data_9IZB
# 
_entry.id   9IZB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9IZB         pdb_00009izb 10.2210/pdb9izb/pdb 
WWPDB D_1300049143 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IZB 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              leijian@scu.edu.cn 
_pdbx_contact_author.name_first         Jian 
_pdbx_contact_author.name_last          Lei 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9326-0554 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Deng, X.Y.' 1 0009-0002-8205-6229 
'Zeng, R.'   2 0000-0001-9716-6354 
'Yang, S.Y.' 3 0000-0001-5147-3746 
'Lei, J.'    4 0000-0001-9326-0554 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of SARS-CoV-2 main protease in complex with TMP1' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Deng, X.Y.' 1 0009-0002-8205-6229 
primary 'Zeng, R.'   2 0000-0001-9716-6354 
primary 'Yang, S.Y.' 3 0000-0001-5147-3746 
primary 'Lei, J.'    4 0000-0001-9326-0554 
# 
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 '3C-like proteinase nsp5' 33825.547 1  3.4.22.69 ? ? ? 
2 polymer syn TMP1                      719.236   1  ?         ? ? ? 
3 water   nat water                     18.015    91 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
A ? 
2 'polypeptide(L)' no yes '(YXY)(CHG)(FP9)(005)(A1L3F)' XXPXX B ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER   n 
1 2   GLY   n 
1 3   PHE   n 
1 4   ARG   n 
1 5   LYS   n 
1 6   MET   n 
1 7   ALA   n 
1 8   PHE   n 
1 9   PRO   n 
1 10  SER   n 
1 11  GLY   n 
1 12  LYS   n 
1 13  VAL   n 
1 14  GLU   n 
1 15  GLY   n 
1 16  CYS   n 
1 17  MET   n 
1 18  VAL   n 
1 19  GLN   n 
1 20  VAL   n 
1 21  THR   n 
1 22  CYS   n 
1 23  GLY   n 
1 24  THR   n 
1 25  THR   n 
1 26  THR   n 
1 27  LEU   n 
1 28  ASN   n 
1 29  GLY   n 
1 30  LEU   n 
1 31  TRP   n 
1 32  LEU   n 
1 33  ASP   n 
1 34  ASP   n 
1 35  VAL   n 
1 36  VAL   n 
1 37  TYR   n 
1 38  CYS   n 
1 39  PRO   n 
1 40  ARG   n 
1 41  HIS   n 
1 42  VAL   n 
1 43  ILE   n 
1 44  CYS   n 
1 45  THR   n 
1 46  SER   n 
1 47  GLU   n 
1 48  ASP   n 
1 49  MET   n 
1 50  LEU   n 
1 51  ASN   n 
1 52  PRO   n 
1 53  ASN   n 
1 54  TYR   n 
1 55  GLU   n 
1 56  ASP   n 
1 57  LEU   n 
1 58  LEU   n 
1 59  ILE   n 
1 60  ARG   n 
1 61  LYS   n 
1 62  SER   n 
1 63  ASN   n 
1 64  HIS   n 
1 65  ASN   n 
1 66  PHE   n 
1 67  LEU   n 
1 68  VAL   n 
1 69  GLN   n 
1 70  ALA   n 
1 71  GLY   n 
1 72  ASN   n 
1 73  VAL   n 
1 74  GLN   n 
1 75  LEU   n 
1 76  ARG   n 
1 77  VAL   n 
1 78  ILE   n 
1 79  GLY   n 
1 80  HIS   n 
1 81  SER   n 
1 82  MET   n 
1 83  GLN   n 
1 84  ASN   n 
1 85  CYS   n 
1 86  VAL   n 
1 87  LEU   n 
1 88  LYS   n 
1 89  LEU   n 
1 90  LYS   n 
1 91  VAL   n 
1 92  ASP   n 
1 93  THR   n 
1 94  ALA   n 
1 95  ASN   n 
1 96  PRO   n 
1 97  LYS   n 
1 98  THR   n 
1 99  PRO   n 
1 100 LYS   n 
1 101 TYR   n 
1 102 LYS   n 
1 103 PHE   n 
1 104 VAL   n 
1 105 ARG   n 
1 106 ILE   n 
1 107 GLN   n 
1 108 PRO   n 
1 109 GLY   n 
1 110 GLN   n 
1 111 THR   n 
1 112 PHE   n 
1 113 SER   n 
1 114 VAL   n 
1 115 LEU   n 
1 116 ALA   n 
1 117 CYS   n 
1 118 TYR   n 
1 119 ASN   n 
1 120 GLY   n 
1 121 SER   n 
1 122 PRO   n 
1 123 SER   n 
1 124 GLY   n 
1 125 VAL   n 
1 126 TYR   n 
1 127 GLN   n 
1 128 CYS   n 
1 129 ALA   n 
1 130 MET   n 
1 131 ARG   n 
1 132 PRO   n 
1 133 ASN   n 
1 134 PHE   n 
1 135 THR   n 
1 136 ILE   n 
1 137 LYS   n 
1 138 GLY   n 
1 139 SER   n 
1 140 PHE   n 
1 141 LEU   n 
1 142 ASN   n 
1 143 GLY   n 
1 144 SER   n 
1 145 CYS   n 
1 146 GLY   n 
1 147 SER   n 
1 148 VAL   n 
1 149 GLY   n 
1 150 PHE   n 
1 151 ASN   n 
1 152 ILE   n 
1 153 ASP   n 
1 154 TYR   n 
1 155 ASP   n 
1 156 CYS   n 
1 157 VAL   n 
1 158 SER   n 
1 159 PHE   n 
1 160 CYS   n 
1 161 TYR   n 
1 162 MET   n 
1 163 HIS   n 
1 164 HIS   n 
1 165 MET   n 
1 166 GLU   n 
1 167 LEU   n 
1 168 PRO   n 
1 169 THR   n 
1 170 GLY   n 
1 171 VAL   n 
1 172 HIS   n 
1 173 ALA   n 
1 174 GLY   n 
1 175 THR   n 
1 176 ASP   n 
1 177 LEU   n 
1 178 GLU   n 
1 179 GLY   n 
1 180 ASN   n 
1 181 PHE   n 
1 182 TYR   n 
1 183 GLY   n 
1 184 PRO   n 
1 185 PHE   n 
1 186 VAL   n 
1 187 ASP   n 
1 188 ARG   n 
1 189 GLN   n 
1 190 THR   n 
1 191 ALA   n 
1 192 GLN   n 
1 193 ALA   n 
1 194 ALA   n 
1 195 GLY   n 
1 196 THR   n 
1 197 ASP   n 
1 198 THR   n 
1 199 THR   n 
1 200 ILE   n 
1 201 THR   n 
1 202 VAL   n 
1 203 ASN   n 
1 204 VAL   n 
1 205 LEU   n 
1 206 ALA   n 
1 207 TRP   n 
1 208 LEU   n 
1 209 TYR   n 
1 210 ALA   n 
1 211 ALA   n 
1 212 VAL   n 
1 213 ILE   n 
1 214 ASN   n 
1 215 GLY   n 
1 216 ASP   n 
1 217 ARG   n 
1 218 TRP   n 
1 219 PHE   n 
1 220 LEU   n 
1 221 ASN   n 
1 222 ARG   n 
1 223 PHE   n 
1 224 THR   n 
1 225 THR   n 
1 226 THR   n 
1 227 LEU   n 
1 228 ASN   n 
1 229 ASP   n 
1 230 PHE   n 
1 231 ASN   n 
1 232 LEU   n 
1 233 VAL   n 
1 234 ALA   n 
1 235 MET   n 
1 236 LYS   n 
1 237 TYR   n 
1 238 ASN   n 
1 239 TYR   n 
1 240 GLU   n 
1 241 PRO   n 
1 242 LEU   n 
1 243 THR   n 
1 244 GLN   n 
1 245 ASP   n 
1 246 HIS   n 
1 247 VAL   n 
1 248 ASP   n 
1 249 ILE   n 
1 250 LEU   n 
1 251 GLY   n 
1 252 PRO   n 
1 253 LEU   n 
1 254 SER   n 
1 255 ALA   n 
1 256 GLN   n 
1 257 THR   n 
1 258 GLY   n 
1 259 ILE   n 
1 260 ALA   n 
1 261 VAL   n 
1 262 LEU   n 
1 263 ASP   n 
1 264 MET   n 
1 265 CYS   n 
1 266 ALA   n 
1 267 SER   n 
1 268 LEU   n 
1 269 LYS   n 
1 270 GLU   n 
1 271 LEU   n 
1 272 LEU   n 
1 273 GLN   n 
1 274 ASN   n 
1 275 GLY   n 
1 276 MET   n 
1 277 ASN   n 
1 278 GLY   n 
1 279 ARG   n 
1 280 THR   n 
1 281 ILE   n 
1 282 LEU   n 
1 283 GLY   n 
1 284 SER   n 
1 285 ALA   n 
1 286 LEU   n 
1 287 LEU   n 
1 288 GLU   n 
1 289 ASP   n 
1 290 GLU   n 
1 291 PHE   n 
1 292 THR   n 
1 293 PRO   n 
1 294 PHE   n 
1 295 ASP   n 
1 296 VAL   n 
1 297 VAL   n 
1 298 ARG   n 
1 299 GLN   n 
1 300 CYS   n 
1 301 SER   n 
1 302 GLY   n 
1 303 VAL   n 
1 304 THR   n 
1 305 PHE   n 
1 306 GLN   n 
2 1   YXY   n 
2 2   CHG   n 
2 3   FP9   n 
2 4   005   n 
2 5   A1L3F 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       5 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
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 
005   peptide-like        . '(2S,3S)-3-amino-2-hydroxy-4-phenylbutanoic acid' ? 'C10 H13 N O3'   195.215 
A1L3F non-polymer         . '(5-chloranylpyridin-2-yl)methanamine'            ? 'C6 H7 Cl N2'    142.586 
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 
CHG   'L-peptide linking' . CYCLOHEXYL-GLYCINE                                ? 'C8 H15 N O2'    157.210 
CYS   'L-peptide linking' y CYSTEINE                                          ? 'C3 H7 N O2 S'   121.158 
FP9   'L-peptide linking' n '(4R)-4-fluoro-L-proline'                         ? 'C5 H8 F N O2'   133.121 
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 
YXY   non-polymer         . 4,4-difluorocyclohexane-1-carboxamide             ? 'C7 H11 F2 N O'  163.165 
# 
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   SER   1   1   1   SER   SER A . n 
A 1 2   GLY   2   2   2   GLY   GLY A . n 
A 1 3   PHE   3   3   3   PHE   PHE A . n 
A 1 4   ARG   4   4   4   ARG   ARG A . n 
A 1 5   LYS   5   5   5   LYS   LYS A . n 
A 1 6   MET   6   6   6   MET   MET A . n 
A 1 7   ALA   7   7   7   ALA   ALA A . n 
A 1 8   PHE   8   8   8   PHE   PHE A . n 
A 1 9   PRO   9   9   9   PRO   PRO A . n 
A 1 10  SER   10  10  10  SER   SER A . n 
A 1 11  GLY   11  11  11  GLY   GLY A . n 
A 1 12  LYS   12  12  12  LYS   LYS A . n 
A 1 13  VAL   13  13  13  VAL   VAL A . n 
A 1 14  GLU   14  14  14  GLU   GLU A . n 
A 1 15  GLY   15  15  15  GLY   GLY A . n 
A 1 16  CYS   16  16  16  CYS   CYS A . n 
A 1 17  MET   17  17  17  MET   MET A . n 
A 1 18  VAL   18  18  18  VAL   VAL A . n 
A 1 19  GLN   19  19  19  GLN   GLN A . n 
A 1 20  VAL   20  20  20  VAL   VAL A . n 
A 1 21  THR   21  21  21  THR   THR A . n 
A 1 22  CYS   22  22  22  CYS   CYS A . n 
A 1 23  GLY   23  23  23  GLY   GLY A . n 
A 1 24  THR   24  24  24  THR   THR A . n 
A 1 25  THR   25  25  25  THR   THR A . n 
A 1 26  THR   26  26  26  THR   THR A . n 
A 1 27  LEU   27  27  27  LEU   LEU A . n 
A 1 28  ASN   28  28  28  ASN   ASN A . n 
A 1 29  GLY   29  29  29  GLY   GLY A . n 
A 1 30  LEU   30  30  30  LEU   LEU A . n 
A 1 31  TRP   31  31  31  TRP   TRP A . n 
A 1 32  LEU   32  32  32  LEU   LEU A . n 
A 1 33  ASP   33  33  33  ASP   ASP A . n 
A 1 34  ASP   34  34  34  ASP   ASP A . n 
A 1 35  VAL   35  35  35  VAL   VAL A . n 
A 1 36  VAL   36  36  36  VAL   VAL A . n 
A 1 37  TYR   37  37  37  TYR   TYR A . n 
A 1 38  CYS   38  38  38  CYS   CYS A . n 
A 1 39  PRO   39  39  39  PRO   PRO A . n 
A 1 40  ARG   40  40  40  ARG   ARG A . n 
A 1 41  HIS   41  41  41  HIS   HIS A . n 
A 1 42  VAL   42  42  42  VAL   VAL A . n 
A 1 43  ILE   43  43  43  ILE   ILE A . n 
A 1 44  CYS   44  44  44  CYS   CYS A . n 
A 1 45  THR   45  45  45  THR   THR A . n 
A 1 46  SER   46  46  46  SER   SER A . n 
A 1 47  GLU   47  47  47  GLU   GLU A . n 
A 1 48  ASP   48  48  48  ASP   ASP A . n 
A 1 49  MET   49  49  49  MET   MET A . n 
A 1 50  LEU   50  50  50  LEU   LEU A . n 
A 1 51  ASN   51  51  51  ASN   ASN A . n 
A 1 52  PRO   52  52  52  PRO   PRO A . n 
A 1 53  ASN   53  53  53  ASN   ASN A . n 
A 1 54  TYR   54  54  54  TYR   TYR A . n 
A 1 55  GLU   55  55  55  GLU   GLU A . n 
A 1 56  ASP   56  56  56  ASP   ASP A . n 
A 1 57  LEU   57  57  57  LEU   LEU A . n 
A 1 58  LEU   58  58  58  LEU   LEU A . n 
A 1 59  ILE   59  59  59  ILE   ILE A . n 
A 1 60  ARG   60  60  60  ARG   ARG A . n 
A 1 61  LYS   61  61  61  LYS   LYS A . n 
A 1 62  SER   62  62  62  SER   SER A . n 
A 1 63  ASN   63  63  63  ASN   ASN A . n 
A 1 64  HIS   64  64  64  HIS   HIS A . n 
A 1 65  ASN   65  65  65  ASN   ASN A . n 
A 1 66  PHE   66  66  66  PHE   PHE A . n 
A 1 67  LEU   67  67  67  LEU   LEU A . n 
A 1 68  VAL   68  68  68  VAL   VAL A . n 
A 1 69  GLN   69  69  69  GLN   GLN A . n 
A 1 70  ALA   70  70  70  ALA   ALA A . n 
A 1 71  GLY   71  71  71  GLY   GLY A . n 
A 1 72  ASN   72  72  72  ASN   ASN A . n 
A 1 73  VAL   73  73  73  VAL   VAL A . n 
A 1 74  GLN   74  74  74  GLN   GLN A . n 
A 1 75  LEU   75  75  75  LEU   LEU A . n 
A 1 76  ARG   76  76  76  ARG   ARG A . n 
A 1 77  VAL   77  77  77  VAL   VAL A . n 
A 1 78  ILE   78  78  78  ILE   ILE A . n 
A 1 79  GLY   79  79  79  GLY   GLY A . n 
A 1 80  HIS   80  80  80  HIS   HIS A . n 
A 1 81  SER   81  81  81  SER   SER A . n 
A 1 82  MET   82  82  82  MET   MET A . n 
A 1 83  GLN   83  83  83  GLN   GLN A . n 
A 1 84  ASN   84  84  84  ASN   ASN A . n 
A 1 85  CYS   85  85  85  CYS   CYS A . n 
A 1 86  VAL   86  86  86  VAL   VAL A . n 
A 1 87  LEU   87  87  87  LEU   LEU A . n 
A 1 88  LYS   88  88  88  LYS   LYS A . n 
A 1 89  LEU   89  89  89  LEU   LEU A . n 
A 1 90  LYS   90  90  90  LYS   LYS A . n 
A 1 91  VAL   91  91  91  VAL   VAL A . n 
A 1 92  ASP   92  92  92  ASP   ASP A . n 
A 1 93  THR   93  93  93  THR   THR A . n 
A 1 94  ALA   94  94  94  ALA   ALA A . n 
A 1 95  ASN   95  95  95  ASN   ASN A . n 
A 1 96  PRO   96  96  96  PRO   PRO A . n 
A 1 97  LYS   97  97  97  LYS   LYS A . n 
A 1 98  THR   98  98  98  THR   THR A . n 
A 1 99  PRO   99  99  99  PRO   PRO A . n 
A 1 100 LYS   100 100 100 LYS   LYS A . n 
A 1 101 TYR   101 101 101 TYR   TYR A . n 
A 1 102 LYS   102 102 102 LYS   LYS A . n 
A 1 103 PHE   103 103 103 PHE   PHE A . n 
A 1 104 VAL   104 104 104 VAL   VAL A . n 
A 1 105 ARG   105 105 105 ARG   ARG A . n 
A 1 106 ILE   106 106 106 ILE   ILE A . n 
A 1 107 GLN   107 107 107 GLN   GLN A . n 
A 1 108 PRO   108 108 108 PRO   PRO A . n 
A 1 109 GLY   109 109 109 GLY   GLY A . n 
A 1 110 GLN   110 110 110 GLN   GLN A . n 
A 1 111 THR   111 111 111 THR   THR A . n 
A 1 112 PHE   112 112 112 PHE   PHE A . n 
A 1 113 SER   113 113 113 SER   SER A . n 
A 1 114 VAL   114 114 114 VAL   VAL A . n 
A 1 115 LEU   115 115 115 LEU   LEU A . n 
A 1 116 ALA   116 116 116 ALA   ALA A . n 
A 1 117 CYS   117 117 117 CYS   CYS A . n 
A 1 118 TYR   118 118 118 TYR   TYR A . n 
A 1 119 ASN   119 119 119 ASN   ASN A . n 
A 1 120 GLY   120 120 120 GLY   GLY A . n 
A 1 121 SER   121 121 121 SER   SER A . n 
A 1 122 PRO   122 122 122 PRO   PRO A . n 
A 1 123 SER   123 123 123 SER   SER A . n 
A 1 124 GLY   124 124 124 GLY   GLY A . n 
A 1 125 VAL   125 125 125 VAL   VAL A . n 
A 1 126 TYR   126 126 126 TYR   TYR A . n 
A 1 127 GLN   127 127 127 GLN   GLN A . n 
A 1 128 CYS   128 128 128 CYS   CYS A . n 
A 1 129 ALA   129 129 129 ALA   ALA A . n 
A 1 130 MET   130 130 130 MET   MET A . n 
A 1 131 ARG   131 131 131 ARG   ARG A . n 
A 1 132 PRO   132 132 132 PRO   PRO A . n 
A 1 133 ASN   133 133 133 ASN   ASN A . n 
A 1 134 PHE   134 134 134 PHE   PHE A . n 
A 1 135 THR   135 135 135 THR   THR A . n 
A 1 136 ILE   136 136 136 ILE   ILE A . n 
A 1 137 LYS   137 137 137 LYS   LYS A . n 
A 1 138 GLY   138 138 138 GLY   GLY A . n 
A 1 139 SER   139 139 139 SER   SER A . n 
A 1 140 PHE   140 140 140 PHE   PHE A . n 
A 1 141 LEU   141 141 141 LEU   LEU A . n 
A 1 142 ASN   142 142 142 ASN   ASN A . n 
A 1 143 GLY   143 143 143 GLY   GLY A . n 
A 1 144 SER   144 144 144 SER   SER A . n 
A 1 145 CYS   145 145 145 CYS   CYS A . n 
A 1 146 GLY   146 146 146 GLY   GLY A . n 
A 1 147 SER   147 147 147 SER   SER A . n 
A 1 148 VAL   148 148 148 VAL   VAL A . n 
A 1 149 GLY   149 149 149 GLY   GLY A . n 
A 1 150 PHE   150 150 150 PHE   PHE A . n 
A 1 151 ASN   151 151 151 ASN   ASN A . n 
A 1 152 ILE   152 152 152 ILE   ILE A . n 
A 1 153 ASP   153 153 153 ASP   ASP A . n 
A 1 154 TYR   154 154 154 TYR   TYR A . n 
A 1 155 ASP   155 155 155 ASP   ASP A . n 
A 1 156 CYS   156 156 156 CYS   CYS A . n 
A 1 157 VAL   157 157 157 VAL   VAL A . n 
A 1 158 SER   158 158 158 SER   SER A . n 
A 1 159 PHE   159 159 159 PHE   PHE A . n 
A 1 160 CYS   160 160 160 CYS   CYS A . n 
A 1 161 TYR   161 161 161 TYR   TYR A . n 
A 1 162 MET   162 162 162 MET   MET A . n 
A 1 163 HIS   163 163 163 HIS   HIS A . n 
A 1 164 HIS   164 164 164 HIS   HIS A . n 
A 1 165 MET   165 165 165 MET   MET A . n 
A 1 166 GLU   166 166 166 GLU   GLU A . n 
A 1 167 LEU   167 167 167 LEU   LEU A . n 
A 1 168 PRO   168 168 168 PRO   PRO A . n 
A 1 169 THR   169 169 169 THR   THR A . n 
A 1 170 GLY   170 170 170 GLY   GLY A . n 
A 1 171 VAL   171 171 171 VAL   VAL A . n 
A 1 172 HIS   172 172 172 HIS   HIS A . n 
A 1 173 ALA   173 173 173 ALA   ALA A . n 
A 1 174 GLY   174 174 174 GLY   GLY A . n 
A 1 175 THR   175 175 175 THR   THR A . n 
A 1 176 ASP   176 176 176 ASP   ASP A . n 
A 1 177 LEU   177 177 177 LEU   LEU A . n 
A 1 178 GLU   178 178 178 GLU   GLU A . n 
A 1 179 GLY   179 179 179 GLY   GLY A . n 
A 1 180 ASN   180 180 180 ASN   ASN A . n 
A 1 181 PHE   181 181 181 PHE   PHE A . n 
A 1 182 TYR   182 182 182 TYR   TYR A . n 
A 1 183 GLY   183 183 183 GLY   GLY A . n 
A 1 184 PRO   184 184 184 PRO   PRO A . n 
A 1 185 PHE   185 185 185 PHE   PHE A . n 
A 1 186 VAL   186 186 186 VAL   VAL A . n 
A 1 187 ASP   187 187 187 ASP   ASP A . n 
A 1 188 ARG   188 188 188 ARG   ARG A . n 
A 1 189 GLN   189 189 189 GLN   GLN A . n 
A 1 190 THR   190 190 190 THR   THR A . n 
A 1 191 ALA   191 191 191 ALA   ALA A . n 
A 1 192 GLN   192 192 192 GLN   GLN A . n 
A 1 193 ALA   193 193 193 ALA   ALA A . n 
A 1 194 ALA   194 194 194 ALA   ALA A . n 
A 1 195 GLY   195 195 195 GLY   GLY A . n 
A 1 196 THR   196 196 196 THR   THR A . n 
A 1 197 ASP   197 197 197 ASP   ASP A . n 
A 1 198 THR   198 198 198 THR   THR A . n 
A 1 199 THR   199 199 199 THR   THR A . n 
A 1 200 ILE   200 200 200 ILE   ILE A . n 
A 1 201 THR   201 201 201 THR   THR A . n 
A 1 202 VAL   202 202 202 VAL   VAL A . n 
A 1 203 ASN   203 203 203 ASN   ASN A . n 
A 1 204 VAL   204 204 204 VAL   VAL A . n 
A 1 205 LEU   205 205 205 LEU   LEU A . n 
A 1 206 ALA   206 206 206 ALA   ALA A . n 
A 1 207 TRP   207 207 207 TRP   TRP A . n 
A 1 208 LEU   208 208 208 LEU   LEU A . n 
A 1 209 TYR   209 209 209 TYR   TYR A . n 
A 1 210 ALA   210 210 210 ALA   ALA A . n 
A 1 211 ALA   211 211 211 ALA   ALA A . n 
A 1 212 VAL   212 212 212 VAL   VAL A . n 
A 1 213 ILE   213 213 213 ILE   ILE A . n 
A 1 214 ASN   214 214 214 ASN   ASN A . n 
A 1 215 GLY   215 215 215 GLY   GLY A . n 
A 1 216 ASP   216 216 216 ASP   ASP A . n 
A 1 217 ARG   217 217 217 ARG   ARG A . n 
A 1 218 TRP   218 218 218 TRP   TRP A . n 
A 1 219 PHE   219 219 219 PHE   PHE A . n 
A 1 220 LEU   220 220 220 LEU   LEU A . n 
A 1 221 ASN   221 221 221 ASN   ASN A . n 
A 1 222 ARG   222 222 222 ARG   ARG A . n 
A 1 223 PHE   223 223 223 PHE   PHE A . n 
A 1 224 THR   224 224 224 THR   THR A . n 
A 1 225 THR   225 225 225 THR   THR A . n 
A 1 226 THR   226 226 226 THR   THR A . n 
A 1 227 LEU   227 227 227 LEU   LEU A . n 
A 1 228 ASN   228 228 228 ASN   ASN A . n 
A 1 229 ASP   229 229 229 ASP   ASP A . n 
A 1 230 PHE   230 230 230 PHE   PHE A . n 
A 1 231 ASN   231 231 231 ASN   ASN A . n 
A 1 232 LEU   232 232 232 LEU   LEU A . n 
A 1 233 VAL   233 233 233 VAL   VAL A . n 
A 1 234 ALA   234 234 234 ALA   ALA A . n 
A 1 235 MET   235 235 235 MET   MET A . n 
A 1 236 LYS   236 236 236 LYS   LYS A . n 
A 1 237 TYR   237 237 237 TYR   TYR A . n 
A 1 238 ASN   238 238 238 ASN   ASN A . n 
A 1 239 TYR   239 239 239 TYR   TYR A . n 
A 1 240 GLU   240 240 240 GLU   GLU A . n 
A 1 241 PRO   241 241 241 PRO   PRO A . n 
A 1 242 LEU   242 242 242 LEU   LEU A . n 
A 1 243 THR   243 243 243 THR   THR A . n 
A 1 244 GLN   244 244 244 GLN   GLN A . n 
A 1 245 ASP   245 245 245 ASP   ASP A . n 
A 1 246 HIS   246 246 246 HIS   HIS A . n 
A 1 247 VAL   247 247 247 VAL   VAL A . n 
A 1 248 ASP   248 248 248 ASP   ASP A . n 
A 1 249 ILE   249 249 249 ILE   ILE A . n 
A 1 250 LEU   250 250 250 LEU   LEU A . n 
A 1 251 GLY   251 251 251 GLY   GLY A . n 
A 1 252 PRO   252 252 252 PRO   PRO A . n 
A 1 253 LEU   253 253 253 LEU   LEU A . n 
A 1 254 SER   254 254 254 SER   SER A . n 
A 1 255 ALA   255 255 255 ALA   ALA A . n 
A 1 256 GLN   256 256 256 GLN   GLN A . n 
A 1 257 THR   257 257 257 THR   THR A . n 
A 1 258 GLY   258 258 258 GLY   GLY A . n 
A 1 259 ILE   259 259 259 ILE   ILE A . n 
A 1 260 ALA   260 260 260 ALA   ALA A . n 
A 1 261 VAL   261 261 261 VAL   VAL A . n 
A 1 262 LEU   262 262 262 LEU   LEU A . n 
A 1 263 ASP   263 263 263 ASP   ASP A . n 
A 1 264 MET   264 264 264 MET   MET A . n 
A 1 265 CYS   265 265 265 CYS   CYS A . n 
A 1 266 ALA   266 266 266 ALA   ALA A . n 
A 1 267 SER   267 267 267 SER   SER A . n 
A 1 268 LEU   268 268 268 LEU   LEU A . n 
A 1 269 LYS   269 269 269 LYS   LYS A . n 
A 1 270 GLU   270 270 270 GLU   GLU A . n 
A 1 271 LEU   271 271 271 LEU   LEU A . n 
A 1 272 LEU   272 272 272 LEU   LEU A . n 
A 1 273 GLN   273 273 273 GLN   GLN A . n 
A 1 274 ASN   274 274 274 ASN   ASN A . n 
A 1 275 GLY   275 275 275 GLY   GLY A . n 
A 1 276 MET   276 276 276 MET   MET A . n 
A 1 277 ASN   277 277 277 ASN   ASN A . n 
A 1 278 GLY   278 278 278 GLY   GLY A . n 
A 1 279 ARG   279 279 279 ARG   ARG A . n 
A 1 280 THR   280 280 280 THR   THR A . n 
A 1 281 ILE   281 281 281 ILE   ILE A . n 
A 1 282 LEU   282 282 282 LEU   LEU A . n 
A 1 283 GLY   283 283 283 GLY   GLY A . n 
A 1 284 SER   284 284 284 SER   SER A . n 
A 1 285 ALA   285 285 285 ALA   ALA A . n 
A 1 286 LEU   286 286 286 LEU   LEU A . n 
A 1 287 LEU   287 287 287 LEU   LEU A . n 
A 1 288 GLU   288 288 288 GLU   GLU A . n 
A 1 289 ASP   289 289 289 ASP   ASP A . n 
A 1 290 GLU   290 290 290 GLU   GLU A . n 
A 1 291 PHE   291 291 291 PHE   PHE A . n 
A 1 292 THR   292 292 292 THR   THR A . n 
A 1 293 PRO   293 293 293 PRO   PRO A . n 
A 1 294 PHE   294 294 294 PHE   PHE A . n 
A 1 295 ASP   295 295 295 ASP   ASP A . n 
A 1 296 VAL   296 296 296 VAL   VAL A . n 
A 1 297 VAL   297 297 297 VAL   VAL A . n 
A 1 298 ARG   298 298 298 ARG   ARG A . n 
A 1 299 GLN   299 299 299 GLN   GLN A . n 
A 1 300 CYS   300 300 300 CYS   CYS A . n 
A 1 301 SER   301 301 301 SER   SER A . n 
A 1 302 GLY   302 302 ?   ?     ?   A . n 
A 1 303 VAL   303 303 ?   ?     ?   A . n 
A 1 304 THR   304 304 ?   ?     ?   A . n 
A 1 305 PHE   305 305 ?   ?     ?   A . n 
A 1 306 GLN   306 306 ?   ?     ?   A . n 
B 2 1   YXY   1   1   401 YXY   LIG B . n 
B 2 2   CHG   2   2   401 CHG   LIG B . n 
B 2 3   FP9   3   3   401 FP9   LIG B . n 
B 2 4   005   4   4   401 005   LIG B . n 
B 2 5   A1L3F 5   5   401 A1L3F LIG B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 005   ? ? 005   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 A1L3F ? ? A1L3F ? ? 'SUBJECT OF INVESTIGATION' ? 
3 FP9   ? ? FP9   ? ? 'SUBJECT OF INVESTIGATION' ? 
4 CHG   ? ? CHG   ? ? 'SUBJECT OF INVESTIGATION' ? 
5 YXY   ? ? YXY   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
C 3 HOH 1  401 31  HOH HOH A . 
C 3 HOH 2  402 6   HOH HOH A . 
C 3 HOH 3  403 56  HOH HOH A . 
C 3 HOH 4  404 40  HOH HOH A . 
C 3 HOH 5  405 15  HOH HOH A . 
C 3 HOH 6  406 77  HOH HOH A . 
C 3 HOH 7  407 54  HOH HOH A . 
C 3 HOH 8  408 29  HOH HOH A . 
C 3 HOH 9  409 57  HOH HOH A . 
C 3 HOH 10 410 49  HOH HOH A . 
C 3 HOH 11 411 2   HOH HOH A . 
C 3 HOH 12 412 18  HOH HOH A . 
C 3 HOH 13 413 45  HOH HOH A . 
C 3 HOH 14 414 69  HOH HOH A . 
C 3 HOH 15 415 22  HOH HOH A . 
C 3 HOH 16 416 99  HOH HOH A . 
C 3 HOH 17 417 19  HOH HOH A . 
C 3 HOH 18 418 11  HOH HOH A . 
C 3 HOH 19 419 102 HOH HOH A . 
C 3 HOH 20 420 13  HOH HOH A . 
C 3 HOH 21 421 26  HOH HOH A . 
C 3 HOH 22 422 82  HOH HOH A . 
C 3 HOH 23 423 73  HOH HOH A . 
C 3 HOH 24 424 83  HOH HOH A . 
C 3 HOH 25 425 20  HOH HOH A . 
C 3 HOH 26 426 111 HOH HOH A . 
C 3 HOH 27 427 25  HOH HOH A . 
C 3 HOH 28 428 96  HOH HOH A . 
C 3 HOH 29 429 61  HOH HOH A . 
C 3 HOH 30 430 1   HOH HOH A . 
C 3 HOH 31 431 75  HOH HOH A . 
C 3 HOH 32 432 110 HOH HOH A . 
C 3 HOH 33 433 60  HOH HOH A . 
C 3 HOH 34 434 24  HOH HOH A . 
C 3 HOH 35 435 12  HOH HOH A . 
C 3 HOH 36 436 4   HOH HOH A . 
C 3 HOH 37 437 50  HOH HOH A . 
C 3 HOH 38 438 8   HOH HOH A . 
C 3 HOH 39 439 5   HOH HOH A . 
C 3 HOH 40 440 59  HOH HOH A . 
C 3 HOH 41 441 10  HOH HOH A . 
C 3 HOH 42 442 114 HOH HOH A . 
C 3 HOH 43 443 67  HOH HOH A . 
C 3 HOH 44 444 66  HOH HOH A . 
C 3 HOH 45 445 52  HOH HOH A . 
C 3 HOH 46 446 30  HOH HOH A . 
C 3 HOH 47 447 91  HOH HOH A . 
C 3 HOH 48 448 70  HOH HOH A . 
C 3 HOH 49 449 38  HOH HOH A . 
C 3 HOH 50 450 17  HOH HOH A . 
C 3 HOH 51 451 64  HOH HOH A . 
C 3 HOH 52 452 74  HOH HOH A . 
C 3 HOH 53 453 65  HOH HOH A . 
C 3 HOH 54 454 7   HOH HOH A . 
C 3 HOH 55 455 103 HOH HOH A . 
C 3 HOH 56 456 76  HOH HOH A . 
C 3 HOH 57 457 36  HOH HOH A . 
C 3 HOH 58 458 101 HOH HOH A . 
C 3 HOH 59 459 78  HOH HOH A . 
C 3 HOH 60 460 21  HOH HOH A . 
C 3 HOH 61 461 58  HOH HOH A . 
C 3 HOH 62 462 44  HOH HOH A . 
C 3 HOH 63 463 113 HOH HOH A . 
C 3 HOH 64 464 79  HOH HOH A . 
C 3 HOH 65 465 16  HOH HOH A . 
C 3 HOH 66 466 72  HOH HOH A . 
C 3 HOH 67 467 33  HOH HOH A . 
C 3 HOH 68 468 84  HOH HOH A . 
C 3 HOH 69 469 9   HOH HOH A . 
C 3 HOH 70 470 109 HOH HOH A . 
C 3 HOH 71 471 80  HOH HOH A . 
C 3 HOH 72 472 106 HOH HOH A . 
C 3 HOH 73 473 104 HOH HOH A . 
C 3 HOH 74 474 108 HOH HOH A . 
C 3 HOH 75 475 63  HOH HOH A . 
C 3 HOH 76 476 86  HOH HOH A . 
C 3 HOH 77 477 46  HOH HOH A . 
C 3 HOH 78 478 97  HOH HOH A . 
C 3 HOH 79 479 95  HOH HOH A . 
C 3 HOH 80 480 39  HOH HOH A . 
C 3 HOH 81 481 37  HOH HOH A . 
C 3 HOH 82 482 85  HOH HOH A . 
C 3 HOH 83 483 34  HOH HOH A . 
C 3 HOH 84 484 81  HOH HOH A . 
C 3 HOH 85 485 98  HOH HOH A . 
C 3 HOH 86 486 68  HOH HOH A . 
C 3 HOH 87 487 94  HOH HOH A . 
C 3 HOH 88 488 105 HOH HOH A . 
C 3 HOH 89 489 107 HOH HOH A . 
C 3 HOH 90 490 47  HOH HOH A . 
C 3 HOH 91 491 42  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 47  ? CB  ? A GLU 47  CB  
2  1 Y 1 A GLU 47  ? CG  ? A GLU 47  CG  
3  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
4  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
5  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
6  1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
7  1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
8  1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
9  1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
10 1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
11 1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
12 1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.18.2_3874: ???)' 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.26 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IZB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.162 
_cell.length_a_esd                 ? 
_cell.length_b                     53.710 
_cell.length_b_esd                 ? 
_cell.length_c                     44.258 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IZB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IZB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.89 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          34.10 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Magnesium chloride hexahydrate, 0.1 M Tris pH 8.5, 25% w/v PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97852 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97852 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IZB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.60 
_reflns.d_resolution_low                               55.12 
_reflns.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.number_all                                     ? 
_reflns.number_obs                                     8040 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.113 
_reflns.pdbx_Rpim_I_all                                0.046 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.103 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.61 
_reflns_shell.d_res_low                                     2.72 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             957 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.530 
_reflns_shell.pdbx_Rpim_I_all                               0.212 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.918 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.484 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IZB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.60 
_refine.ls_d_res_low                             55.00 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     8034 
_refine.ls_number_reflns_R_free                  393 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.58 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1972 
_refine.ls_R_factor_R_free                       0.2526 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1942 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      7C7P 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 32.72 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.42 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2367 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             91 
_refine_hist.number_atoms_total               2458 
_refine_hist.d_res_high                       2.60 
_refine_hist.d_res_low                        55.00 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  ? 2422 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.321  ? 3294 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 22.086 ? 338  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.071  ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 425  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.60 2.98  . . 131 2509 99.00  . . . . 0.2706 . . . . . . . . . . . 0.3725 
'X-RAY DIFFRACTION' 2.98 3.75  . . 130 2531 100.00 . . . . 0.2091 . . . . . . . . . . . 0.2616 
'X-RAY DIFFRACTION' 3.75 55.00 . . 132 2601 100.00 . . . . 0.1624 . . . . . . . . . . . 0.2161 
# 
_struct.entry_id                     9IZB 
_struct.title                        'Crystal structure of SARS-CoV-2 main protease in complex with TMP1' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9IZB 
_struct_keywords.text            'Severe acute respiratory syndrome coronavirus 2, main protease, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP R1A_SARS2 P0DTC1 ? 1 
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
3264 
2 PDB 9IZB      9IZB   ? 2 ? 1    
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9IZB A 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
2 2 9IZB B 1 ? 5   ? 9IZB   1    ? 5    ? 1 5   
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C 
1 2 A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 2_556 -x,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 -8.6418833948 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 43.4060873080 
# 
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  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 SER A 46  ? LEU A 50  ? SER A 46  LEU A 50  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? LYS A 61  ? ASN A 53  LYS A 61  1 ? 9  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? GLY A 215 ? ILE A 200 GLY A 215 1 ? 16 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? ASN A 274 ? ALA A 260 ASN A 274 1 ? 15 
HELX_P HELX_P11 AB2 THR A 292 ? SER A 301 ? THR A 292 SER A 301 1 ? 10 
# 
_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 
covale1 covale none ? A CYS 145 SG  ? ? ? 1_555 B 005   4 CA  ? ? A CYS 145 B 005   4 1_555 ? ? ? ? ? ? ? 1.773 ? ? 
covale2 covale one  ? B YXY 1   C02 ? ? ? 1_555 B CHG   2 N   ? ? B YXY 1   B CHG   2 1_555 ? ? ? ? ? ? ? 1.461 ? ? 
covale3 covale both ? B CHG 2   C   ? ? ? 1_555 B FP9   3 N   ? ? B CHG 2   B FP9   3 1_555 ? ? ? ? ? ? ? 1.463 ? ? 
covale4 covale both ? B FP9 3   C   ? ? ? 1_555 B 005   4 N   ? ? B FP9 3   B 005   4 1_555 ? ? ? ? ? ? ? 1.445 ? ? 
