data_3SBI
# 
_entry.id   3SBI 
# 
_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   3SBI         pdb_00003sbi 10.2210/pdb3sbi/pdb 
RCSB  RCSB066001   ?            ?                   
WWPDB D_1000066001 ?            ?                   
# 
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 3SAX 'human carbonic anhydrase II with 2-chloro-5-{[(5-ethyl-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 
# 
_pdbx_database_status.entry_id                        3SBI 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-06-05 
_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           3SBI 
_cell.length_a           42.348 
_cell.length_b           41.314 
_cell.length_c           72.240 
_cell.angle_alpha        90.000 
_cell.angle_beta         104.250 
_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                         3SBI 
_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 'DIMETHYL SULFOXIDE'                                   78.133    2   ?       ? ? ? 
4 non-polymer syn BICINE                                                 163.172   1   ?       ? ? ? 
5 non-polymer syn '4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' 309.364   1   ?       ? ? ? 
6 water       nat water                                                  18.015    320 ?       ? ? ? 
# 
_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              3SBI 
_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  
E90 non-polymer         . '4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' ? 'C12 H11 N3 O3 S2' 309.364 
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          3SBI 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   41.2 
_exptl_crystal.density_Matthews      2.1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.pH              9 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    '0.1M Na-bicine pH 9, 2M Na-malonate pH 7.55, VAPOR DIFFUSION, temperature 293K' 
_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                'Bent, vertically focussing mirrors' 
# 
_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                     3SBI 
_reflns.d_resolution_high            1.4 
_reflns.d_resolution_low             20.68 
_reflns.number_all                   ? 
_reflns.number_obs                   46467 
_reflns.pdbx_Rmerge_I_obs            0.043 
_reflns.pdbx_netI_over_sigmaI        25.200 
_reflns.pdbx_Rsym_value              0.043 
_reflns.pdbx_redundancy              6.000 
_reflns.percent_possible_obs         97.100 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.B_iso_Wilson_estimate        12.4 
_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_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 
1.40 1.48  ? 40332 ? 0.344 2.0  0.344 ? 6.00 ? 6675 95.70 1  1 
1.48 1.57  ? 37923 ? 0.236 3.1  0.236 ? 6.00 ? 6304 95.90 2  1 
1.57 1.67  ? 35727 ? 0.164 4.4  0.164 ? 6.00 ? 5941 96.70 3  1 
1.67 1.81  ? 33749 ? 0.111 6.6  0.111 ? 6.00 ? 5614 97.10 4  1 
1.81 1.98  ? 31000 ? 0.068 10.7 0.068 ? 6.00 ? 5164 97.40 5  1 
1.98 2.21  ? 28009 ? 0.043 16.4 0.043 ? 6.00 ? 4678 97.70 6  1 
2.21 2.56  ? 24972 ? 0.033 21.5 0.033 ? 6.00 ? 4189 98.30 7  1 
2.56 3.13  ? 21161 ? 0.025 26.7 0.025 ? 5.90 ? 3561 98.60 8  1 
3.13 4.43  ? 16324 ? 0.018 32.9 0.018 ? 5.90 ? 2784 99.00 9  1 
4.43 20.68 ? 8744  ? 0.018 31.5 0.018 ? 5.60 ? 1557 98.10 10 1 
# 
_refine.entry_id                                 3SBI 
_refine.ls_d_res_high                            1.400 
_refine.ls_d_res_low                             20.660 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    96.880 
_refine.ls_number_reflns_obs                     46451 
_refine.ls_number_reflns_all                     46451 
_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                          0.138 
_refine.ls_R_factor_obs                          0.138 
_refine.ls_R_factor_R_work                       0.133 
_refine.ls_wR_factor_R_work                      0.132 
_refine.ls_R_factor_R_free                       0.183 
_refine.ls_wR_factor_R_free                      0.174 
_refine.ls_percent_reflns_R_free                 10.100 
_refine.ls_number_reflns_R_free                  4705 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               14.597 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            0.210 
_refine.aniso_B[2][2]                            -0.190 
_refine.aniso_B[3][3]                            -0.040 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.050 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_refine.overall_SU_R_Cruickshank_DPI             0.072 
_refine.overall_SU_R_free                        0.066 
_refine.pdbx_overall_ESU_R_Free                  0.066 
_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                   0.913 
_refine.B_iso_max                                51.52 
_refine.B_iso_min                                4.36 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.pdbx_ls_sigma_I                          0 
_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         40 
_refine_hist.number_atoms_solvent             320 
_refine_hist.number_atoms_total               2419 
_refine_hist.d_res_high                       1.400 
_refine_hist.d_res_low                        20.660 
# 
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         2308 0.029  0.021  ? ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      3148 2.234  1.960  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   287  6.795  5.000  ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   107  32.908 24.860 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   379  12.767 15.000 ? ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   7    22.742 15.000 ? ? 'X-RAY DIFFRACTION' 
r_chiral_restr           322  0.182  0.200  ? ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     1818 0.014  0.020  ? ? 'X-RAY DIFFRACTION' 
r_nbd_refined            1061 0.234  0.200  ? ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          1529 0.313  0.200  ? ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    233  0.166  0.200  ? ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      3    0.034  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   92   0.202  0.200  ? ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 63   0.197  0.200  ? ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1384 2.721  1.500  ? ? 'X-RAY DIFFRACTION' 
r_mcangle_it             2252 3.637  2.000  ? ? 'X-RAY DIFFRACTION' 
r_scbond_it              924  4.662  3.000  ? ? 'X-RAY DIFFRACTION' 
r_scangle_it             896  5.924  4.500  ? ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr       2308 3.065  3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_free        321  13.699 3.000  ? ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded      2233 7.853  3.000  ? ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.d_res_high                       1.400 
_refine_ls_shell.d_res_low                        1.436 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               95.380 
_refine_ls_shell.number_reflns_R_work             3028 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.180 
_refine_ls_shell.R_factor_R_free                  0.277 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             316 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                3344 
_refine_ls_shell.number_reflns_obs                3028 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3SBI 
_struct.title                     
'Crystal structure of human carbonic anhydrase isozyme II with 4-[(2-pyrimidinylsulfanyl)acetyl]benzenesulfonamide' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3SBI 
_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 3 ? 
E N N 4 ? 
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 ? ? ? ? ? ? ? 2.032 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  262 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F E90 . N20 ? ? A ZN  262 A E90 266 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
# 
_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 -0.94 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 3.75  
# 
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  TYR A 88  ? TRP A 97  ? TYR A 88  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  TYR A 88  ? TRP A 97  ? TYR A 88  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 GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
B 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
C 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
C 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
C 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
C 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
C 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
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 DMS 263 ? 4  'BINDING SITE FOR RESIDUE DMS A 263' 
AC3 Software A DMS 264 ? 6  'BINDING SITE FOR RESIDUE DMS A 264' 
AC4 Software A BCN 265 ? 7  'BINDING SITE FOR RESIDUE BCN A 265' 
AC5 Software A E90 266 ? 12 'BINDING SITE FOR RESIDUE E90 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  E90 F .   ? E90 A 266 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH G .   ? HOH A 518 . ? 1_555 ? 
9  AC3 6  ILE A 91  ? ILE A 91  . ? 1_555 ? 
10 AC3 6  GLN A 92  ? GLN A 92  . ? 1_555 ? 
11 AC3 6  PHE A 130 ? PHE A 131 . ? 1_555 ? 
12 AC3 6  E90 F .   ? E90 A 266 . ? 1_555 ? 
13 AC3 6  HOH G .   ? HOH A 391 . ? 1_555 ? 
14 AC3 6  HOH G .   ? HOH A 501 . ? 1_555 ? 
15 AC4 7  LYS A 148 ? LYS A 149 . ? 1_555 ? 
16 AC4 7  LYS A 212 ? LYS A 213 . ? 1_555 ? 
17 AC4 7  GLU A 213 ? GLU A 214 . ? 1_555 ? 
18 AC4 7  PRO A 214 ? PRO A 215 . ? 1_555 ? 
19 AC4 7  HOH G .   ? HOH A 376 . ? 1_555 ? 
20 AC4 7  HOH G .   ? HOH A 545 . ? 1_555 ? 
21 AC4 7  HOH G .   ? HOH A 564 . ? 1_555 ? 
22 AC5 12 HIS A 94  ? HIS A 94  . ? 1_555 ? 
23 AC5 12 HIS A 96  ? HIS A 96  . ? 1_555 ? 
24 AC5 12 HIS A 119 ? HIS A 119 . ? 1_555 ? 
25 AC5 12 PHE A 130 ? PHE A 131 . ? 1_555 ? 
26 AC5 12 LEU A 197 ? LEU A 198 . ? 1_555 ? 
27 AC5 12 THR A 198 ? THR A 199 . ? 1_555 ? 
28 AC5 12 THR A 199 ? THR A 200 . ? 1_555 ? 
29 AC5 12 PRO A 201 ? PRO A 202 . ? 1_555 ? 
30 AC5 12 TRP A 208 ? TRP A 209 . ? 1_555 ? 
31 AC5 12 ZN  B .   ? ZN  A 262 . ? 1_555 ? 
32 AC5 12 DMS D .   ? DMS A 264 . ? 1_555 ? 
33 AC5 12 HOH G .   ? HOH A 499 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3SBI 
_atom_sites.fract_transf_matrix[1][1]   0.023614 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005996 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024205 
_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]   0.014282 
_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  
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   ? 13.851  -0.149  6.472   1.00 22.37 ? 3   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 3   ? 13.519  -1.118  7.559   1.00 24.51 ? 3   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 3   ? 12.474  -0.568  8.549   1.00 24.76 ? 3   HIS A C   1 
ATOM   4    O  O   . HIS A 1 3   ? 12.759  -0.360  9.768   1.00 28.40 ? 3   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 3   ? 14.746  -1.504  8.386   1.00 23.88 ? 3   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 3   ? 14.507  -2.710  9.228   1.00 26.36 ? 3   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 3   ? 14.611  -3.991  8.714   1.00 26.88 ? 3   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 3   ? 14.117  -2.837  10.526  1.00 25.73 ? 3   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 3   ? 14.354  -4.860  9.680   1.00 28.00 ? 3   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 3   ? 14.070  -4.191  10.791  1.00 24.94 ? 3   HIS A NE2 1 
ATOM   11   N  N   . HIS A 1 4   ? 11.246  -0.376  8.037   1.00 22.62 ? 4   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 4   ? 10.173  0.145   8.898   1.00 20.77 ? 4   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 4   ? 9.396   -0.998  9.599   1.00 17.64 ? 4   HIS A C   1 
ATOM   14   O  O   . HIS A 1 4   ? 9.521   -2.178  9.263   1.00 19.76 ? 4   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 4   ? 9.192   0.936   8.032   1.00 23.13 ? 4   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 4   ? 8.794   0.224   6.787   1.00 27.09 ? 4   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 4   ? 9.388   0.470   5.568   0.01 26.10 ? 4   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 4   ? 7.860   -0.731  6.563   0.01 26.35 ? 4   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 4   ? 8.837   -0.301  4.648   0.01 26.36 ? 4   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 4   ? 7.907   -1.040  5.225   0.01 26.32 ? 4   HIS A NE2 1 
ATOM   21   N  N   . TRP A 1 5   ? 8.591   -0.593  10.538  1.00 17.41 ? 5   TRP A N   1 
ATOM   22   C  CA  . TRP A 1 5   ? 7.806   -1.574  11.323  1.00 14.52 ? 5   TRP A CA  1 
ATOM   23   C  C   . TRP A 1 5   ? 6.797   -2.307  10.475  1.00 13.59 ? 5   TRP A C   1 
ATOM   24   O  O   . TRP A 1 5   ? 6.291   -1.811  9.452   1.00 14.94 ? 5   TRP A O   1 
ATOM   25   C  CB  . TRP A 1 5   ? 7.120   -0.813  12.486  1.00 13.51 ? 5   TRP A CB  1 
ATOM   26   C  CG  . TRP A 1 5   ? 5.946   0.035   12.118  1.00 14.18 ? 5   TRP A CG  1 
ATOM   27   C  CD1 . TRP A 1 5   ? 5.938   1.387   11.813  1.00 12.69 ? 5   TRP A CD1 1 
ATOM   28   C  CD2 . TRP A 1 5   ? 4.594   -0.400  12.050  1.00 12.61 ? 5   TRP A CD2 1 
ATOM   29   N  NE1 . TRP A 1 5   ? 4.669   1.807   11.593  1.00 12.76 ? 5   TRP A NE1 1 
ATOM   30   C  CE2 . TRP A 1 5   ? 3.811   0.727   11.663  1.00 10.90 ? 5   TRP A CE2 1 
ATOM   31   C  CE3 . TRP A 1 5   ? 3.938   -1.652  12.284  1.00 12.06 ? 5   TRP A CE3 1 
ATOM   32   C  CZ2 . TRP A 1 5   ? 2.413   0.656   11.519  1.00 12.26 ? 5   TRP A CZ2 1 
ATOM   33   C  CZ3 . TRP A 1 5   ? 2.517   -1.702  12.082  1.00 11.95 ? 5   TRP A CZ3 1 
ATOM   34   C  CH2 . TRP A 1 5   ? 1.800   -0.526  11.695  1.00 11.04 ? 5   TRP A CH2 1 
ATOM   35   N  N   . GLY A 1 6   ? 6.463   -3.481  10.950  1.00 12.65 ? 6   GLY A N   1 
ATOM   36   C  CA  . GLY A 1 6   ? 5.443   -4.303  10.287  1.00 12.15 ? 6   GLY A CA  1 
ATOM   37   C  C   . GLY A 1 6   ? 5.092   -5.449  11.215  1.00 12.10 ? 6   GLY A C   1 
ATOM   38   O  O   . GLY A 1 6   ? 5.109   -5.320  12.497  1.00 12.48 ? 6   GLY A O   1 
ATOM   39   N  N   A TYR A 1 7   ? 4.640   -6.505  10.506  0.50 11.84 ? 7   TYR A N   1 
ATOM   40   N  N   B TYR A 1 7   ? 4.903   -6.645  10.694  0.50 14.43 ? 7   TYR A N   1 
ATOM   41   C  CA  A TYR A 1 7   ? 4.200   -7.782  11.125  0.50 13.19 ? 7   TYR A CA  1 
ATOM   42   C  CA  B TYR A 1 7   ? 4.570   -7.718  11.662  0.50 15.18 ? 7   TYR A CA  1 
ATOM   43   C  C   A TYR A 1 7   ? 5.077   -9.003  10.769  0.50 15.24 ? 7   TYR A C   1 
ATOM   44   C  C   B TYR A 1 7   ? 5.365   -8.964  11.360  0.50 16.73 ? 7   TYR A C   1 
ATOM   45   O  O   A TYR A 1 7   ? 4.509   -10.078 10.553  0.50 13.54 ? 7   TYR A O   1 
ATOM   46   O  O   B TYR A 1 7   ? 5.221   -9.995  12.162  0.50 15.06 ? 7   TYR A O   1 
ATOM   47   C  CB  A TYR A 1 7   ? 2.689   -8.028  10.892  0.50 10.02 ? 7   TYR A CB  1 
ATOM   48   C  CB  B TYR A 1 7   ? 3.113   -8.094  11.501  0.50 14.69 ? 7   TYR A CB  1 
ATOM   49   C  CG  A TYR A 1 7   ? 1.825   -6.924  11.511  0.50 8.33  ? 7   TYR A CG  1 
ATOM   50   C  CG  B TYR A 1 7   ? 2.154   -7.056  12.008  0.50 11.09 ? 7   TYR A CG  1 
ATOM   51   C  CD1 A TYR A 1 7   ? 1.460   -6.950  12.869  0.50 10.12 ? 7   TYR A CD1 1 
ATOM   52   C  CD1 B TYR A 1 7   ? 1.681   -7.107  13.338  0.50 8.65  ? 7   TYR A CD1 1 
ATOM   53   C  CD2 A TYR A 1 7   ? 1.330   -5.880  10.713  0.50 6.97  ? 7   TYR A CD2 1 
ATOM   54   C  CD2 B TYR A 1 7   ? 1.684   -6.052  11.155  0.50 9.89  ? 7   TYR A CD2 1 
ATOM   55   C  CE1 A TYR A 1 7   ? 0.659   -5.924  13.403  0.50 6.80  ? 7   TYR A CE1 1 
ATOM   56   C  CE1 B TYR A 1 7   ? 0.781   -6.107  13.800  0.50 9.88  ? 7   TYR A CE1 1 
ATOM   57   C  CE2 A TYR A 1 7   ? 0.518   -4.871  11.227  0.50 6.64  ? 7   TYR A CE2 1 
ATOM   58   C  CE2 B TYR A 1 7   ? 0.794   -5.093  11.572  0.50 8.94  ? 7   TYR A CE2 1 
ATOM   59   C  CZ  A TYR A 1 7   ? 0.150   -4.912  12.586  0.50 5.80  ? 7   TYR A CZ  1 
ATOM   60   C  CZ  B TYR A 1 7   ? 0.323   -5.128  12.907  0.50 10.28 ? 7   TYR A CZ  1 
ATOM   61   O  OH  A TYR A 1 7   ? -0.654  -3.958  13.155  0.50 7.39  ? 7   TYR A OH  1 
ATOM   62   O  OH  B TYR A 1 7   ? -0.585  -4.188  13.330  0.50 9.43  ? 7   TYR A OH  1 
ATOM   63   N  N   A GLY A 1 8   ? 6.443   -8.850  10.847  0.50 14.57 ? 8   GLY A N   1 
ATOM   64   N  N   B GLY A 1 8   ? 6.024   -8.855  10.133  0.50 15.21 ? 8   GLY A N   1 
ATOM   65   C  CA  A GLY A 1 8   ? 7.467   -9.966  10.724  0.50 13.52 ? 8   GLY A CA  1 
ATOM   66   C  CA  B GLY A 1 8   ? 6.812   -9.919  9.429   0.50 15.54 ? 8   GLY A CA  1 
ATOM   67   C  C   A GLY A 1 8   ? 8.567   -10.271 11.809  0.50 14.98 ? 8   GLY A C   1 
ATOM   68   C  C   B GLY A 1 8   ? 7.845   -10.523 10.327  0.50 16.99 ? 8   GLY A C   1 
ATOM   69   O  O   A GLY A 1 8   ? 8.704   -9.626  12.885  0.50 13.61 ? 8   GLY A O   1 
ATOM   70   O  O   B GLY A 1 8   ? 7.843   -10.293 11.522  0.50 16.74 ? 8   GLY A O   1 
ATOM   71   N  N   A LYS A 1 9   ? 9.377   -11.299 11.563  0.50 16.29 ? 9   LYS A N   1 
ATOM   72   N  N   B LYS A 1 9   ? 8.752   -11.331 9.786   0.50 17.17 ? 9   LYS A N   1 
ATOM   73   C  CA  A LYS A 1 9   ? 10.420  -11.736 12.501  0.50 17.93 ? 9   LYS A CA  1 
ATOM   74   C  CA  B LYS A 1 9   ? 9.896   -11.612 10.612  0.50 20.52 ? 9   LYS A CA  1 
ATOM   75   C  C   A LYS A 1 9   ? 11.303  -10.612 12.815  0.50 18.00 ? 9   LYS A C   1 
ATOM   76   C  C   B LYS A 1 9   ? 10.802  -10.366 10.396  0.50 20.72 ? 9   LYS A C   1 
ATOM   77   O  O   A LYS A 1 9   ? 11.705  -10.436 13.969  0.50 16.77 ? 9   LYS A O   1 
ATOM   78   O  O   B LYS A 1 9   ? 10.991  -9.873  9.288   0.50 23.42 ? 9   LYS A O   1 
ATOM   79   C  CB  A LYS A 1 9   ? 11.332  -12.707 11.847  0.50 17.58 ? 9   LYS A CB  1 
ATOM   80   C  CB  B LYS A 1 9   ? 10.577  -12.957 10.305  0.50 20.66 ? 9   LYS A CB  1 
ATOM   81   C  CG  A LYS A 1 9   ? 12.277  -13.314 12.789  0.50 18.63 ? 9   LYS A CG  1 
ATOM   82   C  CG  B LYS A 1 9   ? 10.217  -13.525 9.031   0.50 22.85 ? 9   LYS A CG  1 
ATOM   83   C  CD  A LYS A 1 9   ? 13.061  -14.490 12.256  0.50 19.03 ? 9   LYS A CD  1 
ATOM   84   C  CD  B LYS A 1 9   ? 9.003   -14.390 9.234   0.50 24.35 ? 9   LYS A CD  1 
ATOM   85   C  CE  A LYS A 1 9   ? 13.931  -15.054 13.374  0.00 21.67 ? 9   LYS A CE  1 
ATOM   86   C  CE  B LYS A 1 9   ? 9.370   -15.855 9.145   0.50 27.90 ? 9   LYS A CE  1 
ATOM   87   N  NZ  A LYS A 1 9   ? 15.123  -15.783 12.869  0.00 20.47 ? 9   LYS A NZ  1 
ATOM   88   N  NZ  B LYS A 1 9   ? 9.872   -16.195 7.780   0.50 30.11 ? 9   LYS A NZ  1 
ATOM   89   N  N   A HIS A 1 10  ? 11.591  -9.871  11.740  0.50 19.71 ? 10  HIS A N   1 
ATOM   90   N  N   B HIS A 1 10  ? 11.305  -9.818  11.444  0.50 21.72 ? 10  HIS A N   1 
ATOM   91   C  CA  A HIS A 1 10  ? 12.559  -8.862  11.726  0.50 18.91 ? 10  HIS A CA  1 
ATOM   92   C  CA  B HIS A 1 10  ? 12.339  -8.876  11.299  0.50 19.73 ? 10  HIS A CA  1 
ATOM   93   C  C   A HIS A 1 10  ? 11.962  -7.488  12.001  0.50 17.78 ? 10  HIS A C   1 
ATOM   94   C  C   B HIS A 1 10  ? 11.939  -7.529  11.817  0.50 18.53 ? 10  HIS A C   1 
ATOM   95   O  O   A HIS A 1 10  ? 12.732  -6.660  12.484  0.50 18.26 ? 10  HIS A O   1 
ATOM   96   O  O   B HIS A 1 10  ? 12.781  -6.818  12.337  0.50 18.69 ? 10  HIS A O   1 
ATOM   97   C  CB  A HIS A 1 10  ? 13.417  -8.933  10.387  0.50 16.67 ? 10  HIS A CB  1 
ATOM   98   C  CB  B HIS A 1 10  ? 12.961  -8.867  9.860   0.50 17.84 ? 10  HIS A CB  1 
ATOM   99   C  CG  A HIS A 1 10  ? 13.860  -10.341 9.999   0.50 19.41 ? 10  HIS A CG  1 
ATOM   100  C  CG  B HIS A 1 10  ? 13.514  -10.200 9.456   0.50 18.82 ? 10  HIS A CG  1 
ATOM   101  N  ND1 A HIS A 1 10  ? 14.799  -11.046 10.725  0.50 21.99 ? 10  HIS A ND1 1 
ATOM   102  N  ND1 B HIS A 1 10  ? 14.428  -10.845 10.245  0.50 15.10 ? 10  HIS A ND1 1 
ATOM   103  C  CD2 A HIS A 1 10  ? 13.523  -11.142 8.944   0.50 18.05 ? 10  HIS A CD2 1 
ATOM   104  C  CD2 B HIS A 1 10  ? 13.284  -11.027 8.396   0.50 16.30 ? 10  HIS A CD2 1 
ATOM   105  C  CE1 A HIS A 1 10  ? 14.991  -12.231 10.162  0.50 15.20 ? 10  HIS A CE1 1 
ATOM   106  C  CE1 B HIS A 1 10  ? 14.761  -12.001 9.711   0.50 14.33 ? 10  HIS A CE1 1 
ATOM   107  N  NE2 A HIS A 1 10  ? 14.223  -12.319 9.085   0.50 20.19 ? 10  HIS A NE2 1 
ATOM   108  N  NE2 B HIS A 1 10  ? 14.061  -12.147 8.585   0.50 14.96 ? 10  HIS A NE2 1 
ATOM   109  N  N   . ASN A 1 11  ? 10.628  -7.245  11.773  1.00 17.07 ? 11  ASN A N   1 
ATOM   110  C  CA  . ASN A 1 11  ? 10.131  -5.911  12.040  1.00 16.07 ? 11  ASN A CA  1 
ATOM   111  C  C   . ASN A 1 11  ? 8.795   -5.936  12.807  1.00 14.38 ? 11  ASN A C   1 
ATOM   112  O  O   . ASN A 1 11  ? 8.128   -4.908  12.923  1.00 15.60 ? 11  ASN A O   1 
ATOM   113  C  CB  . ASN A 1 11  ? 9.924   -5.139  10.759  1.00 15.68 ? 11  ASN A CB  1 
ATOM   114  C  CG  . ASN A 1 11  ? 8.881   -5.758  9.849   1.00 17.19 ? 11  ASN A CG  1 
ATOM   115  O  OD1 . ASN A 1 11  ? 8.333   -6.862  10.114  1.00 19.07 ? 11  ASN A OD1 1 
ATOM   116  N  ND2 . ASN A 1 11  ? 8.618   -5.072  8.730   1.00 17.97 ? 11  ASN A ND2 1 
ATOM   117  N  N   . GLY A 1 12  ? 8.469   -7.056  13.420  1.00 14.49 ? 12  GLY A N   1 
ATOM   118  C  CA  . GLY A 1 12  ? 7.159   -7.216  14.138  1.00 12.06 ? 12  GLY A CA  1 
ATOM   119  C  C   . GLY A 1 12  ? 7.153   -6.698  15.546  1.00 12.14 ? 12  GLY A C   1 
ATOM   120  O  O   . GLY A 1 12  ? 8.021   -5.936  15.945  1.00 12.39 ? 12  GLY A O   1 
ATOM   121  N  N   . PRO A 1 13  ? 6.033   -6.963  16.243  1.00 10.58 ? 13  PRO A N   1 
ATOM   122  C  CA  . PRO A 1 13  ? 5.798   -6.375  17.543  1.00 11.11 ? 13  PRO A CA  1 
ATOM   123  C  C   . PRO A 1 13  ? 6.947   -6.336  18.537  1.00 11.32 ? 13  PRO A C   1 
ATOM   124  O  O   . PRO A 1 13  ? 7.102   -5.321  19.283  1.00 12.17 ? 13  PRO A O   1 
ATOM   125  C  CB  . PRO A 1 13  ? 4.564   -7.146  18.077  1.00 12.11 ? 13  PRO A CB  1 
ATOM   126  C  CG  . PRO A 1 13  ? 3.745   -7.439  16.838  1.00 13.21 ? 13  PRO A CG  1 
ATOM   127  C  CD  . PRO A 1 13  ? 4.873   -7.755  15.763  1.00 12.23 ? 13  PRO A CD  1 
ATOM   128  N  N   A GLU A 1 14  ? 7.754   -7.389  18.478  0.50 10.86 ? 14  GLU A N   1 
ATOM   129  N  N   B GLU A 1 14  ? 7.759   -7.401  18.679  0.50 12.34 ? 14  GLU A N   1 
ATOM   130  C  CA  A GLU A 1 14  ? 8.825   -7.532  19.425  0.50 11.62 ? 14  GLU A CA  1 
ATOM   131  C  CA  B GLU A 1 14  ? 8.826   -7.314  19.724  0.50 13.84 ? 14  GLU A CA  1 
ATOM   132  C  C   A GLU A 1 14  ? 10.004  -6.572  19.164  0.50 10.80 ? 14  GLU A C   1 
ATOM   133  C  C   B GLU A 1 14  ? 10.003  -6.383  19.281  0.50 12.60 ? 14  GLU A C   1 
ATOM   134  O  O   A GLU A 1 14  ? 10.914  -6.465  19.998  0.50 11.96 ? 14  GLU A O   1 
ATOM   135  O  O   B GLU A 1 14  ? 10.922  -6.111  20.109  0.50 13.96 ? 14  GLU A O   1 
ATOM   136  C  CB  A GLU A 1 14  ? 9.298   -8.969  19.435  0.50 12.79 ? 14  GLU A CB  1 
ATOM   137  C  CB  B GLU A 1 14  ? 9.407   -8.663  20.217  0.50 16.04 ? 14  GLU A CB  1 
ATOM   138  C  CG  A GLU A 1 14  ? 9.959   -9.442  18.199  0.50 12.51 ? 14  GLU A CG  1 
ATOM   139  C  CG  B GLU A 1 14  ? 8.455   -9.875  20.460  0.50 18.56 ? 14  GLU A CG  1 
ATOM   140  C  CD  A GLU A 1 14  ? 9.101   -10.015 17.052  0.50 14.78 ? 14  GLU A CD  1 
ATOM   141  C  CD  B GLU A 1 14  ? 7.392   -9.679  21.585  0.50 24.27 ? 14  GLU A CD  1 
ATOM   142  O  OE1 A GLU A 1 14  ? 7.881   -9.660  16.941  0.50 10.37 ? 14  GLU A OE1 1 
ATOM   143  O  OE1 B GLU A 1 14  ? 7.820   -9.502  22.745  0.50 27.42 ? 14  GLU A OE1 1 
ATOM   144  O  OE2 A GLU A 1 14  ? 9.762   -10.829 16.278  0.50 16.16 ? 14  GLU A OE2 1 
ATOM   145  O  OE2 B GLU A 1 14  ? 6.127   -9.750  21.329  0.50 25.07 ? 14  GLU A OE2 1 
ATOM   146  N  N   . HIS A 1 15  ? 9.937   -5.839  18.046  1.00 11.71 ? 15  HIS A N   1 
ATOM   147  C  CA  . HIS A 1 15  ? 10.977  -4.905  17.608  1.00 11.89 ? 15  HIS A CA  1 
ATOM   148  C  C   . HIS A 1 15  ? 10.554  -3.431  17.764  1.00 11.48 ? 15  HIS A C   1 
ATOM   149  O  O   . HIS A 1 15  ? 11.395  -2.516  17.655  1.00 13.26 ? 15  HIS A O   1 
ATOM   150  C  CB  . HIS A 1 15  ? 11.314  -5.112  16.088  1.00 11.74 ? 15  HIS A CB  1 
ATOM   151  C  CG  . HIS A 1 15  ? 12.021  -6.404  15.861  1.00 12.18 ? 15  HIS A CG  1 
ATOM   152  N  ND1 . HIS A 1 15  ? 13.396  -6.502  16.062  1.00 16.60 ? 15  HIS A ND1 1 
ATOM   153  C  CD2 . HIS A 1 15  ? 11.573  -7.660  15.550  1.00 16.27 ? 15  HIS A CD2 1 
ATOM   154  C  CE1 . HIS A 1 15  ? 13.766  -7.761  15.849  1.00 19.78 ? 15  HIS A CE1 1 
ATOM   155  N  NE2 . HIS A 1 15  ? 12.699  -8.485  15.553  1.00 17.35 ? 15  HIS A NE2 1 
ATOM   156  N  N   . TRP A 1 16  ? 9.230   -3.189  17.941  1.00 10.37 ? 16  TRP A N   1 
ATOM   157  C  CA  . TRP A 1 16  ? 8.717   -1.838  17.798  1.00 10.15 ? 16  TRP A CA  1 
ATOM   158  C  C   . TRP A 1 16  ? 9.297   -0.856  18.818  1.00 10.98 ? 16  TRP A C   1 
ATOM   159  O  O   . TRP A 1 16  ? 9.417   0.310   18.531  1.00 11.84 ? 16  TRP A O   1 
ATOM   160  C  CB  . TRP A 1 16  ? 7.169   -1.874  17.977  1.00 9.75  ? 16  TRP A CB  1 
ATOM   161  C  CG  . TRP A 1 16  ? 6.476   -2.568  16.828  1.00 9.92  ? 16  TRP A CG  1 
ATOM   162  C  CD1 . TRP A 1 16  ? 7.039   -2.999  15.616  1.00 8.62  ? 16  TRP A CD1 1 
ATOM   163  C  CD2 . TRP A 1 16  ? 5.063   -2.889  16.768  1.00 8.12  ? 16  TRP A CD2 1 
ATOM   164  N  NE1 . TRP A 1 16  ? 6.071   -3.639  14.844  1.00 10.16 ? 16  TRP A NE1 1 
ATOM   165  C  CE2 . TRP A 1 16  ? 4.837   -3.537  15.501  1.00 10.37 ? 16  TRP A CE2 1 
ATOM   166  C  CE3 . TRP A 1 16  ? 3.989   -2.660  17.658  1.00 9.24  ? 16  TRP A CE3 1 
ATOM   167  C  CZ2 . TRP A 1 16  ? 3.558   -3.971  15.122  1.00 9.60  ? 16  TRP A CZ2 1 
ATOM   168  C  CZ3 . TRP A 1 16  ? 2.735   -3.147  17.268  1.00 8.05  ? 16  TRP A CZ3 1 
ATOM   169  C  CH2 . TRP A 1 16  ? 2.508   -3.760  16.034  1.00 8.75  ? 16  TRP A CH2 1 
ATOM   170  N  N   . HIS A 1 17  ? 9.704   -1.388  19.964  1.00 10.50 ? 17  HIS A N   1 
ATOM   171  C  CA  . HIS A 1 17  ? 10.205  -0.571  21.077  1.00 12.25 ? 17  HIS A CA  1 
ATOM   172  C  C   . HIS A 1 17  ? 11.473  0.242   20.662  1.00 13.01 ? 17  HIS A C   1 
ATOM   173  O  O   . HIS A 1 17  ? 11.747  1.313   21.261  1.00 13.08 ? 17  HIS A O   1 
ATOM   174  C  CB  . HIS A 1 17  ? 10.465  -1.356  22.388  1.00 11.65 ? 17  HIS A CB  1 
ATOM   175  C  CG  . HIS A 1 17  ? 11.684  -2.230  22.282  1.00 12.08 ? 17  HIS A CG  1 
ATOM   176  N  ND1 . HIS A 1 17  ? 12.921  -1.807  22.718  1.00 14.76 ? 17  HIS A ND1 1 
ATOM   177  C  CD2 . HIS A 1 17  ? 11.869  -3.453  21.723  1.00 14.86 ? 17  HIS A CD2 1 
ATOM   178  C  CE1 . HIS A 1 17  ? 13.821  -2.738  22.427  1.00 16.25 ? 17  HIS A CE1 1 
ATOM   179  N  NE2 . HIS A 1 17  ? 13.217  -3.749  21.832  1.00 15.54 ? 17  HIS A NE2 1 
ATOM   180  N  N   . LYS A 1 18  ? 12.241  -0.318  19.714  1.00 13.09 ? 18  LYS A N   1 
ATOM   181  C  CA  . LYS A 1 18  ? 13.469  0.426   19.291  1.00 14.01 ? 18  LYS A CA  1 
ATOM   182  C  C   . LYS A 1 18  ? 13.137  1.747   18.572  1.00 14.13 ? 18  LYS A C   1 
ATOM   183  O  O   . LYS A 1 18  ? 13.827  2.770   18.817  1.00 18.03 ? 18  LYS A O   1 
ATOM   184  C  CB  . LYS A 1 18  ? 14.336  -0.431  18.407  1.00 15.62 ? 18  LYS A CB  1 
ATOM   185  C  CG  . LYS A 1 18  ? 14.927  -1.641  19.168  1.00 14.24 ? 18  LYS A CG  1 
ATOM   186  C  CD  . LYS A 1 18  ? 15.631  -2.624  18.245  1.00 15.27 ? 18  LYS A CD  1 
ATOM   187  C  CE  . LYS A 1 18  ? 14.635  -3.637  17.616  1.00 16.17 ? 18  LYS A CE  1 
ATOM   188  N  NZ  . LYS A 1 18  ? 15.240  -4.510  16.496  1.00 13.63 ? 18  LYS A NZ  1 
ATOM   189  N  N   . ASP A 1 19  ? 12.098  1.789   17.737  1.00 13.55 ? 19  ASP A N   1 
ATOM   190  C  CA  . ASP A 1 19  ? 11.676  3.082   17.168  1.00 14.91 ? 19  ASP A CA  1 
ATOM   191  C  C   . ASP A 1 19  ? 10.624  3.839   18.025  1.00 15.28 ? 19  ASP A C   1 
ATOM   192  O  O   . ASP A 1 19  ? 10.538  5.072   17.896  1.00 16.59 ? 19  ASP A O   1 
ATOM   193  C  CB  . ASP A 1 19  ? 11.154  2.900   15.777  1.00 17.79 ? 19  ASP A CB  1 
ATOM   194  C  CG  . ASP A 1 19  ? 12.253  2.886   14.711  1.00 20.96 ? 19  ASP A CG  1 
ATOM   195  O  OD1 . ASP A 1 19  ? 13.313  3.487   14.906  1.00 24.66 ? 19  ASP A OD1 1 
ATOM   196  O  OD2 . ASP A 1 19  ? 12.059  2.272   13.663  1.00 33.40 ? 19  ASP A OD2 1 
ATOM   197  N  N   . PHE A 1 20  ? 9.867   3.099   18.863  1.00 11.81 ? 20  PHE A N   1 
ATOM   198  C  CA  . PHE A 1 20  ? 8.760   3.689   19.618  1.00 11.70 ? 20  PHE A CA  1 
ATOM   199  C  C   . PHE A 1 20  ? 8.865   3.237   21.080  1.00 11.01 ? 20  PHE A C   1 
ATOM   200  O  O   . PHE A 1 20  ? 8.247   2.223   21.451  1.00 10.77 ? 20  PHE A O   1 
ATOM   201  C  CB  . PHE A 1 20  ? 7.414   3.233   18.980  1.00 12.75 ? 20  PHE A CB  1 
ATOM   202  C  CG  . PHE A 1 20  ? 7.304   3.642   17.527  1.00 11.39 ? 20  PHE A CG  1 
ATOM   203  C  CD1 . PHE A 1 20  ? 6.911   4.938   17.185  1.00 13.58 ? 20  PHE A CD1 1 
ATOM   204  C  CD2 . PHE A 1 20  ? 7.696   2.741   16.512  1.00 12.10 ? 20  PHE A CD2 1 
ATOM   205  C  CE1 . PHE A 1 20  ? 6.891   5.300   15.821  1.00 13.94 ? 20  PHE A CE1 1 
ATOM   206  C  CE2 . PHE A 1 20  ? 7.691   3.079   15.176  1.00 14.20 ? 20  PHE A CE2 1 
ATOM   207  C  CZ  . PHE A 1 20  ? 7.280   4.370   14.825  1.00 13.95 ? 20  PHE A CZ  1 
ATOM   208  N  N   . PRO A 1 21  ? 9.761   3.862   21.881  1.00 11.91 ? 21  PRO A N   1 
ATOM   209  C  CA  . PRO A 1 21  ? 10.004  3.317   23.227  1.00 11.36 ? 21  PRO A CA  1 
ATOM   210  C  C   . PRO A 1 21  ? 8.750   3.205   24.121  1.00 11.46 ? 21  PRO A C   1 
ATOM   211  O  O   . PRO A 1 21  ? 8.778   2.427   25.087  1.00 11.67 ? 21  PRO A O   1 
ATOM   212  C  CB  . PRO A 1 21  ? 11.083  4.259   23.839  1.00 13.30 ? 21  PRO A CB  1 
ATOM   213  C  CG  . PRO A 1 21  ? 11.356  5.294   22.751  1.00 17.16 ? 21  PRO A CG  1 
ATOM   214  C  CD  . PRO A 1 21  ? 10.701  4.930   21.475  1.00 13.02 ? 21  PRO A CD  1 
ATOM   215  N  N   A ILE A 1 22  ? 7.679   3.990   23.839  0.50 10.15 ? 22  ILE A N   1 
ATOM   216  N  N   B ILE A 1 22  ? 7.714   4.015   23.795  0.50 9.57  ? 22  ILE A N   1 
ATOM   217  C  CA  A ILE A 1 22  ? 6.422   3.831   24.598  0.50 10.45 ? 22  ILE A CA  1 
ATOM   218  C  CA  B ILE A 1 22  ? 6.426   3.939   24.465  0.50 9.10  ? 22  ILE A CA  1 
ATOM   219  C  C   A ILE A 1 22  ? 5.858   2.408   24.469  0.50 10.41 ? 22  ILE A C   1 
ATOM   220  C  C   B ILE A 1 22  ? 5.833   2.504   24.384  0.50 9.65  ? 22  ILE A C   1 
ATOM   221  O  O   A ILE A 1 22  ? 4.975   2.041   25.269  0.50 10.35 ? 22  ILE A O   1 
ATOM   222  O  O   B ILE A 1 22  ? 4.913   2.225   25.164  0.50 8.80  ? 22  ILE A O   1 
ATOM   223  C  CB  A ILE A 1 22  ? 5.344   4.898   24.252  0.50 9.95  ? 22  ILE A CB  1 
ATOM   224  C  CB  B ILE A 1 22  ? 5.455   5.075   23.972  0.50 9.14  ? 22  ILE A CB  1 
ATOM   225  C  CG1 A ILE A 1 22  ? 4.370   5.124   25.410  0.50 12.35 ? 22  ILE A CG1 1 
ATOM   226  C  CG1 B ILE A 1 22  ? 4.379   5.384   25.042  0.50 8.91  ? 22  ILE A CG1 1 
ATOM   227  C  CG2 A ILE A 1 22  ? 4.606   4.486   22.980  0.50 11.25 ? 22  ILE A CG2 1 
ATOM   228  C  CG2 B ILE A 1 22  ? 4.935   4.628   22.601  0.50 11.54 ? 22  ILE A CG2 1 
ATOM   229  C  CD1 A ILE A 1 22  ? 4.998   5.846   26.538  0.50 11.94 ? 22  ILE A CD1 1 
ATOM   230  C  CD1 B ILE A 1 22  ? 3.386   6.528   24.845  0.50 7.65  ? 22  ILE A CD1 1 
ATOM   231  N  N   . ALA A 1 23  ? 6.353   1.615   23.518  1.00 10.18 ? 23  ALA A N   1 
ATOM   232  C  CA  . ALA A 1 23  ? 5.903   0.197   23.429  1.00 9.48  ? 23  ALA A CA  1 
ATOM   233  C  C   . ALA A 1 23  ? 6.000   -0.533  24.792  1.00 10.71 ? 23  ALA A C   1 
ATOM   234  O  O   . ALA A 1 23  ? 5.272   -1.540  24.999  1.00 9.82  ? 23  ALA A O   1 
ATOM   235  C  CB  . ALA A 1 23  ? 6.771   -0.536  22.433  1.00 11.25 ? 23  ALA A CB  1 
ATOM   236  N  N   . LYS A 1 24  ? 6.914   -0.062  25.681  1.00 11.34 ? 24  LYS A N   1 
ATOM   237  C  CA  . LYS A 1 24  ? 7.117   -0.699  27.020  1.00 11.05 ? 24  LYS A CA  1 
ATOM   238  C  C   . LYS A 1 24  ? 6.534   0.205   28.093  1.00 12.44 ? 24  LYS A C   1 
ATOM   239  O  O   . LYS A 1 24  ? 6.915   0.086   29.260  1.00 15.52 ? 24  LYS A O   1 
ATOM   240  C  CB  . LYS A 1 24  ? 8.623   -0.976  27.305  1.00 12.30 ? 24  LYS A CB  1 
ATOM   241  C  CG  . LYS A 1 24  ? 9.196   -1.948  26.286  1.00 15.76 ? 24  LYS A CG  1 
ATOM   242  C  CD  . LYS A 1 24  ? 10.694  -2.163  26.697  1.00 20.14 ? 24  LYS A CD  1 
ATOM   243  C  CE  . LYS A 1 24  ? 11.462  -3.116  25.818  1.00 21.70 ? 24  LYS A CE  1 
ATOM   244  N  NZ  . LYS A 1 24  ? 11.021  -4.483  25.988  1.00 26.49 ? 24  LYS A NZ  1 
ATOM   245  N  N   . GLY A 1 25  ? 5.513   0.994   27.711  1.00 11.36 ? 25  GLY A N   1 
ATOM   246  C  CA  . GLY A 1 25  ? 4.911   1.988   28.601  1.00 11.60 ? 25  GLY A CA  1 
ATOM   247  C  C   . GLY A 1 25  ? 3.959   1.387   29.633  1.00 10.29 ? 25  GLY A C   1 
ATOM   248  O  O   . GLY A 1 25  ? 3.730   0.118   29.742  1.00 13.04 ? 25  GLY A O   1 
ATOM   249  N  N   . GLU A 1 26  ? 3.307   2.285   30.365  1.00 11.80 ? 26  GLU A N   1 
ATOM   250  C  CA  . GLU A 1 26  ? 2.412   1.838   31.461  1.00 12.07 ? 26  GLU A CA  1 
ATOM   251  C  C   . GLU A 1 26  ? 0.961   1.598   31.086  1.00 11.19 ? 26  GLU A C   1 
ATOM   252  O  O   . GLU A 1 26  ? 0.197   1.109   31.950  1.00 11.64 ? 26  GLU A O   1 
ATOM   253  C  CB  . GLU A 1 26  ? 2.436   2.913   32.575  1.00 13.64 ? 26  GLU A CB  1 
ATOM   254  C  CG  . GLU A 1 26  ? 3.869   3.227   33.160  1.00 16.46 ? 26  GLU A CG  1 
ATOM   255  C  CD  . GLU A 1 26  ? 4.450   1.941   33.802  1.00 24.17 ? 26  GLU A CD  1 
ATOM   256  O  OE1 . GLU A 1 26  ? 3.776   1.343   34.667  1.00 28.02 ? 26  GLU A OE1 1 
ATOM   257  O  OE2 . GLU A 1 26  ? 5.535   1.485   33.344  1.00 29.56 ? 26  GLU A OE2 1 
ATOM   258  N  N   . ARG A 1 27  ? 0.571   1.942   29.824  1.00 8.58  ? 27  ARG A N   1 
ATOM   259  C  CA  . ARG A 1 27  ? -0.864  1.727   29.442  1.00 8.38  ? 27  ARG A CA  1 
ATOM   260  C  C   . ARG A 1 27  ? -0.943  1.309   27.975  1.00 6.93  ? 27  ARG A C   1 
ATOM   261  O  O   . ARG A 1 27  ? -1.618  1.954   27.124  1.00 8.13  ? 27  ARG A O   1 
ATOM   262  C  CB  . ARG A 1 27  ? -1.836  2.927   29.777  1.00 11.90 ? 27  ARG A CB  1 
ATOM   263  C  CG  . ARG A 1 27  ? -1.476  4.243   29.186  1.00 14.18 ? 27  ARG A CG  1 
ATOM   264  C  CD  . ARG A 1 27  ? -2.513  5.333   29.494  1.00 15.46 ? 27  ARG A CD  1 
ATOM   265  N  NE  . ARG A 1 27  ? -3.659  5.301   28.585  1.00 14.91 ? 27  ARG A NE  1 
ATOM   266  C  CZ  . ARG A 1 27  ? -4.571  6.265   28.489  1.00 12.20 ? 27  ARG A CZ  1 
ATOM   267  N  NH1 . ARG A 1 27  ? -4.478  7.352   29.245  1.00 14.52 ? 27  ARG A NH1 1 
ATOM   268  N  NH2 . ARG A 1 27  ? -5.579  6.144   27.635  1.00 13.23 ? 27  ARG A NH2 1 
ATOM   269  N  N   . GLN A 1 28  ? -0.210  0.186   27.716  1.00 6.90  ? 28  GLN A N   1 
ATOM   270  C  CA  . GLN A 1 28  ? -0.190  -0.339  26.317  1.00 6.01  ? 28  GLN A CA  1 
ATOM   271  C  C   . GLN A 1 28  ? -1.359  -1.345  26.044  1.00 6.55  ? 28  GLN A C   1 
ATOM   272  O  O   . GLN A 1 28  ? -1.855  -2.024  26.999  1.00 7.07  ? 28  GLN A O   1 
ATOM   273  C  CB  . GLN A 1 28  ? 1.138   -1.048  26.037  1.00 6.98  ? 28  GLN A CB  1 
ATOM   274  C  CG  . GLN A 1 28  ? 2.284   0.031   26.015  1.00 8.09  ? 28  GLN A CG  1 
ATOM   275  C  CD  . GLN A 1 28  ? 2.146   0.865   24.704  1.00 8.15  ? 28  GLN A CD  1 
ATOM   276  O  OE1 . GLN A 1 28  ? 2.336   0.303   23.575  1.00 7.59  ? 28  GLN A OE1 1 
ATOM   277  N  NE2 . GLN A 1 28  ? 1.791   2.193   24.851  1.00 7.92  ? 28  GLN A NE2 1 
ATOM   278  N  N   . SER A 1 29  ? -1.745  -1.371  24.774  1.00 5.66  ? 29  SER A N   1 
ATOM   279  C  CA  . SER A 1 29  ? -2.824  -2.279  24.362  1.00 5.21  ? 29  SER A CA  1 
ATOM   280  C  C   . SER A 1 29  ? -2.315  -3.161  23.219  1.00 5.58  ? 29  SER A C   1 
ATOM   281  O  O   . SER A 1 29  ? -1.355  -2.775  22.546  1.00 6.16  ? 29  SER A O   1 
ATOM   282  C  CB  . SER A 1 29  ? -4.006  -1.421  23.763  1.00 6.91  ? 29  SER A CB  1 
ATOM   283  O  OG  . SER A 1 29  ? -4.586  -0.692  24.880  1.00 5.75  ? 29  SER A OG  1 
ATOM   284  N  N   . PRO A 1 30  ? -2.937  -4.302  22.953  1.00 5.65  ? 30  PRO A N   1 
ATOM   285  C  CA  . PRO A 1 30  ? -4.100  -4.844  23.679  1.00 5.12  ? 30  PRO A CA  1 
ATOM   286  C  C   . PRO A 1 30  ? -3.697  -5.492  25.022  1.00 5.09  ? 30  PRO A C   1 
ATOM   287  O  O   . PRO A 1 30  ? -2.476  -5.531  25.317  1.00 6.61  ? 30  PRO A O   1 
ATOM   288  C  CB  . PRO A 1 30  ? -4.651  -5.892  22.727  1.00 5.84  ? 30  PRO A CB  1 
ATOM   289  C  CG  . PRO A 1 30  ? -3.353  -6.503  22.088  1.00 7.47  ? 30  PRO A CG  1 
ATOM   290  C  CD  . PRO A 1 30  ? -2.457  -5.220  21.903  1.00 6.73  ? 30  PRO A CD  1 
ATOM   291  N  N   . VAL A 1 31  ? -4.682  -6.088  25.708  1.00 5.41  ? 31  VAL A N   1 
ATOM   292  C  CA  . VAL A 1 31  ? -4.486  -6.812  26.964  1.00 6.08  ? 31  VAL A CA  1 
ATOM   293  C  C   . VAL A 1 31  ? -5.381  -8.047  26.916  1.00 5.82  ? 31  VAL A C   1 
ATOM   294  O  O   . VAL A 1 31  ? -6.366  -8.119  26.145  1.00 6.42  ? 31  VAL A O   1 
ATOM   295  C  CB  . VAL A 1 31  ? -4.816  -5.945  28.233  1.00 7.11  ? 31  VAL A CB  1 
ATOM   296  C  CG1 . VAL A 1 31  ? -3.839  -4.781  28.315  1.00 7.83  ? 31  VAL A CG1 1 
ATOM   297  C  CG2 . VAL A 1 31  ? -6.302  -5.523  28.278  1.00 8.66  ? 31  VAL A CG2 1 
ATOM   298  N  N   . ASP A 1 32  ? -5.034  -9.029  27.761  1.00 6.66  ? 32  ASP A N   1 
ATOM   299  C  CA  . ASP A 1 32  ? -5.936  -10.140 28.051  1.00 6.43  ? 32  ASP A CA  1 
ATOM   300  C  C   . ASP A 1 32  ? -6.990  -9.604  29.036  1.00 7.34  ? 32  ASP A C   1 
ATOM   301  O  O   . ASP A 1 32  ? -6.684  -8.944  30.044  1.00 8.26  ? 32  ASP A O   1 
ATOM   302  C  CB  . ASP A 1 32  ? -5.200  -11.299 28.707  1.00 7.91  ? 32  ASP A CB  1 
ATOM   303  C  CG  . ASP A 1 32  ? -6.150  -12.501 28.984  1.00 10.23 ? 32  ASP A CG  1 
ATOM   304  O  OD1 . ASP A 1 32  ? -6.848  -12.911 28.036  1.00 8.13  ? 32  ASP A OD1 1 
ATOM   305  O  OD2 . ASP A 1 32  ? -6.171  -12.950 30.191  1.00 10.83 ? 32  ASP A OD2 1 
ATOM   306  N  N   . ILE A 1 33  ? -8.269  -9.948  28.748  1.00 7.07  ? 33  ILE A N   1 
ATOM   307  C  CA  . ILE A 1 33  ? -9.407  -9.574  29.615  1.00 8.36  ? 33  ILE A CA  1 
ATOM   308  C  C   . ILE A 1 33  ? -9.677  -10.826 30.481  1.00 8.24  ? 33  ILE A C   1 
ATOM   309  O  O   . ILE A 1 33  ? -10.226 -11.817 30.004  1.00 9.50  ? 33  ILE A O   1 
ATOM   310  C  CB  . ILE A 1 33  ? -10.638 -9.166  28.793  1.00 7.54  ? 33  ILE A CB  1 
ATOM   311  C  CG1 . ILE A 1 33  ? -10.216 -7.914  27.954  1.00 7.57  ? 33  ILE A CG1 1 
ATOM   312  C  CG2 . ILE A 1 33  ? -11.850 -8.836  29.781  1.00 10.68 ? 33  ILE A CG2 1 
ATOM   313  C  CD1 . ILE A 1 33  ? -11.330 -7.567  26.789  1.00 9.24  ? 33  ILE A CD1 1 
ATOM   314  N  N   A ASP A 1 34  ? -9.277  -10.751 31.746  0.50 9.58  ? 34  ASP A N   1 
ATOM   315  N  N   B ASP A 1 34  ? -9.244  -10.762 31.751  0.50 9.56  ? 34  ASP A N   1 
ATOM   316  C  CA  A ASP A 1 34  ? -9.572  -11.849 32.656  0.50 10.60 ? 34  ASP A CA  1 
ATOM   317  C  CA  B ASP A 1 34  ? -9.556  -11.805 32.766  0.50 10.37 ? 34  ASP A CA  1 
ATOM   318  C  C   A ASP A 1 34  ? -10.947 -11.572 33.271  0.50 11.00 ? 34  ASP A C   1 
ATOM   319  C  C   B ASP A 1 34  ? -10.981 -11.514 33.253  0.50 10.81 ? 34  ASP A C   1 
ATOM   320  O  O   A ASP A 1 34  ? -11.119 -10.634 34.075  0.50 12.51 ? 34  ASP A O   1 
ATOM   321  O  O   B ASP A 1 34  ? -11.224 -10.498 33.946  0.50 11.45 ? 34  ASP A O   1 
ATOM   322  C  CB  A ASP A 1 34  ? -8.501  -11.905 33.723  0.50 10.60 ? 34  ASP A CB  1 
ATOM   323  C  CB  B ASP A 1 34  ? -8.545  -11.692 33.926  0.50 10.94 ? 34  ASP A CB  1 
ATOM   324  C  CG  A ASP A 1 34  ? -8.642  -13.137 34.605  0.50 13.57 ? 34  ASP A CG  1 
ATOM   325  C  CG  B ASP A 1 34  ? -8.802  -12.725 35.076  0.50 11.57 ? 34  ASP A CG  1 
ATOM   326  O  OD1 A ASP A 1 34  ? -9.089  -12.985 35.769  0.50 14.53 ? 34  ASP A OD1 1 
ATOM   327  O  OD1 B ASP A 1 34  ? -9.966  -13.160 35.291  0.50 13.06 ? 34  ASP A OD1 1 
ATOM   328  O  OD2 A ASP A 1 34  ? -8.316  -14.244 34.113  0.50 14.83 ? 34  ASP A OD2 1 
ATOM   329  O  OD2 B ASP A 1 34  ? -7.800  -13.115 35.778  0.50 15.00 ? 34  ASP A OD2 1 
ATOM   330  N  N   . THR A 1 35  ? -11.936 -12.310 32.791  1.00 11.70 ? 35  THR A N   1 
ATOM   331  C  CA  . THR A 1 35  ? -13.330 -11.993 33.003  1.00 12.96 ? 35  THR A CA  1 
ATOM   332  C  C   . THR A 1 35  ? -13.737 -12.115 34.437  1.00 12.89 ? 35  THR A C   1 
ATOM   333  O  O   . THR A 1 35  ? -14.700 -11.447 34.897  1.00 15.37 ? 35  THR A O   1 
ATOM   334  C  CB  . THR A 1 35  ? -14.205 -12.931 32.178  1.00 13.64 ? 35  THR A CB  1 
ATOM   335  O  OG1 . THR A 1 35  ? -14.129 -14.289 32.635  1.00 14.99 ? 35  THR A OG1 1 
ATOM   336  C  CG2 . THR A 1 35  ? -13.983 -12.786 30.673  1.00 13.87 ? 35  THR A CG2 1 
ATOM   337  N  N   . HIS A 1 36  ? -13.032 -12.956 35.161  1.00 15.14 ? 36  HIS A N   1 
ATOM   338  C  CA  . HIS A 1 36  ? -13.327 -13.130 36.610  1.00 15.29 ? 36  HIS A CA  1 
ATOM   339  C  C   . HIS A 1 36  ? -12.868 -11.977 37.424  1.00 15.28 ? 36  HIS A C   1 
ATOM   340  O  O   . HIS A 1 36  ? -13.554 -11.655 38.442  1.00 18.46 ? 36  HIS A O   1 
ATOM   341  C  CB  . HIS A 1 36  ? -12.787 -14.483 37.084  1.00 16.46 ? 36  HIS A CB  1 
ATOM   342  C  CG  . HIS A 1 36  ? -13.620 -15.591 36.545  1.00 20.48 ? 36  HIS A CG  1 
ATOM   343  N  ND1 . HIS A 1 36  ? -13.190 -16.454 35.541  1.00 22.59 ? 36  HIS A ND1 1 
ATOM   344  C  CD2 . HIS A 1 36  ? -14.948 -15.831 36.723  1.00 20.86 ? 36  HIS A CD2 1 
ATOM   345  C  CE1 . HIS A 1 36  ? -14.201 -17.224 35.189  1.00 23.52 ? 36  HIS A CE1 1 
ATOM   346  N  NE2 . HIS A 1 36  ? -15.266 -16.903 35.909  1.00 27.50 ? 36  HIS A NE2 1 
ATOM   347  N  N   A THR A 1 37  ? -11.747 -11.316 37.037  0.50 15.08 ? 37  THR A N   1 
ATOM   348  N  N   B THR A 1 37  ? -11.726 -11.349 37.040  0.50 14.83 ? 37  THR A N   1 
ATOM   349  C  CA  A THR A 1 37  ? -11.198 -10.158 37.790  0.50 14.53 ? 37  THR A CA  1 
ATOM   350  C  CA  B THR A 1 37  ? -11.108 -10.196 37.734  0.50 14.75 ? 37  THR A CA  1 
ATOM   351  C  C   A THR A 1 37  ? -11.608 -8.739  37.276  0.50 14.18 ? 37  THR A C   1 
ATOM   352  C  C   B THR A 1 37  ? -11.780 -8.825  37.363  0.50 14.02 ? 37  THR A C   1 
ATOM   353  O  O   A THR A 1 37  ? -11.229 -7.694  37.877  0.50 13.47 ? 37  THR A O   1 
ATOM   354  O  O   B THR A 1 37  ? -11.777 -7.895  38.168  0.50 15.63 ? 37  THR A O   1 
ATOM   355  C  CB  A THR A 1 37  ? -9.704  -10.242 38.014  0.50 14.86 ? 37  THR A CB  1 
ATOM   356  C  CB  B THR A 1 37  ? -9.594  -10.148 37.486  0.50 15.21 ? 37  THR A CB  1 
ATOM   357  O  OG1 A THR A 1 37  ? -8.978  -10.111 36.792  0.50 15.39 ? 37  THR A OG1 1 
ATOM   358  O  OG1 B THR A 1 37  ? -9.013  -11.366 37.918  0.50 17.93 ? 37  THR A OG1 1 
ATOM   359  C  CG2 A THR A 1 37  ? -9.342  -11.546 38.661  0.50 13.79 ? 37  THR A CG2 1 
ATOM   360  C  CG2 B THR A 1 37  ? -8.897  -8.945  38.232  0.50 14.00 ? 37  THR A CG2 1 
ATOM   361  N  N   . ALA A 1 38  ? -12.322 -8.726  36.151  1.00 13.71 ? 38  ALA A N   1 
ATOM   362  C  CA  . ALA A 1 38  ? -12.972 -7.464  35.700  1.00 12.03 ? 38  ALA A CA  1 
ATOM   363  C  C   . ALA A 1 38  ? -14.048 -7.119  36.729  1.00 16.05 ? 38  ALA A C   1 
ATOM   364  O  O   . ALA A 1 38  ? -14.770 -8.001  37.178  1.00 20.82 ? 38  ALA A O   1 
ATOM   365  C  CB  . ALA A 1 38  ? -13.563 -7.591  34.284  1.00 12.46 ? 38  ALA A CB  1 
ATOM   366  N  N   . LYS A 1 39  ? -14.085 -5.867  37.143  1.00 15.30 ? 39  LYS A N   1 
ATOM   367  C  CA  . LYS A 1 39  ? -15.058 -5.448  38.197  1.00 16.78 ? 39  LYS A CA  1 
ATOM   368  C  C   . LYS A 1 39  ? -16.367 -4.962  37.482  1.00 14.57 ? 39  LYS A C   1 
ATOM   369  O  O   . LYS A 1 39  ? -16.288 -4.022  36.713  1.00 13.22 ? 39  LYS A O   1 
ATOM   370  C  CB  . LYS A 1 39  ? -14.365 -4.262  38.876  1.00 19.52 ? 39  LYS A CB  1 
ATOM   371  C  CG  . LYS A 1 39  ? -15.147 -3.484  39.875  1.00 23.48 ? 39  LYS A CG  1 
ATOM   372  C  CD  . LYS A 1 39  ? -15.301 -4.210  41.253  1.00 21.22 ? 39  LYS A CD  1 
ATOM   373  C  CE  . LYS A 1 39  ? -16.131 -3.340  42.142  1.00 25.55 ? 39  LYS A CE  1 
ATOM   374  N  NZ  . LYS A 1 39  ? -16.374 -4.064  43.351  1.00 25.67 ? 39  LYS A NZ  1 
ATOM   375  N  N   . TYR A 1 40  ? -17.534 -5.497  37.831  1.00 15.57 ? 40  TYR A N   1 
ATOM   376  C  CA  . TYR A 1 40  ? -18.754 -4.866  37.419  1.00 15.70 ? 40  TYR A CA  1 
ATOM   377  C  C   . TYR A 1 40  ? -18.837 -3.448  38.040  1.00 15.82 ? 40  TYR A C   1 
ATOM   378  O  O   . TYR A 1 40  ? -18.647 -3.252  39.290  1.00 15.73 ? 40  TYR A O   1 
ATOM   379  C  CB  . TYR A 1 40  ? -19.992 -5.746  37.810  1.00 18.73 ? 40  TYR A CB  1 
ATOM   380  C  CG  . TYR A 1 40  ? -21.283 -5.050  37.711  1.00 20.16 ? 40  TYR A CG  1 
ATOM   381  C  CD1 . TYR A 1 40  ? -21.725 -4.544  36.464  1.00 23.97 ? 40  TYR A CD1 1 
ATOM   382  C  CD2 . TYR A 1 40  ? -22.126 -4.905  38.841  1.00 25.25 ? 40  TYR A CD2 1 
ATOM   383  C  CE1 . TYR A 1 40  ? -22.939 -3.872  36.319  1.00 22.21 ? 40  TYR A CE1 1 
ATOM   384  C  CE2 . TYR A 1 40  ? -23.369 -4.226  38.719  1.00 24.65 ? 40  TYR A CE2 1 
ATOM   385  C  CZ  . TYR A 1 40  ? -23.774 -3.726  37.461  1.00 24.25 ? 40  TYR A CZ  1 
ATOM   386  O  OH  . TYR A 1 40  ? -24.955 -3.028  37.305  1.00 27.31 ? 40  TYR A OH  1 
ATOM   387  N  N   . ASP A 1 41  ? -19.200 -2.443  37.208  1.00 13.54 ? 41  ASP A N   1 
ATOM   388  C  CA  . ASP A 1 41  ? -19.293 -1.055  37.722  1.00 15.07 ? 41  ASP A CA  1 
ATOM   389  C  C   . ASP A 1 41  ? -20.683 -0.551  37.409  1.00 18.14 ? 41  ASP A C   1 
ATOM   390  O  O   . ASP A 1 41  ? -21.029 -0.293  36.250  1.00 16.00 ? 41  ASP A O   1 
ATOM   391  C  CB  . ASP A 1 41  ? -18.225 -0.180  37.054  1.00 17.62 ? 41  ASP A CB  1 
ATOM   392  C  CG  . ASP A 1 41  ? -18.269 1.247   37.517  1.00 20.85 ? 41  ASP A CG  1 
ATOM   393  O  OD1 . ASP A 1 41  ? -19.211 1.657   38.221  1.00 21.44 ? 41  ASP A OD1 1 
ATOM   394  O  OD2 . ASP A 1 41  ? -17.287 1.935   37.176  1.00 24.90 ? 41  ASP A OD2 1 
ATOM   395  N  N   . PRO A 1 42  ? -21.532 -0.502  38.459  1.00 20.06 ? 42  PRO A N   1 
ATOM   396  C  CA  . PRO A 1 42  ? -22.907 -0.054  38.226  1.00 20.95 ? 42  PRO A CA  1 
ATOM   397  C  C   . PRO A 1 42  ? -22.992 1.380   37.782  1.00 21.36 ? 42  PRO A C   1 
ATOM   398  O  O   . PRO A 1 42  ? -24.078 1.817   37.326  1.00 24.92 ? 42  PRO A O   1 
ATOM   399  C  CB  . PRO A 1 42  ? -23.564 -0.251  39.614  1.00 22.14 ? 42  PRO A CB  1 
ATOM   400  C  CG  . PRO A 1 42  ? -22.436 -0.121  40.568  1.00 21.88 ? 42  PRO A CG  1 
ATOM   401  C  CD  . PRO A 1 42  ? -21.352 -0.916  39.873  1.00 21.06 ? 42  PRO A CD  1 
ATOM   402  N  N   . SER A 1 43  ? -21.942 2.150   38.015  1.00 20.22 ? 43  SER A N   1 
ATOM   403  C  CA  . SER A 1 43  ? -21.947 3.556   37.570  1.00 23.08 ? 43  SER A CA  1 
ATOM   404  C  C   . SER A 1 43  ? -21.706 3.739   36.048  1.00 21.39 ? 43  SER A C   1 
ATOM   405  O  O   . SER A 1 43  ? -21.764 4.899   35.507  1.00 24.37 ? 43  SER A O   1 
ATOM   406  C  CB  . SER A 1 43  ? -20.925 4.412   38.334  1.00 23.70 ? 43  SER A CB  1 
ATOM   407  O  OG  . SER A 1 43  ? -19.631 4.231   37.853  1.00 26.60 ? 43  SER A OG  1 
ATOM   408  N  N   . LEU A 1 44  ? -21.372 2.632   35.360  1.00 19.40 ? 44  LEU A N   1 
ATOM   409  C  CA  . LEU A 1 44  ? -21.152 2.730   33.876  1.00 18.05 ? 44  LEU A CA  1 
ATOM   410  C  C   . LEU A 1 44  ? -22.477 2.888   33.170  1.00 19.30 ? 44  LEU A C   1 
ATOM   411  O  O   . LEU A 1 44  ? -23.471 2.301   33.571  1.00 20.91 ? 44  LEU A O   1 
ATOM   412  C  CB  . LEU A 1 44  ? -20.396 1.483   33.338  1.00 17.53 ? 44  LEU A CB  1 
ATOM   413  C  CG  . LEU A 1 44  ? -18.910 1.432   33.632  1.00 14.70 ? 44  LEU A CG  1 
ATOM   414  C  CD1 . LEU A 1 44  ? -18.401 0.076   33.226  1.00 13.59 ? 44  LEU A CD1 1 
ATOM   415  C  CD2 . LEU A 1 44  ? -18.111 2.499   32.932  1.00 18.00 ? 44  LEU A CD2 1 
ATOM   416  N  N   . LYS A 1 45  ? -22.522 3.689   32.112  1.00 17.89 ? 45  LYS A N   1 
ATOM   417  C  CA  . LYS A 1 45  ? -23.819 3.887   31.336  1.00 18.20 ? 45  LYS A CA  1 
ATOM   418  C  C   . LYS A 1 45  ? -23.851 3.013   30.136  1.00 16.40 ? 45  LYS A C   1 
ATOM   419  O  O   . LYS A 1 45  ? -22.810 2.480   29.714  1.00 17.00 ? 45  LYS A O   1 
ATOM   420  C  CB  . LYS A 1 45  ? -23.924 5.320   30.872  1.00 19.36 ? 45  LYS A CB  1 
ATOM   421  C  CG  . LYS A 1 45  ? -23.710 6.317   32.023  1.00 22.97 ? 45  LYS A CG  1 
ATOM   422  C  CD  . LYS A 1 45  ? -23.614 7.729   31.496  1.00 25.78 ? 45  LYS A CD  1 
ATOM   423  C  CE  . LYS A 1 45  ? -23.232 8.716   32.593  0.01 24.89 ? 45  LYS A CE  1 
ATOM   424  N  NZ  . LYS A 1 45  ? -24.303 8.886   33.616  0.01 24.79 ? 45  LYS A NZ  1 
ATOM   425  N  N   . PRO A 1 46  ? -25.057 2.748   29.645  1.00 15.01 ? 46  PRO A N   1 
ATOM   426  C  CA  . PRO A 1 46  ? -25.188 2.057   28.334  1.00 14.61 ? 46  PRO A CA  1 
ATOM   427  C  C   . PRO A 1 46  ? -24.388 2.866   27.307  1.00 13.85 ? 46  PRO A C   1 
ATOM   428  O  O   . PRO A 1 46  ? -24.300 4.103   27.391  1.00 13.88 ? 46  PRO A O   1 
ATOM   429  C  CB  . PRO A 1 46  ? -26.687 2.145   28.001  1.00 14.65 ? 46  PRO A CB  1 
ATOM   430  C  CG  . PRO A 1 46  ? -27.378 2.419   29.341  1.00 16.19 ? 46  PRO A CG  1 
ATOM   431  C  CD  . PRO A 1 46  ? -26.371 3.133   30.258  1.00 16.05 ? 46  PRO A CD  1 
ATOM   432  N  N   . LEU A 1 47  ? -23.761 2.147   26.366  1.00 14.65 ? 47  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 47  ? -23.043 2.798   25.307  1.00 12.38 ? 47  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 47  ? -24.058 3.355   24.301  1.00 14.67 ? 47  LEU A C   1 
ATOM   435  O  O   . LEU A 1 47  ? -25.049 2.645   24.011  1.00 17.58 ? 47  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 47  ? -22.268 1.721   24.543  1.00 16.37 ? 47  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 47  ? -21.174 2.086   23.647  1.00 16.77 ? 47  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 47  ? -20.104 2.957   24.448  1.00 19.41 ? 47  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 47  ? -20.545 0.771   23.157  1.00 17.55 ? 47  LEU A CD2 1 
ATOM   440  N  N   . SER A 1 48  ? -23.788 4.553   23.809  1.00 12.15 ? 48  SER A N   1 
ATOM   441  C  CA  . SER A 1 48  ? -24.663 5.230   22.826  1.00 12.57 ? 48  SER A CA  1 
ATOM   442  C  C   . SER A 1 48  ? -23.899 5.288   21.488  1.00 12.05 ? 48  SER A C   1 
ATOM   443  O  O   . SER A 1 48  ? -22.879 6.000   21.314  1.00 12.88 ? 48  SER A O   1 
ATOM   444  C  CB  . SER A 1 48  ? -25.012 6.678   23.238  1.00 14.53 ? 48  SER A CB  1 
ATOM   445  O  OG  . SER A 1 48  ? -25.598 7.366   22.118  1.00 18.14 ? 48  SER A OG  1 
ATOM   446  N  N   . VAL A 1 49  ? -24.343 4.496   20.553  1.00 13.60 ? 49  VAL A N   1 
ATOM   447  C  CA  . VAL A 1 49  ? -23.757 4.450   19.206  1.00 14.06 ? 49  VAL A CA  1 
ATOM   448  C  C   . VAL A 1 49  ? -24.761 5.057   18.190  1.00 15.99 ? 49  VAL A C   1 
ATOM   449  O  O   . VAL A 1 49  ? -25.879 4.549   18.011  1.00 17.09 ? 49  VAL A O   1 
ATOM   450  C  CB  . VAL A 1 49  ? -23.503 2.971   18.806  1.00 16.41 ? 49  VAL A CB  1 
ATOM   451  C  CG1 . VAL A 1 49  ? -22.908 2.919   17.410  1.00 19.50 ? 49  VAL A CG1 1 
ATOM   452  C  CG2 . VAL A 1 49  ? -22.640 2.280   19.850  1.00 15.28 ? 49  VAL A CG2 1 
ATOM   453  N  N   . SER A 1 50  ? -24.402 6.183   17.609  1.00 15.11 ? 50  SER A N   1 
ATOM   454  C  CA  . SER A 1 50  ? -25.336 6.860   16.715  1.00 15.87 ? 50  SER A CA  1 
ATOM   455  C  C   . SER A 1 50  ? -24.694 6.943   15.357  1.00 16.50 ? 50  SER A C   1 
ATOM   456  O  O   . SER A 1 50  ? -24.008 7.894   15.059  1.00 16.10 ? 50  SER A O   1 
ATOM   457  C  CB  . SER A 1 50  ? -25.675 8.292   17.224  1.00 18.19 ? 50  SER A CB  1 
ATOM   458  O  OG  . SER A 1 50  ? -26.289 8.222   18.495  1.00 24.81 ? 50  SER A OG  1 
ATOM   459  N  N   . TYR A 1 51  ? -24.923 5.920   14.520  1.00 16.65 ? 51  TYR A N   1 
ATOM   460  C  CA  . TYR A 1 51  ? -24.329 5.796   13.212  1.00 14.92 ? 51  TYR A CA  1 
ATOM   461  C  C   . TYR A 1 51  ? -25.313 6.053   12.031  1.00 16.76 ? 51  TYR A C   1 
ATOM   462  O  O   . TYR A 1 51  ? -24.899 5.899   10.892  1.00 17.08 ? 51  TYR A O   1 
ATOM   463  C  CB  . TYR A 1 51  ? -23.638 4.427   13.018  1.00 14.48 ? 51  TYR A CB  1 
ATOM   464  C  CG  . TYR A 1 51  ? -22.388 4.150   13.813  1.00 11.84 ? 51  TYR A CG  1 
ATOM   465  C  CD1 . TYR A 1 51  ? -21.658 5.184   14.485  1.00 12.79 ? 51  TYR A CD1 1 
ATOM   466  C  CD2 . TYR A 1 51  ? -21.911 2.821   13.902  1.00 10.10 ? 51  TYR A CD2 1 
ATOM   467  C  CE1 . TYR A 1 51  ? -20.453 4.858   15.173  1.00 11.10 ? 51  TYR A CE1 1 
ATOM   468  C  CE2 . TYR A 1 51  ? -20.737 2.530   14.584  1.00 10.79 ? 51  TYR A CE2 1 
ATOM   469  C  CZ  . TYR A 1 51  ? -20.037 3.538   15.246  1.00 10.94 ? 51  TYR A CZ  1 
ATOM   470  O  OH  . TYR A 1 51  ? -18.872 3.210   15.893  1.00 11.37 ? 51  TYR A OH  1 
ATOM   471  N  N   A ASP A 1 52  ? -26.543 6.469   12.350  0.50 18.05 ? 52  ASP A N   1 
ATOM   472  N  N   B ASP A 1 52  ? -26.569 6.410   12.325  0.50 18.33 ? 52  ASP A N   1 
ATOM   473  C  CA  A ASP A 1 52  ? -27.608 6.742   11.351  0.50 19.34 ? 52  ASP A CA  1 
ATOM   474  C  CA  B ASP A 1 52  ? -27.606 6.757   11.299  0.50 19.24 ? 52  ASP A CA  1 
ATOM   475  C  C   A ASP A 1 52  ? -27.246 7.735   10.255  0.50 20.02 ? 52  ASP A C   1 
ATOM   476  C  C   B ASP A 1 52  ? -27.026 7.588   10.153  0.50 20.95 ? 52  ASP A C   1 
ATOM   477  O  O   A ASP A 1 52  ? -27.765 7.621   9.141   0.50 19.11 ? 52  ASP A O   1 
ATOM   478  O  O   B ASP A 1 52  ? -27.186 7.252   8.940   0.50 20.51 ? 52  ASP A O   1 
ATOM   479  C  CB  A ASP A 1 52  ? -28.921 7.131   12.043  0.50 19.85 ? 52  ASP A CB  1 
ATOM   480  C  CB  B ASP A 1 52  ? -28.772 7.524   11.965  0.50 21.28 ? 52  ASP A CB  1 
ATOM   481  C  CG  A ASP A 1 52  ? -28.714 8.153   13.171  0.50 22.29 ? 52  ASP A CG  1 
ATOM   482  C  CG  B ASP A 1 52  ? -30.063 7.446   11.187  0.50 24.13 ? 52  ASP A CG  1 
ATOM   483  O  OD1 A ASP A 1 52  ? -27.989 7.889   14.184  0.50 23.78 ? 52  ASP A OD1 1 
ATOM   484  O  OD1 B ASP A 1 52  ? -30.083 6.869   10.071  0.50 27.20 ? 52  ASP A OD1 1 
ATOM   485  O  OD2 A ASP A 1 52  ? -29.328 9.222   13.066  0.50 27.20 ? 52  ASP A OD2 1 
ATOM   486  O  OD2 B ASP A 1 52  ? -31.102 7.948   11.696  0.50 27.54 ? 52  ASP A OD2 1 
ATOM   487  N  N   . GLN A 1 53  ? -26.323 8.652   10.518  1.00 20.56 ? 53  GLN A N   1 
ATOM   488  C  CA  . GLN A 1 53  ? -25.867 9.585   9.440   1.00 21.24 ? 53  GLN A CA  1 
ATOM   489  C  C   . GLN A 1 53  ? -24.422 9.422   9.002   1.00 19.35 ? 53  GLN A C   1 
ATOM   490  O  O   . GLN A 1 53  ? -23.832 10.345  8.418   1.00 18.93 ? 53  GLN A O   1 
ATOM   491  C  CB  . GLN A 1 53  ? -26.089 11.031  9.868   1.00 23.77 ? 53  GLN A CB  1 
ATOM   492  C  CG  . GLN A 1 53  ? -27.531 11.264  10.320  1.00 30.38 ? 53  GLN A CG  1 
ATOM   493  C  CD  . GLN A 1 53  ? -28.509 11.182  9.189   1.00 36.09 ? 53  GLN A CD  1 
ATOM   494  O  OE1 . GLN A 1 53  ? -29.552 11.789  9.296   1.00 44.39 ? 53  GLN A OE1 1 
ATOM   495  N  NE2 . GLN A 1 53  ? -28.198 10.453  8.120   0.01 37.12 ? 53  GLN A NE2 1 
ATOM   496  N  N   . ALA A 1 54  ? -23.856 8.251   9.240   1.00 17.73 ? 54  ALA A N   1 
ATOM   497  C  CA  . ALA A 1 54  ? -22.464 8.047   8.880   1.00 15.27 ? 54  ALA A CA  1 
ATOM   498  C  C   . ALA A 1 54  ? -22.229 8.180   7.335   1.00 16.07 ? 54  ALA A C   1 
ATOM   499  O  O   . ALA A 1 54  ? -23.107 7.782   6.508   1.00 19.84 ? 54  ALA A O   1 
ATOM   500  C  CB  . ALA A 1 54  ? -21.989 6.665   9.392   1.00 17.19 ? 54  ALA A CB  1 
ATOM   501  N  N   . THR A 1 55  ? -21.125 8.814   6.936   1.00 13.60 ? 55  THR A N   1 
ATOM   502  C  CA  . THR A 1 55  ? -20.768 8.977   5.535   1.00 14.26 ? 55  THR A CA  1 
ATOM   503  C  C   . THR A 1 55  ? -19.430 8.366   5.279   1.00 12.42 ? 55  THR A C   1 
ATOM   504  O  O   . THR A 1 55  ? -18.401 8.988   5.560   1.00 12.35 ? 55  THR A O   1 
ATOM   505  C  CB  . THR A 1 55  ? -20.660 10.537  5.172   1.00 17.28 ? 55  THR A CB  1 
ATOM   506  O  OG1 . THR A 1 55  ? -21.920 11.124  5.247   1.00 20.15 ? 55  THR A OG1 1 
ATOM   507  C  CG2 . THR A 1 55  ? -20.195 10.634  3.663   1.00 18.16 ? 55  THR A CG2 1 
ATOM   508  N  N   . SER A 1 56  ? -19.419 7.121   4.794   1.00 13.68 ? 56  SER A N   1 
ATOM   509  C  CA  . SER A 1 56  ? -18.142 6.560   4.441   1.00 14.84 ? 56  SER A CA  1 
ATOM   510  C  C   . SER A 1 56  ? -17.693 7.217   3.137   1.00 15.47 ? 56  SER A C   1 
ATOM   511  O  O   . SER A 1 56  ? -18.550 7.681   2.340   1.00 16.37 ? 56  SER A O   1 
ATOM   512  C  CB  . SER A 1 56  ? -18.244 5.023   4.254   1.00 14.41 ? 56  SER A CB  1 
ATOM   513  O  OG  . SER A 1 56  ? -19.067 4.683   3.091   1.00 16.84 ? 56  SER A OG  1 
ATOM   514  N  N   . LEU A 1 57  ? -16.397 7.262   2.905   1.00 13.02 ? 57  LEU A N   1 
ATOM   515  C  CA  . LEU A 1 57  ? -15.854 7.906   1.695   1.00 16.03 ? 57  LEU A CA  1 
ATOM   516  C  C   . LEU A 1 57  ? -15.033 6.966   0.803   1.00 15.01 ? 57  LEU A C   1 
ATOM   517  O  O   . LEU A 1 57  ? -15.090 7.020   -0.443  1.00 15.96 ? 57  LEU A O   1 
ATOM   518  C  CB  . LEU A 1 57  ? -14.893 9.024   2.059   1.00 17.93 ? 57  LEU A CB  1 
ATOM   519  C  CG  . LEU A 1 57  ? -15.698 10.209  2.666   1.00 20.19 ? 57  LEU A CG  1 
ATOM   520  C  CD1 . LEU A 1 57  ? -14.711 11.246  3.204   1.00 25.17 ? 57  LEU A CD1 1 
ATOM   521  C  CD2 . LEU A 1 57  ? -16.792 10.878  1.760   1.00 22.16 ? 57  LEU A CD2 1 
ATOM   522  N  N   . ARG A 1 58  ? -14.150 6.206   1.423   1.00 15.13 ? 58  ARG A N   1 
ATOM   523  C  CA  . ARG A 1 58  ? -13.065 5.514   0.708   1.00 13.96 ? 58  ARG A CA  1 
ATOM   524  C  C   . ARG A 1 58  ? -12.556 4.356   1.550   1.00 12.96 ? 58  ARG A C   1 
ATOM   525  O  O   . ARG A 1 58  ? -12.691 4.345   2.786   1.00 13.79 ? 58  ARG A O   1 
ATOM   526  C  CB  . ARG A 1 58  ? -11.882 6.502   0.590   1.00 16.11 ? 58  ARG A CB  1 
ATOM   527  C  CG  . ARG A 1 58  ? -10.868 6.120   -0.419  1.00 16.90 ? 58  ARG A CG  1 
ATOM   528  C  CD  . ARG A 1 58  ? -9.872  7.235   -0.525  1.00 19.11 ? 58  ARG A CD  1 
ATOM   529  N  NE  . ARG A 1 58  ? -9.019  7.212   0.655   1.00 14.55 ? 58  ARG A NE  1 
ATOM   530  C  CZ  . ARG A 1 58  ? -7.709  7.392   0.642   1.00 13.68 ? 58  ARG A CZ  1 
ATOM   531  N  NH1 . ARG A 1 58  ? -7.065  7.632   -0.495  1.00 16.87 ? 58  ARG A NH1 1 
ATOM   532  N  NH2 . ARG A 1 58  ? -7.037  7.329   1.779   1.00 15.82 ? 58  ARG A NH2 1 
ATOM   533  N  N   . ILE A 1 59  ? -11.949 3.373   0.866   1.00 12.48 ? 59  ILE A N   1 
ATOM   534  C  CA  . ILE A 1 59  ? -11.251 2.261   1.547   1.00 12.74 ? 59  ILE A CA  1 
ATOM   535  C  C   . ILE A 1 59  ? -9.805  2.248   1.015   1.00 11.76 ? 59  ILE A C   1 
ATOM   536  O  O   . ILE A 1 59  ? -9.539  2.430   -0.192  1.00 13.72 ? 59  ILE A O   1 
ATOM   537  C  CB  . ILE A 1 59  ? -12.006 0.918   1.314   1.00 12.42 ? 59  ILE A CB  1 
ATOM   538  C  CG1 . ILE A 1 59  ? -11.443 -0.219  2.193   1.00 12.94 ? 59  ILE A CG1 1 
ATOM   539  C  CG2 . ILE A 1 59  ? -11.984 0.514   -0.252  1.00 14.39 ? 59  ILE A CG2 1 
ATOM   540  C  CD1 . ILE A 1 59  ? -12.317 -1.519  2.028   1.00 13.20 ? 59  ILE A CD1 1 
ATOM   541  N  N   . LEU A 1 60  ? -8.851  1.999   1.941   1.00 12.62 ? 60  LEU A N   1 
ATOM   542  C  CA  . LEU A 1 60  ? -7.454  2.159   1.684   1.00 11.84 ? 60  LEU A CA  1 
ATOM   543  C  C   . LEU A 1 60  ? -6.682  0.929   2.255   1.00 12.13 ? 60  LEU A C   1 
ATOM   544  O  O   . LEU A 1 60  ? -6.883  0.580   3.420   1.00 11.00 ? 60  LEU A O   1 
ATOM   545  C  CB  . LEU A 1 60  ? -6.920  3.457   2.459   1.00 14.62 ? 60  LEU A CB  1 
ATOM   546  C  CG  . LEU A 1 60  ? -5.373  3.581   2.367   1.00 15.30 ? 60  LEU A CG  1 
ATOM   547  C  CD1 . LEU A 1 60  ? -4.862  3.843   0.864   1.00 15.46 ? 60  LEU A CD1 1 
ATOM   548  C  CD2 . LEU A 1 60  ? -4.813  4.652   3.347   1.00 14.47 ? 60  LEU A CD2 1 
ATOM   549  N  N   . ASN A 1 61  ? -5.812  0.342   1.431   1.00 11.40 ? 61  ASN A N   1 
ATOM   550  C  CA  . ASN A 1 61  ? -4.836  -0.625  1.917   1.00 11.36 ? 61  ASN A CA  1 
ATOM   551  C  C   . ASN A 1 61  ? -3.599  0.211   2.266   1.00 12.87 ? 61  ASN A C   1 
ATOM   552  O  O   . ASN A 1 61  ? -2.941  0.779   1.395   1.00 14.66 ? 61  ASN A O   1 
ATOM   553  C  CB  . ASN A 1 61  ? -4.517  -1.658  0.833   1.00 12.52 ? 61  ASN A CB  1 
ATOM   554  C  CG  . ASN A 1 61  ? -3.433  -2.684  1.250   1.00 13.04 ? 61  ASN A CG  1 
ATOM   555  O  OD1 . ASN A 1 61  ? -2.544  -2.393  2.101   1.00 13.63 ? 61  ASN A OD1 1 
ATOM   556  N  ND2 . ASN A 1 61  ? -3.463  -3.907  0.644   1.00 15.23 ? 61  ASN A ND2 1 
ATOM   557  N  N   . ASN A 1 62  ? -3.324  0.275   3.574   1.00 12.78 ? 62  ASN A N   1 
ATOM   558  C  CA  . ASN A 1 62  ? -2.253  1.135   4.065   1.00 11.88 ? 62  ASN A CA  1 
