . HOH G .   ? 0.3260 0.1653 0.3352 -0.0394 0.0397  -0.0207 610 HOH A O    
3180 O  O    . HOH G .   ? 0.3662 0.3258 0.3671 0.1185  -0.1374 -0.0375 611 HOH A O    
3181 O  O    . HOH G .   ? 0.6096 0.3713 0.4603 -0.0274 0.0080  -0.0746 612 HOH A O    
3182 O  O    . HOH G .   ? 0.2948 0.1980 0.2669 0.0003  -0.0143 0.0566  613 HOH A O    
3183 O  O    . HOH G .   ? 0.4977 0.3831 0.2985 0.0082  0.0722  -0.1005 614 HOH A O    
3184 O  O    . HOH G .   ? 0.1500 0.3434 0.5375 0.0151  -0.0313 0.0832  615 HOH A O    
3185 O  O    . HOH G .   ? 0.5985 0.2831 0.2930 0.0524  0.0065  -0.0348 616 HOH A O    
3186 O  O    . HOH G .   ? 0.3740 0.1727 0.3966 -0.0005 0.0741  0.0715  617 HOH A O    
3187 O  O    . HOH G .   ? 0.3961 0.2527 0.3533 -0.0098 0.0579  -0.0533 618 HOH A O    
3188 O  O    . HOH G .   ? 0.2863 0.2924 0.4412 -0.0263 -0.0706 -0.0041 619 HOH A O    
3189 O  O    . HOH G .   ? 0.4957 0.4208 0.4700 -0.0456 0.0104  -0.0680 620 HOH A O    
3190 O  O    . HOH G .   ? 0.3995 0.3941 0.5626 -0.0346 -0.0824 0.0065  621 HOH A 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   3   HIS HIS 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 
# 
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 
B 2 ZN  1   262 1   ZN  ZN  A . 
C 3 E50 1   263 1   E50 E50 A . 
D 4 BCN 1   264 1   BCN BCN A . 
E 5 DMS 1   265 1   DMS DMS A . 
F 5 DMS 1   266 2   DMS DMS A . 
G 6 HOH 1   126 126 HOH HOH A . 
G 6 HOH 2   267 267 HOH HOH A . 
G 6 HOH 3   268 268 HOH HOH A . 
G 6 HOH 4   269 269 HOH HOH A . 
G 6 HOH 5   270 270 HOH HOH A . 
G 6 HOH 6   271 271 HOH HOH A . 
G 6 HOH 7   272 272 HOH HOH A . 
G 6 HOH 8   273 273 HOH HOH A . 
G 6 HOH 9   274 274 HOH HOH A . 
G 6 HOH 10  275 275 HOH HOH A . 
G 6 HOH 11  276 276 HOH HOH A . 
G 6 HOH 12  277 277 HOH HOH A . 
G 6 HOH 13  278 278 HOH HOH A . 
G 6 HOH 14  279 279 HOH HOH A . 
G 6 HOH 15  280 280 HOH HOH A . 
G 6 HOH 16  281 281 HOH HOH A . 
G 6 HOH 17  282 282 HOH HOH A . 
G 6 HOH 18  283 283 HOH HOH A . 
G 6 HOH 19  284 284 HOH HOH A . 
G 6 HOH 20  285 285 HOH HOH A . 
G 6 HOH 21  286 286 HOH HOH A . 
G 6 HOH 22  287 287 HOH HOH A . 
G 6 HOH 23  288 288 HOH HOH A . 
G 6 HOH 24  289 289 HOH HOH A . 
G 6 HOH 25  290 290 HOH HOH A . 
G 6 HOH 26  291 291 HOH HOH A . 
G 6 HOH 27  292 292 HOH HOH A . 
G 6 HOH 28  293 293 HOH HOH A . 
G 6 HOH 29  294 294 HOH HOH A . 
G 6 HOH 30  295 295 HOH HOH A . 
G 6 HOH 31  296 296 HOH HOH A . 
G 6 HOH 32  297 297 HOH HOH A . 
G 6 HOH 33  298 298 HOH HOH A . 
G 6 HOH 34  299 299 HOH HOH A . 
G 6 HOH 35  300 300 HOH HOH A . 
G 6 HOH 36  301 301 HOH HOH A . 
G 6 HOH 37  302 302 HOH HOH A . 
G 6 HOH 38  303 303 HOH HOH A . 
G 6 HOH 39  304 304 HOH HOH A . 
G 6 HOH 40  305 305 HOH HOH A . 
G 6 HOH 41  306 306 HOH HOH A . 
G 6 HOH 42  307 307 HOH HOH A . 
G 6 HOH 43  308 308 HOH HOH A . 
G 6 HOH 44  309 309 HOH HOH A . 
G 6 HOH 45  310 310 HOH HOH A . 
G 6 HOH 46  311 311 HOH HOH A . 
G 6 HOH 47  312 312 HOH HOH A . 
G 6 HOH 48  313 313 HOH HOH A . 
G 6 HOH 49  314 314 HOH HOH A . 
G 6 HOH 50  315 315 HOH HOH A . 
G 6 HOH 51  316 316 HOH HOH A . 
G 6 HOH 52  317 317 HOH HOH A . 
G 6 HOH 53  318 318 HOH HOH A . 
G 6 HOH 54  319 319 HOH HOH A . 
G 6 HOH 55  320 320 HOH HOH A . 
G 6 HOH 56  321 321 HOH HOH A . 
G 6 HOH 57  322 322 HOH HOH A . 
G 6 HOH 58  323 323 HOH HOH A . 
G 6 HOH 59  324 324 HOH HOH A . 
G 6 HOH 60  325 325 HOH HOH A . 
G 6 HOH 61  326 326 HOH HOH A . 
G 6 HOH 62  327 327 HOH HOH A . 
G 6 HOH 63  328 328 HOH HOH A . 
G 6 HOH 64  329 329 HOH HOH A . 
G 6 HOH 65  330 330 HOH HOH A . 
G 6 HOH 66  331 331 HOH HOH A . 
G 6 HOH 67  332 332 HOH HOH A . 
G 6 HOH 68  333 333 HOH HOH A . 
G 6 HOH 69  334 334 HOH HOH A . 
G 6 HOH 70  335 335 HOH HOH A . 
G 6 HOH 71  336 336 HOH HOH A . 
G 6 HOH 72  337 337 HOH HOH A . 
G 6 HOH 73  338 338 HOH HOH A . 
G 6 HOH 74  339 339 HOH HOH A . 
G 6 HOH 75  340 340 HOH HOH A . 
G 6 HOH 76  341 341 HOH HOH A . 
G 6 HOH 77  342 342 HOH HOH A . 