covale5 covale both ? B 005 4   C   ? ? ? 1_555 B A1L3F 5 N17 ? ? B 005 4   B A1L3F 5 1_555 ? ? ? ? ? ? ? 1.453 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 FP9   B 3   ? .   . . . FP9   B 3   ? 1_555 .   . . . .     .  .  PRO 1 FP9   Fluorination      'Named protein modification' 
2 005   B 4   ? .   . . . 005   B 4   ? 1_555 .   . . . .     .  .  PHE 1 005   'Beta-amino acid' 'Named protein modification' 
3 005   B 4   ? .   . . . 005   B 4   ? 1_555 .   . . . .     .  .  PHE 2 005   Hydroxylation     'Named protein modification' 
4 YXY   B 1   ? .   . . . YXY   B 1   ? 1_555 .   . . . .     .  .  ?   1 YXY   None              'Non-standard residue'       
5 CHG   B 2   ? .   . . . CHG   B 2   ? 1_555 .   . . . .     .  .  ?   1 CHG   None              'Non-standard residue'       
6 A1L3F B 5   ? .   . . . A1L3F B 5   ? 1_555 .   . . . .     .  .  ?   1 A1L3F None              'Non-standard residue'       
7 CYS   A 145 ? 005 B 4 ? CYS   A 145 ? 1_555 005 B 4 ? 1_555 SG CA .   . .     None              'Non-standard linkage'       
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-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 
AA1 1 PHE A 66  ? VAL A 68  ? PHE A 66  VAL A 68  
AA1 2 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 3 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 4 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 5 VAL A 86  ? LYS A 90  ? VAL A 86  LYS A 90  
AA1 6 MET A 82  ? GLN A 83  ? MET A 82  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
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 
AA1 1 2 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 2 3 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 3 4 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 4 5 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 5 6 O VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   9IZB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 64.22   -133.91 
2 1 ALA A 70  ? ? 58.43   -148.57 
3 1 CYS A 85  ? ? 89.71   10.48   
4 1 LEU A 141 ? ? -102.43 -167.32 
5 1 ASP A 155 ? ? 73.66   -12.72  
6 1 HIS A 164 ? ? -120.02 -54.47  
7 1 PHE A 219 ? ? -69.37  1.11    
8 1 FP9 B 3   ? ? -55.95  30.97   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   FP9 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    3 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   005 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    4 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -142.86 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -16.3101 
_pdbx_refine_tls.origin_y         0.8985 
_pdbx_refine_tls.origin_z         16.3457 
_pdbx_refine_tls.T[1][1]          0.2509 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0022 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0173 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2844 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0089 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2919 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.0982 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1780 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.2355 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.6457 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0166 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.8783 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0633 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0444 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0164 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0281 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0534 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0799 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1596 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1240 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0000 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       491 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.10 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 GLY 302 ? A GLY 302 
2 1 Y 1 A VAL 303 ? A VAL 303 
3 1 Y 1 A THR 304 ? A THR 304 
4 1 Y 1 A PHE 305 ? A PHE 305 
5 1 Y 1 A GLN 306 ? A GLN 306 
# 
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 
005   C    C  N N 1   
005   N    N  N N 2   
005   O    O  N N 3   
005   CA   C  N S 4   
005   CD   C  Y N 5   
005   CG   C  N N 6   
005   CH   C  Y N 7   
005   CB1  C  N S 8   
005   OB2  O  N N 9   
005   CE1  C  Y N 10  
005   CE2  C  Y N 11  
005   CZ1  C  Y N 12  
005   CZ2  C  Y N 13  
005   OXT  O  N N 14  
005   HN   H  N N 15  
005   HNA  H  N N 16  
005   HA   H  N N 17  
005   HG   H  N N 18  
005   HGA  H  N N 19  
005   HH   H  N N 20  
005   HB1  H  N N 21  
005   HOB2 H  N N 22  
005   HE1  H  N N 23  
005   HE2  H  N N 24  
005   HZ1  H  N N 25  
005   HZ2  H  N N 26  
005   HXT  H  N N 27  
A1L3F C21  C  Y N 28  
A1L3F C22  C  Y N 29  
A1L3F C24  C  Y N 30  
A1L3F C18  C  N N 31  
A1L3F C19  C  Y N 32  
A1L3F C25  C  Y N 33  
A1L3F N17  N  N N 34  
A1L3F N20  N  Y N 35  
A1L3F CL23 CL N N 36  
A1L3F H1   H  N N 37  
A1L3F H2   H  N N 38  
A1L3F H3   H  N N 39  
A1L3F H4   H  N N 40  
A1L3F H5   H  N N 41  
A1L3F H6   H  N N 42  
A1L3F H7   H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CHG   N    N  N N 117 
CHG   CA   C  N S 118 
CHG   C    C  N N 119 
CHG   O    O  N N 120 
CHG   C1   C  N N 121 
CHG   C2   C  N N 122 
CHG   C3   C  N N 123 
CHG   C4   C  N N 124 
CHG   C5   C  N N 125 
CHG   C6   C  N N 126 
CHG   OXT  O  N N 127 
CHG   H    H  N N 128 
CHG   H2   H  N N 129 
CHG   HA   H  N N 130 
CHG   H1   H  N N 131 
CHG   H2B  H  N N 132 
CHG   H2A  H  N N 133 
CHG   H3   H  N N 134 
CHG   H3A  H  N N 135 
CHG   H4   H  N N 136 
CHG   H4A  H  N N 137 
CHG   H5   H  N N 138 
CHG   H5A  H  N N 139 
CHG   H6   H  N N 140 
CHG   H6A  H  N N 141 
CHG   HXT  H  N N 142 
CYS   N    N  N N 143 
CYS   CA   C  N R 144 
CYS   C    C  N N 145 
CYS   O    O  N N 146 
CYS   CB   C  N N 147 
CYS   SG   S  N N 148 
CYS   OXT  O  N N 149 
CYS   H    H  N N 150 
CYS   H2   H  N N 151 
CYS   HA   H  N N 152 
CYS   HB2  H  N N 153 
CYS   HB3  H  N N 154 
CYS   HG   H  N N 155 
CYS   HXT  H  N N 156 
FP9   C    C  N N 157 
FP9   N    N  N N 158 
FP9   O    O  N N 159 
FP9   CA   C  N S 160 
FP9   CB   C  N N 161 
FP9   CD   C  N N 162 
FP9   FD   F  N N 163 
FP9   CG   C  N R 164 
FP9   OXT  O  N N 165 
FP9   H    H  N N 166 
FP9   HA   H  N N 167 
FP9   HB   H  N N 168 
FP9   HBA  H  N N 169 
FP9   HD   H  N N 170 
FP9   HDA  H  N N 171 
FP9   HG   H  N N 172 
FP9   HXT  H  N N 173 
GLN   N    N  N N 174 
GLN   CA   C  N S 175 
GLN   C    C  N N 176 
GLN   O    O  N N 177 
GLN   CB   C  N N 178 
GLN   CG   C  N N 179 
GLN   CD   C  N N 180 
GLN   OE1  O  N N 181 
GLN   NE2  N  N N 182 
GLN   OXT  O  N N 183 
GLN   H    H  N N 184 
GLN   H2   H  N N 185 
GLN   HA   H  N N 186 
GLN   HB2  H  N N 187 
GLN   HB3  H  N N 188 
GLN   HG2  H  N N 189 
GLN   HG3  H  N N 190 
GLN   HE21 H  N N 191 
GLN   HE22 H  N N 192 
GLN   HXT  H  N N 193 
GLU   N    N  N N 194 
GLU   CA   C  N S 195 
GLU   C    C  N N 196 
GLU   O    O  N N 197 
GLU   CB   C  N N 198 
GLU   CG   C  N N 199 
GLU   CD   C  N N 200 
GLU   OE1  O  N N 201 
GLU   OE2  O  N N 202 
GLU   OXT  O  N N 203 
GLU   H    H  N N 204 
GLU   H2   H  N N 205 
GLU   HA   H  N N 206 
GLU   HB2  H  N N 207 
GLU   HB3  H  N N 208 
GLU   HG2  H  N N 209 
GLU   HG3  H  N N 210 
GLU   HE2  H  N N 211 
GLU   HXT  H  N N 212 
GLY   N    N  N N 213 
GLY   CA   C  N N 214 
GLY   C    C  N N 215 
GLY   O    O  N N 216 
GLY   OXT  O  N N 217 
GLY   H    H  N N 218 
GLY   H2   H  N N 219 
GLY   HA2  H  N N 220 
GLY   HA3  H  N N 221 
GLY   HXT  H  N N 222 
HIS   N    N  N N 223 
HIS   CA   C  N S 224 
HIS   C    C  N N 225 
HIS   O    O  N N 226 
HIS   CB   C  N N 227 
HIS   CG   C  Y N 228 
HIS   ND1  N  Y N 229 
HIS   CD2  C  Y N 230 
HIS   CE1  C  Y N 231 
HIS   NE2  N  Y N 232 
HIS   OXT  O  N N 233 
HIS   H    H  N N 234 
HIS   H2   H  N N 235 
HIS   HA   H  N N 236 
HIS   HB2  H  N N 237 
HIS   HB3  H  N N 238 
HIS   HD1  H  N N 239 
HIS   HD2  H  N N 240 
HIS   HE1  H  N N 241 
HIS   HE2  H  N N 242 
HIS   HXT  H  N N 243 
HOH   O    O  N N 244 
HOH   H1   H  N N 245 
HOH   H2   H  N N 246 
ILE   N    N  N N 247 
ILE   CA   C  N S 248 
ILE   C    C  N N 249 
ILE   O    O  N N 250 
ILE   CB   C  N S 251 
ILE   CG1  C  N N 252 
ILE   CG2  C  N N 253 
ILE   CD1  C  N N 254 
ILE   OXT  O  N N 255 
ILE   H    H  N N 256 
ILE   H2   H  N N 257 
ILE   HA   H  N N 258 
ILE   HB   H  N N 259 
ILE   HG12 H  N N 260 
ILE   HG13 H  N N 261 
ILE   HG21 H  N N 262 
ILE   HG22 H  N N 263 
ILE   HG23 H  N N 264 
ILE   HD11 H  N N 265 
ILE   HD12 H  N N 266 
ILE   HD13 H  N N 267 
ILE   HXT  H  N N 268 
LEU   N    N  N N 269 
LEU   CA   C  N S 270 
LEU   C    C  N N 271 
LEU   O    O  N N 272 
LEU   CB   C  N N 273 
LEU   CG   C  N N 274 
LEU   CD1  C  N N 275 
LEU   CD2  C  N N 276 
LEU   OXT  O  N N 277 
LEU   H    H  N N 278 
LEU   H2   H  N N 279 
LEU   HA   H  N N 280 
LEU   HB2  H  N N 281 
LEU   HB3  H  N N 282 
LEU   HG   H  N N 283 
LEU   HD11 H  N N 284 
LEU   HD12 H  N N 285 
LEU   HD13 H  N N 286 
LEU   HD21 H  N N 287 
LEU   HD22 H  N N 288 
LEU   HD23 H  N N 289 
LEU   HXT  H  N N 290 
LYS   N    N  N N 291 
LYS   CA   C  N S 292 
LYS   C    C  N N 293 
LYS   O    O  N N 294 
LYS   CB   C  N N 295 
LYS   CG   C  N N 296 
LYS   CD   C  N N 297 
LYS   CE   C  N N 298 
LYS   NZ   N  N N 299 
LYS   OXT  O  N N 300 
LYS   H    H  N N 301 
LYS   H2   H  N N 302 
LYS   HA   H  N N 303 
LYS   HB2  H  N N 304 
LYS   HB3  H  N N 305 
LYS   HG2  H  N N 306 
LYS   HG3  H  N N 307 
LYS   HD2  H  N N 308 
LYS   HD3  H  N N 309 
LYS   HE2  H  N N 310 
LYS   HE3  H  N N 311 
LYS   HZ1  H  N N 312 
LYS   HZ2  H  N N 313 
LYS   HZ3  H  N N 314 
LYS   HXT  H  N N 315 
MET   N    N  N N 316 
MET   CA   C  N S 317 
MET   C    C  N N 318 
MET   O    O  N N 319 
MET   CB   C  N N 320 
MET   CG   C  N N 321 
MET   SD   S  N N 322 
MET   CE   C  N N 323 
MET   OXT  O  N N 324 
MET   H    H  N N 325 
MET   H2   H  N N 326 
MET   HA   H  N N 327 
MET   HB2  H  N N 328 
MET   HB3  H  N N 329 
MET   HG2  H  N N 330 
MET   HG3  H  N N 331 
MET   HE1  H  N N 332 
MET   HE2  H  N N 333 
MET   HE3  H  N N 334 
MET   HXT  H  N N 335 
PHE   N    N  N N 336 
PHE   CA   C  N S 337 
PHE   C    C  N N 338 
PHE   O    O  N N 339 
PHE   CB   C  N N 340 
PHE   CG   C  Y N 341 
PHE   CD1  C  Y N 342 
PHE   CD2  C  Y N 343 
PHE   CE1  C  Y N 344 
PHE   CE2  C  Y N 345 
PHE   CZ   C  Y N 346 
PHE   OXT  O  N N 347 
PHE   H    H  N N 348 
PHE   H2   H  N N 349 
PHE   HA   H  N N 350 
PHE   HB2  H  N N 351 
PHE   HB3  H  N N 352 
PHE   HD1  H  N N 353 
PHE   HD2  H  N N 354 
PHE   HE1  H  N N 355 
PHE   HE2  H  N N 356 
PHE   HZ   H  N N 357 
PHE   HXT  H  N N 358 
PRO   N    N  N N 359 
PRO   CA   C  N S 360 
PRO   C    C  N N 361 
PRO   O    O  N N 362 
PRO   CB   C  N N 363 
PRO   CG   C  N N 364 
PRO   CD   C  N N 365 
PRO   OXT  O  N N 366 
PRO   H    H  N N 367 
PRO   HA   H  N N 368 
PRO   HB2  H  N N 369 
PRO   HB3  H  N N 370 
PRO   HG2  H  N N 371 
PRO   HG3  H  N N 372 
PRO   HD2  H  N N 373 
PRO   HD3  H  N N 374 
PRO   HXT  H  N N 375 
SER   N    N  N N 376 
SER   CA   C  N S 377 
SER   C    C  N N 378 
SER   O    O  N N 379 
SER   CB   C  N N 380 
SER   OG   O  N N 381 
SER   OXT  O  N N 382 
SER   H    H  N N 383 
SER   H2   H  N N 384 
SER   HA   H  N N 385 
SER   HB2  H  N N 386 
SER   HB3  H  N N 387 
SER   HG   H  N N 388 
SER   HXT  H  N N 389 
THR   N    N  N N 390 
THR   CA   C  N S 391 
THR   C    C  N N 392 
THR   O    O  N N 393 
THR   CB   C  N R 394 
THR   OG1  O  N N 395 
THR   CG2  C  N N 396 
THR   OXT  O  N N 397 
THR   H    H  N N 398 
THR   H2   H  N N 399 
THR   HA   H  N N 400 
THR   HB   H  N N 401 
THR   HG1  H  N N 402 
THR   HG21 H  N N 403 
THR   HG22 H  N N 404 
THR   HG23 H  N N 405 
THR   HXT  H  N N 406 
TRP   N    N  N N 407 
TRP   CA   C  N S 408 
TRP   C    C  N N 409 
TRP   O    O  N N 410 
TRP   CB   C  N N 411 
TRP   CG   C  Y N 412 
TRP   CD1  C  Y N 413 
TRP   CD2  C  Y N 414 
TRP   NE1  N  Y N 415 
TRP   CE2  C  Y N 416 
TRP   CE3  C  Y N 417 
TRP   CZ2  C  Y N 418 
TRP   CZ3  C  Y N 419 
TRP   CH2  C  Y N 420 
TRP   OXT  O  N N 421 
TRP   H    H  N N 422 
TRP   H2   H  N N 423 
TRP   HA   H  N N 424 
TRP   HB2  H  N N 425 
TRP   HB3  H  N N 426 
TRP   HD1  H  N N 427 
TRP   HE1  H  N N 428 
TRP   HE3  H  N N 429 
TRP   HZ2  H  N N 430 
TRP   HZ3  H  N N 431 
TRP   HH2  H  N N 432 
TRP   HXT  H  N N 433 
TYR   N    N  N N 434 
TYR   CA   C  N S 435 
TYR   C    C  N N 436 
TYR   O    O  N N 437 
TYR   CB   C  N N 438 
TYR   CG   C  Y N 439 
TYR   CD1  C  Y N 440 
TYR   CD2  C  Y N 441 
TYR   CE1  C  Y N 442 
TYR   CE2  C  Y N 443 
TYR   CZ   C  Y N 444 
TYR   OH   O  N N 445 
TYR   OXT  O  N N 446 
TYR   H    H  N N 447 
TYR   H2   H  N N 448 
TYR   HA   H  N N 449 
TYR   HB2  H  N N 450 
TYR   HB3  H  N N 451 
TYR   HD1  H  N N 452 
TYR   HD2  H  N N 453 
TYR   HE1  H  N N 454 
TYR   HE2  H  N N 455 
TYR   HH   H  N N 456 
TYR   HXT  H  N N 457 
VAL   N    N  N N 458 
VAL   CA   C  N S 459 
VAL   C    C  N N 460 
VAL   O    O  N N 461 
VAL   CB   C  N N 462 
VAL   CG1  C  N N 463 
VAL   CG2  C  N N 464 
VAL   OXT  O  N N 465 
VAL   H    H  N N 466 
VAL   H2   H  N N 467 
VAL   HA   H  N N 468 
VAL   HB   H  N N 469 
VAL   HG11 H  N N 470 
VAL   HG12 H  N N 471 
VAL   HG13 H  N N 472 
VAL   HG21 H  N N 473 
VAL   HG22 H  N N 474 
VAL   HG23 H  N N 475 
VAL   HXT  H  N N 476 
YXY   C10  C  N N 477 
YXY   N01  N  N N 478 
YXY   C02  C  N N 479 
YXY   O03  O  N N 480 
YXY   C04  C  N N 481 
YXY   C05  C  N N 482 
YXY   C06  C  N N 483 
YXY   C07  C  N N 484 
YXY   F08  F  N N 485 
YXY   F09  F  N N 486 
YXY   C11  C  N N 487 
YXY   H1   H  N N 488 
YXY   H2   H  N N 489 
YXY   H3   H  N N 490 
YXY   H4   H  N N 491 
YXY   H5   H  N N 492 
YXY   H6   H  N N 493 
YXY   H7   H  N N 494 
YXY   H8   H  N N 495 
YXY   H9   H  N N 496 
YXY   H10  H  N N 497 
YXY   H11  H  N N 498 
# 
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 
005   C    CA   sing N N 1   
005   C    O    doub N N 2   
005   C    OXT  sing N N 3   
005   N    CB1  sing N N 4   
005   N    HN   sing N N 5   
005   N    HNA  sing N N 6   
005   CA   OB2  sing N N 7   
005   CA   HA   sing N N 8   
005   CD   CG   sing N N 9   
005   CG   HG   sing N N 10  
005   CG   HGA  sing N N 11  
005   CH   CZ1  doub Y N 12  
005   CH   CZ2  sing Y N 13  
005   CH   HH   sing N N 14  
005   CB1  CA   sing N N 15  
005   CB1  CG   sing N N 16  
005   CB1  HB1  sing N N 17  
005   OB2  HOB2 sing N N 18  
005   CE1  CD   doub Y N 19  
005   CE1  HE1  sing N N 20  
005   CE2  CD   sing Y N 21  
005   CE2  HE2  sing N N 22  
005   CZ1  CE1  sing Y N 23  
005   CZ1  HZ1  sing N N 24  
005   CZ2  CE2  doub Y N 25  
005   CZ2  HZ2  sing N N 26  
005   OXT  HXT  sing N N 27  
A1L3F C24  C25  doub Y N 28  
A1L3F C24  C22  sing Y N 29  
A1L3F C25  C19  sing Y N 30  
A1L3F CL23 C22  sing N N 31  
A1L3F N17  C18  sing N N 32  
A1L3F C22  C21  doub Y N 33  
A1L3F C19  C18  sing N N 34  
A1L3F C19  N20  doub Y N 35  
A1L3F C21  N20  sing Y N 36  
A1L3F C21  H1   sing N N 37  
A1L3F C24  H2   sing N N 38  
A1L3F C18  H3   sing N N 39  
A1L3F C18  H4   sing N N 40  
A1L3F C25  H5   sing N N 41  
A1L3F N17  H6   sing N N 42  
A1L3F N17  H7   sing N N 43  
ALA   N    CA   sing N N 44  
ALA   N    H    sing N N 45  
ALA   N    H2   sing N N 46  
ALA   CA   C    sing N N 47  
ALA   CA   CB   sing N N 48  
ALA   CA   HA   sing N N 49  
ALA   C    O    doub N N 50  
ALA   C    OXT  sing N N 51  
ALA   CB   HB1  sing N N 52  
ALA   CB   HB2  sing N N 53  
ALA   CB   HB3  sing N N 54  
ALA   OXT  HXT  sing N N 55  
ARG   N    CA   sing N N 56  
ARG   N    H    sing N N 57  
ARG   N    H2   sing N N 58  
ARG   CA   C    sing N N 59  
ARG   CA   CB   sing N N 60  
ARG   CA   HA   sing N N 61  
ARG   C    O    doub N N 62  
ARG   C    OXT  sing N N 63  
ARG   CB   CG   sing N N 64  
ARG   CB   HB2  sing N N 65  
ARG   CB   HB3  sing N N 66  
ARG   CG   CD   sing N N 67  
ARG   CG   HG2  sing N N 68  
ARG   CG   HG3  sing N N 69  
ARG   CD   NE   sing N N 70  
ARG   CD   HD2  sing N N 71  
ARG   CD   HD3  sing N N 72  
ARG   NE   CZ   sing N N 73  
ARG   NE   HE   sing N N 74  
ARG   CZ   NH1  sing N N 75  
ARG   CZ   NH2  doub N N 76  
ARG   NH1  HH11 sing N N 77  
ARG   NH1  HH12 sing N N 78  
ARG   NH2  HH21 sing N N 79  
ARG   NH2  HH22 sing N N 80  
ARG   OXT  HXT  sing N N 81  
ASN   N    CA   sing N N 82  
ASN   N    H    sing N N 83  
ASN   N    H2   sing N N 84  
ASN   CA   C    sing N N 85  
ASN   CA   CB   sing N N 86  
ASN   CA   HA   sing N N 87  
ASN   C    O    doub N N 88  
ASN   C    OXT  sing N N 89  
ASN   CB   CG   sing N N 90  
ASN   CB   HB2  sing N N 91  
ASN   CB   HB3  sing N N 92  
ASN   CG   OD1  doub N N 93  
ASN   CG   ND2  sing N N 94  
ASN   ND2  HD21 sing N N 95  
ASN   ND2  HD22 sing N N 96  
ASN   OXT  HXT  sing N N 97  
ASP   N    CA   sing N N 98  
ASP   N    H    sing N N 99  
ASP   N    H2   sing N N 100 
ASP   CA   C    sing N N 101 
ASP   CA   CB   sing N N 102 
ASP   CA   HA   sing N N 103 
ASP   C    O    doub N N 104 
ASP   C    OXT  sing N N 105 
ASP   CB   CG   sing N N 106 
ASP   CB   HB2  sing N N 107 
ASP   CB   HB3  sing N N 108 
ASP   CG   OD1  doub N N 109 
ASP   CG   OD2  sing N N 110 
ASP   OD2  HD2  sing N N 111 
ASP   OXT  HXT  sing N N 112 
CHG   N    CA   sing N N 113 
CHG   N    H    sing N N 114 
CHG   N    H2   sing N N 115 
CHG   C1   CA   sing N N 116 
CHG   CA   C    sing N N 117 
CHG   CA   HA   sing N N 118 
CHG   O    C    doub N N 119 
CHG   C    OXT  sing N N 120 
CHG   C6   C1   sing N N 121 
CHG   C2   C1   sing N N 122 
CHG   C1   H1   sing N N 123 
CHG   C3   C2   sing N N 124 
CHG   C2   H2B  sing N N 125 
CHG   C2   H2A  sing N N 126 
CHG   C4   C3   sing N N 127 
CHG   C3   H3   sing N N 128 
CHG   C3   H3A  sing N N 129 
CHG   C4   C5   sing N N 130 
CHG   C4   H4   sing N N 131 
CHG   C4   H4A  sing N N 132 
CHG   C5   C6   sing N N 133 
CHG   C5   H5   sing N N 134 
CHG   C5   H5A  sing N N 135 
CHG   C6   H6   sing N N 136 
CHG   C6   H6A  sing N N 137 
CHG   OXT  HXT  sing N N 138 
CYS   N    CA   sing N N 139 
CYS   N    H    sing N N 140 
CYS   N    H2   sing N N 141 
CYS   CA   C    sing N N 142 
CYS   CA   CB   sing N N 143 
CYS   CA   HA   sing N N 144 
CYS   C    O    doub N N 145 
CYS   C    OXT  sing N N 146 
CYS   CB   SG   sing N N 147 
CYS   CB   HB2  sing N N 148 
CYS   CB   HB3  sing N N 149 
CYS   SG   HG   sing N N 150 
CYS   OXT  HXT  sing N N 151 
FP9   C    O    doub N N 152 
FP9   C    CA   sing N N 153 
FP9   C    OXT  sing N N 154 
FP9   N    CA   sing N N 155 
FP9   N    CD   sing N N 156 
FP9   N    H    sing N N 157 
FP9   CA   CB   sing N N 158 
FP9   CA   HA   sing N N 159 
FP9   CB   CG   sing N N 160 
FP9   CB   HB   sing N N 161 
FP9   CB   HBA  sing N N 162 
FP9   CD   CG   sing N N 163 
FP9   CD   HD   sing N N 164 
FP9   CD   HDA  sing N N 165 
FP9   FD   CG   sing N N 166 
FP9   CG   HG   sing N N 167 
FP9   OXT  HXT  sing N N 168 
GLN   N    CA   sing N N 169 
GLN   N    H    sing N N 170 
GLN   N    H2   sing N N 171 
GLN   CA   C    sing N N 172 
GLN   CA   CB   sing N N 173 
GLN   CA   HA   sing N N 174 
GLN   C    O    doub N N 175 
GLN   C    OXT  sing N N 176 
GLN   CB   CG   sing N N 177 
GLN   CB   HB2  sing N N 178 
GLN   CB   HB3  sing N N 179 
GLN   CG   CD   sing N N 180 
GLN   CG   HG2  sing N N 181 
GLN   CG   HG3  sing N N 182 
GLN   CD   OE1  doub N N 183 
GLN   CD   NE2  sing N N 184 
GLN   NE2  HE21 sing N N 185 
GLN   NE2  HE22 sing N N 186 
GLN   OXT  HXT  sing N N 187 
GLU   N    CA   sing N N 188 
GLU   N    H    sing N N 189 
GLU   N    H2   sing N N 190 
GLU   CA   C    sing N N 191 
GLU   CA   CB   sing N N 192 
GLU   CA   HA   sing N N 193 
GLU   C    O    doub N N 194 
GLU   C    OXT  sing N N 195 
GLU   CB   CG   sing N N 196 
GLU   CB   HB2  sing N N 197 
GLU   CB   HB3  sing N N 198 
GLU   CG   CD   sing N N 199 
GLU   CG   HG2  sing N N 200 
GLU   CG   HG3  sing N N 201 
GLU   CD   OE1  doub N N 202 
GLU   CD   OE2  sing N N 203 
GLU   OE2  HE2  sing N N 204 
GLU   OXT  HXT  sing N N 205 
GLY   N    CA   sing N N 206 
GLY   N    H    sing N N 207 
GLY   N    H2   sing N N 208 
GLY   CA   C    sing N N 209 
GLY   CA   HA2  sing N N 210 
GLY   CA   HA3  sing N N 211 
GLY   C    O    doub N N 212 
GLY   C    OXT  sing N N 213 
GLY   OXT  HXT  sing N N 214 
HIS   N    CA   sing N N 215 
HIS   N    H    sing N N 216 
HIS   N    H2   sing N N 217 
HIS   CA   C    sing N N 218 
HIS   CA   CB   sing N N 219 
HIS   CA   HA   sing N N 220 
HIS   C    O    doub N N 221 
HIS   C    OXT  sing N N 222 
HIS   CB   CG   sing N N 223 
HIS   CB   HB2  sing N N 224 
HIS   CB   HB3  sing N N 225 
HIS   CG   ND1  sing Y N 226 
HIS   CG   CD2  doub Y N 227 
HIS   ND1  CE1  doub Y N 228 
HIS   ND1  HD1  sing N N 229 
HIS   CD2  NE2  sing Y N 230 
HIS   CD2  HD2  sing N N 231 
HIS   CE1  NE2  sing Y N 232 
HIS   CE1  HE1  sing N N 233 
HIS   NE2  HE2  sing N N 234 
HIS   OXT  HXT  sing N N 235 
HOH   O    H1   sing N N 236 
HOH   O    H2   sing N N 237 
ILE   N    CA   sing N N 238 
ILE   N    H    sing N N 239 
ILE   N    H2   sing N N 240 
ILE   CA   C    sing N N 241 
ILE   CA   CB   sing N N 242 
ILE   CA   HA   sing N N 243 
ILE   C    O    doub N N 244 
ILE   C    OXT  sing N N 245 
ILE   CB   CG1  sing N N 246 
ILE   CB   CG2  sing N N 247 
ILE   CB   HB   sing N N 248 
ILE   CG1  CD1  sing N N 249 
ILE   CG1  HG12 sing N N 250 
ILE   CG1  HG13 sing N N 251 
ILE   CG2  HG21 sing N N 252 
ILE   CG2  HG22 sing N N 253 
ILE   CG2  HG23 sing N N 254 
ILE   CD1  HD11 sing N N 255 
ILE   CD1  HD12 sing N N 256 
ILE   CD1  HD13 sing N N 257 
ILE   OXT  HXT  sing N N 258 
LEU   N    CA   sing N N 259 
LEU   N    H    sing N N 260 
LEU   N    H2   sing N N 261 
LEU   CA   C    sing N N 262 
LEU   CA   CB   sing N N 263 
LEU   CA   HA   sing N N 264 
LEU   C    O    doub N N 265 
LEU   C    OXT  sing N N 266 
LEU   CB   CG   sing N N 267 
LEU   CB   HB2  sing N N 268 
LEU   CB   HB3  sing N N 269 
LEU   CG   CD1  sing N N 270 
LEU   CG   CD2  sing N N 271 
LEU   CG   HG   sing N N 272 
LEU   CD1  HD11 sing N N 273 
LEU   CD1  HD12 sing N N 274 
LEU   CD1  HD13 sing N N 275 
LEU   CD2  HD21 sing N N 276 
LEU   CD2  HD22 sing N N 277 
LEU   CD2  HD23 sing N N 278 
LEU   OXT  HXT  sing N N 279 
LYS   N    CA   sing N N 280 
LYS   N    H    sing N N 281 
LYS   N    H2   sing N N 282 
LYS   CA   C    sing N N 283 
LYS   CA   CB   sing N N 284 
LYS   CA   HA   sing N N 285 
LYS   C    O    doub N N 286 
LYS   C    OXT  sing N N 287 
LYS   CB   CG   sing N N 288 
LYS   CB   HB2  sing N N 289 
LYS   CB   HB3  sing N N 290 
LYS   CG   CD   sing N N 291 
LYS   CG   HG2  sing N N 292 
LYS   CG   HG3  sing N N 293 
LYS   CD   CE   sing N N 294 
LYS   CD   HD2  sing N N 295 
LYS   CD   HD3  sing N N 296 
LYS   CE   NZ   sing N N 297 
LYS   CE   HE2  sing N N 298 
LYS   CE   HE3  sing N N 299 
LYS   NZ   HZ1  sing N N 300 
LYS   NZ   HZ2  sing N N 301 
LYS   NZ   HZ3  sing N N 302 
LYS   OXT  HXT  sing N N 303 
MET   N    CA   sing N N 304 
MET   N    H    sing N N 305 
MET   N    H2   sing N N 306 
MET   CA   C    sing N N 307 
MET   CA   CB   sing N N 308 
MET   CA   HA   sing N N 309 
MET   C    O    doub N N 310 
MET   C    OXT  sing N N 311 
MET   CB   CG   sing N N 312 
MET   CB   HB2  sing N N 313 
MET   CB   HB3  sing N N 314 
MET   CG   SD   sing N N 315 
MET   CG   HG2  sing N N 316 
MET   CG   HG3  sing N N 317 
MET   SD   CE   sing N N 318 
MET   CE   HE1  sing N N 319 
MET   CE   HE2  sing N N 320 
MET   CE   HE3  sing N N 321 
MET   OXT  HXT  sing N N 322 
PHE   N    CA   sing N N 323 
PHE   N    H    sing N N 324 
PHE   N    H2   sing N N 325 
PHE   CA   C    sing N N 326 
PHE   CA   CB   sing N N 327 
PHE   CA   HA   sing N N 328 
PHE   C    O    doub N N 329 
PHE   C    OXT  sing N N 330 
PHE   CB   CG   sing N N 331 
PHE   CB   HB2  sing N N 332 
PHE   CB   HB3  sing N N 333 
PHE   CG   CD1  doub Y N 334 
PHE   CG   CD2  sing Y N 335 
PHE   CD1  CE1  sing Y N 336 
PHE   CD1  HD1  sing N N 337 
PHE   CD2  CE2  doub Y N 338 
PHE   CD2  HD2  sing N N 339 
PHE   CE1  CZ   doub Y N 340 
PHE   CE1  HE1  sing N N 341 
PHE   CE2  CZ   sing Y N 342 
PHE   CE2  HE2  sing N N 343 
PHE   CZ   HZ   sing N N 344 
PHE   OXT  HXT  sing N N 345 
PRO   N    CA   sing N N 346 
PRO   N    CD   sing N N 347 
PRO   N    H    sing N N 348 
PRO   CA   C    sing N N 349 
PRO   CA   CB   sing N N 350 
PRO   CA   HA   sing N N 351 
PRO   C    O    doub N N 352 
PRO   C    OXT  sing N N 353 
PRO   CB   CG   sing N N 354 
PRO   CB   HB2  sing N N 355 
PRO   CB   HB3  sing N N 356 
PRO   CG   CD   sing N N 357 
PRO   CG   HG2  sing N N 358 
PRO   CG   HG3  sing N N 359 
PRO   CD   HD2  sing N N 360 
PRO   CD   HD3  sing N N 361 
PRO   OXT  HXT  sing N N 362 
SER   N    CA   sing N N 363 
SER   N    H    sing N N 364 
SER   N    H2   sing N N 365 
SER   CA   C    sing N N 366 
SER   CA   CB   sing N N 367 
SER   CA   HA   sing N N 368 
SER   C    O    doub N N 369 
SER   C    OXT  sing N N 370 
SER   CB   OG   sing N N 371 
SER   CB   HB2  sing N N 372 
SER   CB   HB3  sing N N 373 
SER   OG   HG   sing N N 374 
SER   OXT  HXT  sing N N 375 
THR   N    CA   sing N N 376 
THR   N    H    sing N N 377 
THR   N    H2   sing N N 378 
THR   CA   C    sing N N 379 
THR   CA   CB   sing N N 380 
THR   CA   HA   sing N N 381 
THR   C    O    doub N N 382 
THR   C    OXT  sing N N 383 
THR   CB   OG1  sing N N 384 
THR   CB   CG2  sing N N 385 
THR   CB   HB   sing N N 386 
THR   OG1  HG1  sing N N 387 
THR   CG2  HG21 sing N N 388 
THR   CG2  HG22 sing N N 389 
THR   CG2  HG23 sing N N 390 
THR   OXT  HXT  sing N N 391 
TRP   N    CA   sing N N 392 
TRP   N    H    sing N N 393 
TRP   N    H2   sing N N 394 
TRP   CA   C    sing N N 395 
TRP   CA   CB   sing N N 396 
TRP   CA   HA   sing N N 397 
TRP   C    O    doub N N 398 
TRP   C    OXT  sing N N 399 
TRP   CB   CG   sing N N 400 
TRP   CB   HB2  sing N N 401 
TRP   CB   HB3  sing N N 402 
TRP   CG   CD1  doub Y N 403 
TRP   CG   CD2  sing Y N 404 
TRP   CD1  NE1  sing Y N 405 
TRP   CD1  HD1  sing N N 406 
TRP   CD2  CE2  doub Y N 407 
TRP   CD2  CE3  sing Y N 408 
TRP   NE1  CE2  sing Y N 409 
TRP   NE1  HE1  sing N N 410 
TRP   CE2  CZ2  sing Y N 411 
TRP   CE3  CZ3  doub Y N 412 
TRP   CE3  HE3  sing N N 413 
TRP   CZ2  CH2  doub Y N 414 
TRP   CZ2  HZ2  sing N N 415 
TRP   CZ3  CH2  sing Y N 416 
TRP   CZ3  HZ3  sing N N 417 
TRP   CH2  HH2  sing N N 418 
TRP   OXT  HXT  sing N N 419 
TYR   N    CA   sing N N 420 
TYR   N    H    sing N N 421 
TYR   N    H2   sing N N 422 
TYR   CA   C    sing N N 423 
TYR   CA   CB   sing N N 424 
TYR   CA   HA   sing N N 425 
TYR   C    O    doub N N 426 
TYR   C    OXT  sing N N 427 
TYR   CB   CG   sing N N 428 
TYR   CB   HB2  sing N N 429 
TYR   CB   HB3  sing N N 430 
TYR   CG   CD1  doub Y N 431 
TYR   CG   CD2  sing Y N 432 
TYR   CD1  CE1  sing Y N 433 
TYR   CD1  HD1  sing N N 434 
TYR   CD2  CE2  doub Y N 435 
TYR   CD2  HD2  sing N N 436 
TYR   CE1  CZ   doub Y N 437 
TYR   CE1  HE1  sing N N 438 
TYR   CE2  CZ   sing Y N 439 
TYR   CE2  HE2  sing N N 440 
TYR   CZ   OH   sing N N 441 
TYR   OH   HH   sing N N 442 
TYR   OXT  HXT  sing N N 443 
VAL   N    CA   sing N N 444 
VAL   N    H    sing N N 445 
VAL   N    H2   sing N N 446 
VAL   CA   C    sing N N 447 
VAL   CA   CB   sing N N 448 
VAL   CA   HA   sing N N 449 
VAL   C    O    doub N N 450 
VAL   C    OXT  sing N N 451 
VAL   CB   CG1  sing N N 452 
VAL   CB   CG2  sing N N 453 
VAL   CB   HB   sing N N 454 
VAL   CG1  HG11 sing N N 455 
VAL   CG1  HG12 sing N N 456 
VAL   CG1  HG13 sing N N 457 
VAL   CG2  HG21 sing N N 458 
VAL   CG2  HG22 sing N N 459 
VAL   CG2  HG23 sing N N 460 
VAL   OXT  HXT  sing N N 461 
YXY   C06  C05  sing N N 462 
YXY   C06  C07  sing N N 463 
YXY   N01  C02  sing N N 464 
YXY   C05  C04  sing N N 465 
YXY   O03  C02  doub N N 466 
YXY   C02  C04  sing N N 467 
YXY   F09  C07  sing N N 468 
YXY   C07  C10  sing N N 469 
YXY   C07  F08  sing N N 470 
YXY   C04  C11  sing N N 471 
YXY   C10  C11  sing N N 472 
YXY   C10  H1   sing N N 473 
YXY   C10  H2   sing N N 474 
YXY   N01  H3   sing N N 475 
YXY   N01  H4   sing N N 476 
YXY   C04  H5   sing N N 477 
YXY   C05  H6   sing N N 478 
YXY   C05  H7   sing N N 479 
YXY   C06  H8   sing N N 480 
YXY   C06  H9   sing N N 481 
YXY   C11  H10  sing N N 482 
YXY   C11  H11  sing N N 483 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Technology (MoST, China)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2022YFC2303700 
_pdbx_audit_support.ordinal                1 
# 
_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   7C7P 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IZB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008916 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001776 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018618 
_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]   0.023039 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
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    . SER   A 1 1   ? -1.254  4.890   38.023  1.00 34.06  ? 1   SER   A N    1 
ATOM   2    C  CA   . SER   A 1 1   ? -1.967  6.006   37.402  1.00 39.46  ? 1   SER   A CA   1 
ATOM   3    C  C    . SER   A 1 1   ? -1.898  5.955   35.877  1.00 47.15  ? 1   SER   A C    1 
ATOM   4    O  O    . SER   A 1 1   ? -1.699  4.892   35.277  1.00 43.24  ? 1   SER   A O    1 
ATOM   5    C  CB   . SER   A 1 1   ? -1.407  7.352   37.862  1.00 39.52  ? 1   SER   A CB   1 
ATOM   6    O  OG   . SER   A 1 1   ? -1.684  7.615   39.221  1.00 47.59  ? 1   SER   A OG   1 
ATOM   7    N  N    . GLY   A 1 2   ? -2.046  7.123   35.261  1.00 41.68  ? 2   GLY   A N    1 
ATOM   8    C  CA   . GLY   A 1 2   ? -2.033  7.251   33.821  1.00 42.95  ? 2   GLY   A CA   1 
ATOM   9    C  C    . GLY   A 1 2   ? -3.396  6.988   33.206  1.00 48.90  ? 2   GLY   A C    1 
ATOM   10   O  O    . GLY   A 1 2   ? -4.281  6.380   33.812  1.00 47.18  ? 2   GLY   A O    1 
ATOM   11   N  N    . PHE   A 1 3   ? -3.560  7.451   31.965  1.00 50.05  ? 3   PHE   A N    1 
ATOM   12   C  CA   . PHE   A 1 3   ? -4.846  7.264   31.291  1.00 48.90  ? 3   PHE   A CA   1 
ATOM   13   C  C    . PHE   A 1 3   ? -4.610  7.290   29.777  1.00 50.99  ? 3   PHE   A C    1 
ATOM   14   O  O    . PHE   A 1 3   ? -4.647  8.358   29.165  1.00 54.09  ? 3   PHE   A O    1 
ATOM   15   C  CB   . PHE   A 1 3   ? -5.844  8.321   31.716  1.00 47.84  ? 3   PHE   A CB   1 
ATOM   16   C  CG   . PHE   A 1 3   ? -7.272  7.917   31.514  1.00 47.81  ? 3   PHE   A CG   1 
ATOM   17   C  CD1  . PHE   A 1 3   ? -7.953  7.209   32.492  1.00 46.28  ? 3   PHE   A CD1  1 
ATOM   18   C  CD2  . PHE   A 1 3   ? -7.935  8.232   30.340  1.00 46.60  ? 3   PHE   A CD2  1 
ATOM   19   C  CE1  . PHE   A 1 3   ? -9.265  6.828   32.305  1.00 43.07  ? 3   PHE   A CE1  1 
ATOM   20   C  CE2  . PHE   A 1 3   ? -9.254  7.855   30.147  1.00 45.34  ? 3   PHE   A CE2  1 
ATOM   21   C  CZ   . PHE   A 1 3   ? -9.921  7.155   31.130  1.00 43.26  ? 3   PHE   A CZ   1 
ATOM   22   N  N    . ARG   A 1 4   ? -4.497  6.099   29.206  1.00 51.32  ? 4   ARG   A N    1 
ATOM   23   C  CA   . ARG   A 1 4   ? -4.241  5.988   27.759  1.00 47.14  ? 4   ARG   A CA   1 
ATOM   24   C  C    . ARG   A 1 4   ? -5.415  5.282   27.108  1.00 47.58  ? 4   ARG   A C    1 
ATOM   25   O  O    . ARG   A 1 4   ? -6.166  4.634   27.827  1.00 47.58  ? 4   ARG   A O    1 
ATOM   26   C  CB   . ARG   A 1 4   ? -3.006  5.109   27.571  1.00 46.16  ? 4   ARG   A CB   1 
ATOM   27   C  CG   . ARG   A 1 4   ? -1.698  5.745   28.005  1.00 45.85  ? 4   ARG   A CG   1 
ATOM   28   C  CD   . ARG   A 1 4   ? -1.012  6.413   26.836  1.00 52.25  ? 4   ARG   A CD   1 
ATOM   29   N  NE   . ARG   A 1 4   ? 0.414   6.497   27.102  1.00 57.86  ? 4   ARG   A NE   1 
ATOM   30   C  CZ   . ARG   A 1 4   ? 1.303   7.009   26.267  1.00 56.98  ? 4   ARG   A CZ   1 
ATOM   31   N  NH1  . ARG   A 1 4   ? 0.916   7.489   25.100  1.00 60.67  ? 4   ARG   A NH1  1 
ATOM   32   N  NH2  . ARG   A 1 4   ? 2.577   7.037   26.602  1.00 53.00  ? 4   ARG   A NH2  1 
ATOM   33   N  N    . LYS   A 1 5   ? -5.611  5.476   25.809  1.00 45.61  ? 5   LYS   A N    1 
ATOM   34   C  CA   . LYS   A 1 5   ? -6.608  4.672   25.106  1.00 44.54  ? 5   LYS   A CA   1 
ATOM   35   C  C    . LYS   A 1 5   ? -6.158  3.216   25.146  1.00 46.34  ? 5   LYS   A C    1 
ATOM   36   O  O    . LYS   A 1 5   ? -5.150  2.846   24.528  1.00 39.89  ? 5   LYS   A O    1 
ATOM   37   C  CB   . LYS   A 1 5   ? -6.842  5.119   23.662  1.00 35.33  ? 5   LYS   A CB   1 
ATOM   38   C  CG   . LYS   A 1 5   ? -7.752  6.309   23.484  1.00 37.85  ? 5   LYS   A CG   1 
ATOM   39   C  CD   . LYS   A 1 5   ? -8.236  6.452   22.039  1.00 44.30  ? 5   LYS   A CD   1 
ATOM   40   C  CE   . LYS   A 1 5   ? -8.623  7.895   21.668  1.00 48.77  ? 5   LYS   A CE   1 
ATOM   41   N  NZ   . LYS   A 1 5   ? -9.606  8.553   22.586  1.00 50.73  ? 5   LYS   A NZ   1 
ATOM   42   N  N    . MET   A 1 6   ? -6.895  2.399   25.897  1.00 42.12  ? 6   MET   A N    1 
ATOM   43   C  CA   . MET   A 1 6   ? -6.668  0.969   25.921  1.00 38.95  ? 6   MET   A CA   1 
ATOM   44   C  C    . MET   A 1 6   ? -7.599  0.260   24.965  1.00 40.41  ? 6   MET   A C    1 
ATOM   45   O  O    . MET   A 1 6   ? -8.737  0.683   24.748  1.00 43.18  ? 6   MET   A O    1 
ATOM   46   C  CB   . MET   A 1 6   ? -6.892  0.397   27.302  1.00 38.44  ? 6   MET   A CB   1 
ATOM   47   C  CG   . MET   A 1 6   ? -5.732  0.579   28.183  1.00 45.43  ? 6   MET   A CG   1 
ATOM   48   S  SD   . MET   A 1 6   ? -6.149  -0.015  29.821  1.00 45.17  ? 6   MET   A SD   1 
ATOM   49   C  CE   . MET   A 1 6   ? -4.995  0.981   30.708  1.00 35.90  ? 6   MET   A CE   1 
ATOM   50   N  N    . ALA   A 1 7   ? -7.102  -0.830  24.399  1.00 33.75  ? 7   ALA   A N    1 
ATOM   51   C  CA   . ALA   A 1 7   ? -7.940  -1.799  23.723  1.00 36.63  ? 7   ALA   A CA   1 
ATOM   52   C  C    . ALA   A 1 7   ? -8.006  -3.053  24.580  1.00 37.70  ? 7   ALA   A C    1 
ATOM   53   O  O    . ALA   A 1 7   ? -7.170  -3.273  25.460  1.00 38.02  ? 7   ALA   A O    1 
ATOM   54   C  CB   . ALA   A 1 7   ? -7.402  -2.131  22.323  1.00 34.65  ? 7   ALA   A CB   1 
ATOM   55   N  N    . PHE   A 1 8   ? -9.015  -3.871  24.331  1.00 37.10  ? 8   PHE   A N    1 
ATOM   56   C  CA   . PHE   A 1 8   ? -9.058  -5.152  25.000  1.00 34.82  ? 8   PHE   A CA   1 
ATOM   57   C  C    . PHE   A 1 8   ? -7.890  -6.005  24.522  1.00 36.80  ? 8   PHE   A C    1 
ATOM   58   O  O    . PHE   A 1 8   ? -7.344  -5.773  23.435  1.00 39.78  ? 8   PHE   A O    1 
ATOM   59   C  CB   . PHE   A 1 8   ? -10.369 -5.862  24.703  1.00 40.47  ? 8   PHE   A CB   1 
ATOM   60   C  CG   . PHE   A 1 8   ? -11.556 -5.186  25.296  1.00 44.54  ? 8   PHE   A CG   1 
ATOM   61   C  CD1  . PHE   A 1 8   ? -11.843 -5.308  26.646  1.00 49.53  ? 8   PHE   A CD1  1 
ATOM   62   C  CD2  . PHE   A 1 8   ? -12.367 -4.402  24.514  1.00 42.30  ? 8   PHE   A CD2  1 
ATOM   63   C  CE1  . PHE   A 1 8   ? -12.935 -4.674  27.197  1.00 50.69  ? 8   PHE   A CE1  1 
ATOM   64   C  CE2  . PHE   A 1 8   ? -13.436 -3.776  25.056  1.00 47.64  ? 8   PHE   A CE2  1 