ATOM   559  C  C   . ASN A 1 62  ? -0.938  0.346   4.288   1.00 13.53 ? 62  ASN A C   1 
ATOM   560  O  O   . ASN A 1 62  ? 0.080   0.845   4.918   1.00 18.79 ? 62  ASN A O   1 
ATOM   561  C  CB  . ASN A 1 62  ? -2.619  1.934   5.336   1.00 14.19 ? 62  ASN A CB  1 
ATOM   562  C  CG  . ASN A 1 62  ? -2.731  0.987   6.556   1.00 13.33 ? 62  ASN A CG  1 
ATOM   563  O  OD1 . ASN A 1 62  ? -2.510  -0.251  6.482   1.00 12.59 ? 62  ASN A OD1 1 
ATOM   564  N  ND2 . ASN A 1 62  ? -2.932  1.581   7.716   1.00 17.94 ? 62  ASN A ND2 1 
ATOM   565  N  N   . GLY A 1 63  ? -0.894  -0.906  3.809   1.00 13.32 ? 63  GLY A N   1 
ATOM   566  C  CA  . GLY A 1 63  ? 0.229   -1.740  4.014   1.00 11.83 ? 63  GLY A CA  1 
ATOM   567  C  C   . GLY A 1 63  ? 0.288   -2.551  5.318   1.00 13.83 ? 63  GLY A C   1 
ATOM   568  O  O   . GLY A 1 63  ? 1.152   -3.419  5.521   1.00 12.45 ? 63  GLY A O   1 
ATOM   569  N  N   . HIS A 1 64  ? -0.686  -2.283  6.190   1.00 11.09 ? 64  HIS A N   1 
ATOM   570  C  CA  . HIS A 1 64  ? -0.773  -2.987  7.546   1.00 11.97 ? 64  HIS A CA  1 
ATOM   571  C  C   . HIS A 1 64  ? -2.130  -3.626  7.682   1.00 11.72 ? 64  HIS A C   1 
ATOM   572  O  O   . HIS A 1 64  ? -2.232  -4.755  8.233   1.00 15.04 ? 64  HIS A O   1 
ATOM   573  C  CB  . HIS A 1 64  ? -0.559  -1.989  8.694   1.00 14.02 ? 64  HIS A CB  1 
ATOM   574  C  CG  . HIS A 1 64  ? 0.739   -1.242  8.537   1.00 17.14 ? 64  HIS A CG  1 
ATOM   575  N  ND1 . HIS A 1 64  ? 1.967   -1.885  8.625   1.00 17.50 ? 64  HIS A ND1 1 
ATOM   576  C  CD2 . HIS A 1 64  ? 1.011   0.061   8.307   1.00 16.73 ? 64  HIS A CD2 1 
ATOM   577  C  CE1 . HIS A 1 64  ? 2.950   -1.011  8.473   1.00 19.71 ? 64  HIS A CE1 1 
ATOM   578  N  NE2 . HIS A 1 64  ? 2.399   0.181   8.285   1.00 20.03 ? 64  HIS A NE2 1 
ATOM   579  N  N   . ALA A 1 65  ? -3.157  -2.988  7.146   1.00 9.94  ? 65  ALA A N   1 
ATOM   580  C  CA  . ALA A 1 65  ? -4.554  -3.421  7.222   1.00 10.86 ? 65  ALA A CA  1 
ATOM   581  C  C   . ALA A 1 65  ? -5.302  -2.675  6.068   1.00 9.14  ? 65  ALA A C   1 
ATOM   582  O  O   . ALA A 1 65  ? -4.627  -2.003  5.200   1.00 11.29 ? 65  ALA A O   1 
ATOM   583  C  CB  . ALA A 1 65  ? -5.237  -3.139  8.625   1.00 9.58  ? 65  ALA A CB  1 
ATOM   584  N  N   . PHE A 1 66  ? -6.623  -2.759  6.098   1.00 9.74  ? 66  PHE A N   1 
ATOM   585  C  CA  . PHE A 1 66  ? -7.369  -1.761  5.262   1.00 10.25 ? 66  PHE A CA  1 
ATOM   586  C  C   . PHE A 1 66  ? -8.209  -0.862  6.151   1.00 10.10 ? 66  PHE A C   1 
ATOM   587  O  O   . PHE A 1 66  ? -8.855  -1.376  7.128   1.00 9.85  ? 66  PHE A O   1 
ATOM   588  C  CB  . PHE A 1 66  ? -8.197  -2.437  4.133   1.00 9.70  ? 66  PHE A CB  1 
ATOM   589  C  CG  . PHE A 1 66  ? -9.274  -3.404  4.674   1.00 10.45 ? 66  PHE A CG  1 
ATOM   590  C  CD1 . PHE A 1 66  ? -10.538 -2.936  5.053   1.00 12.64 ? 66  PHE A CD1 1 
ATOM   591  C  CD2 . PHE A 1 66  ? -9.027  -4.792  4.807   1.00 10.27 ? 66  PHE A CD2 1 
ATOM   592  C  CE1 . PHE A 1 66  ? -11.514 -3.801  5.538   1.00 11.46 ? 66  PHE A CE1 1 
ATOM   593  C  CE2 . PHE A 1 66  ? -10.012 -5.663  5.362   1.00 10.58 ? 66  PHE A CE2 1 
ATOM   594  C  CZ  . PHE A 1 66  ? -11.234 -5.182  5.674   1.00 11.48 ? 66  PHE A CZ  1 
ATOM   595  N  N   . ASN A 1 67  ? -8.308  0.429   5.774   1.00 9.00  ? 67  ASN A N   1 
ATOM   596  C  CA  . ASN A 1 67  ? -9.152  1.381   6.562   1.00 9.35  ? 67  ASN A CA  1 
ATOM   597  C  C   . ASN A 1 67  ? -10.373 1.800   5.740   1.00 10.07 ? 67  ASN A C   1 
ATOM   598  O  O   . ASN A 1 67  ? -10.229 2.193   4.577   1.00 11.52 ? 67  ASN A O   1 
ATOM   599  C  CB  . ASN A 1 67  ? -8.472  2.681   6.959   1.00 10.28 ? 67  ASN A CB  1 
ATOM   600  C  CG  . ASN A 1 67  ? -7.310  2.466   7.863   1.00 11.07 ? 67  ASN A CG  1 
ATOM   601  O  OD1 . ASN A 1 67  ? -7.174  1.400   8.537   1.00 13.23 ? 67  ASN A OD1 1 
ATOM   602  N  ND2 . ASN A 1 67  ? -6.485  3.545   8.006   1.00 15.99 ? 67  ASN A ND2 1 
ATOM   603  N  N   . VAL A 1 68  ? -11.575 1.670   6.328   1.00 9.24  ? 68  VAL A N   1 
ATOM   604  C  CA  . VAL A 1 68  ? -12.743 2.312   5.753   1.00 9.88  ? 68  VAL A CA  1 
ATOM   605  C  C   . VAL A 1 68  ? -12.911 3.675   6.429   1.00 13.18 ? 68  VAL A C   1 
ATOM   606  O  O   . VAL A 1 68  ? -13.054 3.751   7.676   1.00 11.86 ? 68  VAL A O   1 
ATOM   607  C  CB  . VAL A 1 68  ? -14.040 1.421   5.915   1.00 11.07 ? 68  VAL A CB  1 
ATOM   608  C  CG1 . VAL A 1 68  ? -15.314 2.208   5.452   1.00 11.65 ? 68  VAL A CG1 1 
ATOM   609  C  CG2 . VAL A 1 68  ? -13.887 0.122   5.140   1.00 10.99 ? 68  VAL A CG2 1 
ATOM   610  N  N   . GLU A 1 69  ? -12.858 4.708   5.595   1.00 12.81 ? 69  GLU A N   1 
ATOM   611  C  CA  . GLU A 1 69  ? -12.728 6.056   6.158   1.00 13.01 ? 69  GLU A CA  1 
ATOM   612  C  C   . GLU A 1 69  ? -14.036 6.787   6.081   1.00 15.27 ? 69  GLU A C   1 
ATOM   613  O  O   . GLU A 1 69  ? -14.819 6.574   5.074   1.00 16.49 ? 69  GLU A O   1 
ATOM   614  C  CB  . GLU A 1 69  ? -11.847 6.861   5.239   1.00 15.72 ? 69  GLU A CB  1 
ATOM   615  C  CG  . GLU A 1 69  ? -10.437 6.300   5.247   1.00 13.11 ? 69  GLU A CG  1 
ATOM   616  C  CD  . GLU A 1 69  ? -9.628  6.737   4.051   1.00 16.70 ? 69  GLU A CD  1 
ATOM   617  O  OE1 . GLU A 1 69  ? -10.198 7.452   3.157   1.00 16.57 ? 69  GLU A OE1 1 
ATOM   618  O  OE2 . GLU A 1 69  ? -8.452  6.340   3.990   1.00 16.07 ? 69  GLU A OE2 1 
ATOM   619  N  N   . PHE A 1 70  ? -14.255 7.685   7.030   1.00 13.67 ? 70  PHE A N   1 
ATOM   620  C  CA  . PHE A 1 70  ? -15.513 8.419   7.093   1.00 12.28 ? 70  PHE A CA  1 
ATOM   621  C  C   . PHE A 1 70  ? -15.292 9.917   7.032   1.00 12.18 ? 70  PHE A C   1 
ATOM   622  O  O   . PHE A 1 70  ? -14.231 10.412  7.404   1.00 12.84 ? 70  PHE A O   1 
ATOM   623  C  CB  . PHE A 1 70  ? -16.227 8.055   8.384   1.00 11.34 ? 70  PHE A CB  1 
ATOM   624  C  CG  . PHE A 1 70  ? -16.818 6.675   8.333   1.00 11.14 ? 70  PHE A CG  1 
ATOM   625  C  CD1 . PHE A 1 70  ? -15.970 5.557   8.537   1.00 10.63 ? 70  PHE A CD1 1 
ATOM   626  C  CD2 . PHE A 1 70  ? -18.177 6.521   8.027   1.00 11.64 ? 70  PHE A CD2 1 
ATOM   627  C  CE1 . PHE A 1 70  ? -16.465 4.272   8.450   1.00 13.53 ? 70  PHE A CE1 1 
ATOM   628  C  CE2 . PHE A 1 70  ? -18.709 5.199   7.875   1.00 10.60 ? 70  PHE A CE2 1 
ATOM   629  C  CZ  . PHE A 1 70  ? -17.830 4.072   8.110   1.00 10.91 ? 70  PHE A CZ  1 
ATOM   630  N  N   A ASP A 1 71  ? -16.363 10.613  6.615   0.50 13.60 ? 71  ASP A N   1 
ATOM   631  N  N   B ASP A 1 71  ? -16.316 10.652  6.599   0.50 13.41 ? 71  ASP A N   1 
ATOM   632  C  CA  A ASP A 1 71  ? -16.396 12.076  6.741   0.50 13.19 ? 71  ASP A CA  1 
ATOM   633  C  CA  B ASP A 1 71  ? -16.191 12.122  6.610   0.50 12.46 ? 71  ASP A CA  1 
ATOM   634  C  C   A ASP A 1 71  ? -16.511 12.351  8.214   0.50 14.34 ? 71  ASP A C   1 
ATOM   635  C  C   B ASP A 1 71  ? -16.534 12.576  8.028   0.50 13.95 ? 71  ASP A C   1 
ATOM   636  O  O   A ASP A 1 71  ? -17.511 12.003  8.830   0.50 16.17 ? 71  ASP A O   1 
ATOM   637  O  O   B ASP A 1 71  ? -17.701 12.524  8.426   0.50 14.58 ? 71  ASP A O   1 
ATOM   638  C  CB  A ASP A 1 71  ? -17.636 12.661  6.052   0.50 13.74 ? 71  ASP A CB  1 
ATOM   639  C  CB  B ASP A 1 71  ? -17.114 12.707  5.503   0.50 12.10 ? 71  ASP A CB  1 
ATOM   640  C  CG  A ASP A 1 71  ? -17.796 14.194  6.295   0.50 13.35 ? 71  ASP A CG  1 
ATOM   641  C  CG  B ASP A 1 71  ? -17.133 14.224  5.460   0.50 12.77 ? 71  ASP A CG  1 
ATOM   642  O  OD1 A ASP A 1 71  ? -16.885 14.819  6.824   0.50 14.26 ? 71  ASP A OD1 1 
ATOM   643  O  OD1 B ASP A 1 71  ? -16.302 14.836  6.132   0.50 16.94 ? 71  ASP A OD1 1 
ATOM   644  O  OD2 A ASP A 1 71  ? -18.861 14.764  6.038   0.50 18.09 ? 71  ASP A OD2 1 
ATOM   645  O  OD2 B ASP A 1 71  ? -17.984 14.765  4.696   0.50 17.71 ? 71  ASP A OD2 1 
ATOM   646  N  N   . ASP A 1 72  ? -15.502 12.980  8.777   1.00 13.59 ? 72  ASP A N   1 
ATOM   647  C  CA  . ASP A 1 72  ? -15.643 13.384  10.187  1.00 14.21 ? 72  ASP A CA  1 
ATOM   648  C  C   . ASP A 1 72  ? -15.623 14.899  10.331  1.00 15.91 ? 72  ASP A C   1 
ATOM   649  O  O   . ASP A 1 72  ? -15.197 15.413  11.364  1.00 17.60 ? 72  ASP A O   1 
ATOM   650  C  CB  . ASP A 1 72  ? -14.544 12.758  11.055  1.00 14.93 ? 72  ASP A CB  1 
ATOM   651  C  CG  . ASP A 1 72  ? -13.162 13.250  10.692  1.00 14.50 ? 72  ASP A CG  1 
ATOM   652  O  OD1 . ASP A 1 72  ? -13.079 14.025  9.651   1.00 16.39 ? 72  ASP A OD1 1 
ATOM   653  O  OD2 . ASP A 1 72  ? -12.210 12.936  11.431  1.00 15.32 ? 72  ASP A OD2 1 
ATOM   654  N  N   . SER A 1 73  ? -16.103 15.599  9.304   1.00 16.67 ? 73  SER A N   1 
ATOM   655  C  CA  . SER A 1 73  ? -16.039 17.112  9.355   1.00 18.02 ? 73  SER A CA  1 
ATOM   656  C  C   . SER A 1 73  ? -17.326 17.690  9.939   1.00 19.80 ? 73  SER A C   1 
ATOM   657  O  O   . SER A 1 73  ? -17.466 18.929  10.052  1.00 18.79 ? 73  SER A O   1 
ATOM   658  C  CB  . SER A 1 73  ? -15.787 17.685  7.978   1.00 20.81 ? 73  SER A CB  1 
ATOM   659  O  OG  . SER A 1 73  ? -16.896 17.466  7.133   1.00 20.07 ? 73  SER A OG  1 
ATOM   660  N  N   . GLN A 1 74  ? -18.265 16.847  10.364  1.00 19.54 ? 74  GLN A N   1 
ATOM   661  C  CA  . GLN A 1 74  ? -19.444 17.330  11.050  1.00 21.84 ? 74  GLN A CA  1 
ATOM   662  C  C   . GLN A 1 74  ? -19.822 16.249  11.997  1.00 20.35 ? 74  GLN A C   1 
ATOM   663  O  O   . GLN A 1 74  ? -19.341 15.149  11.871  1.00 17.77 ? 74  GLN A O   1 
ATOM   664  C  CB  . GLN A 1 74  ? -20.653 17.404  10.091  1.00 22.84 ? 74  GLN A CB  1 
ATOM   665  C  CG  . GLN A 1 74  ? -20.614 18.487  9.050   1.00 27.77 ? 74  GLN A CG  1 
ATOM   666  C  CD  . GLN A 1 74  ? -21.896 18.452  8.302   1.00 32.05 ? 74  GLN A CD  1 
ATOM   667  O  OE1 . GLN A 1 74  ? -21.972 18.027  7.142   1.00 32.26 ? 74  GLN A OE1 1 
ATOM   668  N  NE2 . GLN A 1 74  ? -22.954 18.799  9.005   1.00 37.98 ? 74  GLN A NE2 1 
ATOM   669  N  N   A ASP A 1 75  ? -20.716 16.510  12.984  0.50 21.02 ? 75  ASP A N   1 
ATOM   670  N  N   B ASP A 1 75  ? -20.828 16.632  12.768  0.50 20.26 ? 75  ASP A N   1 
ATOM   671  C  CA  A ASP A 1 75  ? -21.075 15.501  14.015  0.50 20.72 ? 75  ASP A CA  1 
ATOM   672  C  CA  B ASP A 1 75  ? -21.405 15.880  13.774  0.50 19.56 ? 75  ASP A CA  1 
ATOM   673  C  C   A ASP A 1 75  ? -22.168 14.588  13.465  0.50 20.95 ? 75  ASP A C   1 
ATOM   674  C  C   B ASP A 1 75  ? -22.239 14.773  13.021  0.50 20.78 ? 75  ASP A C   1 
ATOM   675  O  O   A ASP A 1 75  ? -23.367 14.896  13.596  0.50 22.58 ? 75  ASP A O   1 
ATOM   676  O  O   B ASP A 1 75  ? -23.351 15.090  12.591  0.50 22.55 ? 75  ASP A O   1 
ATOM   677  C  CB  A ASP A 1 75  ? -21.585 16.130  15.319  0.50 22.70 ? 75  ASP A CB  1 
ATOM   678  C  CB  B ASP A 1 75  ? -22.260 16.885  14.606  0.50 19.86 ? 75  ASP A CB  1 
ATOM   679  C  CG  A ASP A 1 75  ? -20.616 16.020  16.470  0.50 19.02 ? 75  ASP A CG  1 
ATOM   680  C  CG  B ASP A 1 75  ? -22.511 16.385  16.026  0.50 20.93 ? 75  ASP A CG  1 
ATOM   681  O  OD1 A ASP A 1 75  ? -19.841 15.014  16.553  0.50 17.97 ? 75  ASP A OD1 1 
ATOM   682  O  OD1 B ASP A 1 75  ? -22.525 17.169  17.010  0.50 26.77 ? 75  ASP A OD1 1 
ATOM   683  O  OD2 A ASP A 1 75  ? -20.715 16.900  17.363  0.50 24.47 ? 75  ASP A OD2 1 
ATOM   684  O  OD2 B ASP A 1 75  ? -22.587 15.178  16.176  0.50 17.49 ? 75  ASP A OD2 1 
ATOM   685  N  N   . LYS A 1 76  ? -21.721 13.552  12.779  1.00 19.75 ? 76  LYS A N   1 
ATOM   686  C  CA  . LYS A 1 76  ? -22.588 12.505  12.055  1.00 20.79 ? 76  LYS A CA  1 
ATOM   687  C  C   . LYS A 1 76  ? -22.672 11.004  12.471  1.00 22.61 ? 76  LYS A C   1 
ATOM   688  O  O   . LYS A 1 76  ? -23.603 10.230  12.082  1.00 26.34 ? 76  LYS A O   1 
ATOM   689  C  CB  . LYS A 1 76  ? -22.125 12.402  10.611  1.00 20.49 ? 76  LYS A CB  1 
ATOM   690  C  CG  . LYS A 1 76  ? -22.550 13.531  9.649   1.00 24.60 ? 76  LYS A CG  1 
ATOM   691  C  CD  . LYS A 1 76  ? -21.731 13.342  8.314   1.00 22.98 ? 76  LYS A CD  1 
ATOM   692  C  CE  . LYS A 1 76  ? -22.116 14.393  7.239   1.00 25.94 ? 76  LYS A CE  1 
ATOM   693  N  NZ  . LYS A 1 76  ? -21.597 14.129  5.885   1.00 27.02 ? 76  LYS A NZ  1 
ATOM   694  N  N   . ALA A 1 77  ? -21.610 10.533  12.999  1.00 19.94 ? 77  ALA A N   1 
ATOM   695  C  CA  . ALA A 1 77  ? -21.459 9.093   13.412  1.00 15.79 ? 77  ALA A CA  1 
ATOM   696  C  C   . ALA A 1 77  ? -20.717 9.268   14.721  1.00 14.90 ? 77  ALA A C   1 
ATOM   697  O  O   . ALA A 1 77  ? -19.469 9.438   14.704  1.00 17.89 ? 77  ALA A O   1 
ATOM   698  C  CB  . ALA A 1 77  ? -20.576 8.359   12.358  1.00 16.72 ? 77  ALA A CB  1 
ATOM   699  N  N   . VAL A 1 78  ? -21.440 9.244   15.820  1.00 12.64 ? 78  VAL A N   1 
ATOM   700  C  CA  . VAL A 1 78  ? -20.728 9.463   17.132  1.00 13.17 ? 78  VAL A CA  1 
ATOM   701  C  C   . VAL A 1 78  ? -20.978 8.433   18.203  1.00 11.68 ? 78  VAL A C   1 
ATOM   702  O  O   . VAL A 1 78  ? -22.060 7.782   18.270  1.00 13.06 ? 78  VAL A O   1 
ATOM   703  C  CB  . VAL A 1 78  ? -21.060 10.859  17.709  1.00 17.22 ? 78  VAL A CB  1 
ATOM   704  C  CG1 . VAL A 1 78  ? -20.842 11.943  16.653  1.00 19.49 ? 78  VAL A CG1 1 
ATOM   705  C  CG2 . VAL A 1 78  ? -22.496 10.885  18.200  1.00 16.14 ? 78  VAL A CG2 1 
ATOM   706  N  N   . LEU A 1 79  ? -19.951 8.285   19.034  1.00 10.56 ? 79  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 79  ? -20.008 7.401   20.169  1.00 11.04 ? 79  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 79  ? -20.049 8.283   21.410  1.00 10.37 ? 79  LEU A C   1 
ATOM   709  O  O   . LEU A 1 79  ? -19.234 9.229   21.513  1.00 11.84 ? 79  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 79  ? -18.719 6.520   20.130  1.00 11.50 ? 79  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 79  ? -18.563 5.408   21.124  1.00 12.65 ? 79  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 79  ? -19.628 4.348   20.899  1.00 15.08 ? 79  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 79  ? -17.164 4.797   21.126  1.00 10.54 ? 79  LEU A CD2 1 
ATOM   714  N  N   . LYS A 1 80  ? -20.903 7.955   22.378  1.00 12.06 ? 80  LYS A N   1 
ATOM   715  C  CA  . LYS A 1 80  ? -20.880 8.660   23.643  1.00 12.81 ? 80  LYS A CA  1 
ATOM   716  C  C   . LYS A 1 80  ? -21.540 7.730   24.680  1.00 12.11 ? 80  LYS A C   1 
ATOM   717  O  O   . LYS A 1 80  ? -21.797 6.558   24.398  1.00 11.75 ? 80  LYS A O   1 
ATOM   718  C  CB  . LYS A 1 80  ? -21.628 9.947   23.552  1.00 17.94 ? 80  LYS A CB  1 
ATOM   719  C  CG  . LYS A 1 80  ? -23.096 9.798   23.436  1.00 17.25 ? 80  LYS A CG  1 
ATOM   720  C  CD  . LYS A 1 80  ? -23.812 11.242  23.184  1.00 20.15 ? 80  LYS A CD  1 
ATOM   721  C  CE  . LYS A 1 80  ? -25.361 10.989  22.852  1.00 26.03 ? 80  LYS A CE  1 
ATOM   722  N  NZ  . LYS A 1 80  ? -26.180 10.369  23.968  1.00 36.40 ? 80  LYS A NZ  1 
ATOM   723  N  N   . GLY A 1 81  ? -21.630 8.221   25.942  1.00 13.11 ? 81  GLY A N   1 
ATOM   724  C  CA  . GLY A 1 81  ? -22.128 7.361   27.004  1.00 12.73 ? 81  GLY A CA  1 
ATOM   725  C  C   . GLY A 1 81  ? -21.110 6.323   27.326  1.00 14.03 ? 81  GLY A C   1 
ATOM   726  O  O   . GLY A 1 81  ? -19.901 6.552   27.163  1.00 12.92 ? 81  GLY A O   1 
ATOM   727  N  N   . GLY A 1 82  ? -21.569 5.196   27.848  1.00 14.91 ? 82  GLY A N   1 
ATOM   728  C  CA  . GLY A 1 82  ? -20.582 4.183   28.200  1.00 14.83 ? 82  GLY A CA  1 
ATOM   729  C  C   . GLY A 1 82  ? -19.718 4.785   29.332  1.00 13.64 ? 82  GLY A C   1 
ATOM   730  O  O   . GLY A 1 82  ? -20.231 5.544   30.165  1.00 17.40 ? 82  GLY A O   1 
ATOM   731  N  N   . PRO A 1 83  ? -18.367 4.561   29.273  1.00 12.65 ? 83  PRO A N   1 
ATOM   732  C  CA  . PRO A 1 83  ? -17.447 5.203   30.252  1.00 11.38 ? 83  PRO A CA  1 
ATOM   733  C  C   . PRO A 1 83  ? -17.031 6.656   29.850  1.00 13.98 ? 83  PRO A C   1 
ATOM   734  O  O   . PRO A 1 83  ? -16.273 7.275   30.576  1.00 15.77 ? 83  PRO A O   1 
ATOM   735  C  CB  . PRO A 1 83  ? -16.161 4.314   30.111  1.00 14.13 ? 83  PRO A CB  1 
ATOM   736  C  CG  . PRO A 1 83  ? -16.112 4.012   28.624  1.00 11.84 ? 83  PRO A CG  1 
ATOM   737  C  CD  . PRO A 1 83  ? -17.614 3.730   28.283  1.00 11.15 ? 83  PRO A CD  1 
ATOM   738  N  N   . LEU A 1 84  ? -17.539 7.175   28.731  1.00 13.19 ? 84  LEU A N   1 
ATOM   739  C  CA  . LEU A 1 84  ? -16.965 8.389   28.103  1.00 12.89 ? 84  LEU A CA  1 
ATOM   740  C  C   . LEU A 1 84  ? -17.612 9.644   28.711  1.00 15.46 ? 84  LEU A C   1 
ATOM   741  O  O   . LEU A 1 84  ? -18.800 9.663   29.022  1.00 16.06 ? 84  LEU A O   1 
ATOM   742  C  CB  . LEU A 1 84  ? -17.252 8.385   26.606  1.00 11.45 ? 84  LEU A CB  1 
ATOM   743  C  CG  . LEU A 1 84  ? -16.667 7.118   25.933  1.00 9.43  ? 84  LEU A CG  1 
ATOM   744  C  CD1 . LEU A 1 84  ? -17.109 7.055   24.460  1.00 11.96 ? 84  LEU A CD1 1 
ATOM   745  C  CD2 . LEU A 1 84  ? -15.096 7.131   26.049  1.00 11.83 ? 84  LEU A CD2 1 
ATOM   746  N  N   . ASP A 1 85  ? -16.844 10.706  28.718  1.00 15.96 ? 85  ASP A N   1 
ATOM   747  C  CA  . ASP A 1 85  ? -17.319 12.080  28.976  1.00 20.27 ? 85  ASP A CA  1 
ATOM   748  C  C   . ASP A 1 85  ? -17.348 12.693  27.576  1.00 18.76 ? 85  ASP A C   1 
ATOM   749  O  O   . ASP A 1 85  ? -16.364 12.661  26.816  1.00 21.85 ? 85  ASP A O   1 
ATOM   750  C  CB  . ASP A 1 85  ? -16.331 12.833  29.969  1.00 21.69 ? 85  ASP A CB  1 
ATOM   751  C  CG  . ASP A 1 85  ? -16.424 12.352  31.386  1.00 28.01 ? 85  ASP A CG  1 
ATOM   752  O  OD1 . ASP A 1 85  ? -17.526 11.860  31.794  1.00 34.23 ? 85  ASP A OD1 1 
ATOM   753  O  OD2 . ASP A 1 85  ? -15.386 12.506  32.138  1.00 31.46 ? 85  ASP A OD2 1 
ATOM   754  N  N   . GLY A 1 86  ? -18.433 13.326  27.217  1.00 21.06 ? 86  GLY A N   1 
ATOM   755  C  CA  . GLY A 1 86  ? -18.408 13.984  25.957  1.00 18.50 ? 86  GLY A CA  1 
ATOM   756  C  C   . GLY A 1 86  ? -18.597 13.050  24.736  1.00 17.00 ? 86  GLY A C   1 
ATOM   757  O  O   . GLY A 1 86  ? -19.072 11.877  24.840  1.00 21.05 ? 86  GLY A O   1 
ATOM   758  N  N   A THR A 1 87  ? -18.301 13.613  23.562  0.50 14.85 ? 87  THR A N   1 
ATOM   759  N  N   B THR A 1 87  ? -18.214 13.556  23.581  0.50 14.11 ? 87  THR A N   1 
ATOM   760  C  CA  A THR A 1 87  ? -18.708 13.076  22.250  0.50 14.06 ? 87  THR A CA  1 
ATOM   761  C  CA  B THR A 1 87  ? -18.635 12.910  22.353  0.50 12.82 ? 87  THR A CA  1 
ATOM   762  C  C   A THR A 1 87  ? -17.471 12.684  21.478  0.50 11.97 ? 87  THR A C   1 
ATOM   763  C  C   B THR A 1 87  ? -17.512 12.711  21.381  0.50 11.64 ? 87  THR A C   1 
ATOM   764  O  O   A THR A 1 87  ? -16.463 13.408  21.512  0.50 10.14 ? 87  THR A O   1 
ATOM   765  O  O   B THR A 1 87  ? -16.679 13.588  21.123  0.50 10.09 ? 87  THR A O   1 
ATOM   766  C  CB  A THR A 1 87  ? -19.482 14.196  21.395  0.50 15.40 ? 87  THR A CB  1 
ATOM   767  C  CB  B THR A 1 87  ? -19.674 13.765  21.643  0.50 13.46 ? 87  THR A CB  1 
ATOM   768  O  OG1 A THR A 1 87  ? -20.728 14.555  22.019  0.50 15.67 ? 87  THR A OG1 1 
ATOM   769  O  OG1 B THR A 1 87  ? -19.107 15.079  21.471  0.50 12.58 ? 87  THR A OG1 1 
ATOM   770  C  CG2 A THR A 1 87  ? -19.781 13.757  19.951  0.50 15.12 ? 87  THR A CG2 1 
ATOM   771  C  CG2 B THR A 1 87  ? -20.970 13.881  22.474  0.50 12.41 ? 87  THR A CG2 1 
ATOM   772  N  N   . TYR A 1 88  ? -17.537 11.509  20.817  1.00 10.40 ? 88  TYR A N   1 
ATOM   773  C  CA  . TYR A 1 88  ? -16.419 11.068  19.977  1.00 8.95  ? 88  TYR A CA  1 
ATOM   774  C  C   . TYR A 1 88  ? -16.888 10.761  18.560  1.00 10.09 ? 88  TYR A C   1 
ATOM   775  O  O   . TYR A 1 88  ? -17.886 10.060  18.415  1.00 12.68 ? 88  TYR A O   1 
ATOM   776  C  CB  . TYR A 1 88  ? -15.724 9.832   20.586  1.00 9.61  ? 88  TYR A CB  1 
ATOM   777  C  CG  . TYR A 1 88  ? -14.986 10.070  21.908  1.00 8.42  ? 88  TYR A CG  1 
ATOM   778  C  CD1 . TYR A 1 88  ? -15.674 10.423  23.083  1.00 9.11  ? 88  TYR A CD1 1 
ATOM   779  C  CD2 . TYR A 1 88  ? -13.571 9.881   21.980  1.00 8.06  ? 88  TYR A CD2 1 
ATOM   780  C  CE1 . TYR A 1 88  ? -14.974 10.610  24.320  1.00 8.44  ? 88  TYR A CE1 1 
ATOM   781  C  CE2 . TYR A 1 88  ? -12.874 10.071  23.232  1.00 6.57  ? 88  TYR A CE2 1 
ATOM   782  C  CZ  . TYR A 1 88  ? -13.572 10.359  24.381  1.00 8.92  ? 88  TYR A CZ  1 
ATOM   783  O  OH  . TYR A 1 88  ? -12.860 10.489  25.547  1.00 8.36  ? 88  TYR A OH  1 
ATOM   784  N  N   . ARG A 1 89  ? -16.186 11.251  17.563  1.00 8.91  ? 89  ARG A N   1 
ATOM   785  C  CA  . ARG A 1 89  ? -16.639 11.148  16.156  1.00 9.67  ? 89  ARG A CA  1 
ATOM   786  C  C   . ARG A 1 89  ? -15.881 10.031  15.460  1.00 6.81  ? 89  ARG A C   1 
ATOM   787  O  O   . ARG A 1 89  ? -14.627 9.928   15.543  1.00 7.49  ? 89  ARG A O   1 
ATOM   788  C  CB  . ARG A 1 89  ? -16.277 12.464  15.457  1.00 12.06 ? 89  ARG A CB  1 
ATOM   789  C  CG  . ARG A 1 89  ? -17.130 12.690  14.310  1.00 16.17 ? 89  ARG A CG  1 
ATOM   790  C  CD  . ARG A 1 89  ? -16.938 14.157  13.856  1.00 18.90 ? 89  ARG A CD  1 
ATOM   791  N  NE  . ARG A 1 89  ? -17.672 15.168  14.666  1.00 16.70 ? 89  ARG A NE  1 
ATOM   792  C  CZ  . ARG A 1 89  ? -17.519 16.477  14.499  1.00 16.65 ? 89  ARG A CZ  1 
ATOM   793  N  NH1 . ARG A 1 89  ? -16.677 16.967  13.565  1.00 19.43 ? 89  ARG A NH1 1 
ATOM   794  N  NH2 . ARG A 1 89  ? -18.186 17.341  15.277  1.00 20.82 ? 89  ARG A NH2 1 
ATOM   795  N  N   . LEU A 1 90  ? -16.665 9.195   14.769  1.00 7.67  ? 90  LEU A N   1 
ATOM   796  C  CA  . LEU A 1 90  ? -16.047 8.136   13.966  1.00 8.18  ? 90  LEU A CA  1 
ATOM   797  C  C   . LEU A 1 90  ? -15.170 8.697   12.805  1.00 8.22  ? 90  LEU A C   1 
ATOM   798  O  O   . LEU A 1 90  ? -15.694 9.464   11.938  1.00 10.09 ? 90  LEU A O   1 
ATOM   799  C  CB  . LEU A 1 90  ? -17.141 7.239   13.368  1.00 8.42  ? 90  LEU A CB  1 
ATOM   800  C  CG  . LEU A 1 90  ? -16.693 6.056   12.504  1.00 10.18 ? 90  LEU A CG  1 
ATOM   801  C  CD1 . LEU A 1 90  ? -15.945 4.958   13.321  1.00 10.31 ? 90  LEU A CD1 1 
ATOM   802  C  CD2 . LEU A 1 90  ? -17.984 5.378   11.874  1.00 11.80 ? 90  LEU A CD2 1 
ATOM   803  N  N   . ILE A 1 91  ? -13.917 8.221   12.739  1.00 7.62  ? 91  ILE A N   1 
ATOM   804  C  CA  . ILE A 1 91  ? -13.022 8.580   11.636  1.00 8.41  ? 91  ILE A CA  1 
ATOM   805  C  C   . ILE A 1 91  ? -12.751 7.378   10.672  1.00 8.95  ? 91  ILE A C   1 
ATOM   806  O  O   . ILE A 1 91  ? -12.626 7.601   9.460   1.00 7.45  ? 91  ILE A O   1 
ATOM   807  C  CB  . ILE A 1 91  ? -11.690 9.265   12.131  1.00 9.83  ? 91  ILE A CB  1 
ATOM   808  C  CG1 . ILE A 1 91  ? -10.820 9.649   10.925  1.00 10.68 ? 91  ILE A CG1 1 
ATOM   809  C  CG2 . ILE A 1 91  ? -10.903 8.423   13.212  1.00 11.19 ? 91  ILE A CG2 1 
ATOM   810  C  CD1 . ILE A 1 91  ? -9.672  10.549  11.404  1.00 13.60 ? 91  ILE A CD1 1 
ATOM   811  N  N   . GLN A 1 92  ? -12.589 6.145   11.223  1.00 8.07  ? 92  GLN A N   1 
ATOM   812  C  CA  . GLN A 1 92  ? -12.280 5.023   10.353  1.00 7.62  ? 92  GLN A CA  1 
ATOM   813  C  C   . GLN A 1 92  ? -12.550 3.741   11.127  1.00 7.67  ? 92  GLN A C   1 
ATOM   814  O  O   . GLN A 1 92  ? -12.595 3.802   12.348  1.00 7.48  ? 92  GLN A O   1 
ATOM   815  C  CB  . GLN A 1 92  ? -10.860 5.051   9.803   1.00 9.56  ? 92  GLN A CB  1 
ATOM   816  C  CG  . GLN A 1 92  ? -9.762  5.166   10.932  1.00 9.48  ? 92  GLN A CG  1 
ATOM   817  C  CD  . GLN A 1 92  ? -9.035  3.803   11.217  1.00 8.63  ? 92  GLN A CD  1 
ATOM   818  O  OE1 . GLN A 1 92  ? -9.632  2.712   11.192  1.00 10.06 ? 92  GLN A OE1 1 
ATOM   819  N  NE2 . GLN A 1 92  ? -7.739  3.890   11.606  1.00 9.64  ? 92  GLN A NE2 1 
ATOM   820  N  N   . PHE A 1 93  ? -12.763 2.628   10.375  1.00 8.10  ? 93  PHE A N   1 
ATOM   821  C  CA  . PHE A 1 93  ? -12.615 1.326   11.042  1.00 7.84  ? 93  PHE A CA  1 
ATOM   822  C  C   . PHE A 1 93  ? -11.664 0.476   10.209  1.00 6.21  ? 93  PHE A C   1 
ATOM   823  O  O   . PHE A 1 93  ? -11.400 0.713   9.016   1.00 8.31  ? 93  PHE A O   1 
ATOM   824  C  CB  . PHE A 1 93  ? -14.006 0.656   11.266  1.00 8.34  ? 93  PHE A CB  1 
ATOM   825  C  CG  . PHE A 1 93  ? -14.709 0.187   10.000  1.00 8.24  ? 93  PHE A CG  1 
ATOM   826  C  CD1 . PHE A 1 93  ? -14.293 -0.963  9.343   1.00 9.33  ? 93  PHE A CD1 1 
ATOM   827  C  CD2 . PHE A 1 93  ? -15.874 0.860   9.593   1.00 10.17 ? 93  PHE A CD2 1 
ATOM   828  C  CE1 . PHE A 1 93  ? -15.007 -1.421  8.208   1.00 9.88  ? 93  PHE A CE1 1 
ATOM   829  C  CE2 . PHE A 1 93  ? -16.564 0.401   8.435   1.00 10.90 ? 93  PHE A CE2 1 
ATOM   830  C  CZ  . PHE A 1 93  ? -16.120 -0.698  7.758   1.00 11.58 ? 93  PHE A CZ  1 
ATOM   831  N  N   . HIS A 1 94  ? -11.135 -0.559  10.885  1.00 7.24  ? 94  HIS A N   1 
ATOM   832  C  CA  . HIS A 1 94  ? -10.223 -1.531  10.278  1.00 7.03  ? 94  HIS A CA  1 
ATOM   833  C  C   . HIS A 1 94  ? -10.305 -2.821  11.081  1.00 6.11  ? 94  HIS A C   1 
ATOM   834  O  O   . HIS A 1 94  ? -10.948 -2.810  12.150  1.00 5.96  ? 94  HIS A O   1 
ATOM   835  C  CB  . HIS A 1 94  ? -8.762  -1.035  10.232  1.00 7.98  ? 94  HIS A CB  1 
ATOM   836  C  CG  . HIS A 1 94  ? -8.226  -0.769  11.628  1.00 6.75  ? 94  HIS A CG  1 
ATOM   837  N  ND1 . HIS A 1 94  ? -8.403  0.444   12.251  1.00 6.11  ? 94  HIS A ND1 1 
ATOM   838  C  CD2 . HIS A 1 94  ? -7.625  -1.580  12.536  1.00 6.40  ? 94  HIS A CD2 1 
ATOM   839  C  CE1 . HIS A 1 94  ? -7.962  0.346   13.514  1.00 6.03  ? 94  HIS A CE1 1 
ATOM   840  N  NE2 . HIS A 1 94  ? -7.455  -0.866  13.667  1.00 5.63  ? 94  HIS A NE2 1 
ATOM   841  N  N   . PHE A 1 95  ? -9.618  -3.879  10.606  1.00 7.07  ? 95  PHE A N   1 
ATOM   842  C  CA  . PHE A 1 95  ? -9.593  -5.129  11.321  1.00 6.93  ? 95  PHE A CA  1 
ATOM   843  C  C   . PHE A 1 95  ? -8.136  -5.604  11.544  1.00 5.93  ? 95  PHE A C   1 
ATOM   844  O  O   . PHE A 1 95  ? -7.195  -5.103  10.853  1.00 7.41  ? 95  PHE A O   1 
ATOM   845  C  CB  . PHE A 1 95  ? -10.327 -6.257  10.495  1.00 6.79  ? 95  PHE A CB  1 
ATOM   846  C  CG  . PHE A 1 95  ? -11.753 -5.931  10.183  1.00 5.97  ? 95  PHE A CG  1 
ATOM   847  C  CD1 . PHE A 1 95  ? -12.086 -5.133  9.099   1.00 6.96  ? 95  PHE A CD1 1 
ATOM   848  C  CD2 . PHE A 1 95  ? -12.778 -6.585  10.830  1.00 7.37  ? 95  PHE A CD2 1 
ATOM   849  C  CE1 . PHE A 1 95  ? -13.393 -4.869  8.739   1.00 7.95  ? 95  PHE A CE1 1 
ATOM   850  C  CE2 . PHE A 1 95  ? -14.109 -6.390  10.517  1.00 7.01  ? 95  PHE A CE2 1 
ATOM   851  C  CZ  . PHE A 1 95  ? -14.406 -5.495  9.441   1.00 8.20  ? 95  PHE A CZ  1 
ATOM   852  N  N   . HIS A 1 96  ? -8.029  -6.551  12.474  1.00 6.30  ? 96  HIS A N   1 
ATOM   853  C  CA  . HIS A 1 96  ? -6.804  -7.359  12.624  1.00 5.89  ? 96  HIS A CA  1 
ATOM   854  C  C   . HIS A 1 96  ? -7.240  -8.824  12.486  1.00 5.68  ? 96  HIS A C   1 
ATOM   855  O  O   . HIS A 1 96  ? -8.310  -9.187  13.020  1.00 6.98  ? 96  HIS A O   1 
ATOM   856  C  CB  . HIS A 1 96  ? -6.125  -7.109  14.023  1.00 5.59  ? 96  HIS A CB  1 
ATOM   857  C  CG  . HIS A 1 96  ? -5.853  -5.655  14.290  1.00 7.29  ? 96  HIS A CG  1 
ATOM   858  N  ND1 . HIS A 1 96  ? -4.608  -5.094  14.095  1.00 6.58  ? 96  HIS A ND1 1 
ATOM   859  C  CD2 . HIS A 1 96  ? -6.695  -4.639  14.667  1.00 7.40  ? 96  HIS A CD2 1 
ATOM   860  C  CE1 . HIS A 1 96  ? -4.681  -3.788  14.443  1.00 7.40  ? 96  HIS A CE1 1 
ATOM   861  N  NE2 . HIS A 1 96  ? -5.945  -3.479  14.704  1.00 6.60  ? 96  HIS A NE2 1 
ATOM   862  N  N   . TRP A 1 97  ? -6.428  -9.649  11.794  1.00 5.91  ? 97  TRP A N   1 
ATOM   863  C  CA  . TRP A 1 97  ? -6.815  -11.023 11.625  1.00 5.90  ? 97  TRP A CA  1 
ATOM   864  C  C   . TRP A 1 97  ? -5.665  -11.969 11.506  1.00 6.46  ? 97  TRP A C   1 
ATOM   865  O  O   . TRP A 1 97  ? -4.462  -11.525 11.371  1.00 7.15  ? 97  TRP A O   1 
ATOM   866  C  CB  . TRP A 1 97  ? -7.734  -11.185 10.340  1.00 7.61  ? 97  TRP A CB  1 
ATOM   867  C  CG  . TRP A 1 97  ? -7.143  -10.777 9.067   1.00 6.67  ? 97  TRP A CG  1 
ATOM   868  C  CD1 . TRP A 1 97  ? -6.443  -11.611 8.196   1.00 10.40 ? 97  TRP A CD1 1 
ATOM   869  C  CD2 . TRP A 1 97  ? -7.062  -9.451  8.528   1.00 7.21  ? 97  TRP A CD2 1 
ATOM   870  N  NE1 . TRP A 1 97  ? -6.008  -10.873 7.060   1.00 9.21  ? 97  TRP A NE1 1 
ATOM   871  C  CE2 . TRP A 1 97  ? -6.338  -9.542  7.302   1.00 8.65  ? 97  TRP A CE2 1 
ATOM   872  C  CE3 . TRP A 1 97  ? -7.594  -8.199  8.911   1.00 8.08  ? 97  TRP A CE3 1 
ATOM   873  C  CZ2 . TRP A 1 97  ? -6.174  -8.408  6.461   1.00 10.44 ? 97  TRP A CZ2 1 
ATOM   874  C  CZ3 . TRP A 1 97  ? -7.355  -7.065  8.107   1.00 10.25 ? 97  TRP A CZ3 1 
ATOM   875  C  CH2 . TRP A 1 97  ? -6.683  -7.176  6.905   1.00 9.87  ? 97  TRP A CH2 1 
ATOM   876  N  N   . GLY A 1 98  ? -5.998  -13.281 11.477  1.00 6.55  ? 98  GLY A N   1 
ATOM   877  C  CA  . GLY A 1 98  ? -4.922  -14.254 11.516  1.00 7.36  ? 98  GLY A CA  1 
ATOM   878  C  C   . GLY A 1 98  ? -4.675  -14.991 10.190  1.00 8.12  ? 98  GLY A C   1 
ATOM   879  O  O   . GLY A 1 98  ? -5.402  -14.811 9.206   1.00 8.44  ? 98  GLY A O   1 
ATOM   880  N  N   . SER A 1 99  ? -3.640  -15.852 10.208  1.00 8.07  ? 99  SER A N   1 
ATOM   881  C  CA  . SER A 1 99  ? -3.385  -16.762 9.065   1.00 8.82  ? 99  SER A CA  1 
ATOM   882  C  C   . SER A 1 99  ? -4.291  -18.038 9.167   1.00 9.78  ? 99  SER A C   1 
ATOM   883  O  O   . SER A 1 99  ? -4.415  -18.763 8.201   1.00 11.23 ? 99  SER A O   1 
ATOM   884  C  CB  . SER A 1 99  ? -1.938  -17.125 9.032   1.00 11.48 ? 99  SER A CB  1 
ATOM   885  O  OG  . SER A 1 99  ? -1.511  -17.681 10.285  1.00 12.44 ? 99  SER A OG  1 
ATOM   886  N  N   . LEU A 1 100 ? -4.878  -18.240 10.362  1.00 9.98  ? 100 LEU A N   1 
ATOM   887  C  CA  . LEU A 1 100 ? -5.705  -19.360 10.675  1.00 11.68 ? 100 LEU A CA  1 
ATOM   888  C  C   . LEU A 1 100 ? -6.851  -18.905 11.540  1.00 10.35 ? 100 LEU A C   1 
ATOM   889  O  O   . LEU A 1 100 ? -6.700  -17.916 12.261  1.00 10.35 ? 100 LEU A O   1 
ATOM   890  C  CB  . LEU A 1 100 ? -4.916  -20.349 11.613  1.00 16.02 ? 100 LEU A CB  1 
ATOM   891  C  CG  . LEU A 1 100 ? -3.553  -20.789 11.105  1.00 17.64 ? 100 LEU A CG  1 
ATOM   892  C  CD1 . LEU A 1 100 ? -2.446  -21.082 12.144  1.00 24.07 ? 100 LEU A CD1 1 
ATOM   893  C  CD2 . LEU A 1 100 ? -3.851  -21.993 10.191  1.00 21.41 ? 100 LEU A CD2 1 
ATOM   894  N  N   . ASP A 1 101 ? -7.923  -19.703 11.605  1.00 10.55 ? 101 ASP A N   1 
ATOM   895  C  CA  . ASP A 1 101 ? -9.073  -19.246 12.372  1.00 9.49  ? 101 ASP A CA  1 
ATOM   896  C  C   . ASP A 1 101 ? -8.817  -19.153 13.889  1.00 10.48 ? 101 ASP A C   1 
ATOM   897  O  O   . ASP A 1 101 ? -9.503  -18.414 14.595  1.00 11.04 ? 101 ASP A O   1 
ATOM   898  C  CB  . ASP A 1 101 ? -10.328 -20.118 12.139  1.00 10.03 ? 101 ASP A CB  1 
ATOM   899  C  CG  . ASP A 1 101 ? -10.785 -20.160 10.721  1.00 11.56 ? 101 ASP A CG  1 
ATOM   900  O  OD1 . ASP A 1 101 ? -10.457 -19.283 9.905   1.00 12.46 ? 101 ASP A OD1 1 
ATOM   901  O  OD2 . ASP A 1 101 ? -11.606 -21.057 10.450  1.00 19.38 ? 101 ASP A OD2 1 
ATOM   902  N  N   . GLY A 1 102 ? -7.825  -19.938 14.345  1.00 11.09 ? 102 GLY A N   1 
ATOM   903  C  CA  . GLY A 1 102 ? -7.507  -19.902 15.792  1.00 10.25 ? 102 GLY A CA  1 
ATOM   904  C  C   . GLY A 1 102 ? -6.747  -18.732 16.347  1.00 9.67  ? 102 GLY A C   1 
ATOM   905  O  O   . GLY A 1 102 ? -6.394  -18.737 17.541  1.00 10.72 ? 102 GLY A O   1 
ATOM   906  N  N   . GLN A 1 103 ? -6.471  -17.725 15.516  1.00 7.92  ? 103 GLN A N   1 
ATOM   907  C  CA  . GLN A 1 103 ? -5.757  -16.557 16.062  1.00 8.49  ? 103 GLN A CA  1 
ATOM   908  C  C   . GLN A 1 103 ? -6.137  -15.355 15.167  1.00 6.15  ? 103 GLN A C   1 
ATOM   909  O  O   . GLN A 1 103 ? -6.676  -15.574 14.022  1.00 8.72  ? 103 GLN A O   1 
ATOM   910  C  CB  . GLN A 1 103 ? -4.249  -16.796 16.075  1.00 9.44  ? 103 GLN A CB  1 
ATOM   911  C  CG  . GLN A 1 103 ? -3.675  -17.013 14.636  1.00 9.92  ? 103 GLN A CG  1 
ATOM   912  C  CD  . GLN A 1 103 ? -2.218  -17.508 14.722  1.00 12.47 ? 103 GLN A CD  1 
ATOM   913  O  OE1 . GLN A 1 103 ? -2.003  -18.406 15.511  1.00 20.02 ? 103 GLN A OE1 1 
ATOM   914  N  NE2 . GLN A 1 103 ? -1.278  -17.029 13.925  1.00 13.74 ? 103 GLN A NE2 1 
ATOM   915  N  N   . GLY A 1 104 ? -5.807  -14.154 15.652  1.00 7.44  ? 104 GLY A N   1 
ATOM   916  C  CA  . GLY A 1 104 ? -6.092  -12.943 14.797  1.00 7.04  ? 104 GLY A CA  1 
ATOM   917  C  C   . GLY A 1 104 ? -6.551  -11.792 15.651  1.00 6.22  ? 104 GLY A C   1 
ATOM   918  O  O   . GLY A 1 104 ? -6.311  -10.617 15.340  1.00 7.69  ? 104 GLY A O   1 
ATOM   919  N  N   . SER A 1 105 ? -7.252  -12.085 16.794  1.00 5.58  ? 105 SER A N   1 
ATOM   920  C  CA  . SER A 1 105 ? -7.651  -10.952 17.660  1.00 5.91  ? 105 SER A CA  1 
ATOM   921  C  C   . SER A 1 105 ? -6.437  -10.349 18.392  1.00 5.45  ? 105 SER A C   1 
ATOM   922  O  O   . SER A 1 105 ? -5.406  -11.050 18.594  1.00 6.21  ? 105 SER A O   1 
ATOM   923  C  CB  . SER A 1 105 ? -8.799  -11.258 18.602  1.00 6.79  ? 105 SER A CB  1 
ATOM   924  O  OG  . SER A 1 105 ? -8.420  -12.207 19.594  1.00 6.28  ? 105 SER A OG  1 
ATOM   925  N  N   . GLU A 1 106 ? -6.592  -9.087  18.820  1.00 4.80  ? 106 GLU A N   1 
ATOM   926  C  CA  . GLU A 1 106 ? -5.573  -8.387  19.613  1.00 5.28  ? 106 GLU A CA  1 
ATOM   927  C  C   . GLU A 1 106 ? -5.926  -8.568  21.098  1.00 5.77  ? 106 GLU A C   1 
ATOM   928  O  O   . GLU A 1 106 ? -5.114  -9.153  21.901  1.00 6.66  ? 106 GLU A O   1 
ATOM   929  C  CB  . GLU A 1 106 ? -5.562  -6.913  19.197  1.00 6.10  ? 106 GLU A CB  1 
ATOM   930  C  CG  . GLU A 1 106 ? -5.089  -6.808  17.728  1.00 7.96  ? 106 GLU A CG  1 
ATOM   931  C  CD  . GLU A 1 106 ? -4.379  -5.527  17.444  1.00 6.25  ? 106 GLU A CD  1 
ATOM   932  O  OE1 . GLU A 1 106 ? -4.964  -4.394  17.726  1.00 5.74  ? 106 GLU A OE1 1 
ATOM   933  O  OE2 . GLU A 1 106 ? -3.194  -5.578  16.936  1.00 7.46  ? 106 GLU A OE2 1 
ATOM   934  N  N   . HIS A 1 107 ? -7.117  -8.116  21.489  1.00 5.32  ? 107 HIS A N   1 
ATOM   935  C  CA  . HIS A 1 107 ? -7.556  -8.477  22.846  1.00 5.41  ? 107 HIS A CA  1 
ATOM   936  C  C   . HIS A 1 107 ? -7.839  -9.975  22.873  1.00 4.38  ? 107 HIS A C   1 
ATOM   937  O  O   . HIS A 1 107 ? -8.198  -10.579 21.827  1.00 5.99  ? 107 HIS A O   1 
ATOM   938  C  CB  . HIS A 1 107 ? -8.842  -7.648  23.245  1.00 5.96  ? 107 HIS A CB  1 
ATOM   939  C  CG  . HIS A 1 107 ? -8.494  -6.193  23.392  1.00 4.43  ? 107 HIS A CG  1 
ATOM   940  N  ND1 . HIS A 1 107 ? -8.532  -5.305  22.330  1.00 6.17  ? 107 HIS A ND1 1 
ATOM   941  C  CD2 . HIS A 1 107 ? -7.983  -5.495  24.447  1.00 5.22  ? 107 HIS A CD2 1 
ATOM   942  C  CE1 . HIS A 1 107 ? -8.109  -4.103  22.741  1.00 4.84  ? 107 HIS A CE1 1 
ATOM   943  N  NE2 . HIS A 1 107 ? -7.760  -4.187  24.038  1.00 5.66  ? 107 HIS A NE2 1 
ATOM   944  N  N   . THR A 1 108 ? -7.725  -10.567 24.060  1.00 6.28  ? 108 THR A N   1 
ATOM   945  C  CA  . THR A 1 108 ? -8.101  -11.955 24.282  1.00 5.90  ? 108 THR A CA  1 
ATOM   946  C  C   . THR A 1 108 ? -9.054  -11.982 25.514  1.00 6.57  ? 108 THR A C   1 
ATOM   947  O  O   . THR A 1 108 ? -9.095  -11.002 26.289  1.00 6.97  ? 108 THR A O   1 
ATOM   948  C  CB  . THR A 1 108 ? -6.863  -12.867 24.511  1.00 6.11  ? 108 THR A CB  1 
ATOM   949  O  OG1 . THR A 1 108 ? -6.037  -12.362 25.575  1.00 6.43  ? 108 THR A OG1 1 
ATOM   950  C  CG2 . THR A 1 108 ? -6.039  -12.961 23.212  1.00 6.88  ? 108 THR A CG2 1 
ATOM   951  N  N   . VAL A 1 109 ? -9.822  -13.068 25.647  1.00 6.38  ? 109 VAL A N   1 
ATOM   952  C  CA  . VAL A 1 109 ? -10.804 -13.151 26.758  1.00 7.12  ? 109 VAL A CA  1 
ATOM   953  C  C   . VAL A 1 109 ? -10.485 -14.438 27.519  1.00 8.60  ? 109 VAL A C   1 
ATOM   954  O  O   . VAL A 1 109 ? -10.616 -15.536 26.947  1.00 8.40  ? 109 VAL A O   1 
ATOM   955  C  CB  . VAL A 1 109 ? -12.241 -13.194 26.225  1.00 9.72  ? 109 VAL A CB  1 
ATOM   956  C  CG1 . VAL A 1 109 ? -13.303 -13.272 27.414  1.00 9.47  ? 109 VAL A CG1 1 
ATOM   957  C  CG2 . VAL A 1 109 ? -12.566 -11.877 25.369  1.00 9.67  ? 109 VAL A CG2 1 
ATOM   958  N  N   . ASP A 1 110 ? -10.027 -14.305 28.771  1.00 8.52  ? 110 ASP A N   1 
ATOM   959  C  CA  . ASP A 1 110 ? -9.491  -15.547 29.439  1.00 9.21  ? 110 ASP A CA  1 
ATOM   960  C  C   . ASP A 1 110 ? -8.558  -16.349 28.524  1.00 9.02  ? 110 ASP A C   1 
ATOM   961  O  O   . ASP A 1 110 ? -8.632  -17.593 28.481  1.00 9.03  ? 110 ASP A O   1 
ATOM   962  C  CB  . ASP A 1 110 ? -10.658 -16.381 29.920  1.00 9.80  ? 110 ASP A CB  1 
ATOM   963  C  CG  . ASP A 1 110 ? -11.483 -15.596 30.969  1.00 10.93 ? 110 ASP A CG  1 
ATOM   964  O  OD1 . ASP A 1 110 ? -10.943 -14.709 31.671  1.00 12.51 ? 110 ASP A OD1 1 
ATOM   965  O  OD2 . ASP A 1 110 ? -12.680 -15.920 31.102  1.00 13.85 ? 110 ASP A OD2 1 
ATOM   966  N  N   . LYS A 1 111 ? -7.633  -15.612 27.851  1.00 8.30  ? 111 LYS A N   1 
ATOM   967  C  CA  . LYS A 1 111 ? -6.599  -16.140 26.945  1.00 8.46  ? 111 LYS A CA  1 
ATOM   968  C  C   . LYS A 1 111 ? -7.177  -16.699 25.602  1.00 8.46  ? 111 LYS A C   1 
ATOM   969  O  O   . LYS A 1 111 ? -6.391  -17.053 24.696  1.00 10.12 ? 111 LYS A O   1 
ATOM   970  C  CB  . LYS A 1 111 ? -5.687  -17.226 27.605  1.00 11.11 ? 111 LYS A CB  1 
ATOM   971  C  CG  . LYS A 1 111 ? -5.017  -16.660 28.838  1.00 12.35 ? 111 LYS A CG  1 
ATOM   972  C  CD  . LYS A 1 111 ? -4.073  -15.504 28.464  1.00 17.23 ? 111 LYS A CD  1 
ATOM   973  C  CE  . LYS A 1 111 ? -3.299  -14.856 29.711  1.00 18.17 ? 111 LYS A CE  1 
ATOM   974  N  NZ  . LYS A 1 111 ? -2.113  -15.685 29.982  1.00 21.43 ? 111 LYS A NZ  1 
ATOM   975  N  N   . LYS A 1 112 ? -8.507  -16.645 25.420  1.00 7.62  ? 112 LYS A N   1 
ATOM   976  C  CA  . LYS A 1 112 ? -9.074  -17.069 24.132  1.00 7.79  ? 112 LYS A CA  1 
ATOM   977  C  C   . LYS A 1 112 ? -8.754  -15.996 23.062  1.00 6.41  ? 112 LYS A C   1 
ATOM   978  O  O   . LYS A 1 112 ? -9.026  -14.782 23.233  1.00 7.40  ? 112 LYS A O   1 
ATOM   979  C  CB  . LYS A 1 112 ? -10.621 -17.172 24.248  1.00 9.71  ? 112 LYS A CB  1 
ATOM   980  C  CG  . LYS A 1 112 ? -11.367 -17.494 22.926  1.00 10.54 ? 112 LYS A CG  1 
ATOM   981  C  CD  . LYS A 1 112 ? -12.899 -17.410 23.073  1.00 11.82 ? 112 LYS A CD  1 
ATOM   982  C  CE  . LYS A 1 112 ? -13.538 -17.596 21.631  1.00 13.72 ? 112 LYS A CE  1 
ATOM   983  N  NZ  . LYS A 1 112 ? -13.377 -18.989 21.167  1.00 14.29 ? 112 LYS A NZ  1 
ATOM   984  N  N   A LYS A 1 113 ? -8.222  -16.498 21.936  0.50 7.29  ? 113 LYS A N   1 
ATOM   985  N  N   B LYS A 1 113 ? -8.277  -16.494 21.910  0.50 7.17  ? 113 LYS A N   1 
ATOM   986  C  CA  A LYS A 1 113 ? -8.044  -15.722 20.688  0.50 6.81  ? 113 LYS A CA  1 
ATOM   987  C  CA  B LYS A 1 113 ? -8.029  -15.676 20.696  0.50 6.75  ? 113 LYS A CA  1 
ATOM   988  C  C   A LYS A 1 113 ? -9.266  -15.934 19.783  0.50 7.18  ? 113 LYS A C   1 
ATOM   989  C  C   B LYS A 1 113 ? -9.123  -15.913 19.648  0.50 6.95  ? 113 LYS A C   1 
ATOM   990  O  O   A LYS A 1 113 ? -9.753  -17.056 19.639  0.50 6.47  ? 113 LYS A O   1 
ATOM   991  O  O   B LYS A 1 113 ? -9.363  -17.056 19.245  0.50 6.64  ? 113 LYS A O   1 
ATOM   992  C  CB  A LYS A 1 113 ? -6.752  -16.134 19.972  0.50 7.69  ? 113 LYS A CB  1 
ATOM   993  C  CB  B LYS A 1 113 ? -6.663  -16.015 20.098  0.50 7.05  ? 113 LYS A CB  1 
ATOM   994  C  CG  A LYS A 1 113 ? -5.476  -15.934 20.771  0.50 6.62  ? 113 LYS A CG  1 
ATOM   995  C  CG  B LYS A 1 113 ? -5.460  -15.483 20.816  0.50 8.05  ? 113 LYS A CG  1 
ATOM   996  C  CD  A LYS A 1 113 ? -4.258  -16.482 19.970  0.50 7.90  ? 113 LYS A CD  1 
ATOM   997  C  CD  B LYS A 1 113 ? -4.189  -16.133 20.256  0.50 8.97  ? 113 LYS A CD  1 
ATOM   998  C  CE  A LYS A 1 113 ? -2.897  -15.990 20.577  0.50 8.10  ? 113 LYS A CE  1 
ATOM   999  C  CE  B LYS A 1 113 ? -2.996  -15.713 21.141  0.50 10.76 ? 113 LYS A CE  1 
ATOM   1000 N  NZ  A LYS A 1 113 ? -2.584  -16.552 21.953  0.50 10.27 ? 113 LYS A NZ  1 
ATOM   1001 N  NZ  B LYS A 1 113 ? -1.734  -16.472 20.860  0.50 12.63 ? 113 LYS A NZ  1 
ATOM   1002 N  N   . TYR A 1 114 ? -9.799  -14.814 19.234  1.00 6.19  ? 114 TYR A N   1 
ATOM   1003 C  CA  . TYR A 1 114 ? -10.742 -14.899 18.170  1.00 6.95  ? 114 TYR A CA  1 
ATOM   1004 C  C   . TYR A 1 114 ? -10.085 -14.803 16.788  1.00 6.38  ? 114 TYR A C   1 
ATOM   1005 O  O   . TYR A 1 114 ? -8.918  -14.511 16.662  1.00 6.88  ? 114 TYR A O   1 
ATOM   1006 C  CB  . TYR A 1 114 ? -11.828 -13.775 18.251  1.00 7.05  ? 114 TYR A CB  1 
ATOM   1007 C  CG  . TYR A 1 114 ? -12.788 -13.966 19.428  1.00 7.74  ? 114 TYR A CG  1 
ATOM   1008 C  CD1 . TYR A 1 114 ? -12.457 -13.566 20.721  1.00 8.67  ? 114 TYR A CD1 1 
ATOM   1009 C  CD2 . TYR A 1 114 ? -14.021 -14.629 19.216  1.00 8.24  ? 114 TYR A CD2 1 
ATOM   1010 C  CE1 . TYR A 1 114 ? -13.352 -13.697 21.794  1.00 8.56  ? 114 TYR A CE1 1 
ATOM   1011 C  CE2 . TYR A 1 114 ? -14.940 -14.791 20.272  1.00 10.12 ? 114 TYR A CE2 1 
ATOM   1012 C  CZ  . TYR A 1 114 ? -14.570 -14.301 21.550  1.00 10.83 ? 114 TYR A CZ  1 
ATOM   1013 O  OH  . TYR A 1 114 ? -15.469 -14.428 22.627  1.00 14.38 ? 114 TYR A OH  1 
ATOM   1014 N  N   . ALA A 1 115 ? -10.855 -15.127 15.743  1.00 6.38  ? 115 ALA A N   1 
ATOM   1015 C  CA  . ALA A 1 115 ? -10.292 -15.171 14.399  1.00 6.77  ? 115 ALA A CA  1 
ATOM   1016 C  C   . ALA A 1 115 ? -9.903  -13.765 13.924  1.00 6.25  ? 115 ALA A C   1 
ATOM   1017 O  O   . ALA A 1 115 ? -9.077  -13.612 13.041  1.00 7.62  ? 115 ALA A O   1 
ATOM   1018 C  CB  . ALA A 1 115 ? -11.371 -15.789 13.413  1.00 8.80  ? 115 ALA A CB  1 
ATOM   1019 N  N   . ALA A 1 116 ? -10.577 -12.726 14.447  1.00 5.66  ? 116 ALA A N   1 
ATOM   1020 C  CA  . ALA A 1 116 ? -10.256 -11.369 13.998  1.00 6.33  ? 116 ALA A CA  1 
ATOM   1021 C  C   . ALA A 1 116 ? -10.865 -10.388 15.006  1.00 6.16  ? 116 ALA A C   1 
ATOM   1022 O  O   . ALA A 1 116 ? -11.616 -10.795 15.911  1.00 6.50  ? 116 ALA A O   1 
ATOM   1023 C  CB  . ALA A 1 116 ? -10.817 -11.117 12.531  1.00 8.35  ? 116 ALA A CB  1 
ATOM   1024 N  N   . GLU A 1 117 ? -10.565 -9.105  14.828  1.00 5.19  ? 117 GLU A N   1 
ATOM   1025 C  CA  . GLU A 1 117 ? -11.066 -8.071  15.729  1.00 5.57  ? 117 GLU A CA  1 
ATOM   1026 C  C   . GLU A 1 117 ? -11.264 -6.777  14.896  1.00 5.44  ? 117 GLU A C   1 
ATOM   1027 O  O   . GLU A 1 117 ? -10.350 -6.382  14.151  1.00 6.19  ? 117 GLU A O   1 
ATOM   1028 C  CB  . GLU A 1 117 ? -10.098 -7.828  16.911  1.00 6.39  ? 117 GLU A CB  1 
ATOM   1029 C  CG  . GLU A 1 117 ? -10.615 -6.838  17.982  1.00 5.63  ? 117 GLU A CG  1 
ATOM   1030 C  CD  . GLU A 1 117 ? -9.714  -6.792  19.218  1.00 5.58  ? 117 GLU A CD  1 
ATOM   1031 O  OE1 . GLU A 1 117 ? -9.046  -7.847  19.510  1.00 6.57  ? 117 GLU A OE1 1 
ATOM   1032 O  OE2 . GLU A 1 117 ? -9.703  -5.691  19.868  1.00 6.45  ? 117 GLU A OE2 1 
ATOM   1033 N  N   . LEU A 1 118 ? -12.459 -6.224  14.987  1.00 6.27  ? 118 LEU A N   1 
ATOM   1034 C  CA  . LEU A 1 118 ? -12.815 -4.966  14.286  1.00 5.51  ? 118 LEU A CA  1 
ATOM   1035 C  C   . LEU A 1 118 ? -12.604 -3.801  15.284  1.00 5.15  ? 118 LEU A C   1 
ATOM   1036 O  O   . LEU A 1 118 ? -13.013 -3.871  16.474  1.00 5.42  ? 118 LEU A O   1 
ATOM   1037 C  CB  . LEU A 1 118 ? -14.324 -5.045  13.955  1.00 5.83  ? 118 LEU A CB  1 
ATOM   1038 C  CG  . LEU A 1 118 ? -15.099 -3.736  13.618  1.00 6.69  ? 118 LEU A CG  1 
ATOM   1039 C  CD1 . LEU A 1 118 ? -14.536 -3.110  12.372  1.00 8.46  ? 118 LEU A CD1 1 
ATOM   1040 C  CD2 . LEU A 1 118 ? -16.624 -4.061  13.355  1.00 8.17  ? 118 LEU A CD2 1 
ATOM   1041 N  N   . HIS A 1 119 ? -11.975 -2.700  14.783  1.00 5.65  ? 119 HIS A N   1 
ATOM   1042 C  CA  . HIS A 1 119 ? -11.757 -1.507  15.596  1.00 6.00  ? 119 HIS A CA  1 
ATOM   1043 C  C   . HIS A 1 119 ? -12.462 -0.335  14.919  1.00 5.78  ? 119 HIS A C   1 
ATOM   1044 O  O   . HIS A 1 119 ? -12.076 0.032   13.754  1.00 6.62  ? 119 HIS A O   1 
ATOM   1045 C  CB  . HIS A 1 119 ? -10.247 -1.243  15.678  1.00 6.34  ? 119 HIS A CB  1 
ATOM   1046 C  CG  . HIS A 1 119 ? -9.578  -2.232  16.604  1.00 6.28  ? 119 HIS A CG  1 
ATOM   1047 N  ND1 . HIS A 1 119 ? -8.210  -2.460  16.635  1.00 6.07  ? 119 HIS A ND1 1 
ATOM   1048 C  CD2 . HIS A 1 119 ? -10.089 -3.034  17.595  1.00 6.83  ? 119 HIS A CD2 1 
ATOM   1049 C  CE1 . HIS A 1 119 ? -7.895  -3.391  17.504  1.00 6.50  ? 119 HIS A CE1 1 
ATOM   1050 N  NE2 . HIS A 1 119 ? -9.009  -3.758  18.128  1.00 6.11  ? 119 HIS A NE2 1 
ATOM   1051 N  N   . LEU A 1 120 ? -13.441 0.244   15.595  1.00 5.77  ? 120 LEU A N   1 
ATOM   1052 C  CA  . LEU A 1 120 ? -14.123 1.494   15.126  1.00 6.37  ? 120 LEU A CA  1 
ATOM   1053 C  C   . LEU A 1 120 ? -13.501 2.649   15.919  1.00 5.16  ? 120 LEU A C   1 
ATOM   1054 O  O   . LEU A 1 120 ? -13.592 2.699   17.145  1.00 5.98  ? 120 LEU A O   1 
ATOM   1055 C  CB  . LEU A 1 120 ? -15.635 1.398   15.356  1.00 7.51  ? 120 LEU A CB  1 
ATOM   1056 C  CG  . LEU A 1 120 ? -16.272 0.322   14.471  1.00 8.18  ? 120 LEU A CG  1 
ATOM   1057 C  CD1 . LEU A 1 120 ? -17.166 -0.545  15.335  1.00 9.25  ? 120 LEU A CD1 1 
ATOM   1058 C  CD2 . LEU A 1 120 ? -17.124 1.022   13.346  1.00 9.31  ? 120 LEU A CD2 1 
ATOM   1059 N  N   . VAL A 1 121 ? -12.748 3.526   15.200  1.00 6.15  ? 121 VAL A N   1 
ATOM   1060 C  CA  . VAL A 1 121 ? -11.875 4.519   15.851  1.00 6.58  ? 121 VAL A CA  1 
ATOM   1061 C  C   . VAL A 1 121 ? -12.593 5.881   15.866  1.00 6.33  ? 121 VAL A C   1 
ATOM   1062 O  O   . VAL A 1 121 ? -13.005 6.356   14.777  1.00 7.07  ? 121 VAL A O   1 
ATOM   1063 C  CB  . VAL A 1 121 ? -10.520 4.588   15.046  1.00 5.98  ? 121 VAL A CB  1 
ATOM   1064 C  CG1 . VAL A 1 121 ? -9.607  5.669   15.658  1.00 7.85  ? 121 VAL A CG1 1 
ATOM   1065 C  CG2 . VAL A 1 121 ? -9.880  3.186   14.877  1.00 6.34  ? 121 VAL A CG2 1 
ATOM   1066 N  N   . HIS A 1 122 ? -12.661 6.486   17.078  1.00 5.56  ? 122 HIS A N   1 
ATOM   1067 C  CA  . HIS A 1 122 ? -13.370 7.762   17.220  1.00 5.62  ? 122 HIS A CA  1 
ATOM   1068 C  C   . HIS A 1 122 ? -12.462 8.756   18.007  1.00 6.46  ? 122 HIS A C   1 
ATOM   1069 O  O   . HIS A 1 122 ? -11.747 8.353   18.933  1.00 6.98  ? 122 HIS A O   1 
ATOM   1070 C  CB  . HIS A 1 122 ? -14.668 7.604   18.066  1.00 7.88  ? 122 HIS A CB  1 
ATOM   1071 C  CG  . HIS A 1 122 ? -15.555 6.453   17.676  1.00 6.25  ? 122 HIS A CG  1 
ATOM   1072 N  ND1 . HIS A 1 122 ? -15.184 5.121   17.901  1.00 5.94  ? 122 HIS A ND1 1 
ATOM   1073 C  CD2 . HIS A 1 122 ? -16.780 6.415   17.062  1.00 7.98  ? 122 HIS A CD2 1 
ATOM   1074 C  CE1 . HIS A 1 122 ? -16.211 4.345   17.484  1.00 8.07  ? 122 HIS A CE1 1 
ATOM   1075 N  NE2 . HIS A 1 122 ? -17.148 5.092   16.895  1.00 7.32  ? 122 HIS A NE2 1 
ATOM   1076 N  N   . TRP A 1 123 ? -12.557 10.040  17.650  1.00 6.27  ? 123 TRP A N   1 
ATOM   1077 C  CA  . TRP A 1 123 ? -11.766 11.050  18.381  1.00 6.22  ? 123 TRP A CA  1 
ATOM   1078 C  C   . TRP A 1 123 ? -12.674 12.052  19.118  1.00 7.33  ? 123 TRP A C   1 
ATOM   1079 O  O   . TRP A 1 123 ? -13.822 12.380  18.681  1.00 8.64  ? 123 TRP A O   1 
ATOM   1080 C  CB  . TRP A 1 123 ? -10.821 11.835  17.444  1.00 8.32  ? 123 TRP A CB  1 
ATOM   1081 C  CG  . TRP A 1 123 ? -11.442 12.424  16.256  1.00 9.56  ? 123 TRP A CG  1 
ATOM   1082 C  CD1 . TRP A 1 123 ? -11.633 11.804  15.001  1.00 9.57  ? 123 TRP A CD1 1 
ATOM   1083 C  CD2 . TRP A 1 123 ? -11.983 13.773  16.123  1.00 10.76 ? 123 TRP A CD2 1 
ATOM   1084 N  NE1 . TRP A 1 123 ? -12.303 12.692  14.134  1.00 11.59 ? 123 TRP A NE1 1 
ATOM   1085 C  CE2 . TRP A 1 123 ? -12.492 13.904  14.787  1.00 11.89 ? 123 TRP A CE2 1 
ATOM   1086 C  CE3 . TRP A 1 123 ? -12.060 14.887  16.969  1.00 10.54 ? 123 TRP A CE3 1 
ATOM   1087 C  CZ2 . TRP A 1 123 ? -13.050 15.089  14.320  1.00 12.59 ? 123 TRP A CZ2 1 
ATOM   1088 C  CZ3 . TRP A 1 123 ? -12.673 16.058  16.472  1.00 11.70 ? 123 TRP A CZ3 1 
ATOM   1089 C  CH2 . TRP A 1 123 ? -13.135 16.162  15.152  1.00 12.95 ? 123 TRP A CH2 1 
ATOM   1090 N  N   . ASN A 1 124 ? -12.146 12.521  20.242  1.00 6.94  ? 124 ASN A N   1 
ATOM   1091 C  CA  . ASN A 1 124 ? -12.923 13.357  21.163  1.00 7.53  ? 124 ASN A CA  1 
ATOM   1092 C  C   . ASN A 1 124 ? -13.101 14.759  20.549  1.00 8.35  ? 124 ASN A C   1 
ATOM   1093 O  O   . ASN A 1 124 ? -12.085 15.466  20.282  1.00 8.05  ? 124 ASN A O   1 
ATOM   1094 C  CB  . ASN A 1 124 ? -12.115 13.465  22.476  1.00 8.54  ? 124 ASN A CB  1 
ATOM   1095 C  CG  . ASN A 1 124 ? -12.924 14.081  23.606  1.00 9.85  ? 124 ASN A CG  1 
ATOM   1096 O  OD1 . ASN A 1 124 ? -13.755 14.944  23.361  1.00 10.18 ? 124 ASN A OD1 1 
ATOM   1097 N  ND2 . ASN A 1 124 ? -12.673 13.598  24.891  1.00 10.75 ? 124 ASN A ND2 1 
ATOM   1098 N  N   . THR A 1 125 ? -14.371 15.184  20.313  1.00 9.31  ? 125 THR A N   1 
ATOM   1099 C  CA  . THR A 1 125 ? -14.540 16.453  19.658  1.00 9.40  ? 125 THR A CA  1 
ATOM   1100 C  C   . THR A 1 125 ? -13.976 17.706  20.360  1.00 9.58  ? 125 THR A C   1 
ATOM   1101 O  O   . THR A 1 125 ? -13.865 18.762  19.801  1.00 12.14 ? 125 THR A O   1 
ATOM   1102 C  CB  . THR A 1 125 ? -16.039 16.661  19.308  1.00 12.80 ? 125 THR A CB  1 
ATOM   1103 O  OG1 . THR A 1 125 ? -16.862 16.646  20.491  1.00 15.68 ? 125 THR A OG1 1 
ATOM   1104 C  CG2 . THR A 1 125 ? -16.496 15.471  18.285  1.00 13.98 ? 125 THR A CG2 1 
ATOM   1105 N  N   . LYS A 1 126 ? -13.717 17.478  21.793  1.00 10.22 ? 127 LYS A N   1 
ATOM   1106 C  CA  . LYS A 1 126 ? -13.206 18.632  22.492  1.00 12.48 ? 127 LYS A CA  1 
ATOM   1107 C  C   . LYS A 1 126 ? -11.787 19.036  22.015  1.00 11.12 ? 127 LYS A C   1 
ATOM   1108 O  O   . LYS A 1 126 ? -11.298 20.137  22.348  1.00 12.84 ? 127 LYS A O   1 
ATOM   1109 C  CB  . LYS A 1 126 ? -13.270 18.396  23.998  1.00 13.04 ? 127 LYS A CB  1 
ATOM   1110 C  CG  . LYS A 1 126 ? -12.158 17.542  24.594  1.00 14.57 ? 127 LYS A CG  1 
ATOM   1111 C  CD  . LYS A 1 126 ? -12.391 17.098  26.109  1.00 18.14 ? 127 LYS A CD  1 
ATOM   1112 C  CE  . LYS A 1 126 ? -11.497 17.903  26.973  1.00 29.24 ? 127 LYS A CE  1 
ATOM   1113 N  NZ  . LYS A 1 126 ? -11.232 16.996  28.193  1.00 35.05 ? 127 LYS A NZ  1 
ATOM   1114 N  N   . TYR A 1 127 ? -11.132 18.167  21.206  1.00 9.46  ? 128 TYR A N   1 
ATOM   1115 C  CA  . TYR A 1 127 ? -9.800  18.469  20.659  1.00 9.41  ? 128 TYR A CA  1 
ATOM   1116 C  C   . TYR A 1 127 ? -9.748  18.872  19.203  1.00 10.01 ? 128 TYR A C   1 
ATOM   1117 O  O   . TYR A 1 127 ? -8.617  19.117  18.657  1.00 10.40 ? 128 TYR A O   1 
ATOM   1118 C  CB  . TYR A 1 127 ? -8.787  17.328  21.011  1.00 9.59  ? 128 TYR A CB  1 
ATOM   1119 C  CG  . TYR A 1 127 ? -8.714  17.013  22.452  1.00 7.90  ? 128 TYR A CG  1 
ATOM   1120 C  CD1 . TYR A 1 127 ? -8.307  18.006  23.364  1.00 10.90 ? 128 TYR A CD1 1 
ATOM   1121 C  CD2 . TYR A 1 127 ? -9.028  15.739  22.923  1.00 9.44  ? 128 TYR A CD2 1 
ATOM   1122 C  CE1 . TYR A 1 127 ? -8.243  17.716  24.714  1.00 9.63  ? 128 TYR A CE1 1 
ATOM   1123 C  CE2 . TYR A 1 127 ? -8.934  15.438  24.305  1.00 8.30  ? 128 TYR A CE2 1 
ATOM   1124 C  CZ  . TYR A 1 127 ? -8.571  16.471  25.195  1.00 9.45  ? 128 TYR A CZ  1 
ATOM   1125 O  OH  . TYR A 1 127 ? -8.505  16.226  26.525  1.00 12.76 ? 128 TYR A OH  1 
ATOM   1126 N  N   . GLY A 1 128 ? -10.918 18.997  18.580  1.00 10.26 ? 129 GLY A N   1 
ATOM   1127 C  CA  . GLY A 1 128 ? -10.983 19.685  17.241  1.00 10.80 ? 129 GLY A CA  1 
ATOM   1128 C  C   . GLY A 1 128 ? -10.647 18.825  16.052  1.00 10.89 ? 129 GLY A C   1 
ATOM   1129 O  O   . GLY A 1 128 ? -11.316 18.923  14.989  1.00 13.40 ? 129 GLY A O   1 
ATOM   1130 N  N   . ASP A 1 129 ? -9.629  17.948  16.176  1.00 11.79 ? 130 ASP A N   1 
ATOM   1131 C  CA  . ASP A 1 129 ? -9.341  16.959  15.110  1.00 11.78 ? 130 ASP A CA  1 
ATOM   1132 C  C   . ASP A 1 129 ? -8.532  15.745  15.648  1.00 12.17 ? 130 ASP A C   1 
ATOM   1133 O  O   . ASP A 1 129 ? -8.109  15.771  16.818  1.00 11.50 ? 130 ASP A O   1 
ATOM   1134 C  CB  . ASP A 1 129 ? -8.730  17.558  13.841  1.00 13.79 ? 130 ASP A CB  1 
ATOM   1135 C  CG  . ASP A 1 129 ? -7.322  18.062  14.047  1.00 12.80 ? 130 ASP A CG  1 
ATOM   1136 O  OD1 . ASP A 1 129 ? -6.664  17.725  15.086  1.00 18.40 ? 130 ASP A OD1 1 
ATOM   1137 O  OD2 . ASP A 1 129 ? -6.800  18.720  13.113  1.00 18.42 ? 130 ASP A OD2 1 
ATOM   1138 N  N   . PHE A 1 130 ? -8.452  14.727  14.792  1.00 11.89 ? 131 PHE A N   1 
ATOM   1139 C  CA  . PHE A 1 130 ? -7.751  13.482  15.200  1.00 10.88 ? 131 PHE A CA  1 
ATOM   1140 C  C   . PHE A 1 130 ? -6.299  13.762  15.580  1.00 9.91  ? 131 PHE A C   1 
ATOM   1141 O  O   . PHE A 1 130 ? -5.805  13.161  16.556  1.00 9.92  ? 131 PHE A O   1 
ATOM   1142 C  CB  . PHE A 1 130 ? -7.829  12.510  14.047  1.00 10.17 ? 131 PHE A CB  1 
ATOM   1143 C  CG  . PHE A 1 130 ? -7.164  11.194  14.299  1.00 9.71  ? 131 PHE A CG  1 
ATOM   1144 C  CD1 . PHE A 1 130 ? -7.869  10.143  14.974  1.00 9.12  ? 131 PHE A CD1 1 
ATOM   1145 C  CD2 . PHE A 1 130 ? -5.834  10.985  13.908  1.00 11.11 ? 131 PHE A CD2 1 
ATOM   1146 C  CE1 . PHE A 1 130 ? -7.232  8.945   15.151  1.00 10.92 ? 131 PHE A CE1 1 
ATOM   1147 C  CE2 . PHE A 1 130 ? -5.211  9.760   14.046  1.00 14.24 ? 131 PHE A CE2 1 
ATOM   1148 C  CZ  . PHE A 1 130 ? -5.900  8.736   14.707  1.00 11.74 ? 131 PHE A CZ  1 
ATOM   1149 N  N   . GLY A 1 131 ? -5.574  14.551  14.791  1.00 12.00 ? 132 GLY A N   1 
ATOM   1150 C  CA  . GLY A 1 131 ? -4.153  14.657  15.106  1.00 12.05 ? 132 GLY A CA  1 
ATOM   1151 C  C   . GLY A 1 131 ? -3.878  15.323  16.441  1.00 12.57 ? 132 GLY A C   1 
ATOM   1152 O  O   . GLY A 1 131 ? -2.847  15.055  17.069  1.00 14.23 ? 132 GLY A O   1 
ATOM   1153 N  N   . LYS A 1 132 ? -4.719  16.316  16.838  1.00 11.30 ? 133 LYS A N   1 
ATOM   1154 C  CA  . LYS A 1 132 ? -4.551  16.878  18.215  1.00 11.46 ? 133 LYS A CA  1 
ATOM   1155 C  C   . LYS A 1 132 ? -5.079  15.894  19.284  1.00 9.27  ? 133 LYS A C   1 
ATOM   1156 O  O   . LYS A 1 132 ? -4.500  15.821  20.423  1.00 11.28 ? 133 LYS A O   1 
ATOM   1157 C  CB  . LYS A 1 132 ? -5.305  18.187  18.343  1.00 11.85 ? 133 LYS A CB  1 
ATOM   1158 C  CG  . LYS A 1 132 ? -4.596  19.348  17.536  1.00 14.35 ? 133 LYS A CG  1 
ATOM   1159 C  CD  . LYS A 1 132 ? -3.154  19.486  18.026  1.00 21.69 ? 133 LYS A CD  1 
ATOM   1160 C  CE  . LYS A 1 132 ? -3.089  20.348  19.276  1.00 31.29 ? 133 LYS A CE  1 
ATOM   1161 N  NZ  . LYS A 1 132 ? -2.823  21.711  18.743  1.00 38.07 ? 133 LYS A NZ  1 
ATOM   1162 N  N   . ALA A 1 133 ? -6.162  15.162  18.935  1.00 9.13  ? 134 ALA A N   1 
ATOM   1163 C  CA  . ALA A 1 133 ? -6.709  14.238  19.952  1.00 8.21  ? 134 ALA A CA  1 
ATOM   1164 C  C   . ALA A 1 133 ? -5.703  13.134  20.356  1.00 8.12  ? 134 ALA A C   1 
ATOM   1165 O  O   . ALA A 1 133 ? -5.692  12.728  21.521  1.00 9.19  ? 134 ALA A O   1 
ATOM   1166 C  CB  . ALA A 1 133 ? -8.012  13.572  19.393  1.00 8.87  ? 134 ALA A CB  1 
ATOM   1167 N  N   . VAL A 1 134 ? -4.894  12.633  19.417  1.00 9.45  ? 135 VAL A N   1 
ATOM   1168 C  CA  . VAL A 1 134 ? -4.003  11.517  19.804  1.00 9.73  ? 135 VAL A CA  1 
ATOM   1169 C  C   . VAL A 1 134 ? -2.893  11.970  20.757  1.00 9.04  ? 135 VAL A C   1 
ATOM   1170 O  O   . VAL A 1 134 ? -2.175  11.108  21.306  1.00 10.20 ? 135 VAL A O   1 
ATOM   1171 C  CB  . VAL A 1 134 ? -3.326  10.793  18.613  1.00 10.13 ? 135 VAL A CB  1 
ATOM   1172 C  CG1 . VAL A 1 134 ? -4.388  10.092  17.753  1.00 12.06 ? 135 VAL A CG1 1 
ATOM   1173 C  CG2 . VAL A 1 134 ? -2.512  11.727  17.792  1.00 11.43 ? 135 VAL A CG2 1 
ATOM   1174 N  N   . GLN A 1 135 ? -2.773  13.322  20.972  1.00 8.99  ? 136 GLN A N   1 
ATOM   1175 C  CA  . GLN A 1 135 ? -1.783  13.795  21.947  1.00 11.12 ? 136 GLN A CA  1 
ATOM   1176 C  C   . GLN A 1 135 ? -2.320  13.935  23.324  1.00 10.71 ? 136 GLN A C   1 
ATOM   1177 O  O   . GLN A 1 135 ? -1.665  14.501  24.252  1.00 12.37 ? 136 GLN A O   1 
ATOM   1178 C  CB  . GLN A 1 135 ? -1.198  15.151  21.390  1.00 12.02 ? 136 GLN A CB  1 
ATOM   1179 C  CG  . GLN A 1 135 ? -0.574  14.996  20.025  1.00 14.34 ? 136 GLN A CG  1 
ATOM   1180 C  CD  . GLN A 1 135 ? -0.160  16.337  19.457  1.00 18.45 ? 136 GLN A CD  1 
ATOM   1181 O  OE1 . GLN A 1 135 ? -0.633  16.772  18.354  1.00 27.10 ? 136 GLN A OE1 1 
ATOM   1182 N  NE2 . GLN A 1 135 ? 0.713   17.023  20.196  1.00 22.23 ? 136 GLN A NE2 1 
ATOM   1183 N  N   . GLN A 1 136 ? -3.540  13.406  23.526  1.00 9.76  ? 137 GLN A N   1 
ATOM   1184 C  CA  . GLN A 1 136 ? -4.232  13.613  24.854  1.00 9.75  ? 137 GLN A CA  1 
ATOM   1185 C  C   . GLN A 1 136 ? -4.626  12.261  25.453  1.00 8.60  ? 137 GLN A C   1 
ATOM   1186 O  O   . GLN A 1 136 ? -4.973  11.330  24.679  1.00 8.37  ? 137 GLN A O   1 
ATOM   1187 C  CB  . GLN A 1 136 ? -5.525  14.433  24.663  1.00 9.40  ? 137 GLN A CB  1 
ATOM   1188 C  CG  . GLN A 1 136 ? -5.296  15.817  23.914  1.00 14.46 ? 137 GLN A CG  1 
ATOM   1189 C  CD  . GLN A 1 136 ? -4.342  16.758  24.731  1.00 14.98 ? 137 GLN A CD  1 
ATOM   1190 O  OE1 . GLN A 1 136 ? -4.148  16.547  25.891  1.00 17.69 ? 137 GLN A OE1 1 
ATOM   1191 N  NE2 . GLN A 1 136 ? -3.670  17.699  24.055  1.00 23.04 ? 137 GLN A NE2 1 
ATOM   1192 N  N   . PRO A 1 137 ? -4.613  12.149  26.783  1.00 9.31  ? 138 PRO A N   1 
ATOM   1193 C  CA  . PRO A 1 137 ? -4.868  10.823  27.379  1.00 9.71  ? 138 PRO A CA  1 
ATOM   1194 C  C   . PRO A 1 137 ? -6.343  10.352  27.247  1.00 10.03 ? 138 PRO A C   1 
ATOM   1195 O  O   . PRO A 1 137 ? -6.600  9.134   27.357  1.00 12.68 ? 138 PRO A O   1 
ATOM   1196 C  CB  . PRO A 1 137 ? -4.547  10.972  28.862  1.00 12.06 ? 138 PRO A CB  1 
ATOM   1197 C  CG  . PRO A 1 137 ? -4.390  12.366  29.078  1.00 15.93 ? 138 PRO A CG  1 
ATOM   1198 C  CD  . PRO A 1 137 ? -4.164  13.141  27.768  1.00 10.86 ? 138 PRO A CD  1 
ATOM   1199 N  N   . ASP A 1 138 ? -7.255  11.290  26.943  1.00 8.17  ? 139 ASP A N   1 
ATOM   1200 C  CA  . ASP A 1 138 ? -8.662  10.940  26.691  1.00 8.54  ? 139 ASP A CA  1 
ATOM   1201 C  C   . ASP A 1 138 ? -8.983  11.341  25.211  1.00 7.45  ? 139 ASP A C   1 
ATOM   1202 O  O   . ASP A 1 138 ? -10.124 11.759  24.995  1.00 8.88  ? 139 ASP A O   1 
ATOM   1203 C  CB  . ASP A 1 138 ? -9.612  11.612  27.729  1.00 9.92  ? 139 ASP A CB  1 
ATOM   1204 C  CG  . ASP A 1 138 ? -9.502  13.117  27.721  1.00 11.56 ? 139 ASP A CG  1 
ATOM   1205 O  OD1 . ASP A 1 138 ? -8.548  13.679  27.114  1.00 11.14 ? 139 ASP A OD1 1 
ATOM   1206 O  OD2 . ASP A 1 138 ? -10.350 13.729  28.395  1.00 15.00 ? 139 ASP A OD2 1 
ATOM   1207 N  N   . GLY A 1 139 ? -8.008  11.218  24.265  1.00 6.85  ? 140 GLY A N   1 
ATOM   1208 C  CA  . GLY A 1 139 ? -8.291  11.722  22.935  1.00 6.66  ? 140 GLY A CA  1 
ATOM   1209 C  C   . GLY A 1 139 ? -9.134  10.809  22.046  1.00 6.44  ? 140 GLY A C   1 
ATOM   1210 O  O   . GLY A 1 139 ? -9.854  11.315  21.180  1.00 7.32  ? 140 GLY A O   1 
ATOM   1211 N  N   . LEU A 1 140 ? -8.980  9.479   22.240  1.00 4.92  ? 141 LEU A N   1 
ATOM   1212 C  CA  . LEU A 1 140 ? -9.692  8.545   21.351  1.00 5.56  ? 141 LEU A CA  1 
ATOM   1213 C  C   . LEU A 1 140 ? -10.546 7.571   22.122  1.00 5.76  ? 141 LEU A C   1 
ATOM   1214 O  O   . LEU A 1 140 ? -10.240 7.290   23.307  1.00 6.37  ? 141 LEU A O   1 
ATOM   1215 C  CB  . LEU A 1 140 ? -8.675  7.730   20.537  1.00 6.01  ? 141 LEU A CB  1 
ATOM   1216 C  CG  . LEU A 1 140 ? -7.713  8.375   19.530  1.00 9.47  ? 141 LEU A CG  1 
ATOM   1217 C  CD1 . LEU A 1 140 ? -7.064  7.299   18.656  1.00 7.98  ? 141 LEU A CD1 1 
ATOM   1218 C  CD2 . LEU A 1 140 ? -8.410  9.427   18.675  1.00 13.74 ? 141 LEU A CD2 1 
ATOM   1219 N  N   . ALA A 1 141 ? -11.609 7.074   21.417  1.00 5.96  ? 142 ALA A N   1 
ATOM   1220 C  CA  . ALA A 1 141 ? -12.346 5.929   21.952  1.00 5.51  ? 142 ALA A CA  1 
ATOM   1221 C  C   . ALA A 1 141 ? -12.410 4.930   20.873  1.00 6.02  ? 142 ALA A C   1 
ATOM   1222 O  O   . ALA A 1 141 ? -12.801 5.271   19.748  1.00 7.84  ? 142 ALA A O   1 
ATOM   1223 C  CB  . ALA A 1 141 ? -13.786 6.342   22.378  1.00 7.16  ? 142 ALA A CB  1 
ATOM   1224 N  N   . VAL A 1 142 ? -11.854 3.706   21.123  1.00 6.38  ? 143 VAL A N   1 
ATOM   1225 C  CA  . VAL A 1 142 ? -11.861 2.668   20.081  1.00 5.87  ? 143 VAL A CA  1 
ATOM   1226 C  C   . VAL A 1 142 ? -12.868 1.588   20.566  1.00 6.05  ? 143 VAL A C   1 
ATOM   1227 O  O   . VAL A 1 142 ? -12.743 1.070   21.703  1.00 5.81  ? 143 VAL A O   1 
ATOM   1228 C  CB  . VAL A 1 142 ? -10.474 2.061   19.718  1.00 5.21  ? 143 VAL A CB  1 
ATOM   1229 C  CG1 . VAL A 1 142 ? -10.642 1.054   18.568  1.00 6.89  ? 143 VAL A CG1 1 
ATOM   1230 C  CG2 . VAL A 1 142 ? -9.529  3.200   19.285  1.00 7.38  ? 143 VAL A CG2 1 
ATOM   1231 N  N   . LEU A 1 143 ? -13.852 1.295   19.704  1.00 5.18  ? 144 LEU A N   1 
ATOM   1232 C  CA  . LEU A 1 143 ? -14.869 0.250   19.993  1.00 5.75  ? 144 LEU A CA  1 
ATOM   1233 C  C   . LEU A 1 143 ? -14.301 -0.997  19.295  1.00 5.42  ? 144 LEU A C   1 
ATOM   1234 O  O   . LEU A 1 143 ? -14.196 -1.060  18.076  1.00 5.70  ? 144 LEU A O   1 
ATOM   1235 C  CB  . LEU A 1 143 ? -16.210 0.726   19.442  1.00 6.76  ? 144 LEU A CB  1 
ATOM   1236 C  CG  . LEU A 1 143 ? -17.332 -0.306  19.533  1.00 8.35  ? 144 LEU A CG  1 
ATOM   1237 C  CD1 . LEU A 1 143 ? -17.591 -0.632  21.003  1.00 9.67  ? 144 LEU A CD1 1 
ATOM   1238 C  CD2 . LEU A 1 143 ? -18.648 0.278   18.927  1.00 9.75  ? 144 LEU A CD2 1 
ATOM   1239 N  N   . GLY A 1 144 ? -14.022 -2.035  20.105  1.00 4.65  ? 145 GLY A N   1 
ATOM   1240 C  CA  . GLY A 1 144 ? -13.473 -3.276  19.594  1.00 5.62  ? 145 GLY A CA  1 