G 6 HOH 78  343 343 HOH HOH A . 
G 6 HOH 79  344 344 HOH HOH A . 
G 6 HOH 80  345 345 HOH HOH A . 
G 6 HOH 81  346 346 HOH HOH A . 
G 6 HOH 82  347 347 HOH HOH A . 
G 6 HOH 83  348 348 HOH HOH A . 
G 6 HOH 84  349 349 HOH HOH A . 
G 6 HOH 85  350 350 HOH HOH A . 
G 6 HOH 86  351 351 HOH HOH A . 
G 6 HOH 87  352 352 HOH HOH A . 
G 6 HOH 88  353 353 HOH HOH A . 
G 6 HOH 89  354 354 HOH HOH A . 
G 6 HOH 90  355 355 HOH HOH A . 
G 6 HOH 91  356 356 HOH HOH A . 
G 6 HOH 92  357 1   HOH HOH A . 
G 6 HOH 93  358 2   HOH HOH A . 
G 6 HOH 94  359 3   HOH HOH A . 
G 6 HOH 95  360 4   HOH HOH A . 
G 6 HOH 96  361 5   HOH HOH A . 
G 6 HOH 97  362 6   HOH HOH A . 
G 6 HOH 98  363 7   HOH HOH A . 
G 6 HOH 99  364 8   HOH HOH A . 
G 6 HOH 100 365 9   HOH HOH A . 
G 6 HOH 101 366 10  HOH HOH A . 
G 6 HOH 102 367 11  HOH HOH A . 
G 6 HOH 103 368 12  HOH HOH A . 
G 6 HOH 104 369 13  HOH HOH A . 
G 6 HOH 105 370 14  HOH HOH A . 
G 6 HOH 106 371 15  HOH HOH A . 
G 6 HOH 107 372 16  HOH HOH A . 
G 6 HOH 108 373 17  HOH HOH A . 
G 6 HOH 109 374 18  HOH HOH A . 
G 6 HOH 110 375 19  HOH HOH A . 
G 6 HOH 111 376 20  HOH HOH A . 
G 6 HOH 112 377 21  HOH HOH A . 
G 6 HOH 113 378 22  HOH HOH A . 
G 6 HOH 114 379 23  HOH HOH A . 
G 6 HOH 115 380 24  HOH HOH A . 
G 6 HOH 116 381 25  HOH HOH A . 
G 6 HOH 117 382 26  HOH HOH A . 
G 6 HOH 118 383 27  HOH HOH A . 
G 6 HOH 119 384 28  HOH HOH A . 
G 6 HOH 120 385 29  HOH HOH A . 
G 6 HOH 121 386 30  HOH HOH A . 
G 6 HOH 122 387 31  HOH HOH A . 
G 6 HOH 123 388 32  HOH HOH A . 
G 6 HOH 124 389 33  HOH HOH A . 
G 6 HOH 125 390 34  HOH HOH A . 
G 6 HOH 126 391 35  HOH HOH A . 
G 6 HOH 127 392 36  HOH HOH A . 
G 6 HOH 128 393 37  HOH HOH A . 
G 6 HOH 129 394 38  HOH HOH A . 
G 6 HOH 130 395 39  HOH HOH A . 
G 6 HOH 131 396 40  HOH HOH A . 
G 6 HOH 132 397 41  HOH HOH A . 
G 6 HOH 133 398 42  HOH HOH A . 
G 6 HOH 134 399 43  HOH HOH A . 
G 6 HOH 135 400 44  HOH HOH A . 
G 6 HOH 136 401 45  HOH HOH A . 
G 6 HOH 137 402 46  HOH HOH A . 
G 6 HOH 138 403 47  HOH HOH A . 
G 6 HOH 139 404 48  HOH HOH A . 
G 6 HOH 140 405 49  HOH HOH A . 
G 6 HOH 141 406 50  HOH HOH A . 
G 6 HOH 142 407 51  HOH HOH A . 
G 6 HOH 143 408 52  HOH HOH A . 
G 6 HOH 144 409 53  HOH HOH A . 
G 6 HOH 145 410 54  HOH HOH A . 
G 6 HOH 146 411 55  HOH HOH A . 
G 6 HOH 147 412 56  HOH HOH A . 
G 6 HOH 148 413 57  HOH HOH A . 
G 6 HOH 149 414 58  HOH HOH A . 
G 6 HOH 150 415 59  HOH HOH A . 
G 6 HOH 151 416 60  HOH HOH A . 
G 6 HOH 152 417 61  HOH HOH A . 
G 6 HOH 153 418 62  HOH HOH A . 
G 6 HOH 154 419 63  HOH HOH A . 
G 6 HOH 155 420 64  HOH HOH A . 
G 6 HOH 156 421 65  HOH HOH A . 
G 6 HOH 157 422 66  HOH HOH A . 
G 6 HOH 158 423 67  HOH HOH A . 
G 6 HOH 159 424 68  HOH HOH A . 
G 6 HOH 160 425 69  HOH HOH A . 
G 6 HOH 161 426 70  HOH HOH A . 
G 6 HOH 162 427 71  HOH HOH A . 
G 6 HOH 163 428 72  HOH HOH A . 
G 6 HOH 164 429 73  HOH HOH A . 
G 6 HOH 165 430 74  HOH HOH A . 
G 6 HOH 166 431 75  HOH HOH A . 
G 6 HOH 167 432 76  HOH HOH A . 
G 6 HOH 168 433 77  HOH HOH A . 
G 6 HOH 169 434 78  HOH HOH A . 
G 6 HOH 170 435 79  HOH HOH A . 
G 6 HOH 171 436 80  HOH HOH A . 
G 6 HOH 172 437 81  HOH HOH A . 
G 6 HOH 173 438 82  HOH HOH A . 
G 6 HOH 174 439 83  HOH HOH A . 
G 6 HOH 175 440 84  HOH HOH A . 
G 6 HOH 176 441 85  HOH HOH A . 
G 6 HOH 177 442 86  HOH HOH A . 
G 6 HOH 178 443 87  HOH HOH A . 
G 6 HOH 179 444 88  HOH HOH A . 
G 6 HOH 180 445 89  HOH HOH A . 
G 6 HOH 181 446 90  HOH HOH A . 
G 6 HOH 182 447 91  HOH HOH A . 
G 6 HOH 183 448 92  HOH HOH A . 
G 6 HOH 184 449 93  HOH HOH A . 
G 6 HOH 185 450 94  HOH HOH A . 
G 6 HOH 186 451 95  HOH HOH A . 
G 6 HOH 187 452 96  HOH HOH A . 
G 6 HOH 188 453 97  HOH HOH A . 
G 6 HOH 189 454 98  HOH HOH A . 