ATOM   65   C  CZ   . PHE   A 1 8   ? -13.728 -3.908  26.402  1.00 51.23  ? 8   PHE   A CZ   1 
ATOM   66   N  N    . PRO   A 1 9   ? -7.459  -6.968  25.328  1.00 39.02  ? 9   PRO   A N    1 
ATOM   67   C  CA   . PRO   A 1 9   ? -6.577  -8.028  24.813  1.00 37.26  ? 9   PRO   A CA   1 
ATOM   68   C  C    . PRO   A 1 9   ? -7.208  -8.720  23.602  1.00 34.81  ? 9   PRO   A C    1 
ATOM   69   O  O    . PRO   A 1 9   ? -8.380  -9.107  23.632  1.00 32.46  ? 9   PRO   A O    1 
ATOM   70   C  CB   . PRO   A 1 9   ? -6.442  -8.967  26.023  1.00 34.68  ? 9   PRO   A CB   1 
ATOM   71   C  CG   . PRO   A 1 9   ? -6.569  -8.023  27.210  1.00 35.05  ? 9   PRO   A CG   1 
ATOM   72   C  CD   . PRO   A 1 9   ? -7.629  -7.039  26.796  1.00 35.95  ? 9   PRO   A CD   1 
ATOM   73   N  N    . SER   A 1 10  ? -6.437  -8.855  22.511  1.00 33.27  ? 10  SER   A N    1 
ATOM   74   C  CA   . SER   A 1 10  ? -7.006  -9.257  21.215  1.00 36.62  ? 10  SER   A CA   1 
ATOM   75   C  C    . SER   A 1 10  ? -6.906  -10.753 20.928  1.00 35.96  ? 10  SER   A C    1 
ATOM   76   O  O    . SER   A 1 10  ? -7.419  -11.204 19.900  1.00 35.47  ? 10  SER   A O    1 
ATOM   77   C  CB   . SER   A 1 10  ? -6.343  -8.498  20.046  1.00 32.20  ? 10  SER   A CB   1 
ATOM   78   O  OG   . SER   A 1 10  ? -4.943  -8.728  19.977  1.00 30.75  ? 10  SER   A OG   1 
ATOM   79   N  N    . GLY   A 1 11  ? -6.264  -11.529 21.801  1.00 36.24  ? 11  GLY   A N    1 
ATOM   80   C  CA   . GLY   A 1 11  ? -5.968  -12.910 21.468  1.00 34.46  ? 11  GLY   A CA   1 
ATOM   81   C  C    . GLY   A 1 11  ? -7.196  -13.704 21.087  1.00 36.36  ? 11  GLY   A C    1 
ATOM   82   O  O    . GLY   A 1 11  ? -7.165  -14.501 20.142  1.00 37.02  ? 11  GLY   A O    1 
ATOM   83   N  N    . LYS   A 1 12  ? -8.296  -13.493 21.809  1.00 35.90  ? 12  LYS   A N    1 
ATOM   84   C  CA   . LYS   A 1 12  ? -9.499  -14.266 21.549  1.00 37.76  ? 12  LYS   A CA   1 
ATOM   85   C  C    . LYS   A 1 12  ? -9.984  -14.044 20.128  1.00 38.98  ? 12  LYS   A C    1 
ATOM   86   O  O    . LYS   A 1 12  ? -10.368 -14.999 19.441  1.00 40.21  ? 12  LYS   A O    1 
ATOM   87   C  CB   . LYS   A 1 12  ? -10.571 -13.909 22.576  1.00 37.95  ? 12  LYS   A CB   1 
ATOM   88   C  CG   . LYS   A 1 12  ? -10.304 -14.574 23.909  1.00 35.39  ? 12  LYS   A CG   1 
ATOM   89   C  CD   . LYS   A 1 12  ? -11.224 -14.069 25.004  1.00 42.28  ? 12  LYS   A CD   1 
ATOM   90   C  CE   . LYS   A 1 12  ? -10.873 -14.745 26.317  1.00 40.86  ? 12  LYS   A CE   1 
ATOM   91   N  NZ   . LYS   A 1 12  ? -11.859 -14.393 27.361  1.00 49.96  ? 12  LYS   A NZ   1 
ATOM   92   N  N    . VAL   A 1 13  ? -9.902  -12.799 19.649  1.00 44.64  ? 13  VAL   A N    1 
ATOM   93   C  CA   . VAL   A 1 13  ? -10.354 -12.464 18.301  1.00 44.43  ? 13  VAL   A CA   1 
ATOM   94   C  C    . VAL   A 1 13  ? -9.309  -12.819 17.238  1.00 39.33  ? 13  VAL   A C    1 
ATOM   95   O  O    . VAL   A 1 13  ? -9.669  -13.101 16.093  1.00 44.32  ? 13  VAL   A O    1 
ATOM   96   C  CB   . VAL   A 1 13  ? -10.744 -10.979 18.248  1.00 43.54  ? 13  VAL   A CB   1 
ATOM   97   C  CG1  . VAL   A 1 13  ? -11.338 -10.632 16.884  1.00 39.14  ? 13  VAL   A CG1  1 
ATOM   98   C  CG2  . VAL   A 1 13  ? -11.717 -10.652 19.406  1.00 39.15  ? 13  VAL   A CG2  1 
ATOM   99   N  N    . GLU   A 1 14  ? -8.019  -12.831 17.579  1.00 34.64  ? 14  GLU   A N    1 
ATOM   100  C  CA   . GLU   A 1 14  ? -7.009  -13.223 16.602  1.00 36.87  ? 14  GLU   A CA   1 
ATOM   101  C  C    . GLU   A 1 14  ? -7.281  -14.626 16.054  1.00 43.09  ? 14  GLU   A C    1 
ATOM   102  O  O    . GLU   A 1 14  ? -7.352  -14.836 14.834  1.00 40.76  ? 14  GLU   A O    1 
ATOM   103  C  CB   . GLU   A 1 14  ? -5.625  -13.149 17.236  1.00 33.64  ? 14  GLU   A CB   1 
ATOM   104  C  CG   . GLU   A 1 14  ? -5.200  -11.753 17.567  1.00 35.01  ? 14  GLU   A CG   1 
ATOM   105  C  CD   . GLU   A 1 14  ? -3.885  -11.687 18.325  1.00 32.88  ? 14  GLU   A CD   1 
ATOM   106  O  OE1  . GLU   A 1 14  ? -3.766  -10.824 19.205  1.00 37.34  ? 14  GLU   A OE1  1 
ATOM   107  O  OE2  . GLU   A 1 14  ? -2.963  -12.470 18.053  1.00 33.71  ? 14  GLU   A OE2  1 
ATOM   108  N  N    . GLY   A 1 15  ? -7.455  -15.599 16.941  1.00 42.66  ? 15  GLY   A N    1 
ATOM   109  C  CA   . GLY   A 1 15  ? -7.733  -16.955 16.527  1.00 39.89  ? 15  GLY   A CA   1 
ATOM   110  C  C    . GLY   A 1 15  ? -9.047  -17.132 15.796  1.00 43.19  ? 15  GLY   A C    1 
ATOM   111  O  O    . GLY   A 1 15  ? -9.493  -18.265 15.612  1.00 46.26  ? 15  GLY   A O    1 
ATOM   112  N  N    . CYS   A 1 16  ? -9.684  -16.038 15.377  1.00 41.20  ? 16  CYS   A N    1 
ATOM   113  C  CA   . CYS   A 1 16  ? -10.866 -16.123 14.533  1.00 45.24  ? 16  CYS   A CA   1 
ATOM   114  C  C    . CYS   A 1 16  ? -10.708 -15.437 13.181  1.00 47.92  ? 16  CYS   A C    1 
ATOM   115  O  O    . CYS   A 1 16  ? -11.650 -15.470 12.378  1.00 49.51  ? 16  CYS   A O    1 
ATOM   116  C  CB   . CYS   A 1 16  ? -12.086 -15.539 15.247  1.00 44.22  ? 16  CYS   A CB   1 
ATOM   117  S  SG   . CYS   A 1 16  ? -12.333 -16.201 16.880  1.00 47.79  ? 16  CYS   A SG   1 
ATOM   118  N  N    . MET   A 1 17  ? -9.558  -14.838 12.887  1.00 44.34  ? 17  MET   A N    1 
ATOM   119  C  CA   . MET   A 1 17  ? -9.400  -14.115 11.632  1.00 46.26  ? 17  MET   A CA   1 
ATOM   120  C  C    . MET   A 1 17  ? -8.863  -15.041 10.553  1.00 51.50  ? 17  MET   A C    1 
ATOM   121  O  O    . MET   A 1 17  ? -7.860  -15.738 10.757  1.00 53.14  ? 17  MET   A O    1 
ATOM   122  C  CB   . MET   A 1 17  ? -8.500  -12.888 11.805  1.00 41.90  ? 17  MET   A CB   1 
ATOM   123  C  CG   . MET   A 1 17  ? -9.017  -12.001 12.901  1.00 39.18  ? 17  MET   A CG   1 
ATOM   124  S  SD   . MET   A 1 17  ? -10.706 -11.409 12.573  1.00 36.03  ? 17  MET   A SD   1 
ATOM   125  C  CE   . MET   A 1 17  ? -10.708 -11.121 10.792  1.00 44.53  ? 17  MET   A CE   1 
ATOM   126  N  N    . VAL   A 1 18  ? -9.551  -15.047 9.409   1.00 48.02  ? 18  VAL   A N    1 
ATOM   127  C  CA   . VAL   A 1 18  ? -9.220  -15.906 8.283   1.00 53.05  ? 18  VAL   A CA   1 
ATOM   128  C  C    . VAL   A 1 18  ? -9.100  -15.053 7.032   1.00 48.11  ? 18  VAL   A C    1 
ATOM   129  O  O    . VAL   A 1 18  ? -9.481  -13.881 7.003   1.00 43.90  ? 18  VAL   A O    1 
ATOM   130  C  CB   . VAL   A 1 18  ? -10.257 -17.033 8.054   1.00 52.36  ? 18  VAL   A CB   1 
ATOM   131  C  CG1  . VAL   A 1 18  ? -10.263 -17.998 9.200   1.00 50.61  ? 18  VAL   A CG1  1 
ATOM   132  C  CG2  . VAL   A 1 18  ? -11.642 -16.436 7.888   1.00 49.55  ? 18  VAL   A CG2  1 
ATOM   133  N  N    . GLN   A 1 19  ? -8.557  -15.677 5.995   1.00 50.57  ? 19  GLN   A N    1 
ATOM   134  C  CA   . GLN   A 1 19  ? -8.435  -15.096 4.673   1.00 50.28  ? 19  GLN   A CA   1 
ATOM   135  C  C    . GLN   A 1 19  ? -9.496  -15.710 3.772   1.00 53.16  ? 19  GLN   A C    1 
ATOM   136  O  O    . GLN   A 1 19  ? -9.624  -16.935 3.709   1.00 60.68  ? 19  GLN   A O    1 
ATOM   137  C  CB   . GLN   A 1 19  ? -7.040  -15.356 4.122   1.00 53.70  ? 19  GLN   A CB   1 
ATOM   138  C  CG   . GLN   A 1 19  ? -6.816  -14.883 2.707   1.00 56.70  ? 19  GLN   A CG   1 
ATOM   139  C  CD   . GLN   A 1 19  ? -5.355  -14.946 2.328   1.00 56.32  ? 19  GLN   A CD   1 
ATOM   140  O  OE1  . GLN   A 1 19  ? -4.517  -15.354 3.140   1.00 55.70  ? 19  GLN   A OE1  1 
ATOM   141  N  NE2  . GLN   A 1 19  ? -5.027  -14.482 1.119   1.00 54.14  ? 19  GLN   A NE2  1 
ATOM   142  N  N    . VAL   A 1 20  ? -10.262 -14.868 3.088   1.00 47.28  ? 20  VAL   A N    1 
ATOM   143  C  CA   . VAL   A 1 20  ? -11.334 -15.331 2.215   1.00 49.77  ? 20  VAL   A CA   1 
ATOM   144  C  C    . VAL   A 1 20  ? -11.131 -14.753 0.824   1.00 49.99  ? 20  VAL   A C    1 
ATOM   145  O  O    . VAL   A 1 20  ? -10.770 -13.580 0.671   1.00 49.78  ? 20  VAL   A O    1 
ATOM   146  C  CB   . VAL   A 1 20  ? -12.724 -14.959 2.766   1.00 51.52  ? 20  VAL   A CB   1 
ATOM   147  C  CG1  . VAL   A 1 20  ? -13.811 -15.390 1.789   1.00 50.99  ? 20  VAL   A CG1  1 
ATOM   148  C  CG2  . VAL   A 1 20  ? -12.942 -15.615 4.143   1.00 49.77  ? 20  VAL   A CG2  1 
ATOM   149  N  N    . THR   A 1 21  ? -11.352 -15.585 -0.191  1.00 54.98  ? 21  THR   A N    1 
ATOM   150  C  CA   . THR   A 1 21  ? -11.140 -15.167 -1.569  1.00 53.44  ? 21  THR   A CA   1 
ATOM   151  C  C    . THR   A 1 21  ? -12.285 -15.665 -2.439  1.00 55.07  ? 21  THR   A C    1 
ATOM   152  O  O    . THR   A 1 21  ? -12.667 -16.835 -2.362  1.00 55.65  ? 21  THR   A O    1 
ATOM   153  C  CB   . THR   A 1 21  ? -9.798  -15.680 -2.103  1.00 46.72  ? 21  THR   A CB   1 
ATOM   154  O  OG1  . THR   A 1 21  ? -8.761  -15.362 -1.174  1.00 43.60  ? 21  THR   A OG1  1 
ATOM   155  C  CG2  . THR   A 1 21  ? -9.482  -14.996 -3.410  1.00 57.53  ? 21  THR   A CG2  1 
ATOM   156  N  N    . CYS   A 1 22  ? -12.845 -14.771 -3.250  1.00 54.21  ? 22  CYS   A N    1 
ATOM   157  C  CA   . CYS   A 1 22  ? -13.851 -15.134 -4.242  1.00 57.27  ? 22  CYS   A CA   1 
ATOM   158  C  C    . CYS   A 1 22  ? -13.427 -14.494 -5.552  1.00 57.90  ? 22  CYS   A C    1 
ATOM   159  O  O    . CYS   A 1 22  ? -13.374 -13.262 -5.656  1.00 60.57  ? 22  CYS   A O    1 
ATOM   160  C  CB   . CYS   A 1 22  ? -15.262 -14.683 -3.822  1.00 55.33  ? 22  CYS   A CB   1 
ATOM   161  S  SG   . CYS   A 1 22  ? -16.638 -15.238 -4.908  1.00 62.21  ? 22  CYS   A SG   1 
ATOM   162  N  N    . GLY   A 1 23  ? -13.110 -15.320 -6.538  1.00 61.68  ? 23  GLY   A N    1 
ATOM   163  C  CA   . GLY   A 1 23  ? -12.382 -14.800 -7.678  1.00 55.77  ? 23  GLY   A CA   1 
ATOM   164  C  C    . GLY   A 1 23  ? -11.020 -14.298 -7.217  1.00 64.19  ? 23  GLY   A C    1 
ATOM   165  O  O    . GLY   A 1 23  ? -10.235 -15.036 -6.613  1.00 60.98  ? 23  GLY   A O    1 
ATOM   166  N  N    . THR   A 1 24  ? -10.723 -13.025 -7.490  1.00 77.51  ? 24  THR   A N    1 
ATOM   167  C  CA   . THR   A 1 24  ? -9.435  -12.424 -7.151  1.00 74.34  ? 24  THR   A CA   1 
ATOM   168  C  C    . THR   A 1 24  ? -9.560  -11.406 -6.029  1.00 76.74  ? 24  THR   A C    1 
ATOM   169  O  O    . THR   A 1 24  ? -8.591  -10.700 -5.716  1.00 77.51  ? 24  THR   A O    1 
ATOM   170  C  CB   . THR   A 1 24  ? -8.804  -11.769 -8.384  1.00 71.55  ? 24  THR   A CB   1 
ATOM   171  O  OG1  . THR   A 1 24  ? -9.599  -10.645 -8.796  1.00 70.28  ? 24  THR   A OG1  1 
ATOM   172  C  CG2  . THR   A 1 24  ? -8.700  -12.784 -9.529  1.00 67.77  ? 24  THR   A CG2  1 
ATOM   173  N  N    . THR   A 1 25  ? -10.731 -11.304 -5.424  1.00 65.38  ? 25  THR   A N    1 
ATOM   174  C  CA   . THR   A 1 25  ? -10.924 -10.429 -4.281  1.00 63.64  ? 25  THR   A CA   1 
ATOM   175  C  C    . THR   A 1 25  ? -10.518 -11.197 -3.028  1.00 52.96  ? 25  THR   A C    1 
ATOM   176  O  O    . THR   A 1 25  ? -11.039 -12.285 -2.774  1.00 52.99  ? 25  THR   A O    1 
ATOM   177  C  CB   . THR   A 1 25  ? -12.377 -9.960  -4.232  1.00 60.84  ? 25  THR   A CB   1 
ATOM   178  O  OG1  . THR   A 1 25  ? -12.712 -9.346  -5.493  1.00 59.98  ? 25  THR   A OG1  1 
ATOM   179  C  CG2  . THR   A 1 25  ? -12.582 -8.965  -3.106  1.00 53.58  ? 25  THR   A CG2  1 
ATOM   180  N  N    . THR   A 1 26  ? -9.531  -10.681 -2.301  1.00 50.80  ? 26  THR   A N    1 
ATOM   181  C  CA   . THR   A 1 26  ? -9.138  -11.224 -1.003  1.00 54.74  ? 26  THR   A CA   1 
ATOM   182  C  C    . THR   A 1 26  ? -9.471  -10.191 0.069   1.00 48.84  ? 26  THR   A C    1 
ATOM   183  O  O    . THR   A 1 26  ? -9.022  -9.040  -0.008  1.00 44.37  ? 26  THR   A O    1 
ATOM   184  C  CB   . THR   A 1 26  ? -7.649  -11.606 -0.944  1.00 52.63  ? 26  THR   A CB   1 
ATOM   185  O  OG1  . THR   A 1 26  ? -6.835  -10.440 -0.725  1.00 52.95  ? 26  THR   A OG1  1 
ATOM   186  C  CG2  . THR   A 1 26  ? -7.210  -12.303 -2.218  1.00 57.29  ? 26  THR   A CG2  1 
ATOM   187  N  N    . LEU   A 1 27  ? -10.283 -10.603 1.038   1.00 44.27  ? 27  LEU   A N    1 
ATOM   188  C  CA   . LEU   A 1 27  ? -10.580 -9.825  2.234   1.00 46.03  ? 27  LEU   A CA   1 
ATOM   189  C  C    . LEU   A 1 27  ? -10.647 -10.746 3.445   1.00 42.15  ? 27  LEU   A C    1 
ATOM   190  O  O    . LEU   A 1 27  ? -10.656 -11.975 3.327   1.00 41.68  ? 27  LEU   A O    1 
ATOM   191  C  CB   . LEU   A 1 27  ? -11.885 -9.014  2.100   1.00 43.56  ? 27  LEU   A CB   1 
ATOM   192  C  CG   . LEU   A 1 27  ? -13.191 -9.688  1.658   1.00 41.83  ? 27  LEU   A CG   1 
ATOM   193  C  CD1  . LEU   A 1 27  ? -13.841 -10.532 2.684   1.00 39.48  ? 27  LEU   A CD1  1 
ATOM   194  C  CD2  . LEU   A 1 27  ? -14.161 -8.575  1.318   1.00 40.28  ? 27  LEU   A CD2  1 
ATOM   195  N  N    . ASN   A 1 28  ? -10.713 -10.128 4.624   1.00 45.71  ? 28  ASN   A N    1 
ATOM   196  C  CA   . ASN   A 1 28  ? -10.680 -10.861 5.883   1.00 40.31  ? 28  ASN   A CA   1 
ATOM   197  C  C    . ASN   A 1 28  ? -12.066 -11.406 6.234   1.00 41.46  ? 28  ASN   A C    1 
ATOM   198  O  O    . ASN   A 1 28  ? -13.095 -10.782 5.939   1.00 35.64  ? 28  ASN   A O    1 
ATOM   199  C  CB   . ASN   A 1 28  ? -10.186 -9.952  7.011   1.00 42.51  ? 28  ASN   A CB   1 
ATOM   200  C  CG   . ASN   A 1 28  ? -8.936  -9.135  6.642   1.00 38.26  ? 28  ASN   A CG   1 
ATOM   201  O  OD1  . ASN   A 1 28  ? -7.809  -9.641  6.720   1.00 32.89  ? 28  ASN   A OD1  1 
ATOM   202  N  ND2  . ASN   A 1 28  ? -9.134  -7.847  6.301   1.00 32.20  ? 28  ASN   A ND2  1 
ATOM   203  N  N    . GLY   A 1 29  ? -12.091 -12.580 6.878   1.00 41.67  ? 29  GLY   A N    1 
ATOM   204  C  CA   . GLY   A 1 29  ? -13.317 -13.105 7.448   1.00 41.74  ? 29  GLY   A CA   1 
ATOM   205  C  C    . GLY   A 1 29  ? -13.198 -13.428 8.924   1.00 41.26  ? 29  GLY   A C    1 
ATOM   206  O  O    . GLY   A 1 29  ? -12.102 -13.562 9.472   1.00 41.21  ? 29  GLY   A O    1 
ATOM   207  N  N    . LEU   A 1 30  ? -14.371 -13.597 9.572   1.00 44.83  ? 30  LEU   A N    1 
ATOM   208  C  CA   . LEU   A 1 30  ? -14.499 -13.939 10.996  1.00 40.06  ? 30  LEU   A CA   1 
ATOM   209  C  C    . LEU   A 1 30  ? -15.067 -15.354 11.157  1.00 42.80  ? 30  LEU   A C    1 
ATOM   210  O  O    . LEU   A 1 30  ? -16.273 -15.570 10.986  1.00 41.91  ? 30  LEU   A O    1 
ATOM   211  C  CB   . LEU   A 1 30  ? -15.388 -12.926 11.727  1.00 38.21  ? 30  LEU   A CB   1 
ATOM   212  C  CG   . LEU   A 1 30  ? -15.494 -13.075 13.266  1.00 40.57  ? 30  LEU   A CG   1 
ATOM   213  C  CD1  . LEU   A 1 30  ? -14.206 -12.691 14.007  1.00 36.51  ? 30  LEU   A CD1  1 
ATOM   214  C  CD2  . LEU   A 1 30  ? -16.696 -12.345 13.852  1.00 36.94  ? 30  LEU   A CD2  1 
ATOM   215  N  N    . TRP   A 1 31  ? -14.208 -16.303 11.541  1.00 44.50  ? 31  TRP   A N    1 
ATOM   216  C  CA   . TRP   A 1 31  ? -14.576 -17.713 11.674  1.00 47.44  ? 31  TRP   A CA   1 
ATOM   217  C  C    . TRP   A 1 31  ? -15.001 -18.015 13.111  1.00 47.30  ? 31  TRP   A C    1 
ATOM   218  O  O    . TRP   A 1 31  ? -14.190 -17.898 14.037  1.00 48.75  ? 31  TRP   A O    1 
ATOM   219  C  CB   . TRP   A 1 31  ? -13.394 -18.593 11.264  1.00 47.94  ? 31  TRP   A CB   1 
ATOM   220  C  CG   . TRP   A 1 31  ? -13.599 -20.101 11.350  1.00 49.95  ? 31  TRP   A CG   1 
ATOM   221  C  CD1  . TRP   A 1 31  ? -14.787 -20.789 11.354  1.00 53.62  ? 31  TRP   A CD1  1 
ATOM   222  C  CD2  . TRP   A 1 31  ? -12.568 -21.093 11.416  1.00 49.47  ? 31  TRP   A CD2  1 
ATOM   223  N  NE1  . TRP   A 1 31  ? -14.552 -22.148 11.428  1.00 52.98  ? 31  TRP   A NE1  1 
ATOM   224  C  CE2  . TRP   A 1 31  ? -13.199 -22.357 11.466  1.00 51.90  ? 31  TRP   A CE2  1 
ATOM   225  C  CE3  . TRP   A 1 31  ? -11.170 -21.033 11.450  1.00 46.25  ? 31  TRP   A CE3  1 
ATOM   226  C  CZ2  . TRP   A 1 31  ? -12.483 -23.540 11.541  1.00 54.83  ? 31  TRP   A CZ2  1 
ATOM   227  C  CZ3  . TRP   A 1 31  ? -10.461 -22.206 11.527  1.00 48.93  ? 31  TRP   A CZ3  1 
ATOM   228  C  CH2  . TRP   A 1 31  ? -11.117 -23.446 11.571  1.00 56.01  ? 31  TRP   A CH2  1 
ATOM   229  N  N    . LEU   A 1 32  ? -16.263 -18.414 13.290  1.00 45.53  ? 32  LEU   A N    1 
ATOM   230  C  CA   . LEU   A 1 32  ? -16.837 -18.687 14.608  1.00 45.43  ? 32  LEU   A CA   1 
ATOM   231  C  C    . LEU   A 1 32  ? -17.744 -19.900 14.495  1.00 50.24  ? 32  LEU   A C    1 
ATOM   232  O  O    . LEU   A 1 32  ? -18.765 -19.837 13.804  1.00 50.26  ? 32  LEU   A O    1 
ATOM   233  C  CB   . LEU   A 1 32  ? -17.640 -17.493 15.142  1.00 48.29  ? 32  LEU   A CB   1 
ATOM   234  C  CG   . LEU   A 1 32  ? -16.997 -16.142 15.502  1.00 46.00  ? 32  LEU   A CG   1 
ATOM   235  C  CD1  . LEU   A 1 32  ? -18.105 -15.142 15.763  1.00 40.15  ? 32  LEU   A CD1  1 
ATOM   236  C  CD2  . LEU   A 1 32  ? -16.036 -16.212 16.690  1.00 42.16  ? 32  LEU   A CD2  1 
ATOM   237  N  N    . ASP   A 1 33  ? -17.393 -20.981 15.193  1.00 52.34  ? 33  ASP   A N    1 
ATOM   238  C  CA   . ASP   A 1 33  ? -18.041 -22.295 15.039  1.00 54.36  ? 33  ASP   A CA   1 
ATOM   239  C  C    . ASP   A 1 33  ? -17.741 -22.754 13.609  1.00 57.39  ? 33  ASP   A C    1 
ATOM   240  O  O    . ASP   A 1 33  ? -16.579 -22.659 13.174  1.00 52.62  ? 33  ASP   A O    1 
ATOM   241  C  CB   . ASP   A 1 33  ? -19.521 -22.201 15.444  1.00 51.94  ? 33  ASP   A CB   1 
ATOM   242  C  CG   . ASP   A 1 33  ? -19.706 -21.579 16.848  1.00 50.28  ? 33  ASP   A CG   1 
ATOM   243  O  OD1  . ASP   A 1 33  ? -18.710 -21.563 17.582  1.00 51.29  ? 33  ASP   A OD1  1 
ATOM   244  O  OD2  . ASP   A 1 33  ? -20.817 -21.120 17.230  1.00 42.42  ? 33  ASP   A OD2  1 
ATOM   245  N  N    . ASP   A 1 34  ? -18.719 -23.257 12.845  1.00 60.99  ? 34  ASP   A N    1 
ATOM   246  C  CA   . ASP   A 1 34  ? -18.497 -23.671 11.461  1.00 62.15  ? 34  ASP   A CA   1 
ATOM   247  C  C    . ASP   A 1 34  ? -19.011 -22.645 10.451  1.00 63.34  ? 34  ASP   A C    1 
ATOM   248  O  O    . ASP   A 1 34  ? -19.511 -23.016 9.386   1.00 68.12  ? 34  ASP   A O    1 
ATOM   249  C  CB   . ASP   A 1 34  ? -19.145 -25.027 11.174  1.00 69.25  ? 34  ASP   A CB   1 
ATOM   250  C  CG   . ASP   A 1 34  ? -20.629 -25.066 11.528  1.00 69.55  ? 34  ASP   A CG   1 
ATOM   251  O  OD1  . ASP   A 1 34  ? -21.141 -24.109 12.148  1.00 69.78  ? 34  ASP   A OD1  1 
ATOM   252  O  OD2  . ASP   A 1 34  ? -21.297 -26.052 11.149  1.00 72.70  ? 34  ASP   A OD2  1 
ATOM   253  N  N    . VAL   A 1 35  ? -18.917 -21.360 10.763  1.00 57.29  ? 35  VAL   A N    1 
ATOM   254  C  CA   . VAL   A 1 35  ? -19.383 -20.302 9.882   1.00 52.45  ? 35  VAL   A CA   1 
ATOM   255  C  C    . VAL   A 1 35  ? -18.266 -19.282 9.758   1.00 49.37  ? 35  VAL   A C    1 
ATOM   256  O  O    . VAL   A 1 35  ? -17.566 -19.003 10.737  1.00 50.07  ? 35  VAL   A O    1 
ATOM   257  C  CB   . VAL   A 1 35  ? -20.678 -19.651 10.409  1.00 53.79  ? 35  VAL   A CB   1 
ATOM   258  C  CG1  . VAL   A 1 35  ? -21.230 -18.690 9.386   1.00 53.64  ? 35  VAL   A CG1  1 
ATOM   259  C  CG2  . VAL   A 1 35  ? -21.715 -20.722 10.741  1.00 51.03  ? 35  VAL   A CG2  1 
ATOM   260  N  N    . VAL   A 1 36  ? -18.069 -18.759 8.554   1.00 47.97  ? 36  VAL   A N    1 
ATOM   261  C  CA   . VAL   A 1 36  ? -17.010 -17.797 8.276   1.00 48.21  ? 36  VAL   A CA   1 
ATOM   262  C  C    . VAL   A 1 36  ? -17.675 -16.547 7.727   1.00 49.87  ? 36  VAL   A C    1 
ATOM   263  O  O    . VAL   A 1 36  ? -18.226 -16.562 6.617   1.00 48.40  ? 36  VAL   A O    1 
ATOM   264  C  CB   . VAL   A 1 36  ? -15.960 -18.337 7.297   1.00 48.43  ? 36  VAL   A CB   1 
ATOM   265  C  CG1  . VAL   A 1 36  ? -15.083 -17.213 6.829   1.00 45.78  ? 36  VAL   A CG1  1 
ATOM   266  C  CG2  . VAL   A 1 36  ? -15.109 -19.401 7.963   1.00 50.63  ? 36  VAL   A CG2  1 
ATOM   267  N  N    . TYR   A 1 37  ? -17.617 -15.466 8.503   1.00 48.36  ? 37  TYR   A N    1 
ATOM   268  C  CA   . TYR   A 1 37  ? -18.339 -14.232 8.230   1.00 42.50  ? 37  TYR   A CA   1 
ATOM   269  C  C    . TYR   A 1 37  ? -17.413 -13.258 7.515   1.00 41.01  ? 37  TYR   A C    1 
ATOM   270  O  O    . TYR   A 1 37  ? -16.269 -13.078 7.942   1.00 39.19  ? 37  TYR   A O    1 
ATOM   271  C  CB   . TYR   A 1 37  ? -18.845 -13.604 9.534   1.00 45.69  ? 37  TYR   A CB   1 
ATOM   272  C  CG   . TYR   A 1 37  ? -19.824 -14.459 10.308  1.00 44.84  ? 37  TYR   A CG   1 
ATOM   273  C  CD1  . TYR   A 1 37  ? -19.376 -15.486 11.125  1.00 39.55  ? 37  TYR   A CD1  1 
ATOM   274  C  CD2  . TYR   A 1 37  ? -21.195 -14.235 10.216  1.00 45.20  ? 37  TYR   A CD2  1 
ATOM   275  C  CE1  . TYR   A 1 37  ? -20.262 -16.281 11.814  1.00 47.07  ? 37  TYR   A CE1  1 
ATOM   276  C  CE2  . TYR   A 1 37  ? -22.094 -15.020 10.911  1.00 48.29  ? 37  TYR   A CE2  1 
ATOM   277  C  CZ   . TYR   A 1 37  ? -21.622 -16.048 11.713  1.00 52.01  ? 37  TYR   A CZ   1 
ATOM   278  O  OH   . TYR   A 1 37  ? -22.497 -16.846 12.429  1.00 56.93  ? 37  TYR   A OH   1 
ATOM   279  N  N    . CYS   A 1 38  ? -17.922 -12.622 6.470   1.00 45.89  ? 38  CYS   A N    1 
ATOM   280  C  CA   . CYS   A 1 38  ? -17.133 -11.645 5.694   1.00 39.81  ? 38  CYS   A CA   1 
ATOM   281  C  C    . CYS   A 1 38  ? -18.056 -10.649 5.059   1.00 36.16  ? 38  CYS   A C    1 
ATOM   282  O  O    . CYS   A 1 38  ? -19.290 -10.843 4.977   1.00 35.89  ? 38  CYS   A O    1 
ATOM   283  C  CB   . CYS   A 1 38  ? -16.256 -12.364 4.650   1.00 41.18  ? 38  CYS   A CB   1 
ATOM   284  S  SG   . CYS   A 1 38  ? -17.103 -13.086 3.183   1.00 42.05  ? 38  CYS   A SG   1 
ATOM   285  N  N    . PRO   A 1 39  ? -17.536 -9.517  4.583   1.00 35.09  ? 39  PRO   A N    1 
ATOM   286  C  CA   . PRO   A 1 39  ? -18.345 -8.574  3.813   1.00 39.04  ? 39  PRO   A CA   1 
ATOM   287  C  C    . PRO   A 1 39  ? -18.784 -9.168  2.476   1.00 40.55  ? 39  PRO   A C    1 
ATOM   288  O  O    . PRO   A 1 39  ? -18.072 -9.964  1.861   1.00 41.92  ? 39  PRO   A O    1 
ATOM   289  C  CB   . PRO   A 1 39  ? -17.401 -7.385  3.605   1.00 41.57  ? 39  PRO   A CB   1 
ATOM   290  C  CG   . PRO   A 1 39  ? -16.368 -7.517  4.730   1.00 37.67  ? 39  PRO   A CG   1 
ATOM   291  C  CD   . PRO   A 1 39  ? -16.174 -8.993  4.848   1.00 33.83  ? 39  PRO   A CD   1 
ATOM   292  N  N    . ARG   A 1 40  ? -19.967 -8.759  2.015   1.00 39.72  ? 40  ARG   A N    1 
ATOM   293  C  CA   . ARG   A 1 40  ? -20.556 -9.422  0.855   1.00 45.60  ? 40  ARG   A CA   1 
ATOM   294  C  C    . ARG   A 1 40  ? -19.913 -9.009  -0.469  1.00 48.40  ? 40  ARG   A C    1 
ATOM   295  O  O    . ARG   A 1 40  ? -20.029 -9.753  -1.449  1.00 44.51  ? 40  ARG   A O    1 
ATOM   296  C  CB   . ARG   A 1 40  ? -22.074 -9.179  0.790   1.00 44.06  ? 40  ARG   A CB   1 
ATOM   297  C  CG   . ARG   A 1 40  ? -22.509 -7.768  0.381   1.00 41.46  ? 40  ARG   A CG   1 
ATOM   298  C  CD   . ARG   A 1 40  ? -23.977 -7.728  0.030   1.00 38.30  ? 40  ARG   A CD   1 
ATOM   299  N  NE   . ARG   A 1 40  ? -24.483 -6.359  0.031   1.00 38.00  ? 40  ARG   A NE   1 
ATOM   300  C  CZ   . ARG   A 1 40  ? -25.750 -6.030  -0.219  1.00 40.39  ? 40  ARG   A CZ   1 
ATOM   301  N  NH1  . ARG   A 1 40  ? -26.645 -6.971  -0.497  1.00 40.32  ? 40  ARG   A NH1  1 
ATOM   302  N  NH2  . ARG   A 1 40  ? -26.124 -4.757  -0.202  1.00 40.33  ? 40  ARG   A NH2  1 
ATOM   303  N  N    . HIS   A 1 41  ? -19.214 -7.844  -0.521  1.00 48.09  ? 41  HIS   A N    1 
ATOM   304  C  CA   . HIS   A 1 41  ? -18.553 -7.404  -1.749  1.00 43.27  ? 41  HIS   A CA   1 
ATOM   305  C  C    . HIS   A 1 41  ? -17.336 -8.239  -2.075  1.00 48.68  ? 41  HIS   A C    1 
ATOM   306  O  O    . HIS   A 1 41  ? -16.581 -7.902  -3.015  1.00 51.49  ? 41  HIS   A O    1 
ATOM   307  C  CB   . HIS   A 1 41  ? -18.191 -5.916  -1.671  1.00 38.94  ? 41  HIS   A CB   1 
ATOM   308  C  CG   . HIS   A 1 41  ? -17.230 -5.552  -0.579  1.00 44.17  ? 41  HIS   A CG   1 
ATOM   309  N  ND1  . HIS   A 1 41  ? -17.633 -4.941  0.595   1.00 43.72  ? 41  HIS   A ND1  1 
ATOM   310  C  CD2  . HIS   A 1 41  ? -15.876 -5.613  -0.522  1.00 44.57  ? 41  HIS   A CD2  1 
ATOM   311  C  CE1  . HIS   A 1 41  ? -16.576 -4.695  1.350   1.00 40.97  ? 41  HIS   A CE1  1 
ATOM   312  N  NE2  . HIS   A 1 41  ? -15.496 -5.090  0.695   1.00 44.06  ? 41  HIS   A NE2  1 
ATOM   313  N  N    . VAL   A 1 42  ? -17.146 -9.331  -1.325  1.00 47.87  ? 42  VAL   A N    1 
ATOM   314  C  CA   . VAL   A 1 42  ? -16.120 -10.305 -1.690  1.00 53.86  ? 42  VAL   A CA   1 
ATOM   315  C  C    . VAL   A 1 42  ? -16.415 -10.899 -3.056  1.00 50.27  ? 42  VAL   A C    1 
ATOM   316  O  O    . VAL   A 1 42  ? -15.494 -11.267 -3.790  1.00 50.45  ? 42  VAL   A O    1 
ATOM   317  C  CB   . VAL   A 1 42  ? -16.003 -11.412 -0.621  1.00 48.18  ? 42  VAL   A CB   1 
ATOM   318  C  CG1  . VAL   A 1 42  ? -17.210 -12.348 -0.661  1.00 43.78  ? 42  VAL   A CG1  1 
ATOM   319  C  CG2  . VAL   A 1 42  ? -14.696 -12.184 -0.794  1.00 46.84  ? 42  VAL   A CG2  1 
ATOM   320  N  N    . ILE   A 1 43  ? -17.695 -11.000 -3.416  1.00 49.75  ? 43  ILE   A N    1 
ATOM   321  C  CA   . ILE   A 1 43  ? -18.089 -11.597 -4.682  1.00 53.36  ? 43  ILE   A CA   1 
ATOM   322  C  C    . ILE   A 1 43  ? -17.892 -10.652 -5.862  1.00 56.50  ? 43  ILE   A C    1 
ATOM   323  O  O    . ILE   A 1 43  ? -17.917 -11.106 -7.009  1.00 65.03  ? 43  ILE   A O    1 
ATOM   324  C  CB   . ILE   A 1 43  ? -19.552 -12.068 -4.610  1.00 54.81  ? 43  ILE   A CB   1 
ATOM   325  C  CG1  . ILE   A 1 43  ? -20.525 -10.892 -4.614  1.00 55.54  ? 43  ILE   A CG1  1 
ATOM   326  C  CG2  . ILE   A 1 43  ? -19.793 -12.868 -3.356  1.00 57.88  ? 43  ILE   A CG2  1 
ATOM   327  C  CD1  . ILE   A 1 43  ? -21.972 -11.318 -4.315  1.00 54.56  ? 43  ILE   A CD1  1 
ATOM   328  N  N    . CYS   A 1 44  ? -17.663 -9.362  -5.620  1.00 59.57  ? 44  CYS   A N    1 
ATOM   329  C  CA   . CYS   A 1 44  ? -17.645 -8.368  -6.690  1.00 62.65  ? 44  CYS   A CA   1 
ATOM   330  C  C    . CYS   A 1 44  ? -16.288 -8.246  -7.374  1.00 65.26  ? 44  CYS   A C    1 
ATOM   331  O  O    . CYS   A 1 44  ? -15.235 -8.265  -6.730  1.00 59.81  ? 44  CYS   A O    1 
ATOM   332  C  CB   . CYS   A 1 44  ? -18.038 -6.998  -6.143  1.00 61.20  ? 44  CYS   A CB   1 
ATOM   333  S  SG   . CYS   A 1 44  ? -19.670 -6.961  -5.489  1.00 66.81  ? 44  CYS   A SG   1 
ATOM   334  N  N    . THR   A 1 45  ? -16.323 -8.087  -8.693  1.00 73.43  ? 45  THR   A N    1 
ATOM   335  C  CA   . THR   A 1 45  ? -15.142 -7.633  -9.405  1.00 82.15  ? 45  THR   A CA   1 
ATOM   336  C  C    . THR   A 1 45  ? -15.017 -6.123  -9.228  1.00 89.18  ? 45  THR   A C    1 
ATOM   337  O  O    . THR   A 1 45  ? -15.874 -5.468  -8.627  1.00 86.33  ? 45  THR   A O    1 
ATOM   338  C  CB   . THR   A 1 45  ? -15.215 -8.006  -10.886 1.00 85.85  ? 45  THR   A CB   1 
ATOM   339  O  OG1  . THR   A 1 45  ? -16.083 -7.095  -11.579 1.00 88.24  ? 45  THR   A OG1  1 
ATOM   340  C  CG2  . THR   A 1 45  ? -15.757 -9.416  -11.049 1.00 83.30  ? 45  THR   A CG2  1 
ATOM   341  N  N    . SER   A 1 46  ? -13.944 -5.552  -9.775  1.00 107.88 ? 46  SER   A N    1 
ATOM   342  C  CA   . SER   A 1 46  ? -13.727 -4.116  -9.630  1.00 105.04 ? 46  SER   A CA   1 
ATOM   343  C  C    . SER   A 1 46  ? -14.778 -3.306  -10.384 1.00 98.25  ? 46  SER   A C    1 
ATOM   344  O  O    . SER   A 1 46  ? -15.222 -2.259  -9.901  1.00 100.23 ? 46  SER   A O    1 
ATOM   345  C  CB   . SER   A 1 46  ? -12.326 -3.762  -10.109 1.00 102.03 ? 46  SER   A CB   1 
ATOM   346  O  OG   . SER   A 1 46  ? -12.040 -4.428  -11.326 1.00 102.64 ? 46  SER   A OG   1 
ATOM   347  N  N    . GLU   A 1 47  ? -15.194 -3.772  -11.562 1.00 90.53  ? 47  GLU   A N    1 
ATOM   348  C  CA   . GLU   A 1 47  ? -16.138 -2.993  -12.356 1.00 88.91  ? 47  GLU   A CA   1 
ATOM   349  C  C    . GLU   A 1 47  ? -17.544 -3.048  -11.780 1.00 85.16  ? 47  GLU   A C    1 
ATOM   350  O  O    . GLU   A 1 47  ? -18.338 -2.124  -12.000 1.00 78.95  ? 47  GLU   A O    1 
ATOM   351  N  N    . ASP   A 1 48  ? -17.870 -4.118  -11.051 1.00 84.65  ? 48  ASP   A N    1 
ATOM   352  C  CA   . ASP   A 1 48  ? -19.205 -4.256  -10.484 1.00 87.94  ? 48  ASP   A CA   1 
ATOM   353  C  C    . ASP   A 1 48  ? -19.453 -3.285  -9.337  1.00 88.02  ? 48  ASP   A C    1 
ATOM   354  O  O    . ASP   A 1 48  ? -20.612 -2.977  -9.040  1.00 87.85  ? 48  ASP   A O    1 
ATOM   355  C  CB   . ASP   A 1 48  ? -19.439 -5.681  -9.966  1.00 84.70  ? 48  ASP   A CB   1 
ATOM   356  C  CG   . ASP   A 1 48  ? -19.218 -6.745  -11.020 1.00 88.93  ? 48  ASP   A CG   1 
ATOM   357  O  OD1  . ASP   A 1 48  ? -19.188 -6.408  -12.226 1.00 93.24  ? 48  ASP   A OD1  1 
ATOM   358  O  OD2  . ASP   A 1 48  ? -19.094 -7.932  -10.636 1.00 86.71  ? 48  ASP   A OD2  1 
ATOM   359  N  N    . MET   A 1 49  ? -18.407 -2.800  -8.690  1.00 85.36  ? 49  MET   A N    1 
ATOM   360  C  CA   . MET   A 1 49  ? -18.621 -2.125  -7.412  1.00 84.68  ? 49  MET   A CA   1 
ATOM   361  C  C    . MET   A 1 49  ? -19.240 -0.738  -7.549  1.00 82.41  ? 49  MET   A C    1 
ATOM   362  O  O    . MET   A 1 49  ? -19.284 -0.008  -6.542  1.00 72.21  ? 49  MET   A O    1 
ATOM   363  C  CB   . MET   A 1 49  ? -17.296 -2.060  -6.648  1.00 78.53  ? 49  MET   A CB   1 
ATOM   364  C  CG   . MET   A 1 49  ? -16.922 -3.407  -6.009  1.00 76.55  ? 49  MET   A CG   1 
ATOM   365  S  SD   . MET   A 1 49  ? -15.213 -3.574  -5.423  1.00 77.57  ? 49  MET   A SD   1 
ATOM   366  C  CE   . MET   A 1 49  ? -15.375 -4.884  -4.207  1.00 59.23  ? 49  MET   A CE   1 
ATOM   367  N  N    . LEU   A 1 50  ? -19.749 -0.339  -8.716  1.00 86.37  ? 50  LEU   A N    1 
ATOM   368  C  CA   . LEU   A 1 50  ? -20.331 0.997   -8.823  1.00 87.16  ? 50  LEU   A CA   1 
ATOM   369  C  C    . LEU   A 1 50  ? -21.742 0.926   -8.233  1.00 82.39  ? 50  LEU   A C    1 
ATOM   370  O  O    . LEU   A 1 50  ? -22.006 1.455   -7.149  1.00 75.72  ? 50  LEU   A O    1 
ATOM   371  C  CB   . LEU   A 1 50  ? -20.315 1.462   -10.285 1.00 86.59  ? 50  LEU   A CB   1 
ATOM   372  C  CG   . LEU   A 1 50  ? -20.375 2.976   -10.586 1.00 97.58  ? 50  LEU   A CG   1 
ATOM   373  C  CD1  . LEU   A 1 50  ? -19.792 3.276   -11.999 1.00 98.01  ? 50  LEU   A CD1  1 
ATOM   374  C  CD2  . LEU   A 1 50  ? -21.710 3.714   -10.310 1.00 82.15  ? 50  LEU   A CD2  1 
ATOM   375  N  N    . ASN   A 1 51  ? -22.563 0.091   -8.860  1.00 80.54  ? 51  ASN   A N    1 
ATOM   376  C  CA   . ASN   A 1 51  ? -23.902 -0.221  -8.312  1.00 74.89  ? 51  ASN   A CA   1 
ATOM   377  C  C    . ASN   A 1 51  ? -24.122 -1.697  -8.640  1.00 75.01  ? 51  ASN   A C    1 
ATOM   378  O  O    . ASN   A 1 51  ? -24.492 -1.999  -9.775  1.00 78.76  ? 51  ASN   A O    1 
ATOM   379  C  CB   . ASN   A 1 51  ? -24.995 0.677   -8.883  1.00 83.75  ? 51  ASN   A CB   1 
ATOM   380  C  CG   . ASN   A 1 51  ? -26.309 0.547   -8.142  1.00 81.84  ? 51  ASN   A CG   1 
ATOM   381  O  OD1  . ASN   A 1 51  ? -26.499 -0.376  -7.356  1.00 78.24  ? 51  ASN   A OD1  1 
ATOM   382  N  ND2  . ASN   A 1 51  ? -27.226 1.468   -8.385  1.00 89.10  ? 51  ASN   A ND2  1 
ATOM   383  N  N    . PRO   A 1 52  ? -23.824 -2.637  -7.732  1.00 71.85  ? 52  PRO   A N    1 
ATOM   384  C  CA   . PRO   A 1 52  ? -23.953 -4.048  -8.030  1.00 62.87  ? 52  PRO   A CA   1 
ATOM   385  C  C    . PRO   A 1 52  ? -25.210 -4.755  -7.527  1.00 55.50  ? 52  PRO   A C    1 
ATOM   386  O  O    . PRO   A 1 52  ? -25.574 -4.544  -6.415  1.00 59.41  ? 52  PRO   A O    1 
ATOM   387  C  CB   . PRO   A 1 52  ? -22.811 -4.658  -7.207  1.00 61.72  ? 52  PRO   A CB   1 
ATOM   388  C  CG   . PRO   A 1 52  ? -22.287 -3.562  -6.296  1.00 66.91  ? 52  PRO   A CG   1 
ATOM   389  C  CD   . PRO   A 1 52  ? -23.247 -2.404  -6.420  1.00 69.26  ? 52  PRO   A CD   1 
ATOM   390  N  N    . ASN   A 1 53  ? -25.829 -5.588  -8.357  1.00 54.43  ? 53  ASN   A N    1 
ATOM   391  C  CA   . ASN   A 1 53  ? -26.950 -6.421  -7.849  1.00 53.92  ? 53  ASN   A CA   1 
ATOM   392  C  C    . ASN   A 1 53  ? -26.288 -7.635  -7.216  1.00 56.06  ? 53  ASN   A C    1 
ATOM   393  O  O    . ASN   A 1 53  ? -25.946 -8.564  -7.939  1.00 57.24  ? 53  ASN   A O    1 
ATOM   394  C  CB   . ASN   A 1 53  ? -28.004 -6.764  -8.897  1.00 49.56  ? 53  ASN   A CB   1 
ATOM   395  C  CG   . ASN   A 1 53  ? -29.374 -6.979  -8.296  1.00 53.79  ? 53  ASN   A CG   1 
ATOM   396  O  OD1  . ASN   A 1 53  ? -29.511 -7.664  -7.290  1.00 62.97  ? 53  ASN   A OD1  1 
ATOM   397  N  ND2  . ASN   A 1 53  ? -30.394 -6.397  -8.904  1.00 44.79  ? 53  ASN   A ND2  1 
ATOM   398  N  N    . TYR   A 1 54  ? -26.128 -7.603  -5.902  1.00 55.82  ? 54  TYR   A N    1 
ATOM   399  C  CA   . TYR   A 1 54  ? -25.365 -8.655  -5.197  1.00 56.59  ? 54  TYR   A CA   1 
ATOM   400  C  C    . TYR   A 1 54  ? -26.074 -9.991  -5.346  1.00 59.99  ? 54  TYR   A C    1 
ATOM   401  O  O    . TYR   A 1 54  ? -25.407 -10.979 -5.619  1.00 58.52  ? 54  TYR   A O    1 
ATOM   402  C  CB   . TYR   A 1 54  ? -25.172 -8.243  -3.737  1.00 50.83  ? 54  TYR   A CB   1 
ATOM   403  C  CG   . TYR   A 1 54  ? -24.132 -7.186  -3.473  1.00 46.43  ? 54  TYR   A CG   1 
ATOM   404  C  CD1  . TYR   A 1 54  ? -22.809 -7.530  -3.280  1.00 45.68  ? 54  TYR   A CD1  1 
ATOM   405  C  CD2  . TYR   A 1 54  ? -24.471 -5.848  -3.381  1.00 42.22  ? 54  TYR   A CD2  1 
ATOM   406  C  CE1  . TYR   A 1 54  ? -21.849 -6.576  -3.006  1.00 39.82  ? 54  TYR   A CE1  1 
ATOM   407  C  CE2  . TYR   A 1 54  ? -23.521 -4.879  -3.114  1.00 41.85  ? 54  TYR   A CE2  1 
ATOM   408  C  CZ   . TYR   A 1 54  ? -22.203 -5.246  -2.928  1.00 43.77  ? 54  TYR   A CZ   1 
ATOM   409  O  OH   . TYR   A 1 54  ? -21.246 -4.313  -2.674  1.00 46.85  ? 54  TYR   A OH   1 
ATOM   410  N  N    . GLU   A 1 55  ? -27.382 -10.003 -5.117  1.00 75.17  ? 55  GLU   A N    1 
ATOM   411  C  CA   . GLU   A 1 55  ? -28.075 -11.280 -5.197  1.00 74.28  ? 55  GLU   A CA   1 
ATOM   412  C  C    . GLU   A 1 55  ? -27.900 -11.900 -6.575  1.00 76.82  ? 55  GLU   A C    1 
ATOM   413  O  O    . GLU   A 1 55  ? -27.708 -13.116 -6.694  1.00 83.78  ? 55  GLU   A O    1 
ATOM   414  C  CB   . GLU   A 1 55  ? -29.554 -11.104 -4.840  1.00 76.61  ? 55  GLU   A CB   1 
ATOM   415  C  CG   . GLU   A 1 55  ? -30.458 -10.706 -5.998  1.00 84.88  ? 55  GLU   A CG   1 
ATOM   416  C  CD   . GLU   A 1 55  ? -31.930 -10.652 -5.623  1.00 94.51  ? 55  GLU   A CD   1 
ATOM   417  O  OE1  . GLU   A 1 55  ? -32.257 -10.959 -4.453  1.00 95.50  ? 55  GLU   A OE1  1 
ATOM   418  O  OE2  . GLU   A 1 55  ? -32.758 -10.309 -6.504  1.00 92.84  ? 55  GLU   A OE2  1 
ATOM   419  N  N    . ASP   A 1 56  ? -27.913 -11.074 -7.625  1.00 64.34  ? 56  ASP   A N    1 
ATOM   420  C  CA   . ASP   A 1 56  ? -27.685 -11.584 -8.970  1.00 58.69  ? 56  ASP   A CA   1 
ATOM   421  C  C    . ASP   A 1 56  ? -26.250 -12.048 -9.139  1.00 58.91  ? 56  ASP   A C    1 
ATOM   422  O  O    . ASP   A 1 56  ? -25.995 -13.032 -9.837  1.00 65.08  ? 56  ASP   A O    1 
ATOM   423  C  CB   . ASP   A 1 56  ? -28.022 -10.510 -10.005 1.00 60.07  ? 56  ASP   A CB   1 
ATOM   424  C  CG   . ASP   A 1 56  ? -29.497 -10.436 -10.293 1.00 55.18  ? 56  ASP   A CG   1 
ATOM   425  O  OD1  . ASP   A 1 56  ? -30.223 -11.293 -9.778  1.00 55.06  ? 56  ASP   A OD1  1 
ATOM   426  O  OD2  . ASP   A 1 56  ? -29.922 -9.536  -11.037 1.00 53.70  ? 56  ASP   A OD2  1 
ATOM   427  N  N    . LEU   A 1 57  ? -25.308 -11.347 -8.512  1.00 57.59  ? 57  LEU   A N    1 
ATOM   428  C  CA   . LEU   A 1 57  ? -23.919 -11.786 -8.495  1.00 61.28  ? 57  LEU   A CA   1 
ATOM   429  C  C    . LEU   A 1 57  ? -23.726 -13.071 -7.703  1.00 62.76  ? 57  LEU   A C    1 
ATOM   430  O  O    . LEU   A 1 57  ? -22.806 -13.844 -7.997  1.00 61.26  ? 57  LEU   A O    1 
ATOM   431  C  CB   . LEU   A 1 57  ? -23.044 -10.671 -7.926  1.00 58.10  ? 57  LEU   A CB   1 
ATOM   432  C  CG   . LEU   A 1 57  ? -22.814 -9.501  -8.865  1.00 58.42  ? 57  LEU   A CG   1 