ATOM   1241 C  C   . GLY A 1 144 ? -14.568 -4.374  19.613  1.00 5.42  ? 145 GLY A C   1 
ATOM   1242 O  O   . GLY A 1 144 ? -15.314 -4.527  20.613  1.00 6.16  ? 145 GLY A O   1 
ATOM   1243 N  N   . ILE A 1 145 ? -14.624 -5.131  18.483  1.00 5.14  ? 146 ILE A N   1 
ATOM   1244 C  CA  . ILE A 1 145 ? -15.665 -6.175  18.375  1.00 5.19  ? 146 ILE A CA  1 
ATOM   1245 C  C   . ILE A 1 145 ? -14.946 -7.425  17.845  1.00 6.23  ? 146 ILE A C   1 
ATOM   1246 O  O   . ILE A 1 145 ? -14.245 -7.406  16.821  1.00 6.74  ? 146 ILE A O   1 
ATOM   1247 C  CB  . ILE A 1 145 ? -16.786 -5.735  17.348  1.00 6.58  ? 146 ILE A CB  1 
ATOM   1248 C  CG1 . ILE A 1 145 ? -17.403 -4.399  17.874  1.00 9.36  ? 146 ILE A CG1 1 
ATOM   1249 C  CG2 . ILE A 1 145 ? -17.798 -6.826  17.128  1.00 9.04  ? 146 ILE A CG2 1 
ATOM   1250 C  CD1 . ILE A 1 145 ? -18.526 -3.772  16.949  1.00 7.79  ? 146 ILE A CD1 1 
ATOM   1251 N  N   . PHE A 1 146 ? -15.155 -8.535  18.550  1.00 5.43  ? 147 PHE A N   1 
ATOM   1252 C  CA  . PHE A 1 146 ? -14.519 -9.833  18.110  1.00 6.61  ? 147 PHE A CA  1 
ATOM   1253 C  C   . PHE A 1 146 ? -15.281 -10.420 16.929  1.00 6.80  ? 147 PHE A C   1 
ATOM   1254 O  O   . PHE A 1 146 ? -16.528 -10.293 16.857  1.00 7.80  ? 147 PHE A O   1 
ATOM   1255 C  CB  . PHE A 1 146 ? -14.520 -10.785 19.275  1.00 5.64  ? 147 PHE A CB  1 
ATOM   1256 C  CG  . PHE A 1 146 ? -13.659 -10.300 20.431  1.00 4.36  ? 147 PHE A CG  1 
ATOM   1257 C  CD1 . PHE A 1 146 ? -12.277 -10.148 20.243  1.00 5.61  ? 147 PHE A CD1 1 
ATOM   1258 C  CD2 . PHE A 1 146 ? -14.202 -10.065 21.693  1.00 7.15  ? 147 PHE A CD2 1 
ATOM   1259 C  CE1 . PHE A 1 146 ? -11.441 -9.747  21.309  1.00 6.77  ? 147 PHE A CE1 1 
ATOM   1260 C  CE2 . PHE A 1 146 ? -13.419 -9.697  22.767  1.00 6.08  ? 147 PHE A CE2 1 
ATOM   1261 C  CZ  . PHE A 1 146 ? -12.045 -9.555  22.570  1.00 6.34  ? 147 PHE A CZ  1 
ATOM   1262 N  N   . LEU A 1 147 ? -14.549 -11.161 16.081  1.00 5.65  ? 148 LEU A N   1 
ATOM   1263 C  CA  . LEU A 1 147 ? -15.142 -11.918 14.966  1.00 6.62  ? 148 LEU A CA  1 
ATOM   1264 C  C   . LEU A 1 147 ? -14.807 -13.411 15.231  1.00 6.14  ? 148 LEU A C   1 
ATOM   1265 O  O   . LEU A 1 147 ? -13.630 -13.745 15.433  1.00 7.24  ? 148 LEU A O   1 
ATOM   1266 C  CB  . LEU A 1 147 ? -14.496 -11.535 13.617  1.00 7.26  ? 148 LEU A CB  1 
ATOM   1267 C  CG  . LEU A 1 147 ? -15.069 -10.262 12.957  1.00 8.32  ? 148 LEU A CG  1 
ATOM   1268 C  CD1 . LEU A 1 147 ? -14.817 -9.004  13.821  1.00 9.07  ? 148 LEU A CD1 1 
ATOM   1269 C  CD2 . LEU A 1 147 ? -14.462 -10.090 11.579  1.00 10.06 ? 148 LEU A CD2 1 
ATOM   1270 N  N   . LYS A 1 148 ? -15.834 -14.273 15.147  1.00 7.83  ? 149 LYS A N   1 
ATOM   1271 C  CA  . LYS A 1 148 ? -15.633 -15.718 15.093  1.00 8.87  ? 149 LYS A CA  1 
ATOM   1272 C  C   . LYS A 1 148 ? -16.163 -16.205 13.712  1.00 8.44  ? 149 LYS A C   1 
ATOM   1273 O  O   . LYS A 1 148 ? -16.981 -15.555 13.060  1.00 9.21  ? 149 LYS A O   1 
ATOM   1274 C  CB  . LYS A 1 148 ? -16.420 -16.400 16.245  1.00 9.07  ? 149 LYS A CB  1 
ATOM   1275 C  CG  . LYS A 1 148 ? -17.947 -16.297 16.179  1.00 10.92 ? 149 LYS A CG  1 
ATOM   1276 C  CD  . LYS A 1 148 ? -18.540 -16.960 17.443  1.00 16.30 ? 149 LYS A CD  1 
ATOM   1277 C  CE  . LYS A 1 148 ? -20.053 -16.953 17.303  1.00 23.32 ? 149 LYS A CE  1 
ATOM   1278 N  NZ  . LYS A 1 148 ? -20.707 -17.914 18.317  1.00 28.07 ? 149 LYS A NZ  1 
ATOM   1279 N  N   . VAL A 1 149 ? -15.648 -17.356 13.290  1.00 8.87  ? 150 VAL A N   1 
ATOM   1280 C  CA  . VAL A 1 149 ? -16.047 -17.954 12.043  1.00 9.34  ? 150 VAL A CA  1 
ATOM   1281 C  C   . VAL A 1 149 ? -17.246 -18.914 12.212  1.00 10.71 ? 150 VAL A C   1 
ATOM   1282 O  O   . VAL A 1 149 ? -17.225 -19.862 13.015  1.00 12.34 ? 150 VAL A O   1 
ATOM   1283 C  CB  . VAL A 1 149 ? -14.811 -18.729 11.449  1.00 9.75  ? 150 VAL A CB  1 
ATOM   1284 C  CG1 . VAL A 1 149 ? -15.213 -19.502 10.129  1.00 12.14 ? 150 VAL A CG1 1 
ATOM   1285 C  CG2 . VAL A 1 149 ? -13.736 -17.721 11.096  1.00 12.99 ? 150 VAL A CG2 1 
ATOM   1286 N  N   . GLY A 1 150 ? -18.281 -18.608 11.456  1.00 9.20  ? 151 GLY A N   1 
ATOM   1287 C  CA  . GLY A 1 150 ? -19.556 -19.411 11.528  1.00 12.11 ? 151 GLY A CA  1 
ATOM   1288 C  C   . GLY A 1 150 ? -20.436 -18.971 10.387  1.00 10.71 ? 151 GLY A C   1 
ATOM   1289 O  O   . GLY A 1 150 ? -20.004 -19.073 9.210   1.00 10.99 ? 151 GLY A O   1 
ATOM   1290 N  N   A SER A 1 151 ? -21.622 -18.458 10.762  0.50 11.71 ? 152 SER A N   1 
ATOM   1291 N  N   B SER A 1 151 ? -21.650 -18.484 10.708  0.50 12.03 ? 152 SER A N   1 
ATOM   1292 C  CA  A SER A 1 151 ? -22.532 -17.811 9.822   0.50 11.57 ? 152 SER A CA  1 
ATOM   1293 C  CA  B SER A 1 151 ? -22.509 -17.910 9.662   0.50 12.35 ? 152 SER A CA  1 
ATOM   1294 C  C   A SER A 1 151 ? -21.866 -16.592 9.134   0.50 11.51 ? 152 SER A C   1 
ATOM   1295 C  C   B SER A 1 151 ? -21.953 -16.594 9.147   0.50 11.56 ? 152 SER A C   1 
ATOM   1296 O  O   A SER A 1 151 ? -20.972 -15.942 9.725   0.50 11.00 ? 152 SER A O   1 
ATOM   1297 O  O   B SER A 1 151 ? -21.291 -15.849 9.891   0.50 10.69 ? 152 SER A O   1 
ATOM   1298 C  CB  A SER A 1 151 ? -23.803 -17.387 10.549  0.50 13.75 ? 152 SER A CB  1 
ATOM   1299 C  CB  B SER A 1 151 ? -23.897 -17.617 10.170  0.50 14.43 ? 152 SER A CB  1 
ATOM   1300 O  OG  A SER A 1 151 ? -24.499 -18.517 11.079  0.50 15.25 ? 152 SER A OG  1 
ATOM   1301 O  OG  B SER A 1 151 ? -23.800 -16.667 11.212  0.50 18.73 ? 152 SER A OG  1 
ATOM   1302 N  N   . ALA A 1 152 ? -22.244 -16.296 7.870   1.00 10.63 ? 153 ALA A N   1 
ATOM   1303 C  CA  . ALA A 1 152 ? -21.784 -15.049 7.283   1.00 11.53 ? 153 ALA A CA  1 
ATOM   1304 C  C   . ALA A 1 152 ? -22.408 -13.819 7.989   1.00 11.52 ? 153 ALA A C   1 
ATOM   1305 O  O   . ALA A 1 152 ? -23.541 -13.865 8.468   1.00 13.43 ? 153 ALA A O   1 
ATOM   1306 C  CB  . ALA A 1 152 ? -22.175 -14.989 5.764   1.00 12.71 ? 153 ALA A CB  1 
ATOM   1307 N  N   . LYS A 1 153 ? -21.696 -12.685 7.876   1.00 11.56 ? 154 LYS A N   1 
ATOM   1308 C  CA  . LYS A 1 153 ? -22.251 -11.361 8.276   1.00 11.17 ? 154 LYS A CA  1 
ATOM   1309 C  C   . LYS A 1 153 ? -22.676 -10.575 7.043   1.00 10.86 ? 154 LYS A C   1 
ATOM   1310 O  O   . LYS A 1 153 ? -21.844 -10.154 6.307   1.00 11.10 ? 154 LYS A O   1 
ATOM   1311 C  CB  . LYS A 1 153 ? -21.197 -10.595 9.096   1.00 11.41 ? 154 LYS A CB  1 
ATOM   1312 C  CG  . LYS A 1 153 ? -21.734 -9.408  9.910   1.00 13.14 ? 154 LYS A CG  1 
ATOM   1313 C  CD  . LYS A 1 153 ? -22.607 -9.798  11.053  1.00 14.31 ? 154 LYS A CD  1 
ATOM   1314 C  CE  . LYS A 1 153 ? -22.861 -8.626  12.040  1.00 17.42 ? 154 LYS A CE  1 
ATOM   1315 N  NZ  . LYS A 1 153 ? -23.907 -9.004  12.970  1.00 24.47 ? 154 LYS A NZ  1 
ATOM   1316 N  N   . PRO A 1 154 ? -24.004 -10.529 6.740   1.00 12.69 ? 155 PRO A N   1 
ATOM   1317 C  CA  . PRO A 1 154 ? -24.414 -9.918  5.454   1.00 14.43 ? 155 PRO A CA  1 
ATOM   1318 C  C   . PRO A 1 154 ? -23.892 -8.504  5.339   1.00 12.64 ? 155 PRO A C   1 
ATOM   1319 O  O   . PRO A 1 154 ? -23.434 -8.086  4.259   1.00 14.51 ? 155 PRO A O   1 
ATOM   1320 C  CB  . PRO A 1 154 ? -25.951 -9.995  5.553   1.00 14.04 ? 155 PRO A CB  1 
ATOM   1321 C  CG  . PRO A 1 154 ? -26.274 -11.207 6.506   1.00 18.03 ? 155 PRO A CG  1 
ATOM   1322 C  CD  . PRO A 1 154 ? -25.169 -11.074 7.535   1.00 14.43 ? 155 PRO A CD  1 
ATOM   1323 N  N   . GLY A 1 155 ? -23.846 -7.783  6.452   1.00 12.05 ? 156 GLY A N   1 
ATOM   1324 C  CA  . GLY A 1 155 ? -23.438 -6.350  6.464   1.00 11.09 ? 156 GLY A CA  1 
ATOM   1325 C  C   . GLY A 1 155 ? -21.940 -6.165  6.182   1.00 12.08 ? 156 GLY A C   1 
ATOM   1326 O  O   . GLY A 1 155 ? -21.503 -5.020  5.936   1.00 14.84 ? 156 GLY A O   1 
ATOM   1327 N  N   . LEU A 1 156 ? -21.156 -7.234  6.279   1.00 12.66 ? 157 LEU A N   1 
ATOM   1328 C  CA  . LEU A 1 156 ? -19.758 -7.221  5.935   1.00 10.66 ? 157 LEU A CA  1 
ATOM   1329 C  C   . LEU A 1 156 ? -19.452 -7.421  4.423   1.00 10.84 ? 157 LEU A C   1 
ATOM   1330 O  O   . LEU A 1 156 ? -18.326 -7.095  3.924   1.00 11.72 ? 157 LEU A O   1 
ATOM   1331 C  CB  . LEU A 1 156 ? -19.029 -8.272  6.769   1.00 12.35 ? 157 LEU A CB  1 
ATOM   1332 C  CG  . LEU A 1 156 ? -17.485 -8.370  6.600   1.00 10.55 ? 157 LEU A CG  1 
ATOM   1333 C  CD1 . LEU A 1 156 ? -16.675 -7.109  6.992   1.00 12.94 ? 157 LEU A CD1 1 
ATOM   1334 C  CD2 . LEU A 1 156 ? -16.820 -9.536  7.393   1.00 12.33 ? 157 LEU A CD2 1 
ATOM   1335 N  N   . GLN A 1 157 ? -20.425 -7.958  3.681   1.00 11.52 ? 158 GLN A N   1 
ATOM   1336 C  CA  . GLN A 1 157 ? -20.135 -8.428  2.327   1.00 13.25 ? 158 GLN A CA  1 
ATOM   1337 C  C   . GLN A 1 157 ? -19.681 -7.309  1.396   1.00 12.82 ? 158 GLN A C   1 
ATOM   1338 O  O   . GLN A 1 157 ? -18.790 -7.545  0.564   1.00 13.86 ? 158 GLN A O   1 
ATOM   1339 C  CB  . GLN A 1 157 ? -21.286 -9.290  1.761   1.00 14.34 ? 158 GLN A CB  1 
ATOM   1340 C  CG  . GLN A 1 157 ? -20.845 -10.038 0.430   1.00 14.25 ? 158 GLN A CG  1 
ATOM   1341 C  CD  . GLN A 1 157 ? -19.682 -11.010 0.701   1.00 13.51 ? 158 GLN A CD  1 
ATOM   1342 O  OE1 . GLN A 1 157 ? -19.625 -11.610 1.824   1.00 15.92 ? 158 GLN A OE1 1 
ATOM   1343 N  NE2 . GLN A 1 157 ? -18.826 -11.288 -0.307  1.00 14.93 ? 158 GLN A NE2 1 
ATOM   1344 N  N   A LYS A 1 158 ? -20.258 -6.105  1.522   0.50 13.75 ? 159 LYS A N   1 
ATOM   1345 N  N   B LYS A 1 158 ? -20.266 -6.104  1.499   0.50 13.63 ? 159 LYS A N   1 
ATOM   1346 C  CA  A LYS A 1 158 ? -19.838 -4.984  0.651   0.50 13.46 ? 159 LYS A CA  1 
ATOM   1347 C  CA  B LYS A 1 158 ? -19.805 -4.981  0.646   0.50 13.41 ? 159 LYS A CA  1 
ATOM   1348 C  C   A LYS A 1 158 ? -18.344 -4.576  0.868   0.50 13.96 ? 159 LYS A C   1 
ATOM   1349 C  C   B LYS A 1 158 ? -18.272 -4.756  0.811   0.50 13.17 ? 159 LYS A C   1 
ATOM   1350 O  O   A LYS A 1 158 ? -17.705 -4.029  -0.023  0.50 14.19 ? 159 LYS A O   1 
ATOM   1351 O  O   B LYS A 1 158 ? -17.539 -4.515  -0.158  0.50 11.56 ? 159 LYS A O   1 
ATOM   1352 C  CB  A LYS A 1 158 ? -20.830 -3.812  0.769   0.50 14.60 ? 159 LYS A CB  1 
ATOM   1353 C  CB  B LYS A 1 158 ? -20.620 -3.709  0.943   0.50 14.30 ? 159 LYS A CB  1 
ATOM   1354 C  CG  A LYS A 1 158 ? -22.200 -4.088  0.128   0.50 17.77 ? 159 LYS A CG  1 
ATOM   1355 C  CG  B LYS A 1 158 ? -20.307 -2.522  0.035   0.50 16.20 ? 159 LYS A CG  1 
ATOM   1356 C  CD  A LYS A 1 158 ? -22.327 -3.516  -1.302  0.50 25.96 ? 159 LYS A CD  1 
ATOM   1357 C  CD  B LYS A 1 158 ? -21.101 -1.223  0.461   0.50 16.09 ? 159 LYS A CD  1 
ATOM   1358 C  CE  A LYS A 1 158 ? -23.773 -3.346  -1.747  0.50 25.01 ? 159 LYS A CE  1 
ATOM   1359 C  CE  B LYS A 1 158 ? -20.726 0.087   -0.346  0.50 17.11 ? 159 LYS A CE  1 
ATOM   1360 N  NZ  A LYS A 1 158 ? -24.394 -4.604  -2.374  0.50 29.73 ? 159 LYS A NZ  1 
ATOM   1361 N  NZ  B LYS A 1 158 ? -21.235 -0.053  -1.831  0.50 16.51 ? 159 LYS A NZ  1 
ATOM   1362 N  N   . VAL A 1 159 ? -17.797 -4.862  2.064   1.00 12.69 ? 160 VAL A N   1 
ATOM   1363 C  CA  . VAL A 1 159 ? -16.386 -4.604  2.343   1.00 11.88 ? 160 VAL A CA  1 
ATOM   1364 C  C   . VAL A 1 159 ? -15.584 -5.743  1.658   1.00 12.38 ? 160 VAL A C   1 
ATOM   1365 O  O   . VAL A 1 159 ? -14.602 -5.505  0.920   1.00 13.07 ? 160 VAL A O   1 
ATOM   1366 C  CB  . VAL A 1 159 ? -16.137 -4.610  3.844   1.00 12.67 ? 160 VAL A CB  1 
ATOM   1367 C  CG1 . VAL A 1 159 ? -14.593 -4.624  4.173   1.00 12.89 ? 160 VAL A CG1 1 
ATOM   1368 C  CG2 . VAL A 1 159 ? -16.799 -3.356  4.462   1.00 14.25 ? 160 VAL A CG2 1 
ATOM   1369 N  N   . VAL A 1 160 ? -16.009 -6.986  1.879   1.00 10.85 ? 161 VAL A N   1 
ATOM   1370 C  CA  . VAL A 1 160 ? -15.282 -8.124  1.325   1.00 13.67 ? 161 VAL A CA  1 
ATOM   1371 C  C   . VAL A 1 160 ? -15.170 -8.018  -0.192  1.00 13.20 ? 161 VAL A C   1 
ATOM   1372 O  O   . VAL A 1 160 ? -14.125 -8.309  -0.795  1.00 14.39 ? 161 VAL A O   1 
ATOM   1373 C  CB  . VAL A 1 160 ? -16.027 -9.499  1.748   1.00 12.89 ? 161 VAL A CB  1 
ATOM   1374 C  CG1 . VAL A 1 160 ? -15.615 -10.653 0.870   1.00 16.57 ? 161 VAL A CG1 1 
ATOM   1375 C  CG2 . VAL A 1 160 ? -15.684 -9.671  3.238   1.00 16.97 ? 161 VAL A CG2 1 
ATOM   1376 N  N   . ASP A 1 161 ? -16.268 -7.631  -0.816  1.00 14.35 ? 162 ASP A N   1 
ATOM   1377 C  CA  . ASP A 1 161 ? -16.266 -7.586  -2.284  1.00 16.78 ? 162 ASP A CA  1 
ATOM   1378 C  C   . ASP A 1 161 ? -15.342 -6.543  -2.968  1.00 17.63 ? 162 ASP A C   1 
ATOM   1379 O  O   . ASP A 1 161 ? -14.999 -6.721  -4.154  1.00 19.48 ? 162 ASP A O   1 
ATOM   1380 C  CB  . ASP A 1 161 ? -17.692 -7.520  -2.834  1.00 17.79 ? 162 ASP A CB  1 
ATOM   1381 C  CG  . ASP A 1 161 ? -18.407 -8.856  -2.796  1.00 17.85 ? 162 ASP A CG  1 
ATOM   1382 O  OD1 . ASP A 1 161 ? -17.710 -9.902  -2.852  1.00 21.87 ? 162 ASP A OD1 1 
ATOM   1383 O  OD2 . ASP A 1 161 ? -19.645 -8.879  -2.700  1.00 20.84 ? 162 ASP A OD2 1 
ATOM   1384 N  N   . VAL A 1 162 ? -14.954 -5.483  -2.229  1.00 15.25 ? 163 VAL A N   1 
ATOM   1385 C  CA  . VAL A 1 162 ? -14.147 -4.425  -2.831  1.00 17.16 ? 163 VAL A CA  1 
ATOM   1386 C  C   . VAL A 1 162 ? -12.656 -4.719  -2.646  1.00 15.26 ? 163 VAL A C   1 
ATOM   1387 O  O   . VAL A 1 162 ? -11.806 -4.057  -3.202  1.00 15.21 ? 163 VAL A O   1 
ATOM   1388 C  CB  . VAL A 1 162 ? -14.563 -3.038  -2.213  1.00 18.28 ? 163 VAL A CB  1 
ATOM   1389 C  CG1 . VAL A 1 162 ? -13.894 -2.831  -0.929  1.00 16.68 ? 163 VAL A CG1 1 
ATOM   1390 C  CG2 . VAL A 1 162 ? -14.373 -1.757  -3.122  1.00 18.17 ? 163 VAL A CG2 1 
ATOM   1391 N  N   . LEU A 1 163 ? -12.321 -5.720  -1.799  1.00 15.91 ? 164 LEU A N   1 
ATOM   1392 C  CA  . LEU A 1 163 ? -10.937 -5.977  -1.451  1.00 13.09 ? 164 LEU A CA  1 
ATOM   1393 C  C   . LEU A 1 163 ? -10.058 -6.352  -2.631  1.00 14.15 ? 164 LEU A C   1 
ATOM   1394 O  O   . LEU A 1 163 ? -8.838  -6.024  -2.647  1.00 15.53 ? 164 LEU A O   1 
ATOM   1395 C  CB  . LEU A 1 163 ? -10.758 -7.020  -0.362  1.00 12.70 ? 164 LEU A CB  1 
ATOM   1396 C  CG  . LEU A 1 163 ? -11.412 -6.667  0.985   1.00 13.03 ? 164 LEU A CG  1 
ATOM   1397 C  CD1 . LEU A 1 163 ? -11.137 -7.873  2.032   1.00 13.88 ? 164 LEU A CD1 1 
ATOM   1398 C  CD2 . LEU A 1 163 ? -10.880 -5.371  1.564   1.00 12.38 ? 164 LEU A CD2 1 
ATOM   1399 N  N   . ASP A 1 164 ? -10.659 -7.014  -3.644  1.00 16.77 ? 165 ASP A N   1 
ATOM   1400 C  CA  . ASP A 1 164 ? -9.750  -7.340  -4.767  1.00 19.97 ? 165 ASP A CA  1 
ATOM   1401 C  C   . ASP A 1 164 ? -9.279  -6.045  -5.514  1.00 20.43 ? 165 ASP A C   1 
ATOM   1402 O  O   . ASP A 1 164 ? -8.203  -6.098  -6.242  1.00 23.19 ? 165 ASP A O   1 
ATOM   1403 C  CB  . ASP A 1 164 ? -10.399 -8.234  -5.787  1.00 21.77 ? 165 ASP A CB  1 
ATOM   1404 C  CG  . ASP A 1 164 ? -11.367 -7.504  -6.585  1.00 23.38 ? 165 ASP A CG  1 
ATOM   1405 O  OD1 . ASP A 1 164 ? -12.368 -7.082  -5.985  1.00 26.61 ? 165 ASP A OD1 1 
ATOM   1406 O  OD2 . ASP A 1 164 ? -11.140 -7.312  -7.852  1.00 32.77 ? 165 ASP A OD2 1 
ATOM   1407 N  N   . SER A 1 165 ? -10.029 -4.926  -5.358  1.00 18.13 ? 166 SER A N   1 
ATOM   1408 C  CA  . SER A 1 165 ? -9.607  -3.661  -6.010  1.00 18.96 ? 166 SER A CA  1 
ATOM   1409 C  C   . SER A 1 165 ? -8.492  -2.917  -5.211  1.00 17.25 ? 166 SER A C   1 
ATOM   1410 O  O   . SER A 1 165 ? -7.931  -1.884  -5.693  1.00 18.99 ? 166 SER A O   1 
ATOM   1411 C  CB  . SER A 1 165 ? -10.822 -2.771  -6.235  1.00 21.87 ? 166 SER A CB  1 
ATOM   1412 O  OG  . SER A 1 165 ? -11.217 -2.212  -5.006  1.00 22.53 ? 166 SER A OG  1 
ATOM   1413 N  N   . ILE A 1 166 ? -8.215  -3.394  -3.967  1.00 14.94 ? 167 ILE A N   1 
ATOM   1414 C  CA  . ILE A 1 166 ? -7.182  -2.719  -3.148  1.00 13.62 ? 167 ILE A CA  1 
ATOM   1415 C  C   . ILE A 1 166 ? -6.144  -3.775  -2.586  1.00 13.41 ? 167 ILE A C   1 
ATOM   1416 O  O   . ILE A 1 166 ? -5.724  -3.791  -1.415  1.00 12.97 ? 167 ILE A O   1 
ATOM   1417 C  CB  . ILE A 1 166 ? -7.790  -1.876  -1.960  1.00 13.19 ? 167 ILE A CB  1 
ATOM   1418 C  CG1 . ILE A 1 166 ? -8.692  -2.723  -1.073  1.00 13.69 ? 167 ILE A CG1 1 
ATOM   1419 C  CG2 . ILE A 1 166 ? -8.498  -0.623  -2.547  1.00 14.56 ? 167 ILE A CG2 1 
ATOM   1420 C  CD1 . ILE A 1 166 ? -8.680  -2.155  0.350   1.00 15.13 ? 167 ILE A CD1 1 
ATOM   1421 N  N   . LYS A 1 167 ? -5.800  -4.693  -3.479  1.00 14.31 ? 168 LYS A N   1 
ATOM   1422 C  CA  . LYS A 1 167 ? -4.987  -5.833  -3.079  1.00 14.64 ? 168 LYS A CA  1 
ATOM   1423 C  C   . LYS A 1 167 ? -3.673  -5.455  -2.431  1.00 14.42 ? 168 LYS A C   1 
ATOM   1424 O  O   . LYS A 1 167 ? -3.320  -6.081  -1.430  1.00 14.25 ? 168 LYS A O   1 
ATOM   1425 C  CB  . LYS A 1 167 ? -4.742  -6.748  -4.297  1.00 14.34 ? 168 LYS A CB  1 
ATOM   1426 C  CG  . LYS A 1 167 ? -3.878  -8.027  -3.942  1.00 17.12 ? 168 LYS A CG  1 
ATOM   1427 C  CD  . LYS A 1 167 ? -3.594  -8.883  -5.242  1.00 20.30 ? 168 LYS A CD  1 
ATOM   1428 C  CE  . LYS A 1 167 ? -2.959  -10.108 -4.736  1.00 26.20 ? 168 LYS A CE  1 
ATOM   1429 N  NZ  . LYS A 1 167 ? -2.779  -11.077 -5.914  1.00 31.07 ? 168 LYS A NZ  1 
ATOM   1430 N  N   . THR A 1 168 ? -3.026  -4.370  -2.929  1.00 14.93 ? 169 THR A N   1 
ATOM   1431 C  CA  . THR A 1 168 ? -1.649  -4.109  -2.550  1.00 13.69 ? 169 THR A CA  1 
ATOM   1432 C  C   . THR A 1 168 ? -1.554  -2.706  -1.873  1.00 13.19 ? 169 THR A C   1 
ATOM   1433 O  O   . THR A 1 168 ? -2.469  -1.827  -1.976  1.00 15.84 ? 169 THR A O   1 
ATOM   1434 C  CB  . THR A 1 168 ? -0.655  -4.174  -3.797  1.00 16.94 ? 169 THR A CB  1 
ATOM   1435 O  OG1 . THR A 1 168 ? -1.263  -3.382  -4.833  1.00 18.15 ? 169 THR A OG1 1 
ATOM   1436 C  CG2 . THR A 1 168 ? -0.536  -5.644  -4.191  1.00 15.16 ? 169 THR A CG2 1 
ATOM   1437 N  N   . LYS A 1 169 ? -0.494  -2.583  -1.113  1.00 15.27 ? 170 LYS A N   1 
ATOM   1438 C  CA  . LYS A 1 169 ? -0.218  -1.383  -0.319  1.00 14.91 ? 170 LYS A CA  1 
ATOM   1439 C  C   . LYS A 1 169 ? -0.293  -0.128  -1.139  1.00 15.78 ? 170 LYS A C   1 
ATOM   1440 O  O   . LYS A 1 169 ? 0.265   -0.059  -2.274  1.00 17.73 ? 170 LYS A O   1 
ATOM   1441 C  CB  . LYS A 1 169 ? 1.195   -1.506  0.176   1.00 14.15 ? 170 LYS A CB  1 
ATOM   1442 C  CG  . LYS A 1 169 ? 1.686   -0.257  1.012   1.00 16.81 ? 170 LYS A CG  1 
ATOM   1443 C  CD  . LYS A 1 169 ? 2.943   -0.478  1.776   1.00 18.11 ? 170 LYS A CD  1 
ATOM   1444 C  CE  . LYS A 1 169 ? 4.025   -0.968  0.777   1.00 27.07 ? 170 LYS A CE  1 
ATOM   1445 N  NZ  . LYS A 1 169 ? 5.383   -1.180  1.398   1.00 33.52 ? 170 LYS A NZ  1 
ATOM   1446 N  N   . GLY A 1 170 ? -0.970  0.850   -0.574  1.00 15.88 ? 171 GLY A N   1 
ATOM   1447 C  CA  . GLY A 1 170 ? -1.125  2.144   -1.311  1.00 17.67 ? 171 GLY A CA  1 
ATOM   1448 C  C   . GLY A 1 170 ? -2.359  2.266   -2.255  1.00 18.83 ? 171 GLY A C   1 
ATOM   1449 O  O   . GLY A 1 170 ? -2.702  3.402   -2.680  1.00 20.49 ? 171 GLY A O   1 
ATOM   1450 N  N   . LYS A 1 171 ? -3.028  1.120   -2.577  1.00 15.24 ? 172 LYS A N   1 
ATOM   1451 C  CA  . LYS A 1 171 ? -4.312  1.195   -3.302  1.00 15.98 ? 172 LYS A CA  1 
ATOM   1452 C  C   . LYS A 1 171 ? -5.526  1.702   -2.509  1.00 14.44 ? 172 LYS A C   1 
ATOM   1453 O  O   . LYS A 1 171 ? -5.760  1.319   -1.338  1.00 15.18 ? 172 LYS A O   1 
ATOM   1454 C  CB  . LYS A 1 171 ? -4.630  -0.120  -4.027  1.00 17.09 ? 172 LYS A CB  1 
ATOM   1455 C  CG  . LYS A 1 171 ? -3.565  -0.435  -5.059  1.00 19.17 ? 172 LYS A CG  1 
ATOM   1456 C  CD  . LYS A 1 171 ? -4.077  -1.520  -6.120  1.00 21.83 ? 172 LYS A CD  1 
ATOM   1457 C  CE  . LYS A 1 171 ? -5.376  -1.155  -6.929  1.00 25.42 ? 172 LYS A CE  1 
ATOM   1458 N  NZ  . LYS A 1 171 ? -5.792  -2.239  -7.921  1.00 24.96 ? 172 LYS A NZ  1 
ATOM   1459 N  N   . SER A 1 172 ? -6.345  2.511   -3.123  1.00 15.98 ? 173 SER A N   1 
ATOM   1460 C  CA  . SER A 1 172 ? -7.607  2.959   -2.535  1.00 16.67 ? 173 SER A CA  1 
ATOM   1461 C  C   . SER A 1 172 ? -8.733  2.858   -3.566  1.00 16.47 ? 173 SER A C   1 
ATOM   1462 O  O   . SER A 1 172 ? -8.461  2.747   -4.848  1.00 19.34 ? 173 SER A O   1 
ATOM   1463 C  CB  . SER A 1 172 ? -7.469  4.417   -2.034  1.00 17.14 ? 173 SER A CB  1 
ATOM   1464 O  OG  . SER A 1 172 ? -7.180  5.316   -3.099  1.00 20.18 ? 173 SER A OG  1 
ATOM   1465 N  N   . ALA A 1 173 ? -9.966  2.891   -3.046  1.00 17.68 ? 174 ALA A N   1 
ATOM   1466 C  CA  . ALA A 1 173 ? -11.180 2.893   -3.885  1.00 17.12 ? 174 ALA A CA  1 
ATOM   1467 C  C   . ALA A 1 173 ? -12.325 3.698   -3.210  1.00 17.97 ? 174 ALA A C   1 
ATOM   1468 O  O   . ALA A 1 173 ? -12.467 3.686   -1.949  1.00 16.49 ? 174 ALA A O   1 
ATOM   1469 C  CB  . ALA A 1 173 ? -11.572 1.457   -4.189  1.00 18.41 ? 174 ALA A CB  1 
ATOM   1470 N  N   . ASP A 1 174 ? -13.151 4.338   -4.032  1.00 20.17 ? 175 ASP A N   1 
ATOM   1471 C  CA  . ASP A 1 174 ? -14.394 4.942   -3.556  1.00 19.29 ? 175 ASP A CA  1 
ATOM   1472 C  C   . ASP A 1 174 ? -15.163 3.929   -2.776  1.00 19.16 ? 175 ASP A C   1 
ATOM   1473 O  O   . ASP A 1 174 ? -15.262 2.782   -3.185  1.00 19.89 ? 175 ASP A O   1 
ATOM   1474 C  CB  . ASP A 1 174 ? -15.238 5.444   -4.775  1.00 20.49 ? 175 ASP A CB  1 
ATOM   1475 C  CG  . ASP A 1 174 ? -14.479 6.460   -5.530  1.00 27.42 ? 175 ASP A CG  1 
ATOM   1476 O  OD1 . ASP A 1 174 ? -13.725 7.215   -4.878  1.00 32.35 ? 175 ASP A OD1 1 
ATOM   1477 O  OD2 . ASP A 1 174 ? -14.592 6.523   -6.769  1.00 27.53 ? 175 ASP A OD2 1 
ATOM   1478 N  N   . PHE A 1 175 ? -15.701 4.362   -1.632  1.00 16.80 ? 176 PHE A N   1 
ATOM   1479 C  CA  . PHE A 1 175 ? -16.487 3.417   -0.841  1.00 15.30 ? 176 PHE A CA  1 
ATOM   1480 C  C   . PHE A 1 175 ? -17.491 4.230   -0.083  1.00 15.01 ? 176 PHE A C   1 
ATOM   1481 O  O   . PHE A 1 175 ? -17.355 4.506   1.141   1.00 16.87 ? 176 PHE A O   1 
ATOM   1482 C  CB  . PHE A 1 175 ? -15.528 2.612   0.068   1.00 15.62 ? 176 PHE A CB  1 
ATOM   1483 C  CG  . PHE A 1 175 ? -16.140 1.354   0.589   1.00 13.24 ? 176 PHE A CG  1 
ATOM   1484 C  CD1 . PHE A 1 175 ? -16.439 0.300   -0.278  1.00 16.64 ? 176 PHE A CD1 1 
ATOM   1485 C  CD2 . PHE A 1 175 ? -16.478 1.254   1.945   1.00 13.86 ? 176 PHE A CD2 1 
ATOM   1486 C  CE1 . PHE A 1 175 ? -17.027 -0.826  0.245   1.00 16.71 ? 176 PHE A CE1 1 
ATOM   1487 C  CE2 . PHE A 1 175 ? -17.065 0.088   2.473   1.00 15.13 ? 176 PHE A CE2 1 
ATOM   1488 C  CZ  . PHE A 1 175 ? -17.332 -0.953  1.610   1.00 16.26 ? 176 PHE A CZ  1 
ATOM   1489 N  N   . THR A 1 176 ? -18.504 4.649   -0.829  1.00 14.77 ? 177 THR A N   1 
ATOM   1490 C  CA  . THR A 1 176 ? -19.580 5.421   -0.253  1.00 15.67 ? 177 THR A CA  1 
ATOM   1491 C  C   . THR A 1 176 ? -20.782 4.616   0.227   1.00 15.29 ? 177 THR A C   1 
ATOM   1492 O  O   . THR A 1 176 ? -20.962 3.440   -0.208  1.00 14.59 ? 177 THR A O   1 
ATOM   1493 C  CB  . THR A 1 176 ? -20.021 6.531   -1.229  1.00 16.33 ? 177 THR A CB  1 
ATOM   1494 O  OG1 . THR A 1 176 ? -20.496 5.914   -2.432  1.00 19.03 ? 177 THR A OG1 1 
ATOM   1495 C  CG2 . THR A 1 176 ? -18.890 7.514   -1.517  1.00 20.33 ? 177 THR A CG2 1 
ATOM   1496 N  N   . ASN A 1 177 ? -21.600 5.198   1.099   1.00 14.27 ? 178 ASN A N   1 
ATOM   1497 C  CA  . ASN A 1 177 ? -22.878 4.649   1.534   1.00 14.61 ? 178 ASN A CA  1 
ATOM   1498 C  C   . ASN A 1 177 ? -22.711 3.344   2.301   1.00 14.63 ? 178 ASN A C   1 
ATOM   1499 O  O   . ASN A 1 177 ? -23.679 2.554   2.311   1.00 18.29 ? 178 ASN A O   1 
ATOM   1500 C  CB  . ASN A 1 177 ? -23.897 4.542   0.406   1.00 14.53 ? 178 ASN A CB  1 
ATOM   1501 C  CG  . ASN A 1 177 ? -24.136 5.919   -0.222  1.00 16.32 ? 178 ASN A CG  1 
ATOM   1502 O  OD1 . ASN A 1 177 ? -24.841 6.753   0.348   1.00 17.69 ? 178 ASN A OD1 1 
ATOM   1503 N  ND2 . ASN A 1 177 ? -23.480 6.169   -1.343  1.00 15.20 ? 178 ASN A ND2 1 
ATOM   1504 N  N   . PHE A 1 178 ? -21.531 3.119   2.921   1.00 12.48 ? 179 PHE A N   1 
ATOM   1505 C  CA  . PHE A 1 178 ? -21.377 1.883   3.713   1.00 13.06 ? 179 PHE A CA  1 
ATOM   1506 C  C   . PHE A 1 178 ? -21.907 2.160   5.102   1.00 12.12 ? 179 PHE A C   1 
ATOM   1507 O  O   . PHE A 1 178 ? -21.470 3.130   5.746   1.00 13.74 ? 179 PHE A O   1 
ATOM   1508 C  CB  . PHE A 1 178 ? -19.939 1.414   3.801   1.00 13.64 ? 179 PHE A CB  1 
ATOM   1509 C  CG  . PHE A 1 178 ? -19.810 0.188   4.647   1.00 12.20 ? 179 PHE A CG  1 
ATOM   1510 C  CD1 . PHE A 1 178 ? -20.279 -1.043  4.108   1.00 13.75 ? 179 PHE A CD1 1 
ATOM   1511 C  CD2 . PHE A 1 178 ? -19.450 0.262   5.989   1.00 11.99 ? 179 PHE A CD2 1 
ATOM   1512 C  CE1 . PHE A 1 178 ? -20.260 -2.172  4.830   1.00 14.13 ? 179 PHE A CE1 1 
ATOM   1513 C  CE2 . PHE A 1 178 ? -19.417 -0.955  6.730   1.00 10.80 ? 179 PHE A CE2 1 
ATOM   1514 C  CZ  . PHE A 1 178 ? -19.896 -2.129  6.166   1.00 12.10 ? 179 PHE A CZ  1 
ATOM   1515 N  N   . ASP A 1 179 ? -22.800 1.309   5.641   1.00 13.46 ? 180 ASP A N   1 
ATOM   1516 C  CA  . ASP A 1 179 ? -23.466 1.508   6.946   1.00 11.68 ? 180 ASP A CA  1 
ATOM   1517 C  C   . ASP A 1 179 ? -22.819 0.636   7.990   1.00 10.54 ? 180 ASP A C   1 
ATOM   1518 O  O   . ASP A 1 179 ? -23.008 -0.576  7.990   1.00 11.26 ? 180 ASP A O   1 
ATOM   1519 C  CB  . ASP A 1 179 ? -24.957 1.135   6.835   1.00 14.37 ? 180 ASP A CB  1 
ATOM   1520 C  CG  . ASP A 1 179 ? -25.768 1.559   8.008   1.00 17.74 ? 180 ASP A CG  1 
ATOM   1521 O  OD1 . ASP A 1 179 ? -25.198 1.841   9.098   1.00 13.99 ? 180 ASP A OD1 1 
ATOM   1522 O  OD2 . ASP A 1 179 ? -27.018 1.691   7.850   1.00 22.56 ? 180 ASP A OD2 1 
ATOM   1523 N  N   . PRO A 1 180 ? -22.048 1.273   8.893   1.00 9.66  ? 181 PRO A N   1 
ATOM   1524 C  CA  . PRO A 1 180 ? -21.330 0.400   9.900   1.00 10.87 ? 181 PRO A CA  1 
ATOM   1525 C  C   . PRO A 1 180 ? -22.272 -0.236  10.930  1.00 9.66  ? 181 PRO A C   1 
ATOM   1526 O  O   . PRO A 1 180 ? -21.816 -1.137  11.698  1.00 10.21 ? 181 PRO A O   1 
ATOM   1527 C  CB  . PRO A 1 180 ? -20.290 1.328   10.539  1.00 12.00 ? 181 PRO A CB  1 
ATOM   1528 C  CG  . PRO A 1 180 ? -20.956 2.704   10.422  1.00 11.90 ? 181 PRO A CG  1 
ATOM   1529 C  CD  . PRO A 1 180 ? -21.746 2.698   9.053   1.00 11.01 ? 181 PRO A CD  1 
ATOM   1530 N  N   . ARG A 1 181 ? -23.551 0.198   10.942  1.00 10.00 ? 182 ARG A N   1 
ATOM   1531 C  CA  . ARG A 1 181 ? -24.490 -0.513  11.881  1.00 10.64 ? 182 ARG A CA  1 
ATOM   1532 C  C   . ARG A 1 181 ? -24.588 -2.015  11.552  1.00 11.81 ? 182 ARG A C   1 
ATOM   1533 O  O   . ARG A 1 181 ? -24.940 -2.838  12.420  1.00 13.42 ? 182 ARG A O   1 
ATOM   1534 C  CB  . ARG A 1 181 ? -25.845 0.128   11.837  1.00 12.42 ? 182 ARG A CB  1 
ATOM   1535 C  CG  . ARG A 1 181 ? -25.763 1.549   12.407  1.00 12.28 ? 182 ARG A CG  1 
ATOM   1536 C  CD  . ARG A 1 181 ? -27.144 2.233   12.343  1.00 15.48 ? 182 ARG A CD  1 
ATOM   1537 N  NE  . ARG A 1 181 ? -27.503 2.480   10.940  1.00 14.72 ? 182 ARG A NE  1 
ATOM   1538 C  CZ  . ARG A 1 181 ? -28.628 3.114   10.606  1.00 18.52 ? 182 ARG A CZ  1 
ATOM   1539 N  NH1 . ARG A 1 181 ? -29.430 3.591   11.565  1.00 23.06 ? 182 ARG A NH1 1 
ATOM   1540 N  NH2 . ARG A 1 181 ? -28.932 3.270   9.318   1.00 21.19 ? 182 ARG A NH2 1 
ATOM   1541 N  N   . GLY A 1 182 ? -24.365 -2.358  10.308  1.00 11.71 ? 183 GLY A N   1 
ATOM   1542 C  CA  . GLY A 1 182 ? -24.450 -3.739  9.880   1.00 11.90 ? 183 GLY A CA  1 
ATOM   1543 C  C   . GLY A 1 182 ? -23.265 -4.619  10.431  1.00 13.41 ? 183 GLY A C   1 
ATOM   1544 O  O   . GLY A 1 182 ? -23.177 -5.854  10.114  1.00 15.47 ? 183 GLY A O   1 
ATOM   1545 N  N   . LEU A 1 183 ? -22.309 -4.049  11.214  1.00 10.88 ? 184 LEU A N   1 
ATOM   1546 C  CA  . LEU A 1 183 ? -21.162 -4.805  11.769  1.00 11.00 ? 184 LEU A CA  1 
ATOM   1547 C  C   . LEU A 1 183 ? -21.305 -4.999  13.273  1.00 10.46 ? 184 LEU A C   1 
ATOM   1548 O  O   . LEU A 1 183 ? -20.404 -5.575  13.880  1.00 11.86 ? 184 LEU A O   1 
ATOM   1549 C  CB  . LEU A 1 183 ? -19.819 -4.089  11.529  1.00 11.90 ? 184 LEU A CB  1 
ATOM   1550 C  CG  . LEU A 1 183 ? -19.555 -3.908  10.016  1.00 11.27 ? 184 LEU A CG  1 
ATOM   1551 C  CD1 . LEU A 1 183 ? -18.319 -3.120  9.857   1.00 12.89 ? 184 LEU A CD1 1 
ATOM   1552 C  CD2 . LEU A 1 183 ? -19.472 -5.250  9.234   1.00 15.50 ? 184 LEU A CD2 1 
ATOM   1553 N  N   . LEU A 1 184 ? -22.400 -4.531  13.846  1.00 10.42 ? 185 LEU A N   1 
ATOM   1554 C  CA  . LEU A 1 184 ? -22.581 -4.554  15.319  1.00 9.69  ? 185 LEU A CA  1 
ATOM   1555 C  C   . LEU A 1 184 ? -23.351 -5.835  15.811  1.00 12.50 ? 185 LEU A C   1 
ATOM   1556 O  O   . LEU A 1 184 ? -24.385 -6.216  15.208  1.00 17.93 ? 185 LEU A O   1 
ATOM   1557 C  CB  . LEU A 1 184 ? -23.429 -3.333  15.831  1.00 9.70  ? 185 LEU A CB  1 
ATOM   1558 C  CG  . LEU A 1 184 ? -22.805 -2.007  15.472  1.00 9.36  ? 185 LEU A CG  1 
ATOM   1559 C  CD1 . LEU A 1 184 ? -23.705 -0.854  15.912  1.00 12.02 ? 185 LEU A CD1 1 
ATOM   1560 C  CD2 . LEU A 1 184 ? -21.371 -1.814  15.995  1.00 11.25 ? 185 LEU A CD2 1 
ATOM   1561 N  N   . PRO A 1 185 ? -22.941 -6.415  16.916  1.00 11.30 ? 186 PRO A N   1 
ATOM   1562 C  CA  . PRO A 1 185 ? -23.731 -7.542  17.439  1.00 10.37 ? 186 PRO A CA  1 
ATOM   1563 C  C   . PRO A 1 185 ? -25.017 -7.004  18.086  1.00 10.67 ? 186 PRO A C   1 
ATOM   1564 O  O   . PRO A 1 185 ? -25.232 -5.800  18.172  1.00 12.58 ? 186 PRO A O   1 
ATOM   1565 C  CB  . PRO A 1 185 ? -22.770 -8.152  18.500  1.00 9.71  ? 186 PRO A CB  1 
ATOM   1566 C  CG  . PRO A 1 185 ? -22.057 -6.926  19.071  1.00 8.84  ? 186 PRO A CG  1 
ATOM   1567 C  CD  . PRO A 1 185 ? -21.814 -5.989  17.777  1.00 9.69  ? 186 PRO A CD  1 
ATOM   1568 N  N   A GLU A 1 186 ? -25.822 -7.903  18.636  0.50 11.74 ? 187 GLU A N   1 
ATOM   1569 N  N   B GLU A 1 186 ? -25.887 -7.918  18.572  0.50 11.55 ? 187 GLU A N   1 
ATOM   1570 C  CA  A GLU A 1 186 ? -27.090 -7.538  19.195  0.50 11.93 ? 187 GLU A CA  1 
ATOM   1571 C  CA  B GLU A 1 186 ? -27.132 -7.546  19.269  0.50 11.81 ? 187 GLU A CA  1 
ATOM   1572 C  C   A GLU A 1 186 ? -26.951 -6.815  20.557  0.50 11.54 ? 187 GLU A C   1 
ATOM   1573 C  C   B GLU A 1 186 ? -26.801 -6.696  20.457  0.50 10.59 ? 187 GLU A C   1 
ATOM   1574 O  O   A GLU A 1 186 ? -27.747 -5.885  20.908  0.50 13.06 ? 187 GLU A O   1 
ATOM   1575 O  O   B GLU A 1 186 ? -27.324 -5.567  20.576  0.50 11.26 ? 187 GLU A O   1 
ATOM   1576 C  CB  A GLU A 1 186 ? -27.882 -8.809  19.292  0.50 13.12 ? 187 GLU A CB  1 
ATOM   1577 C  CB  B GLU A 1 186 ? -27.915 -8.764  19.774  0.50 13.19 ? 187 GLU A CB  1 
ATOM   1578 C  CG  A GLU A 1 186 ? -28.981 -8.663  20.287  0.50 12.01 ? 187 GLU A CG  1 
ATOM   1579 C  CG  B GLU A 1 186 ? -28.907 -9.300  18.783  0.50 13.35 ? 187 GLU A CG  1 
ATOM   1580 C  CD  A GLU A 1 186 ? -29.637 -10.006 20.644  0.50 14.29 ? 187 GLU A CD  1 
ATOM   1581 C  CD  B GLU A 1 186 ? -29.604 -10.594 19.249  0.50 13.55 ? 187 GLU A CD  1 
ATOM   1582 O  OE1 A GLU A 1 186 ? -29.484 -11.006 19.861  0.50 16.81 ? 187 GLU A OE1 1 
ATOM   1583 O  OE1 B GLU A 1 186 ? -29.661 -10.880 20.488  0.50 15.82 ? 187 GLU A OE1 1 
ATOM   1584 O  OE2 A GLU A 1 186 ? -30.270 -10.031 21.729  0.50 16.98 ? 187 GLU A OE2 1 
ATOM   1585 O  OE2 B GLU A 1 186 ? -30.066 -11.296 18.329  0.50 21.53 ? 187 GLU A OE2 1 
ATOM   1586 N  N   . SER A 1 187 ? -25.991 -7.259  21.374  1.00 10.50 ? 188 SER A N   1 
ATOM   1587 C  CA  . SER A 1 187 ? -25.829 -6.684  22.716  1.00 11.11 ? 188 SER A CA  1 
ATOM   1588 C  C   . SER A 1 187 ? -24.673 -5.654  22.679  1.00 10.35 ? 188 SER A C   1 
ATOM   1589 O  O   . SER A 1 187 ? -23.607 -5.924  22.064  1.00 10.12 ? 188 SER A O   1 
ATOM   1590 C  CB  . SER A 1 187 ? -25.371 -7.738  23.705  1.00 13.00 ? 188 SER A CB  1 
ATOM   1591 O  OG  . SER A 1 187 ? -25.143 -7.160  24.990  1.00 13.23 ? 188 SER A OG  1 
ATOM   1592 N  N   . LEU A 1 188 ? -24.831 -4.557  23.426  1.00 9.45  ? 189 LEU A N   1 
ATOM   1593 C  CA  . LEU A 1 188 ? -23.728 -3.547  23.614  1.00 11.06 ? 189 LEU A CA  1 
ATOM   1594 C  C   . LEU A 1 188 ? -23.084 -3.664  25.021  1.00 9.17  ? 189 LEU A C   1 
ATOM   1595 O  O   . LEU A 1 188 ? -22.390 -2.728  25.460  1.00 11.81 ? 189 LEU A O   1 
ATOM   1596 C  CB  . LEU A 1 188 ? -24.186 -2.069  23.296  1.00 11.47 ? 189 LEU A CB  1 
ATOM   1597 C  CG  . LEU A 1 188 ? -24.648 -1.805  21.856  1.00 14.22 ? 189 LEU A CG  1 
ATOM   1598 C  CD1 . LEU A 1 188 ? -25.273 -0.389  21.705  1.00 16.40 ? 189 LEU A CD1 1 
ATOM   1599 C  CD2 . LEU A 1 188 ? -23.528 -2.045  20.784  1.00 16.94 ? 189 LEU A CD2 1 
ATOM   1600 N  N   . ASP A 1 189 ? -23.222 -4.827  25.698  1.00 10.46 ? 190 ASP A N   1 
ATOM   1601 C  CA  . ASP A 1 189 ? -22.466 -5.072  26.971  1.00 11.17 ? 190 ASP A CA  1 
ATOM   1602 C  C   . ASP A 1 189 ? -20.951 -5.037  26.636  1.00 8.91  ? 190 ASP A C   1 
ATOM   1603 O  O   . ASP A 1 189 ? -20.526 -5.540  25.559  1.00 8.99  ? 190 ASP A O   1 
ATOM   1604 C  CB  . ASP A 1 189 ? -22.768 -6.473  27.583  1.00 11.13 ? 190 ASP A CB  1 
ATOM   1605 C  CG  . ASP A 1 189 ? -24.167 -6.550  28.178  1.00 17.85 ? 190 ASP A CG  1 
ATOM   1606 O  OD1 . ASP A 1 189 ? -24.781 -5.491  28.381  1.00 21.14 ? 190 ASP A OD1 1 
ATOM   1607 O  OD2 . ASP A 1 189 ? -24.649 -7.683  28.392  1.00 21.53 ? 190 ASP A OD2 1 
ATOM   1608 N  N   . TYR A 1 190 ? -20.173 -4.434  27.557  1.00 8.48  ? 191 TYR A N   1 
ATOM   1609 C  CA  . TYR A 1 190 ? -18.787 -4.182  27.219  1.00 7.81  ? 191 TYR A CA  1 
ATOM   1610 C  C   . TYR A 1 190 ? -17.842 -4.243  28.454  1.00 7.66  ? 191 TYR A C   1 
ATOM   1611 O  O   . TYR A 1 190 ? -18.288 -4.103  29.617  1.00 8.20  ? 191 TYR A O   1 
ATOM   1612 C  CB  . TYR A 1 190 ? -18.657 -2.785  26.542  1.00 8.72  ? 191 TYR A CB  1 
ATOM   1613 C  CG  . TYR A 1 190 ? -19.006 -1.617  27.451  1.00 7.88  ? 191 TYR A CG  1 
ATOM   1614 C  CD1 . TYR A 1 190 ? -18.064 -1.041  28.333  1.00 8.58  ? 191 TYR A CD1 1 
ATOM   1615 C  CD2 . TYR A 1 190 ? -20.298 -1.117  27.404  1.00 8.74  ? 191 TYR A CD2 1 
ATOM   1616 C  CE1 . TYR A 1 190 ? -18.459 0.008   29.164  1.00 10.03 ? 191 TYR A CE1 1 
ATOM   1617 C  CE2 . TYR A 1 190 ? -20.726 -0.068  28.238  1.00 9.80  ? 191 TYR A CE2 1 
ATOM   1618 C  CZ  . TYR A 1 190 ? -19.805 0.490   29.093  1.00 11.58 ? 191 TYR A CZ  1 
ATOM   1619 O  OH  . TYR A 1 190 ? -20.190 1.533   29.946  1.00 11.28 ? 191 TYR A OH  1 
ATOM   1620 N  N   . TRP A 1 191 ? -16.541 -4.419  28.145  1.00 6.63  ? 192 TRP A N   1 
ATOM   1621 C  CA  . TRP A 1 191 ? -15.490 -4.137  29.122  1.00 6.72  ? 192 TRP A CA  1 
ATOM   1622 C  C   . TRP A 1 191 ? -14.780 -2.811  28.716  1.00 5.83  ? 192 TRP A C   1 
ATOM   1623 O  O   . TRP A 1 191 ? -14.786 -2.467  27.502  1.00 6.83  ? 192 TRP A O   1 
ATOM   1624 C  CB  . TRP A 1 191 ? -14.424 -5.241  29.079  1.00 7.46  ? 192 TRP A CB  1 
ATOM   1625 C  CG  . TRP A 1 191 ? -14.923 -6.590  29.481  1.00 6.02  ? 192 TRP A CG  1 
ATOM   1626 C  CD1 . TRP A 1 191 ? -15.167 -7.006  30.766  1.00 8.44  ? 192 TRP A CD1 1 
ATOM   1627 C  CD2 . TRP A 1 191 ? -15.228 -7.729  28.606  1.00 7.71  ? 192 TRP A CD2 1 
ATOM   1628 N  NE1 . TRP A 1 191 ? -15.571 -8.395  30.761  1.00 9.62  ? 192 TRP A NE1 1 
ATOM   1629 C  CE2 . TRP A 1 191 ? -15.613 -8.831  29.447  1.00 8.00  ? 192 TRP A CE2 1 
ATOM   1630 C  CE3 . TRP A 1 191 ? -15.119 -7.954  27.202  1.00 8.00  ? 192 TRP A CE3 1 
ATOM   1631 C  CZ2 . TRP A 1 191 ? -15.923 -10.135 28.912  1.00 9.38  ? 192 TRP A CZ2 1 
ATOM   1632 C  CZ3 . TRP A 1 191 ? -15.408 -9.232  26.690  1.00 7.60  ? 192 TRP A CZ3 1 
ATOM   1633 C  CH2 . TRP A 1 191 ? -15.813 -10.273 27.572  1.00 9.40  ? 192 TRP A CH2 1 
ATOM   1634 N  N   . THR A 1 192 ? -14.156 -2.137  29.672  1.00 5.57  ? 193 THR A N   1 
ATOM   1635 C  CA  . THR A 1 192 ? -13.464 -0.896  29.294  1.00 5.82  ? 193 THR A CA  1 
ATOM   1636 C  C   . THR A 1 192 ? -12.208 -0.707  30.163  1.00 6.33  ? 193 THR A C   1 
ATOM   1637 O  O   . THR A 1 192 ? -12.186 -1.125  31.338  1.00 6.86  ? 193 THR A O   1 
ATOM   1638 C  CB  . THR A 1 192 ? -14.433 0.353   29.409  1.00 6.13  ? 193 THR A CB  1 
ATOM   1639 O  OG1 . THR A 1 192 ? -13.725 1.534   28.993  1.00 6.47  ? 193 THR A OG1 1 
ATOM   1640 C  CG2 . THR A 1 192 ? -14.981 0.582   30.892  1.00 7.74  ? 193 THR A CG2 1 
ATOM   1641 N  N   . TYR A 1 193 ? -11.154 -0.126  29.570  1.00 6.78  ? 194 TYR A N   1 
ATOM   1642 C  CA  . TYR A 1 193 ? -9.951  0.159   30.326  1.00 6.21  ? 194 TYR A CA  1 
ATOM   1643 C  C   . TYR A 1 193 ? -9.160  1.195   29.555  1.00 7.26  ? 194 TYR A C   1 
ATOM   1644 O  O   . TYR A 1 193 ? -9.396  1.392   28.349  1.00 6.60  ? 194 TYR A O   1 
ATOM   1645 C  CB  . TYR A 1 193 ? -9.105  -1.158  30.528  1.00 6.95  ? 194 TYR A CB  1 
ATOM   1646 C  CG  . TYR A 1 193 ? -8.413  -1.631  29.245  1.00 5.25  ? 194 TYR A CG  1 
ATOM   1647 C  CD1 . TYR A 1 193 ? -9.093  -2.378  28.242  1.00 6.11  ? 194 TYR A CD1 1 
ATOM   1648 C  CD2 . TYR A 1 193 ? -7.097  -1.279  29.042  1.00 7.02  ? 194 TYR A CD2 1 
ATOM   1649 C  CE1 . TYR A 1 193 ? -8.462  -2.675  27.045  1.00 5.14  ? 194 TYR A CE1 1 
ATOM   1650 C  CE2 . TYR A 1 193 ? -6.429  -1.587  27.822  1.00 6.18  ? 194 TYR A CE2 1 
ATOM   1651 C  CZ  . TYR A 1 193 ? -7.114  -2.326  26.853  1.00 5.48  ? 194 TYR A CZ  1 
ATOM   1652 O  OH  . TYR A 1 193 ? -6.451  -2.572  25.674  1.00 5.47  ? 194 TYR A OH  1 
ATOM   1653 N  N   . PRO A 1 194 ? -8.225  1.918   30.218  1.00 5.88  ? 195 PRO A N   1 
ATOM   1654 C  CA  . PRO A 1 194 ? -7.405  2.949   29.528  1.00 6.53  ? 195 PRO A CA  1 
ATOM   1655 C  C   . PRO A 1 194 ? -6.201  2.300   28.833  1.00 5.61  ? 195 PRO A C   1 
ATOM   1656 O  O   . PRO A 1 194 ? -5.444  1.484   29.514  1.00 7.59  ? 195 PRO A O   1 
ATOM   1657 C  CB  . PRO A 1 194 ? -6.883  3.832   30.684  1.00 7.81  ? 195 PRO A CB  1 
ATOM   1658 C  CG  . PRO A 1 194 ? -6.867  2.911   31.905  1.00 8.58  ? 195 PRO A CG  1 
ATOM   1659 C  CD  . PRO A 1 194 ? -8.021  1.888   31.696  1.00 7.86  ? 195 PRO A CD  1 
ATOM   1660 N  N   . GLY A 1 195 ? -5.947  2.624   27.545  1.00 5.35  ? 196 GLY A N   1 
ATOM   1661 C  CA  . GLY A 1 195 ? -4.849  1.967   26.837  1.00 6.36  ? 196 GLY A CA  1 
ATOM   1662 C  C   . GLY A 1 195 ? -4.306  2.857   25.736  1.00 4.68  ? 196 GLY A C   1 
ATOM   1663 O  O   . GLY A 1 195 ? -4.218  4.089   25.867  1.00 5.51  ? 196 GLY A O   1 
ATOM   1664 N  N   . SER A 1 196 ? -3.882  2.157   24.664  1.00 5.07  ? 197 SER A N   1 
ATOM   1665 C  CA  . SER A 1 196 ? -3.060  2.808   23.673  1.00 5.67  ? 197 SER A CA  1 
ATOM   1666 C  C   . SER A 1 196 ? -3.506  2.413   22.213  1.00 5.41  ? 197 SER A C   1 
ATOM   1667 O  O   . SER A 1 196 ? -4.256  1.420   22.039  1.00 6.24  ? 197 SER A O   1 
ATOM   1668 C  CB  . SER A 1 196 ? -1.543  2.407   23.817  1.00 8.11  ? 197 SER A CB  1 
ATOM   1669 O  OG  . SER A 1 196 ? -1.342  1.060   23.387  1.00 6.74  ? 197 SER A OG  1 
ATOM   1670 N  N   . LEU A 1 197 ? -2.955  3.115   21.206  1.00 5.63  ? 198 LEU A N   1 
ATOM   1671 C  CA  . LEU A 1 197 ? -3.012  2.592   19.858  1.00 5.39  ? 198 LEU A CA  1 
ATOM   1672 C  C   . LEU A 1 197 ? -2.268  1.238   19.870  1.00 6.08  ? 198 LEU A C   1 
ATOM   1673 O  O   . LEU A 1 197 ? -1.200  1.095   20.581  1.00 6.91  ? 198 LEU A O   1 
ATOM   1674 C  CB  . LEU A 1 197 ? -2.254  3.518   18.909  1.00 7.34  ? 198 LEU A CB  1 
ATOM   1675 C  CG  . LEU A 1 197 ? -2.811  4.931   18.837  1.00 6.32  ? 198 LEU A CG  1 
ATOM   1676 C  CD1 . LEU A 1 197 ? -1.922  5.737   17.817  1.00 10.61 ? 198 LEU A CD1 1 
ATOM   1677 C  CD2 . LEU A 1 197 ? -4.236  4.999   18.403  1.00 8.80  ? 198 LEU A CD2 1 
ATOM   1678 N  N   . THR A 1 198 ? -2.698  0.256   19.051  1.00 4.78  ? 199 THR A N   1 
ATOM   1679 C  CA  . THR A 1 198 ? -1.994  -1.026  19.046  1.00 5.83  ? 199 THR A CA  1 
ATOM   1680 C  C   . THR A 1 198 ? -0.989  -1.149  17.881  1.00 7.52  ? 199 THR A C   1 
ATOM   1681 O  O   . THR A 1 198 ? -0.409  -2.238  17.689  1.00 7.31  ? 199 THR A O   1 
ATOM   1682 C  CB  . THR A 1 198 ? -3.033  -2.162  18.977  1.00 6.07  ? 199 THR A CB  1 
ATOM   1683 O  OG1 . THR A 1 198 ? -3.592  -2.151  17.653  1.00 5.59  ? 199 THR A OG1 1 
ATOM   1684 C  CG2 . THR A 1 198 ? -4.049  -2.127  20.033  1.00 5.79  ? 199 THR A CG2 1 
ATOM   1685 N  N   . THR A 1 199 ? -0.847  -0.074  17.066  1.00 7.49  ? 200 THR A N   1 
ATOM   1686 C  CA  . THR A 1 199 ? 0.265   0.007   16.159  1.00 7.34  ? 200 THR A CA  1 
ATOM   1687 C  C   . THR A 1 199 ? 1.051   1.277   16.441  1.00 8.81  ? 200 THR A C   1 
ATOM   1688 O  O   . THR A 1 199 ? 0.529   2.186   17.021  1.00 8.76  ? 200 THR A O   1 
ATOM   1689 C  CB  . THR A 1 199 ? -0.179  0.046   14.636  1.00 7.02  ? 200 THR A CB  1 
ATOM   1690 O  OG1 . THR A 1 199 ? -0.776  1.307   14.311  1.00 12.23 ? 200 THR A OG1 1 
ATOM   1691 C  CG2 . THR A 1 199 ? -1.153  -1.041  14.304  1.00 11.03 ? 200 THR A CG2 1 
ATOM   1692 N  N   . PRO A 1 200 ? 2.319   1.326   15.994  1.00 8.23  ? 201 PRO A N   1 
ATOM   1693 C  CA  . PRO A 1 200 ? 3.077   2.619   16.048  1.00 9.10  ? 201 PRO A CA  1 
ATOM   1694 C  C   . PRO A 1 200 ? 2.164   3.738   15.511  1.00 8.01  ? 201 PRO A C   1 
ATOM   1695 O  O   . PRO A 1 200 ? 1.452   3.529   14.478  1.00 9.54  ? 201 PRO A O   1 
ATOM   1696 C  CB  . PRO A 1 200 ? 4.281   2.319   15.072  1.00 10.35 ? 201 PRO A CB  1 
ATOM   1697 C  CG  . PRO A 1 200 ? 4.551   0.855   15.349  1.00 10.18 ? 201 PRO A CG  1 
ATOM   1698 C  CD  . PRO A 1 200 ? 3.129   0.231   15.367  1.00 9.82  ? 201 PRO A CD  1 
ATOM   1699 N  N   . PRO A 1 201 ? 2.201   4.921   16.116  1.00 9.36  ? 202 PRO A N   1 
ATOM   1700 C  CA  . PRO A 1 201 ? 3.103   5.350   17.249  1.00 9.19  ? 202 PRO A CA  1 
ATOM   1701 C  C   . PRO A 1 201 ? 2.771   4.884   18.694  1.00 8.16  ? 202 PRO A C   1 
ATOM   1702 O  O   . PRO A 1 201 ? 3.438   5.344   19.607  1.00 9.70  ? 202 PRO A O   1 
ATOM   1703 C  CB  . PRO A 1 201 ? 3.147   6.895   17.081  1.00 9.70  ? 202 PRO A CB  1 
ATOM   1704 C  CG  . PRO A 1 201 ? 1.706   7.217   16.558  1.00 11.22 ? 202 PRO A CG  1 
ATOM   1705 C  CD  . PRO A 1 201 ? 1.360   6.055   15.602  1.00 9.58  ? 202 PRO A CD  1 
ATOM   1706 N  N   . LEU A 1 202 ? 1.781   3.979   18.844  1.00 6.95  ? 203 LEU A N   1 
ATOM   1707 C  CA  . LEU A 1 202 ? 1.582   3.352   20.143  1.00 7.21  ? 203 LEU A CA  1 
ATOM   1708 C  C   . LEU A 1 202 ? 1.150   4.383   21.245  1.00 7.53  ? 203 LEU A C   1 
ATOM   1709 O  O   . LEU A 1 202 ? 1.335   4.084   22.442  1.00 7.48  ? 203 LEU A O   1 
ATOM   1710 C  CB  . LEU A 1 202 ? 2.765   2.492   20.566  1.00 7.83  ? 203 LEU A CB  1 
ATOM   1711 C  CG  . LEU A 1 202 ? 3.044   1.318   19.563  1.00 7.17  ? 203 LEU A CG  1 
ATOM   1712 C  CD1 . LEU A 1 202 ? 4.374   0.682   20.012  1.00 9.79  ? 203 LEU A CD1 1 
ATOM   1713 C  CD2 . LEU A 1 202 ? 1.946   0.203   19.626  1.00 9.85  ? 203 LEU A CD2 1 
ATOM   1714 N  N   . LEU A 1 203 ? 0.583   5.519   20.817  1.00 7.15  ? 204 LEU A N   1 
ATOM   1715 C  CA  . LEU A 1 203 ? 0.296   6.598   21.762  1.00 7.61  ? 204 LEU A CA  1 
ATOM   1716 C  C   . LEU A 1 203 ? -0.748  6.170   22.824  1.00 6.28  ? 204 LEU A C   1 
ATOM   1717 O  O   . LEU A 1 203 ? -1.727  5.432   22.497  1.00 7.20  ? 204 LEU A O   1 
ATOM   1718 C  CB  . LEU A 1 203 ? -0.200  7.838   20.980  1.00 7.95  ? 204 LEU A CB  1 
ATOM   1719 C  CG  . LEU A 1 203 ? 0.880   8.413   20.057  1.00 10.25 ? 204 LEU A CG  1 
ATOM   1720 C  CD1 . LEU A 1 203 ? 0.246   9.506   19.102  1.00 10.90 ? 204 LEU A CD1 1 
ATOM   1721 C  CD2 . LEU A 1 203 ? 2.129   9.042   20.796  1.00 14.22 ? 204 LEU A CD2 1 
ATOM   1722 N  N   . GLU A 1 204 ? -0.541  6.648   24.058  1.00 7.52  ? 205 GLU A N   1 
ATOM   1723 C  CA  . GLU A 1 204 ? -1.348  6.217   25.203  1.00 6.64  ? 205 GLU A CA  1 
ATOM   1724 C  C   . GLU A 1 204 ? -2.556  7.200   25.296  1.00 6.11  ? 205 GLU A C   1 
ATOM   1725 O  O   . GLU A 1 204 ? -2.653  7.981   26.278  1.00 8.52  ? 205 GLU A O   1 
ATOM   1726 C  CB  . GLU A 1 204 ? -0.529  6.088   26.471  1.00 6.79  ? 205 GLU A CB  1 
ATOM   1727 C  CG  . GLU A 1 204 ? 0.340   4.866   26.286  1.00 8.93  ? 205 GLU A CG  1 
ATOM   1728 C  CD  . GLU A 1 204 ? 1.315   4.596   27.419  1.00 10.25 ? 205 GLU A CD  1 
ATOM   1729 O  OE1 . GLU A 1 204 ? 1.662   5.559   28.149  1.00 12.14 ? 205 GLU A OE1 1 
ATOM   1730 O  OE2 . GLU A 1 204 ? 1.743   3.442   27.579  1.00 8.72  ? 205 GLU A OE2 1 
ATOM   1731 N  N   . CYS A 1 205 ? -3.433  7.154   24.308  1.00 7.06  ? 206 CYS A N   1 
ATOM   1732 C  CA  . CYS A 1 205 ? -4.506  8.127   24.146  1.00 6.48  ? 206 CYS A CA  1 
ATOM   1733 C  C   . CYS A 1 205 ? -5.880  7.501   24.026  1.00 5.58  ? 206 CYS A C   1 
ATOM   1734 O  O   . CYS A 1 205 ? -6.856  8.208   23.654  1.00 7.49  ? 206 CYS A O   1 
ATOM   1735 C  CB  . CYS A 1 205 ? -4.226  9.006   22.915  1.00 8.62  ? 206 CYS A CB  1 
ATOM   1736 S  SG  . CYS A 1 205 ? -4.186  8.010   21.351  1.00 8.29  ? 206 CYS A SG  1 
ATOM   1737 N  N   . VAL A 1 206 ? -6.019  6.177   24.300  1.00 5.92  ? 207 VAL A N   1 
ATOM   1738 C  CA  . VAL A 1 206 ? -7.279  5.480   23.980  1.00 5.80  ? 207 VAL A CA  1 
ATOM   1739 C  C   . VAL A 1 206 ? -8.058  5.036   25.221  1.00 5.52  ? 207 VAL A C   1 
ATOM   1740 O  O   . VAL A 1 206 ? -7.479  4.405   26.099  1.00 6.81  ? 207 VAL A O   1 
ATOM   1741 C  CB  . VAL A 1 206 ? -6.982  4.235   23.119  1.00 7.15  ? 207 VAL A CB  1 
ATOM   1742 C  CG1 . VAL A 1 206 ? -8.324  3.553   22.760  1.00 6.18  ? 207 VAL A CG1 1 
ATOM   1743 C  CG2 . VAL A 1 206 ? -6.161  4.675   21.804  1.00 8.71  ? 207 VAL A CG2 1 
ATOM   1744 N  N   . THR A 1 207 ? -9.376  5.359   25.263  1.00 5.79  ? 208 THR A N   1 
ATOM   1745 C  CA  . THR A 1 207 ? -10.327 4.627   26.133  1.00 5.70  ? 208 THR A CA  1 
ATOM   1746 C  C   . THR A 1 207 ? -10.840 3.428   25.304  1.00 5.20  ? 208 THR A C   1 
ATOM   1747 O  O   . THR A 1 207 ? -11.502 3.633   24.260  1.00 6.07  ? 208 THR A O   1 
ATOM   1748 C  CB  . THR A 1 207 ? -11.521 5.499   26.602  1.00 6.85  ? 208 THR A CB  1 
ATOM   1749 O  OG1 . THR A 1 207 ? -10.960 6.635   27.304  1.00 6.95  ? 208 THR A OG1 1 
ATOM   1750 C  CG2 . THR A 1 207 ? -12.445 4.656   27.481  1.00 7.03  ? 208 THR A CG2 1 
ATOM   1751 N  N   . TRP A 1 208 ? -10.466 2.195   25.712  1.00 5.52  ? 209 TRP A N   1 
ATOM   1752 C  CA  . TRP A 1 208 ? -10.897 1.035   24.993  1.00 5.33  ? 209 TRP A CA  1 
ATOM   1753 C  C   . TRP A 1 208 ? -12.290 0.596   25.494  1.00 7.09  ? 209 TRP A C   1 
ATOM   1754 O  O   . TRP A 1 208 ? -12.519 0.533   26.721  1.00 6.26  ? 209 TRP A O   1 
ATOM   1755 C  CB  . TRP A 1 208 ? -9.889  -0.156  25.219  1.00 6.15  ? 209 TRP A CB  1 
ATOM   1756 C  CG  . TRP A 1 208 ? -8.809  -0.034  24.229  1.00 4.97  ? 209 TRP A CG  1 
ATOM   1757 C  CD1 . TRP A 1 208 ? -7.539  0.567   24.404  1.00 4.91  ? 209 TRP A CD1 1 
ATOM   1758 C  CD2 . TRP A 1 208 ? -8.862  -0.443  22.827  1.00 5.52  ? 209 TRP A CD2 1 
ATOM   1759 N  NE1 . TRP A 1 208 ? -6.849  0.557   23.212  1.00 5.88  ? 209 TRP A NE1 1 
ATOM   1760 C  CE2 . TRP A 1 208 ? -7.599  -0.077  22.220  1.00 4.93  ? 209 TRP A CE2 1 
ATOM   1761 C  CE3 . TRP A 1 208 ? -9.837  -1.104  22.046  1.00 5.13  ? 209 TRP A CE3 1 
ATOM   1762 C  CZ2 . TRP A 1 208 ? -7.330  -0.269  20.859  1.00 5.25  ? 209 TRP A CZ2 1 
ATOM   1763 C  CZ3 . TRP A 1 208 ? -9.535  -1.380  20.715  1.00 6.01  ? 209 TRP A CZ3 1 
ATOM   1764 C  CH2 . TRP A 1 208 ? -8.308  -0.933  20.147  1.00 5.63  ? 209 TRP A CH2 1 
ATOM   1765 N  N   . ILE A 1 209 ? -13.149 0.242   24.540  1.00 4.96  ? 210 ILE A N   1 
ATOM   1766 C  CA  . ILE A 1 209 ? -14.475 -0.281  24.890  1.00 5.39  ? 210 ILE A CA  1 
ATOM   1767 C  C   . ILE A 1 209 ? -14.572 -1.591  24.038  1.00 5.92  ? 210 ILE A C   1 
ATOM   1768 O  O   . ILE A 1 209 ? -14.643 -1.469  22.793  1.00 6.65  ? 210 ILE A O   1 
ATOM   1769 C  CB  . ILE A 1 209 ? -15.574 0.744   24.477  1.00 6.64  ? 210 ILE A CB  1 
ATOM   1770 C  CG1 . ILE A 1 209 ? -15.324 1.996   25.279  1.00 7.76  ? 210 ILE A CG1 1 
ATOM   1771 C  CG2 . ILE A 1 209 ? -17.005 0.080   24.746  1.00 8.31  ? 210 ILE A CG2 1 
ATOM   1772 C  CD1 . ILE A 1 209 ? -16.194 3.175   24.800  1.00 9.64  ? 210 ILE A CD1 1 
ATOM   1773 N  N   . VAL A 1 210 ? -14.578 -2.769  24.701  1.00 5.43  ? 211 VAL A N   1 
ATOM   1774 C  CA  . VAL A 1 210 ? -14.515 -4.054  24.002  1.00 5.10  ? 211 VAL A CA  1 
ATOM   1775 C  C   . VAL A 1 210 ? -15.873 -4.740  24.212  1.00 5.19  ? 211 VAL A C   1 
ATOM   1776 O  O   . VAL A 1 210 ? -16.216 -5.026  25.380  1.00 6.86  ? 211 VAL A O   1 
ATOM   1777 C  CB  . VAL A 1 210 ? -13.289 -4.912  24.414  1.00 5.92  ? 211 VAL A CB  1 
ATOM   1778 C  CG1 . VAL A 1 210 ? -13.329 -6.250  23.598  1.00 7.01  ? 211 VAL A CG1 1 
ATOM   1779 C  CG2 . VAL A 1 210 ? -11.974 -4.117  24.103  1.00 7.01  ? 211 VAL A CG2 1 
ATOM   1780 N  N   . LEU A 1 211 ? -16.627 -5.038  23.117  1.00 5.90  ? 212 LEU A N   1 
ATOM   1781 C  CA  . LEU A 1 211 ? -17.935 -5.652  23.296  1.00 6.05  ? 212 LEU A CA  1 
ATOM   1782 C  C   . LEU A 1 211 ? -17.745 -7.133  23.694  1.00 6.95  ? 212 LEU A C   1 
ATOM   1783 O  O   . LEU A 1 211 ? -16.889 -7.871  23.149  1.00 7.94  ? 212 LEU A O   1 
ATOM   1784 C  CB  . LEU A 1 211 ? -18.760 -5.590  21.982  1.00 7.09  ? 212 LEU A CB  1 
ATOM   1785 C  CG  . LEU A 1 211 ? -19.148 -4.166  21.587  1.00 8.63  ? 212 LEU A CG  1 
ATOM   1786 C  CD1 . LEU A 1 211 ? -20.213 -4.250  20.404  1.00 9.94  ? 212 LEU A CD1 1 
ATOM   1787 C  CD2 . LEU A 1 211 ? -19.615 -3.284  22.760  1.00 9.72  ? 212 LEU A CD2 1 
ATOM   1788 N  N   . LYS A 1 212 ? -18.582 -7.603  24.641  1.00 7.34  ? 213 LYS A N   1 
ATOM   1789 C  CA  . LYS A 1 212 ? -18.540 -9.008  24.992  1.00 7.51  ? 213 LYS A CA  1 
ATOM   1790 C  C   . LYS A 1 212 ? -18.992 -9.954  23.899  1.00 7.79  ? 213 LYS A C   1 
ATOM   1791 O  O   . LYS A 1 212 ? -18.507 -11.065 23.769  1.00 9.79  ? 213 LYS A O   1 
ATOM   1792 C  CB  . LYS A 1 212 ? -19.396 -9.232  26.270  1.00 11.50 ? 213 LYS A CB  1 
ATOM   1793 C  CG  . LYS A 1 212 ? -19.534 -10.742 26.640  1.00 15.09 ? 213 LYS A CG  1 
ATOM   1794 C  CD  . LYS A 1 212 ? -20.276 -10.959 27.955  1.00 16.73 ? 213 LYS A CD  1 
ATOM   1795 C  CE  . LYS A 1 212 ? -20.296 -12.415 28.406  1.00 21.96 ? 213 LYS A CE  1 
ATOM   1796 N  NZ  . LYS A 1 212 ? -21.075 -12.655 29.705  1.00 29.49 ? 213 LYS A NZ  1 
ATOM   1797 N  N   . GLU A 1 213 ? -20.022 -9.540  23.135  1.00 6.98  ? 214 GLU A N   1 
ATOM   1798 C  CA  . GLU A 1 213 ? -20.652 -10.481 22.161  1.00 8.10  ? 214 GLU A CA  1 
ATOM   1799 C  C   . GLU A 1 213 ? -19.893 -10.366 20.827  1.00 6.95  ? 214 GLU A C   1 
ATOM   1800 O  O   . GLU A 1 213 ? -19.808 -9.247  20.248  1.00 6.70  ? 214 GLU A O   1 
ATOM   1801 C  CB  . GLU A 1 213 ? -22.130 -10.113 21.910  1.00 9.09  ? 214 GLU A CB  1 
ATOM   1802 C  CG  . GLU A 1 213 ? -22.818 -11.115 20.993  1.00 11.08 ? 214 GLU A CG  1 
ATOM   1803 C  CD  . GLU A 1 213 ? -24.283 -10.945 20.796  1.00 13.31 ? 214 GLU A CD  1 
ATOM   1804 O  OE1 . GLU A 1 213 ? -24.862 -10.033 21.321  1.00 12.73 ? 214 GLU A OE1 1 
ATOM   1805 O  OE2 . GLU A 1 213 ? -24.830 -11.880 20.098  1.00 20.42 ? 214 GLU A OE2 1 
ATOM   1806 N  N   . PRO A 1 214 ? -19.323 -11.470 20.332  1.00 6.86  ? 215 PRO A N   1 
ATOM   1807 C  CA  . PRO A 1 214 ? -18.666 -11.400 19.027  1.00 7.04  ? 215 PRO A CA  1 
ATOM   1808 C  C   . PRO A 1 214 ? -19.684 -11.396 17.859  1.00 8.43  ? 215 PRO A C   1 
ATOM   1809 O  O   . PRO A 1 214 ? -20.872 -11.807 18.076  1.00 10.40 ? 215 PRO A O   1 
ATOM   1810 C  CB  . PRO A 1 214 ? -17.919 -12.726 18.919  1.00 7.27  ? 215 PRO A CB  1 
ATOM   1811 C  CG  . PRO A 1 214 ? -18.671 -13.672 19.779  1.00 13.70 ? 215 PRO A CG  1 
ATOM   1812 C  CD  . PRO A 1 214 ? -19.259 -12.824 20.924  1.00 7.75  ? 215 PRO A CD  1 
ATOM   1813 N  N   . ILE A 1 215 ? -19.284 -10.956 16.684  1.00 7.97  ? 216 ILE A N   1 
ATOM   1814 C  CA  . ILE A 1 215 ? -20.128 -11.159 15.475  1.00 7.82  ? 216 ILE A CA  1 
ATOM   1815 C  C   . ILE A 1 215 ? -19.568 -12.441 14.825  1.00 7.35  ? 216 ILE A C   1 
ATOM   1816 O  O   . ILE A 1 215 ? -18.383 -12.815 14.957  1.00 8.74  ? 216 ILE A O   1 
ATOM   1817 C  CB  . ILE A 1 215 ? -20.128 -9.989  14.489  1.00 8.78  ? 216 ILE A CB  1 
ATOM   1818 C  CG1 . ILE A 1 215 ? -18.691 -9.598  14.127  1.00 11.60 ? 216 ILE A CG1 1 
ATOM   1819 C  CG2 . ILE A 1 215 ? -20.834 -8.758  15.215  1.00 11.04 ? 216 ILE A CG2 1 
ATOM   1820 C  CD1 . ILE A 1 215 ? -18.669 -8.598  12.809  1.00 11.31 ? 216 ILE A CD1 1 
ATOM   1821 N  N   . SER A 1 216 ? -20.458 -13.116 14.077  1.00 9.27  ? 217 SER A N   1 
ATOM   1822 C  CA  . SER A 1 216 ? -20.027 -14.248 13.198  1.00 8.76  ? 217 SER A CA  1 
ATOM   1823 C  C   . SER A 1 216 ? -19.855 -13.818 11.773  1.00 9.36  ? 217 SER A C   1 
ATOM   1824 O  O   . SER A 1 216 ? -20.694 -13.051 11.276  1.00 9.91  ? 217 SER A O   1 
ATOM   1825 C  CB  . SER A 1 216 ? -21.138 -15.321 13.180  1.00 12.41 ? 217 SER A CB  1 
ATOM   1826 O  OG  . SER A 1 216 ? -21.201 -15.941 14.478  1.00 16.44 ? 217 SER A OG  1 
ATOM   1827 N  N   . VAL A 1 217 ? -18.733 -14.235 11.188  1.00 8.82  ? 218 VAL A N   1 
ATOM   1828 C  CA  . VAL A 1 217 ? -18.482 -14.073 9.765   1.00 9.13  ? 218 VAL A CA  1 
ATOM   1829 C  C   . VAL A 1 217 ? -18.211 -15.425 9.142   1.00 9.10  ? 218 VAL A C   1 
ATOM   1830 O  O   . VAL A 1 217 ? -17.841 -16.376 9.888   1.00 8.91  ? 218 VAL A O   1 
ATOM   1831 C  CB  . VAL A 1 217 ? -17.284 -13.091 9.530   1.00 10.35 ? 218 VAL A CB  1 
ATOM   1832 C  CG1 . VAL A 1 217 ? -17.542 -11.752 10.273  1.00 9.64  ? 218 VAL A CG1 1 
ATOM   1833 C  CG2 . VAL A 1 217 ? -15.906 -13.710 10.013  1.00 11.38 ? 218 VAL A CG2 1 
ATOM   1834 N  N   . SER A 1 218 ? -18.377 -15.574 7.838   1.00 9.40  ? 219 SER A N   1 
ATOM   1835 C  CA  . SER A 1 218 ? -18.121 -16.899 7.292   1.00 9.32  ? 219 SER A CA  1 
ATOM   1836 C  C   . SER A 1 218 ? -16.626 -17.152 7.005   1.00 10.03 ? 219 SER A C   1 
ATOM   1837 O  O   . SER A 1 218 ? -15.809 -16.238 6.880   1.00 9.59  ? 219 SER A O   1 
ATOM   1838 C  CB  . SER A 1 218 ? -18.940 -17.072 5.988   1.00 11.47 ? 219 SER A CB  1 
ATOM   1839 O  OG  . SER A 1 218 ? -18.504 -16.178 4.998   1.00 11.50 ? 219 SER A OG  1 
ATOM   1840 N  N   A SER A 1 219 ? -16.304 -18.423 6.825   0.50 9.16  ? 220 SER A N   1 
ATOM   1841 N  N   B SER A 1 219 ? -16.308 -18.411 6.807   0.50 9.19  ? 220 SER A N   1 
ATOM   1842 C  CA  A SER A 1 219 ? -14.966 -18.805 6.425   0.50 9.60  ? 220 SER A CA  1 
ATOM   1843 C  CA  B SER A 1 219 ? -14.965 -18.769 6.454   0.50 9.67  ? 220 SER A CA  1 
ATOM   1844 C  C   A SER A 1 219 ? -14.634 -18.075 5.110   0.50 11.30 ? 220 SER A C   1 
ATOM   1845 C  C   B SER A 1 219 ? -14.603 -18.152 5.076   0.50 11.28 ? 220 SER A C   1 
ATOM   1846 O  O   A SER A 1 219 ? -13.578 -17.456 5.019   0.50 11.88 ? 220 SER A O   1 
ATOM   1847 O  O   B SER A 1 219 ? -13.466 -17.729 4.881   0.50 11.34 ? 220 SER A O   1 
ATOM   1848 C  CB  A SER A 1 219 ? -14.869 -20.365 6.275   0.50 11.03 ? 220 SER A CB  1 
ATOM   1849 C  CB  B SER A 1 219 ? -14.864 -20.311 6.442   0.50 11.54 ? 220 SER A CB  1 
ATOM   1850 O  OG  A SER A 1 219 ? -15.886 -20.907 5.438   0.50 10.97 ? 220 SER A OG  1 
ATOM   1851 O  OG  B SER A 1 219 ? -13.549 -20.682 6.143   0.50 12.87 ? 220 SER A OG  1 
ATOM   1852 N  N   . GLU A 1 220 ? -15.575 -18.049 4.145   1.00 12.40 ? 221 GLU A N   1 
ATOM   1853 C  CA  . GLU A 1 220 ? -15.288 -17.401 2.854   1.00 13.73 ? 221 GLU A CA  1 
ATOM   1854 C  C   . GLU A 1 220 ? -14.993 -15.882 3.049   1.00 11.59 ? 221 GLU A C   1 
ATOM   1855 O  O   . GLU A 1 220 ? -14.088 -15.347 2.394   1.00 12.57 ? 221 GLU A O   1 
ATOM   1856 C  CB  . GLU A 1 220 ? -16.455 -17.542 1.889   1.00 15.75 ? 221 GLU A CB  1 
ATOM   1857 C  CG  . GLU A 1 220 ? -16.647 -19.032 1.454   1.00 17.82 ? 221 GLU A CG  1 
ATOM   1858 C  CD  . GLU A 1 220 ? -17.683 -19.733 2.316   1.00 19.38 ? 221 GLU A CD  1 
ATOM   1859 O  OE1 . GLU A 1 220 ? -18.067 -19.268 3.400   1.00 17.25 ? 221 GLU A OE1 1 
ATOM   1860 O  OE2 . GLU A 1 220 ? -18.120 -20.866 1.962   1.00 30.34 ? 221 GLU A OE2 1 
ATOM   1861 N  N   . GLN A 1 221 ? -15.718 -15.219 3.963   1.00 10.13 ? 222 GLN A N   1 
ATOM   1862 C  CA  . GLN A 1 221 ? -15.435 -13.798 4.200   1.00 10.28 ? 222 GLN A CA  1 
ATOM   1863 C  C   . GLN A 1 221 ? -13.992 -13.570 4.740   1.00 11.62 ? 222 GLN A C   1 
ATOM   1864 O  O   . GLN A 1 221 ? -13.220 -12.738 4.240   1.00 11.50 ? 222 GLN A O   1 
ATOM   1865 C  CB  . GLN A 1 221 ? -16.477 -13.237 5.171   1.00 10.85 ? 222 GLN A CB  1 
ATOM   1866 C  CG  . GLN A 1 221 ? -17.826 -13.124 4.437   1.00 10.42 ? 222 GLN A CG  1 
ATOM   1867 C  CD  . GLN A 1 221 ? -18.930 -12.529 5.341   1.00 10.84 ? 222 GLN A CD  1 
ATOM   1868 O  OE1 . GLN A 1 221 ? -19.048 -12.910 6.503   1.00 10.42 ? 222 GLN A OE1 1 
ATOM   1869 N  NE2 . GLN A 1 221 ? -19.789 -11.657 4.771   1.00 10.83 ? 222 GLN A NE2 1 
ATOM   1870 N  N   . VAL A 1 222 ? -13.631 -14.350 5.765   1.00 11.16 ? 223 VAL A N   1 
ATOM   1871 C  CA  . VAL A 1 222 ? -12.270 -14.147 6.362   1.00 10.82 ? 223 VAL A CA  1 
ATOM   1872 C  C   . VAL A 1 222 ? -11.121 -14.617 5.343   1.00 11.77 ? 223 VAL A C   1 
ATOM   1873 O  O   . VAL A 1 222 ? -10.005 -14.043 5.285   1.00 12.75 ? 223 VAL A O   1 
ATOM   1874 C  CB  . VAL A 1 222 ? -12.118 -14.694 7.808   1.00 13.20 ? 223 VAL A CB  1 
ATOM   1875 C  CG1 . VAL A 1 222 ? -12.141 -16.189 7.790   1.00 14.29 ? 223 VAL A CG1 1 
ATOM   1876 C  CG2 . VAL A 1 222 ? -10.786 -14.156 8.461   1.00 13.03 ? 223 VAL A CG2 1 
ATOM   1877 N  N   . LEU A 1 223 ? -11.430 -15.633 4.527   1.00 11.41 ? 224 LEU A N   1 
ATOM   1878 C  CA  . LEU A 1 223 ? -10.480 -16.039 3.490   1.00 13.56 ? 224 LEU A CA  1 
ATOM   1879 C  C   . LEU A 1 223 ? -10.184 -14.895 2.544   1.00 14.53 ? 224 LEU A C   1 
ATOM   1880 O  O   . LEU A 1 223 ? -9.035  -14.770 2.094   1.00 14.25 ? 224 LEU A O   1 
ATOM   1881 C  CB  . LEU A 1 223 ? -10.972 -17.283 2.739   1.00 16.74 ? 224 LEU A CB  1 
ATOM   1882 C  CG  . LEU A 1 223 ? -10.843 -18.551 3.581   1.00 18.95 ? 224 LEU A CG  1 
ATOM   1883 C  CD1 . LEU A 1 223 ? -11.819 -19.702 3.126   1.00 26.03 ? 224 LEU A CD1 1 
ATOM   1884 C  CD2 . LEU A 1 223 ? -9.396  -18.989 3.476   1.00 22.08 ? 224 LEU A CD2 1 
ATOM   1885 N  N   . LYS A 1 224 ? -11.173 -14.025 2.290   1.00 12.05 ? 225 LYS A N   1 
ATOM   1886 C  CA  . LYS A 1 224 ? -10.912 -12.884 1.387   1.00 13.65 ? 225 LYS A CA  1 
ATOM   1887 C  C   . LYS A 1 224 ? -10.027 -11.846 2.056   1.00 11.27 ? 225 LYS A C   1 
ATOM   1888 O  O   . LYS A 1 224 ? -9.227  -11.232 1.368   1.00 12.39 ? 225 LYS A O   1 
ATOM   1889 C  CB  . LYS A 1 224 ? -12.241 -12.353 0.798   1.00 14.92 ? 225 LYS A CB  1 
ATOM   1890 C  CG  . LYS A 1 224 ? -12.788 -13.482 -0.260  1.00 18.48 ? 225 LYS A CG  1 
ATOM   1891 C  CD  . LYS A 1 224 ? -14.141 -13.125 -0.795  1.00 21.83 ? 225 LYS A CD  1 
ATOM   1892 C  CE  . LYS A 1 224 ? -14.776 -14.228 -1.713  1.00 23.07 ? 225 LYS A CE  1 
ATOM   1893 N  NZ  . LYS A 1 224 ? -14.543 -15.584 -1.188  1.00 34.72 ? 225 LYS A NZ  1 
ATOM   1894 N  N   . PHE A 1 225 ? -10.103 -11.658 3.382   1.00 10.66 ? 226 PHE A N   1 
ATOM   1895 C  CA  . PHE A 1 225 ? -9.163  -10.776 4.048   1.00 8.68  ? 226 PHE A CA  1 
ATOM   1896 C  C   . PHE A 1 225 ? -7.746  -11.285 3.821   1.00 9.45  ? 226 PHE A C   1 
ATOM   1897 O  O   . PHE A 1 225 ? -6.787  -10.518 3.607   1.00 10.86 ? 226 PHE A O   1 
ATOM   1898 C  CB  . PHE A 1 225 ? -9.381  -10.812 5.602   1.00 10.34 ? 226 PHE A CB  1 
ATOM   1899 C  CG  . PHE A 1 225 ? -10.594 -10.031 6.150   1.00 9.25  ? 226 PHE A CG  1 
ATOM   1900 C  CD1 . PHE A 1 225 ? -11.616 -9.532  5.348   1.00 13.07 ? 226 PHE A CD1 1 
ATOM   1901 C  CD2 . PHE A 1 225 ? -10.708 -9.818  7.526   1.00 13.97 ? 226 PHE A CD2 1 
ATOM   1902 C  CE1 . PHE A 1 225 ? -12.709 -8.830  5.910   1.00 13.23 ? 226 PHE A CE1 1 
ATOM   1903 C  CE2 . PHE A 1 225 ? -11.778 -9.122  8.093   1.00 12.14 ? 226 PHE A CE2 1 
ATOM   1904 C  CZ  . PHE A 1 225 ? -12.793 -8.651  7.293   1.00 12.13 ? 226 PHE A CZ  1 
ATOM   1905 N  N   . ARG A 1 226 ? -7.563  -12.620 3.937   1.00 10.01 ? 227 ARG A N   1 
ATOM   1906 C  CA  . ARG A 1 226 ? -6.235  -13.213 3.859   1.00 11.10 ? 227 ARG A CA  1 
ATOM   1907 C  C   . ARG A 1 226 ? -5.647  -13.210 2.438   1.00 12.20 ? 227 ARG A C   1 
ATOM   1908 O  O   . ARG A 1 226 ? -4.496  -13.681 2.265   1.00 12.36 ? 227 ARG A O   1 
ATOM   1909 C  CB  . ARG A 1 226 ? -6.294  -14.686 4.374   1.00 11.38 ? 227 ARG A CB  1 
ATOM   1910 C  CG  . ARG A 1 226 ? -6.760  -14.815 5.842   1.00 9.78  ? 227 ARG A CG  1 
ATOM   1911 C  CD  . ARG A 1 226 ? -6.646  -16.243 6.351   1.00 12.25 ? 227 ARG A CD  1 
ATOM   1912 N  NE  . ARG A 1 226 ? -7.228  -16.360 7.694   1.00 10.94 ? 227 ARG A NE  1 
ATOM   1913 C  CZ  . ARG A 1 226 ? -8.131  -17.280 8.067   1.00 10.12 ? 227 ARG A CZ  1 
ATOM   1914 N  NH1 . ARG A 1 226 ? -8.564  -18.225 7.165   1.00 14.62 ? 227 ARG A NH1 1 
ATOM   1915 N  NH2 . ARG A 1 226 ? -8.664  -17.207 9.273   1.00 11.36 ? 227 ARG A NH2 1 
ATOM   1916 N  N   . LYS A 1 227 ? -6.420  -12.762 1.429   1.00 11.22 ? 228 LYS A N   1 
ATOM   1917 C  CA  . LYS A 1 227 ? -5.842  -12.628 0.079   1.00 12.85 ? 228 LYS A CA  1 
ATOM   1918 C  C   . LYS A 1 227 ? -5.239  -11.272 -0.167  1.00 12.10 ? 228 LYS A C   1 
ATOM   1919 O  O   . LYS A 1 227 ? -4.574  -11.065 -1.227  1.00 13.95 ? 228 LYS A O   1 
ATOM   1920 C  CB  . LYS A 1 227 ? -7.000  -12.838 -0.926  1.00 13.34 ? 228 LYS A CB  1 
ATOM   1921 C  CG  . LYS A 1 227 ? -7.426  -14.277 -1.111  1.00 15.83 ? 228 LYS A CG  1 
ATOM   1922 C  CD  . LYS A 1 227 ? -8.662  -14.443 -2.142  1.00 20.21 ? 228 LYS A CD  1 