G 6 HOH 190 455 99  HOH HOH A . 
G 6 HOH 191 456 100 HOH HOH A . 
G 6 HOH 192 457 101 HOH HOH A . 
G 6 HOH 193 458 102 HOH HOH A . 
G 6 HOH 194 459 103 HOH HOH A . 
G 6 HOH 195 460 104 HOH HOH A . 
G 6 HOH 196 461 105 HOH HOH A . 
G 6 HOH 197 462 106 HOH HOH A . 
G 6 HOH 198 463 107 HOH HOH A . 
G 6 HOH 199 464 108 HOH HOH A . 
G 6 HOH 200 465 109 HOH HOH A . 
G 6 HOH 201 466 110 HOH HOH A . 
G 6 HOH 202 467 111 HOH HOH A . 
G 6 HOH 203 468 112 HOH HOH A . 
G 6 HOH 204 469 113 HOH HOH A . 
G 6 HOH 205 470 114 HOH HOH A . 
G 6 HOH 206 471 115 HOH HOH A . 
G 6 HOH 207 472 116 HOH HOH A . 
G 6 HOH 208 473 117 HOH HOH A . 
G 6 HOH 209 474 118 HOH HOH A . 
G 6 HOH 210 475 119 HOH HOH A . 
G 6 HOH 211 476 120 HOH HOH A . 
G 6 HOH 212 477 121 HOH HOH A . 
G 6 HOH 213 478 122 HOH HOH A . 
G 6 HOH 214 479 123 HOH HOH A . 
G 6 HOH 215 480 124 HOH HOH A . 
G 6 HOH 216 481 125 HOH HOH A . 
G 6 HOH 217 482 127 HOH HOH A . 
G 6 HOH 218 483 128 HOH HOH A . 
G 6 HOH 219 484 129 HOH HOH A . 
G 6 HOH 220 485 130 HOH HOH A . 
G 6 HOH 221 486 131 HOH HOH A . 
G 6 HOH 222 487 132 HOH HOH A . 
G 6 HOH 223 488 133 HOH HOH A . 
G 6 HOH 224 489 134 HOH HOH A . 
G 6 HOH 225 490 135 HOH HOH A . 
G 6 HOH 226 491 136 HOH HOH A . 
G 6 HOH 227 492 137 HOH HOH A . 
G 6 HOH 228 493 138 HOH HOH A . 
G 6 HOH 229 494 139 HOH HOH A . 
G 6 HOH 230 495 140 HOH HOH A . 
G 6 HOH 231 496 141 HOH HOH A . 
G 6 HOH 232 497 142 HOH HOH A . 
G 6 HOH 233 498 143 HOH HOH A . 
G 6 HOH 234 499 144 HOH HOH A . 
G 6 HOH 235 500 145 HOH HOH A . 
G 6 HOH 236 501 146 HOH HOH A . 
G 6 HOH 237 502 147 HOH HOH A . 
G 6 HOH 238 503 148 HOH HOH A . 
G 6 HOH 239 504 149 HOH HOH A . 
G 6 HOH 240 505 150 HOH HOH A . 
G 6 HOH 241 506 151 HOH HOH A . 
G 6 HOH 242 507 152 HOH HOH A . 
G 6 HOH 243 508 153 HOH HOH A . 
G 6 HOH 244 509 154 HOH HOH A . 
G 6 HOH 245 510 155 HOH HOH A . 
G 6 HOH 246 511 156 HOH HOH A . 
G 6 HOH 247 512 157 HOH HOH A . 
G 6 HOH 248 513 158 HOH HOH A . 
G 6 HOH 249 514 159 HOH HOH A . 
G 6 HOH 250 515 160 HOH HOH A . 
G 6 HOH 251 516 161 HOH HOH A . 
G 6 HOH 252 517 162 HOH HOH A . 
G 6 HOH 253 518 163 HOH HOH A . 
G 6 HOH 254 519 164 HOH HOH A . 
G 6 HOH 255 520 165 HOH HOH A . 
G 6 HOH 256 521 166 HOH HOH A . 
G 6 HOH 257 522 167 HOH HOH A . 
G 6 HOH 258 523 168 HOH HOH A . 
G 6 HOH 259 524 169 HOH HOH A . 
G 6 HOH 260 525 170 HOH HOH A . 
G 6 HOH 261 526 171 HOH HOH A . 
G 6 HOH 262 527 172 HOH HOH A . 
G 6 HOH 263 528 173 HOH HOH A . 
G 6 HOH 264 529 174 HOH HOH A . 
G 6 HOH 265 530 175 HOH HOH A . 
G 6 HOH 266 531 176 HOH HOH A . 
G 6 HOH 267 532 177 HOH HOH A . 
G 6 HOH 268 533 178 HOH HOH A . 
G 6 HOH 269 534 179 HOH HOH A . 
G 6 HOH 270 535 180 HOH HOH A . 
G 6 HOH 271 536 181 HOH HOH A . 
G 6 HOH 272 537 182 HOH HOH A . 
G 6 HOH 273 538 183 HOH HOH A . 
G 6 HOH 274 539 184 HOH HOH A . 
G 6 HOH 275 540 185 HOH HOH A . 
G 6 HOH 276 541 186 HOH HOH A . 
G 6 HOH 277 542 187 HOH HOH A . 
G 6 HOH 278 543 188 HOH HOH A . 
G 6 HOH 279 544 189 HOH HOH A . 
G 6 HOH 280 545 190 HOH HOH A . 
G 6 HOH 281 546 191 HOH HOH A . 
G 6 HOH 282 547 192 HOH HOH A . 
G 6 HOH 283 548 193 HOH HOH A . 
G 6 HOH 284 549 194 HOH HOH A . 
G 6 HOH 285 550 195 HOH HOH A . 
G 6 HOH 286 551 196 HOH HOH A . 
G 6 HOH 287 552 197 HOH HOH A . 
G 6 HOH 288 553 198 HOH HOH A . 
G 6 HOH 289 554 199 HOH HOH A . 
G 6 HOH 290 555 200 HOH HOH A . 
G 6 HOH 291 556 201 HOH HOH A . 
G 6 HOH 292 557 202 HOH HOH A . 
G 6 HOH 293 558 203 HOH HOH A . 
G 6 HOH 294 559 204 HOH HOH A . 
G 6 HOH 295 560 205 HOH HOH A . 
G 6 HOH 296 561 206 HOH HOH A . 
G 6 HOH 297 562 207 HOH HOH A . 
G 6 HOH 298 563 208 HOH HOH A . 
G 6 HOH 299 564 209 HOH HOH A . 
G 6 HOH 300 565 210 HOH HOH A . 