ATOM   433  C  CD1  . LEU   A 1 57  ? -22.230 -8.321  -8.116  1.00 60.76  ? 57  LEU   A CD1  1 
ATOM   434  C  CD2  . LEU   A 1 57  ? -21.808 -10.038 -9.892  1.00 57.80  ? 57  LEU   A CD2  1 
ATOM   435  N  N    . LEU   A 1 58  ? -24.560 -13.311 -6.690  1.00 62.26  ? 58  LEU   A N    1 
ATOM   436  C  CA   . LEU   A 1 58  ? -24.384 -14.510 -5.883  1.00 60.77  ? 58  LEU   A CA   1 
ATOM   437  C  C    . LEU   A 1 58  ? -24.886 -15.754 -6.610  1.00 62.34  ? 58  LEU   A C    1 
ATOM   438  O  O    . LEU   A 1 58  ? -24.349 -16.846 -6.398  1.00 65.11  ? 58  LEU   A O    1 
ATOM   439  C  CB   . LEU   A 1 58  ? -25.072 -14.336 -4.528  1.00 62.52  ? 58  LEU   A CB   1 
ATOM   440  C  CG   . LEU   A 1 58  ? -24.973 -15.461 -3.490  1.00 63.80  ? 58  LEU   A CG   1 
ATOM   441  C  CD1  . LEU   A 1 58  ? -23.599 -16.149 -3.435  1.00 61.59  ? 58  LEU   A CD1  1 
ATOM   442  C  CD2  . LEU   A 1 58  ? -25.304 -14.869 -2.156  1.00 56.16  ? 58  LEU   A CD2  1 
ATOM   443  N  N    . ILE   A 1 59  ? -25.893 -15.616 -7.475  1.00 60.70  ? 59  ILE   A N    1 
ATOM   444  C  CA   . ILE   A 1 59  ? -26.323 -16.748 -8.294  1.00 59.04  ? 59  ILE   A CA   1 
ATOM   445  C  C    . ILE   A 1 59  ? -25.175 -17.250 -9.163  1.00 64.49  ? 59  ILE   A C    1 
ATOM   446  O  O    . ILE   A 1 59  ? -25.000 -18.462 -9.340  1.00 67.68  ? 59  ILE   A O    1 
ATOM   447  C  CB   . ILE   A 1 59  ? -27.557 -16.369 -9.138  1.00 54.78  ? 59  ILE   A CB   1 
ATOM   448  C  CG1  . ILE   A 1 59  ? -28.752 -16.099 -8.223  1.00 52.11  ? 59  ILE   A CG1  1 
ATOM   449  C  CG2  . ILE   A 1 59  ? -27.834 -17.440 -10.234 1.00 51.03  ? 59  ILE   A CG2  1 
ATOM   450  C  CD1  . ILE   A 1 59  ? -29.928 -15.472 -8.913  1.00 52.13  ? 59  ILE   A CD1  1 
ATOM   451  N  N    . ARG   A 1 60  ? -24.376 -16.330 -9.718  1.00 72.29  ? 60  ARG   A N    1 
ATOM   452  C  CA   . ARG   A 1 60  ? -23.226 -16.722 -10.530 1.00 70.84  ? 60  ARG   A CA   1 
ATOM   453  C  C    . ARG   A 1 60  ? -22.307 -17.671 -9.759  1.00 73.89  ? 60  ARG   A C    1 
ATOM   454  O  O    . ARG   A 1 60  ? -21.779 -18.639 -10.322 1.00 75.78  ? 60  ARG   A O    1 
ATOM   455  C  CB   . ARG   A 1 60  ? -22.445 -15.476 -10.977 1.00 76.15  ? 60  ARG   A CB   1 
ATOM   456  C  CG   . ARG   A 1 60  ? -23.181 -14.408 -11.843 1.00 77.59  ? 60  ARG   A CG   1 
ATOM   457  C  CD   . ARG   A 1 60  ? -23.473 -14.886 -13.260 1.00 83.58  ? 60  ARG   A CD   1 
ATOM   458  N  NE   . ARG   A 1 60  ? -22.328 -15.600 -13.817 1.00 85.48  ? 60  ARG   A NE   1 
ATOM   459  C  CZ   . ARG   A 1 60  ? -22.398 -16.446 -14.838 1.00 84.44  ? 60  ARG   A CZ   1 
ATOM   460  N  NH1  . ARG   A 1 60  ? -21.306 -17.067 -15.260 1.00 83.85  ? 60  ARG   A NH1  1 
ATOM   461  N  NH2  . ARG   A 1 60  ? -23.561 -16.677 -15.430 1.00 84.12  ? 60  ARG   A NH2  1 
ATOM   462  N  N    . LYS   A 1 61  ? -22.131 -17.423 -8.461  1.00 71.25  ? 61  LYS   A N    1 
ATOM   463  C  CA   . LYS   A 1 61  ? -21.210 -18.153 -7.599  1.00 73.62  ? 61  LYS   A CA   1 
ATOM   464  C  C    . LYS   A 1 61  ? -21.912 -19.296 -6.855  1.00 74.50  ? 61  LYS   A C    1 
ATOM   465  O  O    . LYS   A 1 61  ? -23.124 -19.271 -6.621  1.00 72.42  ? 61  LYS   A O    1 
ATOM   466  C  CB   . LYS   A 1 61  ? -20.569 -17.196 -6.585  1.00 70.90  ? 61  LYS   A CB   1 
ATOM   467  C  CG   . LYS   A 1 61  ? -20.041 -15.896 -7.163  1.00 66.01  ? 61  LYS   A CG   1 
ATOM   468  C  CD   . LYS   A 1 61  ? -18.672 -16.066 -7.786  1.00 66.89  ? 61  LYS   A CD   1 
ATOM   469  C  CE   . LYS   A 1 61  ? -18.118 -14.715 -8.197  1.00 63.86  ? 61  LYS   A CE   1 
ATOM   470  N  NZ   . LYS   A 1 61  ? -19.175 -13.923 -8.888  1.00 64.03  ? 61  LYS   A NZ   1 
ATOM   471  N  N    . SER   A 1 62  ? -21.114 -20.291 -6.446  1.00 87.05  ? 62  SER   A N    1 
ATOM   472  C  CA   . SER   A 1 62  ? -21.579 -21.465 -5.700  1.00 84.26  ? 62  SER   A CA   1 
ATOM   473  C  C    . SER   A 1 62  ? -20.646 -21.740 -4.513  1.00 82.12  ? 62  SER   A C    1 
ATOM   474  O  O    . SER   A 1 62  ? -19.741 -20.957 -4.212  1.00 83.05  ? 62  SER   A O    1 
ATOM   475  C  CB   . SER   A 1 62  ? -21.680 -22.693 -6.617  1.00 80.36  ? 62  SER   A CB   1 
ATOM   476  O  OG   . SER   A 1 62  ? -22.457 -22.406 -7.768  1.00 78.78  ? 62  SER   A OG   1 
ATOM   477  N  N    . ASN   A 1 63  ? -20.867 -22.878 -3.838  1.00 74.09  ? 63  ASN   A N    1 
ATOM   478  C  CA   . ASN   A 1 63  ? -20.130 -23.189 -2.608  1.00 70.11  ? 63  ASN   A CA   1 
ATOM   479  C  C    . ASN   A 1 63  ? -18.623 -23.266 -2.829  1.00 69.18  ? 63  ASN   A C    1 
ATOM   480  O  O    . ASN   A 1 63  ? -17.841 -22.889 -1.949  1.00 64.10  ? 63  ASN   A O    1 
ATOM   481  C  CB   . ASN   A 1 63  ? -20.607 -24.508 -2.007  1.00 66.14  ? 63  ASN   A CB   1 
ATOM   482  C  CG   . ASN   A 1 63  ? -21.588 -24.323 -0.872  1.00 67.84  ? 63  ASN   A CG   1 
ATOM   483  O  OD1  . ASN   A 1 63  ? -21.783 -23.212 -0.366  1.00 69.23  ? 63  ASN   A OD1  1 
ATOM   484  N  ND2  . ASN   A 1 63  ? -22.166 -25.431 -0.417  1.00 62.25  ? 63  ASN   A ND2  1 
ATOM   485  N  N    . HIS   A 1 64  ? -18.193 -23.796 -3.970  1.00 72.30  ? 64  HIS   A N    1 
ATOM   486  C  CA   . HIS   A 1 64  ? -16.766 -23.976 -4.210  1.00 72.64  ? 64  HIS   A CA   1 
ATOM   487  C  C    . HIS   A 1 64  ? -16.080 -22.679 -4.612  1.00 66.32  ? 64  HIS   A C    1 
ATOM   488  O  O    . HIS   A 1 64  ? -14.847 -22.601 -4.548  1.00 64.98  ? 64  HIS   A O    1 
ATOM   489  C  CB   . HIS   A 1 64  ? -16.541 -25.053 -5.285  1.00 71.87  ? 64  HIS   A CB   1 
ATOM   490  C  CG   . HIS   A 1 64  ? -17.319 -24.829 -6.550  1.00 70.17  ? 64  HIS   A CG   1 
ATOM   491  N  ND1  . HIS   A 1 64  ? -18.685 -24.995 -6.628  1.00 73.98  ? 64  HIS   A ND1  1 
ATOM   492  C  CD2  . HIS   A 1 64  ? -16.917 -24.460 -7.790  1.00 70.26  ? 64  HIS   A CD2  1 
ATOM   493  C  CE1  . HIS   A 1 64  ? -19.093 -24.729 -7.856  1.00 74.95  ? 64  HIS   A CE1  1 
ATOM   494  N  NE2  . HIS   A 1 64  ? -18.038 -24.408 -8.583  1.00 74.66  ? 64  HIS   A NE2  1 
ATOM   495  N  N    . ASN   A 1 65  ? -16.856 -21.666 -5.008  1.00 67.15  ? 65  ASN   A N    1 
ATOM   496  C  CA   . ASN   A 1 65  ? -16.304 -20.399 -5.476  1.00 64.68  ? 65  ASN   A CA   1 
ATOM   497  C  C    . ASN   A 1 65  ? -15.644 -19.593 -4.363  1.00 68.71  ? 65  ASN   A C    1 
ATOM   498  O  O    . ASN   A 1 65  ? -14.881 -18.665 -4.658  1.00 66.33  ? 65  ASN   A O    1 
ATOM   499  C  CB   . ASN   A 1 65  ? -17.403 -19.555 -6.119  1.00 64.39  ? 65  ASN   A CB   1 
ATOM   500  C  CG   . ASN   A 1 65  ? -17.840 -20.087 -7.465  1.00 69.53  ? 65  ASN   A CG   1 
ATOM   501  O  OD1  . ASN   A 1 65  ? -18.575 -21.069 -7.539  1.00 74.96  ? 65  ASN   A OD1  1 
ATOM   502  N  ND2  . ASN   A 1 65  ? -17.405 -19.428 -8.543  1.00 62.09  ? 65  ASN   A ND2  1 
ATOM   503  N  N    . PHE   A 1 66  ? -15.927 -19.910 -3.102  1.00 65.75  ? 66  PHE   A N    1 
ATOM   504  C  CA   . PHE   A 1 66  ? -15.398 -19.170 -1.966  1.00 63.69  ? 66  PHE   A CA   1 
ATOM   505  C  C    . PHE   A 1 66  ? -14.321 -20.000 -1.279  1.00 68.55  ? 66  PHE   A C    1 
ATOM   506  O  O    . PHE   A 1 66  ? -14.557 -21.161 -0.936  1.00 73.16  ? 66  PHE   A O    1 
ATOM   507  C  CB   . PHE   A 1 66  ? -16.503 -18.830 -0.963  1.00 66.06  ? 66  PHE   A CB   1 
ATOM   508  C  CG   . PHE   A 1 66  ? -17.706 -18.157 -1.563  1.00 63.77  ? 66  PHE   A CG   1 
ATOM   509  C  CD1  . PHE   A 1 66  ? -17.683 -16.800 -1.869  1.00 60.44  ? 66  PHE   A CD1  1 
ATOM   510  C  CD2  . PHE   A 1 66  ? -18.876 -18.876 -1.784  1.00 65.60  ? 66  PHE   A CD2  1 
ATOM   511  C  CE1  . PHE   A 1 66  ? -18.801 -16.176 -2.407  1.00 64.19  ? 66  PHE   A CE1  1 
ATOM   512  C  CE2  . PHE   A 1 66  ? -19.996 -18.263 -2.324  1.00 69.18  ? 66  PHE   A CE2  1 
ATOM   513  C  CZ   . PHE   A 1 66  ? -19.960 -16.907 -2.637  1.00 69.75  ? 66  PHE   A CZ   1 
ATOM   514  N  N    . LEU   A 1 67  ? -13.159 -19.394 -1.043  1.00 68.02  ? 67  LEU   A N    1 
ATOM   515  C  CA   . LEU   A 1 67  ? -11.985 -20.108 -0.544  1.00 68.14  ? 67  LEU   A CA   1 
ATOM   516  C  C    . LEU   A 1 67  ? -11.450 -19.443 0.718   1.00 69.20  ? 67  LEU   A C    1 
ATOM   517  O  O    . LEU   A 1 67  ? -10.732 -18.436 0.648   1.00 57.66  ? 67  LEU   A O    1 
ATOM   518  C  CB   . LEU   A 1 67  ? -10.916 -20.164 -1.612  1.00 69.95  ? 67  LEU   A CB   1 
ATOM   519  C  CG   . LEU   A 1 67  ? -11.064 -21.370 -2.517  1.00 78.92  ? 67  LEU   A CG   1 
ATOM   520  C  CD1  . LEU   A 1 67  ? -9.962  -21.222 -3.468  1.00 79.91  ? 67  LEU   A CD1  1 
ATOM   521  C  CD2  . LEU   A 1 67  ? -10.950 -22.685 -1.730  1.00 82.92  ? 67  LEU   A CD2  1 
ATOM   522  N  N    . VAL   A 1 68  ? -11.771 -20.047 1.859   1.00 78.57  ? 68  VAL   A N    1 
ATOM   523  C  CA   . VAL   A 1 68  ? -11.373 -19.533 3.163   1.00 72.30  ? 68  VAL   A CA   1 
ATOM   524  C  C    . VAL   A 1 68  ? -10.015 -20.131 3.513   1.00 75.46  ? 68  VAL   A C    1 
ATOM   525  O  O    . VAL   A 1 68  ? -9.896  -21.344 3.716   1.00 76.64  ? 68  VAL   A O    1 
ATOM   526  C  CB   . VAL   A 1 68  ? -12.419 -19.868 4.227   1.00 76.62  ? 68  VAL   A CB   1 
ATOM   527  C  CG1  . VAL   A 1 68  ? -12.125 -19.097 5.527   1.00 70.47  ? 68  VAL   A CG1  1 
ATOM   528  C  CG2  . VAL   A 1 68  ? -13.824 -19.602 3.681   1.00 72.27  ? 68  VAL   A CG2  1 
ATOM   529  N  N    . GLN   A 1 69  ? -8.996  -19.271 3.606   1.00 71.49  ? 69  GLN   A N    1 
ATOM   530  C  CA   . GLN   A 1 69  ? -7.618  -19.730 3.739   1.00 75.08  ? 69  GLN   A CA   1 
ATOM   531  C  C    . GLN   A 1 69  ? -7.292  -20.177 5.161   1.00 78.83  ? 69  GLN   A C    1 
ATOM   532  O  O    . GLN   A 1 69  ? -6.728  -21.262 5.354   1.00 84.69  ? 69  GLN   A O    1 
ATOM   533  C  CB   . GLN   A 1 69  ? -6.663  -18.625 3.290   1.00 81.67  ? 69  GLN   A CB   1 
ATOM   534  C  CG   . GLN   A 1 69  ? -5.167  -18.947 3.317   1.00 79.14  ? 69  GLN   A CG   1 
ATOM   535  C  CD   . GLN   A 1 69  ? -4.779  -20.042 2.357   1.00 80.44  ? 69  GLN   A CD   1 
ATOM   536  O  OE1  . GLN   A 1 69  ? -4.263  -21.078 2.763   1.00 82.67  ? 69  GLN   A OE1  1 
ATOM   537  N  NE2  . GLN   A 1 69  ? -5.050  -19.830 1.072   1.00 87.34  ? 69  GLN   A NE2  1 
ATOM   538  N  N    . ALA   A 1 70  ? -7.635  -19.368 6.160   1.00 69.83  ? 70  ALA   A N    1 
ATOM   539  C  CA   . ALA   A 1 70  ? -7.195  -19.592 7.550   1.00 75.91  ? 70  ALA   A CA   1 
ATOM   540  C  C    . ALA   A 1 70  ? -5.663  -19.597 7.545   1.00 78.60  ? 70  ALA   A C    1 
ATOM   541  O  O    . ALA   A 1 70  ? -5.038  -18.899 6.735   1.00 86.58  ? 70  ALA   A O    1 
ATOM   542  C  CB   . ALA   A 1 70  ? -7.834  -20.849 8.142   1.00 71.38  ? 70  ALA   A CB   1 
ATOM   543  N  N    . GLY   A 1 71  ? -5.035  -20.363 8.437   1.00 63.03  ? 71  GLY   A N    1 
ATOM   544  C  CA   . GLY   A 1 71  ? -3.597  -20.535 8.337   1.00 65.78  ? 71  GLY   A CA   1 
ATOM   545  C  C    . GLY   A 1 71  ? -3.211  -21.286 7.077   1.00 78.95  ? 71  GLY   A C    1 
ATOM   546  O  O    . GLY   A 1 71  ? -2.409  -20.808 6.269   1.00 77.15  ? 71  GLY   A O    1 
ATOM   547  N  N    . ASN   A 1 72  ? -3.748  -22.488 6.919   1.00 77.91  ? 72  ASN   A N    1 
ATOM   548  C  CA   . ASN   A 1 72  ? -3.527  -23.265 5.680   1.00 78.04  ? 72  ASN   A CA   1 
ATOM   549  C  C    . ASN   A 1 72  ? -4.921  -23.667 5.214   1.00 81.46  ? 72  ASN   A C    1 
ATOM   550  O  O    . ASN   A 1 72  ? -5.775  -23.877 6.082   1.00 81.22  ? 72  ASN   A O    1 
ATOM   551  C  CB   . ASN   A 1 72  ? -2.519  -24.392 5.878   1.00 81.40  ? 72  ASN   A CB   1 
ATOM   552  C  CG   . ASN   A 1 72  ? -1.100  -23.890 6.028   1.00 81.66  ? 72  ASN   A CG   1 
ATOM   553  O  OD1  . ASN   A 1 72  ? -0.651  -23.049 5.254   1.00 78.34  ? 72  ASN   A OD1  1 
ATOM   554  N  ND2  . ASN   A 1 72  ? -0.383  -24.404 7.011   1.00 83.29  ? 72  ASN   A ND2  1 
ATOM   555  N  N    . VAL   A 1 73  ? -5.144  -23.776 3.902   1.00 85.53  ? 73  VAL   A N    1 
ATOM   556  C  CA   . VAL   A 1 73  ? -6.525  -23.961 3.360   1.00 87.81  ? 73  VAL   A CA   1 
ATOM   557  C  C    . VAL   A 1 73  ? -7.127  -25.349 3.599   1.00 91.45  ? 73  VAL   A C    1 
ATOM   558  O  O    . VAL   A 1 73  ? -6.820  -26.273 2.831   1.00 94.77  ? 73  VAL   A O    1 
ATOM   559  C  CB   . VAL   A 1 73  ? -6.640  -23.461 1.905   1.00 85.61  ? 73  VAL   A CB   1 
ATOM   560  C  CG1  . VAL   A 1 73  ? -5.520  -23.965 1.011   1.00 85.74  ? 73  VAL   A CG1  1 
ATOM   561  C  CG2  . VAL   A 1 73  ? -8.006  -23.727 1.295   1.00 85.24  ? 73  VAL   A CG2  1 
ATOM   562  N  N    . GLN   A 1 74  ? -7.934  -25.494 4.652   1.00 96.01  ? 74  GLN   A N    1 
ATOM   563  C  CA   . GLN   A 1 74  ? -8.662  -26.766 4.891   1.00 100.36 ? 74  GLN   A CA   1 
ATOM   564  C  C    . GLN   A 1 74  ? -10.106 -26.454 5.275   1.00 101.75 ? 74  GLN   A C    1 
ATOM   565  O  O    . GLN   A 1 74  ? -10.696 -27.252 6.015   1.00 106.05 ? 74  GLN   A O    1 
ATOM   566  C  CB   . GLN   A 1 74  ? -8.009  -27.628 5.970   1.00 103.33 ? 74  GLN   A CB   1 
ATOM   567  C  CG   . GLN   A 1 74  ? -7.269  -28.849 5.443   1.00 99.95  ? 74  GLN   A CG   1 
ATOM   568  C  CD   . GLN   A 1 74  ? -6.735  -29.696 6.573   1.00 101.95 ? 74  GLN   A CD   1 
ATOM   569  O  OE1  . GLN   A 1 74  ? -7.204  -29.619 7.705   1.00 113.76 ? 74  GLN   A OE1  1 
ATOM   570  N  NE2  . GLN   A 1 74  ? -5.745  -30.520 6.274   1.00 99.91  ? 74  GLN   A NE2  1 
ATOM   571  N  N    . LEU   A 1 75  ? -10.645 -25.337 4.789   1.00 88.15  ? 75  LEU   A N    1 
ATOM   572  C  CA   . LEU   A 1 75  ? -12.058 -24.986 5.081   1.00 83.74  ? 75  LEU   A CA   1 
ATOM   573  C  C    . LEU   A 1 75  ? -12.912 -25.360 3.874   1.00 75.38  ? 75  LEU   A C    1 
ATOM   574  O  O    . LEU   A 1 75  ? -12.663 -24.833 2.784   1.00 72.45  ? 75  LEU   A O    1 
ATOM   575  C  CB   . LEU   A 1 75  ? -12.185 -23.498 5.426   1.00 81.19  ? 75  LEU   A CB   1 
ATOM   576  C  CG   . LEU   A 1 75  ? -11.926 -23.060 6.872   1.00 71.33  ? 75  LEU   A CG   1 
ATOM   577  C  CD1  . LEU   A 1 75  ? -13.073 -23.429 7.783   1.00 63.63  ? 75  LEU   A CD1  1 
ATOM   578  C  CD2  . LEU   A 1 75  ? -10.617 -23.585 7.436   1.00 71.97  ? 75  LEU   A CD2  1 
ATOM   579  N  N    . ARG   A 1 76  ? -13.889 -26.229 4.091   1.00 73.12  ? 76  ARG   A N    1 
ATOM   580  C  CA   . ARG   A 1 76  ? -14.726 -26.709 2.971   1.00 79.00  ? 76  ARG   A CA   1 
ATOM   581  C  C    . ARG   A 1 76  ? -16.081 -26.014 3.036   1.00 74.19  ? 76  ARG   A C    1 
ATOM   582  O  O    . ARG   A 1 76  ? -16.841 -26.285 3.962   1.00 71.42  ? 76  ARG   A O    1 
ATOM   583  C  CB   . ARG   A 1 76  ? -14.857 -28.235 2.995   1.00 79.85  ? 76  ARG   A CB   1 
ATOM   584  C  CG   . ARG   A 1 76  ? -13.536 -28.978 2.867   1.00 83.84  ? 76  ARG   A CG   1 
ATOM   585  C  CD   . ARG   A 1 76  ? -13.259 -29.554 1.492   1.00 85.97  ? 76  ARG   A CD   1 
ATOM   586  N  NE   . ARG   A 1 76  ? -13.181 -28.555 0.439   1.00 72.82  ? 76  ARG   A NE   1 
ATOM   587  C  CZ   . ARG   A 1 76  ? -12.103 -27.839 0.165   1.00 75.09  ? 76  ARG   A CZ   1 
ATOM   588  N  NH1  . ARG   A 1 76  ? -12.127 -26.958 -0.818  1.00 79.28  ? 76  ARG   A NH1  1 
ATOM   589  N  NH2  . ARG   A 1 76  ? -11.008 -27.994 0.884   1.00 78.23  ? 76  ARG   A NH2  1 
ATOM   590  N  N    . VAL   A 1 77  ? -16.363 -25.166 2.053   1.00 72.05  ? 77  VAL   A N    1 
ATOM   591  C  CA   . VAL   A 1 77  ? -17.614 -24.384 2.145   1.00 68.48  ? 77  VAL   A CA   1 
ATOM   592  C  C    . VAL   A 1 77  ? -18.780 -25.339 1.918   1.00 69.86  ? 77  VAL   A C    1 
ATOM   593  O  O    . VAL   A 1 77  ? -18.968 -25.797 0.784   1.00 65.61  ? 77  VAL   A O    1 
ATOM   594  C  CB   . VAL   A 1 77  ? -17.583 -23.131 1.254   1.00 68.79  ? 77  VAL   A CB   1 
ATOM   595  C  CG1  . VAL   A 1 77  ? -18.817 -22.265 1.438   1.00 63.17  ? 77  VAL   A CG1  1 
ATOM   596  C  CG2  . VAL   A 1 77  ? -16.326 -22.317 1.503   1.00 64.19  ? 77  VAL   A CG2  1 
ATOM   597  N  N    . ILE   A 1 78  ? -19.475 -25.672 2.997   1.00 68.13  ? 78  ILE   A N    1 
ATOM   598  C  CA   . ILE   A 1 78  ? -20.634 -26.564 2.948   1.00 66.07  ? 78  ILE   A CA   1 
ATOM   599  C  C    . ILE   A 1 78  ? -21.920 -25.819 2.609   1.00 63.15  ? 78  ILE   A C    1 
ATOM   600  O  O    . ILE   A 1 78  ? -22.911 -26.443 2.208   1.00 59.09  ? 78  ILE   A O    1 
ATOM   601  C  CB   . ILE   A 1 78  ? -20.782 -27.290 4.303   1.00 71.57  ? 78  ILE   A CB   1 
ATOM   602  C  CG1  . ILE   A 1 78  ? -19.501 -28.040 4.676   1.00 68.20  ? 78  ILE   A CG1  1 
ATOM   603  C  CG2  . ILE   A 1 78  ? -21.978 -28.249 4.331   1.00 76.99  ? 78  ILE   A CG2  1 
ATOM   604  C  CD1  . ILE   A 1 78  ? -19.647 -28.848 5.952   1.00 71.13  ? 78  ILE   A CD1  1 
ATOM   605  N  N    . GLY   A 1 79  ? -21.935 -24.503 2.765   1.00 70.16  ? 79  GLY   A N    1 
ATOM   606  C  CA   . GLY   A 1 79  ? -23.121 -23.719 2.474   1.00 69.79  ? 79  GLY   A CA   1 
ATOM   607  C  C    . GLY   A 1 79  ? -22.762 -22.254 2.382   1.00 70.02  ? 79  GLY   A C    1 
ATOM   608  O  O    . GLY   A 1 79  ? -21.674 -21.829 2.779   1.00 70.95  ? 79  GLY   A O    1 
ATOM   609  N  N    . HIS   A 1 80  ? -23.699 -21.483 1.840   1.00 66.55  ? 80  HIS   A N    1 
ATOM   610  C  CA   . HIS   A 1 80  ? -23.516 -20.045 1.720   1.00 62.61  ? 80  HIS   A CA   1 
ATOM   611  C  C    . HIS   A 1 80  ? -24.883 -19.374 1.754   1.00 63.33  ? 80  HIS   A C    1 
ATOM   612  O  O    . HIS   A 1 80  ? -25.917 -19.993 1.471   1.00 58.86  ? 80  HIS   A O    1 
ATOM   613  C  CB   . HIS   A 1 80  ? -22.754 -19.673 0.444   1.00 58.40  ? 80  HIS   A CB   1 
ATOM   614  C  CG   . HIS   A 1 80  ? -23.572 -19.804 -0.802  1.00 63.16  ? 80  HIS   A CG   1 
ATOM   615  N  ND1  . HIS   A 1 80  ? -23.694 -20.993 -1.490  1.00 61.30  ? 80  HIS   A ND1  1 
ATOM   616  C  CD2  . HIS   A 1 80  ? -24.314 -18.897 -1.482  1.00 66.43  ? 80  HIS   A CD2  1 
ATOM   617  C  CE1  . HIS   A 1 80  ? -24.476 -20.813 -2.541  1.00 66.82  ? 80  HIS   A CE1  1 
ATOM   618  N  NE2  . HIS   A 1 80  ? -24.860 -19.548 -2.563  1.00 71.93  ? 80  HIS   A NE2  1 
ATOM   619  N  N    . SER   A 1 81  ? -24.865 -18.088 2.093   1.00 59.18  ? 81  SER   A N    1 
ATOM   620  C  CA   . SER   A 1 81  ? -26.056 -17.298 2.354   1.00 56.09  ? 81  SER   A CA   1 
ATOM   621  C  C    . SER   A 1 81  ? -25.630 -15.837 2.428   1.00 57.68  ? 81  SER   A C    1 
ATOM   622  O  O    . SER   A 1 81  ? -24.488 -15.540 2.793   1.00 59.87  ? 81  SER   A O    1 
ATOM   623  C  CB   . SER   A 1 81  ? -26.728 -17.763 3.661   1.00 58.92  ? 81  SER   A CB   1 
ATOM   624  O  OG   . SER   A 1 81  ? -27.686 -16.846 4.173   1.00 56.14  ? 81  SER   A OG   1 
ATOM   625  N  N    . MET   A 1 82  ? -26.544 -14.930 2.082   1.00 52.13  ? 82  MET   A N    1 
ATOM   626  C  CA   . MET   A 1 82  ? -26.278 -13.493 2.163   1.00 51.04  ? 82  MET   A CA   1 
ATOM   627  C  C    . MET   A 1 82  ? -27.260 -12.840 3.140   1.00 51.48  ? 82  MET   A C    1 
ATOM   628  O  O    . MET   A 1 82  ? -28.427 -12.601 2.810   1.00 52.69  ? 82  MET   A O    1 
ATOM   629  C  CB   . MET   A 1 82  ? -26.350 -12.852 0.779   1.00 51.34  ? 82  MET   A CB   1 
ATOM   630  C  CG   . MET   A 1 82  ? -25.988 -11.363 0.761   1.00 49.16  ? 82  MET   A CG   1 
ATOM   631  S  SD   . MET   A 1 82  ? -26.610 -10.438 -0.667  1.00 50.16  ? 82  MET   A SD   1 
ATOM   632  C  CE   . MET   A 1 82  ? -26.365 -11.591 -2.014  1.00 58.43  ? 82  MET   A CE   1 
ATOM   633  N  N    . GLN   A 1 83  ? -26.789 -12.527 4.341   1.00 52.60  ? 83  GLN   A N    1 
ATOM   634  C  CA   . GLN   A 1 83  ? -27.581 -11.784 5.312   1.00 54.53  ? 83  GLN   A CA   1 
ATOM   635  C  C    . GLN   A 1 83  ? -27.137 -10.330 5.249   1.00 52.74  ? 83  GLN   A C    1 
ATOM   636  O  O    . GLN   A 1 83  ? -26.006 -10.009 5.615   1.00 46.54  ? 83  GLN   A O    1 
ATOM   637  C  CB   . GLN   A 1 83  ? -27.431 -12.353 6.727   1.00 52.66  ? 83  GLN   A CB   1 
ATOM   638  C  CG   . GLN   A 1 83  ? -28.551 -11.903 7.693   1.00 56.54  ? 83  GLN   A CG   1 
ATOM   639  C  CD   . GLN   A 1 83  ? -28.335 -12.288 9.183   1.00 57.54  ? 83  GLN   A CD   1 
ATOM   640  O  OE1  . GLN   A 1 83  ? -27.265 -12.752 9.587   1.00 57.53  ? 83  GLN   A OE1  1 
ATOM   641  N  NE2  . GLN   A 1 83  ? -29.377 -12.097 9.992   1.00 47.06  ? 83  GLN   A NE2  1 
ATOM   642  N  N    . ASN   A 1 84  ? -28.006 -9.477  4.712   1.00 61.63  ? 84  ASN   A N    1 
ATOM   643  C  CA   . ASN   A 1 84  ? -27.979 -8.028  4.920   1.00 64.65  ? 84  ASN   A CA   1 
ATOM   644  C  C    . ASN   A 1 84  ? -26.579 -7.423  4.816   1.00 62.79  ? 84  ASN   A C    1 
ATOM   645  O  O    . ASN   A 1 84  ? -26.170 -6.656  5.684   1.00 64.40  ? 84  ASN   A O    1 
ATOM   646  C  CB   . ASN   A 1 84  ? -28.594 -7.669  6.274   1.00 65.41  ? 84  ASN   A CB   1 
ATOM   647  C  CG   . ASN   A 1 84  ? -30.074 -7.933  6.329   1.00 68.75  ? 84  ASN   A CG   1 
ATOM   648  O  OD1  . ASN   A 1 84  ? -30.552 -8.647  7.205   1.00 76.76  ? 84  ASN   A OD1  1 
ATOM   649  N  ND2  . ASN   A 1 84  ? -30.811 -7.376  5.378   1.00 73.12  ? 84  ASN   A ND2  1 
ATOM   650  N  N    . CYS   A 1 85  ? -25.855 -7.747  3.730   1.00 45.89  ? 85  CYS   A N    1 
ATOM   651  C  CA   . CYS   A 1 85  ? -24.503 -7.244  3.422   1.00 43.72  ? 85  CYS   A CA   1 
ATOM   652  C  C    . CYS   A 1 85  ? -23.349 -8.080  3.976   1.00 44.59  ? 85  CYS   A C    1 
ATOM   653  O  O    . CYS   A 1 85  ? -22.193 -7.638  3.945   1.00 36.39  ? 85  CYS   A O    1 
ATOM   654  C  CB   . CYS   A 1 85  ? -24.251 -5.803  3.898   1.00 42.99  ? 85  CYS   A CB   1 
ATOM   655  S  SG   . CYS   A 1 85  ? -25.286 -4.525  3.207   1.00 44.98  ? 85  CYS   A SG   1 
ATOM   656  N  N    . VAL   A 1 86  ? -23.623 -9.273  4.490   1.00 48.29  ? 86  VAL   A N    1 
ATOM   657  C  CA   . VAL   A 1 86  ? -22.543 -10.179 4.849   1.00 47.40  ? 86  VAL   A CA   1 
ATOM   658  C  C    . VAL   A 1 86  ? -22.802 -11.533 4.206   1.00 49.76  ? 86  VAL   A C    1 
ATOM   659  O  O    . VAL   A 1 86  ? -23.938 -11.885 3.871   1.00 47.48  ? 86  VAL   A O    1 
ATOM   660  C  CB   . VAL   A 1 86  ? -22.361 -10.319 6.379   1.00 49.03  ? 86  VAL   A CB   1 
ATOM   661  C  CG1  . VAL   A 1 86  ? -22.159 -8.941  7.030   1.00 44.14  ? 86  VAL   A CG1  1 
ATOM   662  C  CG2  . VAL   A 1 86  ? -23.523 -11.075 7.007   1.00 50.92  ? 86  VAL   A CG2  1 
ATOM   663  N  N    . LEU   A 1 87  ? -21.720 -12.269 3.989   1.00 56.74  ? 87  LEU   A N    1 
ATOM   664  C  CA   . LEU   A 1 87  ? -21.781 -13.666 3.593   1.00 60.54  ? 87  LEU   A CA   1 
ATOM   665  C  C    . LEU   A 1 87  ? -21.499 -14.538 4.805   1.00 64.69  ? 87  LEU   A C    1 
ATOM   666  O  O    . LEU   A 1 87  ? -20.650 -14.209 5.639   1.00 66.25  ? 87  LEU   A O    1 
ATOM   667  C  CB   . LEU   A 1 87  ? -20.780 -13.978 2.479   1.00 60.23  ? 87  LEU   A CB   1 
ATOM   668  C  CG   . LEU   A 1 87  ? -21.346 -14.036 1.059   1.00 64.34  ? 87  LEU   A CG   1 
ATOM   669  C  CD1  . LEU   A 1 87  ? -21.916 -12.700 0.629   1.00 61.54  ? 87  LEU   A CD1  1 
ATOM   670  C  CD2  . LEU   A 1 87  ? -20.253 -14.478 0.114   1.00 63.25  ? 87  LEU   A CD2  1 
ATOM   671  N  N    . LYS   A 1 88  ? -22.228 -15.643 4.904   1.00 59.27  ? 88  LYS   A N    1 
ATOM   672  C  CA   . LYS   A 1 88  ? -22.033 -16.619 5.970   1.00 56.77  ? 88  LYS   A CA   1 
ATOM   673  C  C    . LYS   A 1 88  ? -21.671 -17.942 5.305   1.00 57.15  ? 88  LYS   A C    1 
ATOM   674  O  O    . LYS   A 1 88  ? -22.528 -18.590 4.690   1.00 56.71  ? 88  LYS   A O    1 
ATOM   675  C  CB   . LYS   A 1 88  ? -23.282 -16.731 6.842   1.00 49.05  ? 88  LYS   A CB   1 
ATOM   676  C  CG   . LYS   A 1 88  ? -23.598 -15.454 7.582   1.00 50.30  ? 88  LYS   A CG   1 
ATOM   677  C  CD   . LYS   A 1 88  ? -24.681 -15.647 8.626   1.00 53.00  ? 88  LYS   A CD   1 
ATOM   678  C  CE   . LYS   A 1 88  ? -26.013 -15.984 7.999   1.00 51.84  ? 88  LYS   A CE   1 
ATOM   679  N  NZ   . LYS   A 1 88  ? -27.049 -16.165 9.038   1.00 50.89  ? 88  LYS   A NZ   1 
ATOM   680  N  N    . LEU   A 1 89  ? -20.398 -18.325 5.412   1.00 55.89  ? 89  LEU   A N    1 
ATOM   681  C  CA   . LEU   A 1 89  ? -19.863 -19.507 4.735   1.00 56.06  ? 89  LEU   A CA   1 
ATOM   682  C  C    . LEU   A 1 89  ? -19.769 -20.662 5.732   1.00 55.28  ? 89  LEU   A C    1 
ATOM   683  O  O    . LEU   A 1 89  ? -18.748 -20.848 6.401   1.00 51.23  ? 89  LEU   A O    1 
ATOM   684  C  CB   . LEU   A 1 89  ? -18.508 -19.203 4.104   1.00 52.70  ? 89  LEU   A CB   1 
ATOM   685  C  CG   . LEU   A 1 89  ? -18.441 -17.971 3.205   1.00 49.28  ? 89  LEU   A CG   1 
ATOM   686  C  CD1  . LEU   A 1 89  ? -17.081 -17.906 2.543   1.00 49.54  ? 89  LEU   A CD1  1 
ATOM   687  C  CD2  . LEU   A 1 89  ? -19.547 -17.980 2.176   1.00 54.41  ? 89  LEU   A CD2  1 
ATOM   688  N  N    . LYS   A 1 90  ? -20.860 -21.436 5.821   1.00 56.15  ? 90  LYS   A N    1 
ATOM   689  C  CA   . LYS   A 1 90  ? -20.867 -22.710 6.528   1.00 54.08  ? 90  LYS   A CA   1 
ATOM   690  C  C    . LYS   A 1 90  ? -19.737 -23.592 6.025   1.00 59.38  ? 90  LYS   A C    1 
ATOM   691  O  O    . LYS   A 1 90  ? -19.596 -23.816 4.821   1.00 61.92  ? 90  LYS   A O    1 
ATOM   692  C  CB   . LYS   A 1 90  ? -22.214 -23.408 6.327   1.00 58.58  ? 90  LYS   A CB   1 
ATOM   693  C  CG   . LYS   A 1 90  ? -22.348 -24.805 6.955   1.00 63.22  ? 90  LYS   A CG   1 
ATOM   694  C  CD   . LYS   A 1 90  ? -22.364 -24.770 8.484   1.00 64.56  ? 90  LYS   A CD   1 
ATOM   695  C  CE   . LYS   A 1 90  ? -23.653 -24.149 9.050   1.00 67.85  ? 90  LYS   A CE   1 
ATOM   696  N  NZ   . LYS   A 1 90  ? -23.706 -24.123 10.565  1.00 65.33  ? 90  LYS   A NZ   1 
ATOM   697  N  N    . VAL   A 1 91  ? -18.923 -24.085 6.955   1.00 61.41  ? 91  VAL   A N    1 
ATOM   698  C  CA   . VAL   A 1 91  ? -17.737 -24.857 6.629   1.00 63.84  ? 91  VAL   A CA   1 
ATOM   699  C  C    . VAL   A 1 91  ? -17.750 -26.167 7.410   1.00 64.78  ? 91  VAL   A C    1 
ATOM   700  O  O    . VAL   A 1 91  ? -18.616 -26.414 8.251   1.00 63.48  ? 91  VAL   A O    1 
ATOM   701  C  CB   . VAL   A 1 91  ? -16.445 -24.066 6.895   1.00 63.30  ? 91  VAL   A CB   1 
ATOM   702  C  CG1  . VAL   A 1 91  ? -16.249 -23.025 5.816   1.00 61.42  ? 91  VAL   A CG1  1 
ATOM   703  C  CG2  . VAL   A 1 91  ? -16.522 -23.390 8.240   1.00 59.32  ? 91  VAL   A CG2  1 
ATOM   704  N  N    . ASP   A 1 92  ? -16.764 -27.014 7.102   1.00 65.22  ? 92  ASP   A N    1 
ATOM   705  C  CA   . ASP   A 1 92  ? -16.708 -28.360 7.666   1.00 68.27  ? 92  ASP   A CA   1 
ATOM   706  C  C    . ASP   A 1 92  ? -16.203 -28.344 9.106   1.00 72.79  ? 92  ASP   A C    1 
ATOM   707  O  O    . ASP   A 1 92  ? -16.885 -28.823 10.017  1.00 69.33  ? 92  ASP   A O    1 
ATOM   708  C  CB   . ASP   A 1 92  ? -15.833 -29.257 6.783   1.00 66.18  ? 92  ASP   A CB   1 
ATOM   709  C  CG   . ASP   A 1 92  ? -14.441 -28.689 6.571   1.00 74.32  ? 92  ASP   A CG   1 
ATOM   710  O  OD1  . ASP   A 1 92  ? -14.227 -27.492 6.888   1.00 72.97  ? 92  ASP   A OD1  1 
ATOM   711  O  OD2  . ASP   A 1 92  ? -13.565 -29.440 6.091   1.00 77.60  ? 92  ASP   A OD2  1 
ATOM   712  N  N    . THR   A 1 93  ? -15.021 -27.784 9.328   1.00 76.90  ? 93  THR   A N    1 
ATOM   713  C  CA   . THR   A 1 93  ? -14.417 -27.714 10.646  1.00 75.02  ? 93  THR   A CA   1 
ATOM   714  C  C    . THR   A 1 93  ? -14.937 -26.537 11.462  1.00 72.58  ? 93  THR   A C    1 
ATOM   715  O  O    . THR   A 1 93  ? -15.007 -25.406 10.972  1.00 72.73  ? 93  THR   A O    1 
ATOM   716  C  CB   . THR   A 1 93  ? -12.895 -27.644 10.515  1.00 80.36  ? 93  THR   A CB   1 
ATOM   717  O  OG1  . THR   A 1 93  ? -12.304 -27.491 11.815  1.00 79.27  ? 93  THR   A OG1  1 
ATOM   718  C  CG2  . THR   A 1 93  ? -12.451 -26.543 9.552   1.00 79.65  ? 93  THR   A CG2  1 
ATOM   719  N  N    . ALA   A 1 94  ? -15.304 -26.824 12.708  1.00 66.71  ? 94  ALA   A N    1 
ATOM   720  C  CA   . ALA   A 1 94  ? -15.632 -25.796 13.683  1.00 60.90  ? 94  ALA   A CA   1 
ATOM   721  C  C    . ALA   A 1 94  ? -14.365 -25.301 14.368  1.00 60.92  ? 94  ALA   A C    1 
ATOM   722  O  O    . ALA   A 1 94  ? -13.504 -26.093 14.767  1.00 55.80  ? 94  ALA   A O    1 
ATOM   723  C  CB   . ALA   A 1 94  ? -16.606 -26.339 14.725  1.00 63.96  ? 94  ALA   A CB   1 
ATOM   724  N  N    . ASN   A 1 95  ? -14.260 -23.987 14.508  1.00 57.85  ? 95  ASN   A N    1 
ATOM   725  C  CA   . ASN   A 1 95  ? -13.025 -23.370 14.944  1.00 53.15  ? 95  ASN   A CA   1 
ATOM   726  C  C    . ASN   A 1 95  ? -12.642 -23.896 16.324  1.00 57.25  ? 95  ASN   A C    1 
ATOM   727  O  O    . ASN   A 1 95  ? -13.425 -23.746 17.279  1.00 61.23  ? 95  ASN   A O    1 
ATOM   728  C  CB   . ASN   A 1 95  ? -13.196 -21.857 14.952  1.00 51.64  ? 95  ASN   A CB   1 
ATOM   729  C  CG   . ASN   A 1 95  ? -11.871 -21.106 15.036  1.00 54.05  ? 95  ASN   A CG   1 
ATOM   730  O  OD1  . ASN   A 1 95  ? -10.797 -21.696 15.170  1.00 55.89  ? 95  ASN   A OD1  1 
ATOM   731  N  ND2  . ASN   A 1 95  ? -11.950 -19.785 14.950  1.00 51.60  ? 95  ASN   A ND2  1 
ATOM   732  N  N    . PRO   A 1 96  ? -11.487 -24.553 16.467  1.00 56.12  ? 96  PRO   A N    1 
ATOM   733  C  CA   . PRO   A 1 96  ? -11.039 -24.958 17.808  1.00 52.47  ? 96  PRO   A CA   1 
ATOM   734  C  C    . PRO   A 1 96  ? -10.903 -23.786 18.760  1.00 56.13  ? 96  PRO   A C    1 
ATOM   735  O  O    . PRO   A 1 96  ? -11.154 -23.933 19.965  1.00 49.80  ? 96  PRO   A O    1 
ATOM   736  C  CB   . PRO   A 1 96  ? -9.683  -25.624 17.537  1.00 54.07  ? 96  PRO   A CB   1 
ATOM   737  C  CG   . PRO   A 1 96  ? -9.269  -25.107 16.189  1.00 57.72  ? 96  PRO   A CG   1 
ATOM   738  C  CD   . PRO   A 1 96  ? -10.538 -24.951 15.418  1.00 53.45  ? 96  PRO   A CD   1 
ATOM   739  N  N    . LYS   A 1 97  ? -10.534 -22.613 18.248  1.00 53.44  ? 97  LYS   A N    1 
ATOM   740  C  CA   . LYS   A 1 97  ? -10.299 -21.443 19.077  1.00 50.20  ? 97  LYS   A CA   1 
ATOM   741  C  C    . LYS   A 1 97  ? -11.506 -20.510 19.134  1.00 49.99  ? 97  LYS   A C    1 
ATOM   742  O  O    . LYS   A 1 97  ? -11.353 -19.331 19.482  1.00 47.66  ? 97  LYS   A O    1 
ATOM   743  C  CB   . LYS   A 1 97  ? -9.046  -20.714 18.585  1.00 48.67  ? 97  LYS   A CB   1 
ATOM   744  C  CG   . LYS   A 1 97  ? -7.799  -21.620 18.618  1.00 53.28  ? 97  LYS   A CG   1 
ATOM   745  C  CD   . LYS   A 1 97  ? -6.490  -20.860 18.374  1.00 57.83  ? 97  LYS   A CD   1 
ATOM   746  C  CE   . LYS   A 1 97  ? -6.249  -20.572 16.889  1.00 55.76  ? 97  LYS   A CE   1 
ATOM   747  N  NZ   . LYS   A 1 97  ? -5.147  -19.589 16.684  1.00 52.77  ? 97  LYS   A NZ   1 
ATOM   748  N  N    . THR   A 1 98  ? -12.701 -21.013 18.819  1.00 49.64  ? 98  THR   A N    1 
ATOM   749  C  CA   . THR   A 1 98  ? -13.905 -20.215 19.000  1.00 48.84  ? 98  THR   A CA   1 
ATOM   750  C  C    . THR   A 1 98  ? -14.023 -19.796 20.457  1.00 50.50  ? 98  THR   A C    1 
ATOM   751  O  O    . THR   A 1 98  ? -14.172 -20.663 21.343  1.00 52.11  ? 98  THR   A O    1 
ATOM   752  C  CB   . THR   A 1 98  ? -15.169 -20.965 18.586  1.00 47.09  ? 98  THR   A CB   1 
ATOM   753  O  OG1  . THR   A 1 98  ? -15.188 -21.156 17.171  1.00 48.14  ? 98  THR   A OG1  1 
ATOM   754  C  CG2  . THR   A 1 98  ? -16.389 -20.153 18.970  1.00 48.42  ? 98  THR   A CG2  1 
ATOM   755  N  N    . PRO   A 1 99  ? -13.951 -18.512 20.772  1.00 45.95  ? 99  PRO   A N    1 
ATOM   756  C  CA   . PRO   A 1 99  ? -14.213 -18.069 22.134  1.00 48.52  ? 99  PRO   A CA   1 
ATOM   757  C  C    . PRO   A 1 99  ? -15.710 -18.038 22.364  1.00 47.39  ? 99  PRO   A C    1 
ATOM   758  O  O    . PRO   A 1 99  ? -16.514 -18.125 21.433  1.00 49.79  ? 99  PRO   A O    1 
ATOM   759  C  CB   . PRO   A 1 99  ? -13.630 -16.654 22.167  1.00 48.49  ? 99  PRO   A CB   1 
ATOM   760  C  CG   . PRO   A 1 99  ? -13.915 -16.150 20.781  1.00 46.90  ? 99  PRO   A CG   1 
ATOM   761  C  CD   . PRO   A 1 99  ? -13.755 -17.367 19.862  1.00 45.36  ? 99  PRO   A CD   1 
ATOM   762  N  N    . LYS   A 1 100 ? -16.081 -17.910 23.626  1.00 50.63  ? 100 LYS   A N    1 
ATOM   763  C  CA   . LYS   A 1 100 ? -17.443 -17.501 23.890  1.00 50.49  ? 100 LYS   A CA   1 
ATOM   764  C  C    . LYS   A 1 100 ? -17.635 -16.135 23.234  1.00 52.67  ? 100 LYS   A C    1 
ATOM   765  O  O    . LYS   A 1 100 ? -16.795 -15.235 23.382  1.00 49.94  ? 100 LYS   A O    1 
ATOM   766  C  CB   . LYS   A 1 100 ? -17.717 -17.472 25.393  1.00 46.31  ? 100 LYS   A CB   1 
ATOM   767  C  CG   . LYS   A 1 100 ? -19.162 -17.195 25.704  1.00 52.39  ? 100 LYS   A CG   1 
ATOM   768  C  CD   . LYS   A 1 100 ? -20.056 -18.182 24.950  1.00 58.15  ? 100 LYS   A CD   1 
ATOM   769  C  CE   . LYS   A 1 100 ? -21.512 -18.084 25.378  1.00 63.98  ? 100 LYS   A CE   1 
ATOM   770  N  NZ   . LYS   A 1 100 ? -22.059 -16.711 25.172  1.00 66.22  ? 100 LYS   A NZ   1 
ATOM   771  N  N    . TYR   A 1 101 ? -18.692 -16.007 22.437  1.00 50.85  ? 101 TYR   A N    1 
ATOM   772  C  CA   . TYR   A 1 101 ? -18.879 -14.808 21.640  1.00 46.73  ? 101 TYR   A CA   1 
ATOM   773  C  C    . TYR   A 1 101 ? -20.361 -14.488 21.534  1.00 45.20  ? 101 TYR   A C    1 
ATOM   774  O  O    . TYR   A 1 101 ? -21.227 -15.297 21.862  1.00 43.63  ? 101 TYR   A O    1 
ATOM   775  C  CB   . TYR   A 1 101 ? -18.265 -14.968 20.240  1.00 50.21  ? 101 TYR   A CB   1 
ATOM   776  C  CG   . TYR   A 1 101 ? -19.061 -15.876 19.294  1.00 48.11  ? 101 TYR   A CG   1 
ATOM   777  C  CD1  . TYR   A 1 101 ? -20.142 -15.386 18.540  1.00 42.44  ? 101 TYR   A CD1  1 
ATOM   778  C  CD2  . TYR   A 1 101 ? -18.731 -17.222 19.160  1.00 49.16  ? 101 TYR   A CD2  1 
ATOM   779  C  CE1  . TYR   A 1 101 ? -20.867 -16.219 17.690  1.00 42.17  ? 101 TYR   A CE1  1 
ATOM   780  C  CE2  . TYR   A 1 101 ? -19.444 -18.060 18.305  1.00 49.07  ? 101 TYR   A CE2  1 
ATOM   781  C  CZ   . TYR   A 1 101 ? -20.505 -17.556 17.579  1.00 45.76  ? 101 TYR   A CZ   1 
ATOM   782  O  OH   . TYR   A 1 101 ? -21.196 -18.408 16.758  1.00 46.64  ? 101 TYR   A OH   1 
ATOM   783  N  N    . LYS   A 1 102 ? -20.635 -13.301 21.007  1.00 52.00  ? 102 LYS   A N    1 
ATOM   784  C  CA   . LYS   A 1 102 ? -21.986 -12.836 20.728  1.00 47.50  ? 102 LYS   A CA   1 
ATOM   785  C  C    . LYS   A 1 102 ? -21.935 -11.644 19.776  1.00 49.23  ? 102 LYS   A C    1 
ATOM   786  O  O    . LYS   A 1 102 ? -20.921 -10.947 19.685  1.00 50.94  ? 102 LYS   A O    1 
ATOM   787  C  CB   . LYS   A 1 102 ? -22.723 -12.521 22.030  1.00 47.21  ? 102 LYS   A CB   1 
ATOM   788  C  CG   . LYS   A 1 102 ? -24.175 -12.007 21.898  1.00 61.18  ? 102 LYS   A CG   1 
ATOM   789  C  CD   . LYS   A 1 102 ? -25.127 -12.952 21.120  1.00 62.03  ? 102 LYS   A CD   1 
ATOM   790  C  CE   . LYS   A 1 102 ? -26.660 -12.669 21.297  1.00 67.45  ? 102 LYS   A CE   1 
ATOM   791  N  NZ   . LYS   A 1 102 ? -27.471 -13.537 20.384  1.00 68.96  ? 102 LYS   A NZ   1 
ATOM   792  N  N    . PHE   A 1 103 ? -23.008 -11.484 19.004  1.00 44.56  ? 103 PHE   A N    1 
ATOM   793  C  CA   . PHE   A 1 103 ? -23.153 -10.374 18.072  1.00 45.02  ? 103 PHE   A CA   1 
ATOM   794  C  C    . PHE   A 1 103 ? -24.004 -9.314  18.745  1.00 43.43  ? 103 PHE   A C    1 
ATOM   795  O  O    . PHE   A 1 103 ? -25.019 -9.639  19.373  1.00 49.88  ? 103 PHE   A O    1 
ATOM   796  C  CB   . PHE   A 1 103 ? -23.791 -10.833 16.757  1.00 39.88  ? 103 PHE   A CB   1 
ATOM   797  C  CG   . PHE   A 1 103 ? -22.945 -11.810 16.001  1.00 38.62  ? 103 PHE   A CG   1 
ATOM   798  C  CD1  . PHE   A 1 103 ? -21.597 -11.966 16.320  1.00 36.11  ? 103 PHE   A CD1  1 
ATOM   799  C  CD2  . PHE   A 1 103 ? -23.497 -12.597 15.002  1.00 36.74  ? 103 PHE   A CD2  1 
ATOM   800  C  CE1  . PHE   A 1 103 ? -20.804 -12.881 15.642  1.00 36.41  ? 103 PHE   A CE1  1 