ATOM   1923 C  CE  . LYS A 1 227 ? -8.166  -14.451 -3.631  1.00 30.29 ? 228 LYS A CE  1 
ATOM   1924 N  NZ  . LYS A 1 227 ? -7.250  -15.671 -3.700  1.00 33.52 ? 228 LYS A NZ  1 
ATOM   1925 N  N   . LEU A 1 228 ? -5.498  -10.284 0.716   1.00 10.79 ? 229 LEU A N   1 
ATOM   1926 C  CA  . LEU A 1 228 ? -4.817  -9.032  0.602   1.00 11.14 ? 229 LEU A CA  1 
ATOM   1927 C  C   . LEU A 1 228 ? -3.302  -9.175  0.726   1.00 13.02 ? 229 LEU A C   1 
ATOM   1928 O  O   . LEU A 1 228 ? -2.768  -10.218 1.177   1.00 12.21 ? 229 LEU A O   1 
ATOM   1929 C  CB  . LEU A 1 228 ? -5.284  -8.047  1.712   1.00 11.20 ? 229 LEU A CB  1 
ATOM   1930 C  CG  . LEU A 1 228 ? -6.761  -7.636  1.545   1.00 12.51 ? 229 LEU A CG  1 
ATOM   1931 C  CD1 . LEU A 1 228 ? -7.237  -6.977  2.838   1.00 12.44 ? 229 LEU A CD1 1 
ATOM   1932 C  CD2 . LEU A 1 228 ? -6.779  -6.581  0.384   1.00 13.70 ? 229 LEU A CD2 1 
ATOM   1933 N  N   . ASN A 1 229 ? -2.601  -8.083  0.410   1.00 13.45 ? 230 ASN A N   1 
ATOM   1934 C  CA  . ASN A 1 229 ? -1.142  -8.162  0.459   1.00 13.24 ? 230 ASN A CA  1 
ATOM   1935 C  C   . ASN A 1 229 ? -0.536  -7.001  1.283   1.00 13.43 ? 230 ASN A C   1 
ATOM   1936 O  O   . ASN A 1 229 ? -1.019  -5.864  1.159   1.00 13.71 ? 230 ASN A O   1 
ATOM   1937 C  CB  . ASN A 1 229 ? -0.624  -7.902  -1.010  1.00 13.52 ? 230 ASN A CB  1 
ATOM   1938 C  CG  . ASN A 1 229 ? -0.576  -9.153  -1.939  1.00 15.44 ? 230 ASN A CG  1 
ATOM   1939 O  OD1 . ASN A 1 229 ? 0.029   -9.043  -3.031  1.00 19.57 ? 230 ASN A OD1 1 
ATOM   1940 N  ND2 . ASN A 1 229 ? -1.261  -10.257 -1.580  1.00 15.55 ? 230 ASN A ND2 1 
ATOM   1941 N  N   . PHE A 1 230 ? 0.538   -7.287  2.043   1.00 12.58 ? 231 PHE A N   1 
ATOM   1942 C  CA  . PHE A 1 230 ? 1.258   -6.197  2.737   1.00 12.33 ? 231 PHE A CA  1 
ATOM   1943 C  C   . PHE A 1 230 ? 2.162   -5.418  1.745   1.00 14.20 ? 231 PHE A C   1 
ATOM   1944 O  O   . PHE A 1 230 ? 2.500   -4.242  1.996   1.00 15.19 ? 231 PHE A O   1 
ATOM   1945 C  CB  . PHE A 1 230 ? 2.259   -6.801  3.692   1.00 12.46 ? 231 PHE A CB  1 
ATOM   1946 C  CG  . PHE A 1 230 ? 1.654   -7.402  4.983   1.00 12.81 ? 231 PHE A CG  1 
ATOM   1947 C  CD1 . PHE A 1 230 ? 0.866   -6.608  5.837   1.00 11.26 ? 231 PHE A CD1 1 
ATOM   1948 C  CD2 . PHE A 1 230 ? 2.036   -8.704  5.373   1.00 11.68 ? 231 PHE A CD2 1 
ATOM   1949 C  CE1 . PHE A 1 230 ? 0.395   -7.176  7.102   1.00 14.03 ? 231 PHE A CE1 1 
ATOM   1950 C  CE2 . PHE A 1 230 ? 1.579   -9.268  6.581   1.00 13.47 ? 231 PHE A CE2 1 
ATOM   1951 C  CZ  . PHE A 1 230 ? 0.778   -8.489  7.461   1.00 12.46 ? 231 PHE A CZ  1 
ATOM   1952 N  N   . ASN A 1 231 ? 2.626   -6.096  0.683   1.00 14.07 ? 232 ASN A N   1 
ATOM   1953 C  CA  . ASN A 1 231 ? 3.491   -5.477  -0.323  1.00 14.80 ? 232 ASN A CA  1 
ATOM   1954 C  C   . ASN A 1 231 ? 2.728   -4.577  -1.296  1.00 15.01 ? 232 ASN A C   1 
ATOM   1955 O  O   . ASN A 1 231 ? 1.498   -4.679  -1.406  1.00 15.62 ? 232 ASN A O   1 
ATOM   1956 C  CB  . ASN A 1 231 ? 4.150   -6.603  -1.131  1.00 17.05 ? 232 ASN A CB  1 
ATOM   1957 C  CG  . ASN A 1 231 ? 3.118   -7.521  -1.740  1.00 13.58 ? 232 ASN A CG  1 
ATOM   1958 O  OD1 . ASN A 1 231 ? 2.603   -8.410  -1.017  1.00 19.11 ? 232 ASN A OD1 1 
ATOM   1959 N  ND2 . ASN A 1 231 ? 2.797   -7.365  -3.040  1.00 17.42 ? 232 ASN A ND2 1 
ATOM   1960 N  N   . GLY A 1 232 ? 3.502   -3.673  -1.983  1.00 17.64 ? 233 GLY A N   1 
ATOM   1961 C  CA  . GLY A 1 232 ? 2.874   -2.901  -3.069  1.00 16.70 ? 233 GLY A CA  1 
ATOM   1962 C  C   . GLY A 1 232 ? 2.894   -3.637  -4.382  1.00 17.42 ? 233 GLY A C   1 
ATOM   1963 O  O   . GLY A 1 232 ? 3.559   -4.702  -4.480  1.00 18.98 ? 233 GLY A O   1 
ATOM   1964 N  N   . GLU A 1 233 ? 2.163   -3.087  -5.368  1.00 17.84 ? 234 GLU A N   1 
ATOM   1965 C  CA  . GLU A 1 233 ? 2.020   -3.700  -6.698  1.00 18.86 ? 234 GLU A CA  1 
ATOM   1966 C  C   . GLU A 1 233 ? 3.389   -3.862  -7.315  1.00 19.68 ? 234 GLU A C   1 
ATOM   1967 O  O   . GLU A 1 233 ? 4.263   -2.984  -7.189  1.00 19.55 ? 234 GLU A O   1 
ATOM   1968 C  CB  . GLU A 1 233 ? 1.128   -2.780  -7.541  1.00 18.42 ? 234 GLU A CB  1 
ATOM   1969 C  CG  . GLU A 1 233 ? 0.794   -3.351  -8.909  1.00 19.30 ? 234 GLU A CG  1 
ATOM   1970 C  CD  . GLU A 1 233 ? 0.015   -2.421  -9.755  1.00 25.48 ? 234 GLU A CD  1 
ATOM   1971 O  OE1 . GLU A 1 233 ? -0.268  -1.235  -9.289  1.00 24.38 ? 234 GLU A OE1 1 
ATOM   1972 O  OE2 . GLU A 1 233 ? -0.259  -2.908  -10.917 1.00 22.94 ? 234 GLU A OE2 1 
ATOM   1973 N  N   . GLY A 1 234 ? 3.580   -5.004  -8.018  1.00 20.59 ? 235 GLY A N   1 
ATOM   1974 C  CA  . GLY A 1 234 ? 4.901   -5.259  -8.628  1.00 22.58 ? 235 GLY A CA  1 
ATOM   1975 C  C   . GLY A 1 234 ? 6.011   -5.643  -7.659  1.00 23.33 ? 235 GLY A C   1 
ATOM   1976 O  O   . GLY A 1 234 ? 7.206   -5.639  -8.048  1.00 25.19 ? 235 GLY A O   1 
ATOM   1977 N  N   . GLU A 1 235 ? 5.643   -5.999  -6.419  1.00 20.69 ? 236 GLU A N   1 
ATOM   1978 C  CA  . GLU A 1 235 ? 6.604   -6.539  -5.413  1.00 19.26 ? 236 GLU A CA  1 
ATOM   1979 C  C   . GLU A 1 235 ? 6.175   -7.995  -5.108  1.00 21.27 ? 236 GLU A C   1 
ATOM   1980 O  O   . GLU A 1 235 ? 4.991   -8.405  -5.374  1.00 22.08 ? 236 GLU A O   1 
ATOM   1981 C  CB  . GLU A 1 235 ? 6.626   -5.721  -4.074  1.00 20.36 ? 236 GLU A CB  1 
ATOM   1982 C  CG  . GLU A 1 235 ? 7.067   -4.258  -4.289  1.00 19.34 ? 236 GLU A CG  1 
ATOM   1983 C  CD  . GLU A 1 235 ? 6.969   -3.412  -3.056  1.00 23.36 ? 236 GLU A CD  1 
ATOM   1984 O  OE1 . GLU A 1 235 ? 6.237   -3.785  -2.081  1.00 25.89 ? 236 GLU A OE1 1 
ATOM   1985 O  OE2 . GLU A 1 235 ? 7.623   -2.352  -3.058  1.00 30.69 ? 236 GLU A OE2 1 
ATOM   1986 N  N   . PRO A 1 236 ? 7.105   -8.776  -4.579  1.00 19.95 ? 237 PRO A N   1 
ATOM   1987 C  CA  . PRO A 1 236 ? 6.766   -10.197 -4.342  1.00 21.00 ? 237 PRO A CA  1 
ATOM   1988 C  C   . PRO A 1 236 ? 5.687   -10.269 -3.268  1.00 19.09 ? 237 PRO A C   1 
ATOM   1989 O  O   . PRO A 1 236 ? 5.650   -9.404  -2.325  1.00 19.28 ? 237 PRO A O   1 
ATOM   1990 C  CB  . PRO A 1 236 ? 8.046   -10.765 -3.744  1.00 20.23 ? 237 PRO A CB  1 
ATOM   1991 C  CG  . PRO A 1 236 ? 9.159   -9.959  -4.457  1.00 23.63 ? 237 PRO A CG  1 
ATOM   1992 C  CD  . PRO A 1 236 ? 8.546   -8.533  -4.289  1.00 23.09 ? 237 PRO A CD  1 
ATOM   1993 N  N   . GLU A 1 237 ? 4.842   -11.297 -3.430  1.00 20.78 ? 238 GLU A N   1 
ATOM   1994 C  CA  . GLU A 1 237 ? 3.638   -11.338 -2.682  1.00 17.63 ? 238 GLU A CA  1 
ATOM   1995 C  C   . GLU A 1 237 ? 3.941   -11.729 -1.220  1.00 17.87 ? 238 GLU A C   1 
ATOM   1996 O  O   . GLU A 1 237 ? 4.532   -12.764 -0.946  1.00 16.05 ? 238 GLU A O   1 
ATOM   1997 C  CB  . GLU A 1 237 ? 2.681   -12.365 -3.273  1.00 18.66 ? 238 GLU A CB  1 
ATOM   1998 C  CG  . GLU A 1 237 ? 1.383   -12.254 -2.558  1.00 19.73 ? 238 GLU A CG  1 
ATOM   1999 C  CD  . GLU A 1 237 ? 0.279   -13.017 -3.206  1.00 16.89 ? 238 GLU A CD  1 
ATOM   2000 O  OE1 . GLU A 1 237 ? 0.630   -14.129 -3.700  1.00 27.28 ? 238 GLU A OE1 1 
ATOM   2001 O  OE2 . GLU A 1 237 ? -0.902  -12.504 -3.288  1.00 19.11 ? 238 GLU A OE2 1 
ATOM   2002 N  N   . GLU A 1 238 ? 3.436   -10.927 -0.280  1.00 14.92 ? 239 GLU A N   1 
ATOM   2003 C  CA  . GLU A 1 238 ? 3.520   -11.209 1.193   1.00 17.85 ? 239 GLU A CA  1 
ATOM   2004 C  C   . GLU A 1 238 ? 2.056   -11.143 1.690   1.00 13.78 ? 239 GLU A C   1 
ATOM   2005 O  O   . GLU A 1 238 ? 1.471   -10.026 1.708   1.00 15.47 ? 239 GLU A O   1 
ATOM   2006 C  CB  . GLU A 1 238 ? 4.239   -10.072 1.901   1.00 16.35 ? 239 GLU A CB  1 
ATOM   2007 C  CG  . GLU A 1 238 ? 5.659   -9.695  1.519   1.00 21.68 ? 239 GLU A CG  1 
ATOM   2008 C  CD  . GLU A 1 238 ? 6.043   -8.247  2.079   1.00 25.73 ? 239 GLU A CD  1 
ATOM   2009 O  OE1 . GLU A 1 238 ? 5.707   -7.935  3.239   1.00 26.84 ? 239 GLU A OE1 1 
ATOM   2010 O  OE2 . GLU A 1 238 ? 6.618   -7.421  1.332   1.00 34.31 ? 239 GLU A OE2 1 
ATOM   2011 N  N   . LEU A 1 239 ? 1.421   -12.309 1.947   1.00 12.81 ? 240 LEU A N   1 
ATOM   2012 C  CA  . LEU A 1 239 ? -0.015  -12.211 2.249   1.00 11.91 ? 240 LEU A CA  1 
ATOM   2013 C  C   . LEU A 1 239 ? -0.217  -11.378 3.557   1.00 10.37 ? 240 LEU A C   1 
ATOM   2014 O  O   . LEU A 1 239 ? 0.527   -11.556 4.578   1.00 12.83 ? 240 LEU A O   1 
ATOM   2015 C  CB  . LEU A 1 239 ? -0.650  -13.607 2.487   1.00 11.29 ? 240 LEU A CB  1 
ATOM   2016 C  CG  . LEU A 1 239 ? -0.703  -14.453 1.217   1.00 12.48 ? 240 LEU A CG  1 
ATOM   2017 C  CD1 . LEU A 1 239 ? -1.231  -15.805 1.664   1.00 16.36 ? 240 LEU A CD1 1 
ATOM   2018 C  CD2 . LEU A 1 239 ? -1.548  -13.805 0.151   1.00 13.75 ? 240 LEU A CD2 1 
ATOM   2019 N  N   . MET A 1 240 ? -1.288  -10.578 3.555   1.00 9.69  ? 241 MET A N   1 
ATOM   2020 C  CA  . MET A 1 240 ? -1.632  -9.728  4.717   1.00 11.92 ? 241 MET A CA  1 
ATOM   2021 C  C   . MET A 1 240 ? -2.400  -10.648 5.686   1.00 11.72 ? 241 MET A C   1 
ATOM   2022 O  O   . MET A 1 240 ? -3.610  -10.819 5.587   1.00 11.01 ? 241 MET A O   1 
ATOM   2023 C  CB  . MET A 1 240 ? -2.502  -8.563  4.262   1.00 12.83 ? 241 MET A CB  1 
ATOM   2024 C  CG  . MET A 1 240 ? -2.857  -7.511  5.465   1.00 11.01 ? 241 MET A CG  1 
ATOM   2025 S  SD  . MET A 1 240 ? -3.790  -6.132  4.935   1.00 14.05 ? 241 MET A SD  1 
ATOM   2026 C  CE  . MET A 1 240 ? -2.435  -5.095  4.227   1.00 12.29 ? 241 MET A CE  1 
ATOM   2027 N  N   . VAL A 1 241 ? -1.611  -11.241 6.572   1.00 9.51  ? 242 VAL A N   1 
ATOM   2028 C  CA  . VAL A 1 241 ? -2.157  -12.115 7.675   1.00 8.29  ? 242 VAL A CA  1 
ATOM   2029 C  C   . VAL A 1 241 ? -1.377  -11.919 8.948   1.00 9.79  ? 242 VAL A C   1 
ATOM   2030 O  O   . VAL A 1 241 ? -0.208  -11.481 8.898   1.00 9.93  ? 242 VAL A O   1 
ATOM   2031 C  CB  . VAL A 1 241 ? -2.089  -13.651 7.288   1.00 10.15 ? 242 VAL A CB  1 
ATOM   2032 C  CG1 . VAL A 1 241 ? -3.049  -13.972 6.018   1.00 9.96  ? 242 VAL A CG1 1 
ATOM   2033 C  CG2 . VAL A 1 241 ? -0.646  -14.119 7.026   1.00 10.87 ? 242 VAL A CG2 1 
ATOM   2034 N  N   . ASP A 1 242 ? -2.022  -12.193 10.075  1.00 7.64  ? 243 ASP A N   1 
ATOM   2035 C  CA  . ASP A 1 242 ? -1.318  -12.078 11.322  1.00 7.44  ? 243 ASP A CA  1 
ATOM   2036 C  C   . ASP A 1 242 ? -0.841  -10.624 11.623  1.00 7.46  ? 243 ASP A C   1 
ATOM   2037 O  O   . ASP A 1 242 ? 0.278   -10.376 12.115  1.00 8.84  ? 243 ASP A O   1 
ATOM   2038 C  CB  . ASP A 1 242 ? -0.220  -13.123 11.517  1.00 8.49  ? 243 ASP A CB  1 
ATOM   2039 C  CG  . ASP A 1 242 ? -0.775  -14.538 11.661  1.00 9.51  ? 243 ASP A CG  1 
ATOM   2040 O  OD1 . ASP A 1 242 ? -1.833  -14.702 12.335  1.00 8.28  ? 243 ASP A OD1 1 
ATOM   2041 O  OD2 . ASP A 1 242 ? -0.162  -15.466 11.102  1.00 10.62 ? 243 ASP A OD2 1 
ATOM   2042 N  N   . ASN A 1 243 ? -1.758  -9.683  11.321  1.00 7.34  ? 244 ASN A N   1 
ATOM   2043 C  CA  . ASN A 1 243 ? -1.428  -8.288  11.558  1.00 7.98  ? 244 ASN A CA  1 
ATOM   2044 C  C   . ASN A 1 243 ? -1.994  -7.836  12.912  1.00 7.28  ? 244 ASN A C   1 
ATOM   2045 O  O   . ASN A 1 243 ? -2.704  -6.805  13.023  1.00 7.57  ? 244 ASN A O   1 
ATOM   2046 C  CB  . ASN A 1 243 ? -1.982  -7.392  10.453  1.00 7.56  ? 244 ASN A CB  1 
ATOM   2047 C  CG  . ASN A 1 243 ? -3.443  -7.615  10.144  1.00 7.93  ? 244 ASN A CG  1 
ATOM   2048 O  OD1 . ASN A 1 243 ? -4.133  -8.433  10.756  1.00 9.76  ? 244 ASN A OD1 1 
ATOM   2049 N  ND2 . ASN A 1 243 ? -3.954  -6.825  9.185   1.00 11.66 ? 244 ASN A ND2 1 
ATOM   2050 N  N   . TRP A 1 244 ? -1.700  -8.618  13.945  1.00 7.42  ? 245 TRP A N   1 
ATOM   2051 C  CA  . TRP A 1 244 ? -2.160  -8.338  15.328  1.00 7.05  ? 245 TRP A CA  1 
ATOM   2052 C  C   . TRP A 1 244 ? -0.976  -8.238  16.242  1.00 7.69  ? 245 TRP A C   1 
ATOM   2053 O  O   . TRP A 1 244 ? 0.049   -8.930  16.045  1.00 8.05  ? 245 TRP A O   1 
ATOM   2054 C  CB  . TRP A 1 244 ? -3.166  -9.410  15.844  1.00 6.96  ? 245 TRP A CB  1 
ATOM   2055 C  CG  . TRP A 1 244 ? -2.667  -10.844 15.635  1.00 6.78  ? 245 TRP A CG  1 
ATOM   2056 C  CD1 . TRP A 1 244 ? -2.810  -11.632 14.481  1.00 7.33  ? 245 TRP A CD1 1 
ATOM   2057 C  CD2 . TRP A 1 244 ? -2.094  -11.725 16.643  1.00 6.01  ? 245 TRP A CD2 1 
ATOM   2058 N  NE1 . TRP A 1 244 ? -2.282  -12.892 14.705  1.00 7.40  ? 245 TRP A NE1 1 
ATOM   2059 C  CE2 . TRP A 1 244 ? -1.847  -12.987 16.011  1.00 7.13  ? 245 TRP A CE2 1 
ATOM   2060 C  CE3 . TRP A 1 244 ? -1.798  -11.569 18.019  1.00 8.01  ? 245 TRP A CE3 1 
ATOM   2061 C  CZ2 . TRP A 1 244 ? -1.227  -14.040 16.703  1.00 8.29  ? 245 TRP A CZ2 1 
ATOM   2062 C  CZ3 . TRP A 1 244 ? -1.194  -12.632 18.704  1.00 8.63  ? 245 TRP A CZ3 1 
ATOM   2063 C  CH2 . TRP A 1 244 ? -0.974  -13.874 18.033  1.00 8.93  ? 245 TRP A CH2 1 
ATOM   2064 N  N   . ARG A 1 245 ? -1.107  -7.347  17.222  1.00 6.29  ? 246 ARG A N   1 
ATOM   2065 C  CA  . ARG A 1 245 ? -0.122  -7.246  18.325  1.00 6.82  ? 246 ARG A CA  1 
ATOM   2066 C  C   . ARG A 1 245 ? -0.629  -8.152  19.487  1.00 6.12  ? 246 ARG A C   1 
ATOM   2067 O  O   . ARG A 1 245 ? -1.816  -8.156  19.774  1.00 7.44  ? 246 ARG A O   1 
ATOM   2068 C  CB  . ARG A 1 245 ? -0.051  -5.763  18.845  1.00 7.11  ? 246 ARG A CB  1 
ATOM   2069 C  CG  . ARG A 1 245 ? 1.048   -5.531  19.881  1.00 6.38  ? 246 ARG A CG  1 
ATOM   2070 C  CD  . ARG A 1 245 ? 0.922   -4.138  20.515  1.00 7.22  ? 246 ARG A CD  1 
ATOM   2071 N  NE  . ARG A 1 245 ? 2.196   -3.821  21.214  1.00 7.56  ? 246 ARG A NE  1 
ATOM   2072 C  CZ  . ARG A 1 245 ? 2.387   -2.776  22.047  1.00 7.24  ? 246 ARG A CZ  1 
ATOM   2073 N  NH1 . ARG A 1 245 ? 1.339   -1.990  22.382  1.00 8.13  ? 246 ARG A NH1 1 
ATOM   2074 N  NH2 . ARG A 1 245 ? 3.631   -2.549  22.500  1.00 9.10  ? 246 ARG A NH2 1 
ATOM   2075 N  N   . PRO A 1 246 ? 0.283   -8.922  20.109  1.00 6.57  ? 247 PRO A N   1 
ATOM   2076 C  CA  . PRO A 1 246 ? -0.136  -9.773  21.235  1.00 7.34  ? 247 PRO A CA  1 
ATOM   2077 C  C   . PRO A 1 246 ? -0.501  -8.955  22.476  1.00 6.92  ? 247 PRO A C   1 
ATOM   2078 O  O   . PRO A 1 246 ? -0.141  -7.765  22.605  1.00 7.62  ? 247 PRO A O   1 
ATOM   2079 C  CB  . PRO A 1 246 ? 1.100   -10.627 21.551  1.00 10.23 ? 247 PRO A CB  1 
ATOM   2080 C  CG  . PRO A 1 246 ? 2.017   -10.404 20.383  1.00 14.09 ? 247 PRO A CG  1 
ATOM   2081 C  CD  . PRO A 1 246 ? 1.697   -9.110  19.737  1.00 8.42  ? 247 PRO A CD  1 
ATOM   2082 N  N   . ALA A 1 247 ? -1.130  -9.629  23.443  1.00 7.12  ? 248 ALA A N   1 
ATOM   2083 C  CA  . ALA A 1 247 ? -1.491  -8.967  24.763  1.00 7.44  ? 248 ALA A CA  1 
ATOM   2084 C  C   . ALA A 1 247 ? -0.235  -8.459  25.451  1.00 7.80  ? 248 ALA A C   1 
ATOM   2085 O  O   . ALA A 1 247 ? 0.812   -9.147  25.449  1.00 9.38  ? 248 ALA A O   1 
ATOM   2086 C  CB  . ALA A 1 247 ? -2.201  -10.012 25.654  1.00 10.25 ? 248 ALA A CB  1 
ATOM   2087 N  N   . GLN A 1 248 ? -0.390  -7.251  26.025  1.00 6.96  ? 249 GLN A N   1 
ATOM   2088 C  CA  . GLN A 1 248 ? 0.689   -6.561  26.731  1.00 7.61  ? 249 GLN A CA  1 
ATOM   2089 C  C   . GLN A 1 248 ? 0.402   -6.553  28.276  1.00 7.96  ? 249 GLN A C   1 
ATOM   2090 O  O   . GLN A 1 248 ? -0.752  -6.720  28.734  1.00 8.12  ? 249 GLN A O   1 
ATOM   2091 C  CB  . GLN A 1 248 ? 0.723   -5.119  26.233  1.00 9.05  ? 249 GLN A CB  1 
ATOM   2092 C  CG  . GLN A 1 248 ? 1.043   -5.070  24.728  1.00 8.68  ? 249 GLN A CG  1 
ATOM   2093 C  CD  . GLN A 1 248 ? 2.399   -5.680  24.378  1.00 10.39 ? 249 GLN A CD  1 
ATOM   2094 O  OE1 . GLN A 1 248 ? 3.423   -5.327  24.972  1.00 12.09 ? 249 GLN A OE1 1 
ATOM   2095 N  NE2 . GLN A 1 248 ? 2.388   -6.656  23.436  1.00 10.35 ? 249 GLN A NE2 1 
ATOM   2096 N  N   . PRO A 1 249 ? 1.436   -6.248  29.058  1.00 10.68 ? 250 PRO A N   1 
ATOM   2097 C  CA  . PRO A 1 249 ? 1.235   -6.275  30.500  1.00 11.31 ? 250 PRO A CA  1 
ATOM   2098 C  C   . PRO A 1 249 ? 0.139   -5.312  30.962  1.00 8.89  ? 250 PRO A C   1 
ATOM   2099 O  O   . PRO A 1 249 ? 0.133   -4.122  30.579  1.00 9.14  ? 250 PRO A O   1 
ATOM   2100 C  CB  . PRO A 1 249 ? 2.647   -5.843  31.052  1.00 12.66 ? 250 PRO A CB  1 
ATOM   2101 C  CG  . PRO A 1 249 ? 3.666   -6.327  30.005  1.00 16.22 ? 250 PRO A CG  1 
ATOM   2102 C  CD  . PRO A 1 249 ? 2.856   -5.982  28.679  1.00 12.99 ? 250 PRO A CD  1 
ATOM   2103 N  N   . LEU A 1 250 ? -0.738  -5.753  31.871  1.00 10.05 ? 251 LEU A N   1 
ATOM   2104 C  CA  . LEU A 1 250 ? -1.811  -4.877  32.367  1.00 9.67  ? 251 LEU A CA  1 
ATOM   2105 C  C   . LEU A 1 250 ? -1.265  -3.767  33.260  1.00 10.18 ? 251 LEU A C   1 
ATOM   2106 O  O   . LEU A 1 250 ? -1.875  -2.700  33.380  1.00 10.56 ? 251 LEU A O   1 
ATOM   2107 C  CB  . LEU A 1 250 ? -2.858  -5.781  33.092  1.00 11.45 ? 251 LEU A CB  1 
ATOM   2108 C  CG  . LEU A 1 250 ? -4.135  -5.079  33.541  1.00 12.63 ? 251 LEU A CG  1 
ATOM   2109 C  CD1 . LEU A 1 250 ? -4.949  -4.536  32.289  1.00 12.17 ? 251 LEU A CD1 1 
ATOM   2110 C  CD2 . LEU A 1 250 ? -5.064  -6.023  34.360  1.00 14.76 ? 251 LEU A CD2 1 
ATOM   2111 N  N   . LYS A 1 251 ? -0.222  -4.110  34.032  1.00 11.11 ? 252 LYS A N   1 
ATOM   2112 C  CA  . LYS A 1 251 ? 0.422   -3.130  34.950  1.00 11.58 ? 252 LYS A CA  1 
ATOM   2113 C  C   . LYS A 1 251 ? -0.644  -2.576  35.900  1.00 12.33 ? 252 LYS A C   1 
ATOM   2114 O  O   . LYS A 1 251 ? -1.454  -3.382  36.419  1.00 15.15 ? 252 LYS A O   1 
ATOM   2115 C  CB  . LYS A 1 251 ? 1.177   -2.046  34.148  1.00 13.73 ? 252 LYS A CB  1 
ATOM   2116 C  CG  . LYS A 1 251 ? 2.313   -2.691  33.334  1.00 16.14 ? 252 LYS A CG  1 
ATOM   2117 C  CD  . LYS A 1 251 ? 3.337   -1.696  32.821  1.00 19.48 ? 252 LYS A CD  1 
ATOM   2118 C  CE  . LYS A 1 251 ? 4.433   -2.451  32.161  1.00 22.17 ? 252 LYS A CE  1 
ATOM   2119 N  NZ  . LYS A 1 251 ? 5.382   -1.492  31.590  1.00 27.12 ? 252 LYS A NZ  1 
ATOM   2120 N  N   . ASN A 1 252 ? -0.613  -1.274  36.148  1.00 12.76 ? 253 ASN A N   1 
ATOM   2121 C  CA  . ASN A 1 252 ? -1.437  -0.753  37.132  1.00 17.82 ? 253 ASN A CA  1 
ATOM   2122 C  C   . ASN A 1 252 ? -2.766  -0.310  36.547  1.00 18.45 ? 253 ASN A C   1 
ATOM   2123 O  O   . ASN A 1 252 ? -2.968  1.001   36.535  1.00 20.97 ? 253 ASN A O   1 
ATOM   2124 C  CB  . ASN A 1 252 ? -0.739  0.496   37.775  1.00 20.62 ? 253 ASN A CB  1 
ATOM   2125 C  CG  . ASN A 1 252 ? -1.522  1.092   39.017  1.00 24.81 ? 253 ASN A CG  1 
ATOM   2126 O  OD1 . ASN A 1 252 ? -2.300  0.396   39.692  1.00 31.13 ? 253 ASN A OD1 1 
ATOM   2127 N  ND2 . ASN A 1 252 ? -1.282  2.382   39.310  1.00 29.90 ? 253 ASN A ND2 1 
ATOM   2128 N  N   . ARG A 1 253 ? -3.576  -1.319  36.013  1.00 12.84 ? 254 ARG A N   1 
ATOM   2129 C  CA  . ARG A 1 253 ? -4.886  -0.984  35.414  1.00 10.00 ? 254 ARG A CA  1 
ATOM   2130 C  C   . ARG A 1 253 ? -6.024  -1.914  35.833  1.00 10.51 ? 254 ARG A C   1 
ATOM   2131 O  O   . ARG A 1 253 ? -5.794  -3.096  36.049  1.00 15.15 ? 254 ARG A O   1 
ATOM   2132 C  CB  . ARG A 1 253 ? -4.787  -0.928  33.864  1.00 9.18  ? 254 ARG A CB  1 
ATOM   2133 C  CG  . ARG A 1 253 ? -3.963  0.234   33.374  1.00 9.37  ? 254 ARG A CG  1 
ATOM   2134 C  CD  . ARG A 1 253 ? -3.869  0.198   31.835  1.00 8.86  ? 254 ARG A CD  1 
ATOM   2135 N  NE  . ARG A 1 253 ? -2.985  -0.943  31.427  1.00 8.56  ? 254 ARG A NE  1 
ATOM   2136 C  CZ  . ARG A 1 253 ? -2.750  -1.240  30.146  1.00 6.81  ? 254 ARG A CZ  1 
ATOM   2137 N  NH1 . ARG A 1 253 ? -3.391  -0.520  29.166  1.00 7.41  ? 254 ARG A NH1 1 
ATOM   2138 N  NH2 . ARG A 1 253 ? -1.891  -2.252  29.822  1.00 6.76  ? 254 ARG A NH2 1 
ATOM   2139 N  N   . GLN A 1 254 ? -7.234  -1.350  35.884  1.00 11.81 ? 255 GLN A N   1 
ATOM   2140 C  CA  . GLN A 1 254 ? -8.424  -2.119  36.226  1.00 13.11 ? 255 GLN A CA  1 
ATOM   2141 C  C   . GLN A 1 254 ? -9.321  -2.187  34.988  1.00 11.81 ? 255 GLN A C   1 
ATOM   2142 O  O   . GLN A 1 254 ? -9.593  -1.103  34.376  1.00 14.52 ? 255 GLN A O   1 
ATOM   2143 C  CB  . GLN A 1 254 ? -9.188  -1.343  37.342  1.00 16.52 ? 255 GLN A CB  1 
ATOM   2144 C  CG  . GLN A 1 254 ? -10.529 -1.804  37.620  1.00 27.40 ? 255 GLN A CG  1 
ATOM   2145 C  CD  . GLN A 1 254 ? -10.526 -3.246  38.143  1.00 33.82 ? 255 GLN A CD  1 
ATOM   2146 O  OE1 . GLN A 1 254 ? -11.370 -4.117  37.726  1.00 38.03 ? 255 GLN A OE1 1 
ATOM   2147 N  NE2 . GLN A 1 254 ? -9.589  -3.521  39.068  1.00 37.96 ? 255 GLN A NE2 1 
ATOM   2148 N  N   . ILE A 1 255 ? -9.726  -3.385  34.576  1.00 9.29  ? 256 ILE A N   1 
ATOM   2149 C  CA  . ILE A 1 255 ? -10.764 -3.527  33.546  1.00 8.35  ? 256 ILE A CA  1 
ATOM   2150 C  C   . ILE A 1 255 ? -12.161 -3.599  34.189  1.00 7.46  ? 256 ILE A C   1 
ATOM   2151 O  O   . ILE A 1 255 ? -12.343 -4.294  35.205  1.00 9.66  ? 256 ILE A O   1 
ATOM   2152 C  CB  . ILE A 1 255 ? -10.488 -4.761  32.701  1.00 8.35  ? 256 ILE A CB  1 
ATOM   2153 C  CG1 . ILE A 1 255 ? -9.027  -4.791  32.185  1.00 9.03  ? 256 ILE A CG1 1 
ATOM   2154 C  CG2 . ILE A 1 255 ? -11.575 -4.958  31.587  1.00 8.55  ? 256 ILE A CG2 1 
ATOM   2155 C  CD1 . ILE A 1 255 ? -8.711  -6.054  31.334  1.00 12.20 ? 256 ILE A CD1 1 
ATOM   2156 N  N   . LYS A 1 256 ? -13.060 -2.729  33.725  1.00 8.53  ? 257 LYS A N   1 
ATOM   2157 C  CA  . LYS A 1 256 ? -14.422 -2.629  34.288  1.00 8.63  ? 257 LYS A CA  1 
ATOM   2158 C  C   . LYS A 1 256 ? -15.376 -3.270  33.311  1.00 7.89  ? 257 LYS A C   1 
ATOM   2159 O  O   . LYS A 1 256 ? -15.197 -3.088  32.095  1.00 10.45 ? 257 LYS A O   1 
ATOM   2160 C  CB  . LYS A 1 256 ? -14.750 -1.144  34.503  1.00 9.92  ? 257 LYS A CB  1 
ATOM   2161 C  CG  . LYS A 1 256 ? -13.756 -0.600  35.622  1.00 15.88 ? 257 LYS A CG  1 
ATOM   2162 C  CD  . LYS A 1 256 ? -13.927 0.793   36.004  1.00 22.91 ? 257 LYS A CD  1 
ATOM   2163 C  CE  . LYS A 1 256 ? -12.681 1.183   36.893  1.00 25.62 ? 257 LYS A CE  1 
ATOM   2164 N  NZ  . LYS A 1 256 ? -12.781 2.733   37.285  1.00 29.77 ? 257 LYS A NZ  1 
ATOM   2165 N  N   . ALA A 1 257 ? -16.420 -3.907  33.848  1.00 8.64  ? 258 ALA A N   1 
ATOM   2166 C  CA  . ALA A 1 257 ? -17.515 -4.525  33.061  1.00 9.82  ? 258 ALA A CA  1 
ATOM   2167 C  C   . ALA A 1 257 ? -18.808 -3.702  33.224  1.00 8.02  ? 258 ALA A C   1 
ATOM   2168 O  O   . ALA A 1 257 ? -19.151 -3.268  34.361  1.00 10.30 ? 258 ALA A O   1 
ATOM   2169 C  CB  . ALA A 1 257 ? -17.767 -5.988  33.467  1.00 11.48 ? 258 ALA A CB  1 
ATOM   2170 N  N   . SER A 1 258 ? -19.517 -3.541  32.092  1.00 10.49 ? 259 SER A N   1 
ATOM   2171 C  CA  . SER A 1 258 ? -20.799 -2.846  32.163  1.00 10.25 ? 259 SER A CA  1 
ATOM   2172 C  C   . SER A 1 258 ? -21.942 -3.786  32.589  1.00 11.93 ? 259 SER A C   1 
ATOM   2173 O  O   . SER A 1 258 ? -23.094 -3.299  32.744  1.00 15.74 ? 259 SER A O   1 
ATOM   2174 C  CB  . SER A 1 258 ? -21.201 -2.234  30.847  1.00 11.30 ? 259 SER A CB  1 
ATOM   2175 O  OG  . SER A 1 258 ? -21.560 -3.281  29.859  1.00 11.12 ? 259 SER A OG  1 
ATOM   2176 N  N   . PHE A 1 259 ? -21.642 -5.070  32.753  1.00 12.12 ? 260 PHE A N   1 
ATOM   2177 C  CA  . PHE A 1 259 ? -22.655 -6.090  32.992  1.00 15.64 ? 260 PHE A CA  1 
ATOM   2178 C  C   . PHE A 1 259 ? -22.274 -6.998  34.155  1.00 19.37 ? 260 PHE A C   1 
ATOM   2179 O  O   . PHE A 1 259 ? -21.101 -7.119  34.502  1.00 17.96 ? 260 PHE A O   1 
ATOM   2180 C  CB  . PHE A 1 259 ? -22.830 -6.938  31.731  1.00 15.24 ? 260 PHE A CB  1 
ATOM   2181 C  CG  . PHE A 1 259 ? -21.563 -7.607  31.280  1.00 15.18 ? 260 PHE A CG  1 
ATOM   2182 C  CD1 . PHE A 1 259 ? -20.631 -6.916  30.525  1.00 12.08 ? 260 PHE A CD1 1 
ATOM   2183 C  CD2 . PHE A 1 259 ? -21.293 -8.917  31.632  1.00 17.01 ? 260 PHE A CD2 1 
ATOM   2184 C  CE1 . PHE A 1 259 ? -19.463 -7.525  30.119  1.00 14.20 ? 260 PHE A CE1 1 
ATOM   2185 C  CE2 . PHE A 1 259 ? -20.127 -9.529  31.227  1.00 18.21 ? 260 PHE A CE2 1 
ATOM   2186 C  CZ  . PHE A 1 259 ? -19.209 -8.832  30.471  1.00 18.57 ? 260 PHE A CZ  1 
ATOM   2187 N  N   . LYS A 1 260 ? -23.267 -7.657  34.741  1.00 30.00 ? 261 LYS A N   1 
ATOM   2188 C  CA  . LYS A 1 260 ? -23.011 -8.572  35.844  1.00 30.00 ? 261 LYS A CA  1 
ATOM   2189 C  C   . LYS A 1 260 ? -22.636 -7.795  37.102  1.00 30.00 ? 261 LYS A C   1 
ATOM   2190 O  O   . LYS A 1 260 ? -23.387 -7.768  38.072  1.00 30.00 ? 261 LYS A O   1 
ATOM   2191 C  CB  . LYS A 1 260 ? -21.885 -9.539  35.476  1.00 20.00 ? 261 LYS A CB  1 
ATOM   2192 C  CG  . LYS A 1 260 ? -22.359 -10.897 34.997  1.00 20.00 ? 261 LYS A CG  1 
ATOM   2193 C  CD  . LYS A 1 260 ? -23.460 -10.758 33.967  1.00 20.00 ? 261 LYS A CD  1 
ATOM   2194 C  CE  . LYS A 1 260 ? -23.337 -11.797 32.857  1.00 20.00 ? 261 LYS A CE  1 
ATOM   2195 N  NZ  . LYS A 1 260 ? -21.967 -12.381 32.748  1.00 20.00 ? 261 LYS A NZ  1 
ATOM   2196 O  OXT . LYS A 1 260 ? -21.641 -7.205  37.234  1.00 30.00 ? 261 LYS A OXT 1 
HETATM 2197 ZN ZN  . ZN  B 2 .   ? -6.713  -1.708  15.340  1.00 6.22  ? 262 ZN  A ZN  1 
HETATM 2198 S  S   . DMS C 3 .   ? 1.312   -11.764 15.016  1.00 21.93 ? 263 DMS A S   1 
HETATM 2199 O  O   . DMS C 3 .   ? 2.381   -10.566 14.251  1.00 26.12 ? 263 DMS A O   1 
HETATM 2200 C  C1  . DMS C 3 .   ? 2.098   -13.280 14.657  1.00 19.42 ? 263 DMS A C1  1 
HETATM 2201 C  C2  . DMS C 3 .   ? 1.726   -11.521 16.713  1.00 19.67 ? 263 DMS A C2  1 
HETATM 2202 S  S   . DMS D 3 .   ? -6.031  7.874   11.212  1.00 40.22 ? 264 DMS A S   1 
HETATM 2203 O  O   . DMS D 3 .   ? -6.414  6.291   10.507  1.00 32.88 ? 264 DMS A O   1 
HETATM 2204 C  C1  . DMS D 3 .   ? -4.276  8.241   10.815  1.00 33.90 ? 264 DMS A C1  1 
HETATM 2205 C  C2  . DMS D 3 .   ? -6.903  9.139   10.243  1.00 36.29 ? 264 DMS A C2  1 
HETATM 2206 N  N1  . BCN E 4 .   ? -21.095 -14.212 23.474  1.00 28.49 ? 265 BCN A N1  1 
HETATM 2207 C  C1  . BCN E 4 .   ? -19.976 -14.207 24.430  1.00 27.18 ? 265 BCN A C1  1 
HETATM 2208 C  C2  . BCN E 4 .   ? -20.060 -15.214 25.554  1.00 29.12 ? 265 BCN A C2  1 
HETATM 2209 O  O21 . BCN E 4 .   ? -19.402 -15.043 26.556  1.00 26.34 ? 265 BCN A O21 1 
HETATM 2210 O  O22 . BCN E 4 .   ? -21.107 -16.024 25.616  1.00 31.98 ? 265 BCN A O22 1 
HETATM 2211 C  C3  . BCN E 4 .   ? -22.223 -13.554 23.295  1.00 29.74 ? 265 BCN A C3  1 
HETATM 2212 C  C4  . BCN E 4 .   ? -23.345 -13.348 24.211  1.00 32.95 ? 265 BCN A C4  1 
HETATM 2213 O  O4  . BCN E 4 .   ? -22.655 -12.371 24.992  1.00 28.06 ? 265 BCN A O4  1 
HETATM 2214 C  C5  . BCN E 4 .   ? -21.327 -15.106 22.433  1.00 32.81 ? 265 BCN A C5  1 
HETATM 2215 C  C6  . BCN E 4 .   ? -19.999 -15.702 22.462  1.00 20.12 ? 265 BCN A C6  1 
HETATM 2216 O  O6  . BCN E 4 .   ? -19.976 -16.534 21.366  1.00 37.55 ? 265 BCN A O6  1 
HETATM 2217 N  N1  . E90 F 5 .   ? -1.479  7.683   14.379  1.00 14.36 ? 266 E90 A N1  1 
HETATM 2218 C  C2  . E90 F 5 .   ? -1.418  7.833   13.018  1.00 15.65 ? 266 E90 A C2  1 
HETATM 2219 N  N3  . E90 F 5 .   ? -1.160  8.992   12.371  1.00 17.43 ? 266 E90 A N3  1 
HETATM 2220 C  C4  . E90 F 5 .   ? -0.988  10.110  13.151  1.00 20.88 ? 266 E90 A C4  1 
HETATM 2221 C  C5  . E90 F 5 .   ? -0.981  10.009  14.559  1.00 19.71 ? 266 E90 A C5  1 
HETATM 2222 C  C6  . E90 F 5 .   ? -1.300  8.759   15.146  1.00 16.62 ? 266 E90 A C6  1 
HETATM 2223 S  S7  . E90 F 5 .   ? -1.594  6.500   11.964  1.00 18.79 ? 266 E90 A S7  1 
HETATM 2224 C  C8  . E90 F 5 .   ? -2.129  5.191   13.130  1.00 14.43 ? 266 E90 A C8  1 
HETATM 2225 C  C9  . E90 F 5 .   ? -3.607  5.329   13.537  1.00 13.05 ? 266 E90 A C9  1 
HETATM 2226 O  O10 . E90 F 5 .   ? -4.323  6.282   13.176  1.00 15.40 ? 266 E90 A O10 1 
HETATM 2227 C  C11 . E90 F 5 .   ? -4.205  4.253   14.393  1.00 9.89  ? 266 E90 A C11 1 
HETATM 2228 C  C12 . E90 F 5 .   ? -3.405  3.172   14.804  1.00 10.44 ? 266 E90 A C12 1 
HETATM 2229 C  C13 . E90 F 5 .   ? -3.948  2.164   15.563  1.00 9.32  ? 266 E90 A C13 1 
HETATM 2230 C  C14 . E90 F 5 .   ? -5.302  2.208   15.873  1.00 5.97  ? 266 E90 A C14 1 
HETATM 2231 C  C15 . E90 F 5 .   ? -6.125  3.232   15.479  1.00 7.31  ? 266 E90 A C15 1 
HETATM 2232 C  C16 . E90 F 5 .   ? -5.545  4.285   14.768  1.00 9.02  ? 266 E90 A C16 1 
HETATM 2233 S  S17 . E90 F 5 .   ? -5.947  0.867   16.839  1.00 6.59  ? 266 E90 A S17 1 
HETATM 2234 O  O18 . E90 F 5 .   ? -5.392  1.064   18.165  1.00 5.76  ? 266 E90 A O18 1 
HETATM 2235 O  O19 . E90 F 5 .   ? -7.402  0.958   16.700  1.00 6.78  ? 266 E90 A O19 1 
HETATM 2236 N  N20 . E90 F 5 .   ? -5.327  -0.512  16.225  1.00 6.38  ? 266 E90 A N20 1 
HETATM 2237 O  O   . HOH G 6 .   ? -26.394 3.491   15.426  1.00 25.28 ? 126 HOH A O   1 
HETATM 2238 O  O   . HOH G 6 .   ? 0.531   7.198   29.935  1.00 29.53 ? 267 HOH A O   1 
HETATM 2239 O  O   . HOH G 6 .   ? -20.126 17.046  23.292  1.00 32.02 ? 268 HOH A O   1 
HETATM 2240 O  O   . HOH G 6 .   ? -4.319  -1.815  38.226  1.00 27.47 ? 269 HOH A O   1 
HETATM 2241 O  O   . HOH G 6 .   ? -2.243  -4.559  -7.058  1.00 31.02 ? 270 HOH A O   1 
HETATM 2242 O  O   . HOH G 6 .   ? -7.177  -10.171 -4.485  1.00 27.87 ? 271 HOH A O   1 
HETATM 2243 O  O   . HOH G 6 .   ? -24.427 -14.226 19.754  1.00 29.03 ? 272 HOH A O   1 
HETATM 2244 O  O   . HOH G 6 .   ? -31.943 6.918   15.314  1.00 35.76 ? 273 HOH A O   1 
HETATM 2245 O  O   . HOH G 6 .   ? -12.739 3.645   -6.969  1.00 31.57 ? 274 HOH A O   1 
HETATM 2246 O  O   . HOH G 6 .   ? 2.024   -4.295  -12.454 1.00 26.48 ? 275 HOH A O   1 
HETATM 2247 O  O   . HOH G 6 .   ? 6.618   -5.772  6.672   1.00 30.24 ? 276 HOH A O   1 
HETATM 2248 O  O   . HOH G 6 .   ? -25.523 4.223   4.041   1.00 34.52 ? 277 HOH A O   1 
HETATM 2249 O  O   . HOH G 6 .   ? -21.882 19.552  12.246  1.00 31.07 ? 278 HOH A O   1 
HETATM 2250 O  O   . HOH G 6 .   ? -3.287  -18.005 0.265   1.00 35.52 ? 279 HOH A O   1 
HETATM 2251 O  O   . HOH G 6 .   ? 6.551   8.563   18.188  1.00 25.98 ? 280 HOH A O   1 
HETATM 2252 O  O   . HOH G 6 .   ? -16.855 -17.776 24.273  1.00 29.19 ? 281 HOH A O   1 
HETATM 2253 O  O   . HOH G 6 .   ? 6.728   -2.017  -8.024  1.00 32.76 ? 282 HOH A O   1 
HETATM 2254 O  O   . HOH G 6 .   ? 7.572   -7.929  -1.050  1.00 29.52 ? 283 HOH A O   1 
HETATM 2255 O  O   . HOH G 6 .   ? 6.190   -8.319  -10.508 1.00 32.67 ? 284 HOH A O   1 
HETATM 2256 O  O   . HOH G 6 .   ? -25.755 -3.485  32.452  1.00 41.40 ? 285 HOH A O   1 
HETATM 2257 O  O   . HOH G 6 .   ? 4.552   -0.775  -5.649  1.00 30.41 ? 286 HOH A O   1 
HETATM 2258 O  O   . HOH G 6 .   ? -24.173 -0.296  31.758  1.00 35.53 ? 287 HOH A O   1 
HETATM 2259 O  O   . HOH G 6 .   ? -7.088  -8.520  -7.137  1.00 34.49 ? 288 HOH A O   1 
HETATM 2260 O  O   . HOH G 6 .   ? -19.997 -2.029  43.225  1.00 39.91 ? 289 HOH A O   1 
HETATM 2261 O  O   . HOH G 6 .   ? 8.854   -11.531 6.663   1.00 33.15 ? 290 HOH A O   1 
HETATM 2262 O  O   . HOH G 6 .   ? 10.054  -2.421  13.984  1.00 28.49 ? 291 HOH A O   1 
HETATM 2263 O  O   . HOH G 6 .   ? -25.779 -1.123  35.285  1.00 32.43 ? 292 HOH A O   1 
HETATM 2264 O  O   . HOH G 6 .   ? -11.005 -5.750  40.762  1.00 31.30 ? 293 HOH A O   1 
HETATM 2265 O  O   . HOH G 6 .   ? 2.626   7.562   13.037  1.00 51.52 ? 294 HOH A O   1 
HETATM 2266 O  O   . HOH G 6 .   ? -10.044 -26.394 5.966   1.00 33.25 ? 295 HOH A O   1 
HETATM 2267 O  O   . HOH G 6 .   ? -14.504 -21.362 3.129   1.00 38.11 ? 296 HOH A O   1 
HETATM 2268 O  O   . HOH G 6 .   ? 1.352   -16.121 -1.881  1.00 34.70 ? 297 HOH A O   1 
HETATM 2269 O  O   . HOH G 6 .   ? 2.425   -14.671 -5.783  1.00 33.68 ? 298 HOH A O   1 
HETATM 2270 O  O   . HOH G 6 .   ? -27.136 -12.939 20.511  1.00 33.40 ? 299 HOH A O   1 
HETATM 2271 O  O   . HOH G 6 .   ? -1.161  -3.773  39.784  1.00 35.19 ? 300 HOH A O   1 
HETATM 2272 O  O   . HOH G 6 .   ? -16.969 19.165  22.263  1.00 44.12 ? 301 HOH A O   1 
HETATM 2273 O  O   . HOH G 6 .   ? -29.062 6.340   15.918  1.00 44.86 ? 302 HOH A O   1 
HETATM 2274 O  O   . HOH G 6 .   ? 14.698  -11.744 13.387  1.00 37.72 ? 303 HOH A O   1 
HETATM 2275 O  O   . HOH G 6 .   ? 5.293   -10.693 18.846  1.00 36.93 ? 304 HOH A O   1 
HETATM 2276 O  O   . HOH G 6 .   ? -25.781 -6.894  34.085  1.00 41.01 ? 305 HOH A O   1 
HETATM 2277 O  O   . HOH G 6 .   ? -27.369 -5.251  27.665  1.00 31.17 ? 306 HOH A O   1 
HETATM 2278 O  O   . HOH G 6 .   ? -27.463 -7.436  26.156  1.00 32.84 ? 307 HOH A O   1 
HETATM 2279 O  O   . HOH G 6 .   ? -10.471 -5.935  38.624  1.00 29.33 ? 308 HOH A O   1 
HETATM 2280 O  O   . HOH G 6 .   ? -13.854 14.808  6.269   1.00 48.15 ? 309 HOH A O   1 
HETATM 2281 O  O   . HOH G 6 .   ? -23.951 19.962  10.818  1.00 51.19 ? 310 HOH A O   1 
HETATM 2282 O  O   . HOH G 6 .   ? -26.841 -6.297  4.659   1.00 35.26 ? 311 HOH A O   1 
HETATM 2283 O  O   . HOH G 6 .   ? -14.088 -5.019  -6.395  1.00 33.56 ? 312 HOH A O   1 
HETATM 2284 O  O   . HOH G 6 .   ? -13.189 -0.758  -6.100  1.00 31.70 ? 313 HOH A O   1 
HETATM 2285 O  O   . HOH G 6 .   ? -24.097 -3.519  3.961   1.00 29.74 ? 314 HOH A O   1 
HETATM 2286 O  O   . HOH G 6 .   ? -6.164  -18.385 3.441   1.00 33.26 ? 315 HOH A O   1 
HETATM 2287 O  O   . HOH G 6 .   ? -6.396  -19.428 5.431   1.00 29.15 ? 316 HOH A O   1 
HETATM 2288 O  O   . HOH G 6 .   ? -10.205 -12.598 40.434  1.00 29.66 ? 317 HOH A O   1 
HETATM 2289 O  O   . HOH G 6 .   ? -16.578 -14.015 -3.164  1.00 30.81 ? 318 HOH A O   1 
HETATM 2290 O  O   . HOH G 6 .   ? -26.985 -11.006 22.761  1.00 30.06 ? 319 HOH A O   1 
HETATM 2291 O  O   . HOH G 6 .   ? 10.118  0.011   14.048  1.00 35.46 ? 320 HOH A O   1 
HETATM 2292 O  O   . HOH G 6 .   ? -1.286  -4.138  15.765  1.00 7.56  ? 321 HOH A O   1 
HETATM 2293 O  O   . HOH G 6 .   ? -4.569  -13.612 18.163  1.00 8.16  ? 322 HOH A O   1 
HETATM 2294 O  O   . HOH G 6 .   ? -17.134 -8.463  20.484  1.00 7.44  ? 323 HOH A O   1 
HETATM 2295 O  O   . HOH G 6 .   ? -3.556  -11.221 20.985  1.00 8.47  ? 324 HOH A O   1 
HETATM 2296 O  O   . HOH G 6 .   ? -7.992  -15.519 11.399  1.00 8.83  ? 325 HOH A O   1 
HETATM 2297 O  O   . HOH G 6 .   ? 4.876   -4.898  21.007  1.00 12.18 ? 326 HOH A O   1 
HETATM 2298 O  O   . HOH G 6 .   ? -12.957 -17.332 16.942  1.00 10.87 ? 327 HOH A O   1 
HETATM 2299 O  O   . HOH G 6 .   ? -2.485  -8.799  29.234  1.00 9.38  ? 328 HOH A O   1 
HETATM 2300 O  O   . HOH G 6 .   ? -8.726  -3.891  7.887   1.00 8.82  ? 329 HOH A O   1 
HETATM 2301 O  O   . HOH G 6 .   ? 3.674   5.066   29.870  1.00 15.74 ? 330 HOH A O   1 
HETATM 2302 O  O   . HOH G 6 .   ? -10.436 -18.383 17.130  1.00 11.09 ? 331 HOH A O   1 
HETATM 2303 O  O   . HOH G 6 .   ? -3.853  -15.973 24.471  1.00 10.98 ? 332 HOH A O   1 
HETATM 2304 O  O   . HOH G 6 .   ? -18.070 -20.562 8.007   1.00 13.36 ? 333 HOH A O   1 
HETATM 2305 O  O   . HOH G 6 .   ? -21.713 -7.204  23.703  1.00 11.28 ? 334 HOH A O   1 
HETATM 2306 O  O   . HOH G 6 .   ? -2.125  -12.368 22.974  1.00 8.98  ? 335 HOH A O   1 
HETATM 2307 O  O   . HOH G 6 .   ? 1.216   8.896   24.491  1.00 16.21 ? 336 HOH A O   1 
HETATM 2308 O  O   . HOH G 6 .   ? 1.271   -1.622  29.504  1.00 11.25 ? 337 HOH A O   1 
HETATM 2309 O  O   . HOH G 6 .   ? -13.547 -18.647 14.646  1.00 13.18 ? 338 HOH A O   1 
HETATM 2310 O  O   . HOH G 6 .   ? -21.947 5.687   4.791   1.00 16.13 ? 339 HOH A O   1 
HETATM 2311 O  O   . HOH G 6 .   ? -3.471  -13.349 25.295  1.00 9.66  ? 340 HOH A O   1 
HETATM 2312 O  O   . HOH G 6 .   ? -14.083 10.408  27.994  1.00 15.90 ? 341 HOH A O   1 
HETATM 2313 O  O   . HOH G 6 .   ? -9.616  -8.040  34.200  1.00 19.22 ? 342 HOH A O   1 
HETATM 2314 O  O   . HOH G 6 .   ? -16.225 -12.364 24.506  1.00 11.65 ? 343 HOH A O   1 
HETATM 2315 O  O   . HOH G 6 .   ? -14.783 -18.666 18.848  1.00 13.63 ? 344 HOH A O   1 
HETATM 2316 O  O   . HOH G 6 .   ? -12.172 2.730   31.087  1.00 17.45 ? 345 HOH A O   1 
HETATM 2317 O  O   . HOH G 6 .   ? 8.568   -3.809  21.131  1.00 13.82 ? 346 HOH A O   1 
HETATM 2318 O  O   . HOH G 6 .   ? -19.351 10.066  8.909   1.00 13.37 ? 347 HOH A O   1 
HETATM 2319 O  O   . HOH G 6 .   ? -21.139 -12.781 -1.865  1.00 17.73 ? 348 HOH A O   1 
HETATM 2320 O  O   . HOH G 6 .   ? -24.131 -0.769  26.554  1.00 15.78 ? 349 HOH A O   1 
HETATM 2321 O  O   . HOH G 6 .   ? -6.830  -20.332 19.618  1.00 11.91 ? 350 HOH A O   1 
HETATM 2322 O  O   . HOH G 6 .   ? -16.340 -9.949  33.121  1.00 16.11 ? 351 HOH A O   1 
HETATM 2323 O  O   . HOH G 6 .   ? 5.448   7.179   20.257  1.00 14.80 ? 352 HOH A O   1 
HETATM 2324 O  O   . HOH G 6 .   ? -24.247 8.570   20.236  1.00 17.10 ? 353 HOH A O   1 
HETATM 2325 O  O   . HOH G 6 .   ? -13.093 -16.937 26.808  1.00 12.82 ? 354 HOH A O   1 
HETATM 2326 O  O   . HOH G 6 .   ? -17.850 -21.327 17.601  1.00 21.58 ? 355 HOH A O   1 
HETATM 2327 O  O   . HOH G 6 .   ? -23.962 -0.802  3.920   1.00 20.23 ? 356 HOH A O   1 
HETATM 2328 O  O   . HOH G 6 .   ? -23.091 -11.718 14.082  1.00 18.57 ? 357 HOH A O   1 
HETATM 2329 O  O   . HOH G 6 .   ? -14.378 -16.738 29.225  1.00 18.50 ? 358 HOH A O   1 
HETATM 2330 O  O   . HOH G 6 .   ? -1.178  -11.197 29.119  1.00 15.51 ? 359 HOH A O   1 
HETATM 2331 O  O   . HOH G 6 .   ? 7.624   6.175   21.687  1.00 15.04 ? 360 HOH A O   1 
HETATM 2332 O  O   . HOH G 6 .   ? -16.372 15.893  23.781  1.00 16.64 ? 361 HOH A O   1 
HETATM 2333 O  O   . HOH G 6 .   ? -20.504 10.744  26.894  1.00 17.36 ? 362 HOH A O   1 
HETATM 2334 O  O   . HOH G 6 .   ? -18.013 10.648  11.345  1.00 14.46 ? 363 HOH A O   1 
HETATM 2335 O  O   . HOH G 6 .   ? -31.089 1.342   26.022  1.00 23.08 ? 364 HOH A O   1 
HETATM 2336 O  O   . HOH G 6 .   ? -8.237  -19.484 21.799  1.00 12.38 ? 365 HOH A O   1 
HETATM 2337 O  O   . HOH G 6 .   ? -7.091  6.000   6.282   1.00 17.28 ? 366 HOH A O   1 
HETATM 2338 O  O   . HOH G 6 .   ? -1.449  1.759   11.589  1.00 18.30 ? 367 HOH A O   1 
HETATM 2339 O  O   . HOH G 6 .   ? -24.913 -7.789  9.067   1.00 17.68 ? 368 HOH A O   1 
HETATM 2340 O  O   . HOH G 6 .   ? -13.872 -21.344 15.240  1.00 17.08 ? 369 HOH A O   1 
HETATM 2341 O  O   . HOH G 6 .   ? -9.093  -5.850  36.058  1.00 15.93 ? 370 HOH A O   1 
HETATM 2342 O  O   . HOH G 6 .   ? -8.171  -22.336 10.504  1.00 18.66 ? 371 HOH A O   1 
HETATM 2343 O  O   . HOH G 6 .   ? -10.742 -19.532 20.151  1.00 16.80 ? 372 HOH A O   1 
HETATM 2344 O  O   . HOH G 6 .   ? -4.729  0.995   43.682  1.00 20.31 ? 373 HOH A O   1 
HETATM 2345 O  O   . HOH G 6 .   ? 1.427   -11.815 25.205  1.00 22.37 ? 374 HOH A O   1 
HETATM 2346 O  O   . HOH G 6 .   ? -19.999 -16.865 2.907   1.00 22.41 ? 375 HOH A O   1 
HETATM 2347 O  O   . HOH G 6 .   ? -16.931 -14.040 26.531  1.00 17.35 ? 376 HOH A O   1 
HETATM 2348 O  O   . HOH G 6 .   ? -7.360  -8.729  32.756  1.00 16.45 ? 377 HOH A O   1 
HETATM 2349 O  O   . HOH G 6 .   ? -1.473  -13.256 27.202  1.00 19.79 ? 378 HOH A O   1 
HETATM 2350 O  O   . HOH G 6 .   ? -22.935 -5.836  2.677   1.00 19.55 ? 379 HOH A O   1 
HETATM 2351 O  O   . HOH G 6 .   ? -15.033 -21.211 17.675  1.00 16.62 ? 380 HOH A O   1 
HETATM 2352 O  O   . HOH G 6 .   ? -4.767  -11.965 32.258  1.00 17.41 ? 381 HOH A O   1 
HETATM 2353 O  O   . HOH G 6 .   ? 4.283   -3.435  26.594  1.00 17.43 ? 382 HOH A O   1 
HETATM 2354 O  O   . HOH G 6 .   ? -10.172 -26.514 12.263  1.00 17.83 ? 383 HOH A O   1 
HETATM 2355 O  O   . HOH G 6 .   ? -6.862  -15.027 31.708  1.00 19.90 ? 384 HOH A O   1 
HETATM 2356 O  O   . HOH G 6 .   ? 4.355   -6.556  7.847   1.00 21.57 ? 385 HOH A O   1 
HETATM 2357 O  O   . HOH G 6 .   ? -26.944 -2.657  14.438  1.00 19.46 ? 386 HOH A O   1 
HETATM 2358 O  O   . HOH G 6 .   ? -28.937 0.287   24.571  1.00 19.57 ? 387 HOH A O   1 
HETATM 2359 O  O   . HOH G 6 .   ? -22.269 -18.387 13.601  1.00 19.75 ? 388 HOH A O   1 
HETATM 2360 O  O   . HOH G 6 .   ? -14.255 14.299  27.308  1.00 20.67 ? 389 HOH A O   1 
HETATM 2361 O  O   . HOH G 6 .   ? 4.364   -2.532  29.049  1.00 21.72 ? 390 HOH A O   1 
HETATM 2362 O  O   . HOH G 6 .   ? -4.495  4.220   10.345  1.00 23.03 ? 391 HOH A O   1 
HETATM 2363 O  O   . HOH G 6 .   ? -1.915  -17.481 25.683  1.00 23.72 ? 392 HOH A O   1 
HETATM 2364 O  O   . HOH G 6 .   ? -18.580 -3.941  -2.654  1.00 23.37 ? 393 HOH A O   1 
HETATM 2365 O  O   . HOH G 6 .   ? -0.527  10.877  23.554  1.00 14.92 ? 394 HOH A O   1 
HETATM 2366 O  O   . HOH G 6 .   ? -23.321 -3.044  6.660   1.00 19.76 ? 395 HOH A O   1 
HETATM 2367 O  O   . HOH G 6 .   ? -15.480 -21.899 13.119  1.00 16.48 ? 396 HOH A O   1 
HETATM 2368 O  O   . HOH G 6 .   ? -4.235  -8.617  31.293  1.00 17.63 ? 397 HOH A O   1 
HETATM 2369 O  O   . HOH G 6 .   ? -2.608  -3.206  11.465  1.00 19.04 ? 398 HOH A O   1 
HETATM 2370 O  O   . HOH G 6 .   ? -0.520  -8.592  32.598  1.00 21.41 ? 399 HOH A O   1 
HETATM 2371 O  O   . HOH G 6 .   ? -8.615  -19.930 26.896  1.00 18.80 ? 400 HOH A O   1 
HETATM 2372 O  O   . HOH G 6 .   ? -7.270  -16.896 1.463   1.00 20.39 ? 401 HOH A O   1 
HETATM 2373 O  O   . HOH G 6 .   ? 0.210   -1.126  -4.718  1.00 17.05 ? 402 HOH A O   1 
HETATM 2374 O  O   . HOH G 6 .   ? -8.554  -14.729 40.826  1.00 17.02 ? 403 HOH A O   1 
HETATM 2375 O  O   . HOH G 6 .   ? -6.094  -4.674  -6.503  1.00 23.49 ? 404 HOH A O   1 
HETATM 2376 O  O   . HOH G 6 .   ? -6.315  -19.804 23.921  1.00 17.88 ? 405 HOH A O   1 
HETATM 2377 O  O   . HOH G 6 .   ? -3.669  -13.018 -2.908  1.00 20.67 ? 406 HOH A O   1 
HETATM 2378 O  O   . HOH G 6 .   ? -17.074 -18.007 20.288  1.00 19.18 ? 407 HOH A O   1 
HETATM 2379 O  O   . HOH G 6 .   ? -0.304  -14.410 22.396  1.00 19.79 ? 408 HOH A O   1 
HETATM 2380 O  O   . HOH G 6 .   ? -16.581 -11.363 41.896  1.00 21.61 ? 409 HOH A O   1 
HETATM 2381 O  O   . HOH G 6 .   ? -7.089  0.192   44.881  1.00 18.11 ? 410 HOH A O   1 
HETATM 2382 O  O   . HOH G 6 .   ? -1.619  11.460  26.045  1.00 23.15 ? 411 HOH A O   1 
HETATM 2383 O  O   . HOH G 6 .   ? -31.104 -6.931  22.495  1.00 24.73 ? 412 HOH A O   1 
HETATM 2384 O  O   . HOH G 6 .   ? 8.236   -5.767  -10.488 1.00 24.65 ? 413 HOH A O   1 
HETATM 2385 O  O   . HOH G 6 .   ? -27.069 -3.981  25.169  1.00 19.40 ? 414 HOH A O   1 
HETATM 2386 O  O   . HOH G 6 .   ? -24.427 -1.505  -6.035  1.00 14.84 ? 415 HOH A O   1 
HETATM 2387 O  O   . HOH G 6 .   ? 1.859   -15.805 9.280   1.00 19.75 ? 416 HOH A O   1 
HETATM 2388 O  O   . HOH G 6 .   ? -15.618 -16.510 25.845  1.00 24.89 ? 417 HOH A O   1 
HETATM 2389 O  O   . HOH G 6 .   ? 2.569   -13.120 5.210   1.00 22.41 ? 418 HOH A O   1 
HETATM 2390 O  O   . HOH G 6 .   ? -29.302 -5.875  24.525  1.00 23.32 ? 419 HOH A O   1 
HETATM 2391 O  O   . HOH G 6 .   ? -0.179  3.507   10.092  1.00 24.36 ? 420 HOH A O   1 
HETATM 2392 O  O   . HOH G 6 .   ? -26.094 6.171   27.143  1.00 20.99 ? 421 HOH A O   1 
HETATM 2393 O  O   . HOH G 6 .   ? -8.584  -15.428 36.899  1.00 23.06 ? 422 HOH A O   1 
HETATM 2394 O  O   . HOH G 6 .   ? -11.115 1.174   33.616  1.00 20.16 ? 423 HOH A O   1 
HETATM 2395 O  O   . HOH G 6 .   ? -19.316 14.372  35.504  1.00 19.41 ? 424 HOH A O   1 
HETATM 2396 O  O   . HOH G 6 .   ? -8.403  -17.597 35.125  1.00 20.22 ? 425 HOH A O   1 
HETATM 2397 O  O   . HOH G 6 .   ? -11.064 -15.221 34.421  1.00 23.01 ? 426 HOH A O   1 
HETATM 2398 O  O   . HOH G 6 .   ? 1.677   12.551  22.758  1.00 24.22 ? 427 HOH A O   1 
HETATM 2399 O  O   . HOH G 6 .   ? 3.775   9.946   23.848  1.00 22.86 ? 428 HOH A O   1 
HETATM 2400 O  O   . HOH G 6 .   ? -18.819 -21.182 14.833  1.00 22.37 ? 429 HOH A O   1 
HETATM 2401 O  O   . HOH G 6 .   ? 2.679   -4.372  7.707   1.00 17.89 ? 430 HOH A O   1 
HETATM 2402 O  O   . HOH G 6 .   ? -18.810 3.636   -3.485  1.00 32.80 ? 431 HOH A O   1 
HETATM 2403 O  O   . HOH G 6 .   ? 5.340   -17.107 5.777   1.00 25.61 ? 432 HOH A O   1 
HETATM 2404 O  O   . HOH G 6 .   ? -34.097 3.102   27.841  1.00 27.11 ? 433 HOH A O   1 
HETATM 2405 O  O   . HOH G 6 .   ? -2.105  -11.950 31.646  1.00 26.83 ? 434 HOH A O   1 
HETATM 2406 O  O   . HOH G 6 .   ? -11.058 -19.712 7.247   1.00 26.47 ? 435 HOH A O   1 
HETATM 2407 O  O   . HOH G 6 .   ? -23.383 -0.494  34.570  1.00 24.34 ? 436 HOH A O   1 
HETATM 2408 O  O   . HOH G 6 .   ? -26.014 -6.222  13.170  1.00 28.20 ? 437 HOH A O   1 
HETATM 2409 O  O   . HOH G 6 .   ? 0.436   0.563   -6.838  1.00 25.98 ? 438 HOH A O   1 
HETATM 2410 O  O   . HOH G 6 .   ? -9.908  1.463   39.304  1.00 24.22 ? 439 HOH A O   1 
HETATM 2411 O  O   . HOH G 6 .   ? -6.612  -5.268  37.511  1.00 18.78 ? 440 HOH A O   1 
HETATM 2412 O  O   . HOH G 6 .   ? -3.976  -15.615 -2.343  1.00 31.82 ? 441 HOH A O   1 
HETATM 2413 O  O   . HOH G 6 .   ? 2.546   -11.477 9.417   1.00 21.81 ? 442 HOH A O   1 
HETATM 2414 O  O   . HOH G 6 .   ? -26.653 -11.597 2.137   1.00 23.69 ? 443 HOH A O   1 
HETATM 2415 O  O   . HOH G 6 .   ? -0.039  -14.384 31.262  1.00 26.87 ? 444 HOH A O   1 
HETATM 2416 O  O   . HOH G 6 .   ? -2.590  4.497   8.455   1.00 25.18 ? 445 HOH A O   1 
HETATM 2417 O  O   . HOH G 6 .   ? -13.148 -22.244 8.627   1.00 22.98 ? 446 HOH A O   1 
HETATM 2418 O  O   . HOH G 6 .   ? -23.690 8.354   3.663   1.00 22.60 ? 447 HOH A O   1 
HETATM 2419 O  O   . HOH G 6 .   ? -19.429 -20.845 5.118   1.00 24.36 ? 448 HOH A O   1 
HETATM 2420 O  O   . HOH G 6 .   ? -33.637 -4.752  23.753  1.00 22.00 ? 449 HOH A O   1 
HETATM 2421 O  O   . HOH G 6 .   ? -12.488 12.574  29.376  1.00 21.78 ? 450 HOH A O   1 
HETATM 2422 O  O   . HOH G 6 .   ? -10.724 -19.094 34.663  1.00 19.14 ? 451 HOH A O   1 
HETATM 2423 O  O   . HOH G 6 .   ? -14.970 6.137   32.862  1.00 30.82 ? 452 HOH A O   1 
HETATM 2424 O  O   . HOH G 6 .   ? -23.520 -13.285 11.320  1.00 18.45 ? 453 HOH A O   1 
HETATM 2425 O  O   . HOH G 6 .   ? -15.273 -10.297 37.661  1.00 26.72 ? 454 HOH A O   1 
HETATM 2426 O  O   . HOH G 6 .   ? -10.600 4.889   31.132  1.00 21.51 ? 455 HOH A O   1 
HETATM 2427 O  O   . HOH G 6 .   ? -6.149  -11.742 36.722  1.00 32.07 ? 456 HOH A O   1 
HETATM 2428 O  O   . HOH G 6 .   ? -7.047  -11.912 44.323  1.00 8.52  ? 457 HOH A O   1 
HETATM 2429 O  O   . HOH G 6 .   ? -32.081 5.542   12.824  1.00 34.58 ? 458 HOH A O   1 
HETATM 2430 O  O   . HOH G 6 .   ? -3.623  -17.032 36.632  1.00 27.03 ? 459 HOH A O   1 
HETATM 2431 O  O   . HOH G 6 .   ? -1.021  -17.593 18.118  1.00 27.21 ? 460 HOH A O   1 
HETATM 2432 O  O   . HOH G 6 .   ? -8.683  0.620   -6.597  1.00 25.69 ? 461 HOH A O   1 
HETATM 2433 O  O   . HOH G 6 .   ? 1.979   -14.278 20.739  1.00 27.18 ? 462 HOH A O   1 
HETATM 2434 O  O   . HOH G 6 .   ? -28.290 11.965  5.348   1.00 26.13 ? 463 HOH A O   1 
HETATM 2435 O  O   . HOH G 6 .   ? -3.073  -0.212  10.559  1.00 20.79 ? 464 HOH A O   1 
HETATM 2436 O  O   . HOH G 6 .   ? -9.387  -10.096 -1.341  1.00 23.16 ? 465 HOH A O   1 
HETATM 2437 O  O   . HOH G 6 .   ? -21.367 -19.703 6.652   1.00 22.57 ? 466 HOH A O   1 
HETATM 2438 O  O   . HOH G 6 .   ? -4.830  7.544   5.833   1.00 20.68 ? 467 HOH A O   1 
HETATM 2439 O  O   . HOH G 6 .   ? -9.625  -25.769 8.146   1.00 26.22 ? 468 HOH A O   1 
HETATM 2440 O  O   . HOH G 6 .   ? -17.396 11.118  -1.939  1.00 24.22 ? 469 HOH A O   1 
HETATM 2441 O  O   . HOH G 6 .   ? -26.577 2.797   20.873  1.00 26.08 ? 470 HOH A O   1 
HETATM 2442 O  O   . HOH G 6 .   ? -4.479  -4.917  11.127  1.00 24.03 ? 471 HOH A O   1 
HETATM 2443 O  O   . HOH G 6 .   ? -4.754  -16.039 0.709   1.00 22.59 ? 472 HOH A O   1 
HETATM 2444 O  O   . HOH G 6 .   ? -21.382 -20.637 14.732  1.00 26.76 ? 473 HOH A O   1 
HETATM 2445 O  O   . HOH G 6 .   ? -17.642 -8.652  -6.300  1.00 23.66 ? 474 HOH A O   1 
HETATM 2446 O  O   . HOH G 6 .   ? -5.100  2.267   37.408  1.00 23.85 ? 475 HOH A O   1 
HETATM 2447 O  O   . HOH G 6 .   ? -25.797 -10.754 17.741  1.00 20.24 ? 476 HOH A O   1 
HETATM 2448 O  O   . HOH G 6 .   ? -17.747 -19.558 35.390  1.00 23.15 ? 477 HOH A O   1 
HETATM 2449 O  O   . HOH G 6 .   ? -16.614 -15.314 33.087  1.00 28.84 ? 478 HOH A O   1 
HETATM 2450 O  O   . HOH G 6 .   ? -32.892 1.986   11.972  1.00 25.96 ? 479 HOH A O   1 
HETATM 2451 O  O   . HOH G 6 .   ? -26.952 -1.292  26.013  1.00 21.61 ? 480 HOH A O   1 
HETATM 2452 O  O   . HOH G 6 .   ? -4.975  -20.796 21.604  1.00 20.19 ? 481 HOH A O   1 
HETATM 2453 O  O   . HOH G 6 .   ? 6.438   -5.527  3.683   1.00 29.27 ? 482 HOH A O   1 
HETATM 2454 O  O   . HOH G 6 .   ? 2.856   -13.551 8.191   1.00 25.12 ? 483 HOH A O   1 
HETATM 2455 O  O   . HOH G 6 .   ? -29.257 -4.112  13.490  1.00 29.14 ? 484 HOH A O   1 
HETATM 2456 O  O   . HOH G 6 .   ? -15.139 11.518  35.242  1.00 35.67 ? 485 HOH A O   1 
HETATM 2457 O  O   . HOH G 6 .   ? -7.772  -4.888  40.104  1.00 27.70 ? 486 HOH A O   1 
HETATM 2458 O  O   . HOH G 6 .   ? -6.058  -23.714 27.755  1.00 26.88 ? 487 HOH A O   1 
HETATM 2459 O  O   . HOH G 6 .   ? -26.487 -7.653  30.415  1.00 28.24 ? 488 HOH A O   1 
HETATM 2460 O  O   . HOH G 6 .   ? -6.100  -26.093 11.950  1.00 25.88 ? 489 HOH A O   1 
HETATM 2461 O  O   . HOH G 6 .   ? -13.307 -22.530 11.815  1.00 30.97 ? 490 HOH A O   1 
HETATM 2462 O  O   . HOH G 6 .   ? 1.484   -17.577 6.968   1.00 29.35 ? 491 HOH A O   1 
HETATM 2463 O  O   . HOH G 6 .   ? 6.679   -0.449  -1.383  1.00 35.77 ? 492 HOH A O   1 
HETATM 2464 O  O   . HOH G 6 .   ? -0.483  14.006  16.179  1.00 25.81 ? 493 HOH A O   1 
HETATM 2465 O  O   . HOH G 6 .   ? -27.698 2.770   23.824  1.00 26.31 ? 494 HOH A O   1 
HETATM 2466 O  O   . HOH G 6 .   ? -10.473 -27.826 8.824   1.00 22.91 ? 495 HOH A O   1 
HETATM 2467 O  O   . HOH G 6 .   ? -4.826  -12.814 40.996  1.00 24.33 ? 496 HOH A O   1 
HETATM 2468 O  O   . HOH G 6 .   ? -7.466  -8.839  -2.461  1.00 27.17 ? 497 HOH A O   1 
HETATM 2469 O  O   . HOH G 6 .   ? -4.672  -7.297  38.084  1.00 28.87 ? 498 HOH A O   1 
HETATM 2470 O  O   . HOH G 6 .   ? -3.976  0.092   13.383  1.00 21.68 ? 499 HOH A O   1 
HETATM 2471 O  O   . HOH G 6 .   ? -3.492  -23.134 21.547  1.00 23.29 ? 500 HOH A O   1 
HETATM 2472 O  O   . HOH G 6 .   ? -8.234  7.347   8.268   1.00 27.98 ? 501 HOH A O   1 
HETATM 2473 O  O   . HOH G 6 .   ? -25.256 8.708   26.043  1.00 28.36 ? 502 HOH A O   1 
HETATM 2474 O  O   . HOH G 6 .   ? -10.676 -32.706 7.774   1.00 20.71 ? 503 HOH A O   1 
HETATM 2475 O  O   . HOH G 6 .   ? -17.791 -12.163 31.709  1.00 26.52 ? 504 HOH A O   1 
HETATM 2476 O  O   . HOH G 6 .   ? -25.743 -15.396 7.954   1.00 29.08 ? 505 HOH A O   1 
HETATM 2477 O  O   . HOH G 6 .   ? -14.324 0.276   42.911  1.00 37.58 ? 506 HOH A O   1 
HETATM 2478 O  O   . HOH G 6 .   ? -25.780 -9.765  14.967  1.00 30.63 ? 507 HOH A O   1 
HETATM 2479 O  O   . HOH G 6 .   ? -1.213  -6.139  36.583  1.00 23.12 ? 508 HOH A O   1 
HETATM 2480 O  O   . HOH G 6 .   ? -24.232 -7.098  0.280   1.00 26.20 ? 509 HOH A O   1 
HETATM 2481 O  O   . HOH G 6 .   ? -1.247  -17.563 -1.901  1.00 28.12 ? 510 HOH A O   1 
HETATM 2482 O  O   . HOH G 6 .   ? -15.263 -20.154 23.276  1.00 25.96 ? 511 HOH A O   1 
HETATM 2483 O  O   . HOH G 6 .   ? 10.176  -8.418  7.848   1.00 26.78 ? 512 HOH A O   1 
HETATM 2484 O  O   . HOH G 6 .   ? -35.928 5.319   28.930  1.00 30.47 ? 513 HOH A O   1 
HETATM 2485 O  O   . HOH G 6 .   ? -36.553 0.787   8.395   1.00 24.06 ? 514 HOH A O   1 
HETATM 2486 O  O   . HOH G 6 .   ? -1.596  -17.492 4.981   1.00 30.55 ? 515 HOH A O   1 
HETATM 2487 O  O   . HOH G 6 .   ? -23.486 -11.162 17.264  1.00 25.58 ? 516 HOH A O   1 
HETATM 2488 O  O   . HOH G 6 .   ? -12.689 6.541   31.431  1.00 29.95 ? 517 HOH A O   1 
HETATM 2489 O  O   . HOH G 6 .   ? 3.405   -13.738 12.335  1.00 29.56 ? 518 HOH A O   1 
HETATM 2490 O  O   . HOH G 6 .   ? 6.152   -11.134 15.541  1.00 29.06 ? 519 HOH A O   1 
HETATM 2491 O  O   . HOH G 6 .   ? -12.945 -9.072  -3.182  1.00 28.50 ? 520 HOH A O   1 
HETATM 2492 O  O   . HOH G 6 .   ? -2.779  6.019   -1.103  1.00 26.70 ? 521 HOH A O   1 
HETATM 2493 O  O   . HOH G 6 .   ? -16.043 3.623   35.441  1.00 31.71 ? 522 HOH A O   1 
HETATM 2494 O  O   . HOH G 6 .   ? -30.464 0.782   28.536  1.00 38.94 ? 523 HOH A O   1 
HETATM 2495 O  O   . HOH G 6 .   ? 4.807   -3.478  2.970   1.00 27.35 ? 524 HOH A O   1 
HETATM 2496 O  O   . HOH G 6 .   ? -11.712 -0.361  43.667  1.00 24.87 ? 525 HOH A O   1 
HETATM 2497 O  O   . HOH G 6 .   ? 1.754   -9.853  31.260  1.00 29.45 ? 526 HOH A O   1 
HETATM 2498 O  O   . HOH G 6 .   ? -11.523 1.054   -7.727  1.00 30.29 ? 527 HOH A O   1 
HETATM 2499 O  O   . HOH G 6 .   ? -23.035 -14.854 16.222  1.00 31.60 ? 528 HOH A O   1 
HETATM 2500 O  O   . HOH G 6 .   ? -2.527  -18.077 31.249  1.00 27.45 ? 529 HOH A O   1 
HETATM 2501 O  O   . HOH G 6 .   ? -2.831  -11.348 38.300  1.00 33.30 ? 530 HOH A O   1 
HETATM 2502 O  O   . HOH G 6 .   ? -16.593 7.449   36.696  1.00 23.44 ? 531 HOH A O   1 
HETATM 2503 O  O   . HOH G 6 .   ? -20.851 8.182   30.227  1.00 22.98 ? 532 HOH A O   1 
HETATM 2504 O  O   . HOH G 6 .   ? 11.225  -3.187  -12.314 1.00 22.57 ? 533 HOH A O   1 
HETATM 2505 O  O   . HOH G 6 .   ? -22.023 -14.166 18.592  1.00 26.40 ? 534 HOH A O   1 
HETATM 2506 O  O   . HOH G 6 .   ? -21.371 13.839  2.138   1.00 29.15 ? 535 HOH A O   1 
HETATM 2507 O  O   . HOH G 6 .   ? 5.480   9.123   22.000  1.00 25.65 ? 536 HOH A O   1 
HETATM 2508 O  O   . HOH G 6 .   ? -39.289 2.878   8.383   1.00 33.76 ? 537 HOH A O   1 
HETATM 2509 O  O   . HOH G 6 .   ? 2.185   8.098   28.054  1.00 32.17 ? 538 HOH A O   1 
HETATM 2510 O  O   . HOH G 6 .   ? -8.953  6.575   -3.941  1.00 28.56 ? 539 HOH A O   1 
HETATM 2511 O  O   . HOH G 6 .   ? -25.411 10.979  19.579  1.00 29.05 ? 540 HOH A O   1 
HETATM 2512 O  O   . HOH G 6 .   ? -12.853 10.916  36.314  1.00 28.96 ? 541 HOH A O   1 
HETATM 2513 O  O   . HOH G 6 .   ? -17.985 -20.714 -1.297  1.00 29.36 ? 542 HOH A O   1 
HETATM 2514 O  O   . HOH G 6 .   ? -24.128 -2.775  29.341  1.00 28.88 ? 543 HOH A O   1 
HETATM 2515 O  O   . HOH G 6 .   ? -2.557  -19.245 21.687  1.00 25.71 ? 544 HOH A O   1 
HETATM 2516 O  O   . HOH G 6 .   ? -17.505 -16.249 22.167  1.00 19.57 ? 545 HOH A O   1 
HETATM 2517 O  O   . HOH G 6 .   ? -5.521  1.791   11.383  1.00 22.66 ? 546 HOH A O   1 
HETATM 2518 O  O   . HOH G 6 .   ? -28.256 -1.390  28.429  1.00 29.39 ? 547 HOH A O   1 
HETATM 2519 O  O   . HOH G 6 .   ? -26.007 8.022   6.194   1.00 27.55 ? 548 HOH A O   1 
HETATM 2520 O  O   . HOH G 6 .   ? -12.168 -30.714 5.949   1.00 32.89 ? 549 HOH A O   1 
HETATM 2521 O  O   . HOH G 6 .   ? -30.658 -0.465  16.087  1.00 31.07 ? 550 HOH A O   1 
HETATM 2522 O  O   . HOH G 6 .   ? 11.946  -6.608  7.918   1.00 26.72 ? 551 HOH A O   1 
HETATM 2523 O  O   . HOH G 6 .   ? -17.305 -6.845  42.633  1.00 28.49 ? 552 HOH A O   1 
HETATM 2524 O  O   . HOH G 6 .   ? 5.779   -14.070 9.018   1.00 34.79 ? 553 HOH A O   1 
HETATM 2525 O  O   . HOH G 6 .   ? -28.211 4.984   25.477  1.00 28.65 ? 554 HOH A O   1 
HETATM 2526 O  O   . HOH G 6 .   ? -30.123 4.217   27.545  1.00 27.57 ? 555 HOH A O   1 
HETATM 2527 O  O   . HOH G 6 .   ? 0.266   0.007   -14.820 1.00 30.49 ? 556 HOH A O   1 
HETATM 2528 O  O   . HOH G 6 .   ? 2.917   1.074   -6.438  1.00 32.02 ? 557 HOH A O   1 
HETATM 2529 O  O   . HOH G 6 .   ? -19.729 -4.250  41.676  1.00 30.08 ? 558 HOH A O   1 
HETATM 2530 O  O   . HOH G 6 .   ? 4.251   -11.604 23.635  1.00 34.36 ? 559 HOH A O   1 
HETATM 2531 O  O   . HOH G 6 .   ? -18.850 -9.070  34.547  1.00 27.51 ? 560 HOH A O   1 
HETATM 2532 O  O   . HOH G 6 .   ? -28.318 5.763   19.197  1.00 28.89 ? 561 HOH A O   1 
HETATM 2533 O  O   . HOH G 6 .   ? -2.613  -15.000 33.054  1.00 33.30 ? 562 HOH A O   1 
HETATM 2534 O  O   . HOH G 6 .   ? -25.496 9.672   13.128  1.00 28.07 ? 563 HOH A O   1 
HETATM 2535 O  O   . HOH G 6 .   ? -22.883 -9.631  25.454  1.00 21.26 ? 564 HOH A O   1 
HETATM 2536 O  O   . HOH G 6 .   ? 5.208   -7.225  22.355  1.00 25.67 ? 565 HOH A O   1 
HETATM 2537 O  O   . HOH G 6 .   ? 14.762  -7.038  7.593   1.00 33.80 ? 566 HOH A O   1 
HETATM 2538 O  O   . HOH G 6 .   ? -5.414  -12.546 -5.269  1.00 35.67 ? 567 HOH A O   1 
HETATM 2539 O  O   . HOH G 6 .   ? -23.944 -17.929 6.332   1.00 31.48 ? 568 HOH A O   1 
HETATM 2540 O  O   . HOH G 6 .   ? -24.884 4.652   8.300   1.00 32.47 ? 569 HOH A O   1 
HETATM 2541 O  O   . HOH G 6 .   ? -20.638 13.922  29.059  1.00 32.80 ? 570 HOH A O   1 
HETATM 2542 O  O   . HOH G 6 .   ? -11.191 -11.273 -3.018  1.00 33.67 ? 571 HOH A O   1 
HETATM 2543 O  O   . HOH G 6 .   ? -12.787 11.072  -5.208  1.00 32.49 ? 572 HOH A O   1 
HETATM 2544 O  O   . HOH G 6 .   ? -17.289 -7.385  39.974  1.00 28.46 ? 573 HOH A O   1 
HETATM 2545 O  O   . HOH G 6 .   ? -15.312 8.300   35.108  1.00 31.31 ? 574 HOH A O   1 
HETATM 2546 O  O   . HOH G 6 .   ? -27.554 0.113   15.110  1.00 28.16 ? 575 HOH A O   1 
HETATM 2547 O  O   . HOH G 6 .   ? 3.075   -9.973  29.472  1.00 33.11 ? 576 HOH A O   1 
HETATM 2548 O  O   . HOH G 6 .   ? -17.219 0.134   -3.914  1.00 38.38 ? 577 HOH A O   1 
HETATM 2549 O  O   . HOH G 6 .   ? -16.475 16.603  26.751  1.00 28.20 ? 578 HOH A O   1 
HETATM 2550 O  O   . HOH G 6 .   ? 0.599   -9.541  -5.532  1.00 29.34 ? 579 HOH A O   1 
HETATM 2551 O  O   . HOH G 6 .   ? -0.215  0.984   -10.864 1.00 29.67 ? 580 HOH A O   1 
HETATM 2552 O  O   . HOH G 6 .   ? -1.778  -15.734 -4.359  1.00 36.94 ? 581 HOH A O   1 
HETATM 2553 O  O   . HOH G 6 .   ? -0.780  6.745   32.171  1.00 31.04 ? 582 HOH A O   1 
HETATM 2554 O  O   . HOH G 6 .   ? -12.413 4.070   35.134  1.00 39.91 ? 583 HOH A O   1 
HETATM 2555 O  O   . HOH G 6 .   ? -17.110 -1.115  40.454  1.00 33.15 ? 584 HOH A O   1 
HETATM 2556 O  O   . HOH G 6 .   ? -19.629 -23.969 5.946   1.00 28.27 ? 585 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   ? 0.2518 0.3248 0.2734 0.0208  -0.0241 -0.0186 3   HIS A N   
2    C  CA  . HIS A 3   ? 0.2548 0.3508 0.3255 0.0153  -0.0276 0.0032  3   HIS A CA  
3    C  C   . HIS A 3   ? 0.2738 0.3634 0.3037 0.0121  -0.0197 0.0057  3   HIS A C   
4    O  O   . HIS A 3   ? 0.3355 0.4068 0.3367 0.0126  -0.0410 -0.0176 3   HIS A O   
5    C  CB  . HIS A 3   ? 0.2675 0.3385 0.3011 0.0017  -0.0438 0.0120  3   HIS A CB  
6    C  CG  . HIS A 3   ? 0.2984 0.3467 0.3565 -0.0120 -0.0375 0.0023  3   HIS A CG  
7    N  ND1 . HIS A 3   ? 0.3162 0.3350 0.3700 0.0156  -0.0522 -0.0103 3   HIS A ND1 
8    C  CD2 . HIS A 3   ? 0.3048 0.3309 0.3417 -0.0293 -0.0281 0.0153  3   HIS A CD2 
9    C  CE1 . HIS A 3   ? 0.3391 0.3558 0.3690 -0.0250 0.0222  -0.0175 3   HIS A CE1 
10   N  NE2 . HIS A 3   ? 0.2728 0.3371 0.3375 -0.0935 -0.0252 -0.0245 3   HIS A NE2 
11   N  N   . HIS A 4   ? 0.1970 0.3472 0.3152 0.0046  0.0083  0.0187  4   HIS A N   
12   C  CA  . HIS A 4   ? 0.2024 0.2876 0.2993 -0.0203 0.0548  0.0417  4   HIS A CA  
13   C  C   . HIS A 4   ? 0.1665 0.2456 0.2578 -0.0318 0.0608  0.0264  4   HIS A C   
14   O  O   . HIS A 4   ? 0.1835 0.2761 0.2908 -0.0295 0.0932  0.0217  4   HIS A O   
15   C  CB  . HIS A 4   ? 0.2398 0.3361 0.3030 -0.0156 0.0339  0.0441  4   HIS A CB  
16   C  CG  . HIS A 4   ? 0.3201 0.3614 0.3479 -0.0027 0.0207  0.0200  4   HIS A CG  
17   N  ND1 . HIS A 4   ? 0.3192 0.3403 0.3320 -0.0015 0.0076  0.0077  4   HIS A ND1 
18   C  CD2 . HIS A 4   ? 0.3230 0.3442 0.3339 0.0003  0.0076  0.0082  4   HIS A CD2 
19   C  CE1 . HIS A 4   ? 0.3266 0.3395 0.3353 -0.0003 0.0041  0.0046  4   HIS A CE1 
20   N  NE2 . HIS A 4   ? 0.3260 0.3393 0.3346 0.0000  0.0043  0.0043  4   HIS A NE2 
21   N  N   . TRP A 5   ? 0.1391 0.2451 0.2773 -0.0243 0.0564  0.0037  5   TRP A N   
22   C  CA  . TRP A 5   ? 0.1303 0.1852 0.2361 -0.0282 0.0628  -0.0140 5   TRP A CA  
23   C  C   . TRP A 5   ? 0.1278 0.1645 0.2237 -0.0062 0.0648  -0.0133 5   TRP A C   
24   O  O   . TRP A 5   ? 0.1622 0.1492 0.2560 -0.0318 0.0665  -0.0077 5   TRP A O   
25   C  CB  . TRP A 5   ? 0.1174 0.1661 0.2298 -0.0193 0.0685  -0.0098 5   TRP A CB  
26   C  CG  . TRP A 5   ? 0.1314 0.1711 0.2363 -0.0186 0.0659  -0.0159 5   TRP A CG  
27   C  CD1 . TRP A 5   ? 0.1447 0.1686 0.1690 0.0082  0.0313  0.0421  5   TRP A CD1 
28   C  CD2 . TRP A 5   ? 0.0831 0.1740 0.2219 -0.0159 -0.0159 -0.0105 5   TRP A CD2 
29   N  NE1 . TRP A 5   ? 0.1515 0.1612 0.1722 0.0041  0.0225  0.0187  5   TRP A NE1 
30   C  CE2 . TRP A 5   ? 0.1111 0.1712 0.1317 -0.0177 0.0386  0.0070  5   TRP A CE2 
31   C  CE3 . TRP A 5   ? 0.1183 0.1844 0.1551 -0.0120 0.0302  -0.0529 5   TRP A CE3 
32   C  CZ2 . TRP A 5   ? 0.1515 0.1632 0.1510 -0.0068 0.0171  0.0003  5   TRP A CZ2 
33   C  CZ3 . TRP A 5   ? 0.1403 0.1670 0.1465 0.0060  0.0197  -0.0317 5   TRP A CZ3 
34   C  CH2 . TRP A 5   ? 0.1074 0.1630 0.1490 -0.0008 0.0221  -0.0373 5   TRP A CH2 
35   N  N   . GLY A 6   ? 0.1360 0.1302 0.2143 -0.0055 0.0544  -0.0160 6   GLY A N   
36   C  CA  . GLY A 6   ? 0.1582 0.0987 0.2046 -0.0146 0.0575  -0.0209 6   GLY A CA  
37   C  C   . GLY A 6   ? 0.1328 0.1356 0.1914 -0.0152 0.0646  -0.0199 6   GLY A C   
38   O  O   . GLY A 6   ? 0.1453 0.1363 0.1924 -0.0023 0.0653  -0.0113 6   GLY A O   
39   N  N   A TYR A 7   ? 0.1547 0.1009 0.1939 -0.0024 0.0575  -0.0252 7   TYR A N   
40   N  N   B TYR A 7   ? 0.1823 0.1442 0.2218 -0.0116 0.0557  -0.0223 7   TYR A N   
41   C  CA  A TYR A 7   ? 0.1339 0.1314 0.2356 0.0035  0.0384  -0.0131 7   TYR A CA  
42   C  CA  B TYR A 7   ? 0.1852 0.1603 0.2311 0.0017  0.0342  -0.0131 7   TYR A CA  
43   C  C   A TYR A 7   ? 0.1535 0.1540 0.2713 0.0015  0.0395  -0.0291 7   TYR A C   
44   C  C   B TYR A 7   ? 0.1982 0.1784 0.2587 -0.0006 0.0353  -0.0241 7   TYR A C   
45   O  O   A TYR A 7   ? 0.1104 0.1323 0.2714 -0.0006 0.0273  -0.0351 7   TYR A O   
46   O  O   B TYR A 7   ? 0.1465 0.1453 0.2804 -0.0020 0.0184  -0.0432 7   TYR A O   
47   C  CB  A TYR A 7   ? 0.1224 0.0892 0.1688 0.0057  0.0498  -0.0131 7   TYR A CB  
48   C  CB  B TYR A 7   ? 0.1856 0.1676 0.2047 0.0043  0.0439  -0.0108 7   TYR A CB  
49   C  CG  A TYR A 7   ? 0.1122 0.0718 0.1325 0.0076  0.0121  -0.0074 7   TYR A CG  
50   C  CG  B TYR A 7   ? 0.1676 0.1118 0.1418 -0.0076 0.0183  -0.0161 7   TYR A CG  