G 6 HOH 301 566 211 HOH HOH A . 
G 6 HOH 302 567 212 HOH HOH A . 
G 6 HOH 303 568 213 HOH HOH A . 
G 6 HOH 304 569 214 HOH HOH A . 
G 6 HOH 305 570 215 HOH HOH A . 
G 6 HOH 306 571 216 HOH HOH A . 
G 6 HOH 307 572 217 HOH HOH A . 
G 6 HOH 308 573 218 HOH HOH A . 
G 6 HOH 309 574 219 HOH HOH A . 
G 6 HOH 310 575 220 HOH HOH A . 
G 6 HOH 311 576 221 HOH HOH A . 
G 6 HOH 312 577 222 HOH HOH A . 
G 6 HOH 313 578 223 HOH HOH A . 
G 6 HOH 314 579 224 HOH HOH A . 
G 6 HOH 315 580 225 HOH HOH A . 
G 6 HOH 316 581 226 HOH HOH A . 
G 6 HOH 317 582 227 HOH HOH A . 
G 6 HOH 318 583 228 HOH HOH A . 
G 6 HOH 319 584 229 HOH HOH A . 
G 6 HOH 320 585 230 HOH HOH A . 
G 6 HOH 321 586 231 HOH HOH A . 
G 6 HOH 322 587 232 HOH HOH A . 
G 6 HOH 323 588 233 HOH HOH A . 
G 6 HOH 324 589 234 HOH HOH A . 
G 6 HOH 325 590 235 HOH HOH A . 
G 6 HOH 326 591 236 HOH HOH A . 
G 6 HOH 327 592 237 HOH HOH A . 
G 6 HOH 328 593 238 HOH HOH A . 
G 6 HOH 329 594 239 HOH HOH A . 
G 6 HOH 330 595 240 HOH HOH A . 
G 6 HOH 331 596 241 HOH HOH A . 
G 6 HOH 332 597 242 HOH HOH A . 
G 6 HOH 333 598 243 HOH HOH A . 
G 6 HOH 334 599 244 HOH HOH A . 
G 6 HOH 335 600 245 HOH HOH A . 
G 6 HOH 336 601 246 HOH HOH A . 
G 6 HOH 337 602 247 HOH HOH A . 
G 6 HOH 338 603 248 HOH HOH A . 
G 6 HOH 339 604 249 HOH HOH A . 
G 6 HOH 340 605 250 HOH HOH A . 
G 6 HOH 341 606 251 HOH HOH A . 
G 6 HOH 342 607 252 HOH HOH A . 
G 6 HOH 343 608 253 HOH HOH A . 
G 6 HOH 344 609 254 HOH HOH A . 
G 6 HOH 345 610 255 HOH HOH A . 
G 6 HOH 346 611 256 HOH HOH A . 
G 6 HOH 347 612 257 HOH HOH A . 
G 6 HOH 348 613 258 HOH HOH A . 
G 6 HOH 349 614 259 HOH HOH A . 
G 6 HOH 350 615 260 HOH HOH A . 
G 6 HOH 351 616 261 HOH HOH A . 
G 6 HOH 352 617 262 HOH HOH A . 
G 6 HOH 353 618 263 HOH HOH A . 
G 6 HOH 354 619 264 HOH HOH A . 
G 6 HOH 355 620 265 HOH HOH A . 
G 6 HOH 356 621 266 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 ? B ZN . ? A ZN 262 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 111.5 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.1  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N23 ? C E50 .   ? A E50 263 ? 1_555 108.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N23 ? C E50 .   ? A E50 263 ? 1_555 115.9 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N23 ? C E50 .   ? A E50 263 ? 1_555 116.8 ? 
# 
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 2012-04-11 
2 'Structure model' 1 1 2012-05-16 
3 'Structure model' 1 2 2017-11-15 
4 'Structure model' 1 3 2023-09-13 
# 
_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' 'Database references'    
2 3 'Structure model' 'Database references'    
3 4 'Structure model' 'Data collection'        
4 4 'Structure model' 'Database references'    
5 4 'Structure model' 'Derived calculations'   
6 4 '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 3 'Structure model' pdbx_database_related         
2 4 'Structure model' chem_comp_atom                
3 4 'Structure model' chem_comp_bond                
4 4 'Structure model' database_2                    
5 4 'Structure model' diffrn_source                 
6 4 'Structure model' pdbx_initial_refinement_model 
7 4 'Structure model' pdbx_struct_conn_angle        
8 4 'Structure model' struct_conn                   
9 4 '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  3 'Structure model' '_pdbx_database_related.db_name'              
2  4 'Structure model' '_database_2.pdbx_DOI'                        
3  4 'Structure model' '_database_2.pdbx_database_accession'         
4  4 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
8  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
9  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
10 4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
11 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
12 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
13 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
14 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
15 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
16 4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
17 4 'Structure model' '_pdbx_struct_conn_angle.value'               
18 4 'Structure model' '_struct_conn.pdbx_dist_value'                
19 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
20 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
21 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
22 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
23 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
24 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
25 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