ATOM   801  C  CE2  . PHE   A 1 103 ? -22.718 -13.522 14.308  1.00 37.29  ? 103 PHE   A CE2  1 
ATOM   802  C  CZ   . PHE   A 1 103 ? -21.364 -13.667 14.629  1.00 38.77  ? 103 PHE   A CZ   1 
ATOM   803  N  N    . VAL   A 1 104 ? -23.588 -8.055  18.620  1.00 37.03  ? 104 VAL   A N    1 
ATOM   804  C  CA   . VAL   A 1 104 ? -24.166 -6.956  19.386  1.00 41.39  ? 104 VAL   A CA   1 
ATOM   805  C  C    . VAL   A 1 104 ? -24.217 -5.713  18.507  1.00 37.88  ? 104 VAL   A C    1 
ATOM   806  O  O    . VAL   A 1 104 ? -23.187 -5.268  17.999  1.00 37.60  ? 104 VAL   A O    1 
ATOM   807  C  CB   . VAL   A 1 104 ? -23.352 -6.672  20.666  1.00 41.28  ? 104 VAL   A CB   1 
ATOM   808  C  CG1  . VAL   A 1 104 ? -23.804 -5.371  21.324  1.00 44.90  ? 104 VAL   A CG1  1 
ATOM   809  C  CG2  . VAL   A 1 104 ? -23.488 -7.826  21.650  1.00 41.53  ? 104 VAL   A CG2  1 
ATOM   810  N  N    . ARG   A 1 105 ? -25.397 -5.130  18.348  1.00 40.03  ? 105 ARG   A N    1 
ATOM   811  C  CA   . ARG   A 1 105 ? -25.494 -3.818  17.723  1.00 40.96  ? 105 ARG   A CA   1 
ATOM   812  C  C    . ARG   A 1 105 ? -25.325 -2.759  18.814  1.00 40.57  ? 105 ARG   A C    1 
ATOM   813  O  O    . ARG   A 1 105 ? -26.238 -2.510  19.599  1.00 40.71  ? 105 ARG   A O    1 
ATOM   814  C  CB   . ARG   A 1 105 ? -26.808 -3.636  16.962  1.00 36.03  ? 105 ARG   A CB   1 
ATOM   815  C  CG   . ARG   A 1 105 ? -26.734 -2.459  15.988  1.00 38.34  ? 105 ARG   A CG   1 
ATOM   816  C  CD   . ARG   A 1 105 ? -27.943 -2.319  15.076  1.00 38.44  ? 105 ARG   A CD   1 
ATOM   817  N  NE   . ARG   A 1 105 ? -27.763 -1.174  14.188  1.00 43.46  ? 105 ARG   A NE   1 
ATOM   818  C  CZ   . ARG   A 1 105 ? -27.334 -1.243  12.923  1.00 46.41  ? 105 ARG   A CZ   1 
ATOM   819  N  NH1  . ARG   A 1 105 ? -27.071 -2.424  12.366  1.00 44.36  ? 105 ARG   A NH1  1 
ATOM   820  N  NH2  . ARG   A 1 105 ? -27.183 -0.127  12.204  1.00 41.69  ? 105 ARG   A NH2  1 
ATOM   821  N  N    . ILE   A 1 106 ? -24.150 -2.142  18.863  1.00 40.87  ? 106 ILE   A N    1 
ATOM   822  C  CA   . ILE   A 1 106 ? -23.897 -1.007  19.741  1.00 43.17  ? 106 ILE   A CA   1 
ATOM   823  C  C    . ILE   A 1 106 ? -24.642 0.256   19.326  1.00 42.40  ? 106 ILE   A C    1 
ATOM   824  O  O    . ILE   A 1 106 ? -25.334 0.304   18.302  1.00 42.78  ? 106 ILE   A O    1 
ATOM   825  C  CB   . ILE   A 1 106 ? -22.389 -0.717  19.828  1.00 41.68  ? 106 ILE   A CB   1 
ATOM   826  C  CG1  . ILE   A 1 106 ? -21.891 -0.166  18.480  1.00 42.22  ? 106 ILE   A CG1  1 
ATOM   827  C  CG2  . ILE   A 1 106 ? -21.650 -1.917  20.358  1.00 39.56  ? 106 ILE   A CG2  1 
ATOM   828  C  CD1  . ILE   A 1 106 ? -20.505 0.378   18.518  1.00 40.61  ? 106 ILE   A CD1  1 
ATOM   829  N  N    . GLN   A 1 107 ? -24.457 1.288   20.125  1.00 42.07  ? 107 GLN   A N    1 
ATOM   830  C  CA   . GLN   A 1 107 ? -25.176 2.542   20.132  1.00 43.89  ? 107 GLN   A CA   1 
ATOM   831  C  C    . GLN   A 1 107 ? -24.149 3.658   20.022  1.00 40.15  ? 107 GLN   A C    1 
ATOM   832  O  O    . GLN   A 1 107 ? -22.972 3.452   20.348  1.00 36.77  ? 107 GLN   A O    1 
ATOM   833  C  CB   . GLN   A 1 107 ? -25.981 2.651   21.439  1.00 48.30  ? 107 GLN   A CB   1 
ATOM   834  C  CG   . GLN   A 1 107 ? -27.170 3.577   21.372  1.00 54.81  ? 107 GLN   A CG   1 
ATOM   835  C  CD   . GLN   A 1 107 ? -28.329 2.994   20.615  1.00 54.99  ? 107 GLN   A CD   1 
ATOM   836  O  OE1  . GLN   A 1 107 ? -28.746 3.540   19.584  1.00 61.07  ? 107 GLN   A OE1  1 
ATOM   837  N  NE2  . GLN   A 1 107 ? -28.907 1.918   21.154  1.00 55.01  ? 107 GLN   A NE2  1 
ATOM   838  N  N    . PRO   A 1 108 ? -24.534 4.836   19.532  1.00 38.11  ? 108 PRO   A N    1 
ATOM   839  C  CA   . PRO   A 1 108 ? -23.569 5.936   19.482  1.00 42.37  ? 108 PRO   A CA   1 
ATOM   840  C  C    . PRO   A 1 108 ? -23.079 6.258   20.883  1.00 48.47  ? 108 PRO   A C    1 
ATOM   841  O  O    . PRO   A 1 108 ? -23.844 6.209   21.852  1.00 48.73  ? 108 PRO   A O    1 
ATOM   842  C  CB   . PRO   A 1 108 ? -24.375 7.092   18.881  1.00 42.19  ? 108 PRO   A CB   1 
ATOM   843  C  CG   . PRO   A 1 108 ? -25.372 6.441   18.046  1.00 43.86  ? 108 PRO   A CG   1 
ATOM   844  C  CD   . PRO   A 1 108 ? -25.767 5.182   18.806  1.00 43.16  ? 108 PRO   A CD   1 
ATOM   845  N  N    . GLY   A 1 109 ? -21.785 6.565   20.989  1.00 46.38  ? 109 GLY   A N    1 
ATOM   846  C  CA   . GLY   A 1 109 ? -21.171 6.818   22.283  1.00 40.64  ? 109 GLY   A CA   1 
ATOM   847  C  C    . GLY   A 1 109 ? -20.427 5.605   22.802  1.00 43.21  ? 109 GLY   A C    1 
ATOM   848  O  O    . GLY   A 1 109 ? -19.324 5.727   23.343  1.00 42.02  ? 109 GLY   A O    1 
ATOM   849  N  N    . GLN   A 1 110 ? -21.014 4.422   22.628  1.00 47.92  ? 110 GLN   A N    1 
ATOM   850  C  CA   . GLN   A 1 110 ? -20.360 3.192   23.050  1.00 45.90  ? 110 GLN   A CA   1 
ATOM   851  C  C    . GLN   A 1 110 ? -19.088 2.921   22.238  1.00 51.52  ? 110 GLN   A C    1 
ATOM   852  O  O    . GLN   A 1 110 ? -18.958 3.308   21.070  1.00 48.43  ? 110 GLN   A O    1 
ATOM   853  C  CB   . GLN   A 1 110 ? -21.323 2.017   22.944  1.00 46.34  ? 110 GLN   A CB   1 
ATOM   854  C  CG   . GLN   A 1 110 ? -22.179 1.843   24.199  1.00 54.72  ? 110 GLN   A CG   1 
ATOM   855  C  CD   . GLN   A 1 110 ? -22.777 0.443   24.331  1.00 60.13  ? 110 GLN   A CD   1 
ATOM   856  O  OE1  . GLN   A 1 110 ? -23.074 -0.229  23.331  1.00 57.55  ? 110 GLN   A OE1  1 
ATOM   857  N  NE2  . GLN   A 1 110 ? -22.954 -0.005  25.576  1.00 62.33  ? 110 GLN   A NE2  1 
ATOM   858  N  N    . THR   A 1 111 ? -18.146 2.236   22.880  1.00 51.82  ? 111 THR   A N    1 
ATOM   859  C  CA   . THR   A 1 111 ? -16.768 2.156   22.433  1.00 46.26  ? 111 THR   A CA   1 
ATOM   860  C  C    . THR   A 1 111 ? -16.446 0.695   22.136  1.00 47.23  ? 111 THR   A C    1 
ATOM   861  O  O    . THR   A 1 111 ? -17.090 -0.213  22.668  1.00 53.69  ? 111 THR   A O    1 
ATOM   862  C  CB   . THR   A 1 111 ? -15.840 2.696   23.532  1.00 44.50  ? 111 THR   A CB   1 
ATOM   863  O  OG1  . THR   A 1 111 ? -14.548 2.977   22.998  1.00 49.99  ? 111 THR   A OG1  1 
ATOM   864  C  CG2  . THR   A 1 111 ? -15.663 1.638   24.615  1.00 43.03  ? 111 THR   A CG2  1 
ATOM   865  N  N    . PHE   A 1 112 ? -15.445 0.449   21.290  1.00 44.12  ? 112 PHE   A N    1 
ATOM   866  C  CA   . PHE   A 1 112 ? -15.046 -0.933  21.035  1.00 40.11  ? 112 PHE   A CA   1 
ATOM   867  C  C    . PHE   A 1 112 ? -13.606 -0.966  20.555  1.00 40.17  ? 112 PHE   A C    1 
ATOM   868  O  O    . PHE   A 1 112 ? -13.055 0.050   20.121  1.00 40.33  ? 112 PHE   A O    1 
ATOM   869  C  CB   . PHE   A 1 112 ? -15.964 -1.617  20.014  1.00 39.39  ? 112 PHE   A CB   1 
ATOM   870  C  CG   . PHE   A 1 112 ? -16.138 -0.843  18.723  1.00 42.27  ? 112 PHE   A CG   1 
ATOM   871  C  CD1  . PHE   A 1 112 ? -17.068 0.189   18.634  1.00 39.29  ? 112 PHE   A CD1  1 
ATOM   872  C  CD2  . PHE   A 1 112 ? -15.395 -1.178  17.585  1.00 40.96  ? 112 PHE   A CD2  1 
ATOM   873  C  CE1  . PHE   A 1 112 ? -17.236 0.892   17.470  1.00 34.70  ? 112 PHE   A CE1  1 
ATOM   874  C  CE2  . PHE   A 1 112 ? -15.563 -0.488  16.396  1.00 37.42  ? 112 PHE   A CE2  1 
ATOM   875  C  CZ   . PHE   A 1 112 ? -16.483 0.558   16.340  1.00 40.79  ? 112 PHE   A CZ   1 
ATOM   876  N  N    . SER   A 1 113 ? -12.999 -2.153  20.641  1.00 37.38  ? 113 SER   A N    1 
ATOM   877  C  CA   . SER   A 1 113 ? -11.664 -2.378  20.097  1.00 34.40  ? 113 SER   A CA   1 
ATOM   878  C  C    . SER   A 1 113 ? -11.728 -2.912  18.671  1.00 37.33  ? 113 SER   A C    1 
ATOM   879  O  O    . SER   A 1 113 ? -12.602 -3.712  18.322  1.00 36.56  ? 113 SER   A O    1 
ATOM   880  C  CB   . SER   A 1 113 ? -10.867 -3.347  20.960  1.00 32.25  ? 113 SER   A CB   1 
ATOM   881  O  OG   . SER   A 1 113 ? -10.473 -2.713  22.159  1.00 40.53  ? 113 SER   A OG   1 
ATOM   882  N  N    . VAL   A 1 114 ? -10.785 -2.470  17.847  1.00 37.60  ? 114 VAL   A N    1 
ATOM   883  C  CA   . VAL   A 1 114 ? -10.695 -2.897  16.460  1.00 32.11  ? 114 VAL   A CA   1 
ATOM   884  C  C    . VAL   A 1 114 ? -9.376  -3.635  16.271  1.00 29.61  ? 114 VAL   A C    1 
ATOM   885  O  O    . VAL   A 1 114 ? -8.312  -3.149  16.683  1.00 25.87  ? 114 VAL   A O    1 
ATOM   886  C  CB   . VAL   A 1 114 ? -10.826 -1.697  15.505  1.00 36.88  ? 114 VAL   A CB   1 
ATOM   887  C  CG1  . VAL   A 1 114 ? -10.433 -2.064  14.057  1.00 34.25  ? 114 VAL   A CG1  1 
ATOM   888  C  CG2  . VAL   A 1 114 ? -12.246 -1.149  15.583  1.00 34.33  ? 114 VAL   A CG2  1 
ATOM   889  N  N    . LEU   A 1 115 ? -9.459  -4.825  15.674  1.00 29.27  ? 115 LEU   A N    1 
ATOM   890  C  CA   . LEU   A 1 115 ? -8.283  -5.591  15.270  1.00 32.56  ? 115 LEU   A CA   1 
ATOM   891  C  C    . LEU   A 1 115 ? -8.128  -5.441  13.756  1.00 33.22  ? 115 LEU   A C    1 
ATOM   892  O  O    . LEU   A 1 115 ? -8.890  -6.038  12.983  1.00 30.22  ? 115 LEU   A O    1 
ATOM   893  C  CB   . LEU   A 1 115 ? -8.411  -7.061  15.683  1.00 26.91  ? 115 LEU   A CB   1 
ATOM   894  C  CG   . LEU   A 1 115 ? -7.193  -7.934  15.362  1.00 30.34  ? 115 LEU   A CG   1 
ATOM   895  C  CD1  . LEU   A 1 115 ? -5.986  -7.535  16.202  1.00 30.08  ? 115 LEU   A CD1  1 
ATOM   896  C  CD2  . LEU   A 1 115 ? -7.475  -9.432  15.481  1.00 31.63  ? 115 LEU   A CD2  1 
ATOM   897  N  N    . ALA   A 1 116 ? -7.156  -4.634  13.328  1.00 33.26  ? 116 ALA   A N    1 
ATOM   898  C  CA   . ALA   A 1 116 ? -6.973  -4.396  11.896  1.00 38.46  ? 116 ALA   A CA   1 
ATOM   899  C  C    . ALA   A 1 116 ? -6.271  -5.596  11.258  1.00 34.76  ? 116 ALA   A C    1 
ATOM   900  O  O    . ALA   A 1 116 ? -5.295  -6.122  11.808  1.00 35.26  ? 116 ALA   A O    1 
ATOM   901  C  CB   . ALA   A 1 116 ? -6.199  -3.102  11.652  1.00 29.28  ? 116 ALA   A CB   1 
ATOM   902  N  N    . CYS   A 1 117 ? -6.799  -6.049  10.122  1.00 29.43  ? 117 CYS   A N    1 
ATOM   903  C  CA   . CYS   A 1 117 ? -6.399  -7.322  9.532   1.00 36.69  ? 117 CYS   A CA   1 
ATOM   904  C  C    . CYS   A 1 117 ? -6.250  -7.192  8.023   1.00 41.35  ? 117 CYS   A C    1 
ATOM   905  O  O    . CYS   A 1 117 ? -7.193  -6.785  7.329   1.00 39.44  ? 117 CYS   A O    1 
ATOM   906  C  CB   . CYS   A 1 117 ? -7.416  -8.429  9.852   1.00 35.82  ? 117 CYS   A CB   1 
ATOM   907  S  SG   . CYS   A 1 117 ? -7.455  -8.949  11.577  1.00 43.30  ? 117 CYS   A SG   1 
ATOM   908  N  N    . TYR   A 1 118 ? -5.079  -7.577  7.520   1.00 42.61  ? 118 TYR   A N    1 
ATOM   909  C  CA   . TYR   A 1 118 ? -4.795  -7.589  6.090   1.00 40.91  ? 118 TYR   A CA   1 
ATOM   910  C  C    . TYR   A 1 118 ? -4.352  -8.995  5.714   1.00 40.99  ? 118 TYR   A C    1 
ATOM   911  O  O    . TYR   A 1 118 ? -3.399  -9.523  6.298   1.00 42.12  ? 118 TYR   A O    1 
ATOM   912  C  CB   . TYR   A 1 118 ? -3.739  -6.534  5.735   1.00 37.33  ? 118 TYR   A CB   1 
ATOM   913  C  CG   . TYR   A 1 118 ? -4.117  -5.164  6.254   1.00 41.74  ? 118 TYR   A CG   1 
ATOM   914  C  CD1  . TYR   A 1 118 ? -3.867  -4.826  7.587   1.00 42.38  ? 118 TYR   A CD1  1 
ATOM   915  C  CD2  . TYR   A 1 118 ? -4.777  -4.225  5.442   1.00 37.90  ? 118 TYR   A CD2  1 
ATOM   916  C  CE1  . TYR   A 1 118 ? -4.229  -3.599  8.103   1.00 38.61  ? 118 TYR   A CE1  1 
ATOM   917  C  CE2  . TYR   A 1 118 ? -5.148  -2.977  5.955   1.00 38.97  ? 118 TYR   A CE2  1 
ATOM   918  C  CZ   . TYR   A 1 118 ? -4.860  -2.669  7.296   1.00 41.87  ? 118 TYR   A CZ   1 
ATOM   919  O  OH   . TYR   A 1 118 ? -5.194  -1.451  7.878   1.00 43.84  ? 118 TYR   A OH   1 
ATOM   920  N  N    . ASN   A 1 119 ? -5.077  -9.611  4.772   1.00 43.20  ? 119 ASN   A N    1 
ATOM   921  C  CA   . ASN   A 1 119 ? -4.805  -10.977 4.303   1.00 46.76  ? 119 ASN   A CA   1 
ATOM   922  C  C    . ASN   A 1 119 ? -4.967  -11.999 5.432   1.00 48.33  ? 119 ASN   A C    1 
ATOM   923  O  O    . ASN   A 1 119 ? -4.188  -12.949 5.556   1.00 45.53  ? 119 ASN   A O    1 
ATOM   924  C  CB   . ASN   A 1 119 ? -3.415  -11.075 3.673   1.00 42.68  ? 119 ASN   A CB   1 
ATOM   925  C  CG   . ASN   A 1 119 ? -3.335  -10.368 2.354   1.00 47.53  ? 119 ASN   A CG   1 
ATOM   926  O  OD1  . ASN   A 1 119 ? -4.021  -10.733 1.399   1.00 58.13  ? 119 ASN   A OD1  1 
ATOM   927  N  ND2  . ASN   A 1 119 ? -2.509  -9.329  2.289   1.00 46.05  ? 119 ASN   A ND2  1 
ATOM   928  N  N    . GLY   A 1 120 ? -5.984  -11.788 6.270   1.00 52.43  ? 120 GLY   A N    1 
ATOM   929  C  CA   . GLY   A 1 120 ? -6.317  -12.700 7.343   1.00 53.41  ? 120 GLY   A CA   1 
ATOM   930  C  C    . GLY   A 1 120 ? -5.412  -12.644 8.562   1.00 50.91  ? 120 GLY   A C    1 
ATOM   931  O  O    . GLY   A 1 120 ? -5.653  -13.382 9.518   1.00 50.14  ? 120 GLY   A O    1 
ATOM   932  N  N    . SER   A 1 121 ? -4.383  -11.803 8.568   1.00 43.76  ? 121 SER   A N    1 
ATOM   933  C  CA   . SER   A 1 121 ? -3.488  -11.741 9.693   1.00 43.46  ? 121 SER   A CA   1 
ATOM   934  C  C    . SER   A 1 121 ? -3.709  -10.459 10.475  1.00 46.68  ? 121 SER   A C    1 
ATOM   935  O  O    . SER   A 1 121 ? -3.814  -9.366  9.889   1.00 44.09  ? 121 SER   A O    1 
ATOM   936  C  CB   . SER   A 1 121 ? -2.047  -11.837 9.278   1.00 40.05  ? 121 SER   A CB   1 
ATOM   937  O  OG   . SER   A 1 121 ? -1.784  -13.158 8.812   1.00 51.01  ? 121 SER   A OG   1 
ATOM   938  N  N    . PRO   A 1 122 ? -3.792  -10.535 11.802  1.00 41.09  ? 122 PRO   A N    1 
ATOM   939  C  CA   . PRO   A 1 122 ? -3.935  -9.315  12.610  1.00 37.45  ? 122 PRO   A CA   1 
ATOM   940  C  C    . PRO   A 1 122 ? -2.665  -8.483  12.549  1.00 38.34  ? 122 PRO   A C    1 
ATOM   941  O  O    . PRO   A 1 122 ? -1.560  -9.012  12.694  1.00 37.91  ? 122 PRO   A O    1 
ATOM   942  C  CB   . PRO   A 1 122 ? -4.179  -9.835  14.040  1.00 42.82  ? 122 PRO   A CB   1 
ATOM   943  C  CG   . PRO   A 1 122 ? -4.512  -11.282 13.914  1.00 41.89  ? 122 PRO   A CG   1 
ATOM   944  C  CD   . PRO   A 1 122 ? -4.268  -11.738 12.517  1.00 43.58  ? 122 PRO   A CD   1 
ATOM   945  N  N    . SER   A 1 123 ? -2.839  -7.182  12.364  1.00 34.16  ? 123 SER   A N    1 
ATOM   946  C  CA   . SER   A 1 123 ? -1.744  -6.229  12.302  1.00 38.07  ? 123 SER   A CA   1 
ATOM   947  C  C    . SER   A 1 123 ? -1.607  -5.341  13.527  1.00 39.76  ? 123 SER   A C    1 
ATOM   948  O  O    . SER   A 1 123 ? -0.476  -5.009  13.923  1.00 34.67  ? 123 SER   A O    1 
ATOM   949  C  CB   . SER   A 1 123 ? -1.899  -5.325  11.071  1.00 41.27  ? 123 SER   A CB   1 
ATOM   950  O  OG   . SER   A 1 123 ? -1.686  -6.075  9.893   1.00 50.11  ? 123 SER   A OG   1 
ATOM   951  N  N    . GLY   A 1 124 ? -2.719  -4.923  14.115  1.00 37.34  ? 124 GLY   A N    1 
ATOM   952  C  CA   . GLY   A 1 124 ? -2.682  -4.040  15.266  1.00 34.95  ? 124 GLY   A CA   1 
ATOM   953  C  C    . GLY   A 1 124 ? -4.058  -3.910  15.874  1.00 33.86  ? 124 GLY   A C    1 
ATOM   954  O  O    . GLY   A 1 124 ? -5.067  -4.319  15.289  1.00 35.64  ? 124 GLY   A O    1 
ATOM   955  N  N    . VAL   A 1 125 ? -4.086  -3.322  17.060  1.00 33.18  ? 125 VAL   A N    1 
ATOM   956  C  CA   . VAL   A 1 125 ? -5.315  -3.200  17.833  1.00 34.40  ? 125 VAL   A CA   1 
ATOM   957  C  C    . VAL   A 1 125 ? -5.382  -1.798  18.450  1.00 28.85  ? 125 VAL   A C    1 
ATOM   958  O  O    . VAL   A 1 125 ? -4.387  -1.281  18.971  1.00 27.70  ? 125 VAL   A O    1 
ATOM   959  C  CB   . VAL   A 1 125 ? -5.385  -4.319  18.895  1.00 32.81  ? 125 VAL   A CB   1 
ATOM   960  C  CG1  . VAL   A 1 125 ? -4.226  -4.202  19.872  1.00 30.61  ? 125 VAL   A CG1  1 
ATOM   961  C  CG2  . VAL   A 1 125 ? -6.730  -4.350  19.572  1.00 29.67  ? 125 VAL   A CG2  1 
ATOM   962  N  N    . TYR   A 1 126 ? -6.544  -1.166  18.340  1.00 24.78  ? 126 TYR   A N    1 
ATOM   963  C  CA   . TYR   A 1 126 ? -6.755  0.183   18.841  1.00 32.00  ? 126 TYR   A CA   1 
ATOM   964  C  C    . TYR   A 1 126 ? -8.211  0.309   19.261  1.00 34.73  ? 126 TYR   A C    1 
ATOM   965  O  O    . TYR   A 1 126 ? -9.060  -0.492  18.861  1.00 32.28  ? 126 TYR   A O    1 
ATOM   966  C  CB   . TYR   A 1 126 ? -6.408  1.261   17.788  1.00 37.73  ? 126 TYR   A CB   1 
ATOM   967  C  CG   . TYR   A 1 126 ? -7.002  1.029   16.400  1.00 34.79  ? 126 TYR   A CG   1 
ATOM   968  C  CD1  . TYR   A 1 126 ? -8.274  1.497   16.063  1.00 35.36  ? 126 TYR   A CD1  1 
ATOM   969  C  CD2  . TYR   A 1 126 ? -6.283  0.352   15.434  1.00 33.48  ? 126 TYR   A CD2  1 
ATOM   970  C  CE1  . TYR   A 1 126 ? -8.806  1.279   14.798  1.00 34.92  ? 126 TYR   A CE1  1 
ATOM   971  C  CE2  . TYR   A 1 126 ? -6.798  0.140   14.175  1.00 37.49  ? 126 TYR   A CE2  1 
ATOM   972  C  CZ   . TYR   A 1 126 ? -8.058  0.600   13.855  1.00 39.70  ? 126 TYR   A CZ   1 
ATOM   973  O  OH   . TYR   A 1 126 ? -8.536  0.372   12.574  1.00 38.88  ? 126 TYR   A OH   1 
ATOM   974  N  N    . GLN   A 1 127 ? -8.502  1.336   20.057  1.00 35.47  ? 127 GLN   A N    1 
ATOM   975  C  CA   . GLN   A 1 127 ? -9.856  1.559   20.549  1.00 36.02  ? 127 GLN   A CA   1 
ATOM   976  C  C    . GLN   A 1 127 ? -10.535 2.651   19.737  1.00 37.04  ? 127 GLN   A C    1 
ATOM   977  O  O    . GLN   A 1 127 ? -9.918  3.666   19.416  1.00 41.05  ? 127 GLN   A O    1 
ATOM   978  C  CB   . GLN   A 1 127 ? -9.841  1.927   22.029  1.00 37.23  ? 127 GLN   A CB   1 
ATOM   979  C  CG   . GLN   A 1 127 ? -11.206 1.997   22.659  1.00 41.02  ? 127 GLN   A CG   1 
ATOM   980  C  CD   . GLN   A 1 127 ? -11.633 0.703   23.327  1.00 43.21  ? 127 GLN   A CD   1 
ATOM   981  O  OE1  . GLN   A 1 127 ? -11.370 -0.395  22.822  1.00 44.96  ? 127 GLN   A OE1  1 
ATOM   982  N  NE2  . GLN   A 1 127 ? -12.294 0.825   24.481  1.00 45.14  ? 127 GLN   A NE2  1 
ATOM   983  N  N    . CYS   A 1 128 ? -11.804 2.419   19.395  1.00 40.07  ? 128 CYS   A N    1 
ATOM   984  C  CA   . CYS   A 1 128 ? -12.625 3.294   18.566  1.00 37.39  ? 128 CYS   A CA   1 
ATOM   985  C  C    . CYS   A 1 128 ? -13.960 3.525   19.254  1.00 39.61  ? 128 CYS   A C    1 
ATOM   986  O  O    . CYS   A 1 128 ? -14.417 2.699   20.044  1.00 38.46  ? 128 CYS   A O    1 
ATOM   987  C  CB   . CYS   A 1 128 ? -12.917 2.674   17.193  1.00 40.46  ? 128 CYS   A CB   1 
ATOM   988  S  SG   . CYS   A 1 128 ? -11.622 2.819   15.979  1.00 52.99  ? 128 CYS   A SG   1 
ATOM   989  N  N    . ALA   A 1 129 ? -14.618 4.631   18.915  1.00 43.29  ? 129 ALA   A N    1 
ATOM   990  C  CA   . ALA   A 1 129 ? -15.999 4.842   19.327  1.00 42.21  ? 129 ALA   A CA   1 
ATOM   991  C  C    . ALA   A 1 129 ? -16.902 4.951   18.104  1.00 41.22  ? 129 ALA   A C    1 
ATOM   992  O  O    . ALA   A 1 129 ? -16.481 5.401   17.031  1.00 39.98  ? 129 ALA   A O    1 
ATOM   993  C  CB   . ALA   A 1 129 ? -16.149 6.091   20.205  1.00 42.27  ? 129 ALA   A CB   1 
ATOM   994  N  N    . MET   A 1 130 ? -18.149 4.516   18.270  1.00 38.81  ? 130 MET   A N    1 
ATOM   995  C  CA   . MET   A 1 130 ? -19.156 4.673   17.226  1.00 42.90  ? 130 MET   A CA   1 
ATOM   996  C  C    . MET   A 1 130 ? -19.716 6.084   17.310  1.00 43.11  ? 130 MET   A C    1 
ATOM   997  O  O    . MET   A 1 130 ? -20.406 6.424   18.274  1.00 44.14  ? 130 MET   A O    1 
ATOM   998  C  CB   . MET   A 1 130 ? -20.278 3.648   17.373  1.00 42.72  ? 130 MET   A CB   1 
ATOM   999  C  CG   . MET   A 1 130 ? -21.405 3.827   16.371  1.00 40.25  ? 130 MET   A CG   1 
ATOM   1000 S  SD   . MET   A 1 130 ? -20.804 3.390   14.726  1.00 37.20  ? 130 MET   A SD   1 
ATOM   1001 C  CE   . MET   A 1 130 ? -20.177 1.747   15.042  1.00 35.77  ? 130 MET   A CE   1 
ATOM   1002 N  N    . ARG   A 1 131 ? -19.424 6.891   16.297  1.00 44.85  ? 131 ARG   A N    1 
ATOM   1003 C  CA   . ARG   A 1 131 ? -19.811 8.282   16.249  1.00 45.12  ? 131 ARG   A CA   1 
ATOM   1004 C  C    . ARG   A 1 131 ? -21.304 8.421   15.958  1.00 48.15  ? 131 ARG   A C    1 
ATOM   1005 O  O    . ARG   A 1 131 ? -21.981 7.442   15.622  1.00 44.86  ? 131 ARG   A O    1 
ATOM   1006 C  CB   . ARG   A 1 131 ? -18.968 8.997   15.199  1.00 48.12  ? 131 ARG   A CB   1 
ATOM   1007 C  CG   . ARG   A 1 131 ? -17.512 9.005   15.550  1.00 51.69  ? 131 ARG   A CG   1 
ATOM   1008 C  CD   . ARG   A 1 131 ? -17.171 10.311  16.198  1.00 51.85  ? 131 ARG   A CD   1 
ATOM   1009 N  NE   . ARG   A 1 131 ? -16.069 10.183  17.120  1.00 49.52  ? 131 ARG   A NE   1 
ATOM   1010 C  CZ   . ARG   A 1 131 ? -15.847 11.050  18.088  1.00 49.77  ? 131 ARG   A CZ   1 
ATOM   1011 N  NH1  . ARG   A 1 131 ? -16.649 12.096  18.222  1.00 52.44  ? 131 ARG   A NH1  1 
ATOM   1012 N  NH2  . ARG   A 1 131 ? -14.832 10.873  18.913  1.00 52.78  ? 131 ARG   A NH2  1 
ATOM   1013 N  N    . PRO   A 1 132 ? -21.853 9.636   16.112  1.00 53.45  ? 132 PRO   A N    1 
ATOM   1014 C  CA   . PRO   A 1 132 ? -23.304 9.808   15.950  1.00 53.80  ? 132 PRO   A CA   1 
ATOM   1015 C  C    . PRO   A 1 132 ? -23.724 9.925   14.504  1.00 54.21  ? 132 PRO   A C    1 
ATOM   1016 O  O    . PRO   A 1 132 ? -24.886 9.634   14.180  1.00 55.10  ? 132 PRO   A O    1 
ATOM   1017 C  CB   . PRO   A 1 132 ? -23.589 11.111  16.719  1.00 54.98  ? 132 PRO   A CB   1 
ATOM   1018 C  CG   . PRO   A 1 132 ? -22.338 11.354  17.552  1.00 55.79  ? 132 PRO   A CG   1 
ATOM   1019 C  CD   . PRO   A 1 132 ? -21.245 10.852  16.679  1.00 56.90  ? 132 PRO   A CD   1 
ATOM   1020 N  N    . ASN   A 1 133 ? -22.819 10.353  13.629  1.00 50.87  ? 133 ASN   A N    1 
ATOM   1021 C  CA   . ASN   A 1 133 ? -23.013 10.129  12.207  1.00 52.35  ? 133 ASN   A CA   1 
ATOM   1022 C  C    . ASN   A 1 133 ? -22.847 8.655   11.831  1.00 52.01  ? 133 ASN   A C    1 
ATOM   1023 O  O    . ASN   A 1 133 ? -22.921 8.330   10.642  1.00 47.89  ? 133 ASN   A O    1 
ATOM   1024 C  CB   . ASN   A 1 133 ? -22.029 10.981  11.404  1.00 55.90  ? 133 ASN   A CB   1 
ATOM   1025 C  CG   . ASN   A 1 133 ? -20.587 10.782  11.845  1.00 54.51  ? 133 ASN   A CG   1 
ATOM   1026 O  OD1  . ASN   A 1 133 ? -20.280 9.900   12.663  1.00 46.94  ? 133 ASN   A OD1  1 
ATOM   1027 N  ND2  . ASN   A 1 133 ? -19.684 11.584  11.274  1.00 52.39  ? 133 ASN   A ND2  1 
ATOM   1028 N  N    . PHE   A 1 134 ? -22.609 7.780   12.823  1.00 51.83  ? 134 PHE   A N    1 
ATOM   1029 C  CA   . PHE   A 1 134 ? -22.466 6.327   12.651  1.00 51.88  ? 134 PHE   A CA   1 
ATOM   1030 C  C    . PHE   A 1 134 ? -21.256 5.959   11.792  1.00 51.36  ? 134 PHE   A C    1 
ATOM   1031 O  O    . PHE   A 1 134 ? -21.240 4.924   11.122  1.00 48.25  ? 134 PHE   A O    1 
ATOM   1032 C  CB   . PHE   A 1 134 ? -23.741 5.700   12.083  1.00 47.32  ? 134 PHE   A CB   1 
ATOM   1033 C  CG   . PHE   A 1 134 ? -24.838 5.573   13.084  1.00 52.12  ? 134 PHE   A CG   1 
ATOM   1034 C  CD1  . PHE   A 1 134 ? -24.793 4.589   14.054  1.00 50.29  ? 134 PHE   A CD1  1 
ATOM   1035 C  CD2  . PHE   A 1 134 ? -25.917 6.450   13.070  1.00 56.28  ? 134 PHE   A CD2  1 
ATOM   1036 C  CE1  . PHE   A 1 134 ? -25.812 4.477   15.001  1.00 50.98  ? 134 PHE   A CE1  1 
ATOM   1037 C  CE2  . PHE   A 1 134 ? -26.938 6.338   14.012  1.00 56.22  ? 134 PHE   A CE2  1 
ATOM   1038 C  CZ   . PHE   A 1 134 ? -26.882 5.349   14.972  1.00 53.69  ? 134 PHE   A CZ   1 
ATOM   1039 N  N    . THR   A 1 135 ? -20.239 6.808   11.795  1.00 47.99  ? 135 THR   A N    1 
ATOM   1040 C  CA   . THR   A 1 135 ? -18.940 6.464   11.254  1.00 44.60  ? 135 THR   A CA   1 
ATOM   1041 C  C    . THR   A 1 135 ? -17.996 6.213   12.412  1.00 42.25  ? 135 THR   A C    1 
ATOM   1042 O  O    . THR   A 1 135 ? -18.308 6.508   13.562  1.00 44.20  ? 135 THR   A O    1 
ATOM   1043 C  CB   . THR   A 1 135 ? -18.394 7.589   10.370  1.00 47.80  ? 135 THR   A CB   1 
ATOM   1044 O  OG1  . THR   A 1 135 ? -17.822 8.604   11.204  1.00 51.72  ? 135 THR   A OG1  1 
ATOM   1045 C  CG2  . THR   A 1 135 ? -19.497 8.206   9.536   1.00 48.47  ? 135 THR   A CG2  1 
ATOM   1046 N  N    . ILE   A 1 136 ? -16.827 5.671   12.113  1.00 43.13  ? 136 ILE   A N    1 
ATOM   1047 C  CA   . ILE   A 1 136 ? -15.770 5.603   13.111  1.00 44.92  ? 136 ILE   A CA   1 
ATOM   1048 C  C    . ILE   A 1 136 ? -14.514 6.212   12.505  1.00 42.74  ? 136 ILE   A C    1 
ATOM   1049 O  O    . ILE   A 1 136 ? -14.285 6.138   11.293  1.00 45.26  ? 136 ILE   A O    1 
ATOM   1050 C  CB   . ILE   A 1 136 ? -15.514 4.153   13.635  1.00 45.98  ? 136 ILE   A CB   1 
ATOM   1051 C  CG1  . ILE   A 1 136 ? -14.964 3.224   12.558  1.00 38.78  ? 136 ILE   A CG1  1 
ATOM   1052 C  CG2  . ILE   A 1 136 ? -16.778 3.527   14.197  1.00 43.68  ? 136 ILE   A CG2  1 
ATOM   1053 C  CD1  . ILE   A 1 136 ? -14.457 1.935   13.120  1.00 34.20  ? 136 ILE   A CD1  1 
ATOM   1054 N  N    . LYS   A 1 137 ? -13.716 6.854   13.348  1.00 43.39  ? 137 LYS   A N    1 
ATOM   1055 C  CA   . LYS   A 1 137 ? -12.411 7.361   12.931  1.00 46.25  ? 137 LYS   A CA   1 
ATOM   1056 C  C    . LYS   A 1 137 ? -11.407 6.265   13.247  1.00 47.38  ? 137 LYS   A C    1 
ATOM   1057 O  O    . LYS   A 1 137 ? -10.920 6.148   14.373  1.00 47.63  ? 137 LYS   A O    1 
ATOM   1058 C  CB   . LYS   A 1 137 ? -12.056 8.671   13.632  1.00 49.28  ? 137 LYS   A CB   1 
ATOM   1059 C  CG   . LYS   A 1 137 ? -13.055 9.795   13.444  1.00 47.31  ? 137 LYS   A CG   1 
ATOM   1060 C  CD   . LYS   A 1 137 ? -12.613 11.068  14.145  1.00 45.79  ? 137 LYS   A CD   1 
ATOM   1061 C  CE   . LYS   A 1 137 ? -13.608 12.200  13.873  1.00 56.22  ? 137 LYS   A CE   1 
ATOM   1062 N  NZ   . LYS   A 1 137 ? -13.761 12.490  12.400  1.00 56.95  ? 137 LYS   A NZ   1 
ATOM   1063 N  N    . GLY   A 1 138 ? -11.122 5.432   12.263  1.00 46.80  ? 138 GLY   A N    1 
ATOM   1064 C  CA   . GLY   A 1 138 ? -10.209 4.343   12.519  1.00 45.17  ? 138 GLY   A CA   1 
ATOM   1065 C  C    . GLY   A 1 138 ? -8.915  4.517   11.763  1.00 41.59  ? 138 GLY   A C    1 
ATOM   1066 O  O    . GLY   A 1 138 ? -8.588  5.611   11.293  1.00 36.18  ? 138 GLY   A O    1 
ATOM   1067 N  N    . SER   A 1 139 ? -8.173  3.427   11.650  1.00 39.18  ? 139 SER   A N    1 
ATOM   1068 C  CA   . SER   A 1 139 ? -6.976  3.357   10.827  1.00 38.98  ? 139 SER   A CA   1 
ATOM   1069 C  C    . SER   A 1 139 ? -7.099  2.084   10.009  1.00 38.96  ? 139 SER   A C    1 
ATOM   1070 O  O    . SER   A 1 139 ? -6.867  0.987   10.523  1.00 47.27  ? 139 SER   A O    1 
ATOM   1071 C  CB   . SER   A 1 139 ? -5.720  3.380   11.673  1.00 40.67  ? 139 SER   A CB   1 
ATOM   1072 O  OG   . SER   A 1 139 ? -4.561  3.379   10.862  1.00 42.39  ? 139 SER   A OG   1 
ATOM   1073 N  N    . PHE   A 1 140 ? -7.503  2.233   8.751   1.00 39.79  ? 140 PHE   A N    1 
ATOM   1074 C  CA   . PHE   A 1 140 ? -7.752  1.109   7.857   1.00 41.57  ? 140 PHE   A CA   1 
ATOM   1075 C  C    . PHE   A 1 140 ? -7.113  1.391   6.510   1.00 43.71  ? 140 PHE   A C    1 
ATOM   1076 O  O    . PHE   A 1 140 ? -7.292  2.484   5.954   1.00 43.99  ? 140 PHE   A O    1 
ATOM   1077 C  CB   . PHE   A 1 140 ? -9.252  0.871   7.651   1.00 40.20  ? 140 PHE   A CB   1 
ATOM   1078 C  CG   . PHE   A 1 140 ? -9.987  0.567   8.897   1.00 41.09  ? 140 PHE   A CG   1 
ATOM   1079 C  CD1  . PHE   A 1 140 ? -9.994  -0.717  9.412   1.00 43.14  ? 140 PHE   A CD1  1 
ATOM   1080 C  CD2  . PHE   A 1 140 ? -10.663 1.561   9.567   1.00 38.87  ? 140 PHE   A CD2  1 
ATOM   1081 C  CE1  . PHE   A 1 140 ? -10.678 -1.006  10.572  1.00 41.71  ? 140 PHE   A CE1  1 
ATOM   1082 C  CE2  . PHE   A 1 140 ? -11.345 1.279   10.729  1.00 43.34  ? 140 PHE   A CE2  1 
ATOM   1083 C  CZ   . PHE   A 1 140 ? -11.354 -0.010  11.238  1.00 39.11  ? 140 PHE   A CZ   1 
ATOM   1084 N  N    . LEU   A 1 141 ? -6.384  0.409   5.994   1.00 40.58  ? 141 LEU   A N    1 
ATOM   1085 C  CA   . LEU   A 1 141 ? -5.882  0.498   4.652   1.00 41.74  ? 141 LEU   A CA   1 
ATOM   1086 C  C    . LEU   A 1 141 ? -6.731  -0.358  3.731   1.00 43.09  ? 141 LEU   A C    1 
ATOM   1087 O  O    . LEU   A 1 141 ? -7.822  -0.816  4.071   1.00 43.59  ? 141 LEU   A O    1 
ATOM   1088 C  CB   . LEU   A 1 141 ? -4.413  0.084   4.588   1.00 40.84  ? 141 LEU   A CB   1 
ATOM   1089 C  CG   . LEU   A 1 141 ? -3.425  0.983   5.326   1.00 42.43  ? 141 LEU   A CG   1 
ATOM   1090 C  CD1  . LEU   A 1 141 ? -2.055  0.368   5.227   1.00 49.24  ? 141 LEU   A CD1  1 
ATOM   1091 C  CD2  . LEU   A 1 141 ? -3.419  2.414   4.789   1.00 37.92  ? 141 LEU   A CD2  1 
ATOM   1092 N  N    . ASN   A 1 142 ? -6.207  -0.558  2.535   1.00 40.32  ? 142 ASN   A N    1 
ATOM   1093 C  CA   . ASN   A 1 142 ? -6.824  -1.364  1.493   1.00 40.65  ? 142 ASN   A CA   1 
ATOM   1094 C  C    . ASN   A 1 142 ? -6.749  -2.834  1.870   1.00 41.46  ? 142 ASN   A C    1 
ATOM   1095 O  O    . ASN   A 1 142 ? -5.685  -3.326  2.247   1.00 42.83  ? 142 ASN   A O    1 
ATOM   1096 C  CB   . ASN   A 1 142 ? -6.080  -1.099  0.198   1.00 44.68  ? 142 ASN   A CB   1 
ATOM   1097 C  CG   . ASN   A 1 142 ? -6.173  0.355   -0.208  1.00 50.66  ? 142 ASN   A CG   1 
ATOM   1098 O  OD1  . ASN   A 1 142 ? -7.243  0.940   -0.256  1.00 49.81  ? 142 ASN   A OD1  1 
ATOM   1099 N  ND2  . ASN   A 1 142 ? -5.009  0.981   -0.411  1.00 58.48  ? 142 ASN   A ND2  1 
ATOM   1100 N  N    . GLY   A 1 143 ? -7.888  -3.528  1.804   1.00 42.35  ? 143 GLY   A N    1 
ATOM   1101 C  CA   . GLY   A 1 143 ? -7.982  -4.860  2.371   1.00 43.28  ? 143 GLY   A CA   1 
ATOM   1102 C  C    . GLY   A 1 143 ? -8.139  -4.931  3.883   1.00 41.02  ? 143 GLY   A C    1 
ATOM   1103 O  O    . GLY   A 1 143 ? -7.984  -6.016  4.465   1.00 40.76  ? 143 GLY   A O    1 
ATOM   1104 N  N    . SER   A 1 144 ? -8.429  -3.820  4.545   1.00 38.65  ? 144 SER   A N    1 
ATOM   1105 C  CA   . SER   A 1 144 ? -8.887  -3.890  5.921   1.00 40.06  ? 144 SER   A CA   1 
ATOM   1106 C  C    . SER   A 1 144 ? -10.327 -4.374  6.027   1.00 42.53  ? 144 SER   A C    1 
ATOM   1107 O  O    . SER   A 1 144 ? -10.801 -4.648  7.145   1.00 41.61  ? 144 SER   A O    1 
ATOM   1108 C  CB   . SER   A 1 144 ? -8.769  -2.519  6.579   1.00 41.27  ? 144 SER   A CB   1 
ATOM   1109 O  OG   . SER   A 1 144 ? -9.393  -1.540  5.763   1.00 43.03  ? 144 SER   A OG   1 
ATOM   1110 N  N    . CYS   A 1 145 ? -11.039 -4.456  4.905   1.00 38.53  ? 145 CYS   A N    1 
ATOM   1111 C  CA   . CYS   A 1 145 ? -12.395 -4.983  4.938   1.00 39.53  ? 145 CYS   A CA   1 
ATOM   1112 C  C    . CYS   A 1 145 ? -12.439 -6.409  5.477   1.00 37.93  ? 145 CYS   A C    1 
ATOM   1113 O  O    . CYS   A 1 145 ? -11.523 -7.212  5.280   1.00 37.11  ? 145 CYS   A O    1 
ATOM   1114 C  CB   . CYS   A 1 145 ? -13.046 -4.822  3.558   1.00 42.50  ? 145 CYS   A CB   1 
ATOM   1115 S  SG   . CYS   A 1 145 ? -12.132 -5.397  2.081   1.00 41.90  ? 145 CYS   A SG   1 
ATOM   1116 N  N    . GLY   A 1 146 ? -13.482 -6.683  6.250   1.00 38.25  ? 146 GLY   A N    1 
ATOM   1117 C  CA   . GLY   A 1 146 ? -13.562 -7.902  7.019   1.00 39.95  ? 146 GLY   A CA   1 
ATOM   1118 C  C    . GLY   A 1 146 ? -12.984 -7.825  8.417   1.00 40.32  ? 146 GLY   A C    1 
ATOM   1119 O  O    . GLY   A 1 146 ? -13.221 -8.748  9.209   1.00 40.54  ? 146 GLY   A O    1 
ATOM   1120 N  N    . SER   A 1 147 ? -12.224 -6.771  8.742   1.00 35.59  ? 147 SER   A N    1 
ATOM   1121 C  CA   . SER   A 1 147 ? -11.729 -6.596  10.099  1.00 32.39  ? 147 SER   A CA   1 
ATOM   1122 C  C    . SER   A 1 147 ? -12.887 -6.270  11.020  1.00 35.59  ? 147 SER   A C    1 
ATOM   1123 O  O    . SER   A 1 147 ? -13.887 -5.670  10.602  1.00 36.71  ? 147 SER   A O    1 
ATOM   1124 C  CB   . SER   A 1 147 ? -10.688 -5.486  10.163  1.00 33.71  ? 147 SER   A CB   1 
ATOM   1125 O  OG   . SER   A 1 147 ? -9.534  -5.847  9.430   1.00 36.46  ? 147 SER   A OG   1 
ATOM   1126 N  N    . VAL   A 1 148 ? -12.757 -6.672  12.288  1.00 32.50  ? 148 VAL   A N    1 
ATOM   1127 C  CA   . VAL   A 1 148 ? -13.903 -6.630  13.184  1.00 34.49  ? 148 VAL   A CA   1 
ATOM   1128 C  C    . VAL   A 1 148 ? -13.625 -5.781  14.429  1.00 35.20  ? 148 VAL   A C    1 
ATOM   1129 O  O    . VAL   A 1 148 ? -12.479 -5.492  14.797  1.00 30.24  ? 148 VAL   A O    1 
ATOM   1130 C  CB   . VAL   A 1 148 ? -14.382 -8.046  13.586  1.00 31.84  ? 148 VAL   A CB   1 
ATOM   1131 C  CG1  . VAL   A 1 148 ? -14.681 -8.862  12.350  1.00 36.25  ? 148 VAL   A CG1  1 
ATOM   1132 C  CG2  . VAL   A 1 148 ? -13.371 -8.743  14.478  1.00 27.97  ? 148 VAL   A CG2  1 
ATOM   1133 N  N    . GLY   A 1 149 ? -14.722 -5.386  15.068  1.00 32.43  ? 149 GLY   A N    1 
ATOM   1134 C  CA   . GLY   A 1 149 ? -14.673 -4.615  16.296  1.00 33.29  ? 149 GLY   A CA   1 
ATOM   1135 C  C    . GLY   A 1 149 ? -15.424 -5.370  17.393  1.00 38.00  ? 149 GLY   A C    1 
ATOM   1136 O  O    . GLY   A 1 149 ? -16.427 -6.033  17.116  1.00 35.34  ? 149 GLY   A O    1 
ATOM   1137 N  N    . PHE   A 1 150 ? -14.927 -5.248  18.613  1.00 35.32  ? 150 PHE   A N    1 
ATOM   1138 C  CA   . PHE   A 1 150 ? -15.420 -6.109  19.674  1.00 38.49  ? 150 PHE   A CA   1 
ATOM   1139 C  C    . PHE   A 1 150 ? -15.294 -5.426  21.029  1.00 42.15  ? 150 PHE   A C    1 
ATOM   1140 O  O    . PHE   A 1 150 ? -14.456 -4.544  21.244  1.00 38.83  ? 150 PHE   A O    1 
ATOM   1141 C  CB   . PHE   A 1 150 ? -14.675 -7.444  19.706  1.00 34.22  ? 150 PHE   A CB   1 
ATOM   1142 C  CG   . PHE   A 1 150 ? -13.165 -7.319  19.733  1.00 34.72  ? 150 PHE   A CG   1 
ATOM   1143 C  CD1  . PHE   A 1 150 ? -12.451 -7.004  18.578  1.00 35.10  ? 150 PHE   A CD1  1 
ATOM   1144 C  CD2  . PHE   A 1 150 ? -12.460 -7.567  20.902  1.00 32.88  ? 150 PHE   A CD2  1 
ATOM   1145 C  CE1  . PHE   A 1 150 ? -11.063 -6.911  18.591  1.00 33.47  ? 150 PHE   A CE1  1 
ATOM   1146 C  CE2  . PHE   A 1 150 ? -11.085 -7.483  20.932  1.00 33.34  ? 150 PHE   A CE2  1 
ATOM   1147 C  CZ   . PHE   A 1 150 ? -10.375 -7.159  19.762  1.00 35.93  ? 150 PHE   A CZ   1 
ATOM   1148 N  N    . ASN   A 1 151 ? -16.147 -5.856  21.941  1.00 38.87  ? 151 ASN   A N    1 
ATOM   1149 C  CA   . ASN   A 1 151 ? -15.893 -5.720  23.363  1.00 46.94  ? 151 ASN   A CA   1 
ATOM   1150 C  C    . ASN   A 1 151 ? -15.645 -7.115  23.933  1.00 47.30  ? 151 ASN   A C    1 
ATOM   1151 O  O    . ASN   A 1 151 ? -16.423 -8.046  23.672  1.00 44.37  ? 151 ASN   A O    1 
ATOM   1152 C  CB   . ASN   A 1 151 ? -17.068 -5.025  24.055  1.00 47.30  ? 151 ASN   A CB   1 
ATOM   1153 C  CG   . ASN   A 1 151 ? -17.017 -3.505  23.894  1.00 43.80  ? 151 ASN   A CG   1 
ATOM   1154 O  OD1  . ASN   A 1 151 ? -17.856 -2.913  23.227  1.00 44.33  ? 151 ASN   A OD1  1 
ATOM   1155 N  ND2  . ASN   A 1 151 ? -16.050 -2.878  24.518  1.00 42.82  ? 151 ASN   A ND2  1 
ATOM   1156 N  N    . ILE   A 1 152 ? -14.527 -7.276  24.649  1.00 46.61  ? 152 ILE   A N    1 
ATOM   1157 C  CA   . ILE   A 1 152 ? -14.355 -8.459  25.486  1.00 53.80  ? 152 ILE   A CA   1 
ATOM   1158 C  C    . ILE   A 1 152 ? -14.627 -8.058  26.927  1.00 56.98  ? 152 ILE   A C    1 
ATOM   1159 O  O    . ILE   A 1 152 ? -13.711 -7.701  27.679  1.00 54.21  ? 152 ILE   A O    1 
ATOM   1160 C  CB   . ILE   A 1 152 ? -12.962 -9.085  25.370  1.00 47.85  ? 152 ILE   A CB   1 
ATOM   1161 C  CG1  . ILE   A 1 152 ? -12.686 -9.488  23.942  1.00 44.19  ? 152 ILE   A CG1  1 
ATOM   1162 C  CG2  . ILE   A 1 152 ? -12.889 -10.344 26.265  1.00 47.91  ? 152 ILE   A CG2  1 
ATOM   1163 C  CD1  . ILE   A 1 152 ? -11.288 -10.022 23.763  1.00 41.94  ? 152 ILE   A CD1  1 
ATOM   1164 N  N    . ASP   A 1 153 ? -15.889 -8.085  27.313  1.00 62.78  ? 153 ASP   A N    1 
ATOM   1165 C  CA   . ASP   A 1 153 ? -16.276 -7.844  28.692  1.00 70.01  ? 153 ASP   A CA   1 
ATOM   1166 C  C    . ASP   A 1 153 ? -16.790 -9.151  29.270  1.00 72.22  ? 153 ASP   A C    1 
ATOM   1167 O  O    . ASP   A 1 153 ? -17.445 -9.931  28.570  1.00 80.15  ? 153 ASP   A O    1 
ATOM   1168 C  CB   . ASP   A 1 153 ? -17.343 -6.741  28.792  1.00 70.71  ? 153 ASP   A CB   1 
ATOM   1169 C  CG   . ASP   A 1 153 ? -16.778 -5.343  28.497  1.00 73.50  ? 153 ASP   A CG   1 