51   C  CD1 A TYR A 7   ? 0.1070 0.1342 0.1431 -0.0146 0.0227  -0.0210 7   TYR A CD1 
52   C  CD1 B TYR A 7   ? 0.1244 0.1424 0.0619 -0.0322 0.0133  -0.0242 7   TYR A CD1 
53   C  CD2 A TYR A 7   ? 0.0815 0.0461 0.1370 -0.0046 0.0082  -0.0003 7   TYR A CD2 
54   C  CD2 B TYR A 7   ? 0.1515 0.1133 0.1110 -0.0272 0.0289  -0.0027 7   TYR A CD2 
55   C  CE1 A TYR A 7   ? 0.0867 0.0784 0.0930 0.0015  0.0100  0.0386  7   TYR A CE1 
56   C  CE1 B TYR A 7   ? 0.0707 0.1310 0.1734 -0.0375 -0.0074 0.0020  7   TYR A CE1 
57   C  CE2 A TYR A 7   ? 0.1291 0.0723 0.0509 -0.0210 0.0478  -0.0221 7   TYR A CE2 
58   C  CE2 B TYR A 7   ? 0.1165 0.1174 0.1054 -0.0196 0.0057  0.0189  7   TYR A CE2 
59   C  CZ  A TYR A 7   ? 0.1102 0.0488 0.0613 0.0109  0.0439  0.0060  7   TYR A CZ  
60   C  CZ  B TYR A 7   ? 0.1453 0.1228 0.1226 -0.0315 0.0262  -0.0153 7   TYR A CZ  
61   O  OH  A TYR A 7   ? 0.0885 0.0917 0.1001 0.0003  0.0313  -0.0208 7   TYR A OH  
62   O  OH  B TYR A 7   ? 0.0996 0.1257 0.1330 -0.0273 0.0192  0.0008  7   TYR A OH  
63   N  N   A GLY A 8   ? 0.1192 0.1526 0.2818 0.0165  0.0342  -0.0388 8   GLY A N   
64   N  N   B GLY A 8   ? 0.1765 0.1673 0.2343 0.0135  0.0359  -0.0381 8   GLY A N   
65   C  CA  A GLY A 8   ? 0.1079 0.1526 0.2530 0.0082  0.0425  -0.0252 8   GLY A CA  
66   C  CA  B GLY A 8   ? 0.1834 0.1737 0.2331 0.0038  0.0311  -0.0270 8   GLY A CA  
67   C  C   A GLY A 8   ? 0.1456 0.1709 0.2524 -0.0074 0.0353  -0.0218 8   GLY A C   
68   C  C   B GLY A 8   ? 0.2011 0.2025 0.2417 -0.0020 0.0335  -0.0136 8   GLY A C   
69   O  O   A GLY A 8   ? 0.0957 0.1438 0.2778 -0.0219 0.1076  -0.0671 8   GLY A O   
70   O  O   B GLY A 8   ? 0.1931 0.2269 0.2158 0.0190  0.0322  -0.0076 8   GLY A O   
71   N  N   A LYS A 9   ? 0.1421 0.2058 0.2709 -0.0077 0.0460  -0.0196 9   LYS A N   
72   N  N   B LYS A 9   ? 0.1982 0.1977 0.2563 0.0003  0.0286  -0.0138 9   LYS A N   
73   C  CA  A LYS A 9   ? 0.1985 0.2090 0.2734 -0.0006 0.0198  -0.0164 9   LYS A CA  
74   C  CA  B LYS A 9   ? 0.2307 0.2584 0.2904 0.0059  0.0263  -0.0037 9   LYS A CA  
75   C  C   A LYS A 9   ? 0.1730 0.2423 0.2684 -0.0017 0.0351  -0.0028 9   LYS A C   
76   C  C   B LYS A 9   ? 0.2032 0.2833 0.3005 0.0005  0.0174  -0.0078 9   LYS A C   
77   O  O   A LYS A 9   ? 0.1393 0.2395 0.2581 -0.0280 0.0467  -0.0221 9   LYS A O   
78   O  O   B LYS A 9   ? 0.2408 0.3163 0.3327 -0.0155 0.0127  0.0109  9   LYS A O   
79   C  CB  A LYS A 9   ? 0.1754 0.2441 0.2485 -0.0001 0.0173  -0.0020 9   LYS A CB  
80   C  CB  B LYS A 9   ? 0.2261 0.2584 0.3005 -0.0049 0.0129  -0.0197 9   LYS A CB  
81   C  CG  A LYS A 9   ? 0.2164 0.2007 0.2908 0.0309  0.0197  0.0052  9   LYS A CG  
82   C  CG  B LYS A 9   ? 0.2724 0.3102 0.2854 0.0027  0.0046  -0.0060 9   LYS A CG  
83   C  CD  A LYS A 9   ? 0.2470 0.2092 0.2667 0.0028  0.0401  -0.0170 9   LYS A CD  
84   C  CD  B LYS A 9   ? 0.2820 0.3517 0.2912 -0.0133 0.0209  -0.0097 9   LYS A CD  
85   C  CE  A LYS A 9   ? 0.2736 0.2770 0.2727 -0.0051 0.0015  0.0027  9   LYS A CE  
86   C  CE  B LYS A 9   ? 0.3447 0.3743 0.3407 0.0124  0.0038  0.0147  9   LYS A CE  
87   N  NZ  A LYS A 9   ? 0.2597 0.2524 0.2657 0.0076  0.0040  -0.0051 9   LYS A NZ  
88   N  NZ  B LYS A 9   ? 0.3398 0.4192 0.3849 0.0190  0.0264  0.0040  9   LYS A NZ  
89   N  N   A HIS A 10  ? 0.1982 0.2377 0.3127 0.0237  0.0680  -0.0197 10  HIS A N   
90   N  N   B HIS A 10  ? 0.2304 0.2761 0.3188 0.0237  0.0395  -0.0098 10  HIS A N   
91   C  CA  A HIS A 10  ? 0.1880 0.2363 0.2940 0.0359  0.0838  -0.0030 10  HIS A CA  
92   C  CA  B HIS A 10  ? 0.1967 0.2652 0.2878 0.0263  0.0476  -0.0032 10  HIS A CA  
93   C  C   A HIS A 10  ? 0.1668 0.2244 0.2843 0.0346  0.0741  -0.0038 10  HIS A C   
94   C  C   B HIS A 10  ? 0.1693 0.2491 0.2854 0.0335  0.0627  -0.0019 10  HIS A C   
95   O  O   A HIS A 10  ? 0.1643 0.2355 0.2937 0.0472  0.0918  -0.0086 10  HIS A O   
96   O  O   B HIS A 10  ? 0.1548 0.2624 0.2929 0.0403  0.0859  -0.0063 10  HIS A O   
97   C  CB  A HIS A 10  ? 0.1460 0.2150 0.2721 0.0315  0.1037  -0.0038 10  HIS A CB  
98   C  CB  B HIS A 10  ? 0.1641 0.2559 0.2577 0.0227  0.0373  -0.0068 10  HIS A CB  
99   C  CG  A HIS A 10  ? 0.2185 0.2570 0.2620 0.0100  0.0520  -0.0091 10  HIS A CG  
100  C  CG  B HIS A 10  ? 0.1957 0.2797 0.2395 0.0001  -0.0062 -0.0266 10  HIS A CG  
101  N  ND1 A HIS A 10  ? 0.2333 0.3230 0.2791 0.0043  0.0922  0.0124  10  HIS A ND1 
102  N  ND1 B HIS A 10  ? 0.1183 0.2533 0.2021 0.0278  0.0264  0.0212  10  HIS A ND1 
103  C  CD2 A HIS A 10  ? 0.1716 0.2452 0.2688 0.0357  0.0502  -0.0103 10  HIS A CD2 
104  C  CD2 B HIS A 10  ? 0.1738 0.2542 0.1912 0.0148  0.0141  -0.0390 10  HIS A CD2 
105  C  CE1 A HIS A 10  ? 0.1332 0.2387 0.2057 -0.0041 0.0225  -0.0083 10  HIS A CE1 
106  C  CE1 B HIS A 10  ? 0.1425 0.2613 0.1406 -0.0263 -0.0281 -0.0293 10  HIS A CE1 
107  N  NE2 A HIS A 10  ? 0.2124 0.2833 0.2714 0.0116  0.0234  -0.0085 10  HIS A NE2 
108  N  NE2 B HIS A 10  ? 0.1694 0.2721 0.1266 -0.0140 -0.0355 -0.0410 10  HIS A NE2 
109  N  N   . ASN A 11  ? 0.1510 0.2229 0.2745 0.0326  0.0948  0.0051  11  ASN A N   
110  C  CA  . ASN A 11  ? 0.1504 0.1973 0.2628 0.0227  0.0939  -0.0188 11  ASN A CA  
111  C  C   . ASN A 11  ? 0.1138 0.1783 0.2542 0.0172  0.0816  -0.0031 11  ASN A C   
112  O  O   . ASN A 11  ? 0.1506 0.1640 0.2782 0.0272  0.0936  0.0154  11  ASN A O   
113  C  CB  . ASN A 11  ? 0.1374 0.1810 0.2773 0.0174  0.0745  -0.0115 11  ASN A CB  
114  C  CG  . ASN A 11  ? 0.1853 0.1747 0.2930 0.0328  0.0860  -0.0443 11  ASN A CG  
115  O  OD1 . ASN A 11  ? 0.1747 0.1996 0.3503 -0.0295 0.0869  -0.0265 11  ASN A OD1 
116  N  ND2 . ASN A 11  ? 0.2113 0.1583 0.3130 -0.0089 0.0375  -0.0200 11  ASN A ND2 
117  N  N   . GLY A 12  ? 0.1447 0.1812 0.2243 -0.0063 0.0768  -0.0070 12  GLY A N   
118  C  CA  . GLY A 12  ? 0.0813 0.1792 0.1977 0.0013  0.0590  -0.0242 12  GLY A CA  
119  C  C   . GLY A 12  ? 0.1004 0.1465 0.2143 -0.0065 0.0573  -0.0151 12  GLY A C   
120  O  O   . GLY A 12  ? 0.1025 0.1501 0.2180 0.0068  0.0496  0.0148  12  GLY A O   
121  N  N   . PRO A 13  ? 0.0788 0.1575 0.1655 -0.0087 0.0584  -0.0225 13  PRO A N   
122  C  CA  . PRO A 13  ? 0.0803 0.1436 0.1979 0.0038  0.0549  -0.0307 13  PRO A CA  
123  C  C   . PRO A 13  ? 0.1025 0.1345 0.1928 0.0124  0.0355  0.0043  13  PRO A C   
124  O  O   . PRO A 13  ? 0.1001 0.1579 0.2042 0.0094  0.0357  -0.0063 13  PRO A O   
125  C  CB  . PRO A 13  ? 0.0822 0.1766 0.2014 -0.0521 0.0859  -0.0099 13  PRO A CB  
126  C  CG  . PRO A 13  ? 0.1270 0.1752 0.1995 0.0005  0.0684  -0.0346 13  PRO A CG  
127  C  CD  . PRO A 13  ? 0.1059 0.1701 0.1888 0.0003  0.0381  -0.0294 13  PRO A CD  
128  N  N   A GLU A 14  ? 0.0987 0.1177 0.1959 0.0096  0.0219  0.0041  14  GLU A N   
129  N  N   B GLU A 14  ? 0.1160 0.1198 0.2330 0.0105  0.0340  0.0111  14  GLU A N   
130  C  CA  A GLU A 14  ? 0.1185 0.1267 0.1961 0.0153  0.0000  0.0038  14  GLU A CA  
131  C  CA  B GLU A 14  ? 0.1517 0.1277 0.2463 0.0153  0.0186  0.0127  14  GLU A CA  
132  C  C   A GLU A 14  ? 0.0939 0.1171 0.1993 0.0337  0.0219  -0.0019 14  GLU A C   
133  C  C   B GLU A 14  ? 0.1124 0.1374 0.2289 0.0329  0.0270  0.0027  14  GLU A C   
134  O  O   A GLU A 14  ? 0.1111 0.1165 0.2268 0.0252  0.0221  0.0219  14  GLU A O   
135  O  O   B GLU A 14  ? 0.1318 0.1291 0.2694 0.0386  0.0154  0.0170  14  GLU A O   
136  C  CB  A GLU A 14  ? 0.1471 0.1525 0.1863 0.0171  -0.0306 -0.0024 14  GLU A CB  
137  C  CB  B GLU A 14  ? 0.1925 0.1604 0.2563 0.0179  0.0186  0.0027  14  GLU A CB  
138  C  CG  A GLU A 14  ? 0.1280 0.1639 0.1835 0.0066  -0.0147 -0.0071 14  GLU A CG  
139  C  CG  B GLU A 14  ? 0.2172 0.2018 0.2861 -0.0041 0.0175  0.0087  14  GLU A CG  
140  C  CD  A GLU A 14  ? 0.1712 0.1831 0.2072 0.0000  0.0089  -0.0135 14  GLU A CD  
141  C  CD  B GLU A 14  ? 0.3064 0.3288 0.2871 0.0015  0.0054  -0.0113 14  GLU A CD  
142  O  OE1 A GLU A 14  ? 0.1178 0.1046 0.1715 0.0344  -0.0553 -0.0557 14  GLU A OE1 
143  O  OE1 B GLU A 14  ? 0.3497 0.3756 0.3165 0.0038  -0.0102 -0.0289 14  GLU A OE1 
144  O  OE2 A GLU A 14  ? 0.3029 0.0910 0.2200 0.0000  0.0091  -0.0467 14  GLU A OE2 
145  O  OE2 B GLU A 14  ? 0.3188 0.3371 0.2966 0.0137  0.0344  -0.0010 14  GLU A OE2 
146  N  N   . HIS A 15  ? 0.1001 0.1271 0.2173 0.0207  0.0048  0.0012  15  HIS A N   
147  C  CA  . HIS A 15  ? 0.1106 0.1253 0.2157 0.0315  0.0342  -0.0089 15  HIS A CA  
148  C  C   . HIS A 15  ? 0.0942 0.1384 0.2036 0.0281  0.0113  -0.0136 15  HIS A C   
149  O  O   . HIS A 15  ? 0.0816 0.1404 0.2815 0.0313  0.0326  -0.0055 15  HIS A O   
150  C  CB  . HIS A 15  ? 0.0793 0.1458 0.2208 0.0305  0.0129  0.0162  15  HIS A CB  
151  C  CG  . HIS A 15  ? 0.1235 0.1622 0.1770 0.0359  0.0524  0.0043  15  HIS A CG  
152  N  ND1 . HIS A 15  ? 0.1370 0.2293 0.2642 0.0979  0.0120  0.0019  15  HIS A ND1 
153  C  CD2 . HIS A 15  ? 0.1137 0.2108 0.2937 0.0822  0.0452  -0.0019 15  HIS A CD2 
154  C  CE1 . HIS A 15  ? 0.2422 0.2775 0.2316 0.0712  0.0297  -0.0104 15  HIS A CE1 
155  N  NE2 . HIS A 15  ? 0.1955 0.1896 0.2739 0.0983  0.0460  -0.0040 15  HIS A NE2 
156  N  N   . TRP A 16  ? 0.0584 0.1410 0.1948 0.0436  0.0223  0.0070  16  TRP A N   
157  C  CA  . TRP A 16  ? 0.0597 0.1226 0.2032 0.0199  -0.0008 -0.0109 16  TRP A CA  
158  C  C   . TRP A 16  ? 0.0668 0.1483 0.2020 0.0088  0.0244  -0.0054 16  TRP A C   
159  O  O   . TRP A 16  ? 0.0900 0.1063 0.2534 0.0082  -0.0183 -0.0133 16  TRP A O   
160  C  CB  . TRP A 16  ? 0.0415 0.1511 0.1777 0.0043  0.0119  -0.0329 16  TRP A CB  
161  C  CG  . TRP A 16  ? 0.0644 0.1133 0.1993 -0.0059 0.0151  0.0052  16  TRP A CG  
162  C  CD1 . TRP A 16  ? 0.0943 0.0851 0.1482 0.0215  0.0219  0.0073  16  TRP A CD1 
163  C  CD2 . TRP A 16  ? 0.0463 0.0752 0.1869 0.0152  0.0214  -0.0164 16  TRP A CD2 
164  N  NE1 . TRP A 16  ? 0.1071 0.1145 0.1643 0.0024  0.0308  -0.0189 16  TRP A NE1 
165  C  CE2 . TRP A 16  ? 0.0675 0.1496 0.1770 -0.0230 0.0210  0.0137  16  TRP A CE2 
166  C  CE3 . TRP A 16  ? 0.0732 0.0833 0.1943 0.0008  0.0364  0.0198  16  TRP A CE3 
167  C  CZ2 . TRP A 16  ? 0.0946 0.0935 0.1766 0.0003  0.0087  0.0127  16  TRP A CZ2 
168  C  CZ3 . TRP A 16  ? 0.0472 0.1043 0.1540 -0.0007 0.0200  -0.0164 16  TRP A CZ3 
169  C  CH2 . TRP A 16  ? 0.0723 0.0949 0.1652 0.0044  0.0189  -0.0186 16  TRP A CH2 
170  N  N   . HIS A 17  ? 0.0476 0.1546 0.1966 0.0081  0.0173  0.0007  17  HIS A N   
171  C  CA  . HIS A 17  ? 0.0667 0.1694 0.2291 -0.0164 -0.0105 0.0015  17  HIS A CA  
172  C  C   . HIS A 17  ? 0.0840 0.1661 0.2442 -0.0199 0.0074  0.0041  17  HIS A C   
173  O  O   . HIS A 17  ? 0.0617 0.1661 0.2689 -0.0092 -0.0109 -0.0100 17  HIS A O   
174  C  CB  . HIS A 17  ? 0.0553 0.1805 0.2067 0.0166  0.0175  0.0105  17  HIS A CB  
175  C  CG  . HIS A 17  ? 0.0637 0.1705 0.2244 -0.0099 -0.0015 0.0034  17  HIS A CG  
176  N  ND1 . HIS A 17  ? 0.0788 0.1826 0.2994 -0.0085 -0.0241 0.0615  17  HIS A ND1 
177  C  CD2 . HIS A 17  ? 0.1327 0.1835 0.2484 0.0504  0.0439  0.0361  17  HIS A CD2 
178  C  CE1 . HIS A 17  ? 0.1464 0.2061 0.2648 0.0705  -0.0035 0.0250  17  HIS A CE1 
179  N  NE2 . HIS A 17  ? 0.1022 0.2146 0.2738 0.0419  0.0287  0.0619  17  HIS A NE2 
180  N  N   . LYS A 18  ? 0.0585 0.1724 0.2662 -0.0100 -0.0109 0.0247  18  LYS A N   
181  C  CA  . LYS A 18  ? 0.0779 0.1884 0.2659 0.0000  0.0135  0.0307  18  LYS A CA  
182  C  C   . LYS A 18  ? 0.0829 0.1766 0.2773 -0.0167 -0.0165 0.0227  18  LYS A C   
183  O  O   . LYS A 18  ? 0.1442 0.2183 0.3224 -0.0379 -0.0549 0.0606  18  LYS A O   
184  C  CB  . LYS A 18  ? 0.0776 0.2078 0.3080 0.0164  0.0010  0.0296  18  LYS A CB  
185  C  CG  . LYS A 18  ? 0.0984 0.1873 0.2552 0.0239  0.0103  0.0381  18  LYS A CG  
186  C  CD  . LYS A 18  ? 0.0797 0.2401 0.2602 0.0207  0.0204  0.0340  18  LYS A CD  
187  C  CE  . LYS A 18  ? 0.1307 0.1941 0.2896 0.0309  0.0237  0.0136  18  LYS A CE  
188  N  NZ  . LYS A 18  ? 0.0829 0.2076 0.2272 0.0401  -0.0087 0.0478  18  LYS A NZ  
189  N  N   . ASP A 19  ? 0.0939 0.1855 0.2352 0.0076  -0.0091 0.0328  19  ASP A N   
190  C  CA  . ASP A 19  ? 0.0998 0.2009 0.2656 -0.0118 0.0176  0.0221  19  ASP A CA  
191  C  C   . ASP A 19  ? 0.1125 0.1923 0.2754 -0.0093 0.0120  0.0174  19  ASP A C   
192  O  O   . ASP A 19  ? 0.1593 0.1662 0.3046 -0.0083 0.0469  0.0421  19  ASP A O   
193  C  CB  . ASP A 19  ? 0.1381 0.2797 0.2580 0.0401  0.0054  0.0313  19  ASP A CB  
194  C  CG  . ASP A 19  ? 0.1747 0.3368 0.2847 -0.0107 0.0218  -0.0175 19  ASP A CG  
195  O  OD1 . ASP A 19  ? 0.2348 0.3536 0.3483 -0.0465 0.0443  0.0098  19  ASP A OD1 
196  O  OD2 . ASP A 19  ? 0.3767 0.4743 0.4180 0.0060  0.0110  -0.0524 19  ASP A OD2 
197  N  N   . PHE A 20  ? 0.0644 0.1521 0.2319 -0.0239 0.0118  0.0076  20  PHE A N   
198  C  CA  . PHE A 20  ? 0.0831 0.1386 0.2225 -0.0252 -0.0003 -0.0142 20  PHE A CA  
199  C  C   . PHE A 20  ? 0.0659 0.1306 0.2218 -0.0292 -0.0130 -0.0007 20  PHE A C   
200  O  O   . PHE A 20  ? 0.0650 0.1183 0.2257 -0.0233 0.0049  0.0115  20  PHE A O   
201  C  CB  . PHE A 20  ? 0.1075 0.1518 0.2251 -0.0331 -0.0140 -0.0082 20  PHE A CB  
202  C  CG  . PHE A 20  ? 0.0551 0.1474 0.2302 -0.0228 0.0230  -0.0021 20  PHE A CG  
203  C  CD1 . PHE A 20  ? 0.0852 0.2088 0.2219 -0.0057 -0.0269 0.0419  20  PHE A CD1 
204  C  CD2 . PHE A 20  ? 0.0980 0.1733 0.1882 -0.0540 0.0318  -0.0005 20  PHE A CD2 
205  C  CE1 . PHE A 20  ? 0.1420 0.1844 0.2031 -0.0076 -0.0097 0.0092  20  PHE A CE1 
206  C  CE2 . PHE A 20  ? 0.0998 0.2021 0.2372 -0.0208 0.0040  0.0156  20  PHE A CE2 
207  C  CZ  . PHE A 20  ? 0.0900 0.2083 0.2315 -0.0368 0.0126  0.0294  20  PHE A CZ  
208  N  N   . PRO A 21  ? 0.0763 0.1533 0.2229 -0.0305 -0.0164 0.0037  21  PRO A N   
209  C  CA  . PRO A 21  ? 0.0662 0.1799 0.1855 -0.0480 -0.0285 0.0055  21  PRO A CA  
210  C  C   . PRO A 21  ? 0.0844 0.1324 0.2187 -0.0102 -0.0238 0.0017  21  PRO A C   
211  O  O   . PRO A 21  ? 0.0702 0.1460 0.2272 -0.0066 -0.0346 0.0124  21  PRO A O   
212  C  CB  . PRO A 21  ? 0.0693 0.2162 0.2194 -0.0447 -0.0491 0.0160  21  PRO A CB  
213  C  CG  . PRO A 21  ? 0.2052 0.2198 0.2269 -0.0811 -0.0192 -0.0237 21  PRO A CG  
214  C  CD  . PRO A 21  ? 0.0903 0.1643 0.2399 -0.0693 -0.0125 0.0175  21  PRO A CD  
215  N  N   A ILE A 22  ? 0.0619 0.1143 0.2092 -0.0125 -0.0186 -0.0143 22  ILE A N   
216  N  N   B ILE A 22  ? 0.0535 0.1025 0.2075 -0.0089 -0.0198 -0.0159 22  ILE A N   
217  C  CA  A ILE A 22  ? 0.0872 0.1208 0.1891 -0.0076 -0.0181 -0.0049 22  ILE A CA  
218  C  CA  B ILE A 22  ? 0.0711 0.0989 0.1756 -0.0046 -0.0241 -0.0080 22  ILE A CA  
219  C  C   A ILE A 22  ? 0.0960 0.1253 0.1744 -0.0038 -0.0304 -0.0076 22  ILE A C   
220  C  C   B ILE A 22  ? 0.0874 0.1146 0.1645 -0.0027 -0.0285 -0.0068 22  ILE A C   
221  O  O   A ILE A 22  ? 0.0806 0.1428 0.1700 0.0048  -0.0135 0.0006  22  ILE A O   
222  O  O   B ILE A 22  ? 0.0441 0.1256 0.1644 0.0114  -0.0010 -0.0071 22  ILE A O   
223  C  CB  A ILE A 22  ? 0.0786 0.1392 0.1601 0.0076  -0.0166 -0.0153 22  ILE A CB  
224  C  CB  B ILE A 22  ? 0.0613 0.1068 0.1791 0.0209  -0.0282 -0.0177 22  ILE A CB  
225  C  CG1 A ILE A 22  ? 0.1054 0.1812 0.1826 0.0024  -0.0141 -0.0200 22  ILE A CG1 
226  C  CG1 B ILE A 22  ? 0.0777 0.0934 0.1673 -0.0152 -0.0196 0.0059  22  ILE A CG1 
227  C  CG2 A ILE A 22  ? 0.1269 0.1402 0.1601 -0.0152 -0.0248 0.0010  22  ILE A CG2 
228  C  CG2 B ILE A 22  ? 0.1275 0.1411 0.1697 -0.0187 -0.0366 0.0081  22  ILE A CG2 
229  C  CD1 A ILE A 22  ? 0.0800 0.2035 0.1698 -0.0237 -0.0195 0.0152  22  ILE A CD1 
230  C  CD1 B ILE A 22  ? 0.0305 0.0909 0.1691 -0.0031 -0.0271 0.0056  22  ILE A CD1 
231  N  N   . ALA A 23  ? 0.0901 0.1111 0.1855 -0.0156 -0.0249 0.0015  23  ALA A N   
232  C  CA  . ALA A 23  ? 0.1016 0.0998 0.1587 -0.0272 -0.0092 -0.0234 23  ALA A CA  
233  C  C   . ALA A 23  ? 0.0838 0.1382 0.1845 0.0060  -0.0187 -0.0092 23  ALA A C   
234  O  O   . ALA A 23  ? 0.0702 0.1352 0.1676 -0.0198 -0.0052 -0.0149 23  ALA A O   
235  C  CB  . ALA A 23  ? 0.0876 0.1140 0.2255 0.0001  -0.0176 -0.0211 23  ALA A CB  
236  N  N   . LYS A 24  ? 0.0952 0.1553 0.1803 0.0017  -0.0109 -0.0144 24  LYS A N   
237  C  CA  . LYS A 24  ? 0.0659 0.1679 0.1859 0.0008  -0.0306 -0.0109 24  LYS A CA  
238  C  C   . LYS A 24  ? 0.1158 0.1852 0.1713 -0.0017 -0.0141 0.0010  24  LYS A C   
239  O  O   . LYS A 24  ? 0.1316 0.2404 0.2176 -0.0175 -0.0427 0.0242  24  LYS A O   
240  C  CB  . LYS A 24  ? 0.0847 0.1752 0.2072 0.0126  -0.0082 0.0074  24  LYS A CB  
241  C  CG  . LYS A 24  ? 0.0946 0.2402 0.2637 0.0373  -0.0023 0.0078  24  LYS A CG  
242  C  CD  . LYS A 24  ? 0.1633 0.2610 0.3407 0.0500  -0.0133 0.0401  24  LYS A CD  
243  C  CE  . LYS A 24  ? 0.2284 0.2868 0.3091 0.0384  0.0208  0.0430  24  LYS A CE  
244  N  NZ  . LYS A 24  ? 0.2529 0.3282 0.4254 0.0227  0.0255  -0.0060 24  LYS A NZ  
245  N  N   . GLY A 25  ? 0.0867 0.1511 0.1935 0.0046  0.0066  -0.0113 25  GLY A N   
246  C  CA  . GLY A 25  ? 0.0878 0.1852 0.1676 -0.0304 -0.0109 -0.0192 25  GLY A CA  
247  C  C   . GLY A 25  ? 0.0982 0.1885 0.1041 -0.0093 -0.0218 -0.0223 25  GLY A C   
248  O  O   . GLY A 25  ? 0.0944 0.2374 0.1633 -0.0137 -0.0469 -0.0115 25  GLY A O   
249  N  N   . GLU A 26  ? 0.0831 0.2372 0.1280 -0.0096 -0.0286 -0.0476 26  GLU A N   
250  C  CA  . GLU A 26  ? 0.1000 0.2232 0.1354 -0.0055 -0.0428 -0.0307 26  GLU A CA  
251  C  C   . GLU A 26  ? 0.1039 0.1932 0.1280 -0.0092 -0.0322 -0.0273 26  GLU A C   
252  O  O   . GLU A 26  ? 0.1111 0.2067 0.1244 0.0031  -0.0474 -0.0010 26  GLU A O   
253  C  CB  . GLU A 26  ? 0.1128 0.2401 0.1651 -0.0219 -0.0452 -0.0489 26  GLU A CB  
254  C  CG  . GLU A 26  ? 0.1212 0.3170 0.1869 -0.0048 -0.0171 -0.0364 26  GLU A CG  
255  C  CD  . GLU A 26  ? 0.2678 0.3748 0.2757 -0.0132 -0.0693 -0.0051 26  GLU A CD  
256  O  OE1 . GLU A 26  ? 0.3130 0.4399 0.3116 -0.0015 -0.1035 -0.0035 26  GLU A OE1 
257  O  OE2 . GLU A 26  ? 0.3217 0.4535 0.3479 0.0034  -0.0690 -0.0081 26  GLU A OE2 
258  N  N   . ARG A 27  ? 0.1032 0.1393 0.0833 -0.0130 -0.0377 -0.0218 27  ARG A N   
259  C  CA  . ARG A 27  ? 0.0946 0.1178 0.1058 0.0089  -0.0295 -0.0183 27  ARG A CA  
260  C  C   . ARG A 27  ? 0.0761 0.0995 0.0876 0.0012  -0.0031 -0.0421 27  ARG A C   
261  O  O   . ARG A 27  ? 0.0535 0.1224 0.1328 0.0102  -0.0339 -0.0186 27  ARG A O   
262  C  CB  . ARG A 27  ? 0.1463 0.1476 0.1582 0.0078  -0.0027 -0.0253 27  ARG A CB  
263  C  CG  . ARG A 27  ? 0.1819 0.1993 0.1573 -0.0005 -0.0328 -0.0190 27  ARG A CG  
264  C  CD  . ARG A 27  ? 0.1621 0.2072 0.2179 0.0416  -0.0430 -0.0132 27  ARG A CD  
265  N  NE  . ARG A 27  ? 0.1564 0.1889 0.2211 -0.0021 -0.0041 -0.0292 27  ARG A NE  
266  C  CZ  . ARG A 27  ? 0.1342 0.1801 0.1489 0.0109  -0.0035 0.0070  27  ARG A CZ  
267  N  NH1 . ARG A 27  ? 0.1648 0.2079 0.1788 -0.0010 0.0146  -0.0825 27  ARG A NH1 
268  N  NH2 . ARG A 27  ? 0.1770 0.1575 0.1679 -0.0423 -0.0278 -0.0344 27  ARG A NH2 
269  N  N   . GLN A 28  ? 0.0487 0.0996 0.1138 0.0137  -0.0253 -0.0294 28  GLN A N   
270  C  CA  . GLN A 28  ? 0.0566 0.0790 0.0928 -0.0017 -0.0242 -0.0329 28  GLN A CA  
271  C  C   . GLN A 28  ? 0.0680 0.0725 0.1081 0.0085  -0.0281 -0.0098 28  GLN A C   
272  O  O   . GLN A 28  ? 0.0680 0.1235 0.0770 0.0020  -0.0125 -0.0065 28  GLN A O   
273  C  CB  . GLN A 28  ? 0.0382 0.0967 0.1300 0.0159  -0.0119 -0.0108 28  GLN A CB  
274  C  CG  . GLN A 28  ? 0.1009 0.0980 0.1084 -0.0062 -0.0252 -0.0049 28  GLN A CG  
275  C  CD  . GLN A 28  ? 0.0705 0.1397 0.0992 -0.0028 -0.0406 -0.0013 28  GLN A CD  
276  O  OE1 . GLN A 28  ? 0.0612 0.0984 0.1287 -0.0114 -0.0057 -0.0209 28  GLN A OE1 
277  N  NE2 . GLN A 28  ? 0.0430 0.1134 0.1443 -0.0057 -0.0355 0.0001  28  GLN A NE2 
278  N  N   . SER A 29  ? 0.0479 0.0723 0.0948 -0.0026 -0.0277 -0.0086 29  SER A N   
279  C  CA  . SER A 29  ? 0.0608 0.0741 0.0630 -0.0118 -0.0207 -0.0269 29  SER A CA  
280  C  C   . SER A 29  ? 0.0375 0.0707 0.1039 0.0006  -0.0241 -0.0254 29  SER A C   
281  O  O   . SER A 29  ? 0.0310 0.0806 0.1226 0.0115  0.0020  -0.0044 29  SER A O   
282  C  CB  . SER A 29  ? 0.0685 0.0861 0.1077 0.0208  -0.0436 -0.0263 29  SER A CB  
283  O  OG  . SER A 29  ? 0.0488 0.0761 0.0934 -0.0149 -0.0043 -0.0225 29  SER A OG  
284  N  N   . PRO A 30  ? 0.0538 0.0716 0.0894 -0.0017 -0.0082 -0.0032 30  PRO A N   
285  C  CA  . PRO A 30  ? 0.0508 0.0579 0.0856 -0.0054 -0.0187 0.0082  30  PRO A CA  
286  C  C   . PRO A 30  ? 0.0639 0.0428 0.0867 0.0115  -0.0006 0.0098  30  PRO A C   
287  O  O   . PRO A 30  ? 0.0761 0.0851 0.0900 0.0041  -0.0211 0.0102  30  PRO A O   
288  C  CB  . PRO A 30  ? 0.0266 0.0899 0.1053 0.0015  -0.0098 -0.0299 30  PRO A CB  
289  C  CG  . PRO A 30  ? 0.0597 0.1009 0.1230 -0.0032 0.0096  0.0070  30  PRO A CG  
290  C  CD  . PRO A 30  ? 0.0700 0.0825 0.1030 0.0052  0.0076  -0.0299 30  PRO A CD  
291  N  N   . VAL A 31  ? 0.0807 0.0456 0.0791 -0.0065 -0.0006 0.0175  31  VAL A N   
292  C  CA  . VAL A 31  ? 0.1009 0.0590 0.0709 -0.0227 -0.0125 0.0143  31  VAL A CA  
293  C  C   . VAL A 31  ? 0.0634 0.0729 0.0846 -0.0070 0.0024  0.0063  31  VAL A C   
294  O  O   . VAL A 31  ? 0.0706 0.0750 0.0983 -0.0074 -0.0182 0.0247  31  VAL A O   
295  C  CB  . VAL A 31  ? 0.0888 0.0813 0.0996 0.0000  -0.0181 -0.0114 31  VAL A CB  
296  C  CG1 . VAL A 31  ? 0.0745 0.0822 0.1406 -0.0309 -0.0082 -0.0081 31  VAL A CG1 
297  C  CG2 . VAL A 31  ? 0.0648 0.1483 0.1158 0.0250  0.0068  -0.0222 31  VAL A CG2 
298  N  N   . ASP A 32  ? 0.1228 0.0583 0.0719 -0.0111 -0.0074 0.0035  32  ASP A N   
299  C  CA  . ASP A 32  ? 0.0732 0.0731 0.0982 0.0046  -0.0046 0.0178  32  ASP A CA  
300  C  C   . ASP A 32  ? 0.0957 0.0793 0.1036 0.0044  -0.0071 -0.0144 32  ASP A C   
301  O  O   . ASP A 32  ? 0.0886 0.1151 0.1099 0.0082  -0.0093 -0.0267 32  ASP A O   
302  C  CB  . ASP A 32  ? 0.1097 0.0635 0.1273 0.0121  -0.0119 0.0331  32  ASP A CB  
303  C  CG  . ASP A 32  ? 0.1287 0.1023 0.1576 0.0154  -0.0242 0.0229  32  ASP A CG  
304  O  OD1 . ASP A 32  ? 0.0967 0.0847 0.1274 -0.0015 -0.0168 0.0082  32  ASP A OD1 
305  O  OD2 . ASP A 32  ? 0.1887 0.1228 0.1000 -0.0346 -0.0342 0.0214  32  ASP A OD2 
306  N  N   . ILE A 33  ? 0.0518 0.1040 0.1127 0.0000  -0.0049 0.0052  33  ILE A N   
307  C  CA  . ILE A 33  ? 0.0934 0.0912 0.1330 0.0173  -0.0046 0.0205  33  ILE A CA  
308  C  C   . ILE A 33  ? 0.1249 0.0883 0.0995 0.0251  0.0140  0.0204  33  ILE A C   
309  O  O   . ILE A 33  ? 0.1352 0.0887 0.1370 0.0000  0.0060  0.0122  33  ILE A O   
310  C  CB  . ILE A 33  ? 0.0566 0.0942 0.1357 0.0204  -0.0087 0.0379  33  ILE A CB  
311  C  CG1 . ILE A 33  ? 0.0707 0.0948 0.1221 -0.0046 0.0013  0.0175  33  ILE A CG1 
312  C  CG2 . ILE A 33  ? 0.0603 0.1880 0.1573 0.0151  0.0522  -0.0062 33  ILE A CG2 
313  C  CD1 . ILE A 33  ? 0.0962 0.1248 0.1298 0.0436  -0.0008 0.0241  33  ILE A CD1 
314  N  N   A ASP A 34  ? 0.1490 0.1146 0.1002 0.0243  -0.0052 0.0231  34  ASP A N   
315  N  N   B ASP A 34  ? 0.1382 0.1208 0.1040 0.0241  -0.0060 0.0229  34  ASP A N   
316  C  CA  A ASP A 34  ? 0.1662 0.1086 0.1275 0.0399  0.0017  0.0282  34  ASP A CA  
317  C  CA  B ASP A 34  ? 0.1472 0.1133 0.1334 0.0388  0.0030  0.0273  34  ASP A CA  
318  C  C   A ASP A 34  ? 0.1862 0.1119 0.1199 0.0287  0.0165  0.0384  34  ASP A C   
319  C  C   B ASP A 34  ? 0.1738 0.1159 0.1208 0.0308  0.0177  0.0361  34  ASP A C   
320  O  O   A ASP A 34  ? 0.2115 0.1411 0.1226 0.0313  0.0015  0.0205  34  ASP A O   
321  O  O   B ASP A 34  ? 0.1909 0.1249 0.1192 0.0436  0.0055  0.0109  34  ASP A O   
322  C  CB  A ASP A 34  ? 0.1882 0.1022 0.1120 0.0432  -0.0006 0.0271  34  ASP A CB  
323  C  CB  B ASP A 34  ? 0.1607 0.1280 0.1269 0.0353  -0.0017 0.0324  34  ASP A CB  
324  C  CG  A ASP A 34  ? 0.2173 0.1608 0.1372 0.0238  -0.0032 0.0397  34  ASP A CG  
325  C  CG  B ASP A 34  ? 0.1474 0.1586 0.1334 0.0273  0.0019  0.0284  34  ASP A CG  
326  O  OD1 A ASP A 34  ? 0.1894 0.1675 0.1952 0.0171  0.0248  0.0441  34  ASP A OD1 
327  O  OD1 B ASP A 34  ? 0.1255 0.1914 0.1791 0.0416  -0.0331 0.0568  34  ASP A OD1 
328  O  OD2 A ASP A 34  ? 0.2255 0.1683 0.1694 0.0934  0.0303  0.0746  34  ASP A OD2 
329  O  OD2 B ASP A 34  ? 0.2021 0.2255 0.1421 0.0469  -0.0027 0.0617  34  ASP A OD2 
330  N  N   . THR A 35  ? 0.1903 0.1472 0.1070 0.0381  0.0187  0.0425  35  THR A N   
331  C  CA  . THR A 35  ? 0.1967 0.1881 0.1077 0.0487  0.0245  0.0362  35  THR A CA  
332  C  C   . THR A 35  ? 0.2089 0.1673 0.1136 0.0531  0.0447  0.0353  35  THR A C   
333  O  O   . THR A 35  ? 0.2176 0.2293 0.1368 0.0626  0.0522  0.0386  35  THR A O   
334  C  CB  . THR A 35  ? 0.1806 0.1600 0.1773 0.0472  0.0256  0.0406  35  THR A CB  
335  O  OG1 . THR A 35  ? 0.2337 0.1612 0.1745 0.0215  0.0727  0.0672  35  THR A OG1 
336  C  CG2 . THR A 35  ? 0.1905 0.2336 0.1030 0.0652  0.0094  0.0637  35  THR A CG2 
337  N  N   . HIS A 36  ? 0.2501 0.1941 0.1309 0.0507  0.0375  0.0531  36  HIS A N   
338  C  CA  . HIS A 36  ? 0.2552 0.1809 0.1446 0.0494  0.0152  0.0505  36  HIS A CA  
339  C  C   . HIS A 36  ? 0.2609 0.2194 0.1001 0.0423  0.0353  0.0143  36  HIS A C   
340  O  O   . HIS A 36  ? 0.2531 0.2911 0.1571 0.0653  0.0217  0.0173  36  HIS A O   
341  C  CB  . HIS A 36  ? 0.2827 0.1924 0.1500 0.0560  0.0005  0.0441  36  HIS A CB  
342  C  CG  . HIS A 36  ? 0.3544 0.2311 0.1923 0.0483  -0.0274 0.0441  36  HIS A CG  
343  N  ND1 . HIS A 36  ? 0.4323 0.2347 0.1910 0.0720  -0.0518 0.0592  36  HIS A ND1 
344  C  CD2 . HIS A 36  ? 0.3788 0.2434 0.1701 -0.0026 -0.0430 0.0670  36  HIS A CD2 
345  C  CE1 . HIS A 36  ? 0.4416 0.2183 0.2337 0.0529  -0.0329 0.0254  36  HIS A CE1 
346  N  NE2 . HIS A 36  ? 0.4587 0.2876 0.2985 0.0443  -0.0706 0.0597  36  HIS A NE2 
347  N  N   A THR A 37  ? 0.2615 0.1743 0.1372 0.0436  0.0390  0.0209  37  THR A N   
348  N  N   B THR A 37  ? 0.2549 0.1697 0.1386 0.0427  0.0324  0.0159  37  THR A N   
349  C  CA  A THR A 37  ? 0.2487 0.1740 0.1291 0.0450  0.0276  0.0350  37  THR A CA  
350  C  CA  B THR A 37  ? 0.2531 0.1727 0.1345 0.0417  0.0255  0.0277  37  THR A CA  
351  C  C   A THR A 37  ? 0.2399 0.1661 0.1327 0.0397  0.0300  0.0302  37  THR A C   
352  C  C   B THR A 37  ? 0.2423 0.1640 0.1263 0.0386  0.0350  0.0271  37  THR A C   
353  O  O   A THR A 37  ? 0.2158 0.1923 0.1036 0.0491  0.0251  0.0275  37  THR A O   
354  O  O   B THR A 37  ? 0.2714 0.1956 0.1266 0.0370  0.0331  0.0111  37  THR A O   
355  C  CB  A THR A 37  ? 0.2560 0.1752 0.1332 0.0281  0.0167  0.0509  37  THR A CB  
356  C  CB  B THR A 37  ? 0.2623 0.1823 0.1334 0.0405  0.0104  0.0296  37  THR A CB  
357  O  OG1 A THR A 37  ? 0.2387 0.1837 0.1623 0.0619  0.0568  0.0386  37  THR A OG1 
358  O  OG1 B THR A 37  ? 0.2885 0.1669 0.2255 0.0408  0.0265  0.0240  37  THR A OG1 
359  C  CG2 A THR A 37  ? 0.2234 0.1682 0.1324 0.0659  0.0115  0.0392  37  THR A CG2 
360  C  CG2 B THR A 37  ? 0.2316 0.1568 0.1436 0.0381  0.0076  0.0193  37  THR A CG2 
361  N  N   . ALA A 38  ? 0.2558 0.1632 0.1019 0.0408  0.0381  0.0252  38  ALA A N   
362  C  CA  . ALA A 38  ? 0.1984 0.1464 0.1122 0.0513  0.0441  0.0068  38  ALA A CA  
363  C  C   . ALA A 38  ? 0.2144 0.1855 0.2097 0.0274  0.0410  -0.0024 38  ALA A C   
364  O  O   . ALA A 38  ? 0.2928 0.2207 0.2775 0.0476  0.0878  0.0184  38  ALA A O   
365  C  CB  . ALA A 38  ? 0.2049 0.1547 0.1134 0.0199  -0.0017 -0.0034 38  ALA A CB  
366  N  N   . LYS A 39  ? 0.2189 0.1992 0.1632 0.0540  0.0254  -0.0006 39  LYS A N   
367  C  CA  . LYS A 39  ? 0.1902 0.2293 0.2180 0.0666  0.0032  -0.0200 39  LYS A CA  
368  C  C   . LYS A 39  ? 0.1673 0.2222 0.1641 0.0456  0.0119  -0.0197 39  LYS A C   
369  O  O   . LYS A 39  ? 0.1367 0.2391 0.1264 0.0472  0.0040  -0.0288 39  LYS A O   
370  C  CB  . LYS A 39  ? 0.2592 0.2653 0.2169 0.0428  -0.0052 -0.0346 39  LYS A CB  
371  C  CG  . LYS A 39  ? 0.2854 0.3501 0.2567 0.0425  0.0034  -0.0057 39  LYS A CG  
372  C  CD  . LYS A 39  ? 0.2223 0.3288 0.2551 0.0628  -0.0080 0.0357  39  LYS A CD  
373  C  CE  . LYS A 39  ? 0.2919 0.3964 0.2822 0.0165  0.0032  0.0160  39  LYS A CE  
374  N  NZ  . LYS A 39  ? 0.2781 0.3399 0.3574 0.0370  -0.0174 0.0929  39  LYS A NZ  
375  N  N   . TYR A 40  ? 0.1997 0.2229 0.1688 0.0278  0.0252  -0.0013 40  TYR A N   
376  C  CA  . TYR A 40  ? 0.1765 0.2363 0.1835 0.0110  0.0430  -0.0099 40  TYR A CA  
377  C  C   . TYR A 40  ? 0.1795 0.2370 0.1844 0.0093  0.0315  -0.0068 40  TYR A C   
378  O  O   . TYR A 40  ? 0.1809 0.2592 0.1571 0.0423  0.0346  -0.0133 40  TYR A O   
379  C  CB  . TYR A 40  ? 0.2110 0.2918 0.2085 -0.0081 0.0410  0.0140  40  TYR A CB  
380  C  CG  . TYR A 40  ? 0.2151 0.3227 0.2280 -0.0153 0.0515  0.0000  40  TYR A CG  
381  C  CD1 . TYR A 40  ? 0.2649 0.3658 0.2797 -0.0155 0.0003  0.0092  40  TYR A CD1 
382  C  CD2 . TYR A 40  ? 0.3305 0.3729 0.2558 0.0071  0.0408  -0.0098 40  TYR A CD2 
383  C  CE1 . TYR A 40  ? 0.2455 0.3945 0.2039 0.0137  0.0206  0.0119  40  TYR A CE1 
384  C  CE2 . TYR A 40  ? 0.2552 0.3989 0.2825 -0.0172 0.0144  0.0041  40  TYR A CE2 
385  C  CZ  . TYR A 40  ? 0.2244 0.4013 0.2957 0.0143  0.0313  0.0109  40  TYR A CZ  
386  O  OH  . TYR A 40  ? 0.2259 0.4542 0.3572 0.0077  0.0362  -0.0082 40  TYR A OH  
387  N  N   . ASP A 41  ? 0.1533 0.1896 0.1712 0.0217  0.0364  -0.0028 41  ASP A N   
388  C  CA  . ASP A 41  ? 0.1783 0.2327 0.1615 0.0286  0.0178  -0.0175 41  ASP A CA  
389  C  C   . ASP A 41  ? 0.2169 0.2845 0.1878 0.0366  0.0219  -0.0015 41  ASP A C   
390  O  O   . ASP A 41  ? 0.1867 0.2444 0.1767 0.0395  0.0076  0.0236  41  ASP A O   
391  C  CB  . ASP A 41  ? 0.2413 0.2176 0.2104 0.0119  0.0052  -0.0115 41  ASP A CB  
392  C  CG  . ASP A 41  ? 0.2785 0.2652 0.2484 -0.0196 -0.0317 -0.0085 41  ASP A CG  
393  O  OD1 . ASP A 41  ? 0.3240 0.2894 0.2013 0.0252  -0.0231 -0.0410 41  ASP A OD1 
394  O  OD2 . ASP A 41  ? 0.2707 0.3032 0.3720 -0.0399 -0.0140 0.0057  41  ASP A OD2 
395  N  N   . PRO A 42  ? 0.2085 0.3468 0.2067 0.0597  0.0324  0.0049  42  PRO A N   
396  C  CA  . PRO A 42  ? 0.2178 0.3488 0.2293 0.0562  0.0357  0.0230  42  PRO A CA  
397  C  C   . PRO A 42  ? 0.2476 0.3398 0.2240 0.0560  0.0362  0.0093  42  PRO A C   
398  O  O   . PRO A 42  ? 0.2634 0.4217 0.2617 0.0768  0.0441  0.0119  42  PRO A O   
399  C  CB  . PRO A 42  ? 0.2261 0.3874 0.2275 0.0617  0.0318  0.0059  42  PRO A CB  
400  C  CG  . PRO A 42  ? 0.2164 0.3878 0.2269 0.0509  0.0194  0.0035  42  PRO A CG  
401  C  CD  . PRO A 42  ? 0.2578 0.3399 0.2022 0.0540  0.0502  0.0176  42  PRO A CD  
402  N  N   . SER A 43  ? 0.2460 0.3160 0.2063 0.0513  0.0394  -0.0124 43  SER A N   
403  C  CA  . SER A 43  ? 0.3162 0.3041 0.2567 0.0397  -0.0012 -0.0205 43  SER A CA  
404  C  C   . SER A 43  ? 0.2953 0.2786 0.2386 0.0542  0.0046  -0.0096 43  SER A C   
405  O  O   . SER A 43  ? 0.3512 0.2972 0.2775 0.0579  0.0153  -0.0287 43  SER A O   
406  C  CB  . SER A 43  ? 0.3172 0.2989 0.2845 0.0248  0.0027  -0.0245 43  SER A CB  
407  O  OG  . SER A 43  ? 0.3932 0.3054 0.3122 -0.0210 -0.0270 -0.0438 43  SER A OG  
408  N  N   . LEU A 44  ? 0.2627 0.2779 0.1966 0.0456  -0.0052 -0.0286 44  LEU A N   
409  C  CA  . LEU A 44  ? 0.2193 0.2649 0.2017 0.0384  -0.0163 0.0068  44  LEU A CA  
410  C  C   . LEU A 44  ? 0.2243 0.2839 0.2250 0.0122  -0.0176 0.0111  44  LEU A C   
411  O  O   . LEU A 44  ? 0.1888 0.3431 0.2627 0.0201  0.0017  0.0803  44  LEU A O   
412  C  CB  . LEU A 44  ? 0.2043 0.2631 0.1985 0.0082  0.0032  -0.0285 44  LEU A CB  
413  C  CG  . LEU A 44  ? 0.1912 0.1909 0.1765 0.0136  -0.0196 0.0055  44  LEU A CG  
414  C  CD1 . LEU A 44  ? 0.1518 0.2031 0.1615 0.0243  0.0350  -0.0183 44  LEU A CD1 
415  C  CD2 . LEU A 44  ? 0.2632 0.2639 0.1565 -0.0270 0.0096  -0.0020 44  LEU A CD2 
416  N  N   . LYS A 45  ? 0.2029 0.2807 0.1961 0.0175  -0.0538 0.0153  45  LYS A N   
417  C  CA  . LYS A 45  ? 0.1928 0.2681 0.2304 0.0238  -0.0485 -0.0171 45  LYS A CA  
418  C  C   . LYS A 45  ? 0.1756 0.2474 0.1999 0.0126  -0.0209 0.0104  45  LYS A C   
419  O  O   . LYS A 45  ? 0.1648 0.2547 0.2261 -0.0164 -0.0157 -0.0210 45  LYS A O   
420  C  CB  . LYS A 45  ? 0.2498 0.2663 0.2194 0.0043  -0.0300 0.0043  45  LYS A CB  
421  C  CG  . LYS A 45  ? 0.2868 0.3040 0.2818 0.0140  -0.0384 -0.0209 45  LYS A CG  
422  C  CD  . LYS A 45  ? 0.3395 0.3384 0.3018 0.0031  0.0003  -0.0035 45  LYS A CD  
423  C  CE  . LYS A 45  ? 0.3174 0.3199 0.3082 0.0023  -0.0024 -0.0015 45  LYS A CE  
424  N  NZ  . LYS A 45  ? 0.3170 0.3170 0.3079 0.0012  -0.0010 -0.0010 45  LYS A NZ  
425  N  N   . PRO A 46  ? 0.1431 0.2215 0.2054 -0.0109 -0.0034 -0.0041 46  PRO A N   
426  C  CA  . PRO A 46  ? 0.1321 0.2286 0.1942 -0.0078 -0.0070 0.0030  46  PRO A CA  
427  C  C   . PRO A 46  ? 0.1196 0.2018 0.2046 0.0017  0.0185  0.0035  46  PRO A C   
428  O  O   . PRO A 46  ? 0.1057 0.2011 0.2207 -0.0020 -0.0051 -0.0019 46  PRO A O   
429  C  CB  . PRO A 46  ? 0.1339 0.2237 0.1989 -0.0028 -0.0293 -0.0173 46  PRO A CB  
430  C  CG  . PRO A 46  ? 0.1195 0.2664 0.2291 0.0007  -0.0142 -0.0091 46  PRO A CG  
431  C  CD  . PRO A 46  ? 0.1503 0.2463 0.2131 0.0115  -0.0003 -0.0294 46  PRO A CD  
432  N  N   . LEU A 47  ? 0.1163 0.2243 0.2158 0.0271  0.0051  0.0030  47  LEU A N   
433  C  CA  . LEU A 47  ? 0.0755 0.1887 0.2061 0.0037  -0.0010 0.0137  47  LEU A CA  
434  C  C   . LEU A 47  ? 0.0967 0.2182 0.2424 -0.0109 -0.0133 0.0176  47  LEU A C   
435  O  O   . LEU A 47  ? 0.0892 0.2671 0.3116 -0.0348 -0.0469 0.0533  47  LEU A O   
436  C  CB  . LEU A 47  ? 0.1185 0.2379 0.2653 -0.0057 0.0218  0.0043  47  LEU A CB  
437  C  CG  . LEU A 47  ? 0.1282 0.2416 0.2674 -0.0183 0.0021  -0.0693 47  LEU A CG  
438  C  CD1 . LEU A 47  ? 0.1273 0.2573 0.3529 -0.0741 -0.0073 -0.0854 47  LEU A CD1 
439  C  CD2 . LEU A 47  ? 0.1228 0.2291 0.3149 0.0273  -0.0087 -0.0777 47  LEU A CD2 
440  N  N   . SER A 48  ? 0.0702 0.1776 0.2135 -0.0027 -0.0035 0.0280  48  SER A N   
441  C  CA  . SER A 48  ? 0.1194 0.1632 0.1949 -0.0157 0.0041  0.0245  48  SER A CA  
442  C  C   . SER A 48  ? 0.1106 0.1576 0.1894 -0.0187 0.0021  0.0017  48  SER A C   
443  O  O   . SER A 48  ? 0.1131 0.1831 0.1931 -0.0445 0.0110  -0.0198 48  SER A O   
444  C  CB  . SER A 48  ? 0.1169 0.1971 0.2377 -0.0163 0.0074  0.0381  48  SER A CB  
445  O  OG  . SER A 48  ? 0.1733 0.2438 0.2721 0.0478  0.0043  0.0452  48  SER A OG  
446  N  N   . VAL A 49  ? 0.1702 0.1905 0.1557 -0.0392 -0.0181 0.0024  49  VAL A N   
447  C  CA  . VAL A 49  ? 0.1569 0.1827 0.1946 -0.0544 -0.0120 0.0111  49  VAL A CA  
448  C  C   . VAL A 49  ? 0.1375 0.2365 0.2337 -0.0438 -0.0293 0.0136  49  VAL A C   
449  O  O   . VAL A 49  ? 0.1557 0.2502 0.2433 -0.0954 -0.0120 -0.0129 49  VAL A O   
450  C  CB  . VAL A 49  ? 0.1931 0.2225 0.2079 -0.0285 -0.0043 -0.0113 49  VAL A CB  
451  C  CG1 . VAL A 49  ? 0.2888 0.2119 0.2402 -0.0586 0.0154  -0.0189 49  VAL A CG1 
452  C  CG2 . VAL A 49  ? 0.1522 0.1924 0.2358 -0.0414 0.0165  -0.0126 49  VAL A CG2 
453  N  N   . SER A 50  ? 0.1403 0.2354 0.1985 -0.0427 -0.0370 0.0100  50  SER A N   
454  C  CA  . SER A 50  ? 0.1228 0.2433 0.2366 -0.0355 -0.0353 0.0179  50  SER A CA  
455  C  C   . SER A 50  ? 0.1555 0.2412 0.2300 -0.0098 -0.0502 0.0153  50  SER A C   
456  O  O   . SER A 50  ? 0.1607 0.2194 0.2315 -0.0264 -0.0866 0.0228  50  SER A O   
457  C  CB  . SER A 50  ? 0.1647 0.2797 0.2466 -0.0205 0.0164  0.0166  50  SER A CB  
458  O  OG  . SER A 50  ? 0.2530 0.3630 0.3264 -0.0027 -0.0038 0.0034  50  SER A OG  
459  N  N   . TYR A 51  ? 0.1645 0.2161 0.2518 -0.0248 -0.0511 -0.0003 51  TYR A N   
460  C  CA  . TYR A 51  ? 0.1626 0.2002 0.2039 -0.0162 -0.0606 0.0328  51  TYR A CA  
461  C  C   . TYR A 51  ? 0.1925 0.2214 0.2226 0.0073  -0.0487 0.0399  51  TYR A C   
462  O  O   . TYR A 51  ? 0.2161 0.2149 0.2176 -0.0008 -0.0841 0.0326  51  TYR A O   
463  C  CB  . TYR A 51  ? 0.1309 0.2031 0.2160 -0.0293 -0.0683 0.0104  51  TYR A CB  
464  C  CG  . TYR A 51  ? 0.1587 0.1433 0.1478 -0.0538 -0.0640 0.0344  51  TYR A CG  
465  C  CD1 . TYR A 51  ? 0.1749 0.1160 0.1946 -0.0452 -0.0262 -0.0098 51  TYR A CD1 
466  C  CD2 . TYR A 51  ? 0.1248 0.1400 0.1190 -0.0276 -0.0308 0.0353  51  TYR A CD2 
467  C  CE1 . TYR A 51  ? 0.1389 0.1298 0.1526 -0.0137 -0.0241 0.0043  51  TYR A CE1 
468  C  CE2 . TYR A 51  ? 0.1625 0.1282 0.1192 -0.0405 -0.0793 0.0028  51  TYR A CE2 
469  C  CZ  . TYR A 51  ? 0.1428 0.1641 0.1088 -0.0379 -0.0399 -0.0052 51  TYR A CZ  
470  O  OH  . TYR A 51  ? 0.1572 0.1068 0.1677 -0.0201 -0.0636 -0.0082 51  TYR A OH  
471  N  N   A ASP A 52  ? 0.1878 0.2596 0.2386 -0.0114 -0.0432 0.0423  52  ASP A N   
472  N  N   B ASP A 52  ? 0.1927 0.2671 0.2363 -0.0115 -0.0454 0.0388  52  ASP A N   
473  C  CA  A ASP A 52  ? 0.2182 0.2619 0.2549 0.0060  -0.0299 0.0518  52  ASP A CA  
474  C  CA  B ASP A 52  ? 0.2182 0.2664 0.2462 0.0024  -0.0388 0.0445  52  ASP A CA  
475  C  C   A ASP A 52  ? 0.2164 0.2674 0.2768 0.0055  -0.0297 0.0419  52  ASP A C   
476  C  C   B ASP A 52  ? 0.2358 0.2853 0.2750 0.0000  -0.0351 0.0351  52  ASP A C   
477  O  O   A ASP A 52  ? 0.2176 0.2485 0.2598 0.0178  -0.0412 0.0612  52  ASP A O   
478  O  O   B ASP A 52  ? 0.2354 0.2771 0.2667 0.0010  -0.0397 0.0392  52  ASP A O   
479  C  CB  A ASP A 52  ? 0.2171 0.2696 0.2671 0.0013  -0.0287 0.0412  52  ASP A CB  
480  C  CB  B ASP A 52  ? 0.2463 0.2950 0.2671 -0.0024 -0.0208 0.0285  52  ASP A CB  
481  C  CG  A ASP A 52  ? 0.2610 0.2906 0.2951 0.0068  -0.0052 0.0179  52  ASP A CG  
482  C  CG  B ASP A 52  ? 0.2907 0.3348 0.2912 0.0176  -0.0227 0.0098  52  ASP A CG  
483  O  OD1 A ASP A 52  ? 0.2555 0.3109 0.3368 -0.0163 0.0031  0.0273  52  ASP A OD1 
484  O  OD1 B ASP A 52  ? 0.3087 0.3863 0.3382 0.0254  -0.0110 -0.0153 52  ASP A OD1 
485  O  OD2 A ASP A 52  ? 0.3719 0.3106 0.3507 0.0000  -0.0156 0.0346  52  ASP A OD2 
486  O  OD2 B ASP A 52  ? 0.3314 0.3336 0.3815 -0.0078 -0.0125 -0.0207 52  ASP A OD2 
487  N  N   . GLN A 53  ? 0.2139 0.2760 0.2912 0.0054  -0.0399 0.0373  53  GLN A N   
488  C  CA  . GLN A 53  ? 0.2223 0.2700 0.3147 -0.0041 -0.0318 0.0220  53  GLN A CA  
489  C  C   . GLN A 53  ? 0.2192 0.2349 0.2809 0.0027  -0.0322 0.0055  53  GLN A C   
490  O  O   . GLN A 53  ? 0.1892 0.2337 0.2962 -0.0088 -0.0662 0.0217  53  GLN A O   
491  C  CB  . GLN A 53  ? 0.2581 0.2980 0.3470 0.0129  -0.0219 0.0108  53  GLN A CB  
492  C  CG  . GLN A 53  ? 0.3269 0.3977 0.4298 0.0032  0.0131  0.0057  53  GLN A CG  
493  C  CD  . GLN A 53  ? 0.4313 0.4738 0.4660 0.0091  -0.0114 0.0328  53  GLN A CD  
494  O  OE1 . GLN A 53  ? 0.5131 0.6201 0.5534 0.0280  -0.0094 0.0130  53  GLN A OE1 
495  N  NE2 . GLN A 53  ? 0.4495 0.4817 0.4792 0.0037  -0.0027 0.0108  53  GLN A NE2 
496  N  N   . ALA A 54  ? 0.2164 0.1759 0.2811 -0.0148 -0.0480 0.0159  54  ALA A N   
497  C  CA  . ALA A 54  ? 0.2064 0.1654 0.2083 -0.0041 -0.0403 -0.0043 54  ALA A CA  
498  C  C   . ALA A 54  ? 0.2167 0.1801 0.2135 -0.0026 -0.0421 -0.0164 54  ALA A C   
499  O  O   . ALA A 54  ? 0.2422 0.2809 0.2305 -0.0476 -0.0749 -0.0425 54  ALA A O   
500  C  CB  . ALA A 54  ? 0.2075 0.1679 0.2774 -0.0017 -0.0229 -0.0063 54  ALA A CB  
501  N  N   . THR A 55  ? 0.1995 0.1544 0.1626 0.0137  -0.0253 0.0260  55  THR A N   
502  C  CA  . THR A 55  ? 0.2204 0.1600 0.1612 0.0311  -0.0527 0.0244  55  THR A CA  
503  C  C   . THR A 55  ? 0.2390 0.1174 0.1152 0.0245  -0.0483 0.0252  55  THR A C   
504  O  O   . THR A 55  ? 0.2467 0.0967 0.1255 0.0176  -0.0546 0.0216  55  THR A O   
505  C  CB  . THR A 55  ? 0.2598 0.1946 0.2021 0.0315  -0.0274 0.0505  55  THR A CB  
506  O  OG1 . THR A 55  ? 0.3098 0.1809 0.2746 0.0186  -0.0524 -0.0010 55  THR A OG1 
507  C  CG2 . THR A 55  ? 0.3119 0.1788 0.1992 0.0856  -0.0062 0.0445  55  THR A CG2 
508  N  N   . SER A 56  ? 0.2764 0.0998 0.1432 0.0073  -0.0653 0.0182  56  SER A N   
509  C  CA  . SER A 56  ? 0.3104 0.1127 0.1407 0.0154  -0.0381 -0.0089 56  SER A CA  
510  C  C   . SER A 56  ? 0.3055 0.1445 0.1377 0.0078  -0.0386 -0.0111 56  SER A C   
511  O  O   . SER A 56  ? 0.3350 0.1512 0.1353 0.0401  -0.0557 -0.0037 56  SER A O   
512  C  CB  . SER A 56  ? 0.2903 0.1244 0.1328 -0.0091 -0.0714 -0.0151 56  SER A CB  
513  O  OG  . SER A 56  ? 0.3648 0.1180 0.1569 -0.0146 -0.0693 -0.0153 56  SER A OG  
514  N  N   . LEU A 57  ? 0.2714 0.1260 0.0973 0.0258  -0.0125 0.0148  57  LEU A N   
515  C  CA  . LEU A 57  ? 0.3209 0.1598 0.1281 0.0274  -0.0062 0.0062  57  LEU A CA  
516  C  C   . LEU A 57  ? 0.2879 0.1424 0.1397 0.0243  0.0031  0.0057  57  LEU A C   
517  O  O   . LEU A 57  ? 0.3456 0.1544 0.1062 0.0311  -0.0115 0.0171  57  LEU A O   
518  C  CB  . LEU A 57  ? 0.3547 0.1888 0.1375 0.0176  0.0174  0.0086  57  LEU A CB  
519  C  CG  . LEU A 57  ? 0.3634 0.2294 0.1741 0.0439  -0.0153 -0.0003 57  LEU A CG  
520  C  CD1 . LEU A 57  ? 0.4093 0.2628 0.2842 -0.0390 0.0346  0.0006  57  LEU A CD1 
521  C  CD2 . LEU A 57  ? 0.4333 0.2003 0.2082 0.0689  -0.0176 0.0131  57  LEU A CD2 
522  N  N   . ARG A 58  ? 0.2872 0.1567 0.1307 0.0333  -0.0093 0.0322  58  ARG A N   
523  C  CA  . ARG A 58  ? 0.2752 0.0983 0.1568 0.0222  -0.0051 0.0410  58  ARG A CA  
524  C  C   . ARG A 58  ? 0.2666 0.0953 0.1307 0.0073  0.0027  0.0366  58  ARG A C   
525  O  O   . ARG A 58  ? 0.2681 0.1194 0.1363 0.0176  -0.0032 0.0386  58  ARG A O   
526  C  CB  . ARG A 58  ? 0.2576 0.1790 0.1754 0.0127  -0.0109 0.0274  58  ARG A CB  
527  C  CG  . ARG A 58  ? 0.2225 0.1802 0.2394 -0.0298 0.0000  0.0403  58  ARG A CG  
528  C  CD  . ARG A 58  ? 0.2517 0.2352 0.2390 -0.0568 -0.0252 0.0441  58  ARG A CD  
529  N  NE  . ARG A 58  ? 0.1379 0.1898 0.2250 -0.0368 -0.0266 0.0571  58  ARG A NE  
530  C  CZ  . ARG A 58  ? 0.1075 0.2189 0.1934 -0.0615 0.0097  0.0535  58  ARG A CZ  
531  N  NH1 . ARG A 58  ? 0.2295 0.2406 0.1705 -0.0294 -0.0073 0.0177  58  ARG A NH1 
532  N  NH2 . ARG A 58  ? 0.1591 0.1835 0.2585 -0.0256 -0.0159 0.0222  58  ARG A NH2 
533  N  N   . ILE A 59  ? 0.2851 0.0824 0.1063 0.0173  -0.0041 0.0193  59  ILE A N   
534  C  CA  . ILE A 59  ? 0.2633 0.1097 0.1110 0.0102  -0.0342 0.0003  59  ILE A CA  
535  C  C   . ILE A 59  ? 0.2526 0.1036 0.0904 0.0032  -0.0287 0.0131  59  ILE A C   
536  O  O   . ILE A 59  ? 0.2969 0.1562 0.0682 0.0037  -0.0007 0.0163  59  ILE A O   
537  C  CB  . ILE A 59  ? 0.2728 0.1036 0.0955 0.0013  -0.0559 -0.0146 59  ILE A CB  
538  C  CG1 . ILE A 59  ? 0.3192 0.1102 0.0622 0.0080  -0.0167 0.0540  59  ILE A CG1 
539  C  CG2 . ILE A 59  ? 0.3263 0.1652 0.0551 0.0024  -0.0537 0.0096  59  ILE A CG2 
540  C  CD1 . ILE A 59  ? 0.2768 0.1260 0.0984 -0.0063 0.0031  0.0086  59  ILE A CD1 
541  N  N   . LEU A 60  ? 0.2377 0.1414 0.1001 -0.0121 -0.0450 0.0109  60  LEU A N   
542  C  CA  . LEU A 60  ? 0.2458 0.0937 0.1104 -0.0266 -0.0241 0.0215  60  LEU A CA  
543  C  C   . LEU A 60  ? 0.2380 0.1037 0.1190 -0.0253 -0.0207 -0.0074 60  LEU A C   
544  O  O   . LEU A 60  ? 0.2178 0.1111 0.0892 -0.0346 -0.0122 0.0083  60  LEU A O   
545  C  CB  . LEU A 60  ? 0.2637 0.1052 0.1864 -0.0263 -0.0164 -0.0001 60  LEU A CB  
546  C  CG  . LEU A 60  ? 0.2850 0.1413 0.1551 -0.0208 -0.0355 0.0168  60  LEU A CG  
547  C  CD1 . LEU A 60  ? 0.2627 0.1521 0.1726 -0.0445 -0.0151 -0.0021 60  LEU A CD1 
548  C  CD2 . LEU A 60  ? 0.2742 0.0888 0.1867 -0.0388 -0.0287 -0.0122 60  LEU A CD2 
549  N  N   . ASN A 61  ? 0.2355 0.1089 0.0883 -0.0568 -0.0024 -0.0093 61  ASN A N   
550  C  CA  . ASN A 61  ? 0.2171 0.0861 0.1282 -0.0366 0.0168  -0.0234 61  ASN A CA  
551  C  C   . ASN A 61  ? 0.2484 0.1249 0.1155 -0.0482 0.0140  -0.0007 61  ASN A C   
552  O  O   . ASN A 61  ? 0.2919 0.1454 0.1196 -0.0601 0.0066  0.0281  61  ASN A O   
553  C  CB  . ASN A 61  ? 0.2583 0.1041 0.1133 -0.0414 0.0261  -0.0239 61  ASN A CB  
554  C  CG  . ASN A 61  ? 0.2233 0.1389 0.1331 -0.0361 0.0043  0.0066  61  ASN A CG  
555  O  OD1 . ASN A 61  ? 0.2416 0.1249 0.1510 -0.0494 0.0146  -0.0071 61  ASN A OD1 
556  N  ND2 . ASN A 61  ? 0.2843 0.1838 0.1104 -0.0392 0.0604  -0.0104 61  ASN A ND2 
557  N  N   . ASN A 62  ? 0.2437 0.1275 0.1142 -0.0502 -0.0154 -0.0059 62  ASN A N   
558  C  CA  . ASN A 62  ? 0.2327 0.1539 0.0646 -0.0614 -0.0194 0.0021  62  ASN A CA  
559  C  C   . ASN A 62  ? 0.2352 0.1621 0.1167 -0.0522 0.0130  0.0012  62  ASN A C   
560  O  O   . ASN A 62  ? 0.3149 0.2031 0.1959 -0.0993 0.0030  0.0155  62  ASN A O   
561  C  CB  . ASN A 62  ? 0.2736 0.1208 0.1446 -0.0357 -0.0114 0.0130  62  ASN A CB  
562  C  CG  . ASN A 62  ? 0.2670 0.1555 0.0840 -0.0577 -0.0096 0.0006  62  ASN A CG  
563  O  OD1 . ASN A 62  ? 0.2491 0.1097 0.1194 -0.0450 0.0165  -0.0136 62  ASN A OD1 
564  N  ND2 . ASN A 62  ? 0.3677 0.1729 0.1407 -0.0511 0.0456  -0.0189 62  ASN A ND2 
565  N  N   . GLY A 63  ? 0.2374 0.1454 0.1231 -0.0522 0.0200  -0.0057 63  GLY A N   
566  C  CA  . GLY A 63  ? 0.1930 0.1564 0.1000 -0.0551 0.0357  0.0277  63  GLY A CA  
567  C  C   . GLY A 63  ? 0.1869 0.1837 0.1547 -0.0476 0.0233  0.0102  63  GLY A C   
568  O  O   . GLY A 63  ? 0.1706 0.1937 0.1086 -0.0232 0.0533  -0.0258 63  GLY A O   
569  N  N   . HIS A 64  ? 0.1548 0.1510 0.1152 -0.0432 0.0524  0.0087  64  HIS A N   
570  C  CA  . HIS A 64  ? 0.1540 0.1769 0.1237 -0.0304 0.0299  0.0074  64  HIS A CA  
571  C  C   . HIS A 64  ? 0.1431 0.1467 0.1553 -0.0317 0.0148  0.0280  64  HIS A C   
572  O  O   . HIS A 64  ? 0.1442 0.1801 0.2469 -0.0168 -0.0035 0.0865  64  HIS A O   
573  C  CB  . HIS A 64  ? 0.1632 0.1913 0.1780 -0.0635 -0.0055 -0.0023 64  HIS A CB  
574  C  CG  . HIS A 64  ? 0.2410 0.2273 0.1827 -0.0412 0.0121  0.0297  64  HIS A CG  
575  N  ND1 . HIS A 64  ? 0.2143 0.2617 0.1888 -0.0288 0.0465  -0.0592 64  HIS A ND1 
576  C  CD2 . HIS A 64  ? 0.2585 0.1838 0.1931 -0.0672 0.0020  0.0121  64  HIS A CD2 
577  C  CE1 . HIS A 64  ? 0.2476 0.3179 0.1833 -0.0829 0.0355  0.0003  64  HIS A CE1 
578  N  NE2 . HIS A 64  ? 0.2458 0.3131 0.2020 -0.0597 0.0254  -0.0082 64  HIS A NE2 
579  N  N   . ALA A 65  ? 0.1465 0.1137 0.1174 -0.0099 0.0182  -0.0046 65  ALA A N   
580  C  CA  . ALA A 65  ? 0.1560 0.1306 0.1262 -0.0192 0.0076  0.0057  65  ALA A CA  
581  C  C   . ALA A 65  ? 0.1615 0.1102 0.0754 -0.0242 0.0023  -0.0331 65  ALA A C   
582  O  O   . ALA A 65  ? 0.1722 0.1206 0.1361 -0.0193 0.0428  0.0074  65  ALA A O   
583  C  CB  . ALA A 65  ? 0.1244 0.1293 0.1101 -0.0173 -0.0020 0.0057  65  ALA A CB  
584  N  N   . PHE A 66  ? 0.1400 0.1163 0.1134 -0.0024 -0.0046 0.0032  66  PHE A N   
585  C  CA  . PHE A 66  ? 0.1486 0.1289 0.1116 -0.0167 -0.0208 -0.0034 66  PHE A CA  
586  C  C   . PHE A 66  ? 0.1697 0.1049 0.1090 -0.0054 -0.0167 0.0083  66  PHE A C   
587  O  O   . PHE A 66  ? 0.1852 0.0815 0.1075 -0.0300 -0.0096 0.0188  66  PHE A O   
588  C  CB  . PHE A 66  ? 0.1320 0.1435 0.0930 -0.0379 -0.0214 0.0348  66  PHE A CB  
589  C  CG  . PHE A 66  ? 0.1937 0.1399 0.0632 -0.0483 -0.0074 0.0204  66  PHE A CG  
590  C  CD1 . PHE A 66  ? 0.2142 0.1891 0.0768 -0.0303 -0.0181 0.0146  66  PHE A CD1 
591  C  CD2 . PHE A 66  ? 0.2046 0.1312 0.0544 -0.0274 -0.0024 -0.0287 66  PHE A CD2 
592  C  CE1 . PHE A 66  ? 0.1794 0.1471 0.1088 -0.0430 -0.0103 -0.0262 66  PHE A CE1 
593  C  CE2 . PHE A 66  ? 0.1928 0.1097 0.0992 -0.0595 -0.0189 -0.0028 66  PHE A CE2 
594  C  CZ  . PHE A 66  ? 0.1744 0.1500 0.1118 -0.0348 -0.0419 -0.0086 66  PHE A CZ  
595  N  N   . ASN A 67  ? 0.1537 0.0930 0.0949 -0.0068 -0.0399 0.0285  67  ASN A N   
596  C  CA  . ASN A 67  ? 0.1945 0.0637 0.0967 -0.0188 -0.0285 0.0077  67  ASN A CA  
597  C  C   . ASN A 67  ? 0.1891 0.0874 0.1059 -0.0210 -0.0293 0.0151  67  ASN A C   
598  O  O   . ASN A 67  ? 0.2298 0.1411 0.0666 -0.0226 -0.0093 0.0256  67  ASN A O   
599  C  CB  . ASN A 67  ? 0.1709 0.0847 0.1349 -0.0599 -0.0315 0.0160  67  ASN A CB  
600  C  CG  . ASN A 67  ? 0.1634 0.1171 0.1399 -0.0498 -0.0087 0.0137  67  ASN A CG  
601  O  OD1 . ASN A 67  ? 0.2344 0.1391 0.1289 -0.0838 -0.0443 0.0474  67  ASN A OD1 
602  N  ND2 . ASN A 67  ? 0.2179 0.1892 0.2002 -0.1014 -0.0027 -0.0010 67  ASN A ND2 
603  N  N   . VAL A 68  ? 0.1912 0.0671 0.0925 0.0017  -0.0331 0.0073  68  VAL A N   
604  C  CA  . VAL A 68  ? 0.2081 0.0878 0.0795 0.0436  -0.0430 0.0028  68  VAL A CA  
605  C  C   . VAL A 68  ? 0.2592 0.1089 0.1324 0.0472  -0.0195 0.0060  68  VAL A C   
606  O  O   . VAL A 68  ? 0.2527 0.0987 0.0993 0.0370  -0.0303 0.0263  68  VAL A O   
607  C  CB  . VAL A 68  ? 0.2180 0.1122 0.0901 0.0381  -0.0342 -0.0059 68  VAL A CB  
608  C  CG1 . VAL A 68  ? 0.1984 0.1192 0.1251 0.0527  -0.0781 -0.0166 68  VAL A CG1 
609  C  CG2 . VAL A 68  ? 0.2013 0.0917 0.1244 0.0335  -0.0282 -0.0370 68  VAL A CG2 
610  N  N   . GLU A 69  ? 0.2831 0.0940 0.1093 0.0198  -0.0054 0.0041  69  GLU A N   
611  C  CA  . GLU A 69  ? 0.2624 0.1111 0.1208 0.0242  -0.0107 0.0063  69  GLU A CA  
612  C  C   . GLU A 69  ? 0.2960 0.1324 0.1518 0.0476  -0.0281 0.0240  69  GLU A C   
613  O  O   . GLU A 69  ? 0.3485 0.1321 0.1457 0.0489  -0.0579 0.0307  69  GLU A O   
614  C  CB  . GLU A 69  ? 0.2644 0.1345 0.1982 0.0225  0.0017  0.0303  69  GLU A CB  
615  C  CG  . GLU A 69  ? 0.1837 0.1576 0.1569 0.0127  0.0305  0.0283  69  GLU A CG  
616  C  CD  . GLU A 69  ? 0.2617 0.1877 0.1849 0.0181  0.0229  0.0065  69  GLU A CD  
617  O  OE1 . GLU A 69  ? 0.2016 0.1989 0.2290 0.0037  -0.0137 0.0313  69  GLU A OE1 
618  O  OE2 . GLU A 69  ? 0.2198 0.1622 0.2286 0.0041  -0.0010 0.0597  69  GLU A OE2 
619  N  N   . PHE A 70  ? 0.2746 0.1167 0.1278 0.0212  -0.0020 0.0388  70  PHE A N   
620  C  CA  . PHE A 70  ? 0.2416 0.0863 0.1386 0.0093  -0.0326 0.0233  70  PHE A CA  
621  C  C   . PHE A 70  ? 0.2246 0.1036 0.1345 0.0105  -0.0306 0.0164  70  PHE A C   
622  O  O   . PHE A 70  ? 0.2398 0.1061 0.1420 0.0108  -0.0595 0.0266  70  PHE A O   
623  C  CB  . PHE A 70  ? 0.2261 0.0982 0.1064 -0.0142 -0.0261 0.0218  70  PHE A CB  
624  C  CG  . PHE A 70  ? 0.1779 0.1111 0.1339 0.0170  -0.0548 0.0288  70  PHE A CG  
625  C  CD1 . PHE A 70  ? 0.2097 0.1025 0.0917 0.0285  -0.0456 -0.0046 70  PHE A CD1 
626  C  CD2 . PHE A 70  ? 0.1741 0.1431 0.1248 -0.0006 -0.0399 0.0175  70  PHE A CD2 
627  C  CE1 . PHE A 70  ? 0.2384 0.1307 0.1447 0.0032  -0.0331 -0.0155 70  PHE A CE1 
628  C  CE2 . PHE A 70  ? 0.1914 0.1231 0.0881 0.0328  -0.0348 0.0348  70  PHE A CE2 
629  C  CZ  . PHE A 70  ? 0.2128 0.0964 0.1052 0.0209  0.0194  0.0097  70  PHE A CZ  
630  N  N   A ASP A 71  ? 0.2387 0.1059 0.1719 0.0221  -0.0308 0.0171  71  ASP A N   
631  N  N   B ASP A 71  ? 0.2377 0.0971 0.1747 0.0221  -0.0377 0.0199  71  ASP A N   
632  C  CA  A ASP A 71  ? 0.2287 0.1074 0.1650 0.0248  -0.0121 0.0208  71  ASP A CA  
633  C  CA  B ASP A 71  ? 0.2187 0.0885 0.1659 0.0236  -0.0300 0.0317  71  ASP A CA  
634  C  C   A ASP A 71  ? 0.2355 0.1086 0.2004 0.0078  -0.0211 0.0205  71  ASP A C   
635  C  C   B ASP A 71  ? 0.2259 0.1022 0.2017 0.0057  -0.0313 0.0259  71  ASP A C   
636  O  O   A ASP A 71  ? 0.2526 0.1280 0.2337 0.0206  0.0054  0.0206  71  ASP A O   
637  O  O   B ASP A 71  ? 0.2165 0.1336 0.2038 0.0127  -0.0315 0.0377  71  ASP A O   
638  C  CB  A ASP A 71  ? 0.2143 0.1293 0.1783 0.0289  -0.0196 0.0238  71  ASP A CB  
639  C  CB  B ASP A 71  ? 0.1896 0.0795 0.1903 0.0399  -0.0469 0.0287  71  ASP A CB  
640  C  CG  A ASP A 71  ? 0.2070 0.1368 0.1633 0.0229  -0.0154 0.0163  71  ASP A CG  
641  C  CG  B ASP A 71  ? 0.2122 0.0951 0.1777 0.0182  -0.0274 0.0485  71  ASP A CG  
642  O  OD1 A ASP A 71  ? 0.2036 0.1133 0.2248 0.0201  -0.0129 0.0308  71  ASP A OD1 
643  O  OD1 B ASP A 71  ? 0.2750 0.1490 0.2196 0.0165  -0.0157 0.0386  71  ASP A OD1 
644  O  OD2 A ASP A 71  ? 0.2415 0.2114 0.2345 0.0183  -0.0546 0.0340  71  ASP A OD2 
645  O  OD2 B ASP A 71  ? 0.2243 0.1611 0.2875 0.0282  -0.0450 0.0340  71  ASP A OD2 
646  N  N   . ASP A 72  ? 0.2395 0.0813 0.1955 -0.0015 -0.0445 0.0241  72  ASP A N   
647  C  CA  . ASP A 72  ? 0.2268 0.0957 0.2172 -0.0104 -0.0194 0.0065  72  ASP A CA  
648  C  C   . ASP A 72  ? 0.2431 0.1164 0.2449 -0.0110 -0.0339 0.0174  72  ASP A C   
649  O  O   . ASP A 72  ? 0.3047 0.1291 0.2348 -0.0049 -0.0359 0.0066  72  ASP A O   
650  C  CB  . ASP A 72  ? 0.2423 0.1118 0.2132 -0.0250 -0.0160 0.0272  72  ASP A CB  
651  C  CG  . ASP A 72  ? 0.2126 0.1314 0.2067 0.0006  -0.0276 -0.0203 72  ASP A CG  
652  O  OD1 . ASP A 72  ? 0.1982 0.1842 0.2401 -0.0143 -0.0480 0.0438  72  ASP A OD1 
653  O  OD2 . ASP A 72  ? 0.2648 0.1816 0.1357 -0.0240 -0.0318 0.0154  72  ASP A OD2 
654  N  N   . SER A 73  ? 0.2688 0.0964 0.2680 -0.0024 -0.0362 0.0252  73  SER A N   
655  C  CA  . SER A 73  ? 0.2711 0.1343 0.2792 0.0065  -0.0223 0.0136  73  SER A CA  
656  C  C   . SER A 73  ? 0.2903 0.1641 0.2980 0.0031  0.0021  -0.0020 73  SER A C   
657  O  O   . SER A 73  ? 0.2860 0.1172 0.3106 -0.0085 -0.0111 0.0104  73  SER A O   
658  C  CB  . SER A 73  ? 0.3080 0.1716 0.3109 0.0038  -0.0076 0.0238  73  SER A CB  
659  O  OG  . SER A 73  ? 0.2955 0.1342 0.3325 0.0243  0.0131  0.0566  73  SER A OG  
660  N  N   . GLN A 74  ? 0.2718 0.1564 0.3141 0.0057  0.0046  -0.0087 74  GLN A N   
661  C  CA  . GLN A 74  ? 0.2764 0.2410 0.3123 -0.0031 -0.0005 -0.0013 74  GLN A CA  
662  C  C   . GLN A 74  ? 0.2572 0.2495 0.2664 0.0006  -0.0286 -0.0142 74  GLN A C   
663  O  O   . GLN A 74  ? 0.2158 0.1953 0.2639 -0.0065 -0.0542 -0.0007 74  GLN A O   
664  C  CB  . GLN A 74  ? 0.2863 0.2540 0.3276 0.0296  0.0073  0.0210  74  GLN A CB  
665  C  CG  . GLN A 74  ? 0.3490 0.3495 0.3565 0.0111  0.0216  0.0313  74  GLN A CG  
666  C  CD  . GLN A 74  ? 0.4093 0.3921 0.4164 0.0013  0.0060  0.0406  74  GLN A CD  
667  O  OE1 . GLN A 74  ? 0.4185 0.3671 0.4399 -0.0093 -0.0215 0.0154  74  GLN A OE1 
668  N  NE2 . GLN A 74  ? 0.4564 0.4932 0.4933 0.0217  0.0273  0.0286  74  GLN A NE2 
669  N  N   A ASP A 75  ? 0.2664 0.2612 0.2711 0.0034  -0.0270 -0.0198 75  ASP A N   
670  N  N   B ASP A 75  ? 0.2518 0.2473 0.2705 -0.0013 -0.0306 -0.0219 75  ASP A N   
671  C  CA  A ASP A 75  ? 0.2541 0.2711 0.2621 -0.0048 -0.0284 -0.0183 75  ASP A CA  
672  C  CA  B ASP A 75  ? 0.2401 0.2401 0.2628 -0.0062 -0.0348 -0.0071 75  ASP A CA  
673  C  C   A ASP A 75  ? 0.2606 0.2667 0.2685 -0.0013 -0.0342 -0.0010 75  ASP A C   
674  C  C   B ASP A 75  ? 0.2496 0.2565 0.2832 -0.0054 -0.0445 -0.0027 75  ASP A C   
675  O  O   A ASP A 75  ? 0.2711 0.3192 0.2678 -0.0102 -0.0221 -0.0010 75  ASP A O   
676  O  O   B ASP A 75  ? 0.2670 0.2879 0.3019 0.0188  -0.0557 0.0373  75  ASP A O   
677  C  CB  A ASP A 75  ? 0.2827 0.2978 0.2820 0.0024  -0.0164 -0.0082 75  ASP A CB  
678  C  CB  B ASP A 75  ? 0.2345 0.2581 0.2617 -0.0010 -0.0303 -0.0024 75  ASP A CB  
679  C  CG  A ASP A 75  ? 0.2504 0.2390 0.2329 0.0121  -0.0060 -0.0013 75  ASP A CG  
680  C  CG  B ASP A 75  ? 0.2795 0.2462 0.2696 -0.0126 0.0035  -0.0086 75  ASP A CG  
681  O  OD1 A ASP A 75  ? 0.1894 0.3244 0.1690 0.0236  0.0267  0.0315  75  ASP A OD1 
682  O  OD1 B ASP A 75  ? 0.3637 0.3303 0.3230 0.0082  0.0439  -0.0390 75  ASP A OD1 
683  O  OD2 A ASP A 75  ? 0.3036 0.2939 0.3321 0.0188  -0.0052 0.0173  75  ASP A OD2 
684  O  OD2 B ASP A 75  ? 0.1391 0.1909 0.3345 0.0201  -0.0062 0.0115  75  ASP A OD2 
685  N  N   . LYS A 76  ? 0.2599 0.2343 0.2563 0.0109  -0.0636 0.0185  76  LYS A N   
686  C  CA  . LYS A 76  ? 0.2695 0.2289 0.2915 -0.0012 -0.0482 0.0181  76  LYS A CA  
687  C  C   . LYS A 76  ? 0.2886 0.2624 0.3080 0.0062  -0.0619 0.0205  76  LYS A C   
688  O  O   . LYS A 76  ? 0.3273 0.3076 0.3659 0.0109  -0.0856 0.0274  76  LYS A O   
689  C  CB  . LYS A 76  ? 0.2998 0.2050 0.2734 -0.0157 -0.0542 0.0065  76  LYS A CB  
690  C  CG  . LYS A 76  ? 0.3615 0.2329 0.3404 0.0194  -0.0178 0.0216  76  LYS A CG  
691  C  CD  . LYS A 76  ? 0.3260 0.2383 0.3088 -0.0119 -0.0351 0.0151  76  LYS A CD  
692  C  CE  . LYS A 76  ? 0.3774 0.2889 0.3192 0.0102  -0.0223 0.0324  76  LYS A CE  
693  N  NZ  . LYS A 76  ? 0.3698 0.3156 0.3411 0.0390  -0.0105 -0.0109 76  LYS A NZ  
694  N  N   . ALA A 77  ? 0.2469 0.2667 0.2440 0.0318  -0.0979 0.0120  77  ALA A N   
695  C  CA  . ALA A 77  ? 0.2169 0.2201 0.1626 -0.0109 -0.0692 -0.0041 77  ALA A CA  
696  C  C   . ALA A 77  ? 0.1781 0.1991 0.1888 -0.0086 -0.0658 -0.0142 77  ALA A C   
697  O  O   . ALA A 77  ? 0.1942 0.2499 0.2354 -0.0163 -0.0649 -0.0615 77  ALA A O   
698  C  CB  . ALA A 77  ? 0.2649 0.2301 0.1403 0.0153  -0.0640 -0.0142 77  ALA A CB  
699  N  N   . VAL A 78  ? 0.1585 0.1561 0.1658 -0.0085 -0.0855 0.0105  78  VAL A N   
700  C  CA  . VAL A 78  ? 0.1621 0.1569 0.1813 -0.0024 -0.0491 0.0200  78  VAL A CA  
701  C  C   . VAL A 78  ? 0.1167 0.1379 0.1888 -0.0152 -0.0370 0.0080  78  VAL A C   
702  O  O   . VAL A 78  ? 0.1134 0.1449 0.2380 -0.0286 -0.0595 0.0249  78  VAL A O   
703  C  CB  . VAL A 78  ? 0.2094 0.2175 0.2273 -0.0041 -0.0353 0.0141  78  VAL A CB  
704  C  CG1 . VAL A 78  ? 0.2925 0.1806 0.2671 0.0024  -0.0315 0.0156  78  VAL A CG1 
705  C  CG2 . VAL A 78  ? 0.1712 0.1844 0.2574 0.0037  0.0041  -0.0015 78  VAL A CG2 
706  N  N   . LEU A 79  ? 0.1217 0.1210 0.1586 0.0204  -0.0219 0.0188  79  LEU A N   
707  C  CA  . LEU A 79  ? 0.1296 0.1324 0.1571 0.0098  -0.0041 0.0077  79  LEU A CA  
708  C  C   . LEU A 79  ? 0.1149 0.1400 0.1392 -0.0013 0.0074  0.0140  79  LEU A C   
709  O  O   . LEU A 79  ? 0.1201 0.1479 0.1816 -0.0295 0.0082  -0.0130 79  LEU A O   
710  C  CB  . LEU A 79  ? 0.1058 0.1569 0.1741 0.0177  -0.0219 0.0394  79  LEU A CB  
711  C  CG  . LEU A 79  ? 0.1410 0.1454 0.1942 -0.0104 -0.0115 0.0076  79  LEU A CG  
712  C  CD1 . LEU A 79  ? 0.1050 0.1878 0.2800 -0.0344 0.0073  0.0406  79  LEU A CD1 
713  C  CD2 . LEU A 79  ? 0.0813 0.1598 0.1589 0.0511  0.0091  0.0198  79  LEU A CD2 
714  N  N   . LYS A 80  ? 0.1463 0.1458 0.1661 -0.0092 0.0143  -0.0110 80  LYS A N   
715  C  CA  . LYS A 80  ? 0.1486 0.1472 0.1906 0.0049  0.0087  0.0031  80  LYS A CA  
716  C  C   . LYS A 80  ? 0.1181 0.1607 0.1812 0.0021  0.0137  -0.0057 80  LYS A C   
717  O  O   . LYS A 80  ? 0.1050 0.1303 0.2110 -0.0006 -0.0083 -0.0003 80  LYS A O   
718  C  CB  . LYS A 80  ? 0.2079 0.2118 0.2616 0.0109  -0.0124 0.0020  80  LYS A CB  
719  C  CG  . LYS A 80  ? 0.1986 0.2194 0.2374 0.0293  -0.0230 -0.0024 80  LYS A CG  
720  C  CD  . LYS A 80  ? 0.2038 0.2178 0.3440 0.0242  -0.0195 0.0127  80  LYS A CD  
721  C  CE  . LYS A 80  ? 0.2456 0.3363 0.4068 0.0153  -0.0077 0.0251  80  LYS A CE  
722  N  NZ  . LYS A 80  ? 0.4284 0.4794 0.4751 0.0031  0.0305  0.0344  80  LYS A NZ  
723  N  N   . GLY A 81  ? 0.1386 0.2125 0.1471 0.0015  0.0080  0.0027  81  GLY A N   
724  C  CA  . GLY A 81  ? 0.1159 0.1837 0.1840 0.0275  0.0340  0.0060  81  GLY A CA  
725  C  C   . GLY A 81  ? 0.1537 0.1677 0.2114 0.0120  0.0092  0.0147  81  GLY A C   
726  O  O   . GLY A 81  ? 0.1386 0.1525 0.1997 -0.0076 -0.0132 -0.0037 81  GLY A O   
727  N  N   . GLY A 82  ? 0.1668 0.1672 0.2323 0.0077  0.0015  0.0087  82  GLY A N   
728  C  CA  . GLY A 82  ? 0.1741 0.1436 0.2458 0.0035  -0.0111 0.0199  82  GLY A CA  
729  C  C   . GLY A 82  ? 0.1700 0.1590 0.1892 0.0373  0.0165  -0.0012 82  GLY A C   
730  O  O   . GLY A 82  ? 0.1896 0.2402 0.2311 0.0425  0.0370  -0.0135 82  GLY A O   
731  N  N   . PRO A 83  ? 0.1327 0.1474 0.2006 0.0232  0.0130  -0.0026 83  PRO A N   
732  C  CA  . PRO A 83  ? 0.1203 0.1465 0.1655 0.0375  0.0161  -0.0023 83  PRO A CA  
733  C  C   . PRO A 83  ? 0.1535 0.1871 0.1905 0.0189  0.0223  -0.0190 83  PRO A C   
734  O  O   . PRO A 83  ? 0.1562 0.2431 0.1996 0.0007  -0.0131 0.0065  83  PRO A O   
735  C  CB  . PRO A 83  ? 0.1600 0.1744 0.2022 0.0500  0.0163  -0.0057 83  PRO A CB  
736  C  CG  . PRO A 83  ? 0.1393 0.1639 0.1465 0.0189  0.0263  0.0164  83  PRO A CG  
737  C  CD  . PRO A 83  ? 0.1167 0.1324 0.1744 0.0153  0.0355  -0.0198 83  PRO A CD  
738  N  N   . LEU A 84  ? 0.1490 0.1632 0.1888 0.0230  0.0264  -0.0175 84  LEU A N   
739  C  CA  . LEU A 84  ? 0.1769 0.1143 0.1985 0.0292  0.0201  -0.0456 84  LEU A CA  
740  C  C   . LEU A 84  ? 0.1870 0.1690 0.2313 0.0318  0.0132  -0.0542 84  LEU A C   
741  O  O   . LEU A 84  ? 0.1992 0.1675 0.2435 0.0065  0.0507  -0.0737 84  LEU A O   
742  C  CB  . LEU A 84  ? 0.1439 0.1092 0.1820 0.0245  0.0093  -0.0284 84  LEU A CB  
743  C  CG  . LEU A 84  ? 0.0820 0.1077 0.1684 0.0135  0.0162  -0.0322 84  LEU A CG  
744  C  CD1 . LEU A 84  ? 0.1328 0.1458 0.1756 0.0077  0.0205  -0.0474 84  LEU A CD1 
745  C  CD2 . LEU A 84  ? 0.1050 0.1163 0.2279 0.0258  0.0219  -0.0597 84  LEU A CD2 
746  N  N   . ASP A 85  ? 0.2146 0.1377 0.2541 0.0256  0.0199  -0.0689 85  ASP A N   
747  C  CA  . ASP A 85  ? 0.2876 0.1837 0.2990 -0.0048 -0.0099 -0.0388 85  ASP A CA  
748  C  C   . ASP A 85  ? 0.2601 0.1529 0.2998 -0.0219 0.0076  -0.0307 85  ASP A C   
749  O  O   . ASP A 85  ? 0.3282 0.2146 0.2872 -0.0132 0.0154  -0.0421 85  ASP A O   
750  C  CB  . ASP A 85  ? 0.3409 0.1952 0.2879 0.0182  -0.0148 -0.0566 85  ASP A CB  
751  C  CG  . ASP A 85  ? 0.3569 0.3278 0.3795 0.0205  0.0006  -0.0207 85  ASP A CG  
752  O  OD1 . ASP A 85  ? 0.4266 0.4322 0.4416 -0.0065 0.0175  0.0040  85  ASP A OD1 
753  O  OD2 . ASP A 85  ? 0.3553 0.4251 0.4150 0.0159  -0.0015 -0.0465 85  ASP A OD2 
754  N  N   . GLY A 86  ? 0.2610 0.2226 0.3163 -0.0575 -0.0066 -0.0222 86  GLY A N   
755  C  CA  . GLY A 86  ? 0.2440 0.2067 0.2522 -0.0502 0.0082  -0.0350 86  GLY A CA  
756  C  C   . GLY A 86  ? 0.2345 0.1788 0.2326 -0.0328 -0.0006 -0.0261 86  GLY A C   
757  O  O   . GLY A 86  ? 0.3091 0.2460 0.2446 -0.0864 -0.0015 -0.0273 86  GLY A O   