26 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
27 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
28 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
29 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
30 4 'Structure model' '_struct_site.pdbx_auth_asym_id'              
31 4 'Structure model' '_struct_site.pdbx_auth_comp_id'              
32 4 '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      .      ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk    refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 1 
MOSFLM      .      ?               package 'Andrew G.W. Leslie' andrew@mrc-lmb.cam.ac.uk 'data reduction'  
http://www.mrc-lmb.cam.ac.uk/harry/mosflm/   ?          ? 2 
SCALA       3.3.16 2010/01/06      other   'Phil R. Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/scala.html   Fortran_77 ? 3 
PDB_EXTRACT 3.006  'June 11, 2008' package PDB                  help@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/    C++        ? 4 
DNA         .      ?               ?       ?                    ?                        'data collection' ? ?          ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   CE 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    159 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    350 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 C A VAL 68  ? B O A VAL 68  ? B 1.377 1.229 0.148 0.019 N 
2 1 C A GLN 74  ? ? N A ASP 75  ? B 1.494 1.336 0.158 0.023 Y 
3 1 C A THR 125 ? ? N A LYS 127 ? B 1.583 1.336 0.247 0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A GLN 74  ? ? C A GLN 74  ? ? N  A ASP 75  ? B 98.88  117.20 -18.32 2.20 Y 
2 1 O  A GLN 74  ? ? C A GLN 74  ? ? N  A ASP 75  ? B 138.27 122.70 15.57  1.60 Y 
3 1 C  A LEU 185 ? B N A PRO 186 ? B CA A PRO 186 ? B 129.11 119.30 9.81   1.50 Y 
# 
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 ASN A 11  ? ? -166.17 3.15    
2  1 ARG A 27  ? ? -145.71 57.65   
3  1 LYS A 76  ? A -105.71 -87.17  
4  1 ALA A 77  ? B 65.41   66.66   
5  1 GLU A 106 ? ? -92.42  -60.48  
6  1 LYS A 111 ? ? 75.36   -4.02   
7  1 PHE A 176 ? A -155.95 79.93   
8  1 PHE A 176 ? B -153.40 82.46   
9  1 PRO A 186 ? A -58.39  -177.97 
10 1 PRO A 237 ? B -47.98  153.25  
11 1 ASN A 244 ? ? -94.26  45.89   
12 1 LYS A 252 ? ? 55.08   -142.42 
# 
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 
# 
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 
E50 N1   N  Y N 122 
E50 C2   C  Y N 123 
E50 N3   N  Y N 124 
E50 C4   C  Y N 125 
E50 C5   C  Y N 126 
E50 C6   C  Y N 127 
E50 S7   S  N N 128 
E50 C8   C  N N 129 
E50 C9   C  N N 130 
E50 O10  O  N N 131 
E50 C11  C  N N 132 
E50 C12  C  N N 133 
E50 C13  C  Y N 134 
E50 C14  C  Y N 135 
E50 C15  C  Y N 136 
E50 C16  C  Y N 137 
E50 C17  C  Y N 138 
E50 C18  C  Y N 139 
E50 S19  S  N N 140 
E50 O20  O  N N 141 
E50 CL21 CL N N 142 
E50 O22  O  N N 143 
E50 N23  N  N N 144 
E50 H4   H  N N 145 
E50 H6   H  N N 146 
E50 H8   H  N N 147 
E50 H8A  H  N N 148 
E50 H11  H  N N 149 
E50 H11A H  N N 150 
E50 H12  H  N N 151 
E50 H12A H  N N 152 
E50 H12B H  N N 153 
E50 H14  H  N N 154 
E50 H17  H  N N 155 
E50 H18  H  N N 156 
E50 HN23 H  N N 157 
E50 HN2A H  N N 158 
GLN N    N  N N 159 
GLN CA   C  N S 160 
GLN C    C  N N 161 
GLN O    O  N N 162 
GLN CB   C  N N 163 
GLN CG   C  N N 164 
GLN CD   C  N N 165 
GLN OE1  O  N N 166 
GLN NE2  N  N N 167 
GLN OXT  O  N N 168 
GLN H    H  N N 169 
GLN H2   H  N N 170 
GLN HA   H  N N 171 
GLN HB2  H  N N 172 
GLN HB3  H  N N 173 
GLN HG2  H  N N 174 
GLN HG3  H  N N 175 
GLN HE21 H  N N 176 
GLN HE22 H  N N 177 
GLN HXT  H  N N 178 
GLU N    N  N N 179 
GLU CA   C  N S 180 
GLU C    C  N N 181 
GLU O    O  N N 182 
GLU CB   C  N N 183 
GLU CG   C  N N 184 
GLU CD   C  N N 185 
GLU OE1  O  N N 186 
GLU OE2  O  N N 187 
GLU OXT  O  N N 188 
GLU H    H  N N 189 
GLU H2   H  N N 190 
GLU HA   H  N N 191 
GLU HB2  H  N N 192 
GLU HB3  H  N N 193 
GLU HG2  H  N N 194 
GLU HG3  H  N N 195 
GLU HE2  H  N N 196 
GLU HXT  H  N N 197 
GLY N    N  N N 198 
GLY CA   C  N N 199 
GLY C    C  N N 200 
GLY O    O  N N 201 
GLY OXT  O  N N 202 
GLY H    H  N N 203 
GLY H2   H  N N 204 
GLY HA2  H  N N 205 
GLY HA3  H  N N 206 
GLY HXT  H  N N 207 
HIS N    N  N N 208 
HIS CA   C  N S 209 
HIS C    C  N N 210 
HIS O    O  N N 211 
HIS CB   C  N N 212 
HIS CG   C  Y N 213 
HIS ND1  N  Y N 214 
HIS CD2  C  Y N 215 
HIS CE1  C  Y N 216 
HIS NE2  N  Y N 217 
HIS OXT  O  N N 218 
HIS H    H  N N 219 
HIS H2   H  N N 220 
HIS HA   H  N N 221 
HIS HB2  H  N N 222 
HIS HB3  H  N N 223 
HIS HD1  H  N N 224 
HIS HD2  H  N N 225 
HIS HE1  H  N N 226 