ATOM   1170 O  OD1  . ASP   A 1 153 ? -15.640 -5.033  28.931  1.00 75.44  ? 153 ASP   A OD1  1 
ATOM   1171 O  OD2  . ASP   A 1 153 ? -17.469 -4.550  27.822  1.00 68.65  ? 153 ASP   A OD2  1 
ATOM   1172 N  N    . TYR   A 1 154 ? -16.456 -9.411  30.527  1.00 68.79  ? 154 TYR   A N    1 
ATOM   1173 C  CA   . TYR   A 1 154 ? -17.004 -10.564 31.219  1.00 70.60  ? 154 TYR   A CA   1 
ATOM   1174 C  C    . TYR   A 1 154 ? -16.758 -11.853 30.423  1.00 68.02  ? 154 TYR   A C    1 
ATOM   1175 O  O    . TYR   A 1 154 ? -17.685 -12.623 30.143  1.00 62.23  ? 154 TYR   A O    1 
ATOM   1176 C  CB   . TYR   A 1 154 ? -18.497 -10.351 31.488  1.00 61.99  ? 154 TYR   A CB   1 
ATOM   1177 N  N    . ASP   A 1 155 ? -15.497 -12.041 29.995  1.00 60.58  ? 155 ASP   A N    1 
ATOM   1178 C  CA   . ASP   A 1 155 ? -15.017 -13.305 29.429  1.00 60.00  ? 155 ASP   A CA   1 
ATOM   1179 C  C    . ASP   A 1 155 ? -15.528 -13.582 28.009  1.00 60.93  ? 155 ASP   A C    1 
ATOM   1180 O  O    . ASP   A 1 155 ? -15.025 -14.460 27.288  1.00 53.26  ? 155 ASP   A O    1 
ATOM   1181 C  CB   . ASP   A 1 155 ? -15.402 -14.457 30.365  1.00 54.84  ? 155 ASP   A CB   1 
ATOM   1182 C  CG   . ASP   A 1 155 ? -15.044 -15.804 29.803  1.00 56.61  ? 155 ASP   A CG   1 
ATOM   1183 O  OD1  . ASP   A 1 155 ? -13.832 -16.063 29.624  1.00 54.46  ? 155 ASP   A OD1  1 
ATOM   1184 O  OD2  . ASP   A 1 155 ? -15.973 -16.595 29.522  1.00 57.14  ? 155 ASP   A OD2  1 
ATOM   1185 N  N    . CYS   A 1 156 ? -16.514 -12.813 27.583  1.00 59.99  ? 156 CYS   A N    1 
ATOM   1186 C  CA   . CYS   A 1 156 ? -17.239 -13.072 26.353  1.00 53.20  ? 156 CYS   A CA   1 
ATOM   1187 C  C    . CYS   A 1 156 ? -16.958 -11.956 25.350  1.00 53.68  ? 156 CYS   A C    1 
ATOM   1188 O  O    . CYS   A 1 156 ? -17.068 -10.763 25.694  1.00 47.55  ? 156 CYS   A O    1 
ATOM   1189 C  CB   . CYS   A 1 156 ? -18.721 -13.194 26.685  1.00 49.44  ? 156 CYS   A CB   1 
ATOM   1190 S  SG   . CYS   A 1 156 ? -19.788 -13.451 25.327  1.00 52.13  ? 156 CYS   A SG   1 
ATOM   1191 N  N    . VAL   A 1 157 ? -16.575 -12.349 24.124  1.00 50.60  ? 157 VAL   A N    1 
ATOM   1192 C  CA   . VAL   A 1 157 ? -16.311 -11.408 23.031  1.00 45.12  ? 157 VAL   A CA   1 
ATOM   1193 C  C    . VAL   A 1 157 ? -17.629 -10.976 22.400  1.00 45.66  ? 157 VAL   A C    1 
ATOM   1194 O  O    . VAL   A 1 157 ? -18.332 -11.791 21.792  1.00 43.45  ? 157 VAL   A O    1 
ATOM   1195 C  CB   . VAL   A 1 157 ? -15.382 -12.021 21.970  1.00 45.16  ? 157 VAL   A CB   1 
ATOM   1196 C  CG1  . VAL   A 1 157 ? -15.176 -11.050 20.792  1.00 36.90  ? 157 VAL   A CG1  1 
ATOM   1197 C  CG2  . VAL   A 1 157 ? -14.040 -12.397 22.574  1.00 46.04  ? 157 VAL   A CG2  1 
ATOM   1198 N  N    . SER   A 1 158 ? -17.958 -9.681  22.527  1.00 45.04  ? 158 SER   A N    1 
ATOM   1199 C  CA   . SER   A 1 158 ? -19.146 -9.086  21.904  1.00 42.56  ? 158 SER   A CA   1 
ATOM   1200 C  C    . SER   A 1 158 ? -18.739 -8.429  20.589  1.00 40.09  ? 158 SER   A C    1 
ATOM   1201 O  O    . SER   A 1 158 ? -18.209 -7.313  20.563  1.00 39.25  ? 158 SER   A O    1 
ATOM   1202 C  CB   . SER   A 1 158 ? -19.808 -8.074  22.827  1.00 39.33  ? 158 SER   A CB   1 
ATOM   1203 O  OG   . SER   A 1 158 ? -20.509 -8.721  23.860  1.00 52.15  ? 158 SER   A OG   1 
ATOM   1204 N  N    . PHE   A 1 159 ? -18.992 -9.113  19.493  1.00 41.61  ? 159 PHE   A N    1 
ATOM   1205 C  CA   . PHE   A 1 159 ? -18.695 -8.522  18.205  1.00 37.68  ? 159 PHE   A CA   1 
ATOM   1206 C  C    . PHE   A 1 159 ? -19.740 -7.466  17.879  1.00 37.19  ? 159 PHE   A C    1 
ATOM   1207 O  O    . PHE   A 1 159 ? -20.941 -7.701  18.028  1.00 41.33  ? 159 PHE   A O    1 
ATOM   1208 C  CB   . PHE   A 1 159 ? -18.633 -9.619  17.154  1.00 34.52  ? 159 PHE   A CB   1 
ATOM   1209 C  CG   . PHE   A 1 159 ? -17.409 -10.479 17.281  1.00 35.71  ? 159 PHE   A CG   1 
ATOM   1210 C  CD1  . PHE   A 1 159 ? -16.156 -9.969  16.967  1.00 34.07  ? 159 PHE   A CD1  1 
ATOM   1211 C  CD2  . PHE   A 1 159 ? -17.495 -11.770 17.753  1.00 40.77  ? 159 PHE   A CD2  1 
ATOM   1212 C  CE1  . PHE   A 1 159 ? -15.015 -10.730 17.093  1.00 30.88  ? 159 PHE   A CE1  1 
ATOM   1213 C  CE2  . PHE   A 1 159 ? -16.350 -12.548 17.874  1.00 40.59  ? 159 PHE   A CE2  1 
ATOM   1214 C  CZ   . PHE   A 1 159 ? -15.106 -12.020 17.536  1.00 35.49  ? 159 PHE   A CZ   1 
ATOM   1215 N  N    . CYS   A 1 160 ? -19.281 -6.277  17.487  1.00 35.20  ? 160 CYS   A N    1 
ATOM   1216 C  CA   . CYS   A 1 160 ? -20.189 -5.214  17.085  1.00 34.67  ? 160 CYS   A CA   1 
ATOM   1217 C  C    . CYS   A 1 160 ? -19.896 -4.604  15.709  1.00 39.61  ? 160 CYS   A C    1 
ATOM   1218 O  O    . CYS   A 1 160 ? -20.825 -4.063  15.079  1.00 36.55  ? 160 CYS   A O    1 
ATOM   1219 C  CB   . CYS   A 1 160 ? -20.197 -4.099  18.139  1.00 32.75  ? 160 CYS   A CB   1 
ATOM   1220 S  SG   . CYS   A 1 160 ? -18.618 -3.236  18.447  1.00 35.80  ? 160 CYS   A SG   1 
ATOM   1221 N  N    . TYR   A 1 161 ? -18.668 -4.688  15.204  1.00 35.14  ? 161 TYR   A N    1 
ATOM   1222 C  CA   . TYR   A 1 161 ? -18.308 -3.979  13.983  1.00 39.51  ? 161 TYR   A CA   1 
ATOM   1223 C  C    . TYR   A 1 161 ? -17.604 -4.909  13.011  1.00 34.47  ? 161 TYR   A C    1 
ATOM   1224 O  O    . TYR   A 1 161 ? -16.663 -5.604  13.398  1.00 36.89  ? 161 TYR   A O    1 
ATOM   1225 C  CB   . TYR   A 1 161 ? -17.409 -2.779  14.307  1.00 37.26  ? 161 TYR   A CB   1 
ATOM   1226 C  CG   . TYR   A 1 161 ? -17.094 -1.931  13.108  1.00 35.21  ? 161 TYR   A CG   1 
ATOM   1227 C  CD1  . TYR   A 1 161 ? -18.102 -1.222  12.473  1.00 34.28  ? 161 TYR   A CD1  1 
ATOM   1228 C  CD2  . TYR   A 1 161 ? -15.784 -1.795  12.636  1.00 34.52  ? 161 TYR   A CD2  1 
ATOM   1229 C  CE1  . TYR   A 1 161 ? -17.828 -0.428  11.382  1.00 39.29  ? 161 TYR   A CE1  1 
ATOM   1230 C  CE2  . TYR   A 1 161 ? -15.495 -0.992  11.529  1.00 31.52  ? 161 TYR   A CE2  1 
ATOM   1231 C  CZ   . TYR   A 1 161 ? -16.526 -0.316  10.906  1.00 35.38  ? 161 TYR   A CZ   1 
ATOM   1232 O  OH   . TYR   A 1 161 ? -16.296 0.484   9.807   1.00 33.55  ? 161 TYR   A OH   1 
ATOM   1233 N  N    . MET   A 1 162 ? -18.064 -4.937  11.765  1.00 36.38  ? 162 MET   A N    1 
ATOM   1234 C  CA   . MET   A 1 162 ? -17.218 -5.373  10.654  1.00 40.04  ? 162 MET   A CA   1 
ATOM   1235 C  C    . MET   A 1 162 ? -16.919 -4.191  9.749   1.00 33.72  ? 162 MET   A C    1 
ATOM   1236 O  O    . MET   A 1 162 ? -17.809 -3.398  9.420   1.00 29.55  ? 162 MET   A O    1 
ATOM   1237 C  CB   . MET   A 1 162 ? -17.823 -6.495  9.809   1.00 34.23  ? 162 MET   A CB   1 
ATOM   1238 C  CG   . MET   A 1 162 ? -16.718 -7.202  9.007   1.00 36.46  ? 162 MET   A CG   1 
ATOM   1239 S  SD   . MET   A 1 162 ? -17.133 -8.821  8.296   1.00 37.33  ? 162 MET   A SD   1 
ATOM   1240 C  CE   . MET   A 1 162 ? -18.770 -8.450  7.689   1.00 31.36  ? 162 MET   A CE   1 
ATOM   1241 N  N    . HIS   A 1 163 ? -15.659 -4.067  9.361   1.00 34.46  ? 163 HIS   A N    1 
ATOM   1242 C  CA   . HIS   A 1 163 ? -15.287 -2.955  8.508   1.00 37.54  ? 163 HIS   A CA   1 
ATOM   1243 C  C    . HIS   A 1 163 ? -15.569 -3.279  7.049   1.00 34.86  ? 163 HIS   A C    1 
ATOM   1244 O  O    . HIS   A 1 163 ? -15.310 -4.393  6.578   1.00 32.30  ? 163 HIS   A O    1 
ATOM   1245 C  CB   . HIS   A 1 163 ? -13.821 -2.593  8.686   1.00 37.40  ? 163 HIS   A CB   1 
ATOM   1246 C  CG   . HIS   A 1 163 ? -13.434 -1.364  7.937   1.00 38.75  ? 163 HIS   A CG   1 
ATOM   1247 N  ND1  . HIS   A 1 163 ? -14.069 -0.154  8.126   1.00 38.81  ? 163 HIS   A ND1  1 
ATOM   1248 C  CD2  . HIS   A 1 163 ? -12.473 -1.147  7.014   1.00 38.83  ? 163 HIS   A CD2  1 
ATOM   1249 C  CE1  . HIS   A 1 163 ? -13.524 0.755   7.342   1.00 39.71  ? 163 HIS   A CE1  1 
ATOM   1250 N  NE2  . HIS   A 1 163 ? -12.549 0.180   6.660   1.00 42.91  ? 163 HIS   A NE2  1 
ATOM   1251 N  N    . HIS   A 1 164 ? -16.103 -2.293  6.337   1.00 32.05  ? 164 HIS   A N    1 
ATOM   1252 C  CA   . HIS   A 1 164 ? -16.383 -2.422  4.912   1.00 39.18  ? 164 HIS   A CA   1 
ATOM   1253 C  C    . HIS   A 1 164 ? -15.645 -1.412  4.048   1.00 41.23  ? 164 HIS   A C    1 
ATOM   1254 O  O    . HIS   A 1 164 ? -14.962 -1.808  3.095   1.00 38.59  ? 164 HIS   A O    1 
ATOM   1255 C  CB   . HIS   A 1 164 ? -17.883 -2.278  4.645   1.00 36.80  ? 164 HIS   A CB   1 
ATOM   1256 C  CG   . HIS   A 1 164 ? -18.672 -3.461  5.060   1.00 33.11  ? 164 HIS   A CG   1 
ATOM   1257 N  ND1  . HIS   A 1 164 ? -19.365 -4.237  4.162   1.00 35.34  ? 164 HIS   A ND1  1 
ATOM   1258 C  CD2  . HIS   A 1 164 ? -18.882 -4.002  6.279   1.00 34.26  ? 164 HIS   A CD2  1 
ATOM   1259 C  CE1  . HIS   A 1 164 ? -19.964 -5.219  4.811   1.00 39.24  ? 164 HIS   A CE1  1 
ATOM   1260 N  NE2  . HIS   A 1 164 ? -19.692 -5.094  6.099   1.00 36.02  ? 164 HIS   A NE2  1 
ATOM   1261 N  N    . MET   A 1 165 ? -15.784 -0.114  4.341   1.00 37.15  ? 165 MET   A N    1 
ATOM   1262 C  CA   . MET   A 1 165 ? -15.498 0.916   3.357   1.00 40.52  ? 165 MET   A CA   1 
ATOM   1263 C  C    . MET   A 1 165 ? -14.980 2.178   4.026   1.00 41.08  ? 165 MET   A C    1 
ATOM   1264 O  O    . MET   A 1 165 ? -15.455 2.576   5.094   1.00 41.94  ? 165 MET   A O    1 
ATOM   1265 C  CB   . MET   A 1 165 ? -16.757 1.238   2.535   1.00 37.50  ? 165 MET   A CB   1 
ATOM   1266 C  CG   . MET   A 1 165 ? -17.862 1.917   3.298   1.00 36.74  ? 165 MET   A CG   1 
ATOM   1267 S  SD   . MET   A 1 165 ? -19.453 1.954   2.425   1.00 39.28  ? 165 MET   A SD   1 
ATOM   1268 C  CE   . MET   A 1 165 ? -19.032 2.554   0.791   1.00 48.17  ? 165 MET   A CE   1 
ATOM   1269 N  N    . GLU   A 1 166 ? -14.003 2.805   3.394   1.00 38.00  ? 166 GLU   A N    1 
ATOM   1270 C  CA   . GLU   A 1 166 ? -13.665 4.160   3.778   1.00 41.24  ? 166 GLU   A CA   1 
ATOM   1271 C  C    . GLU   A 1 166 ? -14.502 5.118   2.941   1.00 44.21  ? 166 GLU   A C    1 
ATOM   1272 O  O    . GLU   A 1 166 ? -14.927 4.791   1.827   1.00 43.30  ? 166 GLU   A O    1 
ATOM   1273 C  CB   . GLU   A 1 166 ? -12.170 4.427   3.599   1.00 39.57  ? 166 GLU   A CB   1 
ATOM   1274 C  CG   . GLU   A 1 166 ? -11.754 5.791   4.067   1.00 39.49  ? 166 GLU   A CG   1 
ATOM   1275 C  CD   . GLU   A 1 166 ? -10.260 5.978   4.068   1.00 41.93  ? 166 GLU   A CD   1 
ATOM   1276 O  OE1  . GLU   A 1 166 ? -9.794  6.895   3.353   1.00 37.98  ? 166 GLU   A OE1  1 
ATOM   1277 O  OE2  . GLU   A 1 166 ? -9.564  5.203   4.784   1.00 40.29  ? 166 GLU   A OE2  1 
ATOM   1278 N  N    . LEU   A 1 167 ? -14.781 6.281   3.504   1.00 45.85  ? 167 LEU   A N    1 
ATOM   1279 C  CA   . LEU   A 1 167 ? -15.642 7.241   2.790   1.00 46.16  ? 167 LEU   A CA   1 
ATOM   1280 C  C    . LEU   A 1 167 ? -14.744 8.332   2.224   1.00 48.27  ? 167 LEU   A C    1 
ATOM   1281 O  O    . LEU   A 1 167 ? -13.578 8.394   2.614   1.00 46.83  ? 167 LEU   A O    1 
ATOM   1282 C  CB   . LEU   A 1 167 ? -16.708 7.778   3.749   1.00 46.87  ? 167 LEU   A CB   1 
ATOM   1283 C  CG   . LEU   A 1 167 ? -17.713 6.767   4.289   1.00 44.92  ? 167 LEU   A CG   1 
ATOM   1284 C  CD1  . LEU   A 1 167 ? -18.662 7.441   5.261   1.00 46.70  ? 167 LEU   A CD1  1 
ATOM   1285 C  CD2  . LEU   A 1 167 ? -18.493 6.119   3.161   1.00 51.14  ? 167 LEU   A CD2  1 
ATOM   1286 N  N    . PRO   A 1 168 ? -15.204 9.181   1.274   1.00 54.49  ? 168 PRO   A N    1 
ATOM   1287 C  CA   . PRO   A 1 168 ? -14.393 10.301  0.810   1.00 54.98  ? 168 PRO   A CA   1 
ATOM   1288 C  C    . PRO   A 1 168 ? -13.885 11.218  1.930   1.00 56.79  ? 168 PRO   A C    1 
ATOM   1289 O  O    . PRO   A 1 168 ? -12.847 11.805  1.745   1.00 59.45  ? 168 PRO   A O    1 
ATOM   1290 C  CB   . PRO   A 1 168 ? -15.312 11.052  -0.147  1.00 56.59  ? 168 PRO   A CB   1 
ATOM   1291 C  CG   . PRO   A 1 168 ? -16.692 10.520  0.105   1.00 56.79  ? 168 PRO   A CG   1 
ATOM   1292 C  CD   . PRO   A 1 168 ? -16.446 9.084   0.481   1.00 54.82  ? 168 PRO   A CD   1 
ATOM   1293 N  N    . THR   A 1 169 ? -14.602 11.299  3.051   1.00 52.70  ? 169 THR   A N    1 
ATOM   1294 C  CA   . THR   A 1 169 ? -14.174 12.101  4.222   1.00 53.96  ? 169 THR   A CA   1 
ATOM   1295 C  C    . THR   A 1 169 ? -12.869 11.538  4.761   1.00 50.93  ? 169 THR   A C    1 
ATOM   1296 O  O    . THR   A 1 169 ? -12.055 12.310  5.266   1.00 52.78  ? 169 THR   A O    1 
ATOM   1297 C  CB   . THR   A 1 169 ? -15.193 11.973  5.353   1.00 55.91  ? 169 THR   A CB   1 
ATOM   1298 O  OG1  . THR   A 1 169 ? -16.490 12.250  4.836   1.00 64.39  ? 169 THR   A OG1  1 
ATOM   1299 C  CG2  . THR   A 1 169 ? -14.928 12.921  6.501   1.00 51.51  ? 169 THR   A CG2  1 
ATOM   1300 N  N    . GLY   A 1 170 ? -12.715 10.227  4.709   1.00 46.68  ? 170 GLY   A N    1 
ATOM   1301 C  CA   . GLY   A 1 170 ? -11.526 9.605   5.298   1.00 46.83  ? 170 GLY   A CA   1 
ATOM   1302 C  C    . GLY   A 1 170 ? -11.950 8.875   6.532   1.00 41.30  ? 170 GLY   A C    1 
ATOM   1303 O  O    . GLY   A 1 170 ? -11.096 8.458   7.303   1.00 40.19  ? 170 GLY   A O    1 
ATOM   1304 N  N    . VAL   A 1 171 ? -13.257 8.792   6.700   1.00 39.22  ? 171 VAL   A N    1 
ATOM   1305 C  CA   . VAL   A 1 171 ? -13.784 8.106   7.898   1.00 45.25  ? 171 VAL   A CA   1 
ATOM   1306 C  C    . VAL   A 1 171 ? -14.254 6.725   7.488   1.00 45.03  ? 171 VAL   A C    1 
ATOM   1307 O  O    . VAL   A 1 171 ? -14.437 6.502   6.288   1.00 40.35  ? 171 VAL   A O    1 
ATOM   1308 C  CB   . VAL   A 1 171 ? -14.838 8.900   8.681   1.00 42.07  ? 171 VAL   A CB   1 
ATOM   1309 C  CG1  . VAL   A 1 171 ? -14.372 10.309  8.993   1.00 45.53  ? 171 VAL   A CG1  1 
ATOM   1310 C  CG2  . VAL   A 1 171 ? -16.181 8.901   7.982   1.00 47.20  ? 171 VAL   A CG2  1 
ATOM   1311 N  N    . HIS   A 1 172 ? -14.475 5.865   8.470   1.00 42.55  ? 172 HIS   A N    1 
ATOM   1312 C  CA   . HIS   A 1 172 ? -14.757 4.452   8.167   1.00 38.78  ? 172 HIS   A CA   1 
ATOM   1313 C  C    . HIS   A 1 172 ? -16.187 4.037   8.473   1.00 40.24  ? 172 HIS   A C    1 
ATOM   1314 O  O    . HIS   A 1 172 ? -16.690 4.378   9.539   1.00 37.74  ? 172 HIS   A O    1 
ATOM   1315 C  CB   . HIS   A 1 172 ? -13.673 3.682   8.896   1.00 37.85  ? 172 HIS   A CB   1 
ATOM   1316 C  CG   . HIS   A 1 172 ? -12.316 4.145   8.500   1.00 42.92  ? 172 HIS   A CG   1 
ATOM   1317 N  ND1  . HIS   A 1 172 ? -11.552 4.950   9.304   1.00 41.93  ? 172 HIS   A ND1  1 
ATOM   1318 C  CD2  . HIS   A 1 172 ? -11.603 3.948   7.375   1.00 41.55  ? 172 HIS   A CD2  1 
ATOM   1319 C  CE1  . HIS   A 1 172 ? -10.415 5.213   8.703   1.00 40.95  ? 172 HIS   A CE1  1 
ATOM   1320 N  NE2  . HIS   A 1 172 ? -10.422 4.611   7.523   1.00 40.14  ? 172 HIS   A NE2  1 
ATOM   1321 N  N    . ALA   A 1 173 ? -16.794 3.305   7.546   1.00 39.08  ? 173 ALA   A N    1 
ATOM   1322 C  CA   . ALA   A 1 173 ? -18.157 2.823   7.711   1.00 39.38  ? 173 ALA   A CA   1 
ATOM   1323 C  C    . ALA   A 1 173 ? -18.223 1.302   7.635   1.00 36.46  ? 173 ALA   A C    1 
ATOM   1324 O  O    . ALA   A 1 173 ? -17.476 0.652   6.897   1.00 33.70  ? 173 ALA   A O    1 
ATOM   1325 C  CB   . ALA   A 1 173 ? -19.093 3.424   6.654   1.00 40.05  ? 173 ALA   A CB   1 
ATOM   1326 N  N    . GLY   A 1 174 ? -19.150 0.747   8.378   1.00 35.84  ? 174 GLY   A N    1 
ATOM   1327 C  CA   . GLY   A 1 174 ? -19.303 -0.681  8.393   1.00 37.34  ? 174 GLY   A CA   1 
ATOM   1328 C  C    . GLY   A 1 174 ? -20.615 -1.109  8.987   1.00 39.81  ? 174 GLY   A C    1 
ATOM   1329 O  O    . GLY   A 1 174 ? -21.587 -0.348  9.016   1.00 37.19  ? 174 GLY   A O    1 
ATOM   1330 N  N    . THR   A 1 175 ? -20.619 -2.355  9.473   1.00 40.46  ? 175 THR   A N    1 
ATOM   1331 C  CA   . THR   A 1 175 ? -21.830 -3.085  9.799   1.00 41.32  ? 175 THR   A CA   1 
ATOM   1332 C  C    . THR   A 1 175 ? -21.690 -3.792  11.144  1.00 40.67  ? 175 THR   A C    1 
ATOM   1333 O  O    . THR   A 1 175 ? -20.580 -4.061  11.624  1.00 37.33  ? 175 THR   A O    1 
ATOM   1334 C  CB   . THR   A 1 175 ? -22.148 -4.125  8.699   1.00 40.13  ? 175 THR   A CB   1 
ATOM   1335 O  OG1  . THR   A 1 175 ? -21.182 -5.189  8.726   1.00 32.71  ? 175 THR   A OG1  1 
ATOM   1336 C  CG2  . THR   A 1 175 ? -22.166 -3.471  7.325   1.00 38.89  ? 175 THR   A CG2  1 
ATOM   1337 N  N    . ASP   A 1 176 ? -22.831 -4.148  11.727  1.00 39.58  ? 176 ASP   A N    1 
ATOM   1338 C  CA   . ASP   A 1 176 ? -22.798 -5.150  12.780  1.00 40.86  ? 176 ASP   A CA   1 
ATOM   1339 C  C    . ASP   A 1 176 ? -22.478 -6.491  12.121  1.00 40.65  ? 176 ASP   A C    1 
ATOM   1340 O  O    . ASP   A 1 176 ? -22.189 -6.567  10.921  1.00 40.48  ? 176 ASP   A O    1 
ATOM   1341 C  CB   . ASP   A 1 176 ? -24.102 -5.144  13.579  1.00 44.64  ? 176 ASP   A CB   1 
ATOM   1342 C  CG   . ASP   A 1 176 ? -25.336 -5.480  12.743  1.00 43.19  ? 176 ASP   A CG   1 
ATOM   1343 O  OD1  . ASP   A 1 176 ? -25.253 -6.252  11.769  1.00 41.00  ? 176 ASP   A OD1  1 
ATOM   1344 O  OD2  . ASP   A 1 176 ? -26.429 -4.998  13.116  1.00 46.26  ? 176 ASP   A OD2  1 
ATOM   1345 N  N    . LEU   A 1 177 ? -22.525 -7.575  12.901  1.00 41.30  ? 177 LEU   A N    1 
ATOM   1346 C  CA   . LEU   A 1 177 ? -22.267 -8.916  12.377  1.00 38.51  ? 177 LEU   A CA   1 
ATOM   1347 C  C    . LEU   A 1 177 ? -23.520 -9.625  11.891  1.00 39.60  ? 177 LEU   A C    1 
ATOM   1348 O  O    . LEU   A 1 177 ? -23.422 -10.764 11.432  1.00 45.61  ? 177 LEU   A O    1 
ATOM   1349 C  CB   . LEU   A 1 177 ? -21.562 -9.793  13.414  1.00 36.66  ? 177 LEU   A CB   1 
ATOM   1350 C  CG   . LEU   A 1 177 ? -20.032 -9.691  13.502  1.00 35.09  ? 177 LEU   A CG   1 
ATOM   1351 C  CD1  . LEU   A 1 177 ? -19.426 -10.106 12.192  1.00 40.34  ? 177 LEU   A CD1  1 
ATOM   1352 C  CD2  . LEU   A 1 177 ? -19.519 -8.313  13.927  1.00 34.40  ? 177 LEU   A CD2  1 
ATOM   1353 N  N    . GLU   A 1 178 ? -24.685 -8.996  11.978  1.00 41.13  ? 178 GLU   A N    1 
ATOM   1354 C  CA   . GLU   A 1 178 ? -25.852 -9.448  11.231  1.00 46.78  ? 178 GLU   A CA   1 
ATOM   1355 C  C    . GLU   A 1 178 ? -25.965 -8.735  9.893   1.00 54.21  ? 178 GLU   A C    1 
ATOM   1356 O  O    . GLU   A 1 178 ? -26.968 -8.897  9.180   1.00 54.54  ? 178 GLU   A O    1 
ATOM   1357 C  CB   . GLU   A 1 178 ? -27.113 -9.237  12.056  1.00 45.06  ? 178 GLU   A CB   1 
ATOM   1358 C  CG   . GLU   A 1 178 ? -27.079 -10.063 13.315  1.00 47.71  ? 178 GLU   A CG   1 
ATOM   1359 C  CD   . GLU   A 1 178 ? -28.421 -10.193 13.972  1.00 52.04  ? 178 GLU   A CD   1 
ATOM   1360 O  OE1  . GLU   A 1 178 ? -29.288 -9.319  13.760  1.00 47.36  ? 178 GLU   A OE1  1 
ATOM   1361 O  OE2  . GLU   A 1 178 ? -28.613 -11.202 14.683  1.00 62.66  ? 178 GLU   A OE2  1 
ATOM   1362 N  N    . GLY   A 1 179 ? -24.962 -7.937  9.554   1.00 58.39  ? 179 GLY   A N    1 
ATOM   1363 C  CA   . GLY   A 1 179 ? -24.896 -7.336  8.253   1.00 54.05  ? 179 GLY   A CA   1 
ATOM   1364 C  C    . GLY   A 1 179 ? -25.280 -5.878  8.171   1.00 52.10  ? 179 GLY   A C    1 
ATOM   1365 O  O    . GLY   A 1 179 ? -24.668 -5.134  7.409   1.00 55.80  ? 179 GLY   A O    1 
ATOM   1366 N  N    . ASN   A 1 180 ? -26.305 -5.451  8.886   1.00 47.27  ? 180 ASN   A N    1 
ATOM   1367 C  CA   . ASN   A 1 180 ? -26.835 -4.123  8.625   1.00 45.35  ? 180 ASN   A CA   1 
ATOM   1368 C  C    . ASN   A 1 180 ? -25.827 -3.041  8.972   1.00 42.13  ? 180 ASN   A C    1 
ATOM   1369 O  O    . ASN   A 1 180 ? -25.200 -3.061  10.037  1.00 40.84  ? 180 ASN   A O    1 
ATOM   1370 C  CB   . ASN   A 1 180 ? -28.130 -3.921  9.393   1.00 48.83  ? 180 ASN   A CB   1 
ATOM   1371 C  CG   . ASN   A 1 180 ? -29.224 -4.799  8.874   1.00 52.23  ? 180 ASN   A CG   1 
ATOM   1372 O  OD1  . ASN   A 1 180 ? -30.010 -4.398  7.999   1.00 52.39  ? 180 ASN   A OD1  1 
ATOM   1373 N  ND2  . ASN   A 1 180 ? -29.259 -6.030  9.368   1.00 53.77  ? 180 ASN   A ND2  1 
ATOM   1374 N  N    . PHE   A 1 181 ? -25.673 -2.095  8.050   1.00 45.53  ? 181 PHE   A N    1 
ATOM   1375 C  CA   . PHE   A 1 181 ? -24.747 -0.991  8.248   1.00 43.26  ? 181 PHE   A CA   1 
ATOM   1376 C  C    . PHE   A 1 181 ? -25.182 -0.146  9.423   1.00 38.93  ? 181 PHE   A C    1 
ATOM   1377 O  O    . PHE   A 1 181 ? -26.372 0.117   9.616   1.00 38.08  ? 181 PHE   A O    1 
ATOM   1378 C  CB   . PHE   A 1 181 ? -24.680 -0.102  7.008   1.00 40.56  ? 181 PHE   A CB   1 
ATOM   1379 C  CG   . PHE   A 1 181 ? -23.673 -0.545  5.985   1.00 43.44  ? 181 PHE   A CG   1 
ATOM   1380 C  CD1  . PHE   A 1 181 ? -22.368 -0.051  6.012   1.00 42.29  ? 181 PHE   A CD1  1 
ATOM   1381 C  CD2  . PHE   A 1 181 ? -24.037 -1.427  4.965   1.00 44.12  ? 181 PHE   A CD2  1 
ATOM   1382 C  CE1  . PHE   A 1 181 ? -21.431 -0.439  5.045   1.00 38.69  ? 181 PHE   A CE1  1 
ATOM   1383 C  CE2  . PHE   A 1 181 ? -23.111 -1.822  3.991   1.00 41.56  ? 181 PHE   A CE2  1 
ATOM   1384 C  CZ   . PHE   A 1 181 ? -21.803 -1.328  4.038   1.00 39.38  ? 181 PHE   A CZ   1 
ATOM   1385 N  N    . TYR   A 1 182 ? -24.204 0.273   10.210  1.00 42.99  ? 182 TYR   A N    1 
ATOM   1386 C  CA   . TYR   A 1 182 ? -24.392 1.429   11.072  1.00 43.17  ? 182 TYR   A CA   1 
ATOM   1387 C  C    . TYR   A 1 182 ? -24.591 2.664   10.197  1.00 45.10  ? 182 TYR   A C    1 
ATOM   1388 O  O    . TYR   A 1 182 ? -23.844 2.894   9.237   1.00 42.72  ? 182 TYR   A O    1 
ATOM   1389 C  CB   . TYR   A 1 182 ? -23.189 1.582   12.002  1.00 40.47  ? 182 TYR   A CB   1 
ATOM   1390 C  CG   . TYR   A 1 182 ? -23.181 0.513   13.060  1.00 41.21  ? 182 TYR   A CG   1 
ATOM   1391 C  CD1  . TYR   A 1 182 ? -23.994 0.624   14.184  1.00 40.46  ? 182 TYR   A CD1  1 
ATOM   1392 C  CD2  . TYR   A 1 182 ? -22.417 -0.645  12.902  1.00 39.74  ? 182 TYR   A CD2  1 
ATOM   1393 C  CE1  . TYR   A 1 182 ? -24.016 -0.374  15.154  1.00 44.75  ? 182 TYR   A CE1  1 
ATOM   1394 C  CE2  . TYR   A 1 182 ? -22.426 -1.653  13.857  1.00 40.05  ? 182 TYR   A CE2  1 
ATOM   1395 C  CZ   . TYR   A 1 182 ? -23.235 -1.517  14.982  1.00 46.81  ? 182 TYR   A CZ   1 
ATOM   1396 O  OH   . TYR   A 1 182 ? -23.262 -2.511  15.938  1.00 47.71  ? 182 TYR   A OH   1 
ATOM   1397 N  N    . GLY   A 1 183 ? -25.631 3.433   10.494  1.00 48.98  ? 183 GLY   A N    1 
ATOM   1398 C  CA   . GLY   A 1 183 ? -25.908 4.631   9.739   1.00 48.78  ? 183 GLY   A CA   1 
ATOM   1399 C  C    . GLY   A 1 183 ? -26.579 4.342   8.421   1.00 45.84  ? 183 GLY   A C    1 
ATOM   1400 O  O    . GLY   A 1 183 ? -26.948 3.205   8.109   1.00 46.85  ? 183 GLY   A O    1 
ATOM   1401 N  N    . PRO   A 1 184 ? -26.739 5.390   7.601   1.00 42.63  ? 184 PRO   A N    1 
ATOM   1402 C  CA   . PRO   A 1 184 ? -27.536 5.281   6.384   1.00 43.87  ? 184 PRO   A CA   1 
ATOM   1403 C  C    . PRO   A 1 184 ? -26.804 4.641   5.218   1.00 46.79  ? 184 PRO   A C    1 
ATOM   1404 O  O    . PRO   A 1 184 ? -27.357 4.600   4.116   1.00 51.14  ? 184 PRO   A O    1 
ATOM   1405 C  CB   . PRO   A 1 184 ? -27.846 6.754   6.081   1.00 43.83  ? 184 PRO   A CB   1 
ATOM   1406 C  CG   . PRO   A 1 184 ? -26.587 7.441   6.481   1.00 43.86  ? 184 PRO   A CG   1 
ATOM   1407 C  CD   . PRO   A 1 184 ? -26.089 6.706   7.709   1.00 46.64  ? 184 PRO   A CD   1 
ATOM   1408 N  N    . PHE   A 1 185 ? -25.604 4.124   5.459   1.00 45.21  ? 185 PHE   A N    1 
ATOM   1409 C  CA   . PHE   A 1 185 ? -24.640 3.849   4.409   1.00 44.97  ? 185 PHE   A CA   1 
ATOM   1410 C  C    . PHE   A 1 185 ? -24.957 2.556   3.659   1.00 42.83  ? 185 PHE   A C    1 
ATOM   1411 O  O    . PHE   A 1 185 ? -25.784 1.743   4.073   1.00 42.67  ? 185 PHE   A O    1 
ATOM   1412 C  CB   . PHE   A 1 185 ? -23.239 3.807   5.010   1.00 46.02  ? 185 PHE   A CB   1 
ATOM   1413 C  CG   . PHE   A 1 185 ? -22.882 5.054   5.774   1.00 46.07  ? 185 PHE   A CG   1 
ATOM   1414 C  CD1  . PHE   A 1 185 ? -22.827 6.288   5.125   1.00 49.27  ? 185 PHE   A CD1  1 
ATOM   1415 C  CD2  . PHE   A 1 185 ? -22.622 5.007   7.132   1.00 43.86  ? 185 PHE   A CD2  1 
ATOM   1416 C  CE1  . PHE   A 1 185 ? -22.505 7.455   5.817   1.00 47.64  ? 185 PHE   A CE1  1 
ATOM   1417 C  CE2  . PHE   A 1 185 ? -22.299 6.168   7.829   1.00 48.27  ? 185 PHE   A CE2  1 
ATOM   1418 C  CZ   . PHE   A 1 185 ? -22.242 7.397   7.163   1.00 47.26  ? 185 PHE   A CZ   1 
ATOM   1419 N  N    . VAL   A 1 186 ? -24.285 2.397   2.514   1.00 47.53  ? 186 VAL   A N    1 
ATOM   1420 C  CA   . VAL   A 1 186 ? -24.487 1.297   1.576   1.00 46.57  ? 186 VAL   A CA   1 
ATOM   1421 C  C    . VAL   A 1 186 ? -23.129 0.895   1.008   1.00 42.57  ? 186 VAL   A C    1 
ATOM   1422 O  O    . VAL   A 1 186 ? -22.182 1.680   0.997   1.00 43.28  ? 186 VAL   A O    1 
ATOM   1423 C  CB   . VAL   A 1 186 ? -25.466 1.681   0.441   1.00 45.29  ? 186 VAL   A CB   1 
ATOM   1424 C  CG1  . VAL   A 1 186 ? -26.909 1.681   0.945   1.00 41.52  ? 186 VAL   A CG1  1 
ATOM   1425 C  CG2  . VAL   A 1 186 ? -25.115 3.051   -0.085  1.00 43.90  ? 186 VAL   A CG2  1 
ATOM   1426 N  N    . ASP   A 1 187 ? -23.029 -0.351  0.551   1.00 43.80  ? 187 ASP   A N    1 
ATOM   1427 C  CA   . ASP   A 1 187 ? -21.742 -0.896  0.120   1.00 42.87  ? 187 ASP   A CA   1 
ATOM   1428 C  C    . ASP   A 1 187 ? -21.615 -0.758  -1.394  1.00 45.26  ? 187 ASP   A C    1 
ATOM   1429 O  O    . ASP   A 1 187 ? -21.567 -1.730  -2.149  1.00 43.30  ? 187 ASP   A O    1 
ATOM   1430 C  CB   . ASP   A 1 187 ? -21.569 -2.353  0.578   1.00 38.18  ? 187 ASP   A CB   1 
ATOM   1431 C  CG   . ASP   A 1 187 ? -22.755 -3.249  0.226   1.00 39.15  ? 187 ASP   A CG   1 
ATOM   1432 O  OD1  . ASP   A 1 187 ? -23.756 -2.765  -0.348  1.00 44.42  ? 187 ASP   A OD1  1 
ATOM   1433 O  OD2  . ASP   A 1 187 ? -22.671 -4.462  0.509   1.00 38.68  ? 187 ASP   A OD2  1 
ATOM   1434 N  N    . ARG   A 1 188 ? -21.570 0.498   -1.823  1.00 48.45  ? 188 ARG   A N    1 
ATOM   1435 C  CA   . ARG   A 1 188 ? -21.300 0.855   -3.207  1.00 54.27  ? 188 ARG   A CA   1 
ATOM   1436 C  C    . ARG   A 1 188 ? -20.250 1.953   -3.230  1.00 54.83  ? 188 ARG   A C    1 
ATOM   1437 O  O    . ARG   A 1 188 ? -20.075 2.683   -2.246  1.00 51.09  ? 188 ARG   A O    1 
ATOM   1438 C  CB   . ARG   A 1 188 ? -22.587 1.299   -3.927  1.00 56.32  ? 188 ARG   A CB   1 
ATOM   1439 C  CG   . ARG   A 1 188 ? -23.655 0.237   -3.803  1.00 61.95  ? 188 ARG   A CG   1 
ATOM   1440 C  CD   . ARG   A 1 188 ? -24.726 0.285   -4.842  1.00 62.57  ? 188 ARG   A CD   1 
ATOM   1441 N  NE   . ARG   A 1 188 ? -25.546 1.487   -4.771  1.00 72.57  ? 188 ARG   A NE   1 
ATOM   1442 C  CZ   . ARG   A 1 188 ? -26.550 1.662   -3.911  1.00 74.70  ? 188 ARG   A CZ   1 
ATOM   1443 N  NH1  . ARG   A 1 188 ? -26.862 0.714   -3.032  1.00 67.14  ? 188 ARG   A NH1  1 
ATOM   1444 N  NH2  . ARG   A 1 188 ? -27.245 2.793   -3.929  1.00 75.08  ? 188 ARG   A NH2  1 
ATOM   1445 N  N    . GLN   A 1 189 ? -19.520 2.042   -4.348  1.00 62.36  ? 189 GLN   A N    1 
ATOM   1446 C  CA   . GLN   A 1 189 ? -18.650 3.196   -4.584  1.00 60.97  ? 189 GLN   A CA   1 
ATOM   1447 C  C    . GLN   A 1 189 ? -19.499 4.312   -5.187  1.00 59.10  ? 189 GLN   A C    1 
ATOM   1448 O  O    . GLN   A 1 189 ? -19.492 4.588   -6.389  1.00 59.76  ? 189 GLN   A O    1 
ATOM   1449 C  CB   . GLN   A 1 189 ? -17.456 2.852   -5.461  1.00 59.75  ? 189 GLN   A CB   1 
ATOM   1450 C  CG   . GLN   A 1 189 ? -16.342 3.903   -5.337  1.00 59.07  ? 189 GLN   A CG   1 
ATOM   1451 C  CD   . GLN   A 1 189 ? -15.733 3.973   -3.932  1.00 55.68  ? 189 GLN   A CD   1 
ATOM   1452 O  OE1  . GLN   A 1 189 ? -14.988 3.084   -3.516  1.00 52.53  ? 189 GLN   A OE1  1 
ATOM   1453 N  NE2  . GLN   A 1 189 ? -16.061 5.032   -3.197  1.00 52.94  ? 189 GLN   A NE2  1 
ATOM   1454 N  N    . THR   A 1 190 ? -20.288 4.915   -4.312  1.00 57.69  ? 190 THR   A N    1 
ATOM   1455 C  CA   . THR   A 1 190 ? -21.035 6.121   -4.596  1.00 58.11  ? 190 THR   A CA   1 
ATOM   1456 C  C    . THR   A 1 190 ? -20.650 7.128   -3.527  1.00 57.60  ? 190 THR   A C    1 
ATOM   1457 O  O    . THR   A 1 190 ? -20.168 6.757   -2.451  1.00 59.59  ? 190 THR   A O    1 
ATOM   1458 C  CB   . THR   A 1 190 ? -22.553 5.869   -4.594  1.00 58.58  ? 190 THR   A CB   1 
ATOM   1459 O  OG1  . THR   A 1 190 ? -22.942 5.282   -3.344  1.00 51.93  ? 190 THR   A OG1  1 
ATOM   1460 C  CG2  . THR   A 1 190 ? -22.939 4.922   -5.742  1.00 55.56  ? 190 THR   A CG2  1 
ATOM   1461 N  N    . ALA   A 1 191 ? -20.827 8.407   -3.833  1.00 56.90  ? 191 ALA   A N    1 
ATOM   1462 C  CA   . ALA   A 1 191 ? -20.494 9.439   -2.863  1.00 55.40  ? 191 ALA   A CA   1 
ATOM   1463 C  C    . ALA   A 1 191 ? -21.496 9.383   -1.707  1.00 55.46  ? 191 ALA   A C    1 
ATOM   1464 O  O    . ALA   A 1 191 ? -22.710 9.423   -1.927  1.00 62.15  ? 191 ALA   A O    1 
ATOM   1465 C  CB   . ALA   A 1 191 ? -20.487 10.802  -3.549  1.00 49.18  ? 191 ALA   A CB   1 
ATOM   1466 N  N    . GLN   A 1 192 ? -21.006 9.243   -0.480  1.00 52.94  ? 192 GLN   A N    1 
ATOM   1467 C  CA   . GLN   A 1 192 ? -21.885 9.053   0.672   1.00 60.83  ? 192 GLN   A CA   1 
ATOM   1468 C  C    . GLN   A 1 192 ? -21.458 9.969   1.807   1.00 64.72  ? 192 GLN   A C    1 
ATOM   1469 O  O    . GLN   A 1 192 ? -20.290 9.969   2.213   1.00 62.50  ? 192 GLN   A O    1 
ATOM   1470 C  CB   . GLN   A 1 192 ? -21.898 7.599   1.156   1.00 54.16  ? 192 GLN   A CB   1 
ATOM   1471 C  CG   . GLN   A 1 192 ? -22.503 6.639   0.161   1.00 55.86  ? 192 GLN   A CG   1 
ATOM   1472 C  CD   . GLN   A 1 192 ? -22.457 5.202   0.622   1.00 52.00  ? 192 GLN   A CD   1 
ATOM   1473 O  OE1  . GLN   A 1 192 ? -22.727 4.892   1.788   1.00 51.99  ? 192 GLN   A OE1  1 
ATOM   1474 N  NE2  . GLN   A 1 192 ? -22.115 4.311   -0.292  1.00 53.21  ? 192 GLN   A NE2  1 
ATOM   1475 N  N    . ALA   A 1 193 ? -22.407 10.728  2.330   1.00 61.04  ? 193 ALA   A N    1 
ATOM   1476 C  CA   . ALA   A 1 193 ? -22.095 11.795  3.262   1.00 68.59  ? 193 ALA   A CA   1 
ATOM   1477 C  C    . ALA   A 1 193 ? -22.406 11.354  4.686   1.00 67.46  ? 193 ALA   A C    1 
ATOM   1478 O  O    . ALA   A 1 193 ? -23.546 10.978  4.998   1.00 62.70  ? 193 ALA   A O    1 
ATOM   1479 C  CB   . ALA   A 1 193 ? -22.866 13.067  2.911   1.00 70.98  ? 193 ALA   A CB   1 
ATOM   1480 N  N    . ALA   A 1 194 ? -21.386 11.390  5.539   1.00 64.03  ? 194 ALA   A N    1 
ATOM   1481 C  CA   . ALA   A 1 194 ? -21.622 11.466  6.971   1.00 62.63  ? 194 ALA   A CA   1 
ATOM   1482 C  C    . ALA   A 1 194 ? -22.157 12.848  7.320   1.00 62.80  ? 194 ALA   A C    1 
ATOM   1483 O  O    . ALA   A 1 194 ? -21.884 13.837  6.629   1.00 62.04  ? 194 ALA   A O    1 
ATOM   1484 C  CB   . ALA   A 1 194 ? -20.334 11.194  7.752   1.00 56.79  ? 194 ALA   A CB   1 
ATOM   1485 N  N    . GLY   A 1 195 ? -22.924 12.912  8.404   1.00 63.24  ? 195 GLY   A N    1 
ATOM   1486 C  CA   . GLY   A 1 195 ? -23.453 14.163  8.901   1.00 59.38  ? 195 GLY   A CA   1 
ATOM   1487 C  C    . GLY   A 1 195 ? -22.507 14.889  9.840   1.00 55.49  ? 195 GLY   A C    1 
ATOM   1488 O  O    . GLY   A 1 195 ? -21.295 14.658  9.858   1.00 51.96  ? 195 GLY   A O    1 
ATOM   1489 N  N    . THR   A 1 196 ? -23.072 15.806  10.619  1.00 55.17  ? 196 THR   A N    1 
ATOM   1490 C  CA   . THR   A 1 196 ? -22.268 16.500  11.614  1.00 53.22  ? 196 THR   A CA   1 
ATOM   1491 C  C    . THR   A 1 196 ? -21.803 15.529  12.692  1.00 54.51  ? 196 THR   A C    1 
ATOM   1492 O  O    . THR   A 1 196 ? -22.537 14.628  13.108  1.00 54.11  ? 196 THR   A O    1 
ATOM   1493 C  CB   . THR   A 1 196 ? -23.054 17.653  12.222  1.00 51.43  ? 196 THR   A CB   1 
ATOM   1494 O  OG1  . THR   A 1 196 ? -24.265 17.151  12.787  1.00 58.27  ? 196 THR   A OG1  1 
ATOM   1495 C  CG2  . THR   A 1 196 ? -23.375 18.697  11.162  1.00 58.39  ? 196 THR   A CG2  1 
ATOM   1496 N  N    . ASP   A 1 197 ? -20.559 15.700  13.130  1.00 60.48  ? 197 ASP   A N    1 
ATOM   1497 C  CA   . ASP   A 1 197 ? -19.962 14.794  14.104  1.00 59.43  ? 197 ASP   A CA   1 
ATOM   1498 C  C    . ASP   A 1 197 ? -20.128 15.403  15.498  1.00 53.73  ? 197 ASP   A C    1 
ATOM   1499 O  O    . ASP   A 1 197 ? -19.205 15.974  16.079  1.00 53.04  ? 197 ASP   A O    1 
ATOM   1500 C  CB   . ASP   A 1 197 ? -18.501 14.522  13.751  1.00 57.47  ? 197 ASP   A CB   1 
ATOM   1501 C  CG   . ASP   A 1 197 ? -17.959 13.307  14.465  1.00 60.11  ? 197 ASP   A CG   1 
ATOM   1502 O  OD1  . ASP   A 1 197 ? -18.792 12.586  15.053  1.00 60.75  ? 197 ASP   A OD1  1 
ATOM   1503 O  OD2  . ASP   A 1 197 ? -16.724 13.088  14.461  1.00 58.10  ? 197 ASP   A OD2  1 
ATOM   1504 N  N    . THR   A 1 198 ? -21.338 15.283  16.038  1.00 49.18  ? 198 THR   A N    1 
ATOM   1505 C  CA   . THR   A 1 198 ? -21.578 15.812  17.373  1.00 53.45  ? 198 THR   A CA   1 
ATOM   1506 C  C    . THR   A 1 198 ? -20.656 15.119  18.366  1.00 50.37  ? 198 THR   A C    1 
ATOM   1507 O  O    . THR   A 1 198 ? -20.442 13.905  18.310  1.00 50.64  ? 198 THR   A O    1 
ATOM   1508 C  CB   . THR   A 1 198 ? -23.042 15.646  17.795  1.00 46.42  ? 198 THR   A CB   1 
ATOM   1509 O  OG1  . THR   A 1 198 ? -23.421 14.270  17.690  1.00 50.63  ? 198 THR   A OG1  1 
ATOM   1510 C  CG2  . THR   A 1 198 ? -23.951 16.478  16.912  1.00 47.63  ? 198 THR   A CG2  1 
ATOM   1511 N  N    . THR   A 1 199 ? -20.075 15.905  19.252  1.00 45.51  ? 199 THR   A N    1 
ATOM   1512 C  CA   . THR   A 1 199 ? -19.165 15.356  20.235  1.00 48.41  ? 199 THR   A CA   1 
ATOM   1513 C  C    . THR   A 1 199 ? -19.950 14.735  21.395  1.00 49.15  ? 199 THR   A C    1 
ATOM   1514 O  O    . THR   A 1 199 ? -21.024 15.226  21.783  1.00 44.58  ? 199 THR   A O    1 
ATOM   1515 C  CB   . THR   A 1 199 ? -18.224 16.459  20.701  1.00 45.53  ? 199 THR   A CB   1 
ATOM   1516 O  OG1  . THR   A 1 199 ? -17.827 17.214  19.550  1.00 43.30  ? 199 THR   A OG1  1 
ATOM   1517 C  CG2  . THR   A 1 199 ? -16.978 15.867  21.352  1.00 43.76  ? 199 THR   A CG2  1 
ATOM   1518 N  N    . ILE   A 1 200 ? -19.434 13.620  21.915  1.00 47.54  ? 200 ILE   A N    1 
ATOM   1519 C  CA   . ILE   A 1 200 ? -20.183 12.789  22.857  1.00 46.13  ? 200 ILE   A CA   1 
ATOM   1520 C  C    . ILE   A 1 200 ? -19.992 13.380  24.252  1.00 42.58  ? 200 ILE   A C    1 
ATOM   1521 O  O    . ILE   A 1 200 ? -19.044 13.047  24.971  1.00 39.38  ? 200 ILE   A O    1 
ATOM   1522 C  CB   . ILE   A 1 200 ? -19.767 11.317  22.794  1.00 41.85  ? 200 ILE   A CB   1 
ATOM   1523 C  CG1  . ILE   A 1 200 ? -19.818 10.819  21.356  1.00 49.40  ? 200 ILE   A CG1  1 
ATOM   1524 C  CG2  . ILE   A 1 200 ? -20.697 10.456  23.658  1.00 39.69  ? 200 ILE   A CG2  1 
ATOM   1525 C  CD1  . ILE   A 1 200 ? -18.463 10.711  20.682  1.00 49.48  ? 200 ILE   A CD1  1 
ATOM   1526 N  N    . THR   A 1 201 ? -20.930 14.244  24.644  1.00 41.47  ? 201 THR   A N    1 
ATOM   1527 C  CA   . THR   A 1 201 ? -20.777 15.026  25.867  1.00 43.24  ? 201 THR   A CA   1 
ATOM   1528 C  C    . THR   A 1 201 ? -20.535 14.143  27.087  1.00 35.87  ? 201 THR   A C    1 
ATOM   1529 O  O    . THR   A 1 201 ? -19.637 14.424  27.893  1.00 35.26  ? 201 THR   A O    1 
ATOM   1530 C  CB   . THR   A 1 201 ? -22.009 15.905  26.067  1.00 46.61  ? 201 THR   A CB   1 
ATOM   1531 O  OG1  . THR   A 1 201 ? -22.299 16.607  24.845  1.00 39.64  ? 201 THR   A OG1  1 
ATOM   1532 C  CG2  . THR   A 1 201 ? -21.779 16.881  27.214  1.00 41.58  ? 201 THR   A CG2  1 
ATOM   1533 N  N    . VAL   A 1 202 ? -21.294 13.053  27.222  1.00 35.56  ? 202 VAL   A N    1 
ATOM   1534 C  CA   . VAL   A 1 202 ? -21.162 12.220  28.415  1.00 36.63  ? 202 VAL   A CA   1 
ATOM   1535 C  C    . VAL   A 1 202 ? -19.772 11.603  28.505  1.00 34.12  ? 202 VAL   A C    1 
ATOM   1536 O  O    . VAL   A 1 202 ? -19.260 11.349  29.601  1.00 32.99  ? 202 VAL   A O    1 
ATOM   1537 C  CB   . VAL   A 1 202 ? -22.287 11.165  28.438  1.00 39.87  ? 202 VAL   A CB   1 