758  N  N   A THR A 87  ? 0.1949 0.1697 0.1995 -0.0013 0.0173  -0.0303 87  THR A N   
759  N  N   B THR A 87  ? 0.1967 0.1544 0.1851 -0.0034 0.0227  -0.0335 87  THR A N   
760  C  CA  A THR A 87  ? 0.1546 0.1781 0.2013 0.0140  0.0196  -0.0197 87  THR A CA  
761  C  CA  B THR A 87  ? 0.1571 0.1510 0.1788 0.0081  0.0195  -0.0137 87  THR A CA  
762  C  C   A THR A 87  ? 0.1146 0.1515 0.1887 0.0074  0.0032  -0.0303 87  THR A C   
763  C  C   B THR A 87  ? 0.1307 0.1352 0.1762 0.0085  0.0043  -0.0259 87  THR A C   
764  O  O   A THR A 87  ? 0.0797 0.1241 0.1816 0.0038  0.0082  -0.0335 87  THR A O   
765  O  O   B THR A 87  ? 0.1511 0.0725 0.1596 0.0184  -0.0110 -0.0261 87  THR A O   
766  C  CB  A THR A 87  ? 0.1647 0.1993 0.2212 0.0205  0.0187  -0.0189 87  THR A CB  
767  C  CB  B THR A 87  ? 0.1655 0.1661 0.1797 0.0015  0.0195  -0.0024 87  THR A CB  
768  O  OG1 A THR A 87  ? 0.1741 0.1949 0.2261 0.0560  0.0359  -0.0361 87  THR A OG1 
769  O  OG1 B THR A 87  ? 0.1389 0.1309 0.2079 -0.0151 0.0509  -0.0031 87  THR A OG1 
770  C  CG2 A THR A 87  ? 0.1813 0.1803 0.2125 0.0068  -0.0010 -0.0109 87  THR A CG2 
771  C  CG2 B THR A 87  ? 0.1605 0.1270 0.1841 -0.0225 0.0395  -0.0122 87  THR A CG2 
772  N  N   . TYR A 88  ? 0.0955 0.1241 0.1756 0.0172  -0.0003 -0.0289 88  TYR A N   
773  C  CA  . TYR A 88  ? 0.0820 0.1124 0.1454 0.0152  -0.0089 -0.0299 88  TYR A CA  
774  C  C   . TYR A 88  ? 0.0984 0.1244 0.1603 0.0031  -0.0313 -0.0087 88  TYR A C   
775  O  O   . TYR A 88  ? 0.1162 0.1654 0.2000 -0.0671 -0.0331 0.0196  88  TYR A O   
776  C  CB  . TYR A 88  ? 0.0860 0.1016 0.1773 0.0293  -0.0342 -0.0174 88  TYR A CB  
777  C  CG  . TYR A 88  ? 0.1004 0.0779 0.1414 0.0216  -0.0315 0.0041  88  TYR A CG  
778  C  CD1 . TYR A 88  ? 0.0942 0.1074 0.1443 0.0070  -0.0377 -0.0379 88  TYR A CD1 
779  C  CD2 . TYR A 88  ? 0.0892 0.0504 0.1668 0.0282  -0.0344 0.0091  88  TYR A CD2 
780  C  CE1 . TYR A 88  ? 0.0761 0.1061 0.1385 0.0043  -0.0010 -0.0239 88  TYR A CE1 
781  C  CE2 . TYR A 88  ? 0.0887 0.0479 0.1127 0.0023  -0.0142 -0.0244 88  TYR A CE2 
782  C  CZ  . TYR A 88  ? 0.1291 0.0698 0.1399 0.0214  -0.0211 -0.0296 88  TYR A CZ  
783  O  OH  . TYR A 88  ? 0.0980 0.1168 0.1025 0.0080  -0.0034 -0.0060 88  TYR A OH  
784  N  N   . ARG A 89  ? 0.1049 0.1034 0.1299 0.0188  -0.0174 -0.0178 89  ARG A N   
785  C  CA  . ARG A 89  ? 0.1438 0.0785 0.1451 0.0013  -0.0280 0.0192  89  ARG A CA  
786  C  C   . ARG A 89  ? 0.0919 0.0758 0.0910 -0.0032 -0.0231 0.0006  89  ARG A C   
787  O  O   . ARG A 89  ? 0.0788 0.0786 0.1271 -0.0154 -0.0174 0.0027  89  ARG A O   
788  C  CB  . ARG A 89  ? 0.1882 0.1086 0.1612 -0.0085 -0.0540 0.0292  89  ARG A CB  
789  C  CG  . ARG A 89  ? 0.2773 0.1840 0.1528 -0.0052 -0.0423 0.0108  89  ARG A CG  
790  C  CD  . ARG A 89  ? 0.3325 0.1409 0.2448 0.0592  -0.0035 0.0640  89  ARG A CD  
791  N  NE  . ARG A 89  ? 0.2374 0.1767 0.2201 0.0516  -0.0068 0.0680  89  ARG A NE  
792  C  CZ  . ARG A 89  ? 0.2289 0.1403 0.2633 0.0275  0.0068  0.0285  89  ARG A CZ  
793  N  NH1 . ARG A 89  ? 0.2994 0.1770 0.2617 0.0656  0.0603  0.0416  89  ARG A NH1 
794  N  NH2 . ARG A 89  ? 0.2477 0.2624 0.2808 0.0696  0.0098  -0.0208 89  ARG A NH2 
795  N  N   . LEU A 90  ? 0.1143 0.0712 0.1059 -0.0232 -0.0317 -0.0021 90  LEU A N   
796  C  CA  . LEU A 90  ? 0.1196 0.0953 0.0955 -0.0109 -0.0368 0.0087  90  LEU A CA  
797  C  C   . LEU A 90  ? 0.1164 0.1025 0.0935 -0.0142 -0.0252 0.0133  90  LEU A C   
798  O  O   . LEU A 90  ? 0.1438 0.1160 0.1235 -0.0098 -0.0292 0.0233  90  LEU A O   
799  C  CB  . LEU A 90  ? 0.1442 0.0808 0.0946 -0.0255 -0.0292 -0.0017 90  LEU A CB  
800  C  CG  . LEU A 90  ? 0.1747 0.1151 0.0967 -0.0098 -0.0417 0.0021  90  LEU A CG  
801  C  CD1 . LEU A 90  ? 0.1751 0.0955 0.1208 -0.0110 -0.0425 0.0049  90  LEU A CD1 
802  C  CD2 . LEU A 90  ? 0.1465 0.1386 0.1633 -0.0041 -0.0961 0.0146  90  LEU A CD2 
803  N  N   . ILE A 91  ? 0.1168 0.0648 0.1079 -0.0159 -0.0043 0.0160  91  ILE A N   
804  C  CA  . ILE A 91  ? 0.1339 0.0576 0.1278 -0.0207 -0.0065 0.0038  91  ILE A CA  
805  C  C   . ILE A 91  ? 0.1558 0.0736 0.1106 0.0017  -0.0097 0.0167  91  ILE A C   
806  O  O   . ILE A 91  ? 0.1352 0.0639 0.0838 -0.0167 -0.0186 0.0305  91  ILE A O   
807  C  CB  . ILE A 91  ? 0.1379 0.0813 0.1539 -0.0190 0.0116  0.0083  91  ILE A CB  
808  C  CG1 . ILE A 91  ? 0.1190 0.1490 0.1375 -0.0781 0.0044  0.0066  91  ILE A CG1 
809  C  CG2 . ILE A 91  ? 0.1600 0.1071 0.1578 0.0006  -0.0200 0.0249  91  ILE A CG2 
810  C  CD1 . ILE A 91  ? 0.1741 0.2160 0.1263 -0.0826 -0.0020 -0.0276 91  ILE A CD1 
811  N  N   . GLN A 92  ? 0.1483 0.0497 0.1086 0.0032  -0.0324 0.0175  92  GLN A N   
812  C  CA  . GLN A 92  ? 0.1467 0.0385 0.1040 0.0104  -0.0046 0.0228  92  GLN A CA  
813  C  C   . GLN A 92  ? 0.1618 0.0652 0.0643 0.0015  -0.0228 0.0228  92  GLN A C   
814  O  O   . GLN A 92  ? 0.1806 0.0482 0.0552 -0.0041 -0.0292 -0.0054 92  GLN A O   
815  C  CB  . GLN A 92  ? 0.1242 0.1131 0.1256 0.0100  0.0007  0.0162  92  GLN A CB  
816  C  CG  . GLN A 92  ? 0.1433 0.0646 0.1521 0.0317  -0.0304 0.0344  92  GLN A CG  
817  C  CD  . GLN A 92  ? 0.1666 0.0993 0.0617 0.0120  -0.0049 0.0023  92  GLN A CD  
818  O  OE1 . GLN A 92  ? 0.2083 0.0506 0.1231 0.0109  -0.0110 0.0144  92  GLN A OE1 
819  N  NE2 . GLN A 92  ? 0.1080 0.1203 0.1377 0.0015  -0.0083 0.0100  92  GLN A NE2 
820  N  N   . PHE A 93  ? 0.1694 0.0588 0.0794 0.0063  -0.0443 0.0076  93  PHE A N   
821  C  CA  . PHE A 93  ? 0.1436 0.0504 0.1037 0.0127  -0.0287 0.0125  93  PHE A CA  
822  C  C   . PHE A 93  ? 0.0982 0.0767 0.0609 -0.0041 -0.0205 0.0184  93  PHE A C   
823  O  O   . PHE A 93  ? 0.1959 0.0736 0.0461 0.0144  -0.0215 0.0006  93  PHE A O   
824  C  CB  . PHE A 93  ? 0.1370 0.0926 0.0872 -0.0237 -0.0661 0.0154  93  PHE A CB  
825  C  CG  . PHE A 93  ? 0.1449 0.0795 0.0883 0.0118  -0.0423 -0.0010 93  PHE A CG  
826  C  CD1 . PHE A 93  ? 0.1720 0.0860 0.0964 -0.0247 -0.0348 0.0007  93  PHE A CD1 
827  C  CD2 . PHE A 93  ? 0.1734 0.1126 0.1004 0.0014  -0.0985 0.0276  93  PHE A CD2 
828  C  CE1 . PHE A 93  ? 0.1377 0.1194 0.1183 -0.0092 -0.0348 -0.0161 93  PHE A CE1 
829  C  CE2 . PHE A 93  ? 0.1952 0.1257 0.0930 0.0320  -0.0754 0.0081  93  PHE A CE2 
830  C  CZ  . PHE A 93  ? 0.2155 0.1108 0.1133 0.0144  -0.0599 -0.0080 93  PHE A CZ  
831  N  N   . HIS A 94  ? 0.1231 0.0470 0.1046 0.0109  -0.0405 0.0311  94  HIS A N   
832  C  CA  . HIS A 94  ? 0.1165 0.0643 0.0863 -0.0071 -0.0267 0.0183  94  HIS A CA  
833  C  C   . HIS A 94  ? 0.0998 0.0678 0.0644 -0.0132 -0.0276 0.0038  94  HIS A C   
834  O  O   . HIS A 94  ? 0.1181 0.0583 0.0502 0.0019  -0.0155 0.0130  94  HIS A O   
835  C  CB  . HIS A 94  ? 0.1031 0.0989 0.1010 -0.0071 -0.0299 0.0083  94  HIS A CB  
836  C  CG  . HIS A 94  ? 0.1201 0.0646 0.0718 -0.0030 -0.0076 0.0060  94  HIS A CG  
837  N  ND1 . HIS A 94  ? 0.1127 0.0539 0.0653 -0.0142 -0.0063 0.0287  94  HIS A ND1 
838  C  CD2 . HIS A 94  ? 0.0860 0.0599 0.0973 -0.0203 0.0188  -0.0156 94  HIS A CD2 
839  C  CE1 . HIS A 94  ? 0.1013 0.0662 0.0614 -0.0046 -0.0228 0.0261  94  HIS A CE1 
840  N  NE2 . HIS A 94  ? 0.1133 0.0402 0.0603 -0.0173 -0.0181 0.0000  94  HIS A NE2 
841  N  N   . PHE A 95  ? 0.1057 0.0552 0.1077 -0.0049 -0.0068 0.0046  95  PHE A N   
842  C  CA  . PHE A 95  ? 0.1036 0.0557 0.1039 0.0023  -0.0217 -0.0003 95  PHE A CA  
843  C  C   . PHE A 95  ? 0.1023 0.0461 0.0768 0.0207  -0.0149 -0.0055 95  PHE A C   
844  O  O   . PHE A 95  ? 0.1230 0.0750 0.0831 -0.0142 -0.0034 0.0092  95  PHE A O   
845  C  CB  . PHE A 95  ? 0.1041 0.0804 0.0736 0.0094  -0.0230 -0.0366 95  PHE A CB  
846  C  CG  . PHE A 95  ? 0.1274 0.0439 0.0555 0.0000  -0.0286 -0.0082 95  PHE A CG  
847  C  CD1 . PHE A 95  ? 0.1208 0.0798 0.0636 -0.0063 -0.0152 -0.0005 95  PHE A CD1 
848  C  CD2 . PHE A 95  ? 0.1095 0.0937 0.0768 -0.0329 -0.0406 -0.0195 95  PHE A CD2 
849  C  CE1 . PHE A 95  ? 0.1212 0.0790 0.1018 0.0060  -0.0065 0.0065  95  PHE A CE1 
850  C  CE2 . PHE A 95  ? 0.1339 0.0655 0.0671 -0.0043 -0.0299 -0.0164 95  PHE A CE2 
851  C  CZ  . PHE A 95  ? 0.1097 0.0943 0.1074 -0.0113 -0.0247 -0.0251 95  PHE A CZ  
852  N  N   . HIS A 96  ? 0.1115 0.0653 0.0621 0.0057  -0.0109 0.0098  96  HIS A N   
853  C  CA  . HIS A 96  ? 0.0806 0.0691 0.0740 0.0041  0.0003  0.0027  96  HIS A CA  
854  C  C   . HIS A 96  ? 0.0833 0.0725 0.0599 0.0026  0.0041  0.0065  96  HIS A C   
855  O  O   . HIS A 96  ? 0.1048 0.0697 0.0907 0.0097  0.0262  0.0071  96  HIS A O   
856  C  CB  . HIS A 96  ? 0.1054 0.0565 0.0505 0.0065  -0.0065 -0.0013 96  HIS A CB  
857  C  CG  . HIS A 96  ? 0.0953 0.0655 0.1162 0.0098  0.0096  -0.0038 96  HIS A CG  
858  N  ND1 . HIS A 96  ? 0.0815 0.0615 0.1068 0.0076  -0.0100 -0.0186 96  HIS A ND1 
859  C  CD2 . HIS A 96  ? 0.0831 0.1025 0.0955 0.0406  -0.0176 0.0141  96  HIS A CD2 
860  C  CE1 . HIS A 96  ? 0.0745 0.0680 0.1385 -0.0167 -0.0222 -0.0152 96  HIS A CE1 
861  N  NE2 . HIS A 96  ? 0.0507 0.0825 0.1174 -0.0185 -0.0057 0.0113  96  HIS A NE2 
862  N  N   . TRP A 97  ? 0.0781 0.0474 0.0988 0.0000  0.0035  -0.0052 97  TRP A N   
863  C  CA  . TRP A 97  ? 0.1146 0.0489 0.0604 0.0176  0.0015  -0.0037 97  TRP A CA  
864  C  C   . TRP A 97  ? 0.1147 0.0628 0.0678 0.0055  0.0108  -0.0166 97  TRP A C   
865  O  O   . TRP A 97  ? 0.1201 0.0593 0.0919 -0.0131 0.0225  -0.0024 97  TRP A O   
866  C  CB  . TRP A 97  ? 0.1457 0.0842 0.0592 -0.0129 0.0226  -0.0274 97  TRP A CB  
867  C  CG  . TRP A 97  ? 0.1147 0.0741 0.0646 -0.0199 -0.0003 -0.0030 97  TRP A CG  
868  C  CD1 . TRP A 97  ? 0.1572 0.1025 0.1352 -0.0049 0.0384  -0.0264 97  TRP A CD1 
869  C  CD2 . TRP A 97  ? 0.1093 0.0976 0.0671 -0.0031 -0.0049 -0.0174 97  TRP A CD2 
870  N  NE1 . TRP A 97  ? 0.1704 0.0756 0.1039 -0.0081 0.0226  -0.0260 97  TRP A NE1 
871  C  CE2 . TRP A 97  ? 0.1806 0.0815 0.0666 -0.0285 -0.0023 -0.0175 97  TRP A CE2 
872  C  CE3 . TRP A 97  ? 0.1587 0.0865 0.0617 0.0035  -0.0346 0.0052  97  TRP A CE3 
873  C  CZ2 . TRP A 97  ? 0.1913 0.0903 0.1150 -0.0272 0.0176  0.0138  97  TRP A CZ2 
874  C  CZ3 . TRP A 97  ? 0.1691 0.1313 0.0888 0.0017  0.0192  0.0010  97  TRP A CZ3 
875  C  CH2 . TRP A 97  ? 0.1758 0.0773 0.1217 -0.0060 0.0204  -0.0071 97  TRP A CH2 
876  N  N   . GLY A 98  ? 0.1395 0.0406 0.0689 -0.0081 0.0068  -0.0144 98  GLY A N   
877  C  CA  . GLY A 98  ? 0.1164 0.0671 0.0958 0.0000  0.0070  -0.0108 98  GLY A CA  
878  C  C   . GLY A 98  ? 0.1014 0.0925 0.1143 0.0055  0.0131  -0.0209 98  GLY A C   
879  O  O   . GLY A 98  ? 0.1431 0.0688 0.1086 -0.0271 0.0046  -0.0104 98  GLY A O   
880  N  N   . SER A 99  ? 0.1174 0.0732 0.1160 0.0013  0.0147  -0.0421 99  SER A N   
881  C  CA  . SER A 99  ? 0.1169 0.0885 0.1295 -0.0115 0.0216  -0.0267 99  SER A CA  
882  C  C   . SER A 99  ? 0.1291 0.1083 0.1339 -0.0206 0.0057  -0.0364 99  SER A C   
883  O  O   . SER A 99  ? 0.2074 0.0964 0.1228 -0.0219 0.0133  -0.0263 99  SER A O   
884  C  CB  . SER A 99  ? 0.1501 0.1219 0.1641 0.0232  0.0281  -0.0461 99  SER A CB  
885  O  OG  . SER A 99  ? 0.1269 0.1106 0.2352 -0.0005 0.0390  -0.0153 99  SER A OG  
886  N  N   . LEU A 100 ? 0.1129 0.0993 0.1668 -0.0353 0.0406  -0.0315 100 LEU A N   
887  C  CA  . LEU A 100 ? 0.1393 0.1048 0.1995 -0.0100 0.0329  -0.0035 100 LEU A CA  
888  C  C   . LEU A 100 ? 0.1195 0.1045 0.1693 -0.0121 0.0227  -0.0187 100 LEU A C   
889  O  O   . LEU A 100 ? 0.1421 0.0799 0.1709 -0.0188 0.0196  -0.0247 100 LEU A O   
890  C  CB  . LEU A 100 ? 0.1896 0.1783 0.2404 0.0000  0.0318  0.0167  100 LEU A CB  
891  C  CG  . LEU A 100 ? 0.1959 0.1931 0.2811 0.0049  0.0126  -0.0068 100 LEU A CG  
892  C  CD1 . LEU A 100 ? 0.2311 0.3578 0.3253 0.0348  0.0127  0.0073  100 LEU A CD1 
893  C  CD2 . LEU A 100 ? 0.2937 0.2987 0.2210 0.0017  0.0878  -0.0759 100 LEU A CD2 
894  N  N   . ASP A 101 ? 0.1025 0.1106 0.1874 -0.0020 0.0179  -0.0043 101 ASP A N   
895  C  CA  . ASP A 101 ? 0.1223 0.0912 0.1469 -0.0307 0.0184  0.0074  101 ASP A CA  
896  C  C   . ASP A 101 ? 0.1518 0.0961 0.1501 -0.0026 0.0131  -0.0038 101 ASP A C   
897  O  O   . ASP A 101 ? 0.1488 0.1070 0.1636 0.0074  0.0149  0.0331  101 ASP A O   
898  C  CB  . ASP A 101 ? 0.1084 0.1169 0.1555 -0.0331 0.0179  0.0245  101 ASP A CB  
899  C  CG  . ASP A 101 ? 0.1219 0.0971 0.2203 -0.0188 -0.0019 -0.0038 101 ASP A CG  
900  O  OD1 . ASP A 101 ? 0.1967 0.1086 0.1680 -0.0205 0.0021  0.0222  101 ASP A OD1 
901  O  OD2 . ASP A 101 ? 0.2542 0.1909 0.2914 -0.1255 -0.0784 -0.0010 101 ASP A OD2 
902  N  N   . GLY A 102 ? 0.1741 0.0905 0.1565 -0.0049 -0.0187 0.0038  102 GLY A N   
903  C  CA  . GLY A 102 ? 0.1618 0.0670 0.1605 -0.0060 -0.0160 0.0098  102 GLY A CA  
904  C  C   . GLY A 102 ? 0.1221 0.0844 0.1609 0.0189  -0.0041 0.0186  102 GLY A C   
905  O  O   . GLY A 102 ? 0.1504 0.1106 0.1464 0.0121  0.0185  0.0230  102 GLY A O   
906  N  N   . GLN A 103 ? 0.1287 0.0506 0.1217 -0.0012 -0.0065 0.0109  103 GLN A N   
907  C  CA  . GLN A 103 ? 0.1093 0.0710 0.1420 0.0035  -0.0065 0.0034  103 GLN A CA  
908  C  C   . GLN A 103 ? 0.1000 0.0401 0.0935 -0.0057 0.0313  0.0010  103 GLN A C   
909  O  O   . GLN A 103 ? 0.1700 0.0604 0.1007 0.0119  0.0010  -0.0085 103 GLN A O   
910  C  CB  . GLN A 103 ? 0.1291 0.0896 0.1396 -0.0040 0.0228  -0.0264 103 GLN A CB  
911  C  CG  . GLN A 103 ? 0.1155 0.1213 0.1400 0.0167  0.0093  -0.0068 103 GLN A CG  
912  C  CD  . GLN A 103 ? 0.1237 0.1508 0.1992 0.0454  0.0076  0.0346  103 GLN A CD  
913  O  OE1 . GLN A 103 ? 0.2153 0.2929 0.2523 0.1253  0.0944  0.1182  103 GLN A OE1 
914  N  NE2 . GLN A 103 ? 0.1558 0.1287 0.2373 0.0243  0.0555  0.0237  103 GLN A NE2 
915  N  N   . GLY A 104 ? 0.0996 0.0608 0.1221 0.0227  0.0013  -0.0174 104 GLY A N   
916  C  CA  . GLY A 104 ? 0.1049 0.0539 0.1084 0.0109  0.0226  -0.0010 104 GLY A CA  
917  C  C   . GLY A 104 ? 0.0910 0.0662 0.0788 0.0129  -0.0285 0.0082  104 GLY A C   
918  O  O   . GLY A 104 ? 0.1034 0.0835 0.1050 -0.0081 0.0126  0.0125  104 GLY A O   
919  N  N   . SER A 105 ? 0.0689 0.0779 0.0648 0.0127  0.0093  -0.0060 105 SER A N   
920  C  CA  . SER A 105 ? 0.0740 0.0657 0.0847 -0.0098 -0.0105 -0.0195 105 SER A CA  
921  C  C   . SER A 105 ? 0.0505 0.0490 0.1074 -0.0043 0.0043  -0.0013 105 SER A C   
922  O  O   . SER A 105 ? 0.0892 0.0454 0.1014 0.0195  -0.0094 -0.0109 105 SER A O   
923  C  CB  . SER A 105 ? 0.0570 0.1041 0.0966 0.0054  0.0131  0.0076  105 SER A CB  
924  O  OG  . SER A 105 ? 0.0718 0.0619 0.1046 0.0065  0.0097  0.0013  105 SER A OG  
925  N  N   . GLU A 106 ? 0.0542 0.0494 0.0786 -0.0085 -0.0044 -0.0082 106 GLU A N   
926  C  CA  . GLU A 106 ? 0.0793 0.0594 0.0619 -0.0161 0.0030  0.0027  106 GLU A CA  
927  C  C   . GLU A 106 ? 0.0618 0.0698 0.0874 -0.0076 0.0046  -0.0043 106 GLU A C   
928  O  O   . GLU A 106 ? 0.0667 0.1005 0.0856 0.0131  -0.0041 -0.0144 106 GLU A O   
929  C  CB  . GLU A 106 ? 0.1099 0.0401 0.0815 -0.0196 -0.0129 -0.0027 106 GLU A CB  
930  C  CG  . GLU A 106 ? 0.1519 0.0577 0.0926 -0.0381 0.0111  0.0089  106 GLU A CG  
931  C  CD  . GLU A 106 ? 0.1020 0.0617 0.0736 -0.0098 0.0026  -0.0010 106 GLU A CD  
932  O  OE1 . GLU A 106 ? 0.0505 0.0402 0.1271 -0.0093 -0.0013 0.0054  106 GLU A OE1 
933  O  OE2 . GLU A 106 ? 0.0716 0.0913 0.1205 -0.0054 0.0065  -0.0098 106 GLU A OE2 
934  N  N   . HIS A 107 ? 0.0585 0.0628 0.0806 -0.0020 0.0155  -0.0012 107 HIS A N   
935  C  CA  . HIS A 107 ? 0.0522 0.0569 0.0964 0.0060  0.0195  -0.0144 107 HIS A CA  
936  C  C   . HIS A 107 ? 0.0269 0.0689 0.0705 -0.0021 0.0001  0.0038  107 HIS A C   
937  O  O   . HIS A 107 ? 0.0756 0.0679 0.0840 -0.0052 -0.0097 0.0071  107 HIS A O   
938  C  CB  . HIS A 107 ? 0.0684 0.0764 0.0815 0.0035  0.0140  -0.0060 107 HIS A CB  
939  C  CG  . HIS A 107 ? 0.0673 0.0495 0.0513 -0.0171 -0.0055 0.0155  107 HIS A CG  
940  N  ND1 . HIS A 107 ? 0.0740 0.0741 0.0863 0.0010  -0.0041 0.0231  107 HIS A ND1 
941  C  CD2 . HIS A 107 ? 0.0463 0.1070 0.0450 0.0168  0.0063  -0.0296 107 HIS A CD2 
942  C  CE1 . HIS A 107 ? 0.0454 0.0558 0.0824 0.0041  0.0141  0.0063  107 HIS A CE1 
943  N  NE2 . HIS A 107 ? 0.0433 0.0755 0.0961 0.0074  -0.0182 -0.0052 107 HIS A NE2 
944  N  N   . THR A 108 ? 0.0869 0.0653 0.0865 -0.0003 0.0093  0.0248  108 THR A N   
945  C  CA  . THR A 108 ? 0.0723 0.0644 0.0876 0.0008  -0.0068 0.0322  108 THR A CA  
946  C  C   . THR A 108 ? 0.0807 0.0766 0.0923 -0.0031 -0.0065 0.0155  108 THR A C   
947  O  O   . THR A 108 ? 0.1045 0.0816 0.0786 -0.0003 -0.0054 0.0043  108 THR A O   
948  C  CB  . THR A 108 ? 0.1046 0.0626 0.0646 0.0137  -0.0272 0.0136  108 THR A CB  
949  O  OG1 . THR A 108 ? 0.0867 0.0788 0.0788 0.0203  -0.0249 -0.0082 108 THR A OG1 
950  C  CG2 . THR A 108 ? 0.1068 0.1095 0.0451 -0.0182 0.0116  -0.0133 108 THR A CG2 
951  N  N   . VAL A 109 ? 0.0655 0.0714 0.1055 -0.0046 0.0052  0.0238  109 VAL A N   
952  C  CA  . VAL A 109 ? 0.0837 0.0869 0.0998 -0.0003 0.0198  0.0337  109 VAL A CA  
953  C  C   . VAL A 109 ? 0.1194 0.0980 0.1089 0.0005  0.0281  0.0346  109 VAL A C   
954  O  O   . VAL A 109 ? 0.1143 0.0788 0.1259 -0.0010 0.0115  0.0192  109 VAL A O   
955  C  CB  . VAL A 109 ? 0.0842 0.1381 0.1469 0.0030  0.0113  0.0348  109 VAL A CB  
956  C  CG1 . VAL A 109 ? 0.0566 0.1460 0.1569 -0.0035 0.0258  0.0390  109 VAL A CG1 
957  C  CG2 . VAL A 109 ? 0.1321 0.0844 0.1508 0.0210  0.0003  0.0383  109 VAL A CG2 
958  N  N   . ASP A 110 ? 0.1299 0.0777 0.1159 0.0115  0.0066  0.0414  110 ASP A N   
959  C  CA  . ASP A 110 ? 0.1396 0.0976 0.1124 0.0035  0.0315  0.0377  110 ASP A CA  
960  C  C   . ASP A 110 ? 0.1500 0.0928 0.0998 0.0125  0.0132  0.0186  110 ASP A C   
961  O  O   . ASP A 110 ? 0.1374 0.0822 0.1234 0.0030  -0.0001 0.0247  110 ASP A O   
962  C  CB  . ASP A 110 ? 0.1478 0.1102 0.1143 0.0194  0.0612  0.0538  110 ASP A CB  
963  C  CG  . ASP A 110 ? 0.1866 0.1140 0.1147 0.0092  0.0855  0.0331  110 ASP A CG  
964  O  OD1 . ASP A 110 ? 0.1640 0.1270 0.1844 0.0178  0.0588  0.0317  110 ASP A OD1 
965  O  OD2 . ASP A 110 ? 0.1761 0.1871 0.1627 0.0187  0.0527  0.0379  110 ASP A OD2 
966  N  N   . LYS A 111 ? 0.1312 0.0806 0.1034 0.0082  0.0098  0.0163  111 LYS A N   
967  C  CA  . LYS A 111 ? 0.1341 0.0856 0.1016 0.0251  -0.0148 -0.0020 111 LYS A CA  
968  C  C   . LYS A 111 ? 0.1400 0.0655 0.1159 0.0179  -0.0184 0.0107  111 LYS A C   
969  O  O   . LYS A 111 ? 0.1386 0.1104 0.1356 0.0178  0.0046  -0.0068 111 LYS A O   
970  C  CB  . LYS A 111 ? 0.1354 0.1385 0.1483 0.0434  -0.0221 0.0201  111 LYS A CB  
971  C  CG  . LYS A 111 ? 0.1824 0.1650 0.1217 0.0485  -0.0326 0.0103  111 LYS A CG  
972  C  CD  . LYS A 111 ? 0.1849 0.2610 0.2085 0.0030  -0.0927 -0.0524 111 LYS A CD  
973  C  CE  . LYS A 111 ? 0.2196 0.2642 0.2063 0.0353  -0.0577 -0.0366 111 LYS A CE  
974  N  NZ  . LYS A 111 ? 0.2430 0.3084 0.2628 0.0383  -0.0953 0.0209  111 LYS A NZ  
975  N  N   . LYS A 112 ? 0.1178 0.0759 0.0957 0.0065  -0.0059 0.0154  112 LYS A N   
976  C  CA  . LYS A 112 ? 0.1064 0.1004 0.0890 -0.0155 0.0096  0.0195  112 LYS A CA  
977  C  C   . LYS A 112 ? 0.0772 0.0840 0.0822 0.0055  0.0087  0.0083  112 LYS A C   
978  O  O   . LYS A 112 ? 0.1154 0.0706 0.0949 0.0166  0.0118  0.0020  112 LYS A O   
979  C  CB  . LYS A 112 ? 0.1154 0.1263 0.1271 -0.0428 -0.0127 0.0093  112 LYS A CB  
980  C  CG  . LYS A 112 ? 0.0904 0.1600 0.1499 -0.0307 0.0028  -0.0307 112 LYS A CG  
981  C  CD  . LYS A 112 ? 0.1246 0.1716 0.1528 -0.0052 -0.0318 0.0003  112 LYS A CD  
982  C  CE  . LYS A 112 ? 0.1770 0.1816 0.1625 -0.0267 -0.0353 -0.0143 112 LYS A CE  
983  N  NZ  . LYS A 112 ? 0.2254 0.1299 0.1874 -0.0285 -0.0414 -0.0015 112 LYS A NZ  
984  N  N   A LYS A 113 ? 0.1077 0.1093 0.0600 0.0063  0.0154  0.0184  113 LYS A N   
985  N  N   B LYS A 113 ? 0.1036 0.1089 0.0596 0.0097  0.0114  0.0126  113 LYS A N   
986  C  CA  A LYS A 113 ? 0.0885 0.0886 0.0815 -0.0017 0.0043  0.0087  113 LYS A CA  
987  C  CA  B LYS A 113 ? 0.0710 0.1027 0.0824 -0.0013 0.0043  0.0010  113 LYS A CA  
988  C  C   A LYS A 113 ? 0.0910 0.0881 0.0935 0.0162  -0.0082 0.0100  113 LYS A C   
989  C  C   B LYS A 113 ? 0.0689 0.0939 0.1011 0.0212  -0.0062 -0.0030 113 LYS A C   
990  O  O   A LYS A 113 ? 0.1142 0.0666 0.0649 -0.0077 -0.0010 0.0219  113 LYS A O   
991  O  O   B LYS A 113 ? 0.0463 0.0912 0.1145 0.0077  -0.0015 -0.0306 113 LYS A O   
992  C  CB  A LYS A 113 ? 0.0637 0.1031 0.1252 0.0046  0.0127  0.0116  113 LYS A CB  
993  C  CB  B LYS A 113 ? 0.0472 0.0935 0.1271 0.0024  0.0104  -0.0038 113 LYS A CB  
994  C  CG  A LYS A 113 ? 0.1050 0.0288 0.1176 0.0148  -0.0076 0.0071  113 LYS A CG  
995  C  CG  B LYS A 113 ? 0.0340 0.1406 0.1309 0.0164  -0.0109 -0.0183 113 LYS A CG  
996  C  CD  A LYS A 113 ? 0.0854 0.1048 0.1101 0.0078  -0.0046 -0.0100 113 LYS A CD  
997  C  CD  B LYS A 113 ? 0.0533 0.1366 0.1510 0.0142  -0.0199 -0.0177 113 LYS A CD  
998  C  CE  A LYS A 113 ? 0.0788 0.1011 0.1275 0.0201  -0.0194 -0.0242 113 LYS A CE  
999  C  CE  B LYS A 113 ? 0.0631 0.1666 0.1791 -0.0071 -0.0348 -0.0192 113 LYS A CE  
1000 N  NZ  A LYS A 113 ? 0.0759 0.1873 0.1271 0.0395  -0.0373 -0.0104 113 LYS A NZ  
1001 N  NZ  B LYS A 113 ? 0.0795 0.1666 0.2336 0.0285  -0.0366 0.0031  113 LYS A NZ  
1002 N  N   . TYR A 114 ? 0.0817 0.0689 0.0842 0.0121  -0.0086 0.0129  114 TYR A N   
1003 C  CA  . TYR A 114 ? 0.1009 0.0797 0.0833 0.0324  -0.0181 0.0197  114 TYR A CA  
1004 C  C   . TYR A 114 ? 0.0914 0.0581 0.0928 -0.0166 0.0020  -0.0173 114 TYR A C   
1005 O  O   . TYR A 114 ? 0.0860 0.0725 0.1027 -0.0109 0.0100  -0.0171 114 TYR A O   
1006 C  CB  . TYR A 114 ? 0.0503 0.0861 0.1313 0.0118  0.0178  -0.0055 114 TYR A CB  
1007 C  CG  . TYR A 114 ? 0.1302 0.0644 0.0993 0.0326  -0.0034 -0.0093 114 TYR A CG  
1008 C  CD1 . TYR A 114 ? 0.1496 0.0731 0.1067 -0.0032 0.0320  0.0254  114 TYR A CD1 
1009 C  CD2 . TYR A 114 ? 0.1253 0.0759 0.1115 -0.0287 0.0054  0.0210  114 TYR A CD2 
1010 C  CE1 . TYR A 114 ? 0.1791 0.0685 0.0776 0.0057  -0.0035 0.0248  114 TYR A CE1 
1011 C  CE2 . TYR A 114 ? 0.1066 0.1263 0.1515 -0.0043 0.0280  0.0286  114 TYR A CE2 
1012 C  CZ  . TYR A 114 ? 0.1267 0.1230 0.1615 0.0071  0.0551  0.0239  114 TYR A CZ  
1013 O  OH  . TYR A 114 ? 0.1835 0.1758 0.1869 0.0008  0.0838  -0.0114 114 TYR A OH  
1014 N  N   . ALA A 115 ? 0.1050 0.0408 0.0966 -0.0211 -0.0071 -0.0129 115 ALA A N   
1015 C  CA  . ALA A 115 ? 0.1374 0.0463 0.0734 -0.0059 -0.0116 -0.0020 115 ALA A CA  
1016 C  C   . ALA A 115 ? 0.0822 0.0664 0.0886 0.0093  -0.0041 -0.0057 115 ALA A C   
1017 O  O   . ALA A 115 ? 0.1115 0.0714 0.1064 -0.0082 0.0099  -0.0136 115 ALA A O   
1018 C  CB  . ALA A 115 ? 0.1119 0.0891 0.1334 0.0060  -0.0121 -0.0023 115 ALA A CB  
1019 N  N   . ALA A 116 ? 0.1005 0.0323 0.0822 0.0107  -0.0063 0.0000  116 ALA A N   
1020 C  CA  . ALA A 116 ? 0.1171 0.0370 0.0863 0.0073  -0.0026 0.0032  116 ALA A CA  
1021 C  C   . ALA A 116 ? 0.0892 0.0494 0.0952 0.0230  -0.0155 0.0063  116 ALA A C   
1022 O  O   . ALA A 116 ? 0.0888 0.0790 0.0790 -0.0012 -0.0028 -0.0012 116 ALA A O   
1023 C  CB  . ALA A 116 ? 0.1349 0.0785 0.1040 -0.0149 -0.0051 0.0091  116 ALA A CB  
1024 N  N   . GLU A 117 ? 0.0983 0.0276 0.0709 -0.0013 -0.0035 0.0000  117 GLU A N   
1025 C  CA  . GLU A 117 ? 0.1111 0.0363 0.0640 0.0026  -0.0110 -0.0040 117 GLU A CA  
1026 C  C   . GLU A 117 ? 0.0822 0.0372 0.0872 0.0066  0.0043  -0.0028 117 GLU A C   
1027 O  O   . GLU A 117 ? 0.0842 0.0697 0.0812 -0.0030 0.0046  0.0183  117 GLU A O   
1028 C  CB  . GLU A 117 ? 0.1000 0.0838 0.0590 0.0013  -0.0175 -0.0122 117 GLU A CB  
1029 C  CG  . GLU A 117 ? 0.0793 0.0745 0.0603 -0.0161 -0.0260 -0.0162 117 GLU A CG  
1030 C  CD  . GLU A 117 ? 0.0711 0.0639 0.0768 -0.0088 0.0046  0.0164  117 GLU A CD  
1031 O  OE1 . GLU A 117 ? 0.1032 0.0671 0.0790 0.0120  -0.0080 -0.0211 117 GLU A OE1 
1032 O  OE2 . GLU A 117 ? 0.0869 0.0594 0.0986 0.0108  -0.0218 -0.0021 117 GLU A OE2 
1033 N  N   . LEU A 118 ? 0.0872 0.0662 0.0847 0.0307  -0.0190 -0.0015 118 LEU A N   
1034 C  CA  . LEU A 118 ? 0.0808 0.0508 0.0773 0.0020  -0.0263 -0.0199 118 LEU A CA  
1035 C  C   . LEU A 118 ? 0.0793 0.0626 0.0539 0.0253  -0.0104 0.0028  118 LEU A C   
1036 O  O   . LEU A 118 ? 0.0904 0.0592 0.0561 -0.0015 -0.0063 -0.0040 118 LEU A O   
1037 C  CB  . LEU A 118 ? 0.0603 0.0612 0.0998 0.0186  -0.0304 -0.0063 118 LEU A CB  
1038 C  CG  . LEU A 118 ? 0.1092 0.0596 0.0854 0.0214  -0.0082 0.0228  118 LEU A CG  
1039 C  CD1 . LEU A 118 ? 0.1413 0.0822 0.0978 0.0015  -0.0207 0.0283  118 LEU A CD1 
1040 C  CD2 . LEU A 118 ? 0.0732 0.1321 0.1050 0.0076  -0.0247 0.0192  118 LEU A CD2 
1041 N  N   . HIS A 119 ? 0.1172 0.0275 0.0698 -0.0010 -0.0103 -0.0003 119 HIS A N   
1042 C  CA  . HIS A 119 ? 0.0942 0.0498 0.0837 -0.0048 -0.0355 0.0189  119 HIS A CA  
1043 C  C   . HIS A 119 ? 0.0952 0.0421 0.0822 0.0019  -0.0285 0.0049  119 HIS A C   
1044 O  O   . HIS A 119 ? 0.1171 0.0531 0.0811 -0.0010 -0.0201 0.0057  119 HIS A O   
1045 C  CB  . HIS A 119 ? 0.0917 0.0833 0.0658 0.0081  -0.0155 0.0007  119 HIS A CB  
1046 C  CG  . HIS A 119 ? 0.1257 0.0649 0.0479 0.0384  0.0007  -0.0005 119 HIS A CG  
1047 N  ND1 . HIS A 119 ? 0.0571 0.0812 0.0921 -0.0071 0.0252  0.0076  119 HIS A ND1 
1048 C  CD2 . HIS A 119 ? 0.1420 0.0791 0.0384 -0.0140 0.0010  0.0142  119 HIS A CD2 
1049 C  CE1 . HIS A 119 ? 0.0913 0.0460 0.1095 0.0054  -0.0261 -0.0120 119 HIS A CE1 
1050 N  NE2 . HIS A 119 ? 0.0415 0.0931 0.0973 -0.0015 -0.0276 0.0089  119 HIS A NE2 
1051 N  N   . LEU A 120 ? 0.1099 0.0443 0.0649 0.0104  -0.0262 -0.0131 120 LEU A N   
1052 C  CA  . LEU A 120 ? 0.1007 0.0377 0.1036 -0.0104 -0.0137 -0.0031 120 LEU A CA  
1053 C  C   . LEU A 120 ? 0.0772 0.0375 0.0813 0.0222  -0.0121 0.0001  120 LEU A C   
1054 O  O   . LEU A 120 ? 0.1014 0.0537 0.0719 -0.0211 -0.0131 0.0165  120 LEU A O   
1055 C  CB  . LEU A 120 ? 0.0967 0.0535 0.1350 0.0076  -0.0159 -0.0195 120 LEU A CB  
1056 C  CG  . LEU A 120 ? 0.1449 0.0781 0.0876 -0.0131 -0.0274 0.0230  120 LEU A CG  
1057 C  CD1 . LEU A 120 ? 0.1467 0.0995 0.1052 -0.0537 -0.0176 -0.0013 120 LEU A CD1 
1058 C  CD2 . LEU A 120 ? 0.1506 0.0993 0.1039 0.0024  -0.0839 0.0074  120 LEU A CD2 
1059 N  N   . VAL A 121 ? 0.0678 0.0614 0.1043 -0.0156 -0.0136 0.0054  121 VAL A N   
1060 C  CA  . VAL A 121 ? 0.0820 0.0599 0.1081 -0.0199 0.0027  0.0122  121 VAL A CA  
1061 C  C   . VAL A 121 ? 0.1058 0.0513 0.0833 -0.0152 -0.0091 -0.0027 121 VAL A C   
1062 O  O   . VAL A 121 ? 0.1138 0.0754 0.0795 -0.0049 -0.0155 0.0116  121 VAL A O   
1063 C  CB  . VAL A 121 ? 0.0696 0.0928 0.0648 -0.0068 -0.0057 0.0006  121 VAL A CB  
1064 C  CG1 . VAL A 121 ? 0.1041 0.0761 0.1181 -0.0289 0.0063  -0.0052 121 VAL A CG1 
1065 C  CG2 . VAL A 121 ? 0.0912 0.0425 0.1070 0.0234  -0.0038 -0.0023 121 VAL A CG2 
1066 N  N   . HIS A 122 ? 0.0800 0.0601 0.0707 -0.0102 -0.0249 -0.0205 122 HIS A N   
1067 C  CA  . HIS A 122 ? 0.0856 0.0384 0.0894 -0.0149 -0.0103 -0.0035 122 HIS A CA  
1068 C  C   . HIS A 122 ? 0.0998 0.0516 0.0937 -0.0052 -0.0161 -0.0027 122 HIS A C   
1069 O  O   . HIS A 122 ? 0.1061 0.0470 0.1118 -0.0046 -0.0436 0.0140  122 HIS A O   
1070 C  CB  . HIS A 122 ? 0.0976 0.0960 0.1057 0.0248  -0.0091 -0.0148 122 HIS A CB  
1071 C  CG  . HIS A 122 ? 0.0896 0.0768 0.0709 -0.0171 -0.0070 0.0143  122 HIS A CG  
1072 N  ND1 . HIS A 122 ? 0.0460 0.0725 0.1072 0.0087  -0.0074 -0.0005 122 HIS A ND1 
1073 C  CD2 . HIS A 122 ? 0.1057 0.0776 0.1198 -0.0054 -0.0300 -0.0019 122 HIS A CD2 
1074 C  CE1 . HIS A 122 ? 0.0812 0.0743 0.1510 0.0041  -0.0230 -0.0005 122 HIS A CE1 
1075 N  NE2 . HIS A 122 ? 0.0912 0.0854 0.1016 -0.0015 -0.0239 -0.0111 122 HIS A NE2 
1076 N  N   . TRP A 123 ? 0.0813 0.0522 0.1049 -0.0006 -0.0183 0.0010  123 TRP A N   
1077 C  CA  . TRP A 123 ? 0.0960 0.0364 0.1037 -0.0030 -0.0163 -0.0159 123 TRP A CA  
1078 C  C   . TRP A 123 ? 0.1010 0.0622 0.1149 -0.0074 -0.0065 -0.0021 123 TRP A C   
1079 O  O   . TRP A 123 ? 0.1163 0.0772 0.1346 0.0062  -0.0434 -0.0125 123 TRP A O   
1080 C  CB  . TRP A 123 ? 0.1122 0.1165 0.0872 -0.0208 -0.0210 -0.0015 123 TRP A CB  
1081 C  CG  . TRP A 123 ? 0.1442 0.0922 0.1264 -0.0229 -0.0270 0.0201  123 TRP A CG  
1082 C  CD1 . TRP A 123 ? 0.1518 0.1005 0.1111 -0.0410 -0.0291 0.0012  123 TRP A CD1 
1083 C  CD2 . TRP A 123 ? 0.2456 0.0578 0.1050 -0.0133 0.0000  0.0141  123 TRP A CD2 
1084 N  NE1 . TRP A 123 ? 0.2509 0.0707 0.1185 -0.0245 -0.0340 -0.0013 123 TRP A NE1 
1085 C  CE2 . TRP A 123 ? 0.2334 0.0535 0.1648 0.0012  -0.0650 0.0125  123 TRP A CE2 
1086 C  CE3 . TRP A 123 ? 0.2036 0.0571 0.1396 -0.0040 0.0008  0.0205  123 TRP A CE3 
1087 C  CZ2 . TRP A 123 ? 0.2915 0.0703 0.1165 0.0105  -0.0184 -0.0031 123 TRP A CZ2 
1088 C  CZ3 . TRP A 123 ? 0.2567 0.0900 0.0980 -0.0193 -0.0216 0.0037  123 TRP A CZ3 
1089 C  CH2 . TRP A 123 ? 0.2545 0.1045 0.1330 -0.0015 -0.0120 0.0116  123 TRP A CH2 
1090 N  N   . ASN A 124 ? 0.0878 0.0910 0.0849 0.0021  -0.0166 -0.0348 124 ASN A N   
1091 C  CA  . ASN A 124 ? 0.1163 0.0697 0.1001 0.0087  -0.0088 -0.0181 124 ASN A CA  
1092 C  C   . ASN A 124 ? 0.0988 0.0973 0.1212 -0.0037 -0.0132 -0.0201 124 ASN A C   
1093 O  O   . ASN A 124 ? 0.0790 0.0895 0.1374 -0.0108 -0.0074 -0.0080 124 ASN A O   
1094 C  CB  . ASN A 124 ? 0.1327 0.0971 0.0946 -0.0082 -0.0020 -0.0309 124 ASN A CB  
1095 C  CG  . ASN A 124 ? 0.1246 0.0763 0.1731 -0.0059 -0.0160 -0.0271 124 ASN A CG  
1096 O  OD1 . ASN A 124 ? 0.1499 0.1025 0.1342 0.0267  -0.0264 -0.0241 124 ASN A OD1 
1097 N  ND2 . ASN A 124 ? 0.1535 0.1107 0.1442 -0.0073 -0.0013 -0.0208 124 ASN A ND2 
1098 N  N   . THR A 125 ? 0.1336 0.0869 0.1331 0.0320  -0.0221 0.0030  125 THR A N   
1099 C  CA  . THR A 125 ? 0.1332 0.0725 0.1514 0.0249  -0.0278 0.0097  125 THR A CA  
1100 C  C   . THR A 125 ? 0.1039 0.0917 0.1683 0.0283  -0.0024 0.0010  125 THR A C   
1101 O  O   . THR A 125 ? 0.1700 0.0894 0.2018 0.0207  -0.0305 0.0194  125 THR A O   
1102 C  CB  . THR A 125 ? 0.1615 0.1192 0.2054 0.0350  -0.0211 0.0159  125 THR A CB  
1103 O  OG1 . THR A 125 ? 0.1770 0.1718 0.2469 0.0546  0.0035  -0.0065 125 THR A OG1 
1104 C  CG2 . THR A 125 ? 0.1734 0.1729 0.1844 0.0274  -0.0274 -0.0195 125 THR A CG2 
1105 N  N   . LYS A 126 ? 0.1718 0.0917 0.1248 -0.0063 0.0110  -0.0465 127 LYS A N   
1106 C  CA  . LYS A 126 ? 0.1852 0.1223 0.1666 -0.0165 0.0057  -0.0483 127 LYS A CA  
1107 C  C   . LYS A 126 ? 0.1790 0.0799 0.1633 -0.0185 -0.0027 -0.0253 127 LYS A C   
1108 O  O   . LYS A 126 ? 0.1932 0.0998 0.1946 -0.0236 -0.0063 -0.0472 127 LYS A O   
1109 C  CB  . LYS A 126 ? 0.1957 0.1138 0.1855 -0.0087 0.0024  -0.0439 127 LYS A CB  
1110 C  CG  . LYS A 126 ? 0.1740 0.1792 0.2003 -0.0241 -0.0054 -0.0340 127 LYS A CG  
1111 C  CD  . LYS A 126 ? 0.3059 0.2129 0.1704 -0.0644 0.0209  -0.0487 127 LYS A CD  
1112 C  CE  . LYS A 126 ? 0.3935 0.3896 0.3276 -0.0680 -0.0113 -0.0046 127 LYS A CE  
1113 N  NZ  . LYS A 126 ? 0.5435 0.4700 0.3183 -0.0203 0.0028  0.0205  127 LYS A NZ  
1114 N  N   . TYR A 127 ? 0.1715 0.0643 0.1235 -0.0141 0.0142  -0.0007 128 TYR A N   
1115 C  CA  . TYR A 127 ? 0.1528 0.0806 0.1241 -0.0083 -0.0310 0.0152  128 TYR A CA  
1116 C  C   . TYR A 127 ? 0.1677 0.0610 0.1514 -0.0107 -0.0153 0.0040  128 TYR A C   
1117 O  O   . TYR A 127 ? 0.1637 0.0741 0.1571 -0.0092 -0.0086 0.0013  128 TYR A O   
1118 C  CB  . TYR A 127 ? 0.1661 0.0768 0.1212 0.0024  -0.0157 -0.0141 128 TYR A CB  
1119 C  CG  . TYR A 127 ? 0.1292 0.0734 0.0973 -0.0133 -0.0362 -0.0244 128 TYR A CG  
1120 C  CD1 . TYR A 127 ? 0.1439 0.1054 0.1647 -0.0120 -0.0313 -0.0188 128 TYR A CD1 
1121 C  CD2 . TYR A 127 ? 0.0969 0.1158 0.1460 -0.0111 -0.0373 0.0019  128 TYR A CD2 
1122 C  CE1 . TYR A 127 ? 0.1767 0.0740 0.1150 -0.0031 -0.0317 -0.0192 128 TYR A CE1 
1123 C  CE2 . TYR A 127 ? 0.1088 0.0808 0.1255 -0.0057 -0.0234 -0.0346 128 TYR A CE2 
1124 C  CZ  . TYR A 127 ? 0.1371 0.1027 0.1189 0.0174  0.0118  -0.0153 128 TYR A CZ  
1125 O  OH  . TYR A 127 ? 0.2459 0.0991 0.1399 0.0237  -0.0271 -0.0414 128 TYR A OH  
1126 N  N   . GLY A 128 ? 0.1528 0.0953 0.1417 -0.0103 -0.0085 0.0071  129 GLY A N   
1127 C  CA  . GLY A 128 ? 0.1952 0.0831 0.1317 -0.0031 0.0092  0.0225  129 GLY A CA  
1128 C  C   . GLY A 128 ? 0.1959 0.0722 0.1454 0.0271  -0.0006 0.0166  129 GLY A C   
1129 O  O   . GLY A 128 ? 0.2653 0.1007 0.1431 0.0115  -0.0275 0.0286  129 GLY A O   
1130 N  N   . ASP A 129 ? 0.2085 0.0822 0.1572 0.0228  -0.0131 0.0020  130 ASP A N   
1131 C  CA  . ASP A 129 ? 0.2329 0.0628 0.1517 0.0252  -0.0007 0.0219  130 ASP A CA  
1132 C  C   . ASP A 129 ? 0.2277 0.0980 0.1367 0.0261  -0.0406 -0.0074 130 ASP A C   
1133 O  O   . ASP A 129 ? 0.2100 0.1142 0.1127 0.0342  -0.0362 -0.0159 130 ASP A O   
1134 C  CB  . ASP A 129 ? 0.2381 0.1280 0.1576 0.0226  0.0012  0.0196  130 ASP A CB  
1135 C  CG  . ASP A 129 ? 0.2460 0.0876 0.1528 0.0292  0.0275  0.0469  130 ASP A CG  
1136 O  OD1 . ASP A 129 ? 0.3379 0.1589 0.2024 -0.0410 -0.0538 0.0043  130 ASP A OD1 
1137 O  OD2 . ASP A 129 ? 0.2781 0.1567 0.2649 0.0076  0.0907  0.0671  130 ASP A OD2 
1138 N  N   . PHE A 130 ? 0.2248 0.0925 0.1345 0.0182  -0.0155 -0.0086 131 PHE A N   
1139 C  CA  . PHE A 130 ? 0.1673 0.1106 0.1353 0.0121  -0.0038 -0.0066 131 PHE A CA  
1140 C  C   . PHE A 130 ? 0.1612 0.0948 0.1206 -0.0220 0.0198  -0.0083 131 PHE A C   
1141 O  O   . PHE A 130 ? 0.1558 0.1244 0.0966 -0.0265 -0.0054 0.0100  131 PHE A O   
1142 C  CB  . PHE A 130 ? 0.2029 0.0834 0.0998 0.0037  0.0066  -0.0135 131 PHE A CB  
1143 C  CG  . PHE A 130 ? 0.1372 0.1048 0.1267 0.0100  0.0110  -0.0318 131 PHE A CG  
1144 C  CD1 . PHE A 130 ? 0.1314 0.0829 0.1323 0.0059  -0.0161 -0.0283 131 PHE A CD1 
1145 C  CD2 . PHE A 130 ? 0.1759 0.0928 0.1533 0.0038  0.0272  -0.0104 131 PHE A CD2 
1146 C  CE1 . PHE A 130 ? 0.1575 0.1086 0.1488 -0.0229 -0.0296 -0.0326 131 PHE A CE1 
1147 C  CE2 . PHE A 130 ? 0.2234 0.1529 0.1647 0.0024  -0.0052 0.0023  131 PHE A CE2 
1148 C  CZ  . PHE A 130 ? 0.1914 0.1440 0.1102 0.0010  -0.0266 -0.0024 131 PHE A CZ  
1149 N  N   . GLY A 131 ? 0.1923 0.1059 0.1578 -0.0377 0.0263  -0.0151 132 GLY A N   
1150 C  CA  . GLY A 131 ? 0.1783 0.1336 0.1457 -0.0239 0.0421  0.0099  132 GLY A CA  
1151 C  C   . GLY A 131 ? 0.1747 0.1172 0.1855 -0.0469 0.0414  0.0078  132 GLY A C   
1152 O  O   . GLY A 131 ? 0.2050 0.1084 0.2272 -0.0003 0.0500  -0.0197 132 GLY A O   
1153 N  N   . LYS A 132 ? 0.1686 0.0743 0.1864 -0.0505 0.0414  0.0052  133 LYS A N   
1154 C  CA  . LYS A 132 ? 0.1761 0.0784 0.1809 -0.0474 0.0231  0.0013  133 LYS A CA  
1155 C  C   . LYS A 132 ? 0.1388 0.0594 0.1539 -0.0185 0.0049  0.0046  133 LYS A C   
1156 O  O   . LYS A 132 ? 0.1481 0.1178 0.1625 -0.0296 -0.0052 0.0027  133 LYS A O   
1157 C  CB  . LYS A 132 ? 0.1439 0.1009 0.2054 -0.0237 0.0082  -0.0032 133 LYS A CB  
1158 C  CG  . LYS A 132 ? 0.1511 0.1439 0.2498 -0.0432 -0.0142 0.0300  133 LYS A CG  
1159 C  CD  . LYS A 132 ? 0.2623 0.1571 0.4049 -0.0249 -0.0087 0.0361  133 LYS A CD  
1160 C  CE  . LYS A 132 ? 0.3633 0.3851 0.4402 -0.0059 -0.0342 0.0110  133 LYS A CE  
1161 N  NZ  . LYS A 132 ? 0.4908 0.4074 0.5483 -0.0208 0.0080  0.0527  133 LYS A NZ  
1162 N  N   . ALA A 133 ? 0.1449 0.0874 0.1142 -0.0368 0.0057  0.0038  134 ALA A N   
1163 C  CA  . ALA A 133 ? 0.1345 0.0782 0.0991 -0.0182 0.0006  0.0038  134 ALA A CA  
1164 C  C   . ALA A 133 ? 0.0964 0.0957 0.1164 -0.0135 -0.0031 -0.0115 134 ALA A C   
1165 O  O   . ALA A 133 ? 0.1145 0.1217 0.1129 -0.0148 -0.0020 -0.0149 134 ALA A O   
1166 C  CB  . ALA A 133 ? 0.1289 0.1000 0.1079 -0.0443 -0.0175 -0.0270 134 ALA A CB  
1167 N  N   . VAL A 134 ? 0.1177 0.1050 0.1363 -0.0107 0.0254  -0.0152 135 VAL A N   
1168 C  CA  . VAL A 134 ? 0.1456 0.1230 0.1009 -0.0162 -0.0003 -0.0076 135 VAL A CA  
1169 C  C   . VAL A 134 ? 0.0912 0.1120 0.1400 -0.0259 0.0211  0.0000  135 VAL A C   
1170 O  O   . VAL A 134 ? 0.1217 0.1018 0.1637 -0.0156 0.0252  0.0049  135 VAL A O   
1171 C  CB  . VAL A 134 ? 0.1379 0.1346 0.1122 -0.0432 0.0423  -0.0113 135 VAL A CB  
1172 C  CG1 . VAL A 134 ? 0.1837 0.1469 0.1273 -0.0559 -0.0282 -0.0153 135 VAL A CG1 
1173 C  CG2 . VAL A 134 ? 0.1274 0.1306 0.1761 -0.0082 0.0626  0.0082  135 VAL A CG2 
1174 N  N   . GLN A 135 ? 0.0935 0.0894 0.1585 -0.0328 0.0221  -0.0010 136 GLN A N   
1175 C  CA  . GLN A 135 ? 0.1115 0.1353 0.1756 -0.0274 0.0152  -0.0098 136 GLN A CA  
1176 C  C   . GLN A 135 ? 0.1165 0.1263 0.1641 -0.0015 -0.0110 -0.0027 136 GLN A C   
1177 O  O   . GLN A 135 ? 0.1321 0.1668 0.1711 -0.0350 -0.0190 -0.0220 136 GLN A O   
1178 C  CB  . GLN A 135 ? 0.1544 0.1226 0.1794 -0.0476 0.0068  -0.0379 136 GLN A CB  
1179 C  CG  . GLN A 135 ? 0.1776 0.1397 0.2273 0.0115  0.0414  0.0406  136 GLN A CG  
1180 C  CD  . GLN A 135 ? 0.2334 0.2291 0.2381 -0.0553 0.0107  -0.0063 136 GLN A CD  
1181 O  OE1 . GLN A 135 ? 0.3237 0.3400 0.3658 -0.0425 0.0179  0.0535  136 GLN A OE1 
1182 N  NE2 . GLN A 135 ? 0.2807 0.2746 0.2892 -0.1026 -0.0137 0.0130  136 GLN A NE2 
1183 N  N   . GLN A 136 ? 0.0989 0.1388 0.1332 -0.0260 0.0204  -0.0266 137 GLN A N   
1184 C  CA  . GLN A 136 ? 0.1267 0.1248 0.1187 0.0000  -0.0015 -0.0156 137 GLN A CA  
1185 C  C   . GLN A 136 ? 0.0942 0.1298 0.1025 0.0115  -0.0092 -0.0074 137 GLN A C   
1186 O  O   . GLN A 136 ? 0.1066 0.1168 0.0946 0.0015  -0.0108 -0.0203 137 GLN A O   
1187 C  CB  . GLN A 136 ? 0.1192 0.1122 0.1255 -0.0020 -0.0032 -0.0065 137 GLN A CB  
1188 C  CG  . GLN A 136 ? 0.2434 0.1456 0.1601 0.0107  -0.0252 0.0103  137 GLN A CG  
1189 C  CD  . GLN A 136 ? 0.1625 0.1482 0.2581 0.0097  0.0082  0.0333  137 GLN A CD  
1190 O  OE1 . GLN A 136 ? 0.2325 0.1668 0.2725 0.0030  -0.0149 -0.0741 137 GLN A OE1 
1191 N  NE2 . GLN A 136 ? 0.2767 0.2309 0.3676 -0.0328 0.0021  0.0520  137 GLN A NE2 
1192 N  N   . PRO A 137 ? 0.1233 0.1377 0.0926 -0.0003 -0.0280 -0.0293 138 PRO A N   
1193 C  CA  . PRO A 137 ? 0.1235 0.1500 0.0952 -0.0043 -0.0077 -0.0211 138 PRO A CA  
1194 C  C   . PRO A 137 ? 0.1147 0.1555 0.1106 0.0043  0.0049  -0.0267 138 PRO A C   
1195 O  O   . PRO A 137 ? 0.1727 0.1464 0.1626 0.0177  -0.0274 -0.0008 138 PRO A O   
1196 C  CB  . PRO A 137 ? 0.1607 0.1870 0.1106 0.0241  -0.0098 -0.0107 138 PRO A CB  
1197 C  CG  . PRO A 137 ? 0.2671 0.2210 0.1171 -0.0136 -0.0328 -0.0094 138 PRO A CG  
1198 C  CD  . PRO A 137 ? 0.1174 0.1907 0.1043 -0.0364 -0.0003 -0.0454 138 PRO A CD  
1199 N  N   . ASP A 138 ? 0.0824 0.1280 0.0998 0.0162  -0.0288 -0.0167 139 ASP A N   
1200 C  CA  . ASP A 138 ? 0.1000 0.1327 0.0913 0.0073  -0.0013 -0.0081 139 ASP A CA  
1201 C  C   . ASP A 138 ? 0.0946 0.0883 0.0998 -0.0063 -0.0038 -0.0078 139 ASP A C   
1202 O  O   . ASP A 138 ? 0.0937 0.1064 0.1370 0.0093  0.0003  -0.0065 139 ASP A O   
1203 C  CB  . ASP A 138 ? 0.1201 0.1296 0.1269 -0.0127 -0.0041 -0.0187 139 ASP A CB  
1204 C  CG  . ASP A 138 ? 0.1353 0.1564 0.1474 0.0088  -0.0206 -0.0252 139 ASP A CG  
1205 O  OD1 . ASP A 138 ? 0.1650 0.1195 0.1386 0.0298  -0.0071 -0.0247 139 ASP A OD1 
1206 O  OD2 . ASP A 138 ? 0.1676 0.2071 0.1952 0.0277  0.0452  -0.0540 139 ASP A OD2 
1207 N  N   . GLY A 139 ? 0.0978 0.0844 0.0777 -0.0034 -0.0087 -0.0146 140 GLY A N   
1208 C  CA  . GLY A 139 ? 0.0976 0.1000 0.0553 -0.0121 -0.0229 -0.0086 140 GLY A CA  
1209 C  C   . GLY A 139 ? 0.0705 0.0797 0.0944 -0.0280 -0.0017 0.0000  140 GLY A C   
1210 O  O   . GLY A 139 ? 0.1273 0.0535 0.0971 0.0217  -0.0185 -0.0183 140 GLY A O   
1211 N  N   . LEU A 140 ? 0.0530 0.0509 0.0829 -0.0159 -0.0027 -0.0034 141 LEU A N   
1212 C  CA  . LEU A 140 ? 0.0706 0.0430 0.0975 -0.0233 0.0159  -0.0275 141 LEU A CA  
1213 C  C   . LEU A 140 ? 0.0825 0.0614 0.0747 -0.0040 -0.0085 -0.0177 141 LEU A C   
1214 O  O   . LEU A 140 ? 0.0926 0.0659 0.0833 -0.0181 -0.0141 -0.0038 141 LEU A O   
1215 C  CB  . LEU A 140 ? 0.0879 0.0755 0.0648 0.0186  0.0136  0.0015  141 LEU A CB  
1216 C  CG  . LEU A 140 ? 0.1447 0.0989 0.1162 0.0450  0.0542  0.0204  141 LEU A CG  
1217 C  CD1 . LEU A 140 ? 0.0944 0.1009 0.1079 0.0351  0.0063  -0.0215 141 LEU A CD1 
1218 C  CD2 . LEU A 140 ? 0.2147 0.1385 0.1686 0.0522  0.0054  0.0487  141 LEU A CD2 
1219 N  N   . ALA A 141 ? 0.0553 0.0550 0.1161 -0.0157 -0.0279 -0.0223 142 ALA A N   
1220 C  CA  . ALA A 141 ? 0.0364 0.0472 0.1255 -0.0057 -0.0076 -0.0250 142 ALA A CA  
1221 C  C   . ALA A 141 ? 0.0601 0.0641 0.1043 -0.0119 -0.0114 -0.0013 142 ALA A C   
1222 O  O   . ALA A 141 ? 0.1183 0.0702 0.1090 0.0057  -0.0500 0.0143  142 ALA A O   
1223 C  CB  . ALA A 141 ? 0.0707 0.0799 0.1212 -0.0159 -0.0054 0.0005  142 ALA A CB  
1224 N  N   . VAL A 142 ? 0.0738 0.0530 0.1156 -0.0032 -0.0136 -0.0052 143 VAL A N   
1225 C  CA  . VAL A 142 ? 0.0684 0.0592 0.0953 -0.0027 0.0138  0.0021  143 VAL A CA  
1226 C  C   . VAL A 142 ? 0.0750 0.0741 0.0807 -0.0092 -0.0003 -0.0063 143 VAL A C   
1227 O  O   . VAL A 142 ? 0.0626 0.1000 0.0579 -0.0024 -0.0091 0.0143  143 VAL A O   
1228 C  CB  . VAL A 142 ? 0.0399 0.0728 0.0849 0.0262  -0.0010 -0.0066 143 VAL A CB  
1229 C  CG1 . VAL A 142 ? 0.0982 0.0860 0.0776 -0.0114 -0.0017 -0.0549 143 VAL A CG1 
1230 C  CG2 . VAL A 142 ? 0.0847 0.0901 0.1054 -0.0286 0.0148  0.0161  143 VAL A CG2 
1231 N  N   . LEU A 143 ? 0.0601 0.0628 0.0740 -0.0168 -0.0313 0.0026  144 LEU A N   
1232 C  CA  . LEU A 143 ? 0.0582 0.0725 0.0874 0.0013  -0.0164 -0.0225 144 LEU A CA  
1233 C  C   . LEU A 143 ? 0.0858 0.0555 0.0646 -0.0133 -0.0082 0.0118  144 LEU A C   
1234 O  O   . LEU A 143 ? 0.1000 0.0549 0.0614 -0.0181 -0.0076 0.0178  144 LEU A O   
1235 C  CB  . LEU A 143 ? 0.0566 0.1052 0.0951 -0.0185 -0.0261 0.0131  144 LEU A CB  
1236 C  CG  . LEU A 143 ? 0.0659 0.1138 0.1374 -0.0182 0.0020  -0.0097 144 LEU A CG  
1237 C  CD1 . LEU A 143 ? 0.0729 0.1421 0.1525 -0.0478 -0.0144 0.0131  144 LEU A CD1 
1238 C  CD2 . LEU A 143 ? 0.0784 0.1289 0.1630 0.0109  -0.0168 0.0005  144 LEU A CD2 
1239 N  N   . GLY A 144 ? 0.0394 0.0455 0.0913 -0.0096 -0.0059 0.0052  145 GLY A N   
1240 C  CA  . GLY A 144 ? 0.0745 0.0315 0.1074 -0.0102 -0.0142 0.0148  145 GLY A CA  
1241 C  C   . GLY A 144 ? 0.0515 0.0530 0.1013 0.0175  -0.0013 -0.0096 145 GLY A C   
1242 O  O   . GLY A 144 ? 0.0770 0.0723 0.0847 -0.0206 0.0037  -0.0132 145 GLY A O   
1243 N  N   . ILE A 145 ? 0.0732 0.0445 0.0776 -0.0085 -0.0124 -0.0212 146 ILE A N   
1244 C  CA  . ILE A 145 ? 0.0578 0.0605 0.0789 0.0033  -0.0395 -0.0177 146 ILE A CA  
1245 C  C   . ILE A 145 ? 0.0604 0.0777 0.0986 -0.0131 -0.0242 -0.0049 146 ILE A C   
1246 O  O   . ILE A 145 ? 0.0993 0.0750 0.0813 -0.0005 -0.0130 -0.0161 146 ILE A O   
1247 C  CB  . ILE A 145 ? 0.0844 0.0828 0.0825 -0.0055 -0.0136 0.0143  146 ILE A CB  
1248 C  CG1 . ILE A 145 ? 0.1129 0.0932 0.1493 -0.0031 -0.0386 -0.0031 146 ILE A CG1 
1249 C  CG2 . ILE A 145 ? 0.0640 0.1140 0.1651 -0.0313 -0.0531 -0.0218 146 ILE A CG2 
1250 C  CD1 . ILE A 145 ? 0.1062 0.0881 0.1016 0.0129  -0.0513 0.0333  146 ILE A CD1 
1251 N  N   . PHE A 146 ? 0.0606 0.0650 0.0804 -0.0068 -0.0041 0.0019  147 PHE A N   
1252 C  CA  . PHE A 146 ? 0.0962 0.0670 0.0878 0.0038  -0.0143 -0.0015 147 PHE A CA  
1253 C  C   . PHE A 146 ? 0.0849 0.0745 0.0988 -0.0071 -0.0013 -0.0024 147 PHE A C   
1254 O  O   . PHE A 146 ? 0.0772 0.0869 0.1320 0.0024  -0.0110 -0.0357 147 PHE A O   
1255 C  CB  . PHE A 146 ? 0.0481 0.0734 0.0928 0.0010  -0.0266 0.0240  147 PHE A CB  
1256 C  CG  . PHE A 146 ? 0.0337 0.0691 0.0625 0.0010  -0.0131 0.0108  147 PHE A CG  
1257 C  CD1 . PHE A 146 ? 0.0469 0.0452 0.1210 0.0091  0.0065  0.0071  147 PHE A CD1 
1258 C  CD2 . PHE A 146 ? 0.1257 0.0499 0.0958 -0.0140 -0.0161 -0.0109 147 PHE A CD2 
1259 C  CE1 . PHE A 146 ? 0.0935 0.0582 0.1055 -0.0010 -0.0164 -0.0210 147 PHE A CE1 
1260 C  CE2 . PHE A 146 ? 0.0498 0.0679 0.1133 -0.0049 -0.0099 0.0000  147 PHE A CE2 
1261 C  CZ  . PHE A 146 ? 0.0715 0.0594 0.1097 0.0157  -0.0282 0.0107  147 PHE A CZ  
1262 N  N   . LEU A 147 ? 0.0740 0.0539 0.0867 -0.0080 0.0015  -0.0194 148 LEU A N   
1263 C  CA  . LEU A 147 ? 0.1119 0.0472 0.0923 0.0023  -0.0141 -0.0262 148 LEU A CA  
1264 C  C   . LEU A 147 ? 0.0928 0.0618 0.0788 0.0065  -0.0208 0.0046  148 LEU A C   
1265 O  O   . LEU A 147 ? 0.0639 0.0678 0.1432 0.0052  -0.0141 0.0104  148 LEU A O   
1266 C  CB  . LEU A 147 ? 0.1506 0.0606 0.0646 0.0046  -0.0038 -0.0104 148 LEU A CB  
1267 C  CG  . LEU A 147 ? 0.1093 0.0668 0.1399 -0.0109 -0.0114 0.0044  148 LEU A CG  
1268 C  CD1 . LEU A 147 ? 0.1828 0.0709 0.0908 -0.0331 -0.0243 -0.0099 148 LEU A CD1 
1269 C  CD2 . LEU A 147 ? 0.1404 0.1122 0.1296 0.0099  -0.0203 -0.0085 148 LEU A CD2 
1270 N  N   . LYS A 148 ? 0.1447 0.0562 0.0964 -0.0192 -0.0041 -0.0168 149 LYS A N   
1271 C  CA  . LYS A 148 ? 0.1469 0.0790 0.1111 -0.0152 -0.0130 -0.0105 149 LYS A CA  
1272 C  C   . LYS A 148 ? 0.1178 0.0831 0.1195 -0.0028 -0.0348 -0.0173 149 LYS A C   
1273 O  O   . LYS A 148 ? 0.1031 0.1140 0.1327 0.0164  -0.0350 -0.0030 149 LYS A O   
1274 C  CB  . LYS A 148 ? 0.1241 0.0815 0.1391 -0.0066 -0.0245 0.0076  149 LYS A CB  
1275 C  CG  . LYS A 148 ? 0.1255 0.1104 0.1788 -0.0179 0.0299  0.0296  149 LYS A CG  
1276 C  CD  . LYS A 148 ? 0.2241 0.1791 0.2158 -0.0231 0.0066  0.0392  149 LYS A CD  
1277 C  CE  . LYS A 148 ? 0.2721 0.3472 0.2664 -0.0373 0.0516  0.0522  149 LYS A CE  
1278 N  NZ  . LYS A 148 ? 0.3382 0.3982 0.3300 -0.0703 0.0886  0.0741  149 LYS A NZ  
1279 N  N   . VAL A 149 ? 0.1421 0.0648 0.1298 0.0057  -0.0430 -0.0183 150 VAL A N   
1280 C  CA  . VAL A 149 ? 0.1040 0.0943 0.1564 -0.0264 -0.0373 -0.0252 150 VAL A CA  
1281 C  C   . VAL A 149 ? 0.1323 0.1238 0.1507 -0.0344 -0.0296 -0.0196 150 VAL A C   
1282 O  O   . VAL A 149 ? 0.1589 0.1285 0.1812 -0.0320 -0.0511 0.0204  150 VAL A O   
1283 C  CB  . VAL A 149 ? 0.1271 0.0967 0.1464 -0.0012 -0.0220 -0.0232 150 VAL A CB  
1284 C  CG1 . VAL A 149 ? 0.2004 0.1009 0.1597 -0.0057 -0.0133 -0.0190 150 VAL A CG1 
1285 C  CG2 . VAL A 149 ? 0.1064 0.1594 0.2273 -0.0300 -0.0068 -0.0564 150 VAL A CG2 
1286 N  N   . GLY A 150 ? 0.0986 0.0989 0.1518 -0.0320 -0.0403 -0.0192 151 GLY A N   
1287 C  CA  . GLY A 150 ? 0.1212 0.1542 0.1848 -0.0465 -0.0465 0.0013  151 GLY A CA  
1288 C  C   . GLY A 150 ? 0.1309 0.1203 0.1557 -0.0258 -0.0163 -0.0052 151 GLY A C   
1289 O  O   . GLY A 150 ? 0.1445 0.1226 0.1503 -0.0507 -0.0218 -0.0080 151 GLY A O   
1290 N  N   A SER A 151 ? 0.1400 0.1342 0.1704 -0.0151 -0.0302 -0.0007 152 SER A N   
1291 N  N   B SER A 151 ? 0.1447 0.1338 0.1787 -0.0219 -0.0256 -0.0024 152 SER A N   
1292 C  CA  A SER A 151 ? 0.1446 0.1368 0.1580 -0.0068 -0.0328 -0.0031 152 SER A CA  
1293 C  CA  B SER A 151 ? 0.1467 0.1388 0.1834 -0.0136 -0.0295 -0.0074 152 SER A CA  
1294 C  C   A SER A 151 ? 0.1605 0.1314 0.1454 -0.0093 -0.0324 -0.0049 152 SER A C   
1295 C  C   B SER A 151 ? 0.1481 0.1354 0.1555 -0.0142 -0.0292 -0.0108 152 SER A C   
1296 O  O   A SER A 151 ? 0.1792 0.1260 0.1128 -0.0071 -0.0359 -0.0092 152 SER A O   
1297 O  O   B SER A 151 ? 0.1018 0.1594 0.1449 -0.0023 -0.0401 -0.0273 152 SER A O   
1298 C  CB  A SER A 151 ? 0.1603 0.1695 0.1924 -0.0068 -0.0271 -0.0164 152 SER A CB  
1299 C  CB  B SER A 151 ? 0.1769 0.1648 0.2065 -0.0197 -0.0074 -0.0148 152 SER A CB  
1300 O  OG  A SER A 151 ? 0.1650 0.2356 0.1787 0.0100  -0.0187 0.0452  152 SER A OG  
1301 O  OG  B SER A 151 ? 0.2301 0.2286 0.2526 -0.0013 -0.0333 -0.0450 152 SER A OG  
1302 N  N   . ALA A 152 ? 0.1521 0.1183 0.1334 -0.0010 -0.0406 0.0031  153 ALA A N   
1303 C  CA  . ALA A 152 ? 0.1752 0.1057 0.1571 0.0048  -0.0313 -0.0038 153 ALA A CA  
1304 C  C   . ALA A 152 ? 0.1659 0.1323 0.1395 -0.0044 -0.0513 -0.0038 153 ALA A C   
1305 O  O   . ALA A 152 ? 0.1767 0.1154 0.2180 -0.0116 -0.0333 -0.0195 153 ALA A O   
1306 C  CB  . ALA A 152 ? 0.2056 0.1389 0.1384 0.0005  -0.0305 -0.0065 153 ALA A CB  
1307 N  N   . LYS A 153 ? 0.1853 0.0715 0.1821 -0.0087 -0.0460 -0.0015 154 LYS A N   
1308 C  CA  . LYS A 153 ? 0.1777 0.1027 0.1438 -0.0068 -0.0414 -0.0049 154 LYS A CA  
1309 C  C   . LYS A 153 ? 0.1537 0.1066 0.1521 0.0012  -0.0416 -0.0274 154 LYS A C   
1310 O  O   . LYS A 153 ? 0.1598 0.1186 0.1429 0.0073  -0.0531 -0.0187 154 LYS A O   
1311 C  CB  . LYS A 153 ? 0.1801 0.1074 0.1458 -0.0086 -0.0767 -0.0289 154 LYS A CB  
1312 C  CG  . LYS A 153 ? 0.2201 0.1206 0.1585 -0.0236 -0.0678 -0.0234 154 LYS A CG  
1313 C  CD  . LYS A 153 ? 0.2275 0.1463 0.1697 -0.0175 -0.0120 -0.0403 154 LYS A CD  
1314 C  CE  . LYS A 153 ? 0.2949 0.2240 0.1429 0.0259  -0.0776 -0.0425 154 LYS A CE  
1315 N  NZ  . LYS A 153 ? 0.4104 0.2870 0.2325 0.0110  0.0000  -0.0105 154 LYS A NZ  
1316 N  N   . PRO A 154 ? 0.1766 0.1429 0.1625 0.0105  -0.0395 0.0005  155 PRO A N   
1317 C  CA  . PRO A 154 ? 0.1864 0.1756 0.1862 -0.0082 -0.0405 0.0311  155 PRO A CA  
1318 C  C   . PRO A 154 ? 0.1679 0.1490 0.1630 0.0013  -0.0582 0.0031  155 PRO A C   
1319 O  O   . PRO A 154 ? 0.2050 0.1621 0.1842 -0.0001 -0.0766 0.0054  155 PRO A O   
1320 C  CB  . PRO A 154 ? 0.1806 0.1618 0.1907 0.0060  -0.0392 0.0148  155 PRO A CB  
1321 C  CG  . PRO A 154 ? 0.2089 0.2373 0.2386 0.0076  -0.0242 0.0282  155 PRO A CG  
1322 C  CD  . PRO A 154 ? 0.1586 0.2092 0.1803 0.0066  -0.0163 0.0130  155 PRO A CD  
1323 N  N   . GLY A 155 ? 0.1772 0.1192 0.1612 0.0066  -0.0535 -0.0007 156 GLY A N   
1324 C  CA  . GLY A 155 ? 0.1598 0.1083 0.1533 -0.0080 -0.0318 0.0104  156 GLY A CA  
1325 C  C   . GLY A 155 ? 0.1808 0.0939 0.1844 -0.0184 -0.0408 0.0211  156 GLY A C   
1326 O  O   . GLY A 155 ? 0.2233 0.1077 0.2329 -0.0054 -0.0577 0.0351  156 GLY A O   
1327 N  N   . LEU A 156 ? 0.1923 0.1399 0.1485 -0.0024 -0.0560 -0.0001 157 LEU A N   
1328 C  CA  . LEU A 156 ? 0.1939 0.1005 0.1106 -0.0103 -0.0608 -0.0063 157 LEU A CA  
1329 C  C   . LEU A 156 ? 0.1896 0.0932 0.1289 -0.0107 -0.0742 -0.0219 157 LEU A C   
1330 O  O   . LEU A 156 ? 0.2020 0.1183 0.1246 -0.0003 -0.0612 -0.0096 157 LEU A O   
1331 C  CB  . LEU A 156 ? 0.1949 0.1328 0.1411 -0.0251 -0.0714 0.0017  157 LEU A CB  
1332 C  CG  . LEU A 156 ? 0.1900 0.1043 0.1063 -0.0294 -0.0562 0.0077  157 LEU A CG  
1333 C  CD1 . LEU A 156 ? 0.2129 0.0926 0.1862 -0.0297 -0.0786 0.0080  157 LEU A CD1 
1334 C  CD2 . LEU A 156 ? 0.2239 0.1313 0.1131 -0.0060 -0.0430 0.0143  157 LEU A CD2 
1335 N  N   . GLN A 157 ? 0.1931 0.1249 0.1195 -0.0195 -0.0847 -0.0162 158 GLN A N   
1336 C  CA  . GLN A 157 ? 0.2034 0.1515 0.1483 -0.0362 -0.0568 -0.0269 158 GLN A CA  
1337 C  C   . GLN A 157 ? 0.1939 0.1456 0.1474 -0.0241 -0.0711 -0.0207 158 GLN A C   
1338 O  O   . GLN A 157 ? 0.2365 0.1332 0.1571 -0.0023 -0.0702 -0.0181 158 GLN A O   
1339 C  CB  . GLN A 157 ? 0.2422 0.1510 0.1515 -0.0428 -0.0825 -0.0231 158 GLN A CB  
1340 C  CG  . GLN A 157 ? 0.2248 0.1594 0.1572 -0.0097 -0.0504 -0.0149 158 GLN A CG  
1341 C  CD  . GLN A 157 ? 0.2150 0.1032 0.1952 -0.0329 0.0043  -0.0287 158 GLN A CD  
1342 O  OE1 . GLN A 157 ? 0.2793 0.1533 0.1719 -0.0362 -0.0493 -0.0020 158 GLN A OE1 
1343 N  NE2 . GLN A 157 ? 0.2807 0.1489 0.1377 -0.0219 -0.0228 -0.0230 158 GLN A NE2 
1344 N  N   A LYS A 158 ? 0.2137 0.1507 0.1580 -0.0248 -0.0526 -0.0107 159 LYS A N   
1345 N  N   B LYS A 158 ? 0.2119 0.1475 0.1580 -0.0244 -0.0577 -0.0096 159 LYS A N   
1346 C  CA  A LYS A 158 ? 0.2144 0.1443 0.1526 -0.0148 -0.0403 -0.0094 159 LYS A CA  
1347 C  CA  B LYS A 158 ? 0.2161 0.1400 0.1533 -0.0137 -0.0505 -0.0054 159 LYS A CA  
1348 C  C   A LYS A 158 ? 0.2254 0.1518 0.1532 -0.0081 -0.0397 -0.0003 159 LYS A C   
1349 C  C   B LYS A 158 ? 0.2280 0.1300 0.1422 -0.0115 -0.0472 -0.0074 159 LYS A C   
1350 O  O   A LYS A 158 ? 0.2297 0.1562 0.1530 0.0041  -0.0428 0.0100  159 LYS A O   
1351 O  O   B LYS A 158 ? 0.2395 0.0971 0.1027 -0.0097 -0.0785 -0.0177 159 LYS A O   
1352 C  CB  A LYS A 158 ? 0.2366 0.1569 0.1611 -0.0076 -0.0250 -0.0052 159 LYS A CB  
1353 C  CB  B LYS A 158 ? 0.2185 0.1543 0.1706 -0.0021 -0.0405 0.0013  159 LYS A CB  
1354 C  CG  A LYS A 158 ? 0.2462 0.2064 0.2225 -0.0027 0.0030  -0.0137 159 LYS A CG  
1355 C  CG  B LYS A 158 ? 0.2460 0.1756 0.1941 -0.0154 -0.0344 0.0024  159 LYS A CG  
1356 C  CD  A LYS A 158 ? 0.3512 0.3371 0.2979 -0.0003 0.0003  -0.0048 159 LYS A CD  
1357 C  CD  B LYS A 158 ? 0.2326 0.1788 0.1999 0.0116  -0.0456 0.0285  159 LYS A CD  
1358 C  CE  A LYS A 158 ? 0.3238 0.3285 0.2978 -0.0071 -0.0375 -0.0190 159 LYS A CE  
1359 C  CE  B LYS A 158 ? 0.2237 0.1934 0.2329 -0.0193 -0.0463 0.0231  159 LYS A CE  
1360 N  NZ  A LYS A 158 ? 0.3756 0.3950 0.3587 -0.0107 -0.0167 -0.0277 159 LYS A NZ  
1361 N  NZ  B LYS A 158 ? 0.2111 0.2558 0.1601 0.0348  -0.0172 0.0335  159 LYS A NZ  
1362 N  N   . VAL A 159 ? 0.2230 0.1167 0.1424 -0.0065 -0.0615 -0.0118 160 VAL A N   
1363 C  CA  . VAL A 159 ? 0.2114 0.1228 0.1171 -0.0125 -0.0544 -0.0188 160 VAL A CA  
1364 C  C   . VAL A 159 ? 0.2207 0.1149 0.1345 -0.0170 -0.0439 -0.0175 160 VAL A C   
1365 O  O   . VAL A 159 ? 0.2329 0.1231 0.1404 -0.0182 -0.0450 -0.0030 160 VAL A O   
1366 C  CB  . VAL A 159 ? 0.2293 0.1413 0.1106 -0.0132 -0.0680 -0.0241 160 VAL A CB  
1367 C  CG1 . VAL A 159 ? 0.2297 0.1292 0.1307 -0.0384 -0.0412 0.0300  160 VAL A CG1 
1368 C  CG2 . VAL A 159 ? 0.2469 0.1639 0.1303 0.0346  -0.0504 -0.0024 160 VAL A CG2 
1369 N  N   . VAL A 160 ? 0.2039 0.0912 0.1172 -0.0262 -0.0183 -0.0126 161 VAL A N   
1370 C  CA  . VAL A 160 ? 0.2508 0.1235 0.1449 -0.0185 -0.0048 -0.0204 161 VAL A CA  
1371 C  C   . VAL A 160 ? 0.2520 0.1084 0.1410 -0.0214 -0.0240 -0.0197 161 VAL A C   
1372 O  O   . VAL A 160 ? 0.2887 0.1177 0.1400 -0.0245 -0.0219 -0.0275 161 VAL A O   
1373 C  CB  . VAL A 160 ? 0.2790 0.0754 0.1352 0.0028  0.0237  -0.0276 161 VAL A CB  
1374 C  CG1 . VAL A 160 ? 0.2829 0.1443 0.2020 -0.0197 -0.0219 -0.0260 161 VAL A CG1 
1375 C  CG2 . VAL A 160 ? 0.3386 0.1314 0.1745 -0.0020 0.0275  0.0116  161 VAL A CG2 
1376 N  N   . ASP A 161 ? 0.2725 0.1543 0.1183 -0.0397 -0.0417 -0.0104 162 ASP A N   
1377 C  CA  . ASP A 161 ? 0.3034 0.1913 0.1428 -0.0535 -0.0498 0.0013  162 ASP A CA  
1378 C  C   . ASP A 161 ? 0.3235 0.2053 0.1407 -0.0465 -0.0350 0.0031  162 ASP A C   
1379 O  O   . ASP A 161 ? 0.3381 0.2337 0.1682 -0.0820 -0.0313 -0.0120 162 ASP A O   
1380 C  CB  . ASP A 161 ? 0.3185 0.2006 0.1568 -0.0480 -0.0164 -0.0211 162 ASP A CB  
1381 C  CG  . ASP A 161 ? 0.3183 0.2178 0.1421 -0.0377 -0.0240 -0.0146 162 ASP A CG  
1382 O  OD1 . ASP A 161 ? 0.3740 0.2230 0.2337 -0.0700 -0.0164 -0.0223 162 ASP A OD1 
1383 O  OD2 . ASP A 161 ? 0.3458 0.2700 0.1759 -0.0581 -0.0548 -0.0439 162 ASP A OD2 
1384 N  N   . VAL A 162 ? 0.2991 0.1553 0.1251 -0.0403 -0.0649 0.0138  163 VAL A N   
1385 C  CA  . VAL A 162 ? 0.3169 0.1759 0.1589 -0.0310 -0.0432 0.0038  163 VAL A CA  
1386 C  C   . VAL A 162 ? 0.3083 0.1533 0.1181 -0.0384 -0.0244 -0.0020 163 VAL A C   
1387 O  O   . VAL A 162 ? 0.3319 0.1665 0.0797 -0.0513 -0.0174 0.0044  163 VAL A O   
1388 C  CB  . VAL A 162 ? 0.3389 0.1637 0.1916 -0.0199 -0.0368 0.0063  163 VAL A CB  
1389 C  CG1 . VAL A 162 ? 0.3075 0.1199 0.2061 0.0068  -0.0601 -0.0133 163 VAL A CG1 
1390 C  CG2 . VAL A 162 ? 0.2967 0.1738 0.2196 -0.0054 -0.0344 0.0254  163 VAL A CG2 
1391 N  N   . LEU A 163 ? 0.3062 0.1352 0.1630 -0.0302 -0.0251 0.0000  164 LEU A N   
1392 C  CA  . LEU A 163 ? 0.2808 0.1295 0.0870 -0.0307 -0.0273 0.0166  164 LEU A CA  
1393 C  C   . LEU A 163 ? 0.2899 0.1281 0.1194 -0.0198 -0.0141 0.0063  164 LEU A C   
1394 O  O   . LEU A 163 ? 0.3104 0.1548 0.1248 -0.0177 0.0059  -0.0031 164 LEU A O   
1395 C  CB  . LEU A 163 ? 0.2685 0.0962 0.1177 -0.0425 -0.0254 -0.0048 164 LEU A CB  
1396 C  CG  . LEU A 163 ? 0.2800 0.1296 0.0851 -0.0579 -0.0040 0.0212  164 LEU A CG  
1397 C  CD1 . LEU A 163 ? 0.2538 0.1456 0.1278 -0.0322 -0.0046 0.0291  164 LEU A CD1 
1398 C  CD2 . LEU A 163 ? 0.2569 0.1400 0.0734 -0.0274 -0.0346 0.0019  164 LEU A CD2 
1399 N  N   . ASP A 164 ? 0.3357 0.1763 0.1251 -0.0408 -0.0015 -0.0119 165 ASP A N   
1400 C  CA  . ASP A 164 ? 0.3817 0.2070 0.1701 -0.0472 0.0026  -0.0211 165 ASP A CA  
1401 C  C   . ASP A 164 ? 0.3725 0.2354 0.1684 -0.0379 0.0026  0.0065  165 ASP A C   
1402 O  O   . ASP A 164 ? 0.4226 0.2276 0.2309 -0.0151 0.0410  0.0208  165 ASP A O   
1403 C  CB  . ASP A 164 ? 0.4100 0.2338 0.1834 -0.0586 -0.0049 -0.0252 165 ASP A CB  
1404 C  CG  . ASP A 164 ? 0.3949 0.2915 0.2018 -0.0662 -0.0146 -0.0401 165 ASP A CG  
1405 O  OD1 . ASP A 164 ? 0.4747 0.3289 0.2074 -0.0820 0.0187  -0.0439 165 ASP A OD1 
1406 O  OD2 . ASP A 164 ? 0.5514 0.4627 0.2311 -0.0265 0.0476  -0.0614 165 ASP A OD2 
1407 N  N   . SER A 165 ? 0.3632 0.1964 0.1292 -0.0538 -0.0126 0.0218  166 SER A N   
1408 C  CA  . SER A 165 ? 0.3564 0.2126 0.1511 -0.0449 -0.0160 0.0162  166 SER A CA  
1409 C  C   . SER A 165 ? 0.3463 0.2022 0.1070 -0.0555 -0.0049 0.0192  166 SER A C   
1410 O  O   . SER A 165 ? 0.4043 0.1896 0.1277 -0.0436 0.0063  0.0322  166 SER A O   
1411 C  CB  . SER A 165 ? 0.3863 0.2462 0.1982 -0.0452 0.0051  0.0168  166 SER A CB  
1412 O  OG  . SER A 165 ? 0.4470 0.2119 0.1970 0.0012  -0.0136 0.0138  166 SER A OG  
1413 N  N   . ILE A 166 ? 0.3174 0.1615 0.0886 -0.0198 -0.0184 0.0260  167 ILE A N   
1414 C  CA  . ILE A 166 ? 0.2717 0.1424 0.1034 -0.0359 0.0181  -0.0041 167 ILE A CA  
1415 C  C   . ILE A 166 ? 0.2605 0.1342 0.1147 -0.0143 0.0122  -0.0313 167 ILE A C   
1416 O  O   . ILE A 166 ? 0.2476 0.1609 0.0842 -0.0478 0.0291  -0.0038 167 ILE A O   
1417 C  CB  . ILE A 166 ? 0.2595 0.1604 0.0813 -0.0370 0.0183  -0.0166 167 ILE A CB  
1418 C  CG1 . ILE A 166 ? 0.2616 0.1859 0.0725 -0.0555 0.0010  -0.0104 167 ILE A CG1 
1419 C  CG2 . ILE A 166 ? 0.2638 0.1425 0.1468 -0.0302 0.0161  0.0008  167 ILE A CG2 
1420 C  CD1 . ILE A 166 ? 0.3034 0.1639 0.1075 -0.0197 0.0041  -0.0091 167 ILE A CD1 
1421 N  N   . LYS A 167 ? 0.2723 0.1389 0.1323 -0.0225 0.0399  -0.0384 168 LYS A N   
1422 C  CA  . LYS A 167 ? 0.2774 0.1594 0.1194 -0.0175 0.0127  -0.0469 168 LYS A CA  
1423 C  C   . LYS A 167 ? 0.2651 0.1670 0.1156 -0.0366 0.0463  -0.0297 168 LYS A C   
1424 O  O   . LYS A 167 ? 0.2576 0.1694 0.1142 -0.0511 0.0329  -0.0017 168 LYS A O   
1425 C  CB  . LYS A 167 ? 0.3203 0.1131 0.1113 -0.0048 0.0099  -0.0684 168 LYS A CB  
1426 C  CG  . LYS A 167 ? 0.2864 0.1877 0.1763 -0.0116 -0.0032 -0.0261 168 LYS A CG  
1427 C  CD  . LYS A 167 ? 0.3512 0.2110 0.2090 -0.0017 0.0000  -0.0869 168 LYS A CD  
1428 C  CE  . LYS A 167 ? 0.4174 0.2772 0.3009 0.0013  -0.0151 -0.0692 168 LYS A CE  
1429 N  NZ  . LYS A 167 ? 0.4377 0.3888 0.3542 0.0144  0.0281  -0.0843 168 LYS A NZ  
1430 N  N   . THR A 168 ? 0.2851 0.1662 0.1156 -0.0293 0.0493  0.0015  169 THR A N   
1431 C  CA  . THR A 168 ? 0.2526 0.1619 0.1057 -0.0278 0.0485  -0.0121 169 THR A CA  
1432 C  C   . THR A 168 ? 0.2236 0.1720 0.1054 -0.0237 0.0649  -0.0006 169 THR A C   
1433 O  O   . THR A 168 ? 0.2782 0.1625 0.1609 -0.0489 0.0675  0.0057  169 THR A O   
1434 C  CB  . THR A 168 ? 0.3093 0.1851 0.1492 -0.0284 0.0496  -0.0131 169 THR A CB  
1435 O  OG1 . THR A 168 ? 0.3233 0.2424 0.1237 -0.0518 0.0395  0.0032  169 THR A OG1 
1436 C  CG2 . THR A 168 ? 0.3082 0.1395 0.1281 -0.0302 0.0749  -0.0240 169 THR A CG2 
1437 N  N   . LYS A 169 ? 0.2603 0.1934 0.1263 -0.0577 0.0707  -0.0038 170 LYS A N   
1438 C  CA  . LYS A 169 ? 0.2761 0.1709 0.1194 -0.0350 0.0274  0.0060  170 LYS A CA  
1439 C  C   . LYS A 169 ? 0.2775 0.1701 0.1519 -0.0419 0.0417  0.0278  170 LYS A C   
1440 O  O   . LYS A 169 ? 0.3134 0.2348 0.1255 -0.0568 0.0276  -0.0035 170 LYS A O   
1441 C  CB  . LYS A 169 ? 0.2291 0.1503 0.1580 -0.0107 0.0320  -0.0120 170 LYS A CB  
1442 C  CG  . LYS A 169 ? 0.2433 0.1831 0.2122 -0.0162 0.0270  -0.0436 170 LYS A CG  
1443 C  CD  . LYS A 169 ? 0.2598 0.2006 0.2276 -0.0228 0.0386  -0.0271 170 LYS A CD  
1444 C  CE  . LYS A 169 ? 0.3026 0.3795 0.3464 -0.0163 0.0421  -0.0368 170 LYS A CE  
1445 N  NZ  . LYS A 169 ? 0.3968 0.4575 0.4192 0.0247  0.0003  0.0097  170 LYS A NZ  
1446 N  N   . GLY A 170 ? 0.3235 0.1612 0.1185 -0.0454 0.0287  0.0248  171 GLY A N   
1447 C  CA  . GLY A 170 ? 0.3138 0.1632 0.1942 -0.0342 -0.0102 0.0509  171 GLY A CA  
1448 C  C   . GLY A 170 ? 0.3328 0.1852 0.1975 -0.0306 0.0024  0.0303  171 GLY A C   
1449 O  O   . GLY A 170 ? 0.3555 0.1641 0.2590 -0.0599 -0.0038 0.0412  171 GLY A O   
1450 N  N   . LYS A 171 ? 0.2910 0.1497 0.1382 -0.0627 0.0307  0.0370  172 LYS A N   
1451 C  CA  . LYS A 171 ? 0.2893 0.1661 0.1515 -0.0333 0.0313  0.0233  172 LYS A CA  
1452 C  C   . LYS A 171 ? 0.2703 0.1557 0.1224 -0.0201 0.0122  0.0176  172 LYS A C   
1453 O  O   . LYS A 171 ? 0.3029 0.1751 0.0987 -0.0131 0.0161  0.0263  172 LYS A O   
1454 C  CB  . LYS A 171 ? 0.2901 0.2013 0.1576 -0.0566 0.0092  0.0125  172 LYS A CB  
1455 C  CG  . LYS A 171 ? 0.3216 0.2072 0.1995 -0.0068 0.0241  -0.0353 172 LYS A CG  
1456 C  CD  . LYS A 171 ? 0.3300 0.2505 0.2487 -0.0362 0.0201  -0.0133 172 LYS A CD  
1457 C  CE  . LYS A 171 ? 0.3896 0.2993 0.2768 -0.0307 -0.0100 -0.0164 172 LYS A CE  
1458 N  NZ  . LYS A 171 ? 0.4318 0.2807 0.2359 -0.0537 0.0489  -0.0116 172 LYS A NZ  
1459 N  N   . SER A 172 ? 0.3142 0.1708 0.1219 -0.0122 0.0118  0.0289  173 SER A N   
1460 C  CA  . SER A 172 ? 0.3285 0.1945 0.1104 -0.0028 0.0185  0.0063  173 SER A CA  
1461 C  C   . SER A 172 ? 0.3083 0.1930 0.1246 0.0122  0.0226  0.0227  173 SER A C   
1462 O  O   . SER A 172 ? 0.4050 0.2595 0.0702 0.0219  0.0082  0.0320  173 SER A O   
1463 C  CB  . SER A 172 ? 0.3210 0.1870 0.1431 -0.0175 0.0211  0.0225  173 SER A CB  