HIS HE2  H  N N 227 
HIS HXT  H  N N 228 
HOH O    O  N N 229 
HOH H1   H  N N 230 
HOH H2   H  N N 231 
ILE N    N  N N 232 
ILE CA   C  N S 233 
ILE C    C  N N 234 
ILE O    O  N N 235 
ILE CB   C  N S 236 
ILE CG1  C  N N 237 
ILE CG2  C  N N 238 
ILE CD1  C  N N 239 
ILE OXT  O  N N 240 
ILE H    H  N N 241 
ILE H2   H  N N 242 
ILE HA   H  N N 243 
ILE HB   H  N N 244 
ILE HG12 H  N N 245 
ILE HG13 H  N N 246 
ILE HG21 H  N N 247 
ILE HG22 H  N N 248 
ILE HG23 H  N N 249 
ILE HD11 H  N N 250 
ILE HD12 H  N N 251 
ILE HD13 H  N N 252 
ILE HXT  H  N N 253 
LEU N    N  N N 254 
LEU CA   C  N S 255 
LEU C    C  N N 256 
LEU O    O  N N 257 
LEU CB   C  N N 258 
LEU CG   C  N N 259 
LEU CD1  C  N N 260 
LEU CD2  C  N N 261 
LEU OXT  O  N N 262 
LEU H    H  N N 263 
LEU H2   H  N N 264 
LEU HA   H  N N 265 
LEU HB2  H  N N 266 
LEU HB3  H  N N 267 
LEU HG   H  N N 268 
LEU HD11 H  N N 269 
LEU HD12 H  N N 270 
LEU HD13 H  N N 271 
LEU HD21 H  N N 272 
LEU HD22 H  N N 273 
LEU HD23 H  N N 274 
LEU HXT  H  N N 275 
LYS N    N  N N 276 
LYS CA   C  N S 277 
LYS C    C  N N 278 
LYS O    O  N N 279 
LYS CB   C  N N 280 
LYS CG   C  N N 281 
LYS CD   C  N N 282 
LYS CE   C  N N 283 
LYS NZ   N  N N 284 
LYS OXT  O  N N 285 
LYS H    H  N N 286 
LYS H2   H  N N 287 
LYS HA   H  N N 288 
LYS HB2  H  N N 289 
LYS HB3  H  N N 290 
LYS HG2  H  N N 291 
LYS HG3  H  N N 292 
LYS HD2  H  N N 293 
LYS HD3  H  N N 294 
LYS HE2  H  N N 295 
LYS HE3  H  N N 296 
LYS HZ1  H  N N 297 
LYS HZ2  H  N N 298 
LYS HZ3  H  N N 299 
LYS HXT  H  N N 300 
MET N    N  N N 301 
MET CA   C  N S 302 
MET C    C  N N 303 
MET O    O  N N 304 
MET CB   C  N N 305 
MET CG   C  N N 306 
MET SD   S  N N 307 
MET CE   C  N N 308 
MET OXT  O  N N 309 
MET H    H  N N 310 
MET H2   H  N N 311 
MET HA   H  N N 312 
MET HB2  H  N N 313 
MET HB3  H  N N 314 
MET HG2  H  N N 315 
MET HG3  H  N N 316 
MET HE1  H  N N 317 
MET HE2  H  N N 318 
MET HE3  H  N N 319 
MET HXT  H  N N 320 
PHE N    N  N N 321 
PHE CA   C  N S 322 
PHE C    C  N N 323 
PHE O    O  N N 324 
PHE CB   C  N N 325 
PHE CG   C  Y N 326 
PHE CD1  C  Y N 327 
PHE CD2  C  Y N 328 
PHE CE1  C  Y N 329 
PHE CE2  C  Y N 330 
PHE CZ   C  Y N 331 
PHE OXT  O  N N 332 
PHE H    H  N N 333 
PHE H2   H  N N 334 
PHE HA   H  N N 335 
PHE HB2  H  N N 336 
PHE HB3  H  N N 337 
PHE HD1  H  N N 338 
PHE HD2  H  N N 339 
PHE HE1  H  N N 340 
PHE HE2  H  N N 341 
PHE HZ   H  N N 342 
PHE HXT  H  N N 343 
PRO N    N  N N 344 
PRO CA   C  N S 345 
PRO C    C  N N 346 
PRO O    O  N N 347 
PRO CB   C  N N 348 
PRO CG   C  N N 349 
PRO CD   C  N N 350 
PRO OXT  O  N N 351 
PRO H    H  N N 352 
PRO HA   H  N N 353 
PRO HB2  H  N N 354 
PRO HB3  H  N N 355 
PRO HG2  H  N N 356 
PRO HG3  H  N N 357 
PRO HD2  H  N N 358 
PRO HD3  H  N N 359 
PRO HXT  H  N N 360 
SER N    N  N N 361 
SER CA   C  N S 362 
SER C    C  N N 363 
SER O    O  N N 364 
SER CB   C  N N 365 
SER OG   O  N N 366 
SER OXT  O  N N 367 
SER H    H  N N 368 
SER H2   H  N N 369 
SER HA   H  N N 370 
SER HB2  H  N N 371 
SER HB3  H  N N 372 
SER HG   H  N N 373 
SER HXT  H  N N 374 
THR N    N  N N 375 
THR CA   C  N S 376 
THR C    C  N N 377 
THR O    O  N N 378 
THR CB   C  N R 379 
THR OG1  O  N N 380 
THR CG2  C  N N 381 
THR OXT  O  N N 382 
THR H    H  N N 383 
THR H2   H  N N 384 
THR HA   H  N N 385 
THR HB   H  N N 386 
THR HG1  H  N N 387 
THR HG21 H  N N 388 
THR HG22 H  N N 389 
THR HG23 H  N N 390 
THR HXT  H  N N 391 
TRP N    N  N N 392 
TRP CA   C  N S 393 
TRP C    C  N N 394 
TRP O    O  N N 395 
TRP CB   C  N N 396 
TRP CG   C  Y N 397 
TRP CD1  C  Y N 398 
TRP CD2  C  Y N 399 
TRP NE1  N  Y N 400 
TRP CE2  C  Y N 401 
TRP CE3  C  Y N 402 
TRP CZ2  C  Y N 403 
TRP CZ3  C  Y N 404 
TRP CH2  C  Y N 405 
TRP OXT  O  N N 406 
TRP H    H  N N 407 
TRP H2   H  N N 408 
TRP HA   H  N N 409 
TRP HB2  H  N N 410 
TRP HB3  H  N N 411 
TRP HD1  H  N N 412 
TRP HE1  H  N N 413 
TRP HE3  H  N N 414 
TRP HZ2  H  N N 415 
TRP HZ3  H  N N 416 
TRP HH2  H  N N 417 
TRP HXT  H  N N 418 
TYR N    N  N N 419 
TYR CA   C  N S 420 
TYR C    C  N N 421 
TYR O    O  N N 422 
TYR CB   C  N N 423 
TYR CG   C  Y N 424 
TYR CD1  C  Y N 425 
TYR CD2  C  Y N 426 
TYR CE1  C  Y N 427 
TYR CE2  C  Y N 428 
TYR CZ   C  Y N 429 
TYR OH   O  N N 430 
TYR OXT  O  N N 431 
TYR H    H  N N 432 
TYR H2   H  N N 433 
TYR HA   H  N N 434 
TYR HB2  H  N N 435 
TYR HB3  H  N N 436 
TYR HD1  H  N N 437 
TYR HD2  H  N N 438 
TYR HE1  H  N N 439 
TYR HE2  H  N N 440 
TYR HH   H  N N 441 
TYR HXT  H  N N 442 
VAL N    N  N N 443 
VAL CA   C  N S 444 
VAL C    C  N N 445 
VAL O    O  N N 446 
VAL CB   C  N N 447 