ATOM   1538 C  CG1  . VAL   A 1 202 ? -22.193 10.240  27.249  1.00 38.29  ? 202 VAL   A CG1  1 
ATOM   1539 C  CG2  . VAL   A 1 202 ? -22.321 10.409  29.789  1.00 40.48  ? 202 VAL   A CG2  1 
ATOM   1540 N  N    . ASN   A 1 203 ? -19.108 11.412  27.373  1.00 39.52  ? 203 ASN   A N    1 
ATOM   1541 C  CA   . ASN   A 1 203 ? -17.754 10.881  27.443  1.00 38.89  ? 203 ASN   A CA   1 
ATOM   1542 C  C    . ASN   A 1 203 ? -16.738 11.963  27.804  1.00 39.55  ? 203 ASN   A C    1 
ATOM   1543 O  O    . ASN   A 1 203 ? -15.819 11.707  28.601  1.00 36.71  ? 203 ASN   A O    1 
ATOM   1544 C  CB   . ASN   A 1 203 ? -17.389 10.201  26.127  1.00 37.06  ? 203 ASN   A CB   1 
ATOM   1545 C  CG   . ASN   A 1 203 ? -18.078 8.864   25.960  1.00 37.27  ? 203 ASN   A CG   1 
ATOM   1546 O  OD1  . ASN   A 1 203 ? -19.213 8.662   26.388  1.00 34.45  ? 203 ASN   A OD1  1 
ATOM   1547 N  ND2  . ASN   A 1 203 ? -17.379 7.931   25.349  1.00 41.24  ? 203 ASN   A ND2  1 
ATOM   1548 N  N    . VAL   A 1 204 ? -16.876 13.169  27.229  1.00 37.37  ? 204 VAL   A N    1 
ATOM   1549 C  CA   . VAL   A 1 204 ? -15.962 14.253  27.592  1.00 37.19  ? 204 VAL   A CA   1 
ATOM   1550 C  C    . VAL   A 1 204 ? -15.958 14.416  29.096  1.00 35.87  ? 204 VAL   A C    1 
ATOM   1551 O  O    . VAL   A 1 204 ? -14.895 14.511  29.727  1.00 35.66  ? 204 VAL   A O    1 
ATOM   1552 C  CB   . VAL   A 1 204 ? -16.346 15.573  26.890  1.00 38.23  ? 204 VAL   A CB   1 
ATOM   1553 C  CG1  . VAL   A 1 204 ? -15.372 16.679  27.272  1.00 36.66  ? 204 VAL   A CG1  1 
ATOM   1554 C  CG2  . VAL   A 1 204 ? -16.364 15.406  25.387  1.00 38.50  ? 204 VAL   A CG2  1 
ATOM   1555 N  N    . LEU   A 1 205 ? -17.155 14.375  29.691  1.00 35.12  ? 205 LEU   A N    1 
ATOM   1556 C  CA   . LEU   A 1 205 ? -17.316 14.487  31.138  1.00 34.49  ? 205 LEU   A CA   1 
ATOM   1557 C  C    . LEU   A 1 205 ? -16.599 13.366  31.877  1.00 33.73  ? 205 LEU   A C    1 
ATOM   1558 O  O    . LEU   A 1 205 ? -15.918 13.614  32.879  1.00 34.91  ? 205 LEU   A O    1 
ATOM   1559 C  CB   . LEU   A 1 205 ? -18.807 14.491  31.482  1.00 31.32  ? 205 LEU   A CB   1 
ATOM   1560 C  CG   . LEU   A 1 205 ? -19.524 15.735  30.955  1.00 29.41  ? 205 LEU   A CG   1 
ATOM   1561 C  CD1  . LEU   A 1 205 ? -21.017 15.570  30.953  1.00 29.76  ? 205 LEU   A CD1  1 
ATOM   1562 C  CD2  . LEU   A 1 205 ? -19.103 16.937  31.772  1.00 33.58  ? 205 LEU   A CD2  1 
ATOM   1563 N  N    . ALA   A 1 206 ? -16.751 12.122  31.407  1.00 36.86  ? 206 ALA   A N    1 
ATOM   1564 C  CA   . ALA   A 1 206 ? -16.076 10.998  32.056  1.00 36.23  ? 206 ALA   A CA   1 
ATOM   1565 C  C    . ALA   A 1 206 ? -14.566 11.137  31.944  1.00 39.05  ? 206 ALA   A C    1 
ATOM   1566 O  O    . ALA   A 1 206 ? -13.831 10.858  32.907  1.00 33.03  ? 206 ALA   A O    1 
ATOM   1567 C  CB   . ALA   A 1 206 ? -16.536 9.677   31.435  1.00 37.26  ? 206 ALA   A CB   1 
ATOM   1568 N  N    . TRP   A 1 207 ? -14.096 11.566  30.758  1.00 38.32  ? 207 TRP   A N    1 
ATOM   1569 C  CA   . TRP   A 1 207 ? -12.678 11.832  30.546  1.00 37.79  ? 207 TRP   A CA   1 
ATOM   1570 C  C    . TRP   A 1 207 ? -12.186 12.964  31.451  1.00 39.75  ? 207 TRP   A C    1 
ATOM   1571 O  O    . TRP   A 1 207 ? -11.030 12.942  31.895  1.00 41.25  ? 207 TRP   A O    1 
ATOM   1572 C  CB   . TRP   A 1 207 ? -12.423 12.142  29.061  1.00 38.74  ? 207 TRP   A CB   1 
ATOM   1573 C  CG   . TRP   A 1 207 ? -11.032 12.686  28.779  1.00 35.42  ? 207 TRP   A CG   1 
ATOM   1574 C  CD1  . TRP   A 1 207 ? -9.859  11.985  28.760  1.00 34.44  ? 207 TRP   A CD1  1 
ATOM   1575 C  CD2  . TRP   A 1 207 ? -10.686 14.041  28.508  1.00 32.89  ? 207 TRP   A CD2  1 
ATOM   1576 N  NE1  . TRP   A 1 207 ? -8.811  12.820  28.483  1.00 30.50  ? 207 TRP   A NE1  1 
ATOM   1577 C  CE2  . TRP   A 1 207 ? -9.291  14.090  28.329  1.00 34.13  ? 207 TRP   A CE2  1 
ATOM   1578 C  CE3  . TRP   A 1 207 ? -11.424 15.221  28.382  1.00 37.43  ? 207 TRP   A CE3  1 
ATOM   1579 C  CZ2  . TRP   A 1 207 ? -8.617  15.274  28.034  1.00 36.68  ? 207 TRP   A CZ2  1 
ATOM   1580 C  CZ3  . TRP   A 1 207 ? -10.750 16.403  28.093  1.00 36.78  ? 207 TRP   A CZ3  1 
ATOM   1581 C  CH2  . TRP   A 1 207 ? -9.361  16.416  27.919  1.00 37.58  ? 207 TRP   A CH2  1 
ATOM   1582 N  N    . LEU   A 1 208 ? -13.048 13.938  31.760  1.00 37.21  ? 208 LEU   A N    1 
ATOM   1583 C  CA   . LEU   A 1 208 ? -12.707 14.939  32.773  1.00 40.79  ? 208 LEU   A CA   1 
ATOM   1584 C  C    . LEU   A 1 208 ? -12.649 14.318  34.165  1.00 41.96  ? 208 LEU   A C    1 
ATOM   1585 O  O    . LEU   A 1 208 ? -11.660 14.490  34.883  1.00 44.77  ? 208 LEU   A O    1 
ATOM   1586 C  CB   . LEU   A 1 208 ? -13.700 16.097  32.731  1.00 34.24  ? 208 LEU   A CB   1 
ATOM   1587 C  CG   . LEU   A 1 208 ? -13.440 16.854  31.430  1.00 34.71  ? 208 LEU   A CG   1 
ATOM   1588 C  CD1  . LEU   A 1 208 ? -14.554 17.817  31.098  1.00 36.49  ? 208 LEU   A CD1  1 
ATOM   1589 C  CD2  . LEU   A 1 208 ? -12.097 17.564  31.511  1.00 39.18  ? 208 LEU   A CD2  1 
ATOM   1590 N  N    . TYR   A 1 209 ? -13.697 13.596  34.573  1.00 39.21  ? 209 TYR   A N    1 
ATOM   1591 C  CA   . TYR   A 1 209 ? -13.634 12.903  35.859  1.00 41.44  ? 209 TYR   A CA   1 
ATOM   1592 C  C    . TYR   A 1 209 ? -12.360 12.073  35.961  1.00 45.27  ? 209 TYR   A C    1 
ATOM   1593 O  O    . TYR   A 1 209 ? -11.688 12.066  37.002  1.00 42.03  ? 209 TYR   A O    1 
ATOM   1594 C  CB   . TYR   A 1 209 ? -14.851 11.998  36.044  1.00 36.51  ? 209 TYR   A CB   1 
ATOM   1595 C  CG   . TYR   A 1 209 ? -16.030 12.696  36.596  1.00 35.40  ? 209 TYR   A CG   1 
ATOM   1596 C  CD1  . TYR   A 1 209 ? -15.969 13.316  37.842  1.00 40.45  ? 209 TYR   A CD1  1 
ATOM   1597 C  CD2  . TYR   A 1 209 ? -17.214 12.753  35.881  1.00 34.45  ? 209 TYR   A CD2  1 
ATOM   1598 C  CE1  . TYR   A 1 209 ? -17.070 13.984  38.368  1.00 41.16  ? 209 TYR   A CE1  1 
ATOM   1599 C  CE2  . TYR   A 1 209 ? -18.333 13.404  36.397  1.00 40.97  ? 209 TYR   A CE2  1 
ATOM   1600 C  CZ   . TYR   A 1 209 ? -18.252 14.021  37.641  1.00 41.72  ? 209 TYR   A CZ   1 
ATOM   1601 O  OH   . TYR   A 1 209 ? -19.339 14.675  38.151  1.00 37.67  ? 209 TYR   A OH   1 
ATOM   1602 N  N    . ALA   A 1 210 ? -12.012 11.371  34.876  1.00 42.99  ? 210 ALA   A N    1 
ATOM   1603 C  CA   . ALA   A 1 210 ? -10.760 10.630  34.839  1.00 42.77  ? 210 ALA   A CA   1 
ATOM   1604 C  C    . ALA   A 1 210 ? -9.578  11.543  35.120  1.00 46.24  ? 210 ALA   A C    1 
ATOM   1605 O  O    . ALA   A 1 210 ? -8.620  11.142  35.800  1.00 43.66  ? 210 ALA   A O    1 
ATOM   1606 C  CB   . ALA   A 1 210 ? -10.598 9.969   33.478  1.00 44.19  ? 210 ALA   A CB   1 
ATOM   1607 N  N    . ALA   A 1 211 ? -9.659  12.781  34.642  1.00 48.99  ? 211 ALA   A N    1 
ATOM   1608 C  CA   . ALA   A 1 211 ? -8.547  13.744  34.812  1.00 52.65  ? 211 ALA   A CA   1 
ATOM   1609 C  C    . ALA   A 1 211 ? -8.352  14.133  36.274  1.00 52.56  ? 211 ALA   A C    1 
ATOM   1610 O  O    . ALA   A 1 211 ? -7.201  14.194  36.713  1.00 55.84  ? 211 ALA   A O    1 
ATOM   1611 C  CB   . ALA   A 1 211 ? -8.793  14.946  33.965  1.00 48.23  ? 211 ALA   A CB   1 
ATOM   1612 N  N    . VAL   A 1 212 ? -9.440  14.407  36.976  1.00 46.07  ? 212 VAL   A N    1 
ATOM   1613 C  CA   . VAL   A 1 212 ? -9.363  14.739  38.423  1.00 50.34  ? 212 VAL   A CA   1 
ATOM   1614 C  C    . VAL   A 1 212 ? -8.691  13.573  39.158  1.00 53.96  ? 212 VAL   A C    1 
ATOM   1615 O  O    . VAL   A 1 212 ? -7.852  13.838  40.028  1.00 52.56  ? 212 VAL   A O    1 
ATOM   1616 C  CB   . VAL   A 1 212 ? -10.770 15.050  38.964  1.00 45.67  ? 212 VAL   A CB   1 
ATOM   1617 C  CG1  . VAL   A 1 212 ? -10.732 15.576  40.386  1.00 44.44  ? 212 VAL   A CG1  1 
ATOM   1618 C  CG2  . VAL   A 1 212 ? -11.521 16.008  38.058  1.00 44.09  ? 212 VAL   A CG2  1 
ATOM   1619 N  N    . ILE   A 1 213 ? -9.042  12.338  38.805  1.00 49.57  ? 213 ILE   A N    1 
ATOM   1620 C  CA   . ILE   A 1 213 ? -8.501  11.129  39.487  1.00 48.65  ? 213 ILE   A CA   1 
ATOM   1621 C  C    . ILE   A 1 213 ? -6.995  11.032  39.246  1.00 52.57  ? 213 ILE   A C    1 
ATOM   1622 O  O    . ILE   A 1 213 ? -6.290  10.577  40.151  1.00 47.09  ? 213 ILE   A O    1 
ATOM   1623 C  CB   . ILE   A 1 213 ? -9.276  9.878   39.039  1.00 49.44  ? 213 ILE   A CB   1 
ATOM   1624 C  CG1  . ILE   A 1 213 ? -10.772 9.986   39.331  1.00 45.44  ? 213 ILE   A CG1  1 
ATOM   1625 C  CG2  . ILE   A 1 213 ? -8.685  8.612   39.635  1.00 54.65  ? 213 ILE   A CG2  1 
ATOM   1626 C  CD1  . ILE   A 1 213 ? -11.610 8.978   38.587  1.00 39.11  ? 213 ILE   A CD1  1 
ATOM   1627 N  N    . ASN   A 1 214 ? -6.527  11.434  38.064  1.00 54.49  ? 214 ASN   A N    1 
ATOM   1628 C  CA   . ASN   A 1 214 ? -5.092  11.287  37.695  1.00 54.93  ? 214 ASN   A CA   1 
ATOM   1629 C  C    . ASN   A 1 214 ? -4.291  12.507  38.140  1.00 53.87  ? 214 ASN   A C    1 
ATOM   1630 O  O    . ASN   A 1 214 ? -3.065  12.460  37.996  1.00 54.77  ? 214 ASN   A O    1 
ATOM   1631 C  CB   . ASN   A 1 214 ? -4.909  10.875  36.231  1.00 52.40  ? 214 ASN   A CB   1 
ATOM   1632 C  CG   . ASN   A 1 214 ? -5.318  9.450   35.946  1.00 48.23  ? 214 ASN   A CG   1 
ATOM   1633 O  OD1  . ASN   A 1 214 ? -4.488  8.552   35.990  1.00 51.78  ? 214 ASN   A OD1  1 
ATOM   1634 N  ND2  . ASN   A 1 214 ? -6.586  9.235   35.648  1.00 44.84  ? 214 ASN   A ND2  1 
ATOM   1635 N  N    . GLY   A 1 215 ? -4.949  13.522  38.700  1.00 55.41  ? 215 GLY   A N    1 
ATOM   1636 C  CA   . GLY   A 1 215 ? -4.246  14.694  39.254  1.00 52.42  ? 215 GLY   A CA   1 
ATOM   1637 C  C    . GLY   A 1 215 ? -4.407  16.014  38.523  1.00 61.18  ? 215 GLY   A C    1 
ATOM   1638 O  O    . GLY   A 1 215 ? -4.110  17.038  39.148  1.00 65.53  ? 215 GLY   A O    1 
ATOM   1639 N  N    . ASP   A 1 216 ? -4.889  16.022  37.280  1.00 61.95  ? 216 ASP   A N    1 
ATOM   1640 C  CA   . ASP   A 1 216 ? -5.148  17.293  36.551  1.00 60.84  ? 216 ASP   A CA   1 
ATOM   1641 C  C    . ASP   A 1 216 ? -6.449  17.902  37.068  1.00 59.65  ? 216 ASP   A C    1 
ATOM   1642 O  O    . ASP   A 1 216 ? -7.478  17.243  36.962  1.00 58.56  ? 216 ASP   A O    1 
ATOM   1643 C  CB   . ASP   A 1 216 ? -5.061  17.099  35.036  1.00 57.82  ? 216 ASP   A CB   1 
ATOM   1644 C  CG   . ASP   A 1 216 ? -3.652  16.805  34.558  1.00 58.06  ? 216 ASP   A CG   1 
ATOM   1645 O  OD1  . ASP   A 1 216 ? -2.719  16.965  35.362  1.00 58.21  ? 216 ASP   A OD1  1 
ATOM   1646 O  OD2  . ASP   A 1 216 ? -3.502  16.421  33.391  1.00 57.80  ? 216 ASP   A OD2  1 
ATOM   1647 N  N    . ARG   A 1 217 ? -6.404  19.135  37.572  1.00 72.60  ? 217 ARG   A N    1 
ATOM   1648 C  CA   . ARG   A 1 217 ? -7.595  19.729  38.221  1.00 70.23  ? 217 ARG   A CA   1 
ATOM   1649 C  C    . ARG   A 1 217 ? -7.724  21.206  37.887  1.00 67.75  ? 217 ARG   A C    1 
ATOM   1650 O  O    . ARG   A 1 217 ? -8.554  21.856  38.500  1.00 73.10  ? 217 ARG   A O    1 
ATOM   1651 C  CB   . ARG   A 1 217 ? -7.438  19.645  39.739  1.00 76.50  ? 217 ARG   A CB   1 
ATOM   1652 C  CG   . ARG   A 1 217 ? -7.896  18.332  40.357  1.00 79.58  ? 217 ARG   A CG   1 
ATOM   1653 C  CD   . ARG   A 1 217 ? -7.717  18.242  41.862  1.00 79.69  ? 217 ARG   A CD   1 
ATOM   1654 N  NE   . ARG   A 1 217 ? -6.319  18.260  42.269  1.00 79.77  ? 217 ARG   A NE   1 
ATOM   1655 C  CZ   . ARG   A 1 217 ? -5.755  19.217  42.994  1.00 80.11  ? 217 ARG   A CZ   1 
ATOM   1656 N  NH1  . ARG   A 1 217 ? -6.473  20.243  43.415  1.00 77.11  ? 217 ARG   A NH1  1 
ATOM   1657 N  NH2  . ARG   A 1 217 ? -4.475  19.139  43.305  1.00 77.34  ? 217 ARG   A NH2  1 
ATOM   1658 N  N    . TRP   A 1 218 ? -6.918  21.720  36.978  1.00 65.17  ? 218 TRP   A N    1 
ATOM   1659 C  CA   . TRP   A 1 218 ? -6.979  23.157  36.714  1.00 63.27  ? 218 TRP   A CA   1 
ATOM   1660 C  C    . TRP   A 1 218 ? -8.335  23.563  36.146  1.00 62.58  ? 218 TRP   A C    1 
ATOM   1661 O  O    . TRP   A 1 218 ? -8.842  24.648  36.451  1.00 64.28  ? 218 TRP   A O    1 
ATOM   1662 C  CB   . TRP   A 1 218 ? -5.841  23.587  35.782  1.00 67.75  ? 218 TRP   A CB   1 
ATOM   1663 C  CG   . TRP   A 1 218 ? -5.907  23.051  34.362  1.00 66.94  ? 218 TRP   A CG   1 
ATOM   1664 C  CD1  . TRP   A 1 218 ? -5.210  21.999  33.861  1.00 62.96  ? 218 TRP   A CD1  1 
ATOM   1665 C  CD2  . TRP   A 1 218 ? -6.693  23.566  33.272  1.00 65.14  ? 218 TRP   A CD2  1 
ATOM   1666 N  NE1  . TRP   A 1 218 ? -5.512  21.818  32.538  1.00 62.85  ? 218 TRP   A NE1  1 
ATOM   1667 C  CE2  . TRP   A 1 218 ? -6.419  22.765  32.149  1.00 63.30  ? 218 TRP   A CE2  1 
ATOM   1668 C  CE3  . TRP   A 1 218 ? -7.606  24.621  33.141  1.00 65.52  ? 218 TRP   A CE3  1 
ATOM   1669 C  CZ2  . TRP   A 1 218 ? -7.019  22.981  30.907  1.00 62.74  ? 218 TRP   A CZ2  1 
ATOM   1670 C  CZ3  . TRP   A 1 218 ? -8.209  24.830  31.906  1.00 66.20  ? 218 TRP   A CZ3  1 
ATOM   1671 C  CH2  . TRP   A 1 218 ? -7.910  24.013  30.807  1.00 62.91  ? 218 TRP   A CH2  1 
ATOM   1672 N  N    . PHE   A 1 219 ? -8.948  22.700  35.332  1.00 63.01  ? 219 PHE   A N    1 
ATOM   1673 C  CA   . PHE   A 1 219 ? -10.248 22.988  34.732  1.00 58.34  ? 219 PHE   A CA   1 
ATOM   1674 C  C    . PHE   A 1 219 ? -11.372 22.992  35.755  1.00 55.40  ? 219 PHE   A C    1 
ATOM   1675 O  O    . PHE   A 1 219 ? -12.534 23.192  35.387  1.00 54.63  ? 219 PHE   A O    1 
ATOM   1676 C  CB   . PHE   A 1 219 ? -10.555 21.971  33.621  1.00 53.77  ? 219 PHE   A CB   1 
ATOM   1677 C  CG   . PHE   A 1 219 ? -10.542 20.540  34.091  1.00 53.67  ? 219 PHE   A CG   1 
ATOM   1678 C  CD1  . PHE   A 1 219 ? -9.342  19.870  34.294  1.00 53.39  ? 219 PHE   A CD1  1 
ATOM   1679 C  CD2  . PHE   A 1 219 ? -11.729 19.872  34.345  1.00 48.57  ? 219 PHE   A CD2  1 
ATOM   1680 C  CE1  . PHE   A 1 219 ? -9.326  18.564  34.743  1.00 49.77  ? 219 PHE   A CE1  1 
ATOM   1681 C  CE2  . PHE   A 1 219 ? -11.719 18.569  34.795  1.00 48.42  ? 219 PHE   A CE2  1 
ATOM   1682 C  CZ   . PHE   A 1 219 ? -10.510 17.914  34.995  1.00 49.30  ? 219 PHE   A CZ   1 
ATOM   1683 N  N    . LEU   A 1 220 ? -11.074 22.769  37.025  1.00 60.20  ? 220 LEU   A N    1 
ATOM   1684 C  CA   . LEU   A 1 220 ? -12.123 22.751  38.029  1.00 61.48  ? 220 LEU   A CA   1 
ATOM   1685 C  C    . LEU   A 1 220 ? -12.482 24.182  38.388  1.00 65.30  ? 220 LEU   A C    1 
ATOM   1686 O  O    . LEU   A 1 220 ? -11.611 25.005  38.690  1.00 64.69  ? 220 LEU   A O    1 
ATOM   1687 C  CB   . LEU   A 1 220 ? -11.690 21.944  39.252  1.00 58.57  ? 220 LEU   A CB   1 
ATOM   1688 C  CG   . LEU   A 1 220 ? -11.592 20.448  38.894  1.00 56.90  ? 220 LEU   A CG   1 
ATOM   1689 C  CD1  . LEU   A 1 220 ? -11.353 19.602  40.108  1.00 54.22  ? 220 LEU   A CD1  1 
ATOM   1690 C  CD2  . LEU   A 1 220 ? -12.843 19.947  38.151  1.00 46.94  ? 220 LEU   A CD2  1 
ATOM   1691 N  N    . ASN   A 1 221 ? -13.765 24.486  38.296  1.00 68.20  ? 221 ASN   A N    1 
ATOM   1692 C  CA   . ASN   A 1 221 ? -14.245 25.840  38.451  1.00 73.48  ? 221 ASN   A CA   1 
ATOM   1693 C  C    . ASN   A 1 221 ? -15.112 25.947  39.688  1.00 80.29  ? 221 ASN   A C    1 
ATOM   1694 O  O    . ASN   A 1 221 ? -15.719 24.980  40.166  1.00 68.02  ? 221 ASN   A O    1 
ATOM   1695 C  CB   . ASN   A 1 221 ? -15.056 26.309  37.237  1.00 68.67  ? 221 ASN   A CB   1 
ATOM   1696 C  CG   . ASN   A 1 221 ? -16.395 25.578  37.104  1.00 66.81  ? 221 ASN   A CG   1 
ATOM   1697 O  OD1  . ASN   A 1 221 ? -16.607 24.502  37.679  1.00 64.88  ? 221 ASN   A OD1  1 
ATOM   1698 N  ND2  . ASN   A 1 221 ? -17.307 26.174  36.350  1.00 65.74  ? 221 ASN   A ND2  1 
ATOM   1699 N  N    . ARG   A 1 222 ? -15.172 27.168  40.164  1.00 100.81 ? 222 ARG   A N    1 
ATOM   1700 C  CA   . ARG   A 1 222 ? -16.038 27.529  41.257  1.00 106.09 ? 222 ARG   A CA   1 
ATOM   1701 C  C    . ARG   A 1 222 ? -17.474 27.729  40.805  1.00 105.09 ? 222 ARG   A C    1 
ATOM   1702 O  O    . ARG   A 1 222 ? -18.317 28.105  41.628  1.00 105.78 ? 222 ARG   A O    1 
ATOM   1703 C  CB   . ARG   A 1 222 ? -15.463 28.781  41.891  1.00 107.86 ? 222 ARG   A CB   1 
ATOM   1704 C  CG   . ARG   A 1 222 ? -13.934 28.691  41.866  1.00 107.49 ? 222 ARG   A CG   1 
ATOM   1705 C  CD   . ARG   A 1 222 ? -13.403 27.687  42.913  1.00 114.00 ? 222 ARG   A CD   1 
ATOM   1706 N  NE   . ARG   A 1 222 ? -13.274 26.297  42.498  1.00 110.31 ? 222 ARG   A NE   1 
ATOM   1707 C  CZ   . ARG   A 1 222 ? -12.156 25.760  42.022  1.00 107.14 ? 222 ARG   A CZ   1 
ATOM   1708 N  NH1  . ARG   A 1 222 ? -11.060 26.500  41.888  1.00 102.88 ? 222 ARG   A NH1  1 
ATOM   1709 N  NH2  . ARG   A 1 222 ? -12.136 24.478  41.683  1.00 106.64 ? 222 ARG   A NH2  1 
ATOM   1710 N  N    . PHE   A 1 223 ? -17.804 27.460  39.533  1.00 83.22  ? 223 PHE   A N    1 
ATOM   1711 C  CA   . PHE   A 1 223 ? -19.193 27.724  39.198  1.00 76.27  ? 223 PHE   A CA   1 
ATOM   1712 C  C    . PHE   A 1 223 ? -19.968 26.415  39.242  1.00 72.97  ? 223 PHE   A C    1 
ATOM   1713 O  O    . PHE   A 1 223 ? -19.425 25.330  39.482  1.00 67.24  ? 223 PHE   A O    1 
ATOM   1714 C  CB   . PHE   A 1 223 ? -19.443 28.312  37.802  1.00 75.40  ? 223 PHE   A CB   1 
ATOM   1715 C  CG   . PHE   A 1 223 ? -18.591 29.509  37.426  1.00 78.82  ? 223 PHE   A CG   1 
ATOM   1716 C  CD1  . PHE   A 1 223 ? -17.714 30.106  38.303  1.00 81.09  ? 223 PHE   A CD1  1 
ATOM   1717 C  CD2  . PHE   A 1 223 ? -18.865 30.167  36.223  1.00 77.75  ? 223 PHE   A CD2  1 
ATOM   1718 C  CE1  . PHE   A 1 223 ? -16.956 31.199  37.915  1.00 84.31  ? 223 PHE   A CE1  1 
ATOM   1719 C  CE2  . PHE   A 1 223 ? -18.157 31.299  35.849  1.00 77.79  ? 223 PHE   A CE2  1 
ATOM   1720 C  CZ   . PHE   A 1 223 ? -17.209 31.814  36.705  1.00 80.24  ? 223 PHE   A CZ   1 
ATOM   1721 N  N    . THR   A 1 224 ? -21.261 26.536  38.984  1.00 70.19  ? 224 THR   A N    1 
ATOM   1722 C  CA   . THR   A 1 224 ? -22.117 25.406  38.673  1.00 67.89  ? 224 THR   A CA   1 
ATOM   1723 C  C    . THR   A 1 224 ? -23.018 25.826  37.512  1.00 68.65  ? 224 THR   A C    1 
ATOM   1724 O  O    . THR   A 1 224 ? -22.897 26.938  36.987  1.00 70.85  ? 224 THR   A O    1 
ATOM   1725 C  CB   . THR   A 1 224 ? -22.910 24.959  39.902  1.00 63.23  ? 224 THR   A CB   1 
ATOM   1726 O  OG1  . THR   A 1 224 ? -23.412 23.640  39.678  1.00 59.20  ? 224 THR   A OG1  1 
ATOM   1727 C  CG2  . THR   A 1 224 ? -24.067 25.909  40.162  1.00 62.23  ? 224 THR   A CG2  1 
ATOM   1728 N  N    . THR   A 1 225 ? -23.908 24.932  37.081  1.00 67.37  ? 225 THR   A N    1 
ATOM   1729 C  CA   . THR   A 1 225 ? -24.875 25.267  36.042  1.00 62.59  ? 225 THR   A CA   1 
ATOM   1730 C  C    . THR   A 1 225 ? -26.017 24.259  36.094  1.00 58.19  ? 225 THR   A C    1 
ATOM   1731 O  O    . THR   A 1 225 ? -26.069 23.378  36.959  1.00 54.24  ? 225 THR   A O    1 
ATOM   1732 C  CB   . THR   A 1 225 ? -24.223 25.306  34.645  1.00 64.69  ? 225 THR   A CB   1 
ATOM   1733 O  OG1  . THR   A 1 225 ? -25.053 26.043  33.728  1.00 65.94  ? 225 THR   A OG1  1 
ATOM   1734 C  CG2  . THR   A 1 225 ? -23.994 23.884  34.090  1.00 55.68  ? 225 THR   A CG2  1 
ATOM   1735 N  N    . THR   A 1 226 ? -26.920 24.397  35.136  1.00 63.43  ? 226 THR   A N    1 
ATOM   1736 C  CA   . THR   A 1 226 ? -28.107 23.584  34.955  1.00 62.30  ? 226 THR   A CA   1 
ATOM   1737 C  C    . THR   A 1 226 ? -27.956 22.728  33.693  1.00 60.30  ? 226 THR   A C    1 
ATOM   1738 O  O    . THR   A 1 226 ? -27.171 23.048  32.799  1.00 58.45  ? 226 THR   A O    1 
ATOM   1739 C  CB   . THR   A 1 226 ? -29.313 24.524  34.866  1.00 62.05  ? 226 THR   A CB   1 
ATOM   1740 O  OG1  . THR   A 1 226 ? -29.488 25.168  36.128  1.00 62.13  ? 226 THR   A OG1  1 
ATOM   1741 C  CG2  . THR   A 1 226 ? -30.579 23.811  34.504  1.00 64.65  ? 226 THR   A CG2  1 
ATOM   1742 N  N    . LEU   A 1 227 ? -28.681 21.605  33.639  1.00 53.73  ? 227 LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 227 ? -28.733 20.819  32.410  1.00 54.22  ? 227 LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 227 ? -29.174 21.677  31.238  1.00 57.04  ? 227 LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 227 ? -28.468 21.786  30.231  1.00 57.12  ? 227 LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 227 ? -29.672 19.620  32.570  1.00 52.15  ? 227 LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 227 ? -29.050 18.338  33.121  1.00 49.73  ? 227 LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 227 ? -30.105 17.335  33.548  1.00 55.20  ? 227 LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 227 ? -28.173 17.722  32.065  1.00 47.52  ? 227 LEU   A CD2  1 
ATOM   1750 N  N    . ASN   A 1 228 ? -30.348 22.307  31.365  1.00 59.11  ? 228 ASN   A N    1 
ATOM   1751 C  CA   . ASN   A 1 228 ? -30.873 23.153  30.296  1.00 61.72  ? 228 ASN   A CA   1 
ATOM   1752 C  C    . ASN   A 1 228 ? -29.902 24.256  29.908  1.00 65.43  ? 228 ASN   A C    1 
ATOM   1753 O  O    . ASN   A 1 228 ? -29.826 24.637  28.737  1.00 65.48  ? 228 ASN   A O    1 
ATOM   1754 C  CB   . ASN   A 1 228 ? -32.207 23.766  30.714  1.00 59.94  ? 228 ASN   A CB   1 
ATOM   1755 C  CG   . ASN   A 1 228 ? -33.296 22.733  30.856  1.00 55.66  ? 228 ASN   A CG   1 
ATOM   1756 O  OD1  . ASN   A 1 228 ? -33.107 21.561  30.516  1.00 51.55  ? 228 ASN   A OD1  1 
ATOM   1757 N  ND2  . ASN   A 1 228 ? -34.454 23.162  31.346  1.00 53.63  ? 228 ASN   A ND2  1 
ATOM   1758 N  N    . ASP   A 1 229 ? -29.154 24.780  30.871  1.00 79.57  ? 229 ASP   A N    1 
ATOM   1759 C  CA   . ASP   A 1 229 ? -28.234 25.864  30.569  1.00 81.42  ? 229 ASP   A CA   1 
ATOM   1760 C  C    . ASP   A 1 229 ? -26.937 25.342  29.970  1.00 78.45  ? 229 ASP   A C    1 
ATOM   1761 O  O    . ASP   A 1 229 ? -26.400 25.937  29.026  1.00 78.44  ? 229 ASP   A O    1 
ATOM   1762 C  CB   . ASP   A 1 229 ? -28.000 26.677  31.838  1.00 86.26  ? 229 ASP   A CB   1 
ATOM   1763 C  CG   . ASP   A 1 229 ? -29.271 27.337  32.317  1.00 89.45  ? 229 ASP   A CG   1 
ATOM   1764 O  OD1  . ASP   A 1 229 ? -29.952 27.965  31.475  1.00 94.05  ? 229 ASP   A OD1  1 
ATOM   1765 O  OD2  . ASP   A 1 229 ? -29.618 27.201  33.507  1.00 96.99  ? 229 ASP   A OD2  1 
ATOM   1766 N  N    . PHE   A 1 230 ? -26.430 24.224  30.490  1.00 64.34  ? 230 PHE   A N    1 
ATOM   1767 C  CA   . PHE   A 1 230 ? -25.298 23.581  29.841  1.00 56.98  ? 230 PHE   A CA   1 
ATOM   1768 C  C    . PHE   A 1 230 ? -25.662 23.169  28.424  1.00 60.07  ? 230 PHE   A C    1 
ATOM   1769 O  O    . PHE   A 1 230 ? -24.841 23.265  27.505  1.00 60.47  ? 230 PHE   A O    1 
ATOM   1770 C  CB   . PHE   A 1 230 ? -24.842 22.360  30.639  1.00 51.43  ? 230 PHE   A CB   1 
ATOM   1771 C  CG   . PHE   A 1 230 ? -23.935 21.460  29.870  1.00 50.20  ? 230 PHE   A CG   1 
ATOM   1772 C  CD1  . PHE   A 1 230 ? -22.568 21.680  29.872  1.00 50.40  ? 230 PHE   A CD1  1 
ATOM   1773 C  CD2  . PHE   A 1 230 ? -24.442 20.418  29.104  1.00 47.99  ? 230 PHE   A CD2  1 
ATOM   1774 C  CE1  . PHE   A 1 230 ? -21.714 20.870  29.136  1.00 47.17  ? 230 PHE   A CE1  1 
ATOM   1775 C  CE2  . PHE   A 1 230 ? -23.599 19.619  28.372  1.00 48.78  ? 230 PHE   A CE2  1 
ATOM   1776 C  CZ   . PHE   A 1 230 ? -22.228 19.852  28.390  1.00 45.52  ? 230 PHE   A CZ   1 
ATOM   1777 N  N    . ASN   A 1 231 ? -26.888 22.687  28.233  1.00 59.26  ? 231 ASN   A N    1 
ATOM   1778 C  CA   . ASN   A 1 231 ? -27.253 22.123  26.944  1.00 54.68  ? 231 ASN   A CA   1 
ATOM   1779 C  C    . ASN   A 1 231 ? -27.318 23.208  25.869  1.00 65.11  ? 231 ASN   A C    1 
ATOM   1780 O  O    . ASN   A 1 231 ? -26.887 22.982  24.726  1.00 68.00  ? 231 ASN   A O    1 
ATOM   1781 C  CB   . ASN   A 1 231 ? -28.570 21.355  27.079  1.00 52.99  ? 231 ASN   A CB   1 
ATOM   1782 C  CG   . ASN   A 1 231 ? -28.367 19.894  27.537  1.00 49.32  ? 231 ASN   A CG   1 
ATOM   1783 O  OD1  . ASN   A 1 231 ? -27.251 19.369  27.533  1.00 47.76  ? 231 ASN   A OD1  1 
ATOM   1784 N  ND2  . ASN   A 1 231 ? -29.457 19.239  27.915  1.00 46.87  ? 231 ASN   A ND2  1 
ATOM   1785 N  N    . LEU   A 1 232 ? -27.820 24.398  26.228  1.00 61.02  ? 232 LEU   A N    1 
ATOM   1786 C  CA   . LEU   A 1 232 ? -27.792 25.546  25.323  1.00 58.70  ? 232 LEU   A CA   1 
ATOM   1787 C  C    . LEU   A 1 232 ? -26.390 25.829  24.812  1.00 61.66  ? 232 LEU   A C    1 
ATOM   1788 O  O    . LEU   A 1 232 ? -26.208 26.200  23.646  1.00 59.78  ? 232 LEU   A O    1 
ATOM   1789 C  CB   . LEU   A 1 232 ? -28.336 26.777  26.039  1.00 61.30  ? 232 LEU   A CB   1 
ATOM   1790 C  CG   . LEU   A 1 232 ? -29.803 27.128  25.795  1.00 67.72  ? 232 LEU   A CG   1 
ATOM   1791 C  CD1  . LEU   A 1 232 ? -30.744 25.951  26.096  1.00 67.42  ? 232 LEU   A CD1  1 
ATOM   1792 C  CD2  . LEU   A 1 232 ? -30.159 28.335  26.653  1.00 65.86  ? 232 LEU   A CD2  1 
ATOM   1793 N  N    . VAL   A 1 233 ? -25.390 25.690  25.687  1.00 62.97  ? 233 VAL   A N    1 
ATOM   1794 C  CA   . VAL   A 1 233 ? -23.991 25.862  25.307  1.00 60.49  ? 233 VAL   A CA   1 
ATOM   1795 C  C    . VAL   A 1 233 ? -23.467 24.643  24.556  1.00 67.40  ? 233 VAL   A C    1 
ATOM   1796 O  O    . VAL   A 1 233 ? -22.647 24.782  23.640  1.00 71.24  ? 233 VAL   A O    1 
ATOM   1797 C  CB   . VAL   A 1 233 ? -23.141 26.156  26.559  1.00 66.63  ? 233 VAL   A CB   1 
ATOM   1798 C  CG1  . VAL   A 1 233 ? -21.678 26.399  26.178  1.00 64.03  ? 233 VAL   A CG1  1 
ATOM   1799 C  CG2  . VAL   A 1 233 ? -23.720 27.334  27.342  1.00 62.37  ? 233 VAL   A CG2  1 
ATOM   1800 N  N    . ALA   A 1 234 ? -23.907 23.436  24.931  1.00 72.88  ? 234 ALA   A N    1 
ATOM   1801 C  CA   . ALA   A 1 234 ? -23.508 22.239  24.195  1.00 74.41  ? 234 ALA   A CA   1 
ATOM   1802 C  C    . ALA   A 1 234 ? -23.891 22.366  22.724  1.00 75.76  ? 234 ALA   A C    1 
ATOM   1803 O  O    . ALA   A 1 234 ? -23.090 22.030  21.833  1.00 74.70  ? 234 ALA   A O    1 
ATOM   1804 C  CB   . ALA   A 1 234 ? -24.151 21.005  24.833  1.00 66.54  ? 234 ALA   A CB   1 
ATOM   1805 N  N    . MET   A 1 235 ? -25.093 22.932  22.476  1.00 67.63  ? 235 MET   A N    1 
ATOM   1806 C  CA   . MET   A 1 235 ? -25.645 23.032  21.123  1.00 67.09  ? 235 MET   A CA   1 
ATOM   1807 C  C    . MET   A 1 235 ? -24.758 23.887  20.220  1.00 68.14  ? 235 MET   A C    1 
ATOM   1808 O  O    . MET   A 1 235 ? -24.505 23.540  19.068  1.00 68.74  ? 235 MET   A O    1 
ATOM   1809 C  CB   . MET   A 1 235 ? -27.045 23.652  21.076  1.00 73.76  ? 235 MET   A CB   1 
ATOM   1810 C  CG   . MET   A 1 235 ? -27.405 23.769  19.600  1.00 86.62  ? 235 MET   A CG   1 
ATOM   1811 S  SD   . MET   A 1 235 ? -29.018 24.388  19.109  1.00 110.22 ? 235 MET   A SD   1 
ATOM   1812 C  CE   . MET   A 1 235 ? -28.722 24.699  17.353  1.00 93.72  ? 235 MET   A CE   1 
ATOM   1813 N  N    . LYS   A 1 236 ? -24.380 25.084  20.668  1.00 64.26  ? 236 LYS   A N    1 
ATOM   1814 C  CA   . LYS   A 1 236 ? -23.585 25.974  19.802  1.00 66.38  ? 236 LYS   A CA   1 
ATOM   1815 C  C    . LYS   A 1 236 ? -22.318 25.283  19.322  1.00 61.78  ? 236 LYS   A C    1 
ATOM   1816 O  O    . LYS   A 1 236 ? -21.997 25.307  18.125  1.00 66.71  ? 236 LYS   A O    1 
ATOM   1817 C  CB   . LYS   A 1 236 ? -23.237 27.286  20.527  1.00 66.02  ? 236 LYS   A CB   1 
ATOM   1818 C  CG   . LYS   A 1 236 ? -24.402 28.262  20.778  1.00 68.66  ? 236 LYS   A CG   1 
ATOM   1819 C  CD   . LYS   A 1 236 ? -24.984 29.004  19.554  1.00 74.95  ? 236 LYS   A CD   1 
ATOM   1820 C  CE   . LYS   A 1 236 ? -26.158 29.895  19.921  1.00 76.02  ? 236 LYS   A CE   1 
ATOM   1821 N  NZ   . LYS   A 1 236 ? -26.540 30.651  18.743  1.00 66.76  ? 236 LYS   A NZ   1 
ATOM   1822 N  N    . TYR   A 1 237 ? -21.660 24.555  20.213  1.00 59.53  ? 237 TYR   A N    1 
ATOM   1823 C  CA   . TYR   A 1 237 ? -20.440 23.847  19.888  1.00 57.85  ? 237 TYR   A CA   1 
ATOM   1824 C  C    . TYR   A 1 237 ? -20.706 22.427  19.384  1.00 52.67  ? 237 TYR   A C    1 
ATOM   1825 O  O    . TYR   A 1 237 ? -19.770 21.630  19.282  1.00 47.93  ? 237 TYR   A O    1 
ATOM   1826 C  CB   . TYR   A 1 237 ? -19.539 23.860  21.120  1.00 55.17  ? 237 TYR   A CB   1 
ATOM   1827 C  CG   . TYR   A 1 237 ? -19.074 25.243  21.555  1.00 57.16  ? 237 TYR   A CG   1 
ATOM   1828 C  CD1  . TYR   A 1 237 ? -17.900 25.795  21.047  1.00 53.77  ? 237 TYR   A CD1  1 
ATOM   1829 C  CD2  . TYR   A 1 237 ? -19.845 26.027  22.419  1.00 59.96  ? 237 TYR   A CD2  1 
ATOM   1830 C  CE1  . TYR   A 1 237 ? -17.476 27.052  21.432  1.00 52.17  ? 237 TYR   A CE1  1 
ATOM   1831 C  CE2  . TYR   A 1 237 ? -19.428 27.312  22.805  1.00 53.38  ? 237 TYR   A CE2  1 
ATOM   1832 C  CZ   . TYR   A 1 237 ? -18.242 27.809  22.306  1.00 53.88  ? 237 TYR   A CZ   1 
ATOM   1833 O  OH   . TYR   A 1 237 ? -17.832 29.068  22.683  1.00 55.80  ? 237 TYR   A OH   1 
ATOM   1834 N  N    . ASN   A 1 238 ? -21.954 22.123  19.020  1.00 48.69  ? 238 ASN   A N    1 
ATOM   1835 C  CA   . ASN   A 1 238 ? -22.321 20.849  18.410  1.00 49.08  ? 238 ASN   A CA   1 
ATOM   1836 C  C    . ASN   A 1 238 ? -21.867 19.685  19.274  1.00 49.97  ? 238 ASN   A C    1 
ATOM   1837 O  O    . ASN   A 1 238 ? -21.261 18.725  18.795  1.00 48.07  ? 238 ASN   A O    1 
ATOM   1838 C  CB   . ASN   A 1 238 ? -21.762 20.722  16.992  1.00 53.59  ? 238 ASN   A CB   1 
ATOM   1839 C  CG   . ASN   A 1 238 ? -22.491 21.618  16.003  1.00 53.25  ? 238 ASN   A CG   1 
ATOM   1840 O  OD1  . ASN   A 1 238 ? -23.579 21.287  15.532  1.00 50.97  ? 238 ASN   A OD1  1 
ATOM   1841 N  ND2  . ASN   A 1 238 ? -21.894 22.765  15.692  1.00 52.64  ? 238 ASN   A ND2  1 
ATOM   1842 N  N    . TYR   A 1 239 ? -22.135 19.804  20.572  1.00 51.81  ? 239 TYR   A N    1 
ATOM   1843 C  CA   . TYR   A 1 239 ? -22.083 18.678  21.481  1.00 42.85  ? 239 TYR   A CA   1 
ATOM   1844 C  C    . TYR   A 1 239 ? -23.442 18.013  21.557  1.00 41.38  ? 239 TYR   A C    1 
ATOM   1845 O  O    . TYR   A 1 239 ? -24.478 18.655  21.399  1.00 45.24  ? 239 TYR   A O    1 
ATOM   1846 C  CB   . TYR   A 1 239 ? -21.653 19.104  22.877  1.00 49.62  ? 239 TYR   A CB   1 
ATOM   1847 C  CG   . TYR   A 1 239 ? -20.173 19.176  23.087  1.00 42.01  ? 239 TYR   A CG   1 
ATOM   1848 C  CD1  . TYR   A 1 239 ? -19.328 19.651  22.122  1.00 46.93  ? 239 TYR   A CD1  1 
ATOM   1849 C  CD2  . TYR   A 1 239 ? -19.624 18.671  24.229  1.00 42.45  ? 239 TYR   A CD2  1 
ATOM   1850 C  CE1  . TYR   A 1 239 ? -17.958 19.681  22.334  1.00 51.73  ? 239 TYR   A CE1  1 
ATOM   1851 C  CE2  . TYR   A 1 239 ? -18.278 18.689  24.452  1.00 47.67  ? 239 TYR   A CE2  1 
ATOM   1852 C  CZ   . TYR   A 1 239 ? -17.436 19.187  23.507  1.00 46.34  ? 239 TYR   A CZ   1 
ATOM   1853 O  OH   . TYR   A 1 239 ? -16.074 19.182  23.765  1.00 42.16  ? 239 TYR   A OH   1 
ATOM   1854 N  N    . GLU   A 1 240 ? -23.425 16.715  21.804  1.00 44.09  ? 240 GLU   A N    1 
ATOM   1855 C  CA   . GLU   A 1 240 ? -24.661 15.992  22.074  1.00 51.51  ? 240 GLU   A CA   1 
ATOM   1856 C  C    . GLU   A 1 240 ? -25.319 16.504  23.364  1.00 48.06  ? 240 GLU   A C    1 
ATOM   1857 O  O    . GLU   A 1 240 ? -24.621 16.781  24.350  1.00 42.26  ? 240 GLU   A O    1 
ATOM   1858 C  CB   . GLU   A 1 240 ? -24.369 14.493  22.195  1.00 50.79  ? 240 GLU   A CB   1 
ATOM   1859 C  CG   . GLU   A 1 240 ? -25.605 13.683  22.482  1.00 46.29  ? 240 GLU   A CG   1 
ATOM   1860 C  CD   . GLU   A 1 240 ? -26.448 13.543  21.235  1.00 54.90  ? 240 GLU   A CD   1 
ATOM   1861 O  OE1  . GLU   A 1 240 ? -25.936 13.867  20.124  1.00 52.18  ? 240 GLU   A OE1  1 
ATOM   1862 O  OE2  . GLU   A 1 240 ? -27.622 13.132  21.369  1.00 53.16  ? 240 GLU   A OE2  1 
ATOM   1863 N  N    . PRO   A 1 241 ? -26.649 16.636  23.397  1.00 47.70  ? 241 PRO   A N    1 
ATOM   1864 C  CA   . PRO   A 1 241 ? -27.307 17.128  24.615  1.00 52.14  ? 241 PRO   A CA   1 
ATOM   1865 C  C    . PRO   A 1 241 ? -27.245 16.104  25.735  1.00 50.55  ? 241 PRO   A C    1 
ATOM   1866 O  O    . PRO   A 1 241 ? -27.310 14.893  25.510  1.00 53.62  ? 241 PRO   A O    1 
ATOM   1867 C  CB   . PRO   A 1 241 ? -28.758 17.363  24.166  1.00 50.95  ? 241 PRO   A CB   1 
ATOM   1868 C  CG   . PRO   A 1 241 ? -28.672 17.477  22.687  1.00 56.35  ? 241 PRO   A CG   1 
ATOM   1869 C  CD   . PRO   A 1 241 ? -27.617 16.492  22.302  1.00 52.17  ? 241 PRO   A CD   1 
ATOM   1870 N  N    . LEU   A 1 242 ? -27.146 16.601  26.962  1.00 48.17  ? 242 LEU   A N    1 
ATOM   1871 C  CA   . LEU   A 1 242 ? -26.926 15.731  28.110  1.00 49.68  ? 242 LEU   A CA   1 
ATOM   1872 C  C    . LEU   A 1 242 ? -28.256 15.298  28.714  1.00 45.48  ? 242 LEU   A C    1 
ATOM   1873 O  O    . LEU   A 1 242 ? -29.140 16.129  28.937  1.00 45.06  ? 242 LEU   A O    1 
ATOM   1874 C  CB   . LEU   A 1 242 ? -26.075 16.443  29.159  1.00 47.36  ? 242 LEU   A CB   1 
ATOM   1875 C  CG   . LEU   A 1 242 ? -25.355 15.496  30.103  1.00 48.19  ? 242 LEU   A CG   1 
ATOM   1876 C  CD1  . LEU   A 1 242 ? -24.317 14.769  29.292  1.00 42.72  ? 242 LEU   A CD1  1 
ATOM   1877 C  CD2  . LEU   A 1 242 ? -24.715 16.270  31.243  1.00 51.35  ? 242 LEU   A CD2  1 
ATOM   1878 N  N    . THR   A 1 243 ? -28.393 14.000  28.978  1.00 46.67  ? 243 THR   A N    1 
ATOM   1879 C  CA   . THR   A 1 243 ? -29.590 13.446  29.604  1.00 46.21  ? 243 THR   A CA   1 
ATOM   1880 C  C    . THR   A 1 243 ? -29.352 13.158  31.083  1.00 44.26  ? 243 THR   A C    1 
ATOM   1881 O  O    . THR   A 1 243 ? -28.226 13.200  31.586  1.00 45.69  ? 243 THR   A O    1 
ATOM   1882 C  CB   . THR   A 1 243 ? -30.030 12.159  28.903  1.00 46.91  ? 243 THR   A CB   1 
ATOM   1883 O  OG1  . THR   A 1 243 ? -29.066 11.126  29.162  1.00 46.54  ? 243 THR   A OG1  1 
ATOM   1884 C  CG2  . THR   A 1 243 ? -30.173 12.382  27.396  1.00 44.33  ? 243 THR   A CG2  1 
ATOM   1885 N  N    . GLN   A 1 244 ? -30.449 12.870  31.787  1.00 51.69  ? 244 GLN   A N    1 
ATOM   1886 C  CA   . GLN   A 1 244 ? -30.336 12.390  33.164  1.00 53.31  ? 244 GLN   A CA   1 
ATOM   1887 C  C    . GLN   A 1 244 ? -29.708 11.003  33.207  1.00 45.22  ? 244 GLN   A C    1 
ATOM   1888 O  O    . GLN   A 1 244 ? -29.030 10.658  34.179  1.00 45.20  ? 244 GLN   A O    1 
ATOM   1889 C  CB   . GLN   A 1 244 ? -31.707 12.369  33.851  1.00 47.27  ? 244 GLN   A CB   1 
ATOM   1890 C  CG   . GLN   A 1 244 ? -31.653 11.879  35.286  1.00 47.81  ? 244 GLN   A CG   1 
ATOM   1891 C  CD   . GLN   A 1 244 ? -30.749 12.737  36.147  1.00 48.71  ? 244 GLN   A CD   1 
ATOM   1892 O  OE1  . GLN   A 1 244 ? -30.829 13.963  36.105  1.00 57.06  ? 244 GLN   A OE1  1 
ATOM   1893 N  NE2  . GLN   A 1 244 ? -29.864 12.103  36.911  1.00 49.09  ? 244 GLN   A NE2  1 
ATOM   1894 N  N    . ASP   A 1 245 ? -29.913 10.204  32.164  1.00 41.54  ? 245 ASP   A N    1 
ATOM   1895 C  CA   . ASP   A 1 245 ? -29.247 8.912   32.108  1.00 44.81  ? 245 ASP   A CA   1 
ATOM   1896 C  C    . ASP   A 1 245 ? -27.734 9.084   32.031  1.00 46.10  ? 245 ASP   A C    1 
ATOM   1897 O  O    . ASP   A 1 245 ? -26.982 8.331   32.661  1.00 39.71  ? 245 ASP   A O    1 
ATOM   1898 C  CB   . ASP   A 1 245 ? -29.785 8.132   30.920  1.00 47.55  ? 245 ASP   A CB   1 
ATOM   1899 C  CG   . ASP   A 1 245 ? -31.249 7.882   31.043  1.00 51.80  ? 245 ASP   A CG   1 
ATOM   1900 O  OD1  . ASP   A 1 245 ? -31.665 7.251   32.033  1.00 64.19  ? 245 ASP   A OD1  1 
ATOM   1901 O  OD2  . ASP   A 1 245 ? -32.001 8.390   30.198  1.00 60.13  ? 245 ASP   A OD2  1 
ATOM   1902 N  N    . HIS   A 1 246 ? -27.271 10.076  31.261  1.00 45.06  ? 246 HIS   A N    1 
ATOM   1903 C  CA   . HIS   A 1 246 ? -25.860 10.441  31.281  1.00 43.24  ? 246 HIS   A CA   1 
ATOM   1904 C  C    . HIS   A 1 246 ? -25.421 10.854  32.681  1.00 43.34  ? 246 HIS   A C    1 
ATOM   1905 O  O    . HIS   A 1 246 ? -24.316 10.515  33.131  1.00 40.96  ? 246 HIS   A O    1 