1464 O  OG  . SER A 172 ? 0.3952 0.1956 0.1758 -0.0052 0.0230  0.0821  173 SER A OG  
1465 N  N   . ALA A 173 ? 0.3134 0.2232 0.1350 0.0381  -0.0097 0.0078  174 ALA A N   
1466 C  CA  . ALA A 173 ? 0.3120 0.2301 0.1084 0.0571  -0.0159 0.0263  174 ALA A CA  
1467 C  C   . ALA A 173 ? 0.3296 0.2294 0.1235 0.0595  -0.0207 0.0274  174 ALA A C   
1468 O  O   . ALA A 173 ? 0.3633 0.1894 0.0736 0.0601  -0.0097 0.0296  174 ALA A O   
1469 C  CB  . ALA A 173 ? 0.3325 0.2377 0.1291 0.0615  -0.0251 -0.0108 174 ALA A CB  
1470 N  N   . ASP A 174 ? 0.3384 0.2782 0.1497 0.0568  -0.0237 0.0665  175 ASP A N   
1471 C  CA  . ASP A 174 ? 0.3226 0.2483 0.1618 0.0386  -0.0219 0.0520  175 ASP A CA  
1472 C  C   . ASP A 174 ? 0.3384 0.2383 0.1512 0.0513  -0.0361 0.0452  175 ASP A C   
1473 O  O   . ASP A 174 ? 0.3848 0.2171 0.1539 0.0590  -0.0320 -0.0089 175 ASP A O   
1474 C  CB  . ASP A 174 ? 0.2901 0.2840 0.2042 0.0496  -0.0249 0.0564  175 ASP A CB  
1475 C  CG  . ASP A 174 ? 0.3744 0.3634 0.3037 0.0007  -0.0205 0.0397  175 ASP A CG  
1476 O  OD1 . ASP A 174 ? 0.4045 0.5080 0.3166 -0.0109 -0.0785 0.0152  175 ASP A OD1 
1477 O  OD2 . ASP A 174 ? 0.3485 0.4174 0.2800 -0.0098 -0.0551 0.0081  175 ASP A OD2 
1478 N  N   . PHE A 175 ? 0.2998 0.2024 0.1360 0.0335  0.0065  0.0078  176 PHE A N   
1479 C  CA  . PHE A 175 ? 0.3080 0.1727 0.1004 0.0315  -0.0222 0.0237  176 PHE A CA  
1480 C  C   . PHE A 175 ? 0.2831 0.1664 0.1206 0.0130  -0.0211 0.0361  176 PHE A C   
1481 O  O   . PHE A 175 ? 0.3070 0.2125 0.1212 0.0487  -0.0653 0.0081  176 PHE A O   
1482 C  CB  . PHE A 175 ? 0.3149 0.1500 0.1284 0.0122  -0.0263 0.0320  176 PHE A CB  
1483 C  CG  . PHE A 175 ? 0.2853 0.1031 0.1145 0.0175  -0.0472 0.0196  176 PHE A CG  
1484 C  CD1 . PHE A 175 ? 0.3320 0.1463 0.1539 -0.0153 -0.0242 -0.0166 176 PHE A CD1 
1485 C  CD2 . PHE A 175 ? 0.2777 0.1266 0.1224 -0.0017 -0.0185 0.0147  176 PHE A CD2 
1486 C  CE1 . PHE A 175 ? 0.3443 0.1357 0.1546 -0.0038 -0.0215 -0.0100 176 PHE A CE1 
1487 C  CE2 . PHE A 175 ? 0.2544 0.1469 0.1736 0.0153  -0.0377 0.0302  176 PHE A CE2 
1488 C  CZ  . PHE A 175 ? 0.3476 0.1115 0.1583 -0.0104 -0.0315 0.0019  176 PHE A CZ  
1489 N  N   . THR A 176 ? 0.2922 0.1389 0.1299 0.0344  -0.0485 0.0335  177 THR A N   
1490 C  CA  . THR A 176 ? 0.2994 0.1621 0.1336 0.0206  -0.0513 0.0423  177 THR A CA  
1491 C  C   . THR A 176 ? 0.2950 0.1677 0.1183 0.0093  -0.0663 0.0377  177 THR A C   
1492 O  O   . THR A 176 ? 0.2987 0.1524 0.1032 -0.0098 -0.0692 0.0173  177 THR A O   
1493 C  CB  . THR A 176 ? 0.3161 0.1587 0.1456 0.0019  -0.0676 0.0546  177 THR A CB  
1494 O  OG1 . THR A 176 ? 0.3722 0.1993 0.1515 0.0641  -0.0847 0.0248  177 THR A OG1 
1495 C  CG2 . THR A 176 ? 0.3267 0.2313 0.2144 0.0020  -0.0592 0.0562  177 THR A CG2 
1496 N  N   . ASN A 177 ? 0.2845 0.1526 0.1049 0.0059  -0.0732 0.0315  178 ASN A N   
1497 C  CA  . ASN A 177 ? 0.2808 0.1420 0.1324 0.0146  -0.0754 0.0258  178 ASN A CA  
1498 C  C   . ASN A 177 ? 0.2674 0.1421 0.1464 0.0006  -0.0756 0.0322  178 ASN A C   
1499 O  O   . ASN A 177 ? 0.3176 0.1600 0.2173 0.0028  -0.0992 0.0878  178 ASN A O   
1500 C  CB  . ASN A 177 ? 0.2749 0.1342 0.1429 0.0173  -0.0625 0.0414  178 ASN A CB  
1501 C  CG  . ASN A 177 ? 0.2581 0.1982 0.1639 0.0456  -0.0557 0.0317  178 ASN A CG  
1502 O  OD1 . ASN A 177 ? 0.3166 0.1853 0.1702 0.0173  -0.0077 0.0078  178 ASN A OD1 
1503 N  ND2 . ASN A 177 ? 0.2518 0.1654 0.1604 0.0282  -0.0456 0.0781  178 ASN A ND2 
1504 N  N   . PHE A 178 ? 0.2720 0.1013 0.1007 0.0295  -0.0810 0.0403  179 PHE A N   
1505 C  CA  . PHE A 178 ? 0.2619 0.1291 0.1052 0.0048  -0.0542 0.0351  179 PHE A CA  
1506 C  C   . PHE A 178 ? 0.2597 0.1023 0.0983 -0.0012 -0.0465 0.0232  179 PHE A C   
1507 O  O   . PHE A 178 ? 0.2828 0.1187 0.1203 0.0010  -0.0877 0.0138  179 PHE A O   
1508 C  CB  . PHE A 178 ? 0.2628 0.1140 0.1414 0.0135  -0.0434 0.0527  179 PHE A CB  
1509 C  CG  . PHE A 178 ? 0.2320 0.1059 0.1253 -0.0252 -0.0019 0.0491  179 PHE A CG  
1510 C  CD1 . PHE A 178 ? 0.2736 0.1164 0.1324 -0.0463 -0.0337 0.0242  179 PHE A CD1 
1511 C  CD2 . PHE A 178 ? 0.1934 0.1722 0.0899 -0.0220 0.0142  0.0353  179 PHE A CD2 
1512 C  CE1 . PHE A 178 ? 0.2968 0.1216 0.1185 -0.0368 -0.0562 0.0110  179 PHE A CE1 
1513 C  CE2 . PHE A 178 ? 0.1859 0.1399 0.0844 -0.0035 -0.0476 -0.0070 179 PHE A CE2 
1514 C  CZ  . PHE A 178 ? 0.2150 0.1210 0.1237 0.0115  -0.0408 0.0177  179 PHE A CZ  
1515 N  N   . ASP A 179 ? 0.2366 0.1630 0.1115 0.0043  -0.0549 0.0304  180 ASP A N   
1516 C  CA  . ASP A 179 ? 0.1898 0.1407 0.1129 0.0226  -0.0568 0.0335  180 ASP A CA  
1517 C  C   . ASP A 179 ? 0.1756 0.1093 0.1156 0.0276  -0.0487 0.0138  180 ASP A C   
1518 O  O   . ASP A 179 ? 0.1745 0.1206 0.1327 -0.0296 -0.0340 -0.0005 180 ASP A O   
1519 C  CB  . ASP A 179 ? 0.2024 0.2027 0.1409 0.0097  -0.0760 0.0370  180 ASP A CB  
1520 C  CG  . ASP A 179 ? 0.1964 0.2570 0.2204 -0.0006 -0.0249 0.0168  180 ASP A CG  
1521 O  OD1 . ASP A 179 ? 0.1921 0.1522 0.1870 0.0126  -0.0454 0.0120  180 ASP A OD1 
1522 O  OD2 . ASP A 179 ? 0.2290 0.3576 0.2703 -0.0057 -0.0811 0.0244  180 ASP A OD2 
1523 N  N   . PRO A 180 ? 0.1551 0.1039 0.1080 0.0140  -0.0548 0.0035  181 PRO A N   
1524 C  CA  . PRO A 180 ? 0.1352 0.1528 0.1248 -0.0012 -0.0527 0.0104  181 PRO A CA  
1525 C  C   . PRO A 180 ? 0.1309 0.1198 0.1160 -0.0010 -0.0509 -0.0012 181 PRO A C   
1526 O  O   . PRO A 180 ? 0.1515 0.1077 0.1287 0.0041  -0.0689 0.0089  181 PRO A O   
1527 C  CB  . PRO A 180 ? 0.1503 0.1715 0.1339 -0.0041 -0.0755 0.0242  181 PRO A CB  
1528 C  CG  . PRO A 180 ? 0.1407 0.1521 0.1594 -0.0105 -0.0692 0.0179  181 PRO A CG  
1529 C  CD  . PRO A 180 ? 0.1701 0.1259 0.1223 -0.0037 -0.0711 0.0148  181 PRO A CD  
1530 N  N   . ARG A 181 ? 0.1113 0.1246 0.1440 0.0000  -0.0395 0.0052  182 ARG A N   
1531 C  CA  . ARG A 181 ? 0.1359 0.1159 0.1522 0.0096  -0.0357 -0.0129 182 ARG A CA  
1532 C  C   . ARG A 181 ? 0.1722 0.1235 0.1528 0.0068  -0.0659 0.0108  182 ARG A C   
1533 O  O   . ARG A 181 ? 0.2140 0.1713 0.1246 -0.0168 -0.0640 0.0285  182 ARG A O   
1534 C  CB  . ARG A 181 ? 0.1332 0.1371 0.2016 0.0142  -0.0287 -0.0071 182 ARG A CB  
1535 C  CG  . ARG A 181 ? 0.1449 0.1260 0.1952 0.0366  -0.0340 -0.0017 182 ARG A CG  
1536 C  CD  . ARG A 181 ? 0.1618 0.1418 0.2843 -0.0088 -0.0176 0.0566  182 ARG A CD  
1537 N  NE  . ARG A 181 ? 0.1025 0.1733 0.2835 -0.0149 -0.0489 0.0590  182 ARG A NE  
1538 C  CZ  . ARG A 181 ? 0.1589 0.2678 0.2768 0.0243  -0.0049 0.0384  182 ARG A CZ  
1539 N  NH1 . ARG A 181 ? 0.2223 0.2930 0.3609 0.0652  -0.0015 0.0516  182 ARG A NH1 
1540 N  NH2 . ARG A 181 ? 0.1270 0.3716 0.3065 0.0465  0.0010  0.0697  182 ARG A NH2 
1541 N  N   . GLY A 182 ? 0.1719 0.1093 0.1637 0.0149  -0.0744 -0.0031 183 GLY A N   
1542 C  CA  . GLY A 182 ? 0.2079 0.0847 0.1594 0.0186  -0.0917 0.0093  183 GLY A CA  
1543 C  C   . GLY A 182 ? 0.2070 0.1289 0.1737 0.0096  -0.0771 0.0129  183 GLY A C   
1544 O  O   . GLY A 182 ? 0.2588 0.1142 0.2146 0.0215  -0.1190 0.0083  183 GLY A O   
1545 N  N   . LEU A 183 ? 0.1664 0.1381 0.1088 0.0146  -0.0850 0.0068  184 LEU A N   
1546 C  CA  . LEU A 183 ? 0.1650 0.1321 0.1206 0.0114  -0.0690 0.0077  184 LEU A CA  
1547 C  C   . LEU A 183 ? 0.1677 0.1142 0.1154 0.0130  -0.0456 0.0103  184 LEU A C   
1548 O  O   . LEU A 183 ? 0.1880 0.1391 0.1234 0.0197  -0.0386 0.0286  184 LEU A O   
1549 C  CB  . LEU A 183 ? 0.1756 0.1600 0.1164 0.0086  -0.0318 0.0326  184 LEU A CB  
1550 C  CG  . LEU A 183 ? 0.1676 0.1298 0.1305 0.0220  -0.0299 0.0342  184 LEU A CG  
1551 C  CD1 . LEU A 183 ? 0.1826 0.2072 0.0996 -0.0049 -0.0489 0.0617  184 LEU A CD1 
1552 C  CD2 . LEU A 183 ? 0.2896 0.1332 0.1659 -0.0082 -0.0315 -0.0153 184 LEU A CD2 
1553 N  N   . LEU A 184 ? 0.1413 0.1199 0.1345 -0.0052 -0.0511 0.0119  185 LEU A N   
1554 C  CA  . LEU A 184 ? 0.1052 0.1203 0.1427 -0.0421 -0.0348 0.0098  185 LEU A CA  
1555 C  C   . LEU A 184 ? 0.1761 0.1307 0.1680 -0.0480 -0.0747 0.0377  185 LEU A C   
1556 O  O   . LEU A 184 ? 0.2117 0.2020 0.2675 -0.1068 -0.1253 0.0650  185 LEU A O   
1557 C  CB  . LEU A 184 ? 0.1345 0.1059 0.1280 -0.0392 -0.0351 0.0049  185 LEU A CB  
1558 C  CG  . LEU A 184 ? 0.0734 0.1264 0.1558 -0.0164 -0.0309 0.0005  185 LEU A CG  
1559 C  CD1 . LEU A 184 ? 0.1280 0.2054 0.1230 0.0164  -0.0198 -0.0007 185 LEU A CD1 
1560 C  CD2 . LEU A 184 ? 0.1158 0.1512 0.1605 -0.0357 -0.0623 0.0186  185 LEU A CD2 
1561 N  N   . PRO A 185 ? 0.1192 0.1368 0.1729 -0.0183 -0.0505 0.0359  186 PRO A N   
1562 C  CA  . PRO A 185 ? 0.1066 0.1210 0.1661 -0.0206 -0.0298 0.0204  186 PRO A CA  
1563 C  C   . PRO A 185 ? 0.0962 0.1077 0.2013 -0.0086 -0.0377 0.0254  186 PRO A C   
1564 O  O   . PRO A 185 ? 0.0754 0.1115 0.2910 0.0195  -0.0438 0.0485  186 PRO A O   
1565 C  CB  . PRO A 185 ? 0.1050 0.1124 0.1514 -0.0136 -0.0259 0.0261  186 PRO A CB  
1566 C  CG  . PRO A 185 ? 0.0919 0.1134 0.1305 0.0256  -0.0348 -0.0140 186 PRO A CG  
1567 C  CD  . PRO A 185 ? 0.1079 0.1152 0.1450 -0.0205 -0.0434 -0.0015 186 PRO A CD  
1568 N  N   A GLU A 186 ? 0.0901 0.1500 0.2056 -0.0278 -0.0210 0.0194  187 GLU A N   
1569 N  N   B GLU A 186 ? 0.0881 0.1460 0.2046 -0.0373 -0.0234 0.0175  187 GLU A N   
1570 C  CA  A GLU A 186 ? 0.0966 0.1596 0.1971 -0.0254 -0.0214 0.0291  187 GLU A CA  
1571 C  CA  B GLU A 186 ? 0.0980 0.1533 0.1974 -0.0432 -0.0182 0.0292  187 GLU A CA  
1572 C  C   A GLU A 186 ? 0.0799 0.1432 0.2153 -0.0160 -0.0154 0.0162  187 GLU A C   
1573 C  C   B GLU A 186 ? 0.0790 0.1241 0.1992 -0.0348 -0.0068 0.0251  187 GLU A C   
1574 O  O   A GLU A 186 ? 0.1034 0.1447 0.2480 -0.0077 -0.0114 0.0054  187 GLU A O   
1575 O  O   B GLU A 186 ? 0.0609 0.1181 0.2487 -0.0458 -0.0174 0.0299  187 GLU A O   
1576 C  CB  A GLU A 186 ? 0.1108 0.1698 0.2176 -0.0159 -0.0379 0.0315  187 GLU A CB  
1577 C  CB  B GLU A 186 ? 0.1235 0.1636 0.2137 -0.0463 -0.0388 0.0237  187 GLU A CB  
1578 C  CG  A GLU A 186 ? 0.1260 0.1675 0.1629 -0.0035 -0.0142 0.0285  187 GLU A CG  
1579 C  CG  B GLU A 186 ? 0.1837 0.1142 0.2090 -0.0467 -0.0417 0.0111  187 GLU A CG  
1580 C  CD  A GLU A 186 ? 0.1709 0.1607 0.2113 0.0034  -0.0184 0.0286  187 GLU A CD  
1581 C  CD  B GLU A 186 ? 0.1208 0.1849 0.2088 -0.0557 0.0007  0.0231  187 GLU A CD  
1582 O  OE1 A GLU A 186 ? 0.1862 0.2052 0.2471 0.0054  0.0071  0.0297  187 GLU A OE1 
1583 O  OE1 B GLU A 186 ? 0.1310 0.2424 0.2275 -0.0610 -0.0120 0.0097  187 GLU A OE1 
1584 O  OE2 A GLU A 186 ? 0.1722 0.1761 0.2966 -0.0076 0.0274  0.0668  187 GLU A OE2 
1585 O  OE2 B GLU A 186 ? 0.2140 0.2522 0.3515 -0.0017 -0.0322 -0.0197 187 GLU A OE2 
1586 N  N   . SER A 187 ? 0.0506 0.1381 0.2101 -0.0186 -0.0267 0.0054  188 SER A N   
1587 C  CA  . SER A 187 ? 0.0731 0.1270 0.2219 -0.0230 -0.0071 0.0160  188 SER A CA  
1588 C  C   . SER A 187 ? 0.0542 0.1177 0.2210 -0.0147 0.0071  0.0153  188 SER A C   
1589 O  O   . SER A 187 ? 0.0459 0.1320 0.2067 -0.0093 -0.0017 -0.0104 188 SER A O   
1590 C  CB  . SER A 187 ? 0.1032 0.1562 0.2344 -0.0155 -0.0010 0.0296  188 SER A CB  
1591 O  OG  . SER A 187 ? 0.1278 0.1488 0.2261 0.0080  0.0041  0.0093  188 SER A OG  
1592 N  N   . LEU A 188 ? 0.0682 0.1106 0.1801 -0.0207 -0.0111 0.0013  189 LEU A N   
1593 C  CA  . LEU A 188 ? 0.0858 0.1328 0.2016 -0.0017 -0.0264 -0.0122 189 LEU A CA  
1594 C  C   . LEU A 188 ? 0.0424 0.1339 0.1722 -0.0080 -0.0104 -0.0089 189 LEU A C   
1595 O  O   . LEU A 188 ? 0.0912 0.1460 0.2113 -0.0203 -0.0254 -0.0362 189 LEU A O   
1596 C  CB  . LEU A 188 ? 0.1263 0.1167 0.1928 -0.0199 -0.0242 0.0051  189 LEU A CB  
1597 C  CG  . LEU A 188 ? 0.1526 0.1845 0.2031 0.0324  -0.0227 0.0063  189 LEU A CG  
1598 C  CD1 . LEU A 188 ? 0.1488 0.1860 0.2883 0.0024  0.0037  -0.0030 189 LEU A CD1 
1599 C  CD2 . LEU A 188 ? 0.0728 0.2867 0.2839 -0.0010 0.0006  0.0465  189 LEU A CD2 
1600 N  N   . ASP A 189 ? 0.0667 0.1658 0.1647 0.0208  -0.0010 0.0007  190 ASP A N   
1601 C  CA  . ASP A 189 ? 0.0741 0.1805 0.1697 -0.0027 0.0114  0.0132  190 ASP A CA  
1602 C  C   . ASP A 189 ? 0.0585 0.1323 0.1478 0.0001  0.0111  0.0019  190 ASP A C   
1603 O  O   . ASP A 189 ? 0.0650 0.1210 0.1553 0.0066  -0.0006 -0.0178 190 ASP A O   
1604 C  CB  . ASP A 189 ? 0.0883 0.1794 0.1551 -0.0109 0.0124  0.0395  190 ASP A CB  
1605 C  CG  . ASP A 189 ? 0.1590 0.2928 0.2264 -0.0236 -0.0253 -0.0034 190 ASP A CG  
1606 O  OD1 . ASP A 189 ? 0.1318 0.3671 0.3043 -0.0252 0.0628  -0.0267 190 ASP A OD1 
1607 O  OD2 . ASP A 189 ? 0.1697 0.3944 0.2540 -0.0702 -0.0035 0.0621  190 ASP A OD2 
1608 N  N   . TYR A 190 ? 0.0364 0.1709 0.1147 -0.0173 0.0087  -0.0129 191 TYR A N   
1609 C  CA  . TYR A 190 ? 0.0489 0.1208 0.1270 -0.0149 0.0031  0.0031  191 TYR A CA  
1610 C  C   . TYR A 190 ? 0.0689 0.1291 0.0928 -0.0273 0.0097  0.0120  191 TYR A C   
1611 O  O   . TYR A 190 ? 0.0770 0.1389 0.0953 -0.0179 0.0222  -0.0049 191 TYR A O   
1612 C  CB  . TYR A 190 ? 0.1014 0.1136 0.1160 -0.0206 -0.0054 -0.0037 191 TYR A CB  
1613 C  CG  . TYR A 190 ? 0.0498 0.1381 0.1113 -0.0243 0.0174  0.0038  191 TYR A CG  
1614 C  CD1 . TYR A 190 ? 0.1016 0.0969 0.1274 -0.0272 -0.0052 -0.0040 191 TYR A CD1 
1615 C  CD2 . TYR A 190 ? 0.0807 0.1467 0.1046 -0.0081 0.0351  0.0000  191 TYR A CD2 
1616 C  CE1 . TYR A 190 ? 0.0919 0.1171 0.1720 -0.0233 0.0194  0.0135  191 TYR A CE1 
1617 C  CE2 . TYR A 190 ? 0.0606 0.1539 0.1578 0.0285  -0.0162 -0.0136 191 TYR A CE2 
1618 C  CZ  . TYR A 190 ? 0.1648 0.1106 0.1643 -0.0208 -0.0179 -0.0082 191 TYR A CZ  
1619 O  OH  . TYR A 190 ? 0.1382 0.1312 0.1589 0.0060  -0.0059 -0.0102 191 TYR A OH  
1620 N  N   . TRP A 191 ? 0.0632 0.0846 0.1041 -0.0313 0.0043  -0.0059 192 TRP A N   
1621 C  CA  . TRP A 191 ? 0.0500 0.0864 0.1186 -0.0322 0.0006  -0.0035 192 TRP A CA  
1622 C  C   . TRP A 191 ? 0.0614 0.0992 0.0605 -0.0252 0.0166  -0.0034 192 TRP A C   
1623 O  O   . TRP A 191 ? 0.1007 0.0946 0.0640 -0.0225 0.0086  -0.0252 192 TRP A O   
1624 C  CB  . TRP A 191 ? 0.0856 0.0876 0.1102 -0.0154 0.0193  -0.0013 192 TRP A CB  
1625 C  CG  . TRP A 191 ? 0.0731 0.0891 0.0664 -0.0107 0.0005  -0.0010 192 TRP A CG  
1626 C  CD1 . TRP A 191 ? 0.1208 0.1134 0.0860 0.0105  0.0201  -0.0285 192 TRP A CD1 
1627 C  CD2 . TRP A 191 ? 0.0788 0.0851 0.1289 -0.0063 0.0054  -0.0065 192 TRP A CD2 
1628 N  NE1 . TRP A 191 ? 0.1612 0.1052 0.0991 0.0046  0.0060  0.0006  192 TRP A NE1 
1629 C  CE2 . TRP A 191 ? 0.1000 0.1022 0.1014 0.0015  -0.0116 -0.0137 192 TRP A CE2 
1630 C  CE3 . TRP A 191 ? 0.0697 0.1271 0.1070 -0.0040 -0.0243 0.0012  192 TRP A CE3 
1631 C  CZ2 . TRP A 191 ? 0.1192 0.0958 0.1411 -0.0119 -0.0126 -0.0035 192 TRP A CZ2 
1632 C  CZ3 . TRP A 191 ? 0.0388 0.1138 0.1363 -0.0074 0.0110  -0.0125 192 TRP A CZ3 
1633 C  CH2 . TRP A 191 ? 0.1001 0.1160 0.1409 0.0048  -0.0292 -0.0211 192 TRP A CH2 
1634 N  N   . THR A 192 ? 0.0495 0.0673 0.0948 -0.0131 -0.0271 0.0017  193 THR A N   
1635 C  CA  . THR A 192 ? 0.0443 0.0928 0.0840 -0.0185 -0.0113 -0.0024 193 THR A CA  
1636 C  C   . THR A 192 ? 0.0560 0.1050 0.0794 -0.0141 0.0138  0.0094  193 THR A C   
1637 O  O   . THR A 192 ? 0.0676 0.1106 0.0822 0.0000  0.0307  0.0184  193 THR A O   
1638 C  CB  . THR A 192 ? 0.0682 0.0939 0.0706 0.0031  0.0035  0.0114  193 THR A CB  
1639 O  OG1 . THR A 192 ? 0.0579 0.0888 0.0991 -0.0063 0.0225  0.0021  193 THR A OG1 
1640 C  CG2 . THR A 192 ? 0.1005 0.1548 0.0384 -0.0115 0.0227  0.0241  193 THR A CG2 
1641 N  N   . TYR A 193 ? 0.0630 0.0876 0.1070 -0.0163 0.0127  0.0057  194 TYR A N   
1642 C  CA  . TYR A 193 ? 0.0486 0.1000 0.0872 -0.0207 0.0153  0.0153  194 TYR A CA  
1643 C  C   . TYR A 193 ? 0.0743 0.0900 0.1115 0.0048  0.0109  -0.0152 194 TYR A C   
1644 O  O   . TYR A 193 ? 0.0779 0.1027 0.0700 -0.0046 0.0000  0.0065  194 TYR A O   
1645 C  CB  . TYR A 193 ? 0.0788 0.0964 0.0888 0.0220  0.0286  -0.0135 194 TYR A CB  
1646 C  CG  . TYR A 193 ? 0.0680 0.0849 0.0463 0.0038  0.0149  0.0315  194 TYR A CG  
1647 C  CD1 . TYR A 193 ? 0.0810 0.0743 0.0767 0.0162  -0.0078 0.0037  194 TYR A CD1 
1648 C  CD2 . TYR A 193 ? 0.0621 0.1099 0.0946 0.0015  -0.0087 -0.0126 194 TYR A CD2 
1649 C  CE1 . TYR A 193 ? 0.0427 0.0630 0.0895 0.0034  0.0276  0.0082  194 TYR A CE1 
1650 C  CE2 . TYR A 193 ? 0.0833 0.0693 0.0822 0.0031  -0.0160 0.0156  194 TYR A CE2 
1651 C  CZ  . TYR A 193 ? 0.0702 0.0759 0.0619 0.0073  -0.0021 0.0120  194 TYR A CZ  
1652 O  OH  . TYR A 193 ? 0.0727 0.0566 0.0785 0.0023  0.0057  -0.0087 194 TYR A OH  
1653 N  N   . PRO A 194 ? 0.0470 0.0989 0.0776 0.0017  -0.0085 -0.0253 195 PRO A N   
1654 C  CA  . PRO A 194 ? 0.0691 0.0867 0.0922 0.0100  0.0220  -0.0175 195 PRO A CA  
1655 C  C   . PRO A 194 ? 0.0732 0.0417 0.0982 -0.0052 0.0044  -0.0192 195 PRO A C   
1656 O  O   . PRO A 194 ? 0.0820 0.1007 0.1054 0.0405  -0.0176 -0.0003 195 PRO A O   
1657 C  CB  . PRO A 194 ? 0.1041 0.0910 0.1014 -0.0007 0.0059  -0.0001 195 PRO A CB  
1658 C  CG  . PRO A 194 ? 0.1086 0.1253 0.0919 -0.0170 -0.0147 0.0060  195 PRO A CG  
1659 C  CD  . PRO A 194 ? 0.1156 0.1377 0.0451 -0.0262 -0.0182 -0.0184 195 PRO A CD  
1660 N  N   . GLY A 195 ? 0.0460 0.0953 0.0618 -0.0046 0.0263  -0.0111 196 GLY A N   
1661 C  CA  . GLY A 195 ? 0.0625 0.0863 0.0928 -0.0048 0.0019  0.0236  196 GLY A CA  
1662 C  C   . GLY A 195 ? 0.0345 0.0747 0.0687 -0.0070 0.0000  -0.0040 196 GLY A C   
1663 O  O   . GLY A 195 ? 0.0562 0.0664 0.0865 -0.0060 0.0063  -0.0041 196 GLY A O   
1664 N  N   . SER A 196 ? 0.0567 0.0791 0.0567 -0.0107 -0.0068 -0.0140 197 SER A N   
1665 C  CA  . SER A 196 ? 0.0682 0.0894 0.0575 0.0186  0.0116  0.0092  197 SER A CA  
1666 C  C   . SER A 196 ? 0.0573 0.0835 0.0649 0.0173  -0.0274 0.0128  197 SER A C   
1667 O  O   . SER A 196 ? 0.0691 0.0885 0.0795 -0.0109 0.0024  0.0060  197 SER A O   
1668 C  CB  . SER A 196 ? 0.0752 0.1111 0.1216 0.0317  -0.0300 -0.0144 197 SER A CB  
1669 O  OG  . SER A 196 ? 0.0576 0.0700 0.1282 0.0127  -0.0001 -0.0109 197 SER A OG  
1670 N  N   . LEU A 197 ? 0.0849 0.0750 0.0542 -0.0008 -0.0010 -0.0164 198 LEU A N   
1671 C  CA  . LEU A 197 ? 0.0691 0.0637 0.0718 -0.0065 0.0125  -0.0216 198 LEU A CA  
1672 C  C   . LEU A 197 ? 0.0741 0.0928 0.0639 0.0027  0.0005  -0.0234 198 LEU A C   
1673 O  O   . LEU A 197 ? 0.0714 0.0763 0.1149 -0.0094 -0.0208 -0.0251 198 LEU A O   
1674 C  CB  . LEU A 197 ? 0.0842 0.0664 0.1281 -0.0052 0.0331  -0.0015 198 LEU A CB  
1675 C  CG  . LEU A 197 ? 0.0865 0.0592 0.0944 -0.0148 -0.0087 0.0006  198 LEU A CG  
1676 C  CD1 . LEU A 197 ? 0.1158 0.0973 0.1902 -0.0322 0.0357  0.0318  198 LEU A CD1 
1677 C  CD2 . LEU A 197 ? 0.0497 0.1451 0.1393 -0.0027 -0.0074 0.0126  198 LEU A CD2 
1678 N  N   . THR A 198 ? 0.0531 0.0621 0.0664 0.0046  0.0060  -0.0190 199 THR A N   
1679 C  CA  . THR A 198 ? 0.0613 0.0450 0.1149 -0.0049 0.0126  -0.0176 199 THR A CA  
1680 C  C   . THR A 198 ? 0.0727 0.0860 0.1267 0.0031  0.0073  -0.0104 199 THR A C   
1681 O  O   . THR A 198 ? 0.0627 0.0923 0.1226 -0.0005 0.0283  -0.0085 199 THR A O   
1682 C  CB  . THR A 198 ? 0.0804 0.0463 0.1040 -0.0068 -0.0159 -0.0196 199 THR A CB  
1683 O  OG1 . THR A 198 ? 0.0592 0.0793 0.0737 0.0031  0.0010  -0.0074 199 THR A OG1 
1684 C  CG2 . THR A 198 ? 0.0332 0.0903 0.0964 -0.0203 -0.0001 -0.0057 199 THR A CG2 
1685 N  N   . THR A 199 ? 0.0568 0.0916 0.1360 -0.0093 0.0306  -0.0049 200 THR A N   
1686 C  CA  . THR A 199 ? 0.0750 0.0763 0.1274 -0.0188 0.0147  -0.0138 200 THR A CA  
1687 C  C   . THR A 199 ? 0.0592 0.1257 0.1496 -0.0215 0.0102  -0.0074 200 THR A C   
1688 O  O   . THR A 199 ? 0.0483 0.1181 0.1662 -0.0274 0.0291  -0.0219 200 THR A O   
1689 C  CB  . THR A 199 ? 0.0873 0.0931 0.0860 0.0057  0.0049  -0.0010 200 THR A CB  
1690 O  OG1 . THR A 199 ? 0.1927 0.1266 0.1454 0.0221  -0.0001 0.0006  200 THR A OG1 
1691 C  CG2 . THR A 199 ? 0.1223 0.1472 0.1493 -0.0789 -0.0174 -0.0187 200 THR A CG2 
1692 N  N   . PRO A 200 ? 0.0605 0.1198 0.1324 -0.0206 0.0362  -0.0228 201 PRO A N   
1693 C  CA  . PRO A 200 ? 0.0576 0.1206 0.1675 -0.0504 0.0195  -0.0146 201 PRO A CA  
1694 C  C   . PRO A 200 ? 0.0772 0.0925 0.1346 -0.0372 0.0305  -0.0339 201 PRO A C   
1695 O  O   . PRO A 200 ? 0.1050 0.1485 0.1089 -0.0328 0.0194  -0.0366 201 PRO A O   
1696 C  CB  . PRO A 200 ? 0.0746 0.1451 0.1733 -0.0366 0.0434  -0.0324 201 PRO A CB  
1697 C  CG  . PRO A 200 ? 0.0622 0.1378 0.1867 -0.0221 0.0285  -0.0315 201 PRO A CG  
1698 C  CD  . PRO A 200 ? 0.0840 0.1456 0.1435 -0.0082 0.0346  -0.0370 201 PRO A CD  
1699 N  N   . PRO A 201 ? 0.0808 0.1158 0.1587 -0.0184 0.0140  -0.0264 202 PRO A N   
1700 C  CA  . PRO A 201 ? 0.1084 0.1088 0.1318 -0.0186 -0.0026 -0.0035 202 PRO A CA  
1701 C  C   . PRO A 201 ? 0.0885 0.0904 0.1307 -0.0060 0.0099  -0.0007 202 PRO A C   
1702 O  O   . PRO A 201 ? 0.1001 0.1014 0.1669 -0.0485 0.0286  -0.0281 202 PRO A O   
1703 C  CB  . PRO A 201 ? 0.1028 0.1001 0.1655 -0.0299 0.0165  0.0034  202 PRO A CB  
1704 C  CG  . PRO A 201 ? 0.1379 0.0942 0.1939 -0.0119 -0.0219 0.0040  202 PRO A CG  
1705 C  CD  . PRO A 201 ? 0.1181 0.1023 0.1435 -0.0083 -0.0153 -0.0096 202 PRO A CD  
1706 N  N   . LEU A 202 ? 0.0571 0.0812 0.1257 -0.0082 0.0252  -0.0185 203 LEU A N   
1707 C  CA  . LEU A 202 ? 0.0454 0.0723 0.1562 -0.0107 -0.0052 -0.0083 203 LEU A CA  
1708 C  C   . LEU A 202 ? 0.0591 0.0725 0.1544 -0.0208 -0.0034 -0.0057 203 LEU A C   
1709 O  O   . LEU A 202 ? 0.0405 0.0992 0.1442 -0.0094 -0.0216 -0.0057 203 LEU A O   
1710 C  CB  . LEU A 202 ? 0.0373 0.0984 0.1616 0.0102  0.0074  -0.0248 203 LEU A CB  
1711 C  CG  . LEU A 202 ? 0.0263 0.0907 0.1554 0.0040  0.0068  -0.0382 203 LEU A CG  
1712 C  CD1 . LEU A 202 ? 0.0353 0.1409 0.1957 0.0263  0.0164  -0.0381 203 LEU A CD1 
1713 C  CD2 . LEU A 202 ? 0.0812 0.1367 0.1564 -0.0242 -0.0152 -0.0458 203 LEU A CD2 
1714 N  N   . LEU A 203 ? 0.0491 0.0724 0.1499 0.0007  -0.0013 -0.0164 204 LEU A N   
1715 C  CA  . LEU A 203 ? 0.0746 0.0932 0.1212 -0.0086 0.0098  -0.0034 204 LEU A CA  
1716 C  C   . LEU A 203 ? 0.0646 0.0700 0.1041 -0.0003 0.0031  -0.0126 204 LEU A C   
1717 O  O   . LEU A 203 ? 0.0944 0.0908 0.0883 -0.0196 -0.0313 -0.0333 204 LEU A O   
1718 C  CB  . LEU A 203 ? 0.0829 0.0752 0.1439 -0.0127 -0.0100 0.0375  204 LEU A CB  
1719 C  CG  . LEU A 203 ? 0.1300 0.1104 0.1490 -0.0148 0.0043  0.0192  204 LEU A CG  
1720 C  CD1 . LEU A 203 ? 0.1095 0.1275 0.1769 -0.0054 0.0083  0.0163  204 LEU A CD1 
1721 C  CD2 . LEU A 203 ? 0.1521 0.1396 0.2483 -0.0478 -0.0115 -0.0137 204 LEU A CD2 
1722 N  N   . GLU A 204 ? 0.0899 0.1045 0.0910 -0.0068 -0.0071 -0.0436 205 GLU A N   
1723 C  CA  . GLU A 204 ? 0.0799 0.0926 0.0797 0.0217  -0.0209 -0.0252 205 GLU A CA  
1724 C  C   . GLU A 204 ? 0.0648 0.0749 0.0925 -0.0097 -0.0219 -0.0073 205 GLU A C   
1725 O  O   . GLU A 204 ? 0.0917 0.1115 0.1206 0.0063  -0.0285 -0.0537 205 GLU A O   
1726 C  CB  . GLU A 204 ? 0.0542 0.0991 0.1043 0.0148  -0.0288 -0.0065 205 GLU A CB  
1727 C  CG  . GLU A 204 ? 0.0610 0.1449 0.1332 0.0496  -0.0397 -0.0071 205 GLU A CG  
1728 C  CD  . GLU A 204 ? 0.1122 0.1249 0.1521 0.0030  -0.0302 -0.0006 205 GLU A CD  
1729 O  OE1 . GLU A 204 ? 0.1361 0.1490 0.1758 0.0063  -0.0978 -0.0472 205 GLU A OE1 
1730 O  OE2 . GLU A 204 ? 0.0571 0.1278 0.1461 -0.0015 -0.0211 -0.0055 205 GLU A OE2 
1731 N  N   . CYS A 205 ? 0.0414 0.1043 0.1226 -0.0120 -0.0319 -0.0243 206 CYS A N   
1732 C  CA  . CYS A 205 ? 0.0540 0.0942 0.0979 -0.0109 -0.0231 -0.0060 206 CYS A CA  
1733 C  C   . CYS A 205 ? 0.0382 0.0813 0.0922 -0.0086 -0.0105 -0.0281 206 CYS A C   
1734 O  O   . CYS A 205 ? 0.0843 0.0840 0.1159 0.0021  -0.0362 0.0105  206 CYS A O   
1735 C  CB  . CYS A 205 ? 0.0970 0.1061 0.1242 -0.0231 -0.0137 0.0010  206 CYS A CB  
1736 S  SG  . CYS A 205 ? 0.1146 0.0930 0.1072 0.0000  -0.0041 -0.0057 206 CYS A SG  
1737 N  N   . VAL A 206 ? 0.0655 0.0646 0.0948 -0.0185 -0.0148 -0.0115 207 VAL A N   
1738 C  CA  . VAL A 206 ? 0.0414 0.0758 0.1031 -0.0024 0.0000  -0.0142 207 VAL A CA  
1739 C  C   . VAL A 206 ? 0.0437 0.0529 0.1129 0.0010  -0.0081 -0.0073 207 VAL A C   
1740 O  O   . VAL A 206 ? 0.0577 0.0834 0.1174 0.0161  -0.0060 -0.0035 207 VAL A O   
1741 C  CB  . VAL A 206 ? 0.0691 0.0710 0.1313 -0.0167 0.0109  -0.0285 207 VAL A CB  
1742 C  CG1 . VAL A 206 ? 0.0455 0.0974 0.0919 -0.0259 -0.0168 -0.0236 207 VAL A CG1 
1743 C  CG2 . VAL A 206 ? 0.1059 0.1000 0.1249 0.0127  0.0211  0.0228  207 VAL A CG2 
1744 N  N   . THR A 207 ? 0.0425 0.0707 0.1067 -0.0054 0.0063  -0.0197 208 THR A N   
1745 C  CA  . THR A 207 ? 0.0587 0.0727 0.0851 0.0017  0.0035  -0.0250 208 THR A CA  
1746 C  C   . THR A 207 ? 0.0551 0.0724 0.0702 0.0088  -0.0044 0.0017  208 THR A C   
1747 O  O   . THR A 207 ? 0.0863 0.0776 0.0667 0.0120  -0.0227 0.0070  208 THR A O   
1748 C  CB  . THR A 207 ? 0.0718 0.0860 0.1023 0.0258  0.0285  -0.0098 208 THR A CB  
1749 O  OG1 . THR A 207 ? 0.1040 0.0648 0.0951 -0.0057 0.0082  -0.0250 208 THR A OG1 
1750 C  CG2 . THR A 207 ? 0.0551 0.0989 0.1129 -0.0254 0.0348  -0.0296 208 THR A CG2 
1751 N  N   . TRP A 208 ? 0.0512 0.0524 0.1059 -0.0160 -0.0093 0.0030  209 TRP A N   
1752 C  CA  . TRP A 208 ? 0.0377 0.0715 0.0932 -0.0023 0.0115  -0.0021 209 TRP A CA  
1753 C  C   . TRP A 208 ? 0.0553 0.1014 0.1124 -0.0161 -0.0035 -0.0013 209 TRP A C   
1754 O  O   . TRP A 208 ? 0.0585 0.0957 0.0835 -0.0126 0.0038  -0.0071 209 TRP A O   
1755 C  CB  . TRP A 208 ? 0.0702 0.0794 0.0842 0.0167  0.0107  0.0182  209 TRP A CB  
1756 C  CG  . TRP A 208 ? 0.0337 0.0743 0.0809 0.0178  0.0009  0.0263  209 TRP A CG  
1757 C  CD1 . TRP A 208 ? 0.0513 0.0870 0.0482 0.0013  0.0205  0.0214  209 TRP A CD1 
1758 C  CD2 . TRP A 208 ? 0.0533 0.0489 0.1074 0.0012  0.0091  0.0052  209 TRP A CD2 
1759 N  NE1 . TRP A 208 ? 0.0612 0.0982 0.0637 0.0093  -0.0151 -0.0027 209 TRP A NE1 
1760 C  CE2 . TRP A 208 ? 0.0709 0.0764 0.0399 0.0165  -0.0076 -0.0097 209 TRP A CE2 
1761 C  CE3 . TRP A 208 ? 0.0651 0.0277 0.1022 0.0085  -0.0144 0.0030  209 TRP A CE3 
1762 C  CZ2 . TRP A 208 ? 0.0693 0.0687 0.0615 0.0331  -0.0264 -0.0222 209 TRP A CZ2 
1763 C  CZ3 . TRP A 208 ? 0.0764 0.0561 0.0955 0.0035  -0.0172 0.0071  209 TRP A CZ3 
1764 C  CH2 . TRP A 208 ? 0.0655 0.0675 0.0806 0.0057  0.0024  0.0010  209 TRP A CH2 
1765 N  N   . ILE A 209 ? 0.0312 0.0720 0.0849 -0.0065 -0.0118 -0.0044 210 ILE A N   
1766 C  CA  . ILE A 209 ? 0.0461 0.0702 0.0885 -0.0107 -0.0302 -0.0118 210 ILE A CA  
1767 C  C   . ILE A 209 ? 0.0600 0.0785 0.0864 -0.0040 0.0013  -0.0035 210 ILE A C   
1768 O  O   . ILE A 209 ? 0.1030 0.0772 0.0722 0.0147  -0.0097 0.0076  210 ILE A O   
1769 C  CB  . ILE A 209 ? 0.0648 0.0531 0.1341 0.0099  -0.0172 -0.0269 210 ILE A CB  
1770 C  CG1 . ILE A 209 ? 0.0923 0.0759 0.1266 0.0283  -0.0127 -0.0252 210 ILE A CG1 
1771 C  CG2 . ILE A 209 ? 0.0481 0.1177 0.1497 -0.0186 -0.0131 0.0043  210 ILE A CG2 
1772 C  CD1 . ILE A 209 ? 0.0847 0.1081 0.1733 0.0340  -0.0284 -0.0157 210 ILE A CD1 
1773 N  N   . VAL A 210 ? 0.0566 0.0592 0.0903 -0.0038 0.0024  -0.0057 211 VAL A N   
1774 C  CA  . VAL A 210 ? 0.0276 0.0819 0.0842 -0.0077 -0.0078 -0.0045 211 VAL A CA  
1775 C  C   . VAL A 210 ? 0.0684 0.0434 0.0855 -0.0049 0.0003  -0.0324 211 VAL A C   
1776 O  O   . VAL A 210 ? 0.0928 0.1101 0.0576 -0.0115 -0.0046 0.0027  211 VAL A O   
1777 C  CB  . VAL A 210 ? 0.0415 0.0883 0.0951 0.0081  -0.0326 -0.0016 211 VAL A CB  
1778 C  CG1 . VAL A 210 ? 0.0825 0.0716 0.1120 -0.0028 -0.0306 -0.0373 211 VAL A CG1 
1779 C  CG2 . VAL A 210 ? 0.0346 0.0966 0.1352 -0.0256 0.0013  -0.0026 211 VAL A CG2 
1780 N  N   . LEU A 211 ? 0.0455 0.0867 0.0917 -0.0263 -0.0152 -0.0164 212 LEU A N   
1781 C  CA  . LEU A 211 ? 0.0432 0.0867 0.1000 -0.0286 -0.0098 -0.0166 212 LEU A CA  
1782 C  C   . LEU A 211 ? 0.0684 0.1040 0.0917 -0.0140 -0.0104 -0.0020 212 LEU A C   
1783 O  O   . LEU A 211 ? 0.0901 0.1077 0.1036 0.0048  -0.0017 -0.0023 212 LEU A O   
1784 C  CB  . LEU A 211 ? 0.0953 0.1018 0.0720 -0.0100 -0.0469 -0.0163 212 LEU A CB  
1785 C  CG  . LEU A 211 ? 0.0643 0.1086 0.1548 -0.0313 -0.0108 0.0006  212 LEU A CG  
1786 C  CD1 . LEU A 211 ? 0.0640 0.1873 0.1262 -0.0170 -0.0344 0.0245  212 LEU A CD1 
1787 C  CD2 . LEU A 211 ? 0.0940 0.1058 0.1694 -0.0151 0.0037  -0.0043 212 LEU A CD2 
1788 N  N   . LYS A 212 ? 0.0759 0.1045 0.0984 -0.0320 0.0046  -0.0052 213 LYS A N   
1789 C  CA  . LYS A 212 ? 0.1045 0.0847 0.0961 -0.0234 0.0241  0.0109  213 LYS A CA  
1790 C  C   . LYS A 212 ? 0.0993 0.0766 0.1199 -0.0198 -0.0030 0.0274  213 LYS A C   
1791 O  O   . LYS A 212 ? 0.0964 0.0926 0.1826 -0.0197 -0.0313 0.0073  213 LYS A O   
1792 C  CB  . LYS A 212 ? 0.1781 0.1382 0.1203 -0.0388 0.0164  0.0219  213 LYS A CB  
1793 C  CG  . LYS A 212 ? 0.2354 0.1585 0.1794 -0.0298 0.0118  0.0377  213 LYS A CG  
1794 C  CD  . LYS A 212 ? 0.2512 0.1763 0.2081 -0.0914 0.0262  0.0115  213 LYS A CD  
1795 C  CE  . LYS A 212 ? 0.3404 0.2489 0.2449 -0.0559 0.0320  0.0575  213 LYS A CE  
1796 N  NZ  . LYS A 212 ? 0.4374 0.3762 0.3070 -0.0557 0.0364  0.0644  213 LYS A NZ  
1797 N  N   . GLU A 213 ? 0.0539 0.0917 0.1194 -0.0247 -0.0208 0.0096  214 GLU A N   
1798 C  CA  . GLU A 213 ? 0.0679 0.1217 0.1181 -0.0168 -0.0070 -0.0032 214 GLU A CA  
1799 C  C   . GLU A 213 ? 0.0666 0.0858 0.1113 -0.0019 -0.0031 -0.0024 214 GLU A C   
1800 O  O   . GLU A 213 ? 0.0750 0.0779 0.1016 0.0006  -0.0223 0.0152  214 GLU A O   
1801 C  CB  . GLU A 213 ? 0.0851 0.1293 0.1307 0.0026  -0.0339 0.0054  214 GLU A CB  
1802 C  CG  . GLU A 213 ? 0.0781 0.1615 0.1812 -0.0313 -0.0262 -0.0006 214 GLU A CG  
1803 C  CD  . GLU A 213 ? 0.1360 0.1765 0.1931 -0.0194 -0.0060 -0.0546 214 GLU A CD  
1804 O  OE1 . GLU A 213 ? 0.1093 0.1216 0.2527 -0.0237 -0.0311 0.0088  214 GLU A OE1 
1805 O  OE2 . GLU A 213 ? 0.2049 0.2628 0.3079 -0.0595 -0.0615 -0.0419 214 GLU A OE2 
1806 N  N   . PRO A 214 ? 0.0903 0.0576 0.1124 0.0096  0.0082  0.0109  215 PRO A N   
1807 C  CA  . PRO A 214 ? 0.1037 0.0854 0.0781 0.0057  -0.0131 -0.0155 215 PRO A CA  
1808 C  C   . PRO A 214 ? 0.1049 0.1125 0.1027 -0.0015 -0.0269 0.0013  215 PRO A C   
1809 O  O   . PRO A 214 ? 0.1215 0.1433 0.1300 -0.0266 -0.0006 0.0452  215 PRO A O   
1810 C  CB  . PRO A 214 ? 0.0807 0.0768 0.1185 -0.0008 -0.0068 0.0125  215 PRO A CB  
1811 C  CG  . PRO A 214 ? 0.1992 0.1404 0.1808 0.0183  0.0379  0.0012  215 PRO A CG  
1812 C  CD  . PRO A 214 ? 0.1149 0.0655 0.1138 0.0111  0.0386  0.0242  215 PRO A CD  
1813 N  N   . ILE A 215 ? 0.1088 0.1092 0.0847 0.0057  -0.0307 -0.0044 216 ILE A N   
1814 C  CA  . ILE A 215 ? 0.1219 0.0888 0.0864 0.0024  -0.0281 -0.0285 216 ILE A CA  
1815 C  C   . ILE A 215 ? 0.1115 0.0688 0.0989 0.0046  -0.0176 -0.0142 216 ILE A C   
1816 O  O   . ILE A 215 ? 0.1048 0.1062 0.1208 0.0006  -0.0275 -0.0285 216 ILE A O   
1817 C  CB  . ILE A 215 ? 0.1492 0.0973 0.0870 0.0256  -0.0041 0.0028  216 ILE A CB  
1818 C  CG1 . ILE A 215 ? 0.1982 0.1256 0.1167 0.0057  -0.0124 0.0065  216 ILE A CG1 
1819 C  CG2 . ILE A 215 ? 0.1321 0.1246 0.1625 0.0192  -0.0185 -0.0113 216 ILE A CG2 
1820 C  CD1 . ILE A 215 ? 0.2079 0.0969 0.1248 -0.0096 -0.0383 0.0097  216 ILE A CD1 
1821 N  N   . SER A 216 ? 0.1299 0.1018 0.1205 -0.0035 -0.0364 -0.0406 217 SER A N   
1822 C  CA  . SER A 216 ? 0.1252 0.1013 0.1063 -0.0137 -0.0132 -0.0397 217 SER A CA  
1823 C  C   . SER A 216 ? 0.1518 0.0707 0.1332 0.0015  -0.0220 -0.0020 217 SER A C   
1824 O  O   . SER A 216 ? 0.1325 0.1174 0.1264 -0.0111 -0.0351 -0.0070 217 SER A O   
1825 C  CB  . SER A 216 ? 0.2240 0.0964 0.1508 -0.0373 0.0157  0.0255  217 SER A CB  
1826 O  OG  . SER A 216 ? 0.1910 0.2171 0.2164 -0.0346 -0.0233 -0.0122 217 SER A OG  
1827 N  N   . VAL A 217 ? 0.1343 0.0828 0.1180 -0.0142 -0.0318 -0.0162 218 VAL A N   
1828 C  CA  . VAL A 217 ? 0.1253 0.0912 0.1300 -0.0120 -0.0148 -0.0118 218 VAL A CA  
1829 C  C   . VAL A 217 ? 0.1409 0.0937 0.1111 -0.0247 -0.0428 -0.0092 218 VAL A C   
1830 O  O   . VAL A 217 ? 0.1460 0.0998 0.0926 -0.0057 -0.0296 -0.0024 218 VAL A O   
1831 C  CB  . VAL A 217 ? 0.1353 0.1007 0.1569 -0.0179 -0.0307 -0.0001 218 VAL A CB  
1832 C  CG1 . VAL A 217 ? 0.1447 0.0601 0.1612 0.0001  -0.0275 -0.0370 218 VAL A CG1 
1833 C  CG2 . VAL A 217 ? 0.1417 0.1018 0.1888 -0.0187 -0.0535 -0.0388 218 VAL A CG2 
1834 N  N   . SER A 218 ? 0.1456 0.0922 0.1190 -0.0197 -0.0200 -0.0166 219 SER A N   
1835 C  CA  . SER A 218 ? 0.1474 0.0864 0.1201 -0.0038 -0.0219 -0.0241 219 SER A CA  
1836 C  C   . SER A 218 ? 0.1666 0.0855 0.1288 -0.0019 -0.0219 -0.0120 219 SER A C   
1837 O  O   . SER A 218 ? 0.1641 0.0698 0.1302 -0.0024 -0.0315 -0.0104 219 SER A O   
1838 C  CB  . SER A 218 ? 0.1855 0.1201 0.1303 -0.0032 -0.0148 -0.0044 219 SER A CB  
1839 O  OG  . SER A 218 ? 0.2010 0.1163 0.1198 -0.0337 -0.0168 -0.0234 219 SER A OG  
1840 N  N   A SER A 219 ? 0.1569 0.0702 0.1206 -0.0015 -0.0183 -0.0171 220 SER A N   
1841 N  N   B SER A 219 ? 0.1548 0.0718 0.1221 0.0000  -0.0181 -0.0162 220 SER A N   
1842 C  CA  A SER A 219 ? 0.1625 0.0646 0.1375 -0.0046 -0.0049 -0.0170 220 SER A CA  
1843 C  CA  B SER A 219 ? 0.1560 0.0689 0.1427 -0.0043 -0.0040 -0.0164 220 SER A CA  
1844 C  C   A SER A 219 ? 0.1801 0.0958 0.1535 -0.0031 0.0003  -0.0258 220 SER A C   
1845 C  C   B SER A 219 ? 0.1792 0.0901 0.1589 -0.0008 0.0000  -0.0266 220 SER A C   
1846 O  O   A SER A 219 ? 0.1629 0.1194 0.1688 -0.0109 -0.0057 -0.0057 220 SER A O   
1847 O  O   B SER A 219 ? 0.1759 0.0784 0.1765 -0.0065 -0.0094 -0.0161 220 SER A O   
1848 C  CB  A SER A 219 ? 0.1704 0.0894 0.1593 -0.0086 -0.0046 -0.0165 220 SER A CB  
1849 C  CB  B SER A 219 ? 0.1630 0.1010 0.1745 -0.0059 -0.0044 -0.0138 220 SER A CB  
1850 O  OG  A SER A 219 ? 0.1870 0.0648 0.1650 -0.0108 -0.0071 -0.0167 220 SER A OG  
1851 O  OG  B SER A 219 ? 0.1350 0.1691 0.1846 -0.0040 0.0046  0.0159  220 SER A OG  
1852 N  N   . GLU A 220 ? 0.1975 0.1102 0.1632 0.0109  0.0019  -0.0162 221 GLU A N   
1853 C  CA  . GLU A 220 ? 0.2092 0.1302 0.1819 -0.0124 -0.0024 -0.0165 221 GLU A CA  
1854 C  C   . GLU A 220 ? 0.1891 0.1119 0.1393 -0.0060 0.0037  -0.0174 221 GLU A C   
1855 O  O   . GLU A 220 ? 0.2322 0.1019 0.1432 -0.0078 0.0195  -0.0242 221 GLU A O   
1856 C  CB  . GLU A 220 ? 0.2811 0.1564 0.1607 -0.0222 -0.0126 -0.0454 221 GLU A CB  
1857 C  CG  . GLU A 220 ? 0.2796 0.1530 0.2444 -0.0274 -0.0176 -0.0676 221 GLU A CG  
1858 C  CD  . GLU A 220 ? 0.3589 0.1363 0.2412 -0.0487 -0.0044 -0.0688 221 GLU A CD  
1859 O  OE1 . GLU A 220 ? 0.2469 0.1779 0.2307 -0.0535 0.0071  -0.0326 221 GLU A OE1 
1860 O  OE2 . GLU A 220 ? 0.4571 0.2777 0.4179 -0.0794 0.0211  -0.1208 221 GLU A OE2 
1861 N  N   . GLN A 221 ? 0.1824 0.0931 0.1093 -0.0076 -0.0027 -0.0035 222 GLN A N   
1862 C  CA  . GLN A 221 ? 0.1637 0.1036 0.1230 0.0028  -0.0091 -0.0013 222 GLN A CA  
1863 C  C   . GLN A 221 ? 0.1794 0.1098 0.1521 -0.0138 -0.0135 0.0107  222 GLN A C   
1864 O  O   . GLN A 221 ? 0.1777 0.1273 0.1316 -0.0091 -0.0017 0.0217  222 GLN A O   
1865 C  CB  . GLN A 221 ? 0.1668 0.1068 0.1386 -0.0185 -0.0242 -0.0147 222 GLN A CB  
1866 C  CG  . GLN A 221 ? 0.1307 0.1212 0.1439 -0.0222 -0.0362 -0.0086 222 GLN A CG  
1867 C  CD  . GLN A 221 ? 0.1722 0.0833 0.1564 -0.0124 -0.0130 -0.0109 222 GLN A CD  
1868 O  OE1 . GLN A 221 ? 0.1442 0.1226 0.1288 0.0104  -0.0262 -0.0188 222 GLN A OE1 
1869 N  NE2 . GLN A 221 ? 0.2029 0.0724 0.1360 -0.0093 -0.0456 0.0028  222 GLN A NE2 
1870 N  N   . VAL A 222 ? 0.1668 0.1168 0.1403 0.0000  -0.0270 0.0315  223 VAL A N   
1871 C  CA  . VAL A 222 ? 0.1510 0.1310 0.1291 0.0041  -0.0153 0.0136  223 VAL A CA  
1872 C  C   . VAL A 222 ? 0.1651 0.1269 0.1551 -0.0031 -0.0078 0.0003  223 VAL A C   
1873 O  O   . VAL A 222 ? 0.1844 0.1330 0.1668 -0.0238 -0.0065 -0.0027 223 VAL A O   
1874 C  CB  . VAL A 222 ? 0.1932 0.1393 0.1690 0.0160  -0.0555 0.0275  223 VAL A CB  
1875 C  CG1 . VAL A 222 ? 0.1763 0.1715 0.1950 0.0017  -0.0027 0.0193  223 VAL A CG1 
1876 C  CG2 . VAL A 222 ? 0.1242 0.1715 0.1989 0.0165  -0.0324 0.0151  223 VAL A CG2 
1877 N  N   . LEU A 223 ? 0.1891 0.1104 0.1339 -0.0100 0.0142  -0.0186 224 LEU A N   
1878 C  CA  . LEU A 223 ? 0.2104 0.1388 0.1659 -0.0245 0.0256  -0.0167 224 LEU A CA  
1879 C  C   . LEU A 223 ? 0.2243 0.1313 0.1961 -0.0131 0.0190  -0.0254 224 LEU A C   
1880 O  O   . LEU A 223 ? 0.2022 0.1587 0.1801 0.0000  0.0320  -0.0189 224 LEU A O   
1881 C  CB  . LEU A 223 ? 0.2549 0.1562 0.2248 -0.0154 0.0190  -0.0322 224 LEU A CB  
1882 C  CG  . LEU A 223 ? 0.2673 0.2186 0.2340 -0.0291 0.0001  -0.0274 224 LEU A CG  
1883 C  CD1 . LEU A 223 ? 0.3468 0.2861 0.3562 -0.0272 -0.0060 -0.0233 224 LEU A CD1 
1884 C  CD2 . LEU A 223 ? 0.3021 0.2340 0.3029 0.0020  -0.0131 -0.0054 224 LEU A CD2 
1885 N  N   . LYS A 224 ? 0.1923 0.1262 0.1391 -0.0161 0.0115  -0.0120 225 LYS A N   
1886 C  CA  . LYS A 224 ? 0.2010 0.1691 0.1486 0.0048  0.0186  -0.0071 225 LYS A CA  
1887 C  C   . LYS A 224 ? 0.1697 0.1544 0.1041 -0.0094 0.0192  0.0089  225 LYS A C   
1888 O  O   . LYS A 224 ? 0.2036 0.1687 0.0980 -0.0412 0.0284  -0.0019 225 LYS A O   
1889 C  CB  . LYS A 224 ? 0.2178 0.1851 0.1640 0.0162  0.0124  0.0161  225 LYS A CB  
1890 C  CG  . LYS A 224 ? 0.2092 0.2465 0.2465 -0.0104 -0.0153 -0.0159 225 LYS A CG  
1891 C  CD  . LYS A 224 ? 0.2793 0.2861 0.2641 0.0035  -0.0133 -0.0126 225 LYS A CD  
1892 C  CE  . LYS A 224 ? 0.2996 0.3084 0.2687 -0.0229 -0.0173 -0.0165 225 LYS A CE  
1893 N  NZ  . LYS A 224 ? 0.4649 0.4036 0.4508 0.0068  0.0592  -0.0226 225 LYS A NZ  
1894 N  N   . PHE A 225 ? 0.1925 0.1206 0.0917 -0.0121 0.0173  0.0041  226 PHE A N   
1895 C  CA  . PHE A 225 ? 0.1680 0.0838 0.0777 -0.0229 0.0225  -0.0097 226 PHE A CA  
1896 C  C   . PHE A 225 ? 0.1884 0.1259 0.0445 -0.0196 0.0096  0.0142  226 PHE A C   
1897 O  O   . PHE A 225 ? 0.1869 0.1210 0.1046 -0.0294 0.0366  -0.0100 226 PHE A O   
1898 C  CB  . PHE A 225 ? 0.1627 0.1342 0.0957 -0.0142 -0.0015 -0.0346 226 PHE A CB  
1899 C  CG  . PHE A 225 ? 0.1345 0.1111 0.1057 -0.0204 0.0131  -0.0037 226 PHE A CG  
1900 C  CD1 . PHE A 225 ? 0.2216 0.1242 0.1504 0.0094  -0.0049 -0.0175 226 PHE A CD1 
1901 C  CD2 . PHE A 225 ? 0.1449 0.2226 0.1632 -0.0434 0.0283  -0.0368 226 PHE A CD2 
1902 C  CE1 . PHE A 225 ? 0.2365 0.1324 0.1339 0.0082  0.0146  0.0096  226 PHE A CE1 
1903 C  CE2 . PHE A 225 ? 0.1316 0.1722 0.1572 -0.0215 0.0104  -0.0480 226 PHE A CE2 
1904 C  CZ  . PHE A 225 ? 0.1672 0.1249 0.1687 -0.0307 0.0165  -0.0564 226 PHE A CZ  
1905 N  N   . ARG A 226 ? 0.1785 0.1022 0.0995 -0.0060 0.0434  -0.0052 227 ARG A N   
1906 C  CA  . ARG A 226 ? 0.1821 0.1321 0.1072 -0.0142 0.0211  0.0092  227 ARG A CA  
1907 C  C   . ARG A 226 ? 0.1898 0.1363 0.1374 -0.0231 0.0252  -0.0030 227 ARG A C   
1908 O  O   . ARG A 226 ? 0.1874 0.1596 0.1226 -0.0089 0.0171  -0.0037 227 ARG A O   
1909 C  CB  . ARG A 226 ? 0.2061 0.0989 0.1273 0.0087  0.0184  0.0166  227 ARG A CB  
1910 C  CG  . ARG A 226 ? 0.1367 0.1183 0.1165 -0.0274 -0.0043 0.0190  227 ARG A CG  
1911 C  CD  . ARG A 226 ? 0.1974 0.0988 0.1693 -0.0229 0.0152  0.0085  227 ARG A CD  
1912 N  NE  . ARG A 226 ? 0.1683 0.0992 0.1481 -0.0350 0.0006  0.0162  227 ARG A NE  
1913 C  CZ  . ARG A 226 ? 0.1615 0.1206 0.1023 -0.0010 0.0077  0.0077  227 ARG A CZ  
1914 N  NH1 . ARG A 226 ? 0.2280 0.1406 0.1869 -0.0586 -0.0201 -0.0610 227 ARG A NH1 
1915 N  NH2 . ARG A 226 ? 0.1955 0.1228 0.1133 -0.0557 0.0256  -0.0085 227 ARG A NH2 
1916 N  N   . LYS A 227 ? 0.1995 0.1306 0.0962 -0.0285 0.0452  -0.0063 228 LYS A N   
1917 C  CA  . LYS A 227 ? 0.2207 0.1546 0.1129 -0.0439 0.0399  -0.0121 228 LYS A CA  
1918 C  C   . LYS A 227 ? 0.2189 0.1235 0.1172 -0.0174 0.0544  -0.0111 228 LYS A C   
1919 O  O   . LYS A 227 ? 0.2620 0.1630 0.1049 -0.0469 0.0546  -0.0392 228 LYS A O   
1920 C  CB  . LYS A 227 ? 0.2124 0.1783 0.1162 -0.0615 0.0175  -0.0098 228 LYS A CB  
1921 C  CG  . LYS A 227 ? 0.2359 0.2038 0.1616 -0.0577 -0.0054 0.0105  228 LYS A CG  
1922 C  CD  . LYS A 227 ? 0.2671 0.2655 0.2352 -0.0573 0.0024  -0.0098 228 LYS A CD  
1923 C  CE  . LYS A 227 ? 0.3828 0.4122 0.3558 -0.0068 0.0315  -0.0071 228 LYS A CE  
1924 N  NZ  . LYS A 227 ? 0.4402 0.4363 0.3971 0.0159  0.0041  -0.0310 228 LYS A NZ  
1925 N  N   . LEU A 228 ? 0.2039 0.1106 0.0953 -0.0298 0.0355  -0.0227 229 LEU A N   
1926 C  CA  . LEU A 228 ? 0.2014 0.1074 0.1145 -0.0397 0.0373  -0.0296 229 LEU A CA  
1927 C  C   . LEU A 228 ? 0.2384 0.1422 0.1138 -0.0441 0.0359  -0.0292 229 LEU A C   
1928 O  O   . LEU A 228 ? 0.2312 0.1061 0.1266 -0.0403 0.0368  -0.0109 229 LEU A O   
1929 C  CB  . LEU A 228 ? 0.2046 0.1403 0.0804 -0.0315 0.0445  -0.0346 229 LEU A CB  
1930 C  CG  . LEU A 228 ? 0.2207 0.1695 0.0851 -0.0255 0.0175  -0.0293 229 LEU A CG  
1931 C  CD1 . LEU A 228 ? 0.2319 0.1553 0.0854 -0.0612 0.0219  -0.0087 229 LEU A CD1 
1932 C  CD2 . LEU A 228 ? 0.3050 0.1185 0.0969 -0.0306 0.0027  0.0229  229 LEU A CD2 
1933 N  N   . ASN A 229 ? 0.2474 0.1590 0.1045 -0.0645 0.0496  -0.0198 230 ASN A N   
1934 C  CA  . ASN A 229 ? 0.2268 0.1806 0.0957 -0.0483 0.0370  -0.0357 230 ASN A CA  
1935 C  C   . ASN A 229 ? 0.2232 0.1682 0.1187 -0.0480 0.0320  -0.0076 230 ASN A C   
1936 O  O   . ASN A 229 ? 0.2212 0.1561 0.1436 -0.0286 0.0146  0.0037  230 ASN A O   
1937 C  CB  . ASN A 229 ? 0.2531 0.1627 0.0978 -0.0211 0.0344  -0.0239 230 ASN A CB  
1938 C  CG  . ASN A 229 ? 0.2772 0.1988 0.1106 -0.0623 0.0344  -0.0511 230 ASN A CG  
1939 O  OD1 . ASN A 229 ? 0.4070 0.2280 0.1084 -0.0634 0.0705  -0.0417 230 ASN A OD1 
1940 N  ND2 . ASN A 229 ? 0.2462 0.1891 0.1553 -0.0798 0.0469  -0.0318 230 ASN A ND2 
1941 N  N   . PHE A 230 ? 0.1733 0.1853 0.1190 -0.0762 0.0461  -0.0273 231 PHE A N   
1942 C  CA  . PHE A 230 ? 0.1999 0.1388 0.1295 -0.0777 0.0256  0.0030  231 PHE A CA  
1943 C  C   . PHE A 230 ? 0.2031 0.1900 0.1463 -0.0627 0.0405  -0.0132 231 PHE A C   
1944 O  O   . PHE A 230 ? 0.2147 0.1888 0.1733 -0.0746 0.0303  0.0068  231 PHE A O   
1945 C  CB  . PHE A 230 ? 0.2143 0.1374 0.1217 -0.0515 0.0049  -0.0156 231 PHE A CB  
1946 C  CG  . PHE A 230 ? 0.2006 0.1314 0.1546 -0.0595 0.0425  -0.0122 231 PHE A CG  
1947 C  CD1 . PHE A 230 ? 0.1715 0.1363 0.1199 -0.0165 -0.0110 -0.0375 231 PHE A CD1 
1948 C  CD2 . PHE A 230 ? 0.1934 0.1363 0.1140 -0.0160 0.0287  -0.0355 231 PHE A CD2 
1949 C  CE1 . PHE A 230 ? 0.1834 0.1817 0.1679 -0.0507 0.0230  -0.0340 231 PHE A CE1 
1950 C  CE2 . PHE A 230 ? 0.2284 0.1411 0.1422 -0.0472 0.0388  -0.0320 231 PHE A CE2 
1951 C  CZ  . PHE A 230 ? 0.1590 0.1718 0.1424 -0.0017 0.0138  -0.0254 231 PHE A CZ  
1952 N  N   . ASN A 231 ? 0.1985 0.2056 0.1303 -0.0697 0.0706  -0.0200 232 ASN A N   
1953 C  CA  . ASN A 231 ? 0.2230 0.1931 0.1463 -0.0615 0.0634  -0.0035 232 ASN A CA  
1954 C  C   . ASN A 231 ? 0.1993 0.1932 0.1777 -0.0603 0.0434  -0.0105 232 ASN A C   
1955 O  O   . ASN A 231 ? 0.2212 0.2178 0.1542 -0.0355 0.0421  -0.0028 232 ASN A O   
1956 C  CB  . ASN A 231 ? 0.2534 0.2154 0.1788 -0.0467 0.0901  -0.0333 232 ASN A CB  
1957 C  CG  . ASN A 231 ? 0.2060 0.1611 0.1488 -0.0302 0.0232  0.0299  232 ASN A CG  
1958 O  OD1 . ASN A 231 ? 0.3896 0.2002 0.1361 -0.0680 0.0909  -0.0041 232 ASN A OD1 
1959 N  ND2 . ASN A 231 ? 0.2865 0.2402 0.1350 -0.0196 0.0614  0.0017  232 ASN A ND2 
1960 N  N   . GLY A 232 ? 0.2588 0.2151 0.1960 -0.0307 0.0480  -0.0021 233 GLY A N   
1961 C  CA  . GLY A 232 ? 0.2664 0.2122 0.1558 -0.0288 0.0599  -0.0046 233 GLY A CA  
1962 C  C   . GLY A 232 ? 0.2570 0.2114 0.1935 -0.0249 0.0458  -0.0074 233 GLY A C   
1963 O  O   . GLY A 232 ? 0.2951 0.2409 0.1849 -0.0234 0.1159  -0.0046 233 GLY A O   
1964 N  N   . GLU A 233 ? 0.2641 0.2446 0.1691 -0.0197 0.0597  -0.0266 234 GLU A N   
1965 C  CA  . GLU A 233 ? 0.2926 0.2419 0.1819 -0.0148 0.0357  -0.0010 234 GLU A CA  
1966 C  C   . GLU A 233 ? 0.3142 0.2427 0.1907 -0.0083 0.0386  -0.0115 234 GLU A C   
1967 O  O   . GLU A 233 ? 0.3151 0.2552 0.1727 -0.0192 0.0595  -0.0104 234 GLU A O   
1968 C  CB  . GLU A 233 ? 0.2782 0.2370 0.1844 -0.0093 0.0300  0.0275  234 GLU A CB  
1969 C  CG  . GLU A 233 ? 0.2603 0.2630 0.2100 -0.0621 0.0368  0.0395  234 GLU A CG  
1970 C  CD  . GLU A 233 ? 0.3506 0.3331 0.2843 -0.0129 -0.0012 -0.0107 234 GLU A CD  
1971 O  OE1 . GLU A 233 ? 0.2961 0.2980 0.3321 -0.0617 -0.0155 0.0187  234 GLU A OE1 
1972 O  OE2 . GLU A 233 ? 0.2953 0.3090 0.2671 -0.0176 -0.0465 -0.0307 234 GLU A OE2 
1973 N  N   . GLY A 234 ? 0.3203 0.2509 0.2110 0.0085  0.0680  -0.0077 235 GLY A N   
1974 C  CA  . GLY A 234 ? 0.3091 0.2850 0.2637 0.0231  0.0326  -0.0052 235 GLY A CA  
1975 C  C   . GLY A 234 ? 0.3029 0.3190 0.2646 0.0152  0.0320  0.0190  235 GLY A C   
1976 O  O   . GLY A 234 ? 0.3116 0.3610 0.2843 0.0520  0.0593  0.0098  235 GLY A O   
1977 N  N   . GLU A 235 ? 0.2865 0.2548 0.2449 -0.0074 0.0399  0.0164  236 GLU A N   
1978 C  CA  . GLU A 235 ? 0.2648 0.2309 0.2361 0.0054  0.0359  0.0131  236 GLU A CA  
1979 C  C   . GLU A 235 ? 0.2746 0.2782 0.2551 -0.0065 0.0562  0.0094  236 GLU A C   
1980 O  O   . GLU A 235 ? 0.2759 0.3370 0.2261 0.0129  0.0612  0.0216  236 GLU A O   
1981 C  CB  . GLU A 235 ? 0.2646 0.2370 0.2721 0.0173  0.0307  0.0093  236 GLU A CB  
1982 C  CG  . GLU A 235 ? 0.2716 0.2304 0.2327 0.0156  0.0423  -0.0027 236 GLU A CG  
1983 C  CD  . GLU A 235 ? 0.3210 0.2809 0.2858 -0.0091 0.0452  -0.0027 236 GLU A CD  
1984 O  OE1 . GLU A 235 ? 0.2807 0.3483 0.3547 -0.0649 0.1164  0.0157  236 GLU A OE1 
1985 O  OE2 . GLU A 235 ? 0.4083 0.3666 0.3910 -0.0626 0.0662  0.0031  236 GLU A OE2 
1986 N  N   . PRO A 236 ? 0.2626 0.2549 0.2405 -0.0051 0.0712  0.0377  237 PRO A N   
1987 C  CA  . PRO A 236 ? 0.2677 0.2854 0.2448 -0.0071 0.0895  0.0263  237 PRO A CA  
1988 C  C   . PRO A 236 ? 0.2408 0.2572 0.2272 -0.0329 0.0948  0.0175  237 PRO A C   
1989 O  O   . PRO A 236 ? 0.2480 0.2752 0.2092 -0.0161 0.0628  0.0135  237 PRO A O   
1990 C  CB  . PRO A 236 ? 0.2329 0.2972 0.2386 0.0015  0.0953  0.0311  237 PRO A CB  
1991 C  CG  . PRO A 236 ? 0.3113 0.2767 0.3097 0.0027  0.0775  0.0703  237 PRO A CG  
1992 C  CD  . PRO A 236 ? 0.3034 0.2872 0.2865 0.0000  0.0579  0.0270  237 PRO A CD  
1993 N  N   . GLU A 237 ? 0.2782 0.2606 0.2505 -0.0317 0.0628  0.0028  238 GLU A N   
1994 C  CA  . GLU A 237 ? 0.2416 0.2302 0.1977 -0.0439 0.0593  -0.0164 238 GLU A CA  
1995 C  C   . GLU A 237 ? 0.2621 0.2254 0.1914 -0.0533 0.0524  -0.0313 238 GLU A C   
1996 O  O   . GLU A 237 ? 0.2236 0.2401 0.1460 -0.0441 0.0546  -0.0423 238 GLU A O   
1997 C  CB  . GLU A 237 ? 0.2847 0.2072 0.2171 -0.0253 0.0236  -0.0362 238 GLU A CB  
1998 C  CG  . GLU A 237 ? 0.2678 0.2623 0.2196 -0.0533 0.0250  -0.0270 238 GLU A CG  
1999 C  CD  . GLU A 237 ? 0.2624 0.1841 0.1950 -0.0171 0.0249  -0.0355 238 GLU A CD  
2000 O  OE1 . GLU A 237 ? 0.3555 0.2513 0.4295 0.0403  -0.0678 -0.0535 238 GLU A OE1 
2001 O  OE2 . GLU A 237 ? 0.2707 0.2089 0.2466 -0.0359 0.0162  -0.0575 238 GLU A OE2 
2002 N  N   . GLU A 238 ? 0.2395 0.1928 0.1345 -0.0908 0.0653  -0.0476 239 GLU A N   
2003 C  CA  . GLU A 238 ? 0.2519 0.2555 0.1708 -0.0648 0.0412  -0.0302 239 GLU A CA  
2004 C  C   . GLU A 238 ? 0.2052 0.1896 0.1288 -0.0421 0.0615  -0.0262 239 GLU A C   
2005 O  O   . GLU A 238 ? 0.2354 0.1989 0.1532 -0.0500 0.0564  -0.0357 239 GLU A O   
2006 C  CB  . GLU A 238 ? 0.2309 0.2265 0.1639 -0.0746 0.0197  -0.0351 239 GLU A CB  
2007 C  CG  . GLU A 238 ? 0.2784 0.2804 0.2649 -0.0247 0.0175  -0.0432 239 GLU A CG  
2008 C  CD  . GLU A 238 ? 0.3497 0.3185 0.3093 -0.0650 0.0146  -0.0324 239 GLU A CD  
2009 O  OE1 . GLU A 238 ? 0.3108 0.3773 0.3318 0.0013  -0.0005 -0.0346 239 GLU A OE1 
2010 O  OE2 . GLU A 238 ? 0.4142 0.4384 0.4510 -0.0649 0.0153  0.0167  239 GLU A OE2 
2011 N  N   . LEU A 239 ? 0.1939 0.1763 0.1162 -0.0401 0.0675  -0.0296 240 LEU A N   
2012 C  CA  . LEU A 239 ? 0.1723 0.1607 0.1194 -0.0260 0.0577  -0.0285 240 LEU A CA  
2013 C  C   . LEU A 239 ? 0.1503 0.1332 0.1104 -0.0261 0.0493  -0.0222 240 LEU A C   
2014 O  O   . LEU A 239 ? 0.1812 0.1948 0.1113 -0.0220 0.0661  -0.0212 240 LEU A O   
2015 C  CB  . LEU A 239 ? 0.1539 0.1428 0.1324 0.0008  0.0405  -0.0237 240 LEU A CB  
2016 C  CG  . LEU A 239 ? 0.1826 0.1489 0.1424 0.0019  0.0175  -0.0208 240 LEU A CG  
2017 C  CD1 . LEU A 239 ? 0.2318 0.1158 0.2739 -0.0086 -0.0313 -0.0344 240 LEU A CD1 
2018 C  CD2 . LEU A 239 ? 0.2140 0.1603 0.1481 -0.0030 0.0092  -0.0357 240 LEU A CD2 
2019 N  N   . MET A 240 ? 0.1604 0.1095 0.0980 -0.0118 0.0511  -0.0212 241 MET A N   
2020 C  CA  . MET A 240 ? 0.2251 0.1165 0.1111 -0.0187 0.0491  -0.0063 241 MET A CA  
2021 C  C   . MET A 240 ? 0.1855 0.1332 0.1264 -0.0383 0.0310  -0.0207 241 MET A C   
2022 O  O   . MET A 240 ? 0.1711 0.1490 0.0980 -0.0260 0.0320  -0.0060 241 MET A O   
2023 C  CB  . MET A 240 ? 0.2258 0.1199 0.1418 0.0076  0.0478  -0.0208 241 MET A CB  
2024 C  CG  . MET A 240 ? 0.1809 0.1255 0.1116 -0.0152 0.0701  -0.0318 241 MET A CG  
2025 S  SD  . MET A 240 ? 0.2663 0.1185 0.1490 -0.0289 0.0641  -0.0284 241 MET A SD  
2026 C  CE  . MET A 240 ? 0.2327 0.1106 0.1235 -0.0754 0.0640  0.0331  241 MET A CE  
2027 N  N   . VAL A 241 ? 0.1806 0.0860 0.0944 -0.0248 0.0428  -0.0153 242 VAL A N   
2028 C  CA  . VAL A 241 ? 0.1332 0.1004 0.0812 -0.0179 0.0192  -0.0130 242 VAL A CA  
2029 C  C   . VAL A 241 ? 0.1406 0.1205 0.1106 -0.0019 0.0231  -0.0233 242 VAL A C   
2030 O  O   . VAL A 241 ? 0.1309 0.1314 0.1147 -0.0299 0.0491  -0.0242 242 VAL A O   
2031 C  CB  . VAL A 241 ? 0.1206 0.1052 0.1597 -0.0209 0.0364  -0.0320 242 VAL A CB  
2032 C  CG1 . VAL A 241 ? 0.1506 0.1156 0.1122 -0.0148 0.0087  -0.0270 242 VAL A CG1 
2033 C  CG2 . VAL A 241 ? 0.0955 0.1587 0.1587 -0.0136 0.0375  -0.0309 242 VAL A CG2 
2034 N  N   . ASP A 242 ? 0.1388 0.0986 0.0527 -0.0177 0.0298  -0.0082 243 ASP A N   
2035 C  CA  . ASP A 242 ? 0.1162 0.0775 0.0887 0.0188  0.0324  -0.0182 243 ASP A CA  
2036 C  C   . ASP A 242 ? 0.0993 0.1025 0.0815 -0.0262 0.0262  -0.0088 243 ASP A C   
2037 O  O   . ASP A 242 ? 0.0995 0.1023 0.1342 -0.0183 0.0294  -0.0335 243 ASP A O   
2038 C  CB  . ASP A 242 ? 0.1077 0.0971 0.1176 0.0010  -0.0013 -0.0241 243 ASP A CB  
2039 C  CG  . ASP A 242 ? 0.1172 0.1255 0.1186 0.0059  0.0253  0.0071  243 ASP A CG  
2040 O  OD1 . ASP A 242 ? 0.1323 0.0861 0.0960 0.0063  0.0237  -0.0285 243 ASP A OD1 
2041 O  OD2 . ASP A 242 ? 0.1120 0.1241 0.1675 0.0055  0.0205  -0.0377 243 ASP A OD2 
2042 N  N   . ASN A 243 ? 0.1160 0.0734 0.0894 -0.0074 0.0200  -0.0331 244 ASN A N   
2043 C  CA  . ASN A 243 ? 0.1327 0.0777 0.0928 0.0000  0.0126  -0.0295 244 ASN A CA  
2044 C  C   . ASN A 243 ? 0.0791 0.0942 0.1032 -0.0121 0.0383  -0.0170 244 ASN A C   
2045 O  O   . ASN A 243 ? 0.1208 0.0962 0.0707 0.0162  0.0331  -0.0062 244 ASN A O   
2046 C  CB  . ASN A 243 ? 0.1000 0.1256 0.0615 -0.0124 0.0351  -0.0193 244 ASN A CB  
2047 C  CG  . ASN A 243 ? 0.1054 0.0940 0.1016 -0.0137 0.0419  -0.0003 244 ASN A CG  
2048 O  OD1 . ASN A 243 ? 0.1203 0.1242 0.1263 -0.0274 0.0275  0.0020  244 ASN A OD1 
2049 N  ND2 . ASN A 243 ? 0.1260 0.1840 0.1332 -0.0311 -0.0065 0.0359  244 ASN A ND2 
2050 N  N   . TRP A 244 ? 0.0916 0.1168 0.0734 -0.0005 0.0105  -0.0083 245 TRP A N   
2051 C  CA  . TRP A 244 ? 0.0734 0.1101 0.0840 -0.0077 -0.0097 -0.0119 245 TRP A CA  
2052 C  C   . TRP A 244 ? 0.0912 0.1067 0.0943 -0.0031 -0.0013 0.0046  245 TRP A C   
2053 O  O   . TRP A 244 ? 0.0895 0.0988 0.1176 0.0091  0.0017  -0.0263 245 TRP A O   
2054 C  CB  . TRP A 244 ? 0.0912 0.0612 0.1119 0.0088  0.0414  -0.0027 245 TRP A CB  
2055 C  CG  . TRP A 244 ? 0.0398 0.1145 0.1032 -0.0024 0.0288  0.0052  245 TRP A CG  
2056 C  CD1 . TRP A 244 ? 0.0944 0.0641 0.1198 0.0124  0.0320  -0.0274 245 TRP A CD1 
2057 C  CD2 . TRP A 244 ? 0.0887 0.0549 0.0847 -0.0131 0.0017  0.0010  245 TRP A CD2 
2058 N  NE1 . TRP A 244 ? 0.1043 0.0813 0.0955 0.0242  0.0140  -0.0071 245 TRP A NE1 
2059 C  CE2 . TRP A 244 ? 0.1070 0.0723 0.0914 0.0197  -0.0073 0.0154  245 TRP A CE2 
2060 C  CE3 . TRP A 244 ? 0.0684 0.1321 0.1039 0.0019  -0.0118 -0.0038 245 TRP A CE3 
2061 C  CZ2 . TRP A 244 ? 0.0815 0.1009 0.1324 0.0024  -0.0065 0.0197  245 TRP A CZ2 
2062 C  CZ3 . TRP A 244 ? 0.1104 0.1190 0.0984 0.0286  0.0046  -0.0091 245 TRP A CZ3 
2063 C  CH2 . TRP A 244 ? 0.1064 0.1062 0.1264 0.0164  0.0013  0.0219  245 TRP A CH2 
2064 N  N   . ARG A 245 ? 0.0976 0.0779 0.0634 -0.0054 -0.0089 -0.0256 246 ARG A N   
2065 C  CA  . ARG A 245 ? 0.0883 0.0864 0.0843 -0.0159 -0.0057 -0.0239 246 ARG A CA  
2066 C  C   . ARG A 245 ? 0.0540 0.0820 0.0962 0.0214  0.0098  -0.0148 246 ARG A C   
2067 O  O   . ARG A 245 ? 0.0614 0.1027 0.1185 0.0059  0.0126  0.0005  246 ARG A O   
2068 C  CB  . ARG A 245 ? 0.0693 0.1036 0.0971 -0.0240 0.0098  -0.0388 246 ARG A CB  
2069 C  CG  . ARG A 245 ? 0.0435 0.0929 0.1060 -0.0150 -0.0176 -0.0444 246 ARG A CG  
2070 C  CD  . ARG A 245 ? 0.0569 0.0887 0.1288 0.0017  -0.0497 -0.0423 246 ARG A CD  
2071 N  NE  . ARG A 245 ? 0.0418 0.1083 0.1370 0.0013  0.0078  -0.0441 246 ARG A NE  
2072 C  CZ  . ARG A 245 ? 0.0506 0.1033 0.1211 -0.0411 -0.0046 -0.0243 246 ARG A CZ  
2073 N  NH1 . ARG A 245 ? 0.0824 0.1122 0.1142 0.0333  0.0223  -0.0370 246 ARG A NH1 
2074 N  NH2 . ARG A 245 ? 0.0361 0.1542 0.1554 -0.0305 -0.0164 -0.0200 246 ARG A NH2 
2075 N  N   . PRO A 246 ? 0.0772 0.1067 0.0657 0.0156  -0.0031 0.0120  247 PRO A N   
2076 C  CA  . PRO A 246 ? 0.0847 0.1086 0.0855 0.0142  0.0076  0.0181  247 PRO A CA  
2077 C  C   . PRO A 246 ? 0.0635 0.1002 0.0989 0.0094  0.0088  0.0115  247 PRO A C   
2078 O  O   . PRO A 246 ? 0.0858 0.0812 0.1224 -0.0065 -0.0049 0.0068  247 PRO A O   
2079 C  CB  . PRO A 246 ? 0.1183 0.1328 0.1374 0.0408  0.0171  0.0164  247 PRO A CB  
2080 C  CG  . PRO A 246 ? 0.1278 0.2208 0.1864 0.0623  0.0261  0.0581  247 PRO A CG  
2081 C  CD  . PRO A 246 ? 0.0512 0.1280 0.1407 0.0276  0.0057  0.0300  247 PRO A CD  
2082 N  N   . ALA A 247 ? 0.0794 0.1106 0.0804 -0.0043 0.0100  0.0082  248 ALA A N   
2083 C  CA  . ALA A 247 ? 0.0970 0.1023 0.0831 0.0088  0.0013  -0.0168 248 ALA A CA  
2084 C  C   . ALA A 247 ? 0.0943 0.0894 0.1124 0.0216  -0.0163 -0.0126 248 ALA A C   
2085 O  O   . ALA A 247 ? 0.1230 0.0870 0.1463 0.0366  -0.0118 -0.0126 248 ALA A O   
2086 C  CB  . ALA A 247 ? 0.1474 0.1296 0.1122 -0.0006 0.0474  0.0221  248 ALA A CB  
2087 N  N   . GLN A 248 ? 0.0775 0.0758 0.1111 0.0142  -0.0324 -0.0166 249 GLN A N   
2088 C  CA  . GLN A 248 ? 0.0761 0.1007 0.1122 0.0093  -0.0038 -0.0155 249 GLN A CA  
2089 C  C   . GLN A 248 ? 0.0788 0.1032 0.1201 0.0303  -0.0266 -0.0020 249 GLN A C   
2090 O  O   . GLN A 248 ? 0.0610 0.1086 0.1391 0.0008  -0.0108 0.0178  249 GLN A O   
2091 C  CB  . GLN A 248 ? 0.1278 0.0639 0.1519 0.0215  -0.0127 -0.0107 249 GLN A CB  
2092 C  CG  . GLN A 248 ? 0.0874 0.0979 0.1443 0.0031  0.0167  0.0007  249 GLN A CG  
2093 C  CD  . GLN A 248 ? 0.1036 0.1460 0.1451 -0.0546 0.0103  0.0012  249 GLN A CD  
2094 O  OE1 . GLN A 248 ? 0.0989 0.2079 0.1524 -0.0406 -0.0254 -0.0390 249 GLN A OE1 
2095 N  NE2 . GLN A 248 ? 0.1192 0.1364 0.1375 -0.0136 -0.0348 -0.0126 249 GLN A NE2 
2096 N  N   . PRO A 249 ? 0.1019 0.1743 0.1293 0.0266  -0.0294 -0.0164 250 PRO A N   
2097 C  CA  . PRO A 249 ? 0.1133 0.1882 0.1281 0.0615  -0.0307 -0.0074 250 PRO A CA  
2098 C  C   . PRO A 249 ? 0.1027 0.1305 0.1043 0.0436  -0.0266 0.0003  250 PRO A C   
2099 O  O   . PRO A 249 ? 0.1089 0.1346 0.1034 0.0281  -0.0274 0.0187  250 PRO A O   
2100 C  CB  . PRO A 249 ? 0.1039 0.2383 0.1388 0.0614  -0.0485 -0.0041 250 PRO A CB  
2101 C  CG  . PRO A 249 ? 0.1694 0.2717 0.1752 0.0403  -0.0679 -0.0342 250 PRO A CG  
2102 C  CD  . PRO A 249 ? 0.0934 0.2212 0.1791 0.0480  -0.0443 -0.0132 250 PRO A CD  
2103 N  N   . LEU A 250 ? 0.1242 0.1410 0.1165 0.0412  -0.0160 0.0008  251 LEU A N   
2104 C  CA  . LEU A 250 ? 0.1162 0.1411 0.1101 0.0109  0.0024  -0.0034 251 LEU A CA  
2105 C  C   . LEU A 250 ? 0.1058 0.1418 0.1389 0.0311  -0.0324 -0.0118 251 LEU A C   
2106 O  O   . LEU A 250 ? 0.1070 0.1274 0.1665 0.0295  -0.0463 -0.0120 251 LEU A O   
2107 C  CB  . LEU A 250 ? 0.1264 0.1474 0.1609 0.0149  -0.0010 -0.0020 251 LEU A CB  
2108 C  CG  . LEU A 250 ? 0.1629 0.1826 0.1342 0.0017  0.0132  0.0035  251 LEU A CG  
2109 C  CD1 . LEU A 250 ? 0.1083 0.2139 0.1402 -0.0181 -0.0104 -0.0205 251 LEU A CD1 
2110 C  CD2 . LEU A 250 ? 0.1691 0.1963 0.1952 -0.0248 0.0461  -0.0184 251 LEU A CD2 
2111 N  N   . LYS A 251 ? 0.1447 0.1476 0.1296 0.0509  -0.0608 -0.0087 252 LYS A N   
2112 C  CA  . LYS A 251 ? 0.1223 0.1765 0.1409 0.0262  -0.0359 -0.0160 252 LYS A CA  
2113 C  C   . LYS A 251 ? 0.1228 0.1819 0.1636 0.0206  -0.0386 -0.0222 252 LYS A C   
2114 O  O   . LYS A 251 ? 0.1664 0.2203 0.1888 0.0054  -0.0055 -0.0135 252 LYS A O   
2115 C  CB  . LYS A 251 ? 0.1773 0.1427 0.2014 0.0177  -0.0394 -0.0164 252 LYS A CB  
2116 C  CG  . LYS A 251 ? 0.1712 0.2334 0.2085 -0.0121 -0.0155 -0.0215 252 LYS A CG  
2117 C  CD  . LYS A 251 ? 0.1472 0.2883 0.3046 0.0000  -0.0023 -0.0273 252 LYS A CD  
2118 C  CE  . LYS A 251 ? 0.2021 0.3054 0.3349 0.0226  0.0137  -0.0074 252 LYS A CE  
2119 N  NZ  . LYS A 251 ? 0.2785 0.3544 0.3974 0.0310  0.0157  0.0306  252 LYS A NZ  
2120 N  N   . ASN A 252 ? 0.1208 0.2076 0.1564 0.0384  -0.0560 -0.0231 253 ASN A N   
2121 C  CA  . ASN A 252 ? 0.1632 0.2778 0.2359 0.0146  -0.0414 -0.0335 253 ASN A CA  
2122 C  C   . ASN A 252 ? 0.1959 0.2469 0.2581 0.0266  -0.0386 -0.0212 253 ASN A C   
2123 O  O   . ASN A 252 ? 0.2377 0.2673 0.2917 0.0353  -0.0297 0.0105  253 ASN A O   
2124 C  CB  . ASN A 252 ? 0.1995 0.3069 0.2770 0.0120  -0.0465 -0.0430 253 ASN A CB  
2125 C  CG  . ASN A 252 ? 0.2922 0.3438 0.3066 0.0065  -0.0203 -0.0198 253 ASN A CG  
2126 O  OD1 . ASN A 252 ? 0.3768 0.4603 0.3458 -0.0298 -0.0008 0.0135  253 ASN A OD1 
2127 N  ND2 . ASN A 252 ? 0.3628 0.3711 0.4023 0.0000  -0.0337 0.0012  253 ASN A ND2 
2128 N  N   . ARG A 253 ? 0.1077 0.2298 0.1503 0.0126  -0.0172 -0.0153 254 ARG A N   
2129 C  CA  . ARG A 253 ? 0.1025 0.1413 0.1361 0.0230  0.0081  -0.0062 254 ARG A CA  
2130 C  C   . ARG A 253 ? 0.1460 0.1393 0.1140 0.0115  0.0107  -0.0193 254 ARG A C   
2131 O  O   . ARG A 253 ? 0.1988 0.1521 0.2246 0.0373  0.0478  0.0197  254 ARG A O   
2132 C  CB  . ARG A 253 ? 0.1176 0.1212 0.1097 -0.0046 -0.0055 -0.0140 254 ARG A CB  
2133 C  CG  . ARG A 253 ? 0.1790 0.0890 0.0882 -0.0113 -0.0184 -0.0291 254 ARG A CG  
2134 C  CD  . ARG A 253 ? 0.1655 0.0991 0.0718 0.0264  0.0190  -0.0171 254 ARG A CD  
2135 N  NE  . ARG A 253 ? 0.1253 0.1334 0.0666 0.0344  -0.0152 -0.0092 254 ARG A NE  
2136 C  CZ  . ARG A 253 ? 0.0807 0.0979 0.0799 -0.0103 0.0032  0.0003  254 ARG A CZ  
2137 N  NH1 . ARG A 253 ? 0.0882 0.0989 0.0944 0.0111  -0.0186 0.0126  254 ARG A NH1 
2138 N  NH2 . ARG A 253 ? 0.0840 0.0811 0.0916 0.0340  -0.0146 -0.0092 254 ARG A NH2 
2139 N  N   . GLN A 254 ? 0.1271 0.1737 0.1478 0.0193  -0.0024 -0.0370 255 GLN A N   
2140 C  CA  . GLN A 254 ? 0.1702 0.1957 0.1321 0.0078  -0.0076 -0.0423 255 GLN A CA  
2141 C  C   . GLN A 254 ? 0.1547 0.1524 0.1414 0.0063  -0.0212 -0.0135 255 GLN A C   
2142 O  O   . GLN A 254 ? 0.1977 0.1560 0.1978 -0.0199 -0.0557 -0.0076 255 GLN A O   
2143 C  CB  . GLN A 254 ? 0.1967 0.2684 0.1623 0.0215  0.0028  -0.0386 255 GLN A CB  
2144 C  CG  . GLN A 254 ? 0.3399 0.3806 0.3203 -0.0207 -0.0034 -0.0207 255 GLN A CG  
2145 C  CD  . GLN A 254 ? 0.4535 0.4315 0.4000 0.0073  -0.0116 0.0271  255 GLN A CD  
2146 O  OE1 . GLN A 254 ? 0.5618 0.4686 0.4144 -0.0068 -0.0487 -0.0076 255 GLN A OE1 
2147 N  NE2 . GLN A 254 ? 0.4995 0.5117 0.4309 0.0008  -0.0434 -0.0003 255 GLN A NE2 
2148 N  N   . ILE A 255 ? 0.1013 0.1406 0.1111 -0.0006 -0.0089 -0.0020 256 ILE A N   
2149 C  CA  . ILE A 255 ? 0.0829 0.1219 0.1125 0.0151  0.0055  0.0021  256 ILE A CA  
2150 C  C   . ILE A 255 ? 0.0576 0.1375 0.0883 0.0159  0.0020  0.0099  256 ILE A C   
2151 O  O   . ILE A 255 ? 0.1203 0.1259 0.1208 0.0195  0.0137  0.0303  256 ILE A O   
2152 C  CB  . ILE A 255 ? 0.0831 0.1168 0.1171 0.0414  -0.0187 -0.0087 256 ILE A CB  
2153 C  CG1 . ILE A 255 ? 0.1127 0.1190 0.1113 0.0261  0.0340  -0.0013 256 ILE A CG1 
2154 C  CG2 . ILE A 255 ? 0.1150 0.1169 0.0928 0.0242  0.0049  0.0104  256 ILE A CG2 
2155 C  CD1 . ILE A 255 ? 0.1428 0.1770 0.1438 0.0035  0.0076  -0.0377 256 ILE A CD1 
2156 N  N   . LYS A 256 ? 0.0935 0.1296 0.1007 -0.0015 -0.0178 0.0066  257 LYS A N   
2157 C  CA  . LYS A 256 ? 0.0983 0.1208 0.1088 -0.0181 0.0057  -0.0131 257 LYS A CA  
2158 C  C   . LYS A 256 ? 0.0599 0.1291 0.1107 -0.0136 0.0146  0.0051  257 LYS A C   
2159 O  O   . LYS A 256 ? 0.1205 0.1984 0.0781 -0.0636 0.0230  0.0176  257 LYS A O   
2160 C  CB  . LYS A 256 ? 0.1064 0.1399 0.1306 0.0264  0.0070  -0.0196 257 LYS A CB  
2161 C  CG  . LYS A 256 ? 0.2081 0.1643 0.2309 -0.0225 0.0012  -0.0672 257 LYS A CG  
2162 C  CD  . LYS A 256 ? 0.3073 0.2434 0.3197 0.0109  -0.0070 -0.0441 257 LYS A CD  
2163 C  CE  . LYS A 256 ? 0.3508 0.3030 0.3195 -0.0392 -0.0142 -0.0542 257 LYS A CE  
2164 N  NZ  . LYS A 256 ? 0.3783 0.3269 0.4259 -0.0006 -0.0206 -0.0491 257 LYS A NZ  
2165 N  N   . ALA A 257 ? 0.0813 0.1600 0.0867 -0.0277 0.0222  0.0186  258 ALA A N   
2166 C  CA  . ALA A 257 ? 0.0833 0.1483 0.1413 -0.0161 -0.0010 0.0026  258 ALA A CA  
2167 C  C   . ALA A 257 ? 0.0781 0.1215 0.1052 -0.0179 0.0148  0.0030  258 ALA A C   
2168 O  O   . ALA A 257 ? 0.1238 0.1655 0.1019 0.0071  0.0192  -0.0223 258 ALA A O   
2169 C  CB  . ALA A 257 ? 0.1213 0.1255 0.1892 -0.0236 0.0076  0.0195  258 ALA A CB  