VAL CG1  C  N N 448 
VAL CG2  C  N N 449 
VAL OXT  O  N N 450 
VAL H    H  N N 451 
VAL H2   H  N N 452 
VAL HA   H  N N 453 
VAL HB   H  N N 454 
VAL HG11 H  N N 455 
VAL HG12 H  N N 456 
VAL HG13 H  N N 457 
VAL HG21 H  N N 458 
VAL HG22 H  N N 459 
VAL HG23 H  N N 460 
VAL HXT  H  N N 461 
ZN  ZN   ZN N N 462 
# 
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 
E50 N1  C6   doub Y N 115 
E50 N1  C2   sing Y N 116 
E50 S7  C2   sing N N 117 
E50 C2  N3   doub Y N 118 
E50 N3  C4   sing Y N 119 
E50 C5  C4   doub Y N 120 
E50 C4  H4   sing N N 121 
E50 C6  C5   sing Y N 122 
E50 C5  C11  sing N N 123 
E50 C6  H6   sing N N 124 
E50 S7  C8   sing N N 125 
E50 C8  C9   sing N N 126 
E50 C8  H8   sing N N 127 
E50 C8  H8A  sing N N 128 
E50 O10 C9   doub N N 129 
E50 C9  C13  sing N N 130 
E50 C11 C12  sing N N 131 
E50 C11 H11  sing N N 132 
E50 C11 H11A sing N N 133 
E50 C12 H12  sing N N 134 
E50 C12 H12A sing N N 135 
E50 C12 H12B sing N N 136 
E50 C13 C18  doub Y N 137 
E50 C13 C14  sing Y N 138 
E50 C14 C15  doub Y N 139 
E50 C14 H14  sing N N 140 
E50 C15 C16  sing Y N 141 
E50 C15 S19  sing N N 142 
E50 C17 C16  doub Y N 143 
E50 C16 CL21 sing N N 144 
E50 C18 C17  sing Y N 145 
E50 C17 H17  sing N N 146 
E50 C18 H18  sing N N 147 
E50 N23 S19  sing N N 148 
E50 O22 S19  doub N N 149 
E50 S19 O20  doub N N 150 
E50 N23 HN23 sing N N 151 
E50 N23 HN2A sing N N 152 
GLN N   CA   sing N N 153 
GLN N   H    sing N N 154 
GLN N   H2   sing N N 155 
GLN CA  C    sing N N 156 
GLN CA  CB   sing N N 157 
GLN CA  HA   sing N N 158 
GLN C   O    doub N N 159 
GLN C   OXT  sing N N 160 
GLN CB  CG   sing N N 161 
GLN CB  HB2  sing N N 162 
GLN CB  HB3  sing N N 163 
GLN CG  CD   sing N N 164 
GLN CG  HG2  sing N N 165 
GLN CG  HG3  sing N N 166 
GLN CD  OE1  doub N N 167 
GLN CD  NE2  sing N N 168 
GLN NE2 HE21 sing N N 169 
GLN NE2 HE22 sing N N 170 
GLN OXT HXT  sing N N 171 
GLU N   CA   sing N N 172 
GLU N   H    sing N N 173 
GLU N   H2   sing N N 174 
GLU CA  C    sing N N 175 
GLU CA  CB   sing N N 176 
GLU CA  HA   sing N N 177 
GLU C   O    doub N N 178 
GLU C   OXT  sing N N 179 
GLU CB  CG   sing N N 180 
GLU CB  HB2  sing N N 181 
GLU CB  HB3  sing N N 182 
GLU CG  CD   sing N N 183 
GLU CG  HG2  sing N N 184 
GLU CG  HG3  sing N N 185 
GLU CD  OE1  doub N N 186 
GLU CD  OE2  sing N N 187 
GLU OE2 HE2  sing N N 188 
GLU OXT HXT  sing N N 189 
GLY N   CA   sing N N 190 
GLY N   H    sing N N 191 
GLY N   H2   sing N N 192 
GLY CA  C    sing N N 193 
GLY CA  HA2  sing N N 194 
GLY CA  HA3  sing N N 195 
GLY C   O    doub N N 196 
GLY C   OXT  sing N N 197 
GLY OXT HXT  sing N N 198 
HIS N   CA   sing N N 199 
HIS N   H    sing N N 200 
HIS N   H2   sing N N 201 
HIS CA  C    sing N N 202 
HIS CA  CB   sing N N 203 
HIS CA  HA   sing N N 204 
HIS C   O    doub N N 205 
HIS C   OXT  sing N N 206 
HIS CB  CG   sing N N 207 
HIS CB  HB2  sing N N 208 
HIS CB  HB3  sing N N 209 
HIS CG  ND1  sing Y N 210 
HIS CG  CD2  doub Y N 211 
HIS ND1 CE1  doub Y N 212 
HIS ND1 HD1  sing N N 213 
HIS CD2 NE2  sing Y N 214 
HIS CD2 HD2  sing N N 215 
HIS CE1 NE2  sing Y N 216 
HIS CE1 HE1  sing N N 217 
HIS NE2 HE2  sing N N 218 
HIS OXT HXT  sing N N 219 
HOH O   H1   sing N N 220 
HOH O   H2   sing N N 221 
ILE N   CA   sing N N 222 
ILE N   H    sing N N 223 
ILE N   H2   sing N N 224 
ILE CA  C    sing N N 225 
ILE CA  CB   sing N N 226 
ILE CA  HA   sing N N 227 
ILE C   O    doub N N 228 
ILE C   OXT  sing N N 229 
ILE CB  CG1  sing N N 230 
ILE CB  CG2  sing N N 231 
ILE CB  HB   sing N N 232 
ILE CG1 CD1  sing N N 233 
ILE CG1 HG12 sing N N 234 
ILE CG1 HG13 sing N N 235 
ILE CG2 HG21 sing N N 236 
ILE CG2 HG22 sing N N 237 
ILE CG2 HG23 sing N N 238 
ILE CD1 HD11 sing N N 239 
ILE CD1 HD12 sing N N 240 
ILE CD1 HD13 sing N N 241 
ILE OXT HXT  sing N N 242 
LEU N   CA   sing N N 243 
LEU N   H    sing N N 244 
LEU N   H2   sing N N 245 
LEU CA  C    sing N N 246 
LEU CA  CB   sing N N 247 
LEU CA  HA   sing N N 248 
LEU C   O    doub N N 249 
LEU C   OXT  sing N N 250 
LEU CB  CG   sing N N 251 
LEU CB  HB2  sing N N 252 
LEU CB  HB3  sing N N 253 
LEU CG  CD1  sing N N 254 
LEU CG  CD2  sing N N 255 
LEU CG  HG   sing N N 256 
LEU CD1 HD11 sing N N 257 
LEU CD1 HD12 sing N N 258 
LEU CD1 HD13 sing N N 259 
LEU CD2 HD21 sing N N 260 
LEU CD2 HD22 sing N N 261 
LEU CD2 HD23 sing N N 262 
LEU OXT HXT  sing N N 263 
LYS N   CA   sing N N 264 
LYS N   H    sing N N 265 
LYS N   H2   sing N N 266 
LYS CA  C    sing N N 267 
LYS CA  CB   sing N N 268 
LYS CA  HA   sing N N 269 
LYS C   O    doub N N 270 
LYS C   OXT  sing N N 271 