2170 N  N   . SER A 258 ? 0.1224 0.1537 0.1223 -0.0051 0.0060  0.0017  259 SER A N   
2171 C  CA  . SER A 258 ? 0.1066 0.1704 0.1125 -0.0052 0.0113  -0.0087 259 SER A CA  
2172 C  C   . SER A 258 ? 0.1137 0.1797 0.1600 -0.0019 0.0196  0.0216  259 SER A C   
2173 O  O   . SER A 258 ? 0.1226 0.2455 0.2301 0.0122  0.0302  0.0192  259 SER A O   
2174 C  CB  . SER A 258 ? 0.1723 0.1514 0.1057 0.0051  -0.0164 0.0065  259 SER A CB  
2175 O  OG  . SER A 258 ? 0.1063 0.1743 0.1418 -0.0175 0.0277  -0.0126 259 SER A OG  
2176 N  N   . PHE A 259 ? 0.1137 0.1905 0.1562 -0.0445 0.0315  0.0000  260 PHE A N   
2177 C  CA  . PHE A 259 ? 0.1547 0.2086 0.2309 -0.0419 0.0328  0.0151  260 PHE A CA  
2178 C  C   . PHE A 259 ? 0.2218 0.2639 0.2502 -0.0408 0.0164  0.0220  260 PHE A C   
2179 O  O   . PHE A 259 ? 0.2336 0.2103 0.2384 -0.0278 0.0001  0.0597  260 PHE A O   
2180 C  CB  . PHE A 259 ? 0.1497 0.2180 0.2114 -0.0309 0.0326  -0.0055 260 PHE A CB  
2181 C  CG  . PHE A 259 ? 0.1507 0.1846 0.2415 -0.0127 0.0164  -0.0023 260 PHE A CG  
2182 C  CD1 . PHE A 259 ? 0.1424 0.1605 0.1560 -0.0057 0.0093  -0.0232 260 PHE A CD1 
2183 C  CD2 . PHE A 259 ? 0.2050 0.2027 0.2383 -0.0052 -0.0034 0.0071  260 PHE A CD2 
2184 C  CE1 . PHE A 259 ? 0.1436 0.1655 0.2301 -0.0311 0.0034  -0.0303 260 PHE A CE1 
2185 C  CE2 . PHE A 259 ? 0.1953 0.2273 0.2691 -0.0103 0.0048  -0.0003 260 PHE A CE2 
2186 C  CZ  . PHE A 259 ? 0.2352 0.2372 0.2333 -0.0041 -0.0028 0.0109  260 PHE A CZ  
2187 N  N   . LYS A 260 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  261 LYS A N   
2188 C  CA  . LYS A 260 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  261 LYS A CA  
2189 C  C   . LYS A 260 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  261 LYS A C   
2190 O  O   . LYS A 260 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  261 LYS A O   
2191 C  CB  . LYS A 260 ? 0.2533 0.2533 0.2533 0.0000  0.0000  0.0000  261 LYS A CB  
2192 C  CG  . LYS A 260 ? 0.2533 0.2533 0.2533 0.0000  0.0000  0.0000  261 LYS A CG  
2193 C  CD  . LYS A 260 ? 0.2533 0.2533 0.2533 0.0000  0.0000  0.0000  261 LYS A CD  
2194 C  CE  . LYS A 260 ? 0.2533 0.2533 0.2533 0.0000  0.0000  0.0000  261 LYS A CE  
2195 N  NZ  . LYS A 260 ? 0.2533 0.2533 0.2533 0.0000  0.0000  0.0000  261 LYS A NZ  
2196 O  OXT . LYS A 260 ? 0.3799 0.3799 0.3799 0.0000  0.0000  0.0000  261 LYS A OXT 
2197 ZN ZN  . ZN  B .   ? 0.0858 0.0727 0.0779 -0.0086 -0.0049 -0.0008 262 ZN  A ZN  
2198 S  S   . DMS C .   ? 0.2189 0.2865 0.3278 -0.0296 0.0423  0.0091  263 DMS A S   
2199 O  O   . DMS C .   ? 0.2876 0.3057 0.3991 -0.0252 0.0194  0.0368  263 DMS A O   
2200 C  C1  . DMS C .   ? 0.2369 0.2255 0.2752 0.0546  0.0723  -0.0052 263 DMS A C1  
2201 C  C2  . DMS C .   ? 0.2376 0.2552 0.2544 -0.0143 0.0421  -0.0445 263 DMS A C2  
2202 S  S   . DMS D .   ? 0.5134 0.4869 0.5278 0.0175  -0.0037 -0.0102 264 DMS A S   
2203 O  O   . DMS D .   ? 0.4307 0.3640 0.4546 0.0001  0.0105  0.0100  264 DMS A O   
2204 C  C1  . DMS D .   ? 0.4596 0.3867 0.4415 -0.0028 0.0093  0.0199  264 DMS A C1  
2205 C  C2  . DMS D .   ? 0.4474 0.4449 0.4866 0.0175  -0.0049 0.0006  264 DMS A C2  
2206 N  N1  . BCN E .   ? 0.3723 0.3537 0.3562 -0.0703 0.0098  0.0073  265 BCN A N1  
2207 C  C1  . BCN E .   ? 0.3378 0.3711 0.3239 -0.0394 -0.0119 0.0557  265 BCN A C1  
2208 C  C2  . BCN E .   ? 0.3837 0.3934 0.3292 -0.0286 -0.0030 0.0300  265 BCN A C2  
2209 O  O21 . BCN E .   ? 0.3601 0.3535 0.2872 -0.0450 0.0254  0.0516  265 BCN A O21 
2210 O  O22 . BCN E .   ? 0.4544 0.3508 0.4099 -0.0318 -0.0093 0.0164  265 BCN A O22 
2211 C  C3  . BCN E .   ? 0.3837 0.3560 0.3903 -0.0443 -0.0003 0.0262  265 BCN A C3  
2212 C  C4  . BCN E .   ? 0.4337 0.4096 0.4086 -0.0148 0.0201  -0.0054 265 BCN A C4  
2213 O  O4  . BCN E .   ? 0.3260 0.3342 0.4059 -0.0428 0.0516  0.0046  265 BCN A O4  
2214 C  C5  . BCN E .   ? 0.4222 0.4192 0.4050 -0.0179 0.0160  0.0082  265 BCN A C5  
2215 C  C6  . BCN E .   ? 0.2784 0.2265 0.2595 -0.0496 0.0483  0.0107  265 BCN A C6  
2216 O  O6  . BCN E .   ? 0.5375 0.4146 0.4747 -0.0513 0.0465  -0.0304 265 BCN A O6  
2217 N  N1  . E90 F .   ? 0.2004 0.1824 0.1625 -0.0059 0.0504  0.0509  266 E90 A N1  
2218 C  C2  . E90 F .   ? 0.2797 0.1427 0.1720 -0.0346 0.0692  0.0070  266 E90 A C2  
2219 N  N3  . E90 F .   ? 0.2836 0.1546 0.2237 -0.0621 0.0790  0.0482  266 E90 A N3  
2220 C  C4  . E90 F .   ? 0.3267 0.2099 0.2567 -0.0192 0.0397  -0.0161 266 E90 A C4  
2221 C  C5  . E90 F .   ? 0.2777 0.2117 0.2595 -0.0092 0.0672  -0.0120 266 E90 A C5  
2222 C  C6  . E90 F .   ? 0.2106 0.2291 0.1916 -0.0046 0.0560  0.0066  266 E90 A C6  
2223 S  S7  . E90 F .   ? 0.3095 0.1645 0.2398 -0.0478 0.1222  0.0251  266 E90 A S7  
2224 C  C8  . E90 F .   ? 0.1691 0.1396 0.2392 -0.0395 0.1152  0.0529  266 E90 A C8  
2225 C  C9  . E90 F .   ? 0.1629 0.1177 0.2150 -0.0207 0.0480  0.0395  266 E90 A C9  
2226 O  O10 . E90 F .   ? 0.2381 0.1088 0.2381 -0.0037 0.0335  0.0531  266 E90 A O10 
2227 C  C11 . E90 F .   ? 0.1837 0.0485 0.1432 -0.0154 0.0340  0.0220  266 E90 A C11 
2228 C  C12 . E90 F .   ? 0.1303 0.1289 0.1375 0.0041  0.0328  0.0230  266 E90 A C12 
2229 C  C13 . E90 F .   ? 0.1404 0.1016 0.1118 -0.0188 0.0339  0.0562  266 E90 A C13 
2230 C  C14 . E90 F .   ? 0.0521 0.0728 0.1019 -0.0108 0.0178  0.0120  266 E90 A C14 
2231 C  C15 . E90 F .   ? 0.1196 0.0480 0.1101 0.0166  -0.0362 0.0165  266 E90 A C15 
2232 C  C16 . E90 F .   ? 0.1237 0.0962 0.1226 -0.0086 -0.0206 -0.0031 266 E90 A C16 
2233 S  S17 . E90 F .   ? 0.0860 0.0826 0.0815 -0.0102 -0.0120 -0.0052 266 E90 A S17 
2234 O  O18 . E90 F .   ? 0.0339 0.0867 0.0980 0.0076  -0.0108 -0.0015 266 E90 A O18 
2235 O  O19 . E90 F .   ? 0.0851 0.0844 0.0878 -0.0249 -0.0081 0.0071  266 E90 A O19 
2236 N  N20 . E90 F .   ? 0.0608 0.0795 0.1022 -0.0188 -0.0077 -0.0274 266 E90 A N20 
2237 O  O   . HOH G .   ? 0.2440 0.4240 0.2925 -0.0912 -0.0518 -0.0837 126 HOH A O   
2238 O  O   . HOH G .   ? 0.4032 0.3934 0.3253 0.0043  0.0065  -0.1204 267 HOH A O   
2239 O  O   . HOH G .   ? 0.3684 0.3896 0.4584 0.0837  0.0164  -0.1150 268 HOH A O   
2240 O  O   . HOH G .   ? 0.3270 0.3625 0.3544 0.0156  -0.1544 0.0529  269 HOH A O   
2241 O  O   . HOH G .   ? 0.4392 0.3837 0.3557 -0.0974 -0.0273 -0.0395 270 HOH A O   
2242 O  O   . HOH G .   ? 0.4011 0.3180 0.3399 0.0013  -0.0586 -0.0148 271 HOH A O   
2243 O  O   . HOH G .   ? 0.4140 0.2907 0.3981 -0.0601 0.0057  0.0093  272 HOH A O   
2244 O  O   . HOH G .   ? 0.3651 0.4162 0.5773 -0.0337 -0.0015 0.0127  273 HOH A O   
2245 O  O   . HOH G .   ? 0.5540 0.4568 0.1885 0.0934  -0.0346 -0.0008 274 HOH A O   
2246 O  O   . HOH G .   ? 0.4226 0.3562 0.2272 -0.0522 0.0555  -0.0449 275 HOH A O   
2247 O  O   . HOH G .   ? 0.3643 0.3640 0.4208 -0.0160 0.0436  0.0104  276 HOH A O   
2248 O  O   . HOH G .   ? 0.4217 0.4690 0.4208 0.0432  -0.0132 0.0926  277 HOH A O   
2249 O  O   . HOH G .   ? 0.4246 0.2924 0.4635 -0.0126 0.0295  0.0771  278 HOH A O   
2250 O  O   . HOH G .   ? 0.2967 0.4896 0.5633 0.0452  -0.0059 -0.0571 279 HOH A O   
2251 O  O   . HOH G .   ? 0.3357 0.2649 0.3862 -0.1331 0.0370  0.0720  280 HOH A O   
2252 O  O   . HOH G .   ? 0.4277 0.3249 0.3564 -0.0074 -0.0679 0.0060  281 HOH A O   
2253 O  O   . HOH G .   ? 0.3601 0.5363 0.3482 0.0102  0.0615  0.0219  282 HOH A O   
2254 O  O   . HOH G .   ? 0.2648 0.4161 0.4408 -0.0105 0.0339  0.0209  283 HOH A O   
2255 O  O   . HOH G .   ? 0.3910 0.4797 0.3707 -0.0003 -0.0241 -0.0568 284 HOH A O   
2256 O  O   . HOH G .   ? 0.3044 0.6025 0.6660 0.0164  0.0199  0.0024  285 HOH A O   
2257 O  O   . HOH G .   ? 0.3543 0.4434 0.3579 -0.0710 0.0003  -0.0940 286 HOH A O   
2258 O  O   . HOH G .   ? 0.4296 0.4922 0.4280 0.0118  0.1160  -0.0013 287 HOH A O   
2259 O  O   . HOH G .   ? 0.5411 0.3464 0.4230 -0.0080 -0.0093 -0.0575 288 HOH A O   
2260 O  O   . HOH G .   ? 0.5260 0.5383 0.4519 -0.0092 0.0274  -0.0012 289 HOH A O   
2261 O  O   . HOH G .   ? 0.5314 0.4323 0.2958 -0.0447 -0.0808 -0.1291 290 HOH A O   
2262 O  O   . HOH G .   ? 0.3136 0.4004 0.3686 -0.0750 0.0820  0.0487  291 HOH A O   
2263 O  O   . HOH G .   ? 0.2718 0.5572 0.4029 -0.0256 0.0071  -0.0199 292 HOH A O   
2264 O  O   . HOH G .   ? 0.3472 0.4562 0.3859 -0.0595 -0.0057 0.0233  293 HOH A O   
2265 O  O   . HOH G .   ? 0.6568 0.6904 0.6104 -0.0264 0.0249  -0.0136 294 HOH A O   
2266 O  O   . HOH G .   ? 0.3989 0.4233 0.4410 -0.0085 0.0500  -0.0403 295 HOH A O   
2267 O  O   . HOH G .   ? 0.4664 0.4900 0.4916 -0.0019 0.0274  -0.0187 296 HOH A O   
2268 O  O   . HOH G .   ? 0.4366 0.4315 0.4503 0.0104  0.0335  0.0982  297 HOH A O   
2269 O  O   . HOH G .   ? 0.4582 0.3680 0.4534 0.1407  0.0099  -0.0812 298 HOH A O   
2270 O  O   . HOH G .   ? 0.4039 0.4254 0.4397 -0.0379 -0.0076 0.0384  299 HOH A O   
2271 O  O   . HOH G .   ? 0.5271 0.5532 0.2565 0.0802  0.0185  -0.0825 300 HOH A O   
2272 O  O   . HOH G .   ? 0.4483 0.6521 0.5759 0.0001  0.0474  0.0031  301 HOH A O   
2273 O  O   . HOH G .   ? 0.5288 0.5232 0.6524 -0.0057 -0.0320 0.0175  302 HOH A O   
2274 O  O   . HOH G .   ? 0.4977 0.5733 0.3621 -0.0055 0.0156  0.0201  303 HOH A O   
2275 O  O   . HOH G .   ? 0.3871 0.4269 0.5889 0.0065  0.0318  -0.0639 304 HOH A O   
2276 O  O   . HOH G .   ? 0.3864 0.5957 0.5759 -0.0476 0.0233  0.0059  305 HOH A O   
2277 O  O   . HOH G .   ? 0.2381 0.4915 0.4546 -0.0015 -0.0208 0.0289  306 HOH A O   
2278 O  O   . HOH G .   ? 0.3808 0.4330 0.4340 -0.0062 0.0568  -0.0383 307 HOH A O   
2279 O  O   . HOH G .   ? 0.3817 0.3980 0.3345 0.0241  0.0219  -0.0137 308 HOH A O   
2280 O  O   . HOH G .   ? 0.5943 0.5792 0.6557 -0.0317 0.0077  0.0015  309 HOH A O   
2281 O  O   . HOH G .   ? 0.6327 0.6219 0.6904 0.0043  -0.0060 0.0105  310 HOH A O   
2282 O  O   . HOH G .   ? 0.4079 0.3973 0.5343 0.0483  0.0231  0.0160  311 HOH A O   
2283 O  O   . HOH G .   ? 0.4474 0.4951 0.3325 -0.0190 0.0212  0.0551  312 HOH A O   
2284 O  O   . HOH G .   ? 0.5159 0.3037 0.3849 0.0308  0.0368  -0.0390 313 HOH A O   
2285 O  O   . HOH G .   ? 0.3761 0.2252 0.5285 0.0261  -0.0527 0.0917  314 HOH A O   
2286 O  O   . HOH G .   ? 0.4879 0.3928 0.3828 0.0599  -0.0196 0.0684  315 HOH A O   
2287 O  O   . HOH G .   ? 0.4093 0.2821 0.4162 0.0944  0.0478  -0.0245 316 HOH A O   
2288 O  O   . HOH G .   ? 0.4259 0.3611 0.3400 0.0668  0.0425  -0.0131 317 HOH A O   
2289 O  O   . HOH G .   ? 0.3713 0.3224 0.4765 -0.0041 0.0662  0.0308  318 HOH A O   
2290 O  O   . HOH G .   ? 0.3930 0.2808 0.4683 -0.0562 0.0785  0.0176  319 HOH A O   
2291 O  O   . HOH G .   ? 0.3332 0.5279 0.4860 -0.0299 -0.0612 -0.0423 320 HOH A O   
2292 O  O   . HOH G .   ? 0.0847 0.1048 0.0979 -0.0211 0.0232  -0.0141 321 HOH A O   
2293 O  O   . HOH G .   ? 0.1242 0.0761 0.1095 0.0020  -0.0098 -0.0254 322 HOH A O   
2294 O  O   . HOH G .   ? 0.0723 0.1055 0.1045 -0.0131 0.0164  -0.0005 323 HOH A O   
2295 O  O   . HOH G .   ? 0.0817 0.1318 0.1081 0.0148  -0.0133 -0.0104 324 HOH A O   
2296 O  O   . HOH G .   ? 0.1221 0.0957 0.1174 -0.0093 -0.0052 -0.0322 325 HOH A O   
2297 O  O   . HOH G .   ? 0.0779 0.1844 0.2006 0.0152  0.0131  0.0154  326 HOH A O   
2298 O  O   . HOH G .   ? 0.1413 0.0998 0.1720 -0.0003 -0.0250 0.0073  327 HOH A O   
2299 O  O   . HOH G .   ? 0.0689 0.1553 0.1321 0.0071  -0.0353 0.0303  328 HOH A O   
2300 O  O   . HOH G .   ? 0.1930 0.0882 0.0539 -0.0460 0.0065  0.0183  329 HOH A O   
2301 O  O   . HOH G .   ? 0.1615 0.1906 0.2458 0.0142  -0.1254 -0.0114 330 HOH A O   
2302 O  O   . HOH G .   ? 0.1896 0.0939 0.1377 -0.0109 0.0142  0.0080  331 HOH A O   
2303 O  O   . HOH G .   ? 0.1396 0.1145 0.1629 0.0342  -0.0186 0.0031  332 HOH A O   
2304 O  O   . HOH G .   ? 0.1960 0.1213 0.1899 -0.0186 -0.0340 -0.0059 333 HOH A O   
2305 O  O   . HOH G .   ? 0.0452 0.1476 0.2354 0.0003  0.0013  -0.0215 334 HOH A O   
2306 O  O   . HOH G .   ? 0.0723 0.0874 0.1813 0.0182  -0.0161 0.0024  335 HOH A O   
2307 O  O   . HOH G .   ? 0.1754 0.1500 0.2906 -0.0560 -0.0703 -0.0252 336 HOH A O   
2308 O  O   . HOH G .   ? 0.1180 0.1634 0.1457 -0.0157 -0.0476 0.0373  337 HOH A O   
2309 O  O   . HOH G .   ? 0.1553 0.1677 0.1773 0.0390  -0.0155 -0.0137 338 HOH A O   
2310 O  O   . HOH G .   ? 0.2879 0.1740 0.1508 -0.0098 -0.0619 0.0436  339 HOH A O   
2311 O  O   . HOH G .   ? 0.0948 0.1106 0.1614 0.0251  -0.0368 0.0083  340 HOH A O   
2312 O  O   . HOH G .   ? 0.2002 0.2623 0.1415 0.0210  0.0359  -0.0447 341 HOH A O   
2313 O  O   . HOH G .   ? 0.2863 0.1783 0.2653 0.0560  0.0465  0.0392  342 HOH A O   
2314 O  O   . HOH G .   ? 0.1068 0.1661 0.1697 0.0108  -0.0098 -0.0089 343 HOH A O   
2315 O  O   . HOH G .   ? 0.1826 0.1809 0.1544 -0.0131 -0.0021 0.0320  344 HOH A O   
2316 O  O   . HOH G .   ? 0.2404 0.2173 0.2052 -0.0535 0.0046  -0.0425 345 HOH A O   
2317 O  O   . HOH G .   ? 0.0974 0.1702 0.2573 -0.0051 0.0024  0.0125  346 HOH A O   
2318 O  O   . HOH G .   ? 0.2179 0.1479 0.1418 -0.0184 -0.0623 0.0003  347 HOH A O   
2319 O  O   . HOH G .   ? 0.3853 0.1339 0.1544 -0.0403 -0.1119 -0.0032 348 HOH A O   
2320 O  O   . HOH G .   ? 0.1493 0.1639 0.2864 0.0031  0.0135  -0.0078 349 HOH A O   
2321 O  O   . HOH G .   ? 0.1586 0.1307 0.1633 -0.0143 -0.0046 0.0044  350 HOH A O   
2322 O  O   . HOH G .   ? 0.2540 0.1885 0.1694 0.0159  0.0233  0.0782  351 HOH A O   
2323 O  O   . HOH G .   ? 0.1206 0.1695 0.2721 -0.0350 -0.0582 0.0223  352 HOH A O   
2324 O  O   . HOH G .   ? 0.1774 0.2113 0.2608 0.0126  -0.0555 -0.0111 353 HOH A O   
2325 O  O   . HOH G .   ? 0.1393 0.1589 0.1888 -0.0041 0.0410  -0.0003 354 HOH A O   
2326 O  O   . HOH G .   ? 0.2268 0.3077 0.2854 0.0160  -0.0110 0.0303  355 HOH A O   
2327 O  O   . HOH G .   ? 0.3756 0.2250 0.1680 -0.0608 -0.0631 -0.0208 356 HOH A O   
2328 O  O   . HOH G .   ? 0.1729 0.2007 0.3318 0.0737  -0.0728 -0.0276 357 HOH A O   
2329 O  O   . HOH G .   ? 0.2054 0.2911 0.2061 -0.0326 0.0219  -0.0408 358 HOH A O   
2330 O  O   . HOH G .   ? 0.2551 0.1612 0.1729 0.0351  -0.0329 0.0318  359 HOH A O   
2331 O  O   . HOH G .   ? 0.1032 0.1923 0.2757 -0.0086 -0.0286 -0.0245 360 HOH A O   
2332 O  O   . HOH G .   ? 0.2122 0.1576 0.2623 0.0414  0.0273  -0.0175 361 HOH A O   
2333 O  O   . HOH G .   ? 0.1745 0.2070 0.2779 0.0032  -0.0326 -0.0185 362 HOH A O   
2334 O  O   . HOH G .   ? 0.2065 0.1970 0.1456 0.0046  -0.0318 0.0222  363 HOH A O   
2335 O  O   . HOH G .   ? 0.1346 0.3152 0.4271 0.0500  -0.0373 0.0540  364 HOH A O   
2336 O  O   . HOH G .   ? 0.2049 0.0761 0.1895 0.0231  -0.0109 -0.0142 365 HOH A O   
2337 O  O   . HOH G .   ? 0.1992 0.2106 0.2467 -0.0256 -0.0109 0.0584  366 HOH A O   
2338 O  O   . HOH G .   ? 0.2587 0.2097 0.2266 -0.0109 -0.0110 0.0161  367 HOH A O   
2339 O  O   . HOH G .   ? 0.2940 0.1443 0.2334 0.0366  -0.0803 0.0073  368 HOH A O   
2340 O  O   . HOH G .   ? 0.2702 0.1312 0.2476 0.0251  -0.1138 -0.0081 369 HOH A O   
2341 O  O   . HOH G .   ? 0.2406 0.2002 0.1643 0.0430  -0.0395 0.0546  370 HOH A O   
2342 O  O   . HOH G .   ? 0.3659 0.1312 0.2117 -0.1009 -0.0236 -0.0326 371 HOH A O   
2343 O  O   . HOH G .   ? 0.2106 0.1738 0.2540 -0.0274 0.0041  -0.0110 372 HOH A O   
2344 O  O   . HOH G .   ? 0.2606 0.1508 0.3601 0.0196  0.1154  0.0000  373 HOH A O   
2345 O  O   . HOH G .   ? 0.3278 0.1819 0.3402 0.1152  -0.0474 0.0197  374 HOH A O   
2346 O  O   . HOH G .   ? 0.2767 0.4121 0.1627 -0.0926 -0.0760 0.0309  375 HOH A O   
2347 O  O   . HOH G .   ? 0.2212 0.2187 0.2192 -0.0031 0.0060  0.0711  376 HOH A O   
2348 O  O   . HOH G .   ? 0.2831 0.2029 0.1392 -0.0157 -0.0212 -0.0421 377 HOH A O   
2349 O  O   . HOH G .   ? 0.2775 0.2031 0.2713 0.0441  -0.1659 -0.0027 378 HOH A O   
2350 O  O   . HOH G .   ? 0.2502 0.2246 0.2678 -0.0283 -0.0377 0.0452  379 HOH A O   
2351 O  O   . HOH G .   ? 0.2519 0.1948 0.1846 0.0001  -0.0489 0.0125  380 HOH A O   
2352 O  O   . HOH G .   ? 0.2904 0.2099 0.1609 -0.0074 -0.0753 -0.0146 381 HOH A O   
2353 O  O   . HOH G .   ? 0.2477 0.1794 0.2351 -0.0636 -0.0571 -0.0037 382 HOH A O   
2354 O  O   . HOH G .   ? 0.3335 0.1647 0.1791 0.0412  -0.0480 -0.0195 383 HOH A O   
2355 O  O   . HOH G .   ? 0.3823 0.1776 0.1961 -0.0703 0.0099  0.0538  384 HOH A O   
2356 O  O   . HOH G .   ? 0.3245 0.2255 0.2693 0.0303  0.1128  -0.0292 385 HOH A O   
2357 O  O   . HOH G .   ? 0.1342 0.3867 0.2183 0.0198  0.0020  0.1172  386 HOH A O   
2358 O  O   . HOH G .   ? 0.0962 0.3023 0.3449 -0.0485 -0.0142 -0.0094 387 HOH A O   
2359 O  O   . HOH G .   ? 0.2714 0.2196 0.2592 0.0060  0.0342  -0.0114 388 HOH A O   
2360 O  O   . HOH G .   ? 0.3083 0.2531 0.2240 -0.0725 0.0612  -0.0992 389 HOH A O   
2361 O  O   . HOH G .   ? 0.2770 0.2520 0.2964 -0.0491 0.0604  -0.0894 390 HOH A O   
2362 O  O   . HOH G .   ? 0.2840 0.2621 0.3285 -0.0230 -0.0610 0.0008  391 HOH A O   
2363 O  O   . HOH G .   ? 0.2578 0.2753 0.3679 0.1292  -0.0346 0.0119  392 HOH A O   
2364 O  O   . HOH G .   ? 0.2460 0.4297 0.2121 -0.0138 -0.0533 0.0197  393 HOH A O   
2365 O  O   . HOH G .   ? 0.1743 0.1802 0.2122 -0.0289 -0.0509 -0.0109 394 HOH A O   
2366 O  O   . HOH G .   ? 0.3058 0.1813 0.2637 -0.0307 -0.0637 -0.0395 395 HOH A O   
2367 O  O   . HOH G .   ? 0.2117 0.1691 0.2453 0.0222  -0.0588 0.0190  396 HOH A O   
2368 O  O   . HOH G .   ? 0.1866 0.3052 0.1779 -0.0186 -0.0046 -0.0496 397 HOH A O   
2369 O  O   . HOH G .   ? 0.1314 0.4731 0.1187 -0.0300 0.0428  0.0197  398 HOH A O   
2370 O  O   . HOH G .   ? 0.3899 0.1700 0.2534 0.0410  0.0040  0.0560  399 HOH A O   
2371 O  O   . HOH G .   ? 0.3134 0.1576 0.2431 -0.0179 -0.0346 -0.0178 400 HOH A O   
2372 O  O   . HOH G .   ? 0.2469 0.2428 0.2849 -0.0027 0.0063  -0.0439 401 HOH A O   
2373 O  O   . HOH G .   ? 0.3238 0.1921 0.1318 -0.0395 0.0606  0.0130  402 HOH A O   
2374 O  O   . HOH G .   ? 0.2079 0.2186 0.2201 -0.0046 -0.0573 0.0066  403 HOH A O   
2375 O  O   . HOH G .   ? 0.4754 0.3001 0.1169 0.0125  0.0245  -0.0186 404 HOH A O   
2376 O  O   . HOH G .   ? 0.2505 0.1715 0.2572 0.0344  -0.0731 -0.0368 405 HOH A O   
2377 O  O   . HOH G .   ? 0.3319 0.2554 0.1981 -0.0193 0.0401  -0.0557 406 HOH A O   
2378 O  O   . HOH G .   ? 0.2040 0.2874 0.2373 -0.0170 0.0326  -0.0264 407 HOH A O   
2379 O  O   . HOH G .   ? 0.1508 0.2135 0.3876 0.0750  -0.0164 -0.0342 408 HOH A O   
2380 O  O   . HOH G .   ? 0.2187 0.2908 0.3113 -0.0110 -0.1022 0.1631  409 HOH A O   
2381 O  O   . HOH G .   ? 0.2906 0.2045 0.1931 -0.0219 -0.0281 0.0115  410 HOH A O   
2382 O  O   . HOH G .   ? 0.2222 0.3941 0.2633 0.0110  0.0054  -0.0148 411 HOH A O   
2383 O  O   . HOH G .   ? 0.3763 0.3544 0.2089 -0.0825 -0.0088 0.0255  412 HOH A O   
2384 O  O   . HOH G .   ? 0.3037 0.4271 0.2056 0.0286  0.0386  0.0189  413 HOH A O   
2385 O  O   . HOH G .   ? 0.1178 0.2308 0.3885 0.0434  0.0641  0.0450  414 HOH A O   
2386 O  O   . HOH G .   ? 0.2646 0.1162 0.1827 0.0245  -0.0199 0.0324  415 HOH A O   
2387 O  O   . HOH G .   ? 0.2359 0.2756 0.2387 0.0077  0.0416  -0.0253 416 HOH A O   
2388 O  O   . HOH G .   ? 0.2649 0.3227 0.3580 0.0171  -0.0711 -0.0076 417 HOH A O   
2389 O  O   . HOH G .   ? 0.2494 0.3492 0.2527 0.0436  -0.0252 -0.0292 418 HOH A O   
2390 O  O   . HOH G .   ? 0.2021 0.2840 0.3998 0.0111  0.0538  0.0683  419 HOH A O   
2391 O  O   . HOH G .   ? 0.4494 0.2323 0.2435 0.0126  0.0195  0.0108  420 HOH A O   
2392 O  O   . HOH G .   ? 0.1774 0.2506 0.3695 0.0649  -0.0197 0.0043  421 HOH A O   
2393 O  O   . HOH G .   ? 0.2897 0.2025 0.3840 0.0155  0.0104  0.1084  422 HOH A O   
2394 O  O   . HOH G .   ? 0.2103 0.2793 0.2764 0.0166  0.1076  0.0048  423 HOH A O   
2395 O  O   . HOH G .   ? 0.3045 0.2431 0.1899 -0.1337 -0.0467 -0.0032 424 HOH A O   
2396 O  O   . HOH G .   ? 0.2538 0.3176 0.1970 -0.0474 0.0217  0.0175  425 HOH A O   
2397 O  O   . HOH G .   ? 0.3163 0.3027 0.2552 -0.0055 -0.0242 -0.0001 426 HOH A O   
2398 O  O   . HOH G .   ? 0.2694 0.2712 0.3797 -0.0179 -0.0088 0.0220  427 HOH A O   
2399 O  O   . HOH G .   ? 0.2135 0.3005 0.3544 -0.0768 -0.0568 -0.0900 428 HOH A O   
2400 O  O   . HOH G .   ? 0.2942 0.2870 0.2688 -0.0460 -0.0131 0.0675  429 HOH A O   
2401 O  O   . HOH G .   ? 0.2182 0.1705 0.2911 -0.0017 0.0098  -0.0491 430 HOH A O   
2402 O  O   . HOH G .   ? 0.5548 0.4314 0.2598 0.1075  -0.1142 -0.0282 431 HOH A O   
2403 O  O   . HOH G .   ? 0.4201 0.3788 0.1740 0.0147  0.0209  -0.1296 432 HOH A O   
2404 O  O   . HOH G .   ? 0.3097 0.4411 0.2793 -0.0115 0.0122  -0.0313 433 HOH A O   
2405 O  O   . HOH G .   ? 0.3427 0.3986 0.2779 0.0063  -0.0417 0.0560  434 HOH A O   
2406 O  O   . HOH G .   ? 0.3795 0.3300 0.2961 -0.0755 0.0006  -0.0489 435 HOH A O   
2407 O  O   . HOH G .   ? 0.2320 0.4049 0.2879 0.0271  -0.0303 0.0850  436 HOH A O   
2408 O  O   . HOH G .   ? 0.3314 0.5018 0.2381 0.0732  -0.0193 0.0010  437 HOH A O   
2409 O  O   . HOH G .   ? 0.3992 0.3246 0.2633 -0.0661 0.0526  0.0894  438 HOH A O   
2410 O  O   . HOH G .   ? 0.4465 0.2474 0.2264 -0.0690 -0.0373 -0.0491 439 HOH A O   
2411 O  O   . HOH G .   ? 0.1974 0.2373 0.2789 0.0292  0.0003  0.0021  440 HOH A O   
2412 O  O   . HOH G .   ? 0.4718 0.3813 0.3560 -0.0496 0.0057  -0.0601 441 HOH A O   
2413 O  O   . HOH G .   ? 0.1974 0.2900 0.3414 -0.0308 0.0199  0.0146  442 HOH A O   
2414 O  O   . HOH G .   ? 0.4137 0.2563 0.2300 0.0487  -0.0359 -0.1316 443 HOH A O   
2415 O  O   . HOH G .   ? 0.4056 0.3034 0.3120 0.0538  -0.0776 0.0026  444 HOH A O   
2416 O  O   . HOH G .   ? 0.3105 0.2577 0.3884 -0.0243 -0.0364 0.0661  445 HOH A O   
2417 O  O   . HOH G .   ? 0.3027 0.2896 0.2808 0.0059  -0.0710 0.0057  446 HOH A O   
2418 O  O   . HOH G .   ? 0.4004 0.2110 0.2473 0.0680  -0.0710 0.0200  447 HOH A O   
2419 O  O   . HOH G .   ? 0.3352 0.2334 0.3571 -0.0357 0.0559  -0.0366 448 HOH A O   
2420 O  O   . HOH G .   ? 0.2244 0.3051 0.3062 0.0278  -0.0463 -0.0509 449 HOH A O   
2421 O  O   . HOH G .   ? 0.2473 0.3195 0.2605 -0.1067 0.0557  -0.0820 450 HOH A O   
2422 O  O   . HOH G .   ? 0.2520 0.2049 0.2703 -0.0237 0.0384  -0.0131 451 HOH A O   
2423 O  O   . HOH G .   ? 0.4957 0.3209 0.3543 0.0741  0.0274  -0.0425 452 HOH A O   
2424 O  O   . HOH G .   ? 0.2050 0.2845 0.2114 -0.0243 -0.0690 0.0161  453 HOH A O   
2425 O  O   . HOH G .   ? 0.3598 0.2410 0.4142 -0.0414 -0.0120 0.0846  454 HOH A O   
2426 O  O   . HOH G .   ? 0.2614 0.2649 0.2911 -0.0593 0.0403  -0.0138 455 HOH A O   
2427 O  O   . HOH G .   ? 0.4384 0.3622 0.4178 0.0628  -0.0555 0.0454  456 HOH A O   
2428 O  O   . HOH G .   ? 0.1237 0.0860 0.1142 0.0234  -0.0080 -0.0038 457 HOH A O   
2429 O  O   . HOH G .   ? 0.3842 0.5194 0.4103 -0.0952 0.0480  0.0579  458 HOH A O   
2430 O  O   . HOH G .   ? 0.5261 0.2713 0.2297 -0.0034 -0.0192 0.0718  459 HOH A O   
2431 O  O   . HOH G .   ? 0.4305 0.2451 0.3580 0.0913  -0.0584 -0.0073 460 HOH A O   
2432 O  O   . HOH G .   ? 0.5838 0.2617 0.1305 0.0041  0.0051  0.0551  461 HOH A O   
2433 O  O   . HOH G .   ? 0.2904 0.3127 0.4295 0.0795  -0.0185 0.0110  462 HOH A O   
2434 O  O   . HOH G .   ? 0.5171 0.2434 0.2319 0.1243  0.0174  0.0137  463 HOH A O   
2435 O  O   . HOH G .   ? 0.3352 0.2232 0.2313 -0.0298 -0.1014 -0.0615 464 HOH A O   
2436 O  O   . HOH G .   ? 0.4142 0.2036 0.2620 0.0644  0.0055  0.0243  465 HOH A O   
2437 O  O   . HOH G .   ? 0.2919 0.2730 0.2925 0.0164  -0.0299 0.0167  466 HOH A O   
2438 O  O   . HOH G .   ? 0.2802 0.2280 0.2775 -0.0322 0.0091  0.0784  467 HOH A O   
2439 O  O   . HOH G .   ? 0.2465 0.3864 0.3634 -0.0820 0.0980  -0.0289 468 HOH A O   
2440 O  O   . HOH G .   ? 0.4047 0.2581 0.2574 -0.0010 0.0165  0.0121  469 HOH A O   
2441 O  O   . HOH G .   ? 0.2387 0.3062 0.4460 -0.1488 -0.0476 0.0205  470 HOH A O   
2442 O  O   . HOH G .   ? 0.3307 0.3029 0.2796 0.0200  0.0131  -0.0450 471 HOH A O   
2443 O  O   . HOH G .   ? 0.2462 0.2822 0.3298 -0.0281 0.0226  -0.0632 472 HOH A O   
2444 O  O   . HOH G .   ? 0.3637 0.2002 0.4528 0.0226  0.0390  0.0520  473 HOH A O   
2445 O  O   . HOH G .   ? 0.4099 0.2092 0.2797 0.0013  0.0013  -0.0498 474 HOH A O   
2446 O  O   . HOH G .   ? 0.2908 0.2094 0.4059 0.0082  0.0027  -0.0666 475 HOH A O   
2447 O  O   . HOH G .   ? 0.2558 0.2688 0.2444 -0.0153 -0.0590 0.0062  476 HOH A O   
2448 O  O   . HOH G .   ? 0.5235 0.2164 0.1396 -0.0212 0.0098  -0.0091 477 HOH A O   
2449 O  O   . HOH G .   ? 0.2976 0.5012 0.2968 0.0057  0.0274  0.1164  478 HOH A O   
2450 O  O   . HOH G .   ? 0.2833 0.2581 0.4449 0.0010  0.0857  -0.0223 479 HOH A O   
2451 O  O   . HOH G .   ? 0.2506 0.2322 0.3382 0.0217  -0.0131 0.0000  480 HOH A O   
2452 O  O   . HOH G .   ? 0.2641 0.1941 0.3088 0.0178  -0.0529 -0.0003 481 HOH A O   
2453 O  O   . HOH G .   ? 0.3360 0.3093 0.4668 0.0331  -0.0104 0.0020  482 HOH A O   
2454 O  O   . HOH G .   ? 0.3059 0.3219 0.3264 -0.0564 -0.0201 -0.0540 483 HOH A O   
2455 O  O   . HOH G .   ? 0.2390 0.3963 0.4717 -0.0516 0.0260  0.0167  484 HOH A O   
2456 O  O   . HOH G .   ? 0.4552 0.4290 0.4711 -0.0500 0.0520  -0.0102 485 HOH A O   
2457 O  O   . HOH G .   ? 0.4356 0.3328 0.2839 0.0458  0.1006  0.1195  486 HOH A O   
2458 O  O   . HOH G .   ? 0.2962 0.4442 0.2808 0.0164  -0.0149 0.0003  487 HOH A O   
2459 O  O   . HOH G .   ? 0.2142 0.4374 0.4215 -0.0142 0.0903  0.0684  488 HOH A O   
2460 O  O   . HOH G .   ? 0.4219 0.3630 0.1982 -0.0103 0.0405  0.0544  489 HOH A O   
2461 O  O   . HOH G .   ? 0.3973 0.2319 0.5475 0.0197  0.0738  0.0469  490 HOH A O   
2462 O  O   . HOH G .   ? 0.3923 0.2991 0.4237 0.0329  0.0291  -0.1138 491 HOH A O   
2463 O  O   . HOH G .   ? 0.4257 0.4973 0.4361 -0.0267 0.0193  -0.0243 492 HOH A O   
2464 O  O   . HOH G .   ? 0.2541 0.3713 0.3551 0.0711  0.1280  0.0353  493 HOH A O   
2465 O  O   . HOH G .   ? 0.1918 0.3537 0.4539 0.0697  0.0017  0.0544  494 HOH A O   
2466 O  O   . HOH G .   ? 0.1910 0.3379 0.3411 0.0408  0.0227  0.0318  495 HOH A O   
2467 O  O   . HOH G .   ? 0.2132 0.2513 0.4599 -0.0212 0.0060  -0.0377 496 HOH A O   
2468 O  O   . HOH G .   ? 0.3364 0.4067 0.2890 -0.0175 0.0124  0.0059  497 HOH A O   
2469 O  O   . HOH G .   ? 0.4452 0.3813 0.2705 0.0513  0.1208  0.0496  498 HOH A O   
2470 O  O   . HOH G .   ? 0.3600 0.1880 0.2757 0.0086  0.1369  0.0163  499 HOH A O   
2471 O  O   . HOH G .   ? 0.3091 0.2370 0.3386 -0.0247 -0.0381 -0.0283 500 HOH A O   
2472 O  O   . HOH G .   ? 0.2478 0.5123 0.3030 -0.0491 -0.0089 0.0156  501 HOH A O   
2473 O  O   . HOH G .   ? 0.3397 0.3883 0.3497 0.0546  0.0173  0.0434  502 HOH A O   
2474 O  O   . HOH G .   ? 0.2657 0.3090 0.2118 -0.0320 0.0227  -0.0208 503 HOH A O   
2475 O  O   . HOH G .   ? 0.2649 0.2764 0.4665 0.0584  -0.0296 0.0229  504 HOH A O   
2476 O  O   . HOH G .   ? 0.3359 0.3343 0.4348 -0.0711 -0.0992 0.0331  505 HOH A O   
2477 O  O   . HOH G .   ? 0.4334 0.4707 0.5236 -0.0052 -0.0568 -0.0266 506 HOH A O   
2478 O  O   . HOH G .   ? 0.5245 0.2949 0.3443 0.0038  0.0804  -0.0878 507 HOH A O   
2479 O  O   . HOH G .   ? 0.4126 0.2577 0.2079 0.0256  -0.0577 0.0724  508 HOH A O   
2480 O  O   . HOH G .   ? 0.3422 0.3896 0.2635 -0.0544 -0.0627 0.0750  509 HOH A O   
2481 O  O   . HOH G .   ? 0.3651 0.3662 0.3371 -0.0355 -0.0307 0.0131  510 HOH A O   
2482 O  O   . HOH G .   ? 0.3136 0.2875 0.3853 0.0346  0.0540  0.0408  511 HOH A O   
2483 O  O   . HOH G .   ? 0.2419 0.3145 0.4611 0.0222  0.0904  -0.0421 512 HOH A O   
2484 O  O   . HOH G .   ? 0.2312 0.3934 0.5332 -0.0728 -0.1028 -0.0436 513 HOH A O   
2485 O  O   . HOH G .   ? 0.3440 0.3003 0.2696 0.0113  0.0195  0.0463  514 HOH A O   
2486 O  O   . HOH G .   ? 0.5450 0.2926 0.3233 0.0015  -0.0130 -0.0588 515 HOH A O   
2487 O  O   . HOH G .   ? 0.2408 0.4180 0.3129 -0.0500 -0.0074 0.0093  516 HOH A O   
2488 O  O   . HOH G .   ? 0.3666 0.5250 0.2462 0.0309  0.0729  0.0175  517 HOH A O   
2489 O  O   . HOH G .   ? 0.2524 0.3729 0.4977 0.0326  0.0524  -0.0186 518 HOH A O   
2490 O  O   . HOH G .   ? 0.2415 0.3671 0.4957 -0.0331 -0.1206 -0.0560 519 HOH A O   
2491 O  O   . HOH G .   ? 0.5350 0.3334 0.2144 -0.0355 0.0027  -0.0991 520 HOH A O   
2492 O  O   . HOH G .   ? 0.2175 0.1752 0.6216 -0.0438 0.0662  0.0581  521 HOH A O   
2493 O  O   . HOH G .   ? 0.4239 0.3701 0.4108 -0.0368 -0.0248 0.0348  522 HOH A O   
2494 O  O   . HOH G .   ? 0.4564 0.5126 0.5102 -0.0504 -0.0102 -0.0322 523 HOH A O   
2495 O  O   . HOH G .   ? 0.3007 0.3120 0.4265 -0.0649 -0.0210 -0.0342 524 HOH A O   
2496 O  O   . HOH G .   ? 0.4348 0.2097 0.3003 -0.0190 -0.0215 -0.0068 525 HOH A O   
2497 O  O   . HOH G .   ? 0.3537 0.2501 0.5151 0.0577  -0.0046 0.0103  526 HOH A O   
2498 O  O   . HOH G .   ? 0.5063 0.3935 0.2506 0.0124  -0.0207 0.0189  527 HOH A O   
2499 O  O   . HOH G .   ? 0.4162 0.4381 0.3464 0.0078  -0.0008 -0.0366 528 HOH A O   
2500 O  O   . HOH G .   ? 0.3393 0.3858 0.3177 -0.0357 -0.0276 0.0141  529 HOH A O   
2501 O  O   . HOH G .   ? 0.4611 0.4089 0.3953 0.0046  -0.0003 0.0388  530 HOH A O   
2502 O  O   . HOH G .   ? 0.3768 0.2851 0.2287 0.0776  -0.0010 -0.0227 531 HOH A O   
2503 O  O   . HOH G .   ? 0.2919 0.3206 0.2603 0.0339  0.1098  -0.0253 532 HOH A O   
2504 O  O   . HOH G .   ? 0.3203 0.2208 0.3162 0.0000  -0.0390 -0.0082 533 HOH A O   
2505 O  O   . HOH G .   ? 0.3594 0.1767 0.4667 -0.0912 -0.0483 0.0055  534 HOH A O   
2506 O  O   . HOH G .   ? 0.4394 0.2725 0.3957 0.0113  -0.1325 0.0637  535 HOH A O   
2507 O  O   . HOH G .   ? 0.2821 0.2886 0.4040 -0.0939 -0.0028 -0.0759 536 HOH A O   
2508 O  O   . HOH G .   ? 0.5601 0.3611 0.3612 -0.0834 0.0324  0.0274  537 HOH A O   
2509 O  O   . HOH G .   ? 0.5241 0.2252 0.4731 -0.0819 -0.0671 -0.0283 538 HOH A O   
2510 O  O   . HOH G .   ? 0.4081 0.2460 0.4311 -0.0130 0.0071  0.0803  539 HOH A O   
2511 O  O   . HOH G .   ? 0.3661 0.3197 0.4180 0.0386  0.0366  0.0162  540 HOH A O   
2512 O  O   . HOH G .   ? 0.4909 0.2402 0.3691 -0.0076 -0.0118 0.0129  541 HOH A O   
2513 O  O   . HOH G .   ? 0.3920 0.3676 0.3560 -0.0467 -0.0592 -0.1178 542 HOH A O   
2514 O  O   . HOH G .   ? 0.1206 0.5853 0.3910 0.0254  0.0093  -0.1545 543 HOH A O   
2515 O  O   . HOH G .   ? 0.3504 0.2072 0.4190 0.0285  -0.0791 0.0357  544 HOH A O   
2516 O  O   . HOH G .   ? 0.2415 0.2338 0.2682 -0.0661 0.0176  0.0697  545 HOH A O   
2517 O  O   . HOH G .   ? 0.2133 0.2061 0.4415 0.0603  0.1142  0.1376  546 HOH A O   
2518 O  O   . HOH G .   ? 0.3270 0.4237 0.3658 -0.0478 0.0210  -0.0285 547 HOH A O   
2519 O  O   . HOH G .   ? 0.3810 0.3112 0.3544 0.0430  -0.1368 0.0619  548 HOH A O   
2520 O  O   . HOH G .   ? 0.3511 0.3949 0.5034 0.0368  0.1102  -0.0153 549 HOH A O   
2521 O  O   . HOH G .   ? 0.2980 0.3701 0.5126 0.0782  0.0359  0.0198  550 HOH A O   
2522 O  O   . HOH G .   ? 0.3052 0.3607 0.3495 0.0021  0.0469  -0.0342 551 HOH A O   
2523 O  O   . HOH G .   ? 0.2813 0.4646 0.3367 0.0071  -0.0289 0.0775  552 HOH A O   
2524 O  O   . HOH G .   ? 0.4392 0.5048 0.3777 0.0118  0.0993  0.0108  553 HOH A O   
2525 O  O   . HOH G .   ? 0.2358 0.3368 0.5159 -0.0476 -0.0608 0.0953  554 HOH A O   
2526 O  O   . HOH G .   ? 0.2574 0.3654 0.4247 0.0216  -0.0148 0.0364  555 HOH A O   
2527 O  O   . HOH G .   ? 0.2933 0.3450 0.5199 -0.0676 -0.0130 0.0027  556 HOH A O   
2528 O  O   . HOH G .   ? 0.4345 0.5037 0.2782 -0.0324 0.0031  0.0362  557 HOH A O   
2529 O  O   . HOH G .   ? 0.4632 0.4405 0.2391 0.0131  0.0306  0.0706  558 HOH A O   
2530 O  O   . HOH G .   ? 0.3291 0.4298 0.5468 0.1275  -0.0068 0.0035  559 HOH A O   
2531 O  O   . HOH G .   ? 0.3980 0.2538 0.3932 0.0548  0.1140  0.0274  560 HOH A O   
2532 O  O   . HOH G .   ? 0.2886 0.2347 0.5741 -0.0524 0.0337  0.0568  561 HOH A O   
2533 O  O   . HOH G .   ? 0.4093 0.4491 0.4068 -0.0007 -0.0285 0.0425  562 HOH A O   
2534 O  O   . HOH G .   ? 0.3143 0.3488 0.4036 0.0186  -0.1186 0.0178  563 HOH A O   
2535 O  O   . HOH G .   ? 0.1805 0.2710 0.3564 -0.0015 -0.0241 0.0197  564 HOH A O   
2536 O  O   . HOH G .   ? 0.3442 0.2969 0.3343 0.1360  0.0516  0.0472  565 HOH A O   
2537 O  O   . HOH G .   ? 0.3404 0.4695 0.4743 0.1151  0.0584  0.0329  566 HOH A O   
2538 O  O   . HOH G .   ? 0.4595 0.4598 0.4361 -0.0010 0.0000  0.0147  567 HOH A O   
2539 O  O   . HOH G .   ? 0.3600 0.4390 0.3971 -0.1013 -0.1354 -0.0859 568 HOH A O   
2540 O  O   . HOH G .   ? 0.5137 0.2851 0.4348 -0.0170 -0.0680 -0.0976 569 HOH A O   
2541 O  O   . HOH G .   ? 0.3429 0.4542 0.4490 0.0386  0.0542  0.0148  570 HOH A O   
2542 O  O   . HOH G .   ? 0.5976 0.3334 0.3481 0.0080  -0.0037 0.0763  571 HOH A O   
2543 O  O   . HOH G .   ? 0.3102 0.5022 0.4219 -0.0275 -0.0060 0.0281  572 HOH A O   
2544 O  O   . HOH G .   ? 0.4247 0.3767 0.2800 0.0763  0.0320  0.0811  573 HOH A O   
2545 O  O   . HOH G .   ? 0.3785 0.4453 0.3658 -0.0878 -0.0408 0.0773  574 HOH A O   
2546 O  O   . HOH G .   ? 0.3407 0.4470 0.2822 0.1115  -0.0052 0.0694  575 HOH A O   
2547 O  O   . HOH G .   ? 0.4847 0.3580 0.4151 0.0113  -0.1220 0.0403  576 HOH A O   
2548 O  O   . HOH G .   ? 0.5260 0.4739 0.4585 0.0650  -0.0520 0.0132  577 HOH A O   
2549 O  O   . HOH G .   ? 0.3607 0.2922 0.4183 0.0416  0.0207  -0.0860 578 HOH A O   
2550 O  O   . HOH G .   ? 0.3853 0.5109 0.2183 0.0065  0.1005  0.0129  579 HOH A O   
2551 O  O   . HOH G .   ? 0.3551 0.2940 0.4779 -0.0813 -0.1133 0.0386  580 HOH A O   
2552 O  O   . HOH G .   ? 0.4463 0.3797 0.5774 0.0342  0.0098  -0.0038 581 HOH A O   
2553 O  O   . HOH G .   ? 0.3938 0.3991 0.3864 -0.0038 0.0010  -0.0791 582 HOH A O   
2554 O  O   . HOH G .   ? 0.5349 0.5852 0.3963 0.0236  -0.0167 -0.0344 583 HOH A O   
2555 O  O   . HOH G .   ? 0.4020 0.4733 0.3844 -0.0217 -0.0476 -0.0322 584 HOH A O   
2556 O  O   . HOH G .   ? 0.3377 0.3080 0.4284 -0.0087 -0.0619 0.0318  585 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 DMS 1   263 1   DMS DMS A . 
D 3 DMS 1   264 2   DMS DMS A . 
E 4 BCN 1   265 1   BCN BCN A . 
F 5 E90 1   266 1   E90 E90 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 1   HOH HOH A . 
G 6 HOH 57  322 2   HOH HOH A . 
G 6 HOH 58  323 3   HOH HOH A . 
G 6 HOH 59  324 4   HOH HOH A . 
G 6 HOH 60  325 5   HOH HOH A . 
G 6 HOH 61  326 6   HOH HOH A . 
G 6 HOH 62  327 7   HOH HOH A . 
G 6 HOH 63  328 8   HOH HOH A . 
G 6 HOH 64  329 9   HOH HOH A . 
G 6 HOH 65  330 10  HOH HOH A . 
G 6 HOH 66  331 11  HOH HOH A . 
G 6 HOH 67  332 12  HOH HOH A . 
G 6 HOH 68  333 13  HOH HOH A . 
G 6 HOH 69  334 14  HOH HOH A . 
G 6 HOH 70  335 15  HOH HOH A . 
G 6 HOH 71  336 16  HOH HOH A . 
G 6 HOH 72  337 17  HOH HOH A . 
G 6 HOH 73  338 18  HOH HOH A . 
G 6 HOH 74  339 19  HOH HOH A . 
G 6 HOH 75  340 20  HOH HOH A . 
G 6 HOH 76  341 21  HOH HOH A . 
G 6 HOH 77  342 22  HOH HOH A . 
G 6 HOH 78  343 23  HOH HOH A . 
G 6 HOH 79  344 24  HOH HOH A . 
G 6 HOH 80  345 25  HOH HOH A . 
G 6 HOH 81  346 26  HOH HOH A . 
G 6 HOH 82  347 27  HOH HOH A . 
G 6 HOH 83  348 28  HOH HOH A . 
G 6 HOH 84  349 29  HOH HOH A . 
G 6 HOH 85  350 30  HOH HOH A . 
G 6 HOH 86  351 31  HOH HOH A . 
G 6 HOH 87  352 32  HOH HOH A . 
G 6 HOH 88  353 33  HOH HOH A . 
G 6 HOH 89  354 34  HOH HOH A . 
G 6 HOH 90  355 35  HOH HOH A . 
G 6 HOH 91  356 36  HOH HOH A . 
G 6 HOH 92  357 37  HOH HOH A . 
G 6 HOH 93  358 38  HOH HOH A . 
G 6 HOH 94  359 39  HOH HOH A . 
G 6 HOH 95  360 40  HOH HOH A . 
G 6 HOH 96  361 41  HOH HOH A . 
G 6 HOH 97  362 42  HOH HOH A . 
G 6 HOH 98  363 43  HOH HOH A . 
G 6 HOH 99  364 44  HOH HOH A . 
G 6 HOH 100 365 45  HOH HOH A . 
G 6 HOH 101 366 46  HOH HOH A . 
G 6 HOH 102 367 47  HOH HOH A . 
G 6 HOH 103 368 48  HOH HOH A . 
G 6 HOH 104 369 49  HOH HOH A . 
G 6 HOH 105 370 50  HOH HOH A . 
G 6 HOH 106 371 51  HOH HOH A . 
G 6 HOH 107 372 52  HOH HOH A . 
G 6 HOH 108 373 53  HOH HOH A . 
G 6 HOH 109 374 54  HOH HOH A . 
G 6 HOH 110 375 55  HOH HOH A . 
G 6 HOH 111 376 56  HOH HOH A . 
G 6 HOH 112 377 57  HOH HOH A . 
G 6 HOH 113 378 58  HOH HOH A . 
G 6 HOH 114 379 59  HOH HOH A . 
G 6 HOH 115 380 60  HOH HOH A . 
G 6 HOH 116 381 61  HOH HOH A . 
G 6 HOH 117 382 62  HOH HOH A . 
G 6 HOH 118 383 63  HOH HOH A . 
G 6 HOH 119 384 64  HOH HOH A . 
G 6 HOH 120 385 65  HOH HOH A . 
G 6 HOH 121 386 66  HOH HOH A . 
G 6 HOH 122 387 67  HOH HOH A . 
G 6 HOH 123 388 68  HOH HOH A . 
G 6 HOH 124 389 69  HOH HOH A . 
G 6 HOH 125 390 70  HOH HOH A . 
G 6 HOH 126 391 71  HOH HOH A . 
G 6 HOH 127 392 72  HOH HOH A . 
G 6 HOH 128 393 73  HOH HOH A . 
G 6 HOH 129 394 74  HOH HOH A . 
G 6 HOH 130 395 75  HOH HOH A . 
G 6 HOH 131 396 76  HOH HOH A . 
G 6 HOH 132 397 77  HOH HOH A . 
G 6 HOH 133 398 78  HOH HOH A . 
G 6 HOH 134 399 79  HOH HOH A . 
G 6 HOH 135 400 80  HOH HOH A . 
G 6 HOH 136 401 81  HOH HOH A . 
G 6 HOH 137 402 82  HOH HOH A . 
G 6 HOH 138 403 83  HOH HOH A . 
G 6 HOH 139 404 84  HOH HOH A . 
G 6 HOH 140 405 85  HOH HOH A . 
G 6 HOH 141 406 86  HOH HOH A . 
G 6 HOH 142 407 87  HOH HOH A . 
G 6 HOH 143 408 88  HOH HOH A . 
G 6 HOH 144 409 89  HOH HOH A . 
G 6 HOH 145 410 90  HOH HOH A . 
G 6 HOH 146 411 91  HOH HOH A . 
G 6 HOH 147 412 92  HOH HOH A . 
G 6 HOH 148 413 93  HOH HOH A . 
G 6 HOH 149 414 94  HOH HOH A . 
G 6 HOH 150 415 95  HOH HOH A . 
G 6 HOH 151 416 96  HOH HOH A . 
G 6 HOH 152 417 97  HOH HOH A . 
G 6 HOH 153 418 98  HOH HOH A . 
G 6 HOH 154 419 99  HOH HOH A . 
G 6 HOH 155 420 100 HOH HOH A . 
G 6 HOH 156 421 101 HOH HOH A . 
G 6 HOH 157 422 102 HOH HOH A . 
G 6 HOH 158 423 103 HOH HOH A . 
G 6 HOH 159 424 104 HOH HOH A . 
G 6 HOH 160 425 105 HOH HOH A . 
G 6 HOH 161 426 106 HOH HOH A . 
G 6 HOH 162 427 107 HOH HOH A . 
G 6 HOH 163 428 108 HOH HOH A . 
G 6 HOH 164 429 109 HOH HOH A . 
G 6 HOH 165 430 110 HOH HOH A . 
G 6 HOH 166 431 111 HOH HOH A . 
G 6 HOH 167 432 112 HOH HOH A . 
G 6 HOH 168 433 113 HOH HOH A . 
G 6 HOH 169 434 114 HOH HOH A . 
G 6 HOH 170 435 115 HOH HOH A . 
G 6 HOH 171 436 116 HOH HOH A . 
G 6 HOH 172 437 117 HOH HOH A . 
G 6 HOH 173 438 118 HOH HOH A . 
G 6 HOH 174 439 119 HOH HOH A . 
G 6 HOH 175 440 120 HOH HOH A . 
G 6 HOH 176 441 121 HOH HOH A . 
G 6 HOH 177 442 122 HOH HOH A . 
G 6 HOH 178 443 123 HOH HOH A . 
G 6 HOH 179 444 124 HOH HOH A . 
G 6 HOH 180 445 125 HOH HOH A . 
G 6 HOH 181 446 127 HOH HOH A . 
G 6 HOH 182 447 128 HOH HOH A . 
G 6 HOH 183 448 129 HOH HOH A . 
G 6 HOH 184 449 130 HOH HOH A . 
G 6 HOH 185 450 131 HOH HOH A . 
G 6 HOH 186 451 132 HOH HOH A . 
G 6 HOH 187 452 133 HOH HOH A . 
G 6 HOH 188 453 134 HOH HOH A . 
G 6 HOH 189 454 135 HOH HOH A . 
G 6 HOH 190 455 136 HOH HOH A . 
G 6 HOH 191 456 137 HOH HOH A . 
G 6 HOH 192 457 138 HOH HOH A . 
G 6 HOH 193 458 139 HOH HOH A . 
G 6 HOH 194 459 140 HOH HOH A . 
G 6 HOH 195 460 141 HOH HOH A . 
G 6 HOH 196 461 142 HOH HOH A . 
G 6 HOH 197 462 143 HOH HOH A . 
G 6 HOH 198 463 144 HOH HOH A . 
G 6 HOH 199 464 145 HOH HOH A . 
G 6 HOH 200 465 146 HOH HOH A . 
G 6 HOH 201 466 147 HOH HOH A . 
G 6 HOH 202 467 148 HOH HOH A . 
G 6 HOH 203 468 149 HOH HOH A . 
G 6 HOH 204 469 150 HOH HOH A . 
G 6 HOH 205 470 151 HOH HOH A . 
G 6 HOH 206 471 152 HOH HOH A . 
G 6 HOH 207 472 153 HOH HOH A . 
G 6 HOH 208 473 154 HOH HOH A . 
G 6 HOH 209 474 155 HOH HOH A . 
G 6 HOH 210 475 156 HOH HOH A . 
G 6 HOH 211 476 157 HOH HOH A . 
G 6 HOH 212 477 158 HOH HOH A . 
G 6 HOH 213 478 159 HOH HOH A . 
G 6 HOH 214 479 160 HOH HOH A . 
G 6 HOH 215 480 161 HOH HOH A . 
G 6 HOH 216 481 162 HOH HOH A . 
G 6 HOH 217 482 163 HOH HOH A . 
G 6 HOH 218 483 164 HOH HOH A . 
G 6 HOH 219 484 165 HOH HOH A . 
G 6 HOH 220 485 166 HOH HOH A . 
G 6 HOH 221 486 167 HOH HOH A . 
G 6 HOH 222 487 168 HOH HOH A . 
G 6 HOH 223 488 169 HOH HOH A . 
G 6 HOH 224 489 170 HOH HOH A . 
G 6 HOH 225 490 171 HOH HOH A . 
G 6 HOH 226 491 172 HOH HOH A . 
G 6 HOH 227 492 173 HOH HOH A . 
G 6 HOH 228 493 174 HOH HOH A . 
G 6 HOH 229 494 175 HOH HOH A . 
G 6 HOH 230 495 176 HOH HOH A . 
G 6 HOH 231 496 177 HOH HOH A . 
G 6 HOH 232 497 178 HOH HOH A . 
G 6 HOH 233 498 179 HOH HOH A . 
G 6 HOH 234 499 180 HOH HOH A . 
G 6 HOH 235 500 181 HOH HOH A . 
G 6 HOH 236 501 182 HOH HOH A . 
G 6 HOH 237 502 183 HOH HOH A . 
G 6 HOH 238 503 184 HOH HOH A . 
G 6 HOH 239 504 185 HOH HOH A . 
G 6 HOH 240 505 186 HOH HOH A . 
G 6 HOH 241 506 187 HOH HOH A . 
G 6 HOH 242 507 188 HOH HOH A . 
G 6 HOH 243 508 189 HOH HOH A . 
G 6 HOH 244 509 190 HOH HOH A . 
G 6 HOH 245 510 191 HOH HOH A . 
G 6 HOH 246 511 192 HOH HOH A . 
G 6 HOH 247 512 193 HOH HOH A . 
G 6 HOH 248 513 194 HOH HOH A . 
G 6 HOH 249 514 195 HOH HOH A . 
G 6 HOH 250 515 196 HOH HOH A . 
G 6 HOH 251 516 197 HOH HOH A . 
G 6 HOH 252 517 198 HOH HOH A . 
G 6 HOH 253 518 199 HOH HOH A . 
G 6 HOH 254 519 200 HOH HOH A . 
G 6 HOH 255 520 201 HOH HOH A . 
G 6 HOH 256 521 202 HOH HOH A . 
G 6 HOH 257 522 203 HOH HOH A . 
G 6 HOH 258 523 204 HOH HOH A . 
G 6 HOH 259 524 205 HOH HOH A . 
G 6 HOH 260 525 206 HOH HOH A . 
G 6 HOH 261 526 207 HOH HOH A . 
G 6 HOH 262 527 208 HOH HOH A . 
G 6 HOH 263 528 209 HOH HOH A . 
G 6 HOH 264 529 210 HOH HOH A . 
G 6 HOH 265 530 211 HOH HOH A . 
G 6 HOH 266 531 212 HOH HOH A . 
G 6 HOH 267 532 213 HOH HOH A . 
G 6 HOH 268 533 214 HOH HOH A . 
G 6 HOH 269 534 215 HOH HOH A . 
G 6 HOH 270 535 216 HOH HOH A . 
G 6 HOH 271 536 217 HOH HOH A . 
G 6 HOH 272 537 218 HOH HOH A . 
G 6 HOH 273 538 219 HOH HOH A . 
G 6 HOH 274 539 220 HOH HOH A . 
G 6 HOH 275 540 221 HOH HOH A . 
G 6 HOH 276 541 222 HOH HOH A . 
G 6 HOH 277 542 223 HOH HOH A . 
G 6 HOH 278 543 224 HOH HOH A . 
G 6 HOH 279 544 225 HOH HOH A . 
G 6 HOH 280 545 226 HOH HOH A . 
G 6 HOH 281 546 227 HOH HOH A . 
G 6 HOH 282 547 228 HOH HOH A . 
G 6 HOH 283 548 229 HOH HOH A . 
G 6 HOH 284 549 230 HOH HOH A . 
G 6 HOH 285 550 231 HOH HOH A . 
G 6 HOH 286 551 232 HOH HOH A . 
G 6 HOH 287 552 233 HOH HOH A . 
G 6 HOH 288 553 234 HOH HOH A . 
G 6 HOH 289 554 235 HOH HOH A . 
G 6 HOH 290 555 236 HOH HOH A . 
G 6 HOH 291 556 237 HOH HOH A . 
G 6 HOH 292 557 238 HOH HOH A . 
G 6 HOH 293 558 239 HOH HOH A . 
G 6 HOH 294 559 240 HOH HOH A . 
G 6 HOH 295 560 241 HOH HOH A . 
G 6 HOH 296 561 242 HOH HOH A . 
G 6 HOH 297 562 243 HOH HOH A . 
G 6 HOH 298 563 244 HOH HOH A . 
G 6 HOH 299 564 245 HOH HOH A . 
G 6 HOH 300 565 246 HOH HOH A . 
G 6 HOH 301 566 247 HOH HOH A . 
G 6 HOH 302 567 248 HOH HOH A . 
G 6 HOH 303 568 249 HOH HOH A . 
G 6 HOH 304 569 250 HOH HOH A . 
G 6 HOH 305 570 251 HOH HOH A . 
G 6 HOH 306 571 252 HOH HOH A . 
G 6 HOH 307 572 253 HOH HOH A . 
G 6 HOH 308 573 254 HOH HOH A . 
G 6 HOH 309 574 255 HOH HOH A . 
G 6 HOH 310 575 256 HOH HOH A . 
G 6 HOH 311 576 257 HOH HOH A . 
G 6 HOH 312 577 258 HOH HOH A . 
G 6 HOH 313 578 259 HOH HOH A . 
G 6 HOH 314 579 260 HOH HOH A . 
G 6 HOH 315 580 261 HOH HOH A . 
G 6 HOH 316 581 262 HOH HOH A . 
G 6 HOH 317 582 263 HOH HOH A . 
G 6 HOH 318 583 264 HOH HOH A . 
G 6 HOH 319 584 265 HOH HOH A . 
G 6 HOH 320 585 266 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_555 104.1 ? 
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_555 113.3 ? 
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 98.6  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N20 ? F E90 .   ? A E90 266 ? 1_555 111.5 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N20 ? F E90 .   ? A E90 266 ? 1_555 113.0 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 262 ? 1_555 N20 ? F E90 .   ? A E90 266 ? 1_555 115.1 ? 
# 
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' Advisory                 
3 3 'Structure model' 'Database references'    
4 4 'Structure model' Advisory                 
5 4 'Structure model' 'Data collection'        
6 4 'Structure model' 'Database references'    
7 4 'Structure model' 'Derived calculations'   
8 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  3 'Structure model' pdbx_unobs_or_zero_occ_atoms  
3  4 'Structure model' chem_comp_atom                
4  4 'Structure model' chem_comp_bond                
5  4 'Structure model' database_2                    
6  4 'Structure model' diffrn_source                 
7  4 'Structure model' pdbx_initial_refinement_model 
8  4 'Structure model' pdbx_struct_conn_angle        
9  4 'Structure model' pdbx_unobs_or_zero_occ_atoms  
10 4 'Structure model' struct_conn                   
11 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       3.2.19 22/12/2005      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   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   THR 
_pdbx_validate_close_contact.auth_seq_id_1    37 
_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    308 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
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 HIS A 10  ? B 117.96  -28.07  
2 1 ASN A 11  ? ? -143.04 17.72   
3 1 ARG A 27  ? ? -144.48 57.12   
4 1 ALA A 65  ? ? -160.66 -169.36 
5 1 LYS A 76  ? ? -137.20 -30.62  
6 1 LYS A 111 ? ? 70.09   -0.13   
7 1 PHE A 176 ? ? -151.78 76.12   
8 1 ASN A 244 ? ? -96.58  50.81   
9 1 LYS A 252 ? ? 56.72   -137.92 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 A LYS 9 ? CE A A LYS 9 CE 
2 1 Y 0 A LYS 9 ? NZ A A LYS 9 NZ 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
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 
E90 N1   N  Y N 122 
E90 C2   C  Y N 123 
E90 N3   N  Y N 124 
E90 C4   C  Y N 125 
E90 C5   C  Y N 126 
E90 C6   C  Y N 127 
E90 S7   S  N N 128 
E90 C8   C  N N 129 
E90 C9   C  N N 130 
E90 O10  O  N N 131 
E90 C11  C  Y N 132 
E90 C12  C  Y N 133 
E90 C13  C  Y N 134 
E90 C14  C  Y N 135 
E90 C15  C  Y N 136 
E90 C16  C  Y N 137 
E90 S17  S  N N 138 
E90 O18  O  N N 139 
E90 O19  O  N N 140 
E90 N20  N  N N 141 
E90 H4   H  N N 142 
E90 H5   H  N N 143 
E90 H6   H  N N 144 
E90 H8   H  N N 145 
E90 H8A  H  N N 146 
E90 H12  H  N N 147 
E90 H13  H  N N 148 
E90 H15  H  N N 149 
E90 H16  H  N N 150 
E90 HN20 H  N N 151 
E90 HN2A H  N N 152 
GLN N    N  N N 153 
GLN CA   C  N S 154 
GLN C    C  N N 155 
GLN O    O  N N 156 
GLN CB   C  N N 157 
GLN CG   C  N N 158 
GLN CD   C  N N 159 
GLN OE1  O  N N 160 
GLN NE2  N  N N 161 
GLN OXT  O  N N 162 
GLN H    H  N N 163 
GLN H2   H  N N 164 
GLN HA   H  N N 165 
GLN HB2  H  N N 166 
GLN HB3  H  N N 167 
GLN HG2  H  N N 168 
GLN HG3  H  N N 169 
GLN HE21 H  N N 170 
GLN HE22 H  N N 171 
GLN HXT  H  N N 172 
GLU N    N  N N 173 
GLU CA   C  N S 174 
GLU C    C  N N 175 
GLU O    O  N N 176 
GLU CB   C  N N 177 
GLU CG   C  N N 178 
GLU CD   C  N N 179 
GLU OE1  O  N N 180 
GLU OE2  O  N N 181 
GLU OXT  O  N N 182 
GLU H    H  N N 183 
GLU H2   H  N N 184 
GLU HA   H  N N 185 
GLU HB2  H  N N 186 
GLU HB3  H  N N 187 
GLU HG2  H  N N 188 
GLU HG3  H  N N 189 
GLU HE2  H  N N 190 
GLU HXT  H  N N 191 
GLY N    N  N N 192 
GLY CA   C  N N 193 
GLY C    C  N N 194 
GLY O    O  N N 195 
GLY OXT  O  N N 196 
GLY H    H  N N 197 
GLY H2   H  N N 198 
GLY HA2  H  N N 199 
GLY HA3  H  N N 200 
GLY HXT  H  N N 201 
HIS N    N  N N 202 
HIS CA   C  N S 203 
HIS C    C  N N 204 
HIS O    O  N N 205 
HIS CB   C  N N 206 
HIS CG   C  Y N 207 
HIS ND1  N  Y N 208 
HIS CD2  C  Y N 209 
HIS CE1  C  Y N 210 
HIS NE2  N  Y N 211 
HIS OXT  O  N N 212 
HIS H    H  N N 213 
HIS H2   H  N N 214 
HIS HA   H  N N 215 
HIS HB2  H  N N 216 
HIS HB3  H  N N 217 
HIS HD1  H  N N 218 
HIS HD2  H  N N 219 
HIS HE1  H  N N 220 
HIS HE2  H  N N 221 
HIS HXT  H  N N 222 
HOH O    O  N N 223 
HOH H1   H  N N 224 
HOH H2   H  N N 225 
ILE N    N  N N 226 
ILE CA   C  N S 227 
ILE C    C  N N 228 
ILE O    O  N N 229 
ILE CB   C  N S 230 
ILE CG1  C  N N 231 
ILE CG2  C  N N 232 
ILE CD1  C  N N 233 
ILE OXT  O  N N 234 
ILE H    H  N N 235 
ILE H2   H  N N 236 
ILE HA   H  N N 237 
ILE HB   H  N N 238 
ILE HG12 H  N N 239 
ILE HG13 H  N N 240 
ILE HG21 H  N N 241 
ILE HG22 H  N N 242 
ILE HG23 H  N N 243 
ILE HD11 H  N N 244 
ILE HD12 H  N N 245 
ILE HD13 H  N N 246 
ILE HXT  H  N N 247 
LEU N    N  N N 248 
LEU CA   C  N S 249 
LEU C    C  N N 250 
LEU O    O  N N 251 
LEU CB   C  N N 252 
LEU CG   C  N N 253 
LEU CD1  C  N N 254 
LEU CD2  C  N N 255 
LEU OXT  O  N N 256 
LEU H    H  N N 257 
LEU H2   H  N N 258 
LEU HA   H  N N 259 
LEU HB2  H  N N 260 
LEU HB3  H  N N 261 
LEU HG   H  N N 262 
LEU HD11 H  N N 263 
LEU HD12 H  N N 264 
LEU HD13 H  N N 265 
LEU HD21 H  N N 266 
LEU HD22 H  N N 267 
LEU HD23 H  N N 268 
LEU HXT  H  N N 269 
LYS N    N  N N 270 
LYS CA   C  N S 271 
LYS C    C  N N 272 
LYS O    O  N N 273 
LYS CB   C  N N 274 
LYS CG   C  N N 275 
LYS CD   C  N N 276 
LYS CE   C  N N 277 
LYS NZ   N  N N 278 
LYS OXT  O  N N 279 
LYS H    H  N N 280 
LYS H2   H  N N 281 
LYS HA   H  N N 282 
LYS HB2  H  N N 283 
LYS HB3  H  N N 284 
LYS HG2  H  N N 285 
LYS HG3  H  N N 286 
LYS HD2  H  N N 287 
LYS HD3  H  N N 288 
LYS HE2  H  N N 289 
LYS HE3  H  N N 290 
LYS HZ1  H  N N 291 
LYS HZ2  H  N N 292 
LYS HZ3  H  N N 293 
LYS HXT  H  N N 294 
MET N    N  N N 295 
MET CA   C  N S 296 
MET C    C  N N 297 
MET O    O  N N 298 
MET CB   C  N N 299 
MET CG   C  N N 300 
MET SD   S  N N 301 
MET CE   C  N N 302 
MET OXT  O  N N 303 
MET H    H  N N 304 
MET H2   H  N N 305 
MET HA   H  N N 306 
MET HB2  H  N N 307 
MET HB3  H  N N 308 
MET HG2  H  N N 309 
MET HG3  H  N N 310 
MET HE1  H  N N 311 
MET HE2  H  N N 312 
MET HE3  H  N N 313 
MET HXT  H  N N 314 
PHE N    N  N N 315 
PHE CA   C  N S 316 
PHE C    C  N N 317 
PHE O    O  N N 318 
PHE CB   C  N N 319 
PHE CG   C  Y N 320 
PHE CD1  C  Y N 321 
PHE CD2  C  Y N 322 
PHE CE1  C  Y N 323 
PHE CE2  C  Y N 324 
PHE CZ   C  Y N 325 
PHE OXT  O  N N 326 
PHE H    H  N N 327 
PHE H2   H  N N 328 
PHE HA   H  N N 329 
PHE HB2  H  N N 330 
PHE HB3  H  N N 331 
PHE HD1  H  N N 332 
PHE HD2  H  N N 333 
PHE HE1  H  N N 334 
PHE HE2  H  N N 335 
PHE HZ   H  N N 336 
PHE HXT  H  N N 337 
PRO N    N  N N 338 
PRO CA   C  N S 339 
PRO C    C  N N 340 
PRO O    O  N N 341 
PRO CB   C  N N 342 
PRO CG   C  N N 343 
PRO CD   C  N N 344 
PRO OXT  O  N N 345 
PRO H    H  N N 346 
PRO HA   H  N N 347 
PRO HB2  H  N N 348 
PRO HB3  H  N N 349 
PRO HG2  H  N N 350 
PRO HG3  H  N N 351 
PRO HD2  H  N N 352 
PRO HD3  H  N N 353 
PRO HXT  H  N N 354 
SER N    N  N N 355 
SER CA   C  N S 356 
SER C    C  N N 357 
SER O    O  N N 358 
SER CB   C  N N 359 
SER OG   O  N N 360 
SER OXT  O  N N 361 
SER H    H  N N 362 
SER H2   H  N N 363 
SER HA   H  N N 364 
SER HB2  H  N N 365 
SER HB3  H  N N 366 
SER HG   H  N N 367 
SER HXT  H  N N 368 
THR N    N  N N 369 
THR CA   C  N S 370 
THR C    C  N N 371 
THR O    O  N N 372 
THR CB   C  N R 373 
THR OG1  O  N N 374 
THR CG2  C  N N 375 
THR OXT  O  N N 376 
THR H    H  N N 377 
THR H2   H  N N 378 
THR HA   H  N N 379 
THR HB   H  N N 380 
THR HG1  H  N N 381 
THR HG21 H  N N 382 
THR HG22 H  N N 383 
THR HG23 H  N N 384 
THR HXT  H  N N 385 
TRP N    N  N N 386 
TRP CA   C  N S 387 
TRP C    C  N N 388 
TRP O    O  N N 389 
TRP CB   C  N N 390 
TRP CG   C  Y N 391 
TRP CD1  C  Y N 392 
TRP CD2  C  Y N 393 
TRP NE1  N  Y N 394 
TRP CE2  C  Y N 395 
TRP CE3  C  Y N 396 
TRP CZ2  C  Y N 397 
TRP CZ3  C  Y N 398 
TRP CH2  C  Y N 399 
TRP OXT  O  N N 400 
TRP H    H  N N 401 
TRP H2   H  N N 402 
TRP HA   H  N N 403 
TRP HB2  H  N N 404 
TRP HB3  H  N N 405 
TRP HD1  H  N N 406 
TRP HE1  H  N N 407 
TRP HE3  H  N N 408 
TRP HZ2  H  N N 409 
TRP HZ3  H  N N 410 
TRP HH2  H  N N 411 
TRP HXT  H  N N 412 
TYR N    N  N N 413 
TYR CA   C  N S 414 
TYR C    C  N N 415 
TYR O    O  N N 416 
TYR CB   C  N N 417 
TYR CG   C  Y N 418 
TYR CD1  C  Y N 419 
TYR CD2  C  Y N 420 
TYR CE1  C  Y N 421 
TYR CE2  C  Y N 422 
TYR CZ   C  Y N 423 
TYR OH   O  N N 424 
TYR OXT  O  N N 425 
TYR H    H  N N 426 
TYR H2   H  N N 427 
TYR HA   H  N N 428 
TYR HB2  H  N N 429 
TYR HB3  H  N N 430 
TYR HD1  H  N N 431 
TYR HD2  H  N N 432 
TYR HE1  H  N N 433 
TYR HE2  H  N N 434 
TYR HH   H  N N 435 
TYR HXT  H  N N 436 
VAL N    N  N N 437 
VAL CA   C  N S 438 
VAL C    C  N N 439 
VAL O    O  N N 440 
VAL CB   C  N N 441 
VAL CG1  C  N N 442 
VAL CG2  C  N N 443 
VAL OXT  O  N N 444 
VAL H    H  N N 445 
VAL H2   H  N N 446 
VAL HA   H  N N 447 
VAL HB   H  N N 448 
VAL HG11 H  N N 449 
VAL HG12 H  N N 450 
VAL HG13 H  N N 451 
VAL HG21 H  N N 452 
VAL HG22 H  N N 453 
VAL HG23 H  N N 454 
VAL HXT  H  N N 455 
ZN  ZN   ZN N N 456 
# 
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 
E90 C2  N1   doub Y N 115 
E90 N1  C6   sing Y N 116 
E90 S7  C2   sing N N 117 
E90 N3  C2   sing Y N 118 
E90 N3  C4   doub Y N 119 
E90 C4  C5   sing Y N 120 
E90 C4  H4   sing N N 121 
E90 C5  C6   doub Y N 122 
E90 C5  H5   sing N N 123 
E90 C6  H6   sing N N 124 
E90 S7  C8   sing N N 125 
E90 C8  C9   sing N N 126 
E90 C8  H8   sing N N 127 
E90 C8  H8A  sing N N 128 
E90 O10 C9   doub N N 129 
E90 C9  C11  sing N N 130 
E90 C11 C16  doub Y N 131 
E90 C11 C12  sing Y N 132 
E90 C12 C13  doub Y N 133 
E90 C12 H12  sing N N 134 
E90 C13 C14  sing Y N 135 
E90 C13 H13  sing N N 136 
E90 C15 C14  doub Y N 137 
E90 C14 S17  sing N N 138 
E90 C16 C15  sing Y N 139 
E90 C15 H15  sing N N 140 
E90 C16 H16  sing N N 141 
E90 N20 S17  sing N N 142 
E90 O19 S17  doub N N 143 
E90 S17 O18  doub N N 144 
E90 N20 HN20 sing N N 145 
E90 N20 HN2A sing N N 146 
GLN N   CA   sing N N 147 
GLN N   H    sing N N 148 
GLN N   H2   sing N N 149 
GLN CA  C    sing N N 150 
GLN CA  CB   sing N N 151 
GLN CA  HA   sing N N 152 
GLN C   O    doub N N 153 
GLN C   OXT  sing N N 154 
GLN CB  CG   sing N N 155 
GLN CB  HB2  sing N N 156 
GLN CB  HB3  sing N N 157 
GLN CG  CD   sing N N 158 
GLN CG  HG2  sing N N 159 
GLN CG  HG3  sing N N 160 
GLN CD  OE1  doub N N 161 
GLN CD  NE2  sing N N 162 
GLN NE2 HE21 sing N N 163 
GLN NE2 HE22 sing N N 164 
GLN OXT HXT  sing N N 165 
GLU N   CA   sing N N 166 
GLU N   H    sing N N 167 
GLU N   H2   sing N N 168 
GLU CA  C    sing N N 169 
GLU CA  CB   sing N N 170 
GLU CA  HA   sing N N 171 
GLU C   O    doub N N 172 
GLU C   OXT  sing N N 173 
GLU CB  CG   sing N N 174 
GLU CB  HB2  sing N N 175 
GLU CB  HB3  sing N N 176 
GLU CG  CD   sing N N 177 
GLU CG  HG2  sing N N 178 
GLU CG  HG3  sing N N 179 
GLU CD  OE1  doub N N 180 
GLU CD  OE2  sing N N 181 
GLU OE2 HE2  sing N N 182 
GLU OXT HXT  sing N N 183 
GLY N   CA   sing N N 184 
GLY N   H    sing N N 185 
GLY N   H2   sing N N 186 
GLY CA  C    sing N N 187 
GLY CA  HA2  sing N N 188 
GLY CA  HA3  sing N N 189 
GLY C   O    doub N N 190 
GLY C   OXT  sing N N 191 
GLY OXT HXT  sing N N 192 
HIS N   CA   sing N N 193 
HIS N   H    sing N N 194 
HIS N   H2   sing N N 195 
HIS CA  C    sing N N 196 
HIS CA  CB   sing N N 197 
HIS CA  HA   sing N N 198 
HIS C   O    doub N N 199 
HIS C   OXT  sing N N 200 
HIS CB  CG   sing N N 201 
HIS CB  HB2  sing N N 202 
HIS CB  HB3  sing N N 203 
HIS CG  ND1  sing Y N 204 
HIS CG  CD2  doub Y N 205 
HIS ND1 CE1  doub Y N 206 
HIS ND1 HD1  sing N N 207 
HIS CD2 NE2  sing Y N 208 
HIS CD2 HD2  sing N N 209 
HIS CE1 NE2  sing Y N 210 
HIS CE1 HE1  sing N N 211 
HIS NE2 HE2  sing N N 212 
HIS OXT HXT  sing N N 213 
HOH O   H1   sing N N 214 
HOH O   H2   sing N N 215 
ILE N   CA   sing N N 216 
ILE N   H    sing N N 217 
ILE N   H2   sing N N 218 
ILE CA  C    sing N N 219 
ILE CA  CB   sing N N 220 
ILE CA  HA   sing N N 221 
ILE C   O    doub N N 222 
ILE C   OXT  sing N N 223 
ILE CB  CG1  sing N N 224 
ILE CB  CG2  sing N N 225 
ILE CB  HB   sing N N 226 
ILE CG1 CD1  sing N N 227 
ILE CG1 HG12 sing N N 228 
ILE CG1 HG13 sing N N 229 
ILE CG2 HG21 sing N N 230 
ILE CG2 HG22 sing N N 231 
ILE CG2 HG23 sing N N 232 
ILE CD1 HD11 sing N N 233 
ILE CD1 HD12 sing N N 234 
ILE CD1 HD13 sing N N 235 
ILE OXT HXT  sing N N 236 
LEU N   CA   sing N N 237 
LEU N   H    sing N N 238 
LEU N   H2   sing N N 239 
LEU CA  C    sing N N 240 
LEU CA  CB   sing N N 241 
LEU CA  HA   sing N N 242 
LEU C   O    doub N N 243 
LEU C   OXT  sing N N 244 
LEU CB  CG   sing N N 245 
LEU CB  HB2  sing N N 246 
LEU CB  HB3  sing N N 247 
LEU CG  CD1  sing N N 248 
LEU CG  CD2  sing N N 249 
LEU CG  HG   sing N N 250 
LEU CD1 HD11 sing N N 251 
LEU CD1 HD12 sing N N 252 
LEU CD1 HD13 sing N N 253 
LEU CD2 HD21 sing N N 254 
LEU CD2 HD22 sing N N 255 
LEU CD2 HD23 sing N N 256 
LEU OXT HXT  sing N N 257 
LYS N   CA   sing N N 258 
LYS N   H    sing N N 259 
LYS N   H2   sing N N 260 
LYS CA  C    sing N N 261 
LYS CA  CB   sing N N 262 
LYS CA  HA   sing N N 263 
LYS C   O    doub N N 264 
LYS C   OXT  sing N N 265 
LYS CB  CG   sing N N 266 
LYS CB  HB2  sing N N 267 
LYS CB  HB3  sing N N 268 
LYS CG  CD   sing N N 269 
LYS CG  HG2  sing N N 270 
LYS CG  HG3  sing N N 271 
LYS CD  CE   sing N N 272 
LYS CD  HD2  sing N N 273 
LYS CD  HD3  sing N N 274 
LYS CE  NZ   sing N N 275 
LYS CE  HE2  sing N N 276 
LYS CE  HE3  sing N N 277 
LYS NZ  HZ1  sing N N 278 
LYS NZ  HZ2  sing N N 279 
LYS NZ  HZ3  sing N N 280 
LYS OXT HXT  sing N N 281 
MET N   CA   sing N N 282 
MET N   H    sing N N 283 
MET N   H2   sing N N 284 
MET CA  C    sing N N 285 
MET CA  CB   sing N N 286 
MET CA  HA   sing N N 287 
MET C   O    doub N N 288 
MET C   OXT  sing N N 289 
MET CB  CG   sing N N 290 
MET CB  HB2  sing N N 291 
MET CB  HB3  sing N N 292 
MET CG  SD   sing N N 293 
MET CG  HG2  sing N N 294 
MET CG  HG3  sing N N 295 
MET SD  CE   sing N N 296 
MET CE  HE1  sing N N 297 
MET CE  HE2  sing N N 298 
MET CE  HE3  sing N N 299 
MET OXT HXT  sing N N 300 
PHE N   CA   sing N N 301 
PHE N   H    sing N N 302 
PHE N   H2   sing N N 303 
PHE CA  C    sing N N 304 
PHE CA  CB   sing N N 305 
PHE CA  HA   sing N N 306 
PHE C   O    doub N N 307 
PHE C   OXT  sing N N 308 
PHE CB  CG   sing N N 309 
PHE CB  HB2  sing N N 310 
PHE CB  HB3  sing N N 311 
PHE CG  CD1  doub Y N 312 
PHE CG  CD2  sing Y N 313 
PHE CD1 CE1  sing Y N 314 
PHE CD1 HD1  sing N N 315 
PHE CD2 CE2  doub Y N 316 
PHE CD2 HD2  sing N N 317 
PHE CE1 CZ   doub Y N 318 
PHE CE1 HE1  sing N N 319 
PHE CE2 CZ   sing Y N 320 
PHE CE2 HE2  sing N N 321 
PHE CZ  HZ   sing N N 322 
PHE OXT HXT  sing N N 323 
PRO N   CA   sing N N 324 
PRO N   CD   sing N N 325 
PRO N   H    sing N N 326 
PRO CA  C    sing N N 327 
PRO CA  CB   sing N N 328 
PRO CA  HA   sing N N 329 
PRO C   O    doub N N 330 
PRO C   OXT  sing N N 331 
PRO CB  CG   sing N N 332 
PRO CB  HB2  sing N N 333 
PRO CB  HB3  sing N N 334 
PRO CG  CD   sing N N 335 
PRO CG  HG2  sing N N 336 
PRO CG  HG3  sing N N 337 
PRO CD  HD2  sing N N 338 
PRO CD  HD3  sing N N 339 
PRO OXT HXT  sing N N 340 
SER N   CA   sing N N 341 
SER N   H    sing N N 342 
SER N   H2   sing N N 343 
SER CA  C    sing N N 344 
SER CA  CB   sing N N 345 
SER CA  HA   sing N N 346 
SER C   O    doub N N 347 
SER C   OXT  sing N N 348 
SER CB  OG   sing N N 349 
SER CB  HB2  sing N N 350 
SER CB  HB3  sing N N 351 
SER OG  HG   sing N N 352 
SER OXT HXT  sing N N 353 
THR N   CA   sing N N 354 
THR N   H    sing N N 355 
THR N   H2   sing N N 356 
THR CA  C    sing N N 357 
THR CA  CB   sing N N 358 
THR CA  HA   sing N N 359 
THR C   O    doub N N 360 
THR C   OXT  sing N N 361 
THR CB  OG1  sing N N 362 
THR CB  CG2  sing N N 363 
THR CB  HB   sing N N 364 
THR OG1 HG1  sing N N 365 
THR CG2 HG21 sing N N 366 
THR CG2 HG22 sing N N 367 
THR CG2 HG23 sing N N 368 
THR OXT HXT  sing N N 369 
TRP N   CA   sing N N 370 
TRP N   H    sing N N 371 
TRP N   H2   sing N N 372 
TRP CA  C    sing N N 373 
TRP CA  CB   sing N N 374 
TRP CA  HA   sing N N 375 
TRP C   O    doub N N 376 
TRP C   OXT  sing N N 377 
TRP CB  CG   sing N N 378 
TRP CB  HB2  sing N N 379 
TRP CB  HB3  sing N N 380 
TRP CG  CD1  doub Y N 381 
TRP CG  CD2  sing Y N 382 
TRP CD1 NE1  sing Y N 383 
TRP CD1 HD1  sing N N 384 
TRP CD2 CE2  doub Y N 385 
TRP CD2 CE3  sing Y N 386 
TRP NE1 CE2  sing Y N 387 
TRP NE1 HE1  sing N N 388 
TRP CE2 CZ2  sing Y N 389 
TRP CE3 CZ3  doub Y N 390 
TRP CE3 HE3  sing N N 391 
TRP CZ2 CH2  doub Y N 392 
TRP CZ2 HZ2  sing N N 393 
TRP CZ3 CH2  sing Y N 394 
TRP CZ3 HZ3  sing N N 395 
TRP CH2 HH2  sing N N 396 
TRP OXT HXT  sing N N 397 
TYR N   CA   sing N N 398 
TYR N   H    sing N N 399 
TYR N   H2   sing N N 400 
TYR CA  C    sing N N 401 
TYR CA  CB   sing N N 402 
TYR CA  HA   sing N N 403 
TYR C   O    doub N N 404 
TYR C   OXT  sing N N 405 
TYR CB  CG   sing N N 406 
TYR CB  HB2  sing N N 407 
TYR CB  HB3  sing N N 408 
TYR CG  CD1  doub Y N 409 
TYR CG  CD2  sing Y N 410 
TYR CD1 CE1  sing Y N 411 
TYR CD1 HD1  sing N N 412 
TYR CD2 CE2  doub Y N 413 
TYR CD2 HD2  sing N N 414 
TYR CE1 CZ   doub Y N 415 
TYR CE1 HE1  sing N N 416 
TYR CE2 CZ   sing Y N 417 
TYR CE2 HE2  sing N N 418 
TYR CZ  OH   sing N N 419 
TYR OH  HH   sing N N 420 
TYR OXT HXT  sing N N 421 
VAL N   CA   sing N N 422 
VAL N   H    sing N N 423 
VAL N   H2   sing N N 424 
VAL CA  C    sing N N 425 
VAL CA  CB   sing N N 426 
VAL CA  HA   sing N N 427 
VAL C   O    doub N N 428 
VAL C   OXT  sing N N 429 
VAL CB  CG1  sing N N 430 
VAL CB  CG2  sing N N 431 
VAL CB  HB   sing N N 432 
VAL CG1 HG11 sing N N 433 
VAL CG1 HG12 sing N N 434 
VAL CG1 HG13 sing N N 435 
VAL CG2 HG21 sing N N 436 
VAL CG2 HG22 sing N N 437 
VAL CG2 HG23 sing N N 438 
VAL OXT HXT  sing N N 439 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                             ZN  
3 'DIMETHYL SULFOXIDE'                                   DMS 
4 BICINE                                                 BCN 
5 '4-[(pyrimidin-2-ylsulfanyl)acetyl]benzenesulfonamide' E90 
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' 
# 