LYS CB  CG   sing N N 272 
LYS CB  HB2  sing N N 273 
LYS CB  HB3  sing N N 274 
LYS CG  CD   sing N N 275 
LYS CG  HG2  sing N N 276 
LYS CG  HG3  sing N N 277 
LYS CD  CE   sing N N 278 
LYS CD  HD2  sing N N 279 
LYS CD  HD3  sing N N 280 
LYS CE  NZ   sing N N 281 
LYS CE  HE2  sing N N 282 
LYS CE  HE3  sing N N 283 
LYS NZ  HZ1  sing N N 284 
LYS NZ  HZ2  sing N N 285 
LYS NZ  HZ3  sing N N 286 
LYS OXT HXT  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
PHE N   CA   sing N N 307 
PHE N   H    sing N N 308 
PHE N   H2   sing N N 309 
PHE CA  C    sing N N 310 
PHE CA  CB   sing N N 311 
PHE CA  HA   sing N N 312 
PHE C   O    doub N N 313 
PHE C   OXT  sing N N 314 
PHE CB  CG   sing N N 315 
PHE CB  HB2  sing N N 316 
PHE CB  HB3  sing N N 317 
PHE CG  CD1  doub Y N 318 
PHE CG  CD2  sing Y N 319 
PHE CD1 CE1  sing Y N 320 
PHE CD1 HD1  sing N N 321 
PHE CD2 CE2  doub Y N 322 
PHE CD2 HD2  sing N N 323 
PHE CE1 CZ   doub Y N 324 
PHE CE1 HE1  sing N N 325 
PHE CE2 CZ   sing Y N 326 
PHE CE2 HE2  sing N N 327 
PHE CZ  HZ   sing N N 328 
PHE OXT HXT  sing N N 329 
PRO N   CA   sing N N 330 
PRO N   CD   sing N N 331 
PRO N   H    sing N N 332 
PRO CA  C    sing N N 333 
PRO CA  CB   sing N N 334 
PRO CA  HA   sing N N 335 
PRO C   O    doub N N 336 
PRO C   OXT  sing N N 337 
PRO CB  CG   sing N N 338 
PRO CB  HB2  sing N N 339 
PRO CB  HB3  sing N N 340 
PRO CG  CD   sing N N 341 
PRO CG  HG2  sing N N 342 
PRO CG  HG3  sing N N 343 
PRO CD  HD2  sing N N 344 
PRO CD  HD3  sing N N 345 
PRO OXT HXT  sing N N 346 
SER N   CA   sing N N 347 
SER N   H    sing N N 348 
SER N   H2   sing N N 349 
SER CA  C    sing N N 350 
SER CA  CB   sing N N 351 
SER CA  HA   sing N N 352 
SER C   O    doub N N 353 
SER C   OXT  sing N N 354 
SER CB  OG   sing N N 355 
SER CB  HB2  sing N N 356 
SER CB  HB3  sing N N 357 
SER OG  HG   sing N N 358 
SER OXT HXT  sing N N 359 
THR N   CA   sing N N 360 
THR N   H    sing N N 361 
THR N   H2   sing N N 362 
THR CA  C    sing N N 363 
THR CA  CB   sing N N 364 
THR CA  HA   sing N N 365 
THR C   O    doub N N 366 
THR C   OXT  sing N N 367 
THR CB  OG1  sing N N 368 
THR CB  CG2  sing N N 369 
THR CB  HB   sing N N 370 
THR OG1 HG1  sing N N 371 
THR CG2 HG21 sing N N 372 
THR CG2 HG22 sing N N 373 
THR CG2 HG23 sing N N 374 
THR OXT HXT  sing N N 375 
TRP N   CA   sing N N 376 
TRP N   H    sing N N 377 
TRP N   H2   sing N N 378 
TRP CA  C    sing N N 379 
TRP CA  CB   sing N N 380 
TRP CA  HA   sing N N 381 
TRP C   O    doub N N 382 
TRP C   OXT  sing N N 383 
TRP CB  CG   sing N N 384 
TRP CB  HB2  sing N N 385 
TRP CB  HB3  sing N N 386 
TRP CG  CD1  doub Y N 387 
TRP CG  CD2  sing Y N 388 
TRP CD1 NE1  sing Y N 389 
TRP CD1 HD1  sing N N 390 
TRP CD2 CE2  doub Y N 391 
TRP CD2 CE3  sing Y N 392 
TRP NE1 CE2  sing Y N 393 
TRP NE1 HE1  sing N N 394 
TRP CE2 CZ2  sing Y N 395 
TRP CE3 CZ3  doub Y N 396 
TRP CE3 HE3  sing N N 397 
TRP CZ2 CH2  doub Y N 398 
TRP CZ2 HZ2  sing N N 399 
TRP CZ3 CH2  sing Y N 400 
TRP CZ3 HZ3  sing N N 401 
TRP CH2 HH2  sing N N 402 
TRP OXT HXT  sing N N 403 
TYR N   CA   sing N N 404 
TYR N   H    sing N N 405 
TYR N   H2   sing N N 406 
TYR CA  C    sing N N 407 
TYR CA  CB   sing N N 408 
TYR CA  HA   sing N N 409 
TYR C   O    doub N N 410 
TYR C   OXT  sing N N 411 
TYR CB  CG   sing N N 412 
TYR CB  HB2  sing N N 413 
TYR CB  HB3  sing N N 414 
TYR CG  CD1  doub Y N 415 
TYR CG  CD2  sing Y N 416 
TYR CD1 CE1  sing Y N 417 
TYR CD1 HD1  sing N N 418 
TYR CD2 CE2  doub Y N 419 
TYR CD2 HD2  sing N N 420 
TYR CE1 CZ   doub Y N 421 
TYR CE1 HE1  sing N N 422 
TYR CE2 CZ   sing Y N 423 
TYR CE2 HE2  sing N N 424 
TYR CZ  OH   sing N N 425 
TYR OH  HH   sing N N 426 
TYR OXT HXT  sing N N 427 
VAL N   CA   sing N N 428 
VAL N   H    sing N N 429 
VAL N   H2   sing N N 430 
VAL CA  C    sing N N 431 
VAL CA  CB   sing N N 432 
VAL CA  HA   sing N N 433 
VAL C   O    doub N N 434 
VAL C   OXT  sing N N 435 
VAL CB  CG1  sing N N 436 
VAL CB  CG2  sing N N 437 
VAL CB  HB   sing N N 438 
VAL CG1 HG11 sing N N 439 
VAL CG1 HG12 sing N N 440 
VAL CG1 HG13 sing N N 441 
VAL CG2 HG21 sing N N 442 
VAL CG2 HG22 sing N N 443 
VAL CG2 HG23 sing N N 444 
VAL OXT HXT  sing N N 445 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                               ZN  
3 '2-chloro-5-{[(5-ethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide' E50 
4 BICINE                                                                   BCN 
5 'DIMETHYL SULFOXIDE'                                                     DMS 
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          'PDB entry 3HLJ' 
# 