ATOM   1906 C  CB   . HIS   A 1 246 ? -25.598 11.585  30.300  1.00 44.96  ? 246 HIS   A CB   1 
ATOM   1907 C  CG   . HIS   A 1 246 ? -25.980 11.283  28.885  1.00 44.68  ? 246 HIS   A CG   1 
ATOM   1908 N  ND1  . HIS   A 1 246 ? -26.298 12.273  27.980  1.00 44.48  ? 246 HIS   A ND1  1 
ATOM   1909 C  CD2  . HIS   A 1 246 ? -26.089 10.111  28.213  1.00 45.03  ? 246 HIS   A CD2  1 
ATOM   1910 C  CE1  . HIS   A 1 246 ? -26.583 11.724  26.810  1.00 44.53  ? 246 HIS   A CE1  1 
ATOM   1911 N  NE2  . HIS   A 1 246 ? -26.464 10.413  26.925  1.00 42.69  ? 246 HIS   A NE2  1 
ATOM   1912 N  N    . VAL   A 1 247 ? -26.261 11.609  33.381  1.00 43.14  ? 247 VAL   A N    1 
ATOM   1913 C  CA   . VAL   A 1 247 ? -25.880 12.026  34.721  1.00 43.34  ? 247 VAL   A CA   1 
ATOM   1914 C  C    . VAL   A 1 247 ? -25.850 10.824  35.653  1.00 47.81  ? 247 VAL   A C    1 
ATOM   1915 O  O    . VAL   A 1 247 ? -24.930 10.682  36.470  1.00 49.60  ? 247 VAL   A O    1 
ATOM   1916 C  CB   . VAL   A 1 247 ? -26.822 13.128  35.224  1.00 43.14  ? 247 VAL   A CB   1 
ATOM   1917 C  CG1  . VAL   A 1 247 ? -26.565 13.407  36.695  1.00 43.07  ? 247 VAL   A CG1  1 
ATOM   1918 C  CG2  . VAL   A 1 247 ? -26.630 14.365  34.393  1.00 41.87  ? 247 VAL   A CG2  1 
ATOM   1919 N  N    . ASP   A 1 248 ? -26.843 9.933   35.529  1.00 48.31  ? 248 ASP   A N    1 
ATOM   1920 C  CA   . ASP   A 1 248 ? -26.851 8.665   36.257  1.00 45.01  ? 248 ASP   A CA   1 
ATOM   1921 C  C    . ASP   A 1 248 ? -25.515 7.942   36.122  1.00 48.29  ? 248 ASP   A C    1 
ATOM   1922 O  O    . ASP   A 1 248 ? -24.788 7.766   37.105  1.00 49.63  ? 248 ASP   A O    1 
ATOM   1923 C  CB   . ASP   A 1 248 ? -27.972 7.759   35.732  1.00 47.03  ? 248 ASP   A CB   1 
ATOM   1924 C  CG   . ASP   A 1 248 ? -29.344 8.227   36.129  1.00 48.45  ? 248 ASP   A CG   1 
ATOM   1925 O  OD1  . ASP   A 1 248 ? -29.468 8.855   37.203  1.00 53.01  ? 248 ASP   A OD1  1 
ATOM   1926 O  OD2  . ASP   A 1 248 ? -30.299 7.949   35.364  1.00 46.12  ? 248 ASP   A OD2  1 
ATOM   1927 N  N    . ILE   A 1 249 ? -25.168 7.541   34.888  1.00 47.25  ? 249 ILE   A N    1 
ATOM   1928 C  CA   . ILE   A 1 249 ? -24.052 6.629   34.642  1.00 41.85  ? 249 ILE   A CA   1 
ATOM   1929 C  C    . ILE   A 1 249 ? -22.713 7.279   34.979  1.00 41.08  ? 249 ILE   A C    1 
ATOM   1930 O  O    . ILE   A 1 249 ? -21.702 6.588   35.154  1.00 39.47  ? 249 ILE   A O    1 
ATOM   1931 C  CB   . ILE   A 1 249 ? -24.133 6.123   33.185  1.00 45.41  ? 249 ILE   A CB   1 
ATOM   1932 C  CG1  . ILE   A 1 249 ? -23.495 4.743   33.030  1.00 47.07  ? 249 ILE   A CG1  1 
ATOM   1933 C  CG2  . ILE   A 1 249 ? -23.502 7.122   32.195  1.00 47.96  ? 249 ILE   A CG2  1 
ATOM   1934 C  CD1  . ILE   A 1 249 ? -23.865 4.039   31.712  1.00 42.64  ? 249 ILE   A CD1  1 
ATOM   1935 N  N    . LEU   A 1 250 ? -22.685 8.593   35.107  1.00 44.78  ? 250 LEU   A N    1 
ATOM   1936 C  CA   . LEU   A 1 250 ? -21.522 9.276   35.649  1.00 47.07  ? 250 LEU   A CA   1 
ATOM   1937 C  C    . LEU   A 1 250 ? -21.507 9.249   37.182  1.00 43.38  ? 250 LEU   A C    1 
ATOM   1938 O  O    . LEU   A 1 250 ? -20.533 9.706   37.796  1.00 41.49  ? 250 LEU   A O    1 
ATOM   1939 C  CB   . LEU   A 1 250 ? -21.488 10.711  35.091  1.00 45.62  ? 250 LEU   A CB   1 
ATOM   1940 C  CG   . LEU   A 1 250 ? -20.967 10.761  33.637  1.00 39.46  ? 250 LEU   A CG   1 
ATOM   1941 C  CD1  . LEU   A 1 250 ? -21.299 12.059  32.900  1.00 36.14  ? 250 LEU   A CD1  1 
ATOM   1942 C  CD2  . LEU   A 1 250 ? -19.457 10.515  33.591  1.00 37.21  ? 250 LEU   A CD2  1 
ATOM   1943 N  N    . GLY   A 1 251 ? -22.539 8.670   37.791  1.00 40.63  ? 251 GLY   A N    1 
ATOM   1944 C  CA   . GLY   A 1 251 ? -22.672 8.549   39.223  1.00 44.99  ? 251 GLY   A CA   1 
ATOM   1945 C  C    . GLY   A 1 251 ? -21.422 8.148   39.974  1.00 44.40  ? 251 GLY   A C    1 
ATOM   1946 O  O    . GLY   A 1 251 ? -20.881 8.923   40.767  1.00 48.13  ? 251 GLY   A O    1 
ATOM   1947 N  N    . PRO   A 1 252 ? -20.951 6.922   39.769  1.00 44.62  ? 252 PRO   A N    1 
ATOM   1948 C  CA   . PRO   A 1 252 ? -19.753 6.477   40.504  1.00 44.60  ? 252 PRO   A CA   1 
ATOM   1949 C  C    . PRO   A 1 252 ? -18.561 7.411   40.368  1.00 43.68  ? 252 PRO   A C    1 
ATOM   1950 O  O    . PRO   A 1 252 ? -17.778 7.541   41.320  1.00 43.06  ? 252 PRO   A O    1 
ATOM   1951 C  CB   . PRO   A 1 252 ? -19.477 5.097   39.899  1.00 44.89  ? 252 PRO   A CB   1 
ATOM   1952 C  CG   . PRO   A 1 252 ? -20.829 4.615   39.477  1.00 50.50  ? 252 PRO   A CG   1 
ATOM   1953 C  CD   . PRO   A 1 252 ? -21.530 5.841   38.948  1.00 48.70  ? 252 PRO   A CD   1 
ATOM   1954 N  N    . LEU   A 1 253 ? -18.417 8.090   39.226  1.00 45.55  ? 253 LEU   A N    1 
ATOM   1955 C  CA   . LEU   A 1 253 ? -17.296 9.006   39.040  1.00 43.56  ? 253 LEU   A CA   1 
ATOM   1956 C  C    . LEU   A 1 253 ? -17.473 10.271  39.881  1.00 43.28  ? 253 LEU   A C    1 
ATOM   1957 O  O    . LEU   A 1 253 ? -16.538 10.717  40.564  1.00 40.61  ? 253 LEU   A O    1 
ATOM   1958 C  CB   . LEU   A 1 253 ? -17.148 9.345   37.558  1.00 41.73  ? 253 LEU   A CB   1 
ATOM   1959 C  CG   . LEU   A 1 253 ? -16.762 8.236   36.561  1.00 44.58  ? 253 LEU   A CG   1 
ATOM   1960 C  CD1  . LEU   A 1 253 ? -16.720 8.781   35.115  1.00 36.39  ? 253 LEU   A CD1  1 
ATOM   1961 C  CD2  . LEU   A 1 253 ? -15.437 7.578   36.931  1.00 42.67  ? 253 LEU   A CD2  1 
ATOM   1962 N  N    . SER   A 1 254 ? -18.675 10.860  39.847  1.00 43.63  ? 254 SER   A N    1 
ATOM   1963 C  CA   . SER   A 1 254 ? -19.001 11.940  40.780  1.00 45.61  ? 254 SER   A CA   1 
ATOM   1964 C  C    . SER   A 1 254 ? -18.784 11.512  42.221  1.00 43.40  ? 254 SER   A C    1 
ATOM   1965 O  O    . SER   A 1 254 ? -18.403 12.335  43.059  1.00 46.97  ? 254 SER   A O    1 
ATOM   1966 C  CB   . SER   A 1 254 ? -20.449 12.393  40.594  1.00 44.74  ? 254 SER   A CB   1 
ATOM   1967 O  OG   . SER   A 1 254 ? -21.340 11.441  41.151  1.00 43.92  ? 254 SER   A OG   1 
ATOM   1968 N  N    . ALA   A 1 255 ? -19.022 10.233  42.519  1.00 45.90  ? 255 ALA   A N    1 
ATOM   1969 C  CA   . ALA   A 1 255 ? -18.814 9.705   43.862  1.00 45.40  ? 255 ALA   A CA   1 
ATOM   1970 C  C    . ALA   A 1 255 ? -17.333 9.680   44.222  1.00 45.93  ? 255 ALA   A C    1 
ATOM   1971 O  O    . ALA   A 1 255 ? -16.911 10.293  45.209  1.00 45.70  ? 255 ALA   A O    1 
ATOM   1972 C  CB   . ALA   A 1 255 ? -19.419 8.304   43.951  1.00 45.51  ? 255 ALA   A CB   1 
ATOM   1973 N  N    . GLN   A 1 256 ? -16.537 8.953   43.431  1.00 47.52  ? 256 GLN   A N    1 
ATOM   1974 C  CA   . GLN   A 1 256 ? -15.087 8.891   43.608  1.00 49.60  ? 256 GLN   A CA   1 
ATOM   1975 C  C    . GLN   A 1 256 ? -14.446 10.271  43.773  1.00 51.84  ? 256 GLN   A C    1 
ATOM   1976 O  O    . GLN   A 1 256 ? -13.595 10.472  44.647  1.00 55.90  ? 256 GLN   A O    1 
ATOM   1977 C  CB   . GLN   A 1 256 ? -14.471 8.169   42.412  1.00 47.08  ? 256 GLN   A CB   1 
ATOM   1978 C  CG   . GLN   A 1 256 ? -13.033 7.770   42.600  1.00 50.70  ? 256 GLN   A CG   1 
ATOM   1979 C  CD   . GLN   A 1 256 ? -12.555 6.849   41.501  1.00 61.54  ? 256 GLN   A CD   1 
ATOM   1980 O  OE1  . GLN   A 1 256 ? -13.342 6.419   40.642  1.00 64.45  ? 256 GLN   A OE1  1 
ATOM   1981 N  NE2  . GLN   A 1 256 ? -11.259 6.529   41.520  1.00 62.29  ? 256 GLN   A NE2  1 
ATOM   1982 N  N    . THR   A 1 257 ? -14.811 11.228  42.926  1.00 47.02  ? 257 THR   A N    1 
ATOM   1983 C  CA   . THR   A 1 257 ? -14.112 12.508  42.929  1.00 50.24  ? 257 THR   A CA   1 
ATOM   1984 C  C    . THR   A 1 257 ? -14.678 13.528  43.919  1.00 48.92  ? 257 THR   A C    1 
ATOM   1985 O  O    . THR   A 1 257 ? -13.975 14.481  44.277  1.00 47.39  ? 257 THR   A O    1 
ATOM   1986 C  CB   . THR   A 1 257 ? -14.124 13.103  41.521  1.00 45.85  ? 257 THR   A CB   1 
ATOM   1987 O  OG1  . THR   A 1 257 ? -15.460 13.052  41.006  1.00 48.53  ? 257 THR   A OG1  1 
ATOM   1988 C  CG2  . THR   A 1 257 ? -13.194 12.323  40.615  1.00 45.58  ? 257 THR   A CG2  1 
ATOM   1989 N  N    . GLY   A 1 258 ? -15.917 13.358  44.363  1.00 46.24  ? 258 GLY   A N    1 
ATOM   1990 C  CA   . GLY   A 1 258 ? -16.562 14.374  45.159  1.00 44.68  ? 258 GLY   A CA   1 
ATOM   1991 C  C    . GLY   A 1 258 ? -16.956 15.600  44.380  1.00 44.53  ? 258 GLY   A C    1 
ATOM   1992 O  O    . GLY   A 1 258 ? -16.902 16.714  44.920  1.00 47.69  ? 258 GLY   A O    1 
ATOM   1993 N  N    . ILE   A 1 259 ? -17.350 15.437  43.120  1.00 44.71  ? 259 ILE   A N    1 
ATOM   1994 C  CA   . ILE   A 1 259 ? -17.693 16.558  42.254  1.00 43.95  ? 259 ILE   A CA   1 
ATOM   1995 C  C    . ILE   A 1 259 ? -19.021 16.250  41.574  1.00 46.37  ? 259 ILE   A C    1 
ATOM   1996 O  O    . ILE   A 1 259 ? -19.113 15.293  40.796  1.00 47.00  ? 259 ILE   A O    1 
ATOM   1997 C  CB   . ILE   A 1 259 ? -16.616 16.804  41.199  1.00 42.15  ? 259 ILE   A CB   1 
ATOM   1998 C  CG1  . ILE   A 1 259 ? -15.273 17.049  41.873  1.00 43.48  ? 259 ILE   A CG1  1 
ATOM   1999 C  CG2  . ILE   A 1 259 ? -17.027 18.005  40.350  1.00 49.67  ? 259 ILE   A CG2  1 
ATOM   2000 C  CD1  . ILE   A 1 259 ? -14.123 17.004  40.930  1.00 43.82  ? 259 ILE   A CD1  1 
ATOM   2001 N  N    . ALA   A 1 260 ? -20.041 17.060  41.850  1.00 46.94  ? 260 ALA   A N    1 
ATOM   2002 C  CA   . ALA   A 1 260 ? -21.356 16.851  41.249  1.00 49.09  ? 260 ALA   A CA   1 
ATOM   2003 C  C    . ALA   A 1 260 ? -21.291 16.942  39.727  1.00 51.26  ? 260 ALA   A C    1 
ATOM   2004 O  O    . ALA   A 1 260 ? -20.469 17.673  39.163  1.00 54.00  ? 260 ALA   A O    1 
ATOM   2005 C  CB   . ALA   A 1 260 ? -22.345 17.885  41.783  1.00 54.97  ? 260 ALA   A CB   1 
ATOM   2006 N  N    . VAL   A 1 261 ? -22.181 16.202  39.052  1.00 53.17  ? 261 VAL   A N    1 
ATOM   2007 C  CA   . VAL   A 1 261 ? -22.124 16.130  37.584  1.00 46.81  ? 261 VAL   A CA   1 
ATOM   2008 C  C    . VAL   A 1 261 ? -22.262 17.525  36.984  1.00 47.61  ? 261 VAL   A C    1 
ATOM   2009 O  O    . VAL   A 1 261 ? -21.431 17.961  36.174  1.00 46.24  ? 261 VAL   A O    1 
ATOM   2010 C  CB   . VAL   A 1 261 ? -23.192 15.156  37.038  1.00 41.22  ? 261 VAL   A CB   1 
ATOM   2011 C  CG1  . VAL   A 1 261 ? -23.310 15.257  35.518  1.00 45.58  ? 261 VAL   A CG1  1 
ATOM   2012 C  CG2  . VAL   A 1 261 ? -22.850 13.722  37.404  1.00 37.25  ? 261 VAL   A CG2  1 
ATOM   2013 N  N    . LEU   A 1 262 ? -23.290 18.262  37.415  1.00 49.33  ? 262 LEU   A N    1 
ATOM   2014 C  CA   . LEU   A 1 262 ? -23.537 19.605  36.904  1.00 50.04  ? 262 LEU   A CA   1 
ATOM   2015 C  C    . LEU   A 1 262 ? -22.362 20.543  37.165  1.00 51.51  ? 262 LEU   A C    1 
ATOM   2016 O  O    . LEU   A 1 262 ? -22.136 21.486  36.395  1.00 49.49  ? 262 LEU   A O    1 
ATOM   2017 C  CB   . LEU   A 1 262 ? -24.812 20.169  37.533  1.00 46.15  ? 262 LEU   A CB   1 
ATOM   2018 C  CG   . LEU   A 1 262 ? -26.072 19.388  37.171  1.00 45.67  ? 262 LEU   A CG   1 
ATOM   2019 C  CD1  . LEU   A 1 262 ? -27.331 20.084  37.670  1.00 41.67  ? 262 LEU   A CD1  1 
ATOM   2020 C  CD2  . LEU   A 1 262 ? -26.119 19.142  35.669  1.00 46.41  ? 262 LEU   A CD2  1 
ATOM   2021 N  N    . ASP   A 1 263 ? -21.619 20.331  38.253  1.00 51.67  ? 263 ASP   A N    1 
ATOM   2022 C  CA   . ASP   A 1 263 ? -20.438 21.162  38.465  1.00 53.09  ? 263 ASP   A CA   1 
ATOM   2023 C  C    . ASP   A 1 263 ? -19.406 20.902  37.389  1.00 48.16  ? 263 ASP   A C    1 
ATOM   2024 O  O    . ASP   A 1 263 ? -18.815 21.842  36.847  1.00 43.93  ? 263 ASP   A O    1 
ATOM   2025 C  CB   . ASP   A 1 263 ? -19.844 20.921  39.852  1.00 55.17  ? 263 ASP   A CB   1 
ATOM   2026 C  CG   . ASP   A 1 263 ? -20.736 21.433  40.960  1.00 52.52  ? 263 ASP   A CG   1 
ATOM   2027 O  OD1  . ASP   A 1 263 ? -21.875 21.837  40.640  1.00 49.60  ? 263 ASP   A OD1  1 
ATOM   2028 O  OD2  . ASP   A 1 263 ? -20.286 21.444  42.134  1.00 54.61  ? 263 ASP   A OD2  1 
ATOM   2029 N  N    . MET   A 1 264 ? -19.198 19.626  37.054  1.00 50.32  ? 264 MET   A N    1 
ATOM   2030 C  CA   . MET   A 1 264 ? -18.349 19.280  35.921  1.00 45.77  ? 264 MET   A CA   1 
ATOM   2031 C  C    . MET   A 1 264 ? -18.923 19.824  34.615  1.00 43.32  ? 264 MET   A C    1 
ATOM   2032 O  O    . MET   A 1 264 ? -18.176 20.251  33.733  1.00 42.64  ? 264 MET   A O    1 
ATOM   2033 C  CB   . MET   A 1 264 ? -18.171 17.763  35.865  1.00 41.95  ? 264 MET   A CB   1 
ATOM   2034 C  CG   . MET   A 1 264 ? -17.044 17.364  34.985  1.00 39.80  ? 264 MET   A CG   1 
ATOM   2035 S  SD   . MET   A 1 264 ? -15.488 17.885  35.711  1.00 44.88  ? 264 MET   A SD   1 
ATOM   2036 C  CE   . MET   A 1 264 ? -15.086 16.469  36.753  1.00 39.45  ? 264 MET   A CE   1 
ATOM   2037 N  N    . CYS   A 1 265 ? -20.251 19.835  34.483  1.00 44.08  ? 265 CYS   A N    1 
ATOM   2038 C  CA   . CYS   A 1 265 ? -20.878 20.459  33.324  1.00 42.46  ? 265 CYS   A CA   1 
ATOM   2039 C  C    . CYS   A 1 265 ? -20.622 21.962  33.268  1.00 46.92  ? 265 CYS   A C    1 
ATOM   2040 O  O    . CYS   A 1 265 ? -20.712 22.569  32.195  1.00 49.27  ? 265 CYS   A O    1 
ATOM   2041 C  CB   . CYS   A 1 265 ? -22.376 20.191  33.340  1.00 40.43  ? 265 CYS   A CB   1 
ATOM   2042 S  SG   . CYS   A 1 265 ? -22.761 18.470  33.157  1.00 52.39  ? 265 CYS   A SG   1 
ATOM   2043 N  N    . ALA   A 1 266 ? -20.342 22.591  34.405  1.00 49.19  ? 266 ALA   A N    1 
ATOM   2044 C  CA   . ALA   A 1 266 ? -20.032 24.015  34.382  1.00 51.26  ? 266 ALA   A CA   1 
ATOM   2045 C  C    . ALA   A 1 266 ? -18.568 24.257  34.060  1.00 51.49  ? 266 ALA   A C    1 
ATOM   2046 O  O    . ALA   A 1 266 ? -18.231 25.291  33.475  1.00 51.08  ? 266 ALA   A O    1 
ATOM   2047 C  CB   . ALA   A 1 266 ? -20.384 24.670  35.719  1.00 52.62  ? 266 ALA   A CB   1 
ATOM   2048 N  N    . SER   A 1 267 ? -17.687 23.337  34.462  1.00 52.20  ? 267 SER   A N    1 
ATOM   2049 C  CA   . SER   A 1 267 ? -16.302 23.410  34.019  1.00 50.40  ? 267 SER   A CA   1 
ATOM   2050 C  C    . SER   A 1 267 ? -16.224 23.200  32.517  1.00 51.19  ? 267 SER   A C    1 
ATOM   2051 O  O    . SER   A 1 267 ? -15.516 23.926  31.806  1.00 51.68  ? 267 SER   A O    1 
ATOM   2052 C  CB   . SER   A 1 267 ? -15.457 22.370  34.757  1.00 48.42  ? 267 SER   A CB   1 
ATOM   2053 O  OG   . SER   A 1 267 ? -15.010 22.856  36.005  1.00 49.04  ? 267 SER   A OG   1 
ATOM   2054 N  N    . LEU   A 1 268 ? -16.975 22.224  32.016  1.00 47.36  ? 268 LEU   A N    1 
ATOM   2055 C  CA   . LEU   A 1 268 ? -16.998 21.974  30.586  1.00 48.64  ? 268 LEU   A CA   1 
ATOM   2056 C  C    . LEU   A 1 268 ? -17.505 23.195  29.837  1.00 47.96  ? 268 LEU   A C    1 
ATOM   2057 O  O    . LEU   A 1 268 ? -16.894 23.608  28.847  1.00 50.22  ? 268 LEU   A O    1 
ATOM   2058 C  CB   . LEU   A 1 268 ? -17.840 20.731  30.291  1.00 44.31  ? 268 LEU   A CB   1 
ATOM   2059 C  CG   . LEU   A 1 268 ? -18.030 20.298  28.839  1.00 43.57  ? 268 LEU   A CG   1 
ATOM   2060 C  CD1  . LEU   A 1 268 ? -16.741 20.341  28.034  1.00 47.54  ? 268 LEU   A CD1  1 
ATOM   2061 C  CD2  . LEU   A 1 268 ? -18.602 18.916  28.821  1.00 45.44  ? 268 LEU   A CD2  1 
ATOM   2062 N  N    . LYS   A 1 269 ? -18.587 23.814  30.320  1.00 47.21  ? 269 LYS   A N    1 
ATOM   2063 C  CA   . LYS   A 1 269 ? -19.106 25.028  29.683  1.00 53.78  ? 269 LYS   A CA   1 
ATOM   2064 C  C    . LYS   A 1 269 ? -18.037 26.111  29.551  1.00 56.13  ? 269 LYS   A C    1 
ATOM   2065 O  O    . LYS   A 1 269 ? -17.798 26.632  28.457  1.00 58.81  ? 269 LYS   A O    1 
ATOM   2066 C  CB   . LYS   A 1 269 ? -20.306 25.568  30.456  1.00 54.70  ? 269 LYS   A CB   1 
ATOM   2067 C  CG   . LYS   A 1 269 ? -20.796 26.898  29.944  1.00 53.68  ? 269 LYS   A CG   1 
ATOM   2068 C  CD   . LYS   A 1 269 ? -21.494 27.698  31.026  1.00 58.32  ? 269 LYS   A CD   1 
ATOM   2069 C  CE   . LYS   A 1 269 ? -22.987 27.365  31.097  1.00 62.24  ? 269 LYS   A CE   1 
ATOM   2070 N  NZ   . LYS   A 1 269 ? -23.743 28.222  32.089  1.00 65.91  ? 269 LYS   A NZ   1 
ATOM   2071 N  N    . GLU   A 1 270 ? -17.384 26.472  30.652  1.00 64.75  ? 270 GLU   A N    1 
ATOM   2072 C  CA   . GLU   A 1 270 ? -16.296 27.444  30.556  1.00 70.62  ? 270 GLU   A CA   1 
ATOM   2073 C  C    . GLU   A 1 270 ? -15.220 26.961  29.591  1.00 69.38  ? 270 GLU   A C    1 
ATOM   2074 O  O    . GLU   A 1 270 ? -14.639 27.750  28.833  1.00 68.67  ? 270 GLU   A O    1 
ATOM   2075 C  CB   . GLU   A 1 270 ? -15.704 27.715  31.943  1.00 69.37  ? 270 GLU   A CB   1 
ATOM   2076 C  CG   . GLU   A 1 270 ? -16.598 28.567  32.814  1.00 67.26  ? 270 GLU   A CG   1 
ATOM   2077 C  CD   . GLU   A 1 270 ? -16.651 29.994  32.328  1.00 71.62  ? 270 GLU   A CD   1 
ATOM   2078 O  OE1  . GLU   A 1 270 ? -15.608 30.673  32.420  1.00 73.47  ? 270 GLU   A OE1  1 
ATOM   2079 O  OE2  . GLU   A 1 270 ? -17.716 30.433  31.834  1.00 83.02  ? 270 GLU   A OE2  1 
ATOM   2080 N  N    . LEU   A 1 271 ? -14.966 25.657  29.586  1.00 58.35  ? 271 LEU   A N    1 
ATOM   2081 C  CA   . LEU   A 1 271 ? -13.914 25.102  28.758  1.00 51.24  ? 271 LEU   A CA   1 
ATOM   2082 C  C    . LEU   A 1 271 ? -14.279 25.164  27.280  1.00 52.73  ? 271 LEU   A C    1 
ATOM   2083 O  O    . LEU   A 1 271 ? -13.386 25.177  26.428  1.00 55.96  ? 271 LEU   A O    1 
ATOM   2084 C  CB   . LEU   A 1 271 ? -13.663 23.678  29.230  1.00 49.12  ? 271 LEU   A CB   1 
ATOM   2085 C  CG   . LEU   A 1 271 ? -12.258 23.108  29.219  1.00 52.05  ? 271 LEU   A CG   1 
ATOM   2086 C  CD1  . LEU   A 1 271 ? -11.351 23.965  30.084  1.00 46.33  ? 271 LEU   A CD1  1 
ATOM   2087 C  CD2  . LEU   A 1 271 ? -12.338 21.684  29.755  1.00 44.56  ? 271 LEU   A CD2  1 
ATOM   2088 N  N    . LEU   A 1 272 ? -15.569 25.226  26.957  1.00 51.66  ? 272 LEU   A N    1 
ATOM   2089 C  CA   . LEU   A 1 272 ? -15.994 25.428  25.582  1.00 50.06  ? 272 LEU   A CA   1 
ATOM   2090 C  C    . LEU   A 1 272 ? -15.961 26.882  25.163  1.00 52.95  ? 272 LEU   A C    1 
ATOM   2091 O  O    . LEU   A 1 272 ? -15.729 27.171  23.982  1.00 58.74  ? 272 LEU   A O    1 
ATOM   2092 C  CB   . LEU   A 1 272 ? -17.406 24.885  25.357  1.00 47.86  ? 272 LEU   A CB   1 
ATOM   2093 C  CG   . LEU   A 1 272 ? -17.496 23.356  25.397  1.00 48.61  ? 272 LEU   A CG   1 
ATOM   2094 C  CD1  . LEU   A 1 272 ? -18.808 22.859  24.834  1.00 50.79  ? 272 LEU   A CD1  1 
ATOM   2095 C  CD2  . LEU   A 1 272 ? -16.336 22.723  24.667  1.00 49.82  ? 272 LEU   A CD2  1 
ATOM   2096 N  N    . GLN   A 1 273 ? -16.186 27.802  26.094  1.00 52.25  ? 273 GLN   A N    1 
ATOM   2097 C  CA   . GLN   A 1 273 ? -16.319 29.208  25.739  1.00 53.19  ? 273 GLN   A CA   1 
ATOM   2098 C  C    . GLN   A 1 273 ? -14.982 29.925  25.721  1.00 52.19  ? 273 GLN   A C    1 
ATOM   2099 O  O    . GLN   A 1 273 ? -14.735 30.745  24.834  1.00 59.35  ? 273 GLN   A O    1 
ATOM   2100 C  CB   . GLN   A 1 273 ? -17.255 29.918  26.718  1.00 57.13  ? 273 GLN   A CB   1 
ATOM   2101 C  CG   . GLN   A 1 273 ? -18.664 29.380  26.735  1.00 54.03  ? 273 GLN   A CG   1 
ATOM   2102 C  CD   . GLN   A 1 273 ? -19.419 29.824  27.962  1.00 58.86  ? 273 GLN   A CD   1 
ATOM   2103 O  OE1  . GLN   A 1 273 ? -18.838 30.400  28.887  1.00 66.27  ? 273 GLN   A OE1  1 
ATOM   2104 N  NE2  . GLN   A 1 273 ? -20.722 29.555  27.987  1.00 58.93  ? 273 GLN   A NE2  1 
ATOM   2105 N  N    . ASN   A 1 274 ? -14.128 29.650  26.700  1.00 55.10  ? 274 ASN   A N    1 
ATOM   2106 C  CA   . ASN   A 1 274 ? -12.840 30.310  26.829  1.00 52.66  ? 274 ASN   A CA   1 
ATOM   2107 C  C    . ASN   A 1 274 ? -11.703 29.415  26.397  1.00 51.69  ? 274 ASN   A C    1 
ATOM   2108 O  O    . ASN   A 1 274 ? -10.546 29.832  26.468  1.00 51.67  ? 274 ASN   A O    1 
ATOM   2109 C  CB   . ASN   A 1 274 ? -12.601 30.758  28.279  1.00 53.08  ? 274 ASN   A CB   1 
ATOM   2110 C  CG   . ASN   A 1 274 ? -13.802 31.412  28.881  1.00 55.11  ? 274 ASN   A CG   1 
ATOM   2111 O  OD1  . ASN   A 1 274 ? -14.350 30.923  29.870  1.00 62.31  ? 274 ASN   A OD1  1 
ATOM   2112 N  ND2  . ASN   A 1 274 ? -14.246 32.512  28.280  1.00 57.99  ? 274 ASN   A ND2  1 
ATOM   2113 N  N    . GLY   A 1 275 ? -12.006 28.185  25.991  1.00 56.78  ? 275 GLY   A N    1 
ATOM   2114 C  CA   . GLY   A 1 275 ? -10.996 27.265  25.512  1.00 54.75  ? 275 GLY   A CA   1 
ATOM   2115 C  C    . GLY   A 1 275 ? -9.981  26.913  26.581  1.00 59.02  ? 275 GLY   A C    1 
ATOM   2116 O  O    . GLY   A 1 275 ? -9.987  27.417  27.699  1.00 61.63  ? 275 GLY   A O    1 
ATOM   2117 N  N    . MET   A 1 276 ? -9.070  26.035  26.200  1.00 64.50  ? 276 MET   A N    1 
ATOM   2118 C  CA   . MET   A 1 276 ? -8.156  25.446  27.164  1.00 68.28  ? 276 MET   A CA   1 
ATOM   2119 C  C    . MET   A 1 276 ? -6.955  26.320  27.502  1.00 72.09  ? 276 MET   A C    1 
ATOM   2120 O  O    . MET   A 1 276 ? -6.114  25.883  28.297  1.00 74.45  ? 276 MET   A O    1 
ATOM   2121 C  CB   . MET   A 1 276 ? -7.659  24.103  26.649  1.00 66.57  ? 276 MET   A CB   1 
ATOM   2122 C  CG   . MET   A 1 276 ? -8.430  22.925  27.175  1.00 57.51  ? 276 MET   A CG   1 
ATOM   2123 S  SD   . MET   A 1 276 ? -7.519  21.482  26.637  1.00 52.83  ? 276 MET   A SD   1 
ATOM   2124 C  CE   . MET   A 1 276 ? -8.808  20.255  26.604  1.00 43.19  ? 276 MET   A CE   1 
ATOM   2125 N  N    . ASN   A 1 277 ? -6.809  27.478  26.880  1.00 74.51  ? 277 ASN   A N    1 
ATOM   2126 C  CA   . ASN   A 1 277 ? -5.718  28.416  27.267  1.00 84.52  ? 277 ASN   A CA   1 
ATOM   2127 C  C    . ASN   A 1 277 ? -4.308  27.806  27.190  1.00 78.80  ? 277 ASN   A C    1 
ATOM   2128 O  O    . ASN   A 1 277 ? -3.455  28.259  27.959  1.00 79.27  ? 277 ASN   A O    1 
ATOM   2129 C  CB   . ASN   A 1 277 ? -6.022  29.126  28.585  1.00 83.50  ? 277 ASN   A CB   1 
ATOM   2130 C  CG   . ASN   A 1 277 ? -7.155  30.120  28.473  1.00 85.84  ? 277 ASN   A CG   1 
ATOM   2131 O  OD1  . ASN   A 1 277 ? -6.981  31.206  27.925  1.00 90.41  ? 277 ASN   A OD1  1 
ATOM   2132 N  ND2  . ASN   A 1 277 ? -8.315  29.759  28.996  1.00 87.86  ? 277 ASN   A ND2  1 
ATOM   2133 N  N    . GLY   A 1 278 ? -4.059  26.838  26.308  1.00 75.09  ? 278 GLY   A N    1 
ATOM   2134 C  CA   . GLY   A 1 278 ? -2.698  26.300  26.093  1.00 75.14  ? 278 GLY   A CA   1 
ATOM   2135 C  C    . GLY   A 1 278 ? -2.312  25.235  27.090  1.00 70.21  ? 278 GLY   A C    1 
ATOM   2136 O  O    . GLY   A 1 278 ? -1.221  24.684  26.976  1.00 73.33  ? 278 GLY   A O    1 
ATOM   2137 N  N    . ARG   A 1 279 ? -3.189  24.962  28.032  1.00 63.31  ? 279 ARG   A N    1 
ATOM   2138 C  CA   . ARG   A 1 279 ? -2.941  23.933  29.054  1.00 63.22  ? 279 ARG   A CA   1 
ATOM   2139 C  C    . ARG   A 1 279 ? -3.375  22.578  28.510  1.00 63.47  ? 279 ARG   A C    1 
ATOM   2140 O  O    . ARG   A 1 279 ? -4.050  22.541  27.479  1.00 61.01  ? 279 ARG   A O    1 
ATOM   2141 C  CB   . ARG   A 1 279 ? -3.657  24.335  30.345  1.00 72.22  ? 279 ARG   A CB   1 
ATOM   2142 C  CG   . ARG   A 1 279 ? -3.073  25.581  30.991  1.00 72.40  ? 279 ARG   A CG   1 
ATOM   2143 C  CD   . ARG   A 1 279 ? -3.926  26.190  32.082  1.00 78.55  ? 279 ARG   A CD   1 
ATOM   2144 N  NE   . ARG   A 1 279 ? -5.138  26.799  31.565  1.00 82.53  ? 279 ARG   A NE   1 
ATOM   2145 C  CZ   . ARG   A 1 279 ? -5.932  27.587  32.275  1.00 81.22  ? 279 ARG   A CZ   1 
ATOM   2146 N  NH1  . ARG   A 1 279 ? -5.628  27.869  33.529  1.00 82.28  ? 279 ARG   A NH1  1 
ATOM   2147 N  NH2  . ARG   A 1 279 ? -7.023  28.095  31.731  1.00 75.94  ? 279 ARG   A NH2  1 
ATOM   2148 N  N    . THR   A 1 280 ? -2.985  21.512  29.195  1.00 59.86  ? 280 THR   A N    1 
ATOM   2149 C  CA   . THR   A 1 280 ? -3.290  20.154  28.710  1.00 52.85  ? 280 THR   A CA   1 
ATOM   2150 C  C    . THR   A 1 280 ? -4.014  19.366  29.784  1.00 48.62  ? 280 THR   A C    1 
ATOM   2151 O  O    . THR   A 1 280 ? -3.565  19.379  30.923  1.00 49.60  ? 280 THR   A O    1 
ATOM   2152 C  CB   . THR   A 1 280 ? -1.998  19.426  28.347  1.00 50.80  ? 280 THR   A CB   1 
ATOM   2153 O  OG1  . THR   A 1 280 ? -1.125  19.474  29.474  1.00 52.40  ? 280 THR   A OG1  1 
ATOM   2154 C  CG2  . THR   A 1 280 ? -1.308  20.028  27.143  1.00 50.73  ? 280 THR   A CG2  1 
ATOM   2155 N  N    . ILE   A 1 281 ? -5.114  18.734  29.417  1.00 48.56  ? 281 ILE   A N    1 
ATOM   2156 C  CA   . ILE   A 1 281 ? -5.793  17.832  30.379  1.00 50.40  ? 281 ILE   A CA   1 
ATOM   2157 C  C    . ILE   A 1 281 ? -5.435  16.405  29.968  1.00 49.26  ? 281 ILE   A C    1 
ATOM   2158 O  O    . ILE   A 1 281 ? -5.751  16.028  28.843  1.00 41.18  ? 281 ILE   A O    1 
ATOM   2159 C  CB   . ILE   A 1 281 ? -7.311  18.069  30.425  1.00 47.57  ? 281 ILE   A CB   1 
ATOM   2160 C  CG1  . ILE   A 1 281 ? -7.658  19.555  30.500  1.00 50.24  ? 281 ILE   A CG1  1 
ATOM   2161 C  CG2  . ILE   A 1 281 ? -7.938  17.282  31.554  1.00 41.41  ? 281 ILE   A CG2  1 
ATOM   2162 C  CD1  . ILE   A 1 281 ? -9.137  19.833  30.512  1.00 49.49  ? 281 ILE   A CD1  1 
ATOM   2163 N  N    . LEU   A 1 282 ? -4.745  15.678  30.839  1.00 56.43  ? 282 LEU   A N    1 
ATOM   2164 C  CA   . LEU   A 1 282 ? -4.370  14.279  30.590  1.00 50.81  ? 282 LEU   A CA   1 
ATOM   2165 C  C    . LEU   A 1 282 ? -3.607  14.114  29.270  1.00 48.75  ? 282 LEU   A C    1 
ATOM   2166 O  O    . LEU   A 1 282 ? -3.797  13.142  28.530  1.00 50.33  ? 282 LEU   A O    1 
ATOM   2167 C  CB   . LEU   A 1 282 ? -5.597  13.366  30.628  1.00 47.50  ? 282 LEU   A CB   1 
ATOM   2168 C  CG   . LEU   A 1 282 ? -6.127  12.954  31.992  1.00 52.22  ? 282 LEU   A CG   1 
ATOM   2169 C  CD1  . LEU   A 1 282 ? -7.246  11.928  31.858  1.00 51.92  ? 282 LEU   A CD1  1 
ATOM   2170 C  CD2  . LEU   A 1 282 ? -4.986  12.396  32.832  1.00 56.14  ? 282 LEU   A CD2  1 
ATOM   2171 N  N    . GLY   A 1 283 ? -2.726  15.070  28.977  1.00 42.42  ? 283 GLY   A N    1 
ATOM   2172 C  CA   . GLY   A 1 283 ? -1.839  14.931  27.851  1.00 43.08  ? 283 GLY   A CA   1 
ATOM   2173 C  C    . GLY   A 1 283 ? -2.417  15.319  26.509  1.00 44.90  ? 283 GLY   A C    1 
ATOM   2174 O  O    . GLY   A 1 283 ? -1.705  15.195  25.504  1.00 47.03  ? 283 GLY   A O    1 
ATOM   2175 N  N    . SER   A 1 284 ? -3.678  15.762  26.457  1.00 40.72  ? 284 SER   A N    1 
ATOM   2176 C  CA   . SER   A 1 284 ? -4.338  16.243  25.247  1.00 40.10  ? 284 SER   A CA   1 
ATOM   2177 C  C    . SER   A 1 284 ? -4.586  17.740  25.372  1.00 46.33  ? 284 SER   A C    1 
ATOM   2178 O  O    . SER   A 1 284 ? -4.885  18.232  26.469  1.00 46.92  ? 284 SER   A O    1 
ATOM   2179 C  CB   . SER   A 1 284 ? -5.686  15.558  25.025  1.00 36.91  ? 284 SER   A CB   1 
ATOM   2180 O  OG   . SER   A 1 284 ? -5.573  14.150  24.999  1.00 42.18  ? 284 SER   A OG   1 
ATOM   2181 N  N    . ALA   A 1 285 ? -4.485  18.464  24.249  1.00 45.67  ? 285 ALA   A N    1 
ATOM   2182 C  CA   . ALA   A 1 285 ? -4.889  19.865  24.207  1.00 41.42  ? 285 ALA   A CA   1 
ATOM   2183 C  C    . ALA   A 1 285 ? -6.280  20.055  23.633  1.00 40.08  ? 285 ALA   A C    1 
ATOM   2184 O  O    . ALA   A 1 285 ? -6.718  21.189  23.462  1.00 44.85  ? 285 ALA   A O    1 
ATOM   2185 C  CB   . ALA   A 1 285 ? -3.895  20.694  23.409  1.00 42.49  ? 285 ALA   A CB   1 
ATOM   2186 N  N    . LEU   A 1 286 ? -6.977  18.977  23.324  1.00 40.01  ? 286 LEU   A N    1 
ATOM   2187 C  CA   . LEU   A 1 286 ? -8.379  19.015  22.949  1.00 40.38  ? 286 LEU   A CA   1 
ATOM   2188 C  C    . LEU   A 1 286 ? -9.180  18.186  23.956  1.00 45.76  ? 286 LEU   A C    1 
ATOM   2189 O  O    . LEU   A 1 286 ? -8.622  17.446  24.780  1.00 41.61  ? 286 LEU   A O    1 
ATOM   2190 C  CB   . LEU   A 1 286 ? -8.574  18.480  21.526  1.00 41.27  ? 286 LEU   A CB   1 
ATOM   2191 C  CG   . LEU   A 1 286 ? -7.778  19.175  20.404  1.00 49.53  ? 286 LEU   A CG   1 
ATOM   2192 C  CD1  . LEU   A 1 286 ? -7.734  18.308  19.139  1.00 44.36  ? 286 LEU   A CD1  1 
ATOM   2193 C  CD2  . LEU   A 1 286 ? -8.260  20.616  20.064  1.00 43.40  ? 286 LEU   A CD2  1 
ATOM   2194 N  N    . LEU   A 1 287 ? -10.502 18.331  23.887  1.00 41.16  ? 287 LEU   A N    1 
ATOM   2195 C  CA   . LEU   A 1 287 ? -11.432 17.604  24.739  1.00 35.22  ? 287 LEU   A CA   1 
ATOM   2196 C  C    . LEU   A 1 287 ? -11.718 16.233  24.133  1.00 40.07  ? 287 LEU   A C    1 
ATOM   2197 O  O    . LEU   A 1 287 ? -12.217 16.144  23.009  1.00 41.04  ? 287 LEU   A O    1 
ATOM   2198 C  CB   . LEU   A 1 287 ? -12.709 18.420  24.899  1.00 33.74  ? 287 LEU   A CB   1 
ATOM   2199 C  CG   . LEU   A 1 287 ? -12.379 19.783  25.506  1.00 39.10  ? 287 LEU   A CG   1 
ATOM   2200 C  CD1  . LEU   A 1 287 ? -13.480 20.790  25.275  1.00 40.24  ? 287 LEU   A CD1  1 
ATOM   2201 C  CD2  . LEU   A 1 287 ? -12.153 19.605  26.989  1.00 42.66  ? 287 LEU   A CD2  1 
ATOM   2202 N  N    . GLU   A 1 288 ? -11.415 15.168  24.880  1.00 37.67  ? 288 GLU   A N    1 
ATOM   2203 C  CA   . GLU   A 1 288 ? -11.488 13.807  24.367  1.00 35.15  ? 288 GLU   A CA   1 
ATOM   2204 C  C    . GLU   A 1 288 ? -12.851 13.182  24.650  1.00 37.83  ? 288 GLU   A C    1 
ATOM   2205 O  O    . GLU   A 1 288 ? -13.335 13.206  25.780  1.00 43.08  ? 288 GLU   A O    1 
ATOM   2206 C  CB   . GLU   A 1 288 ? -10.374 12.955  24.978  1.00 32.34  ? 288 GLU   A CB   1 
ATOM   2207 C  CG   . GLU   A 1 288 ? -8.984  13.456  24.653  1.00 36.18  ? 288 GLU   A CG   1 
ATOM   2208 C  CD   . GLU   A 1 288 ? -8.283  12.649  23.551  1.00 44.78  ? 288 GLU   A CD   1 
ATOM   2209 O  OE1  . GLU   A 1 288 ? -8.978  12.023  22.701  1.00 40.89  ? 288 GLU   A OE1  1 
ATOM   2210 O  OE2  . GLU   A 1 288 ? -7.024  12.646  23.545  1.00 44.67  ? 288 GLU   A OE2  1 
ATOM   2211 N  N    . ASP   A 1 289 ? -13.452 12.581  23.624  1.00 38.73  ? 289 ASP   A N    1 
ATOM   2212 C  CA   . ASP   A 1 289 ? -14.821 12.102  23.722  1.00 38.04  ? 289 ASP   A CA   1 
ATOM   2213 C  C    . ASP   A 1 289 ? -14.970 10.616  23.421  1.00 44.09  ? 289 ASP   A C    1 
ATOM   2214 O  O    . ASP   A 1 289 ? -16.102 10.148  23.232  1.00 44.20  ? 289 ASP   A O    1 
ATOM   2215 C  CB   . ASP   A 1 289 ? -15.738 12.910  22.797  1.00 41.35  ? 289 ASP   A CB   1 
ATOM   2216 C  CG   . ASP   A 1 289 ? -15.411 12.732  21.311  1.00 47.14  ? 289 ASP   A CG   1 
ATOM   2217 O  OD1  . ASP   A 1 289 ? -14.259 12.368  20.943  1.00 46.97  ? 289 ASP   A OD1  1 
ATOM   2218 O  OD2  . ASP   A 1 289 ? -16.331 12.966  20.501  1.00 45.71  ? 289 ASP   A OD2  1 
ATOM   2219 N  N    . GLU   A 1 290 ? -13.871 9.856   23.403  1.00 45.44  ? 290 GLU   A N    1 
ATOM   2220 C  CA   . GLU   A 1 290 ? -13.893 8.439   23.045  1.00 42.78  ? 290 GLU   A CA   1 
ATOM   2221 C  C    . GLU   A 1 290 ? -13.531 7.522   24.211  1.00 41.40  ? 290 GLU   A C    1 
ATOM   2222 O  O    . GLU   A 1 290 ? -13.030 6.419   23.983  1.00 42.68  ? 290 GLU   A O    1 
ATOM   2223 C  CB   . GLU   A 1 290 ? -12.964 8.175   21.859  1.00 45.07  ? 290 GLU   A CB   1 
ATOM   2224 C  CG   . GLU   A 1 290 ? -13.614 8.516   20.532  1.00 47.94  ? 290 GLU   A CG   1 
ATOM   2225 C  CD   . GLU   A 1 290 ? -12.958 7.869   19.322  1.00 49.37  ? 290 GLU   A CD   1 
ATOM   2226 O  OE1  . GLU   A 1 290 ? -13.404 8.205   18.212  1.00 50.98  ? 290 GLU   A OE1  1 
ATOM   2227 O  OE2  . GLU   A 1 290 ? -12.017 7.042   19.467  1.00 48.22  ? 290 GLU   A OE2  1 
ATOM   2228 N  N    . PHE   A 1 291 ? -13.769 7.954   25.453  1.00 43.77  ? 291 PHE   A N    1 
ATOM   2229 C  CA   . PHE   A 1 291 ? -13.804 7.063   26.612  1.00 44.30  ? 291 PHE   A CA   1 
ATOM   2230 C  C    . PHE   A 1 291 ? -15.199 7.109   27.232  1.00 40.19  ? 291 PHE   A C    1 
ATOM   2231 O  O    . PHE   A 1 291 ? -15.660 8.179   27.638  1.00 39.45  ? 291 PHE   A O    1 
ATOM   2232 C  CB   . PHE   A 1 291 ? -12.773 7.468   27.663  1.00 41.51  ? 291 PHE   A CB   1 
ATOM   2233 C  CG   . PHE   A 1 291 ? -11.362 7.548   27.164  1.00 37.55  ? 291 PHE   A CG   1 
ATOM   2234 C  CD1  . PHE   A 1 291 ? -10.544 6.439   27.179  1.00 37.48  ? 291 PHE   A CD1  1 
ATOM   2235 C  CD2  . PHE   A 1 291 ? -10.828 8.755   26.772  1.00 40.54  ? 291 PHE   A CD2  1 
ATOM   2236 C  CE1  . PHE   A 1 291 ? -9.232  6.528   26.769  1.00 42.99  ? 291 PHE   A CE1  1 
ATOM   2237 C  CE2  . PHE   A 1 291 ? -9.513  8.851   26.350  1.00 42.53  ? 291 PHE   A CE2  1 
ATOM   2238 C  CZ   . PHE   A 1 291 ? -8.714  7.744   26.354  1.00 42.61  ? 291 PHE   A CZ   1 
ATOM   2239 N  N    . THR   A 1 292 ? -15.872 5.966   27.322  1.00 38.16  ? 292 THR   A N    1 
ATOM   2240 C  CA   . THR   A 1 292 ? -17.167 5.982   27.992  1.00 43.28  ? 292 THR   A CA   1 
ATOM   2241 C  C    . THR   A 1 292 ? -17.004 6.138   29.515  1.00 43.29  ? 292 THR   A C    1 
ATOM   2242 O  O    . THR   A 1 292 ? -15.911 5.959   30.064  1.00 43.82  ? 292 THR   A O    1 
ATOM   2243 C  CB   . THR   A 1 292 ? -17.969 4.712   27.698  1.00 40.28  ? 292 THR   A CB   1 
ATOM   2244 O  OG1  . THR   A 1 292 ? -17.189 3.558   27.998  1.00 42.01  ? 292 THR   A OG1  1 
ATOM   2245 C  CG2  . THR   A 1 292 ? -18.430 4.677   26.270  1.00 40.04  ? 292 THR   A CG2  1 
ATOM   2246 N  N    . PRO   A 1 293 ? -18.081 6.501   30.216  1.00 40.21  ? 293 PRO   A N    1 
ATOM   2247 C  CA   . PRO   A 1 293 ? -18.055 6.379   31.680  1.00 39.76  ? 293 PRO   A CA   1 
ATOM   2248 C  C    . PRO   A 1 293 ? -17.531 5.029   32.108  1.00 44.10  ? 293 PRO   A C    1 
ATOM   2249 O  O    . PRO   A 1 293 ? -16.633 4.933   32.954  1.00 41.00  ? 293 PRO   A O    1 
ATOM   2250 C  CB   . PRO   A 1 293 ? -19.528 6.555   32.053  1.00 40.31  ? 293 PRO   A CB   1 
ATOM   2251 C  CG   . PRO   A 1 293 ? -20.051 7.434   30.992  1.00 42.91  ? 293 PRO   A CG   1 
ATOM   2252 C  CD   . PRO   A 1 293 ? -19.391 6.973   29.736  1.00 39.20  ? 293 PRO   A CD   1 
ATOM   2253 N  N    . PHE   A 1 294 ? -18.065 3.968   31.498  1.00 48.15  ? 294 PHE   A N    1 
ATOM   2254 C  CA   . PHE   A 1 294 ? -17.630 2.617   31.816  1.00 47.50  ? 294 PHE   A CA   1 
ATOM   2255 C  C    . PHE   A 1 294 ? -16.131 2.444   31.572  1.00 46.67  ? 294 PHE   A C    1 
ATOM   2256 O  O    . PHE   A 1 294 ? -15.423 1.868   32.409  1.00 42.57  ? 294 PHE   A O    1 
ATOM   2257 C  CB   . PHE   A 1 294 ? -18.453 1.613   31.007  1.00 49.52  ? 294 PHE   A CB   1 
ATOM   2258 C  CG   . PHE   A 1 294 ? -18.312 0.192   31.485  1.00 61.33  ? 294 PHE   A CG   1 
ATOM   2259 C  CD1  . PHE   A 1 294 ? -18.423 -0.112  32.842  1.00 64.41  ? 294 PHE   A CD1  1 
ATOM   2260 C  CD2  . PHE   A 1 294 ? -18.050 -0.841  30.591  1.00 60.43  ? 294 PHE   A CD2  1 
ATOM   2261 C  CE1  . PHE   A 1 294 ? -18.292 -1.419  33.301  1.00 63.72  ? 294 PHE   A CE1  1 
ATOM   2262 C  CE2  . PHE   A 1 294 ? -17.922 -2.149  31.042  1.00 65.99  ? 294 PHE   A CE2  1 
ATOM   2263 C  CZ   . PHE   A 1 294 ? -18.036 -2.434  32.402  1.00 69.27  ? 294 PHE   A CZ   1 
ATOM   2264 N  N    . ASP   A 1 295 ? -15.623 2.956   30.443  1.00 43.21  ? 295 ASP   A N    1 
ATOM   2265 C  CA   . ASP   A 1 295 ? -14.189 2.864   30.181  1.00 43.32  ? 295 ASP   A CA   1 
ATOM   2266 C  C    . ASP   A 1 295 ? -13.387 3.491   31.311  1.00 43.55  ? 295 ASP   A C    1 
ATOM   2267 O  O    . ASP   A 1 295 ? -12.389 2.926   31.774  1.00 42.60  ? 295 ASP   A O    1 
ATOM   2268 C  CB   . ASP   A 1 295 ? -13.829 3.549   28.867  1.00 42.52  ? 295 ASP   A CB   1 
ATOM   2269 C  CG   . ASP   A 1 295 ? -14.561 2.982   27.698  1.00 46.90  ? 295 ASP   A CG   1 
ATOM   2270 O  OD1  . ASP   A 1 295 ? -15.279 1.962   27.855  1.00 49.61  ? 295 ASP   A OD1  1 
ATOM   2271 O  OD2  . ASP   A 1 295 ? -14.432 3.582   26.614  1.00 49.49  ? 295 ASP   A OD2  1 
ATOM   2272 N  N    . VAL   A 1 296 ? -13.800 4.678   31.751  1.00 45.05  ? 296 VAL   A N    1 
ATOM   2273 C  CA   . VAL   A 1 296 ? -13.061 5.373   32.800  1.00 44.83  ? 296 VAL   A CA   1 
ATOM   2274 C  C    . VAL   A 1 296 ? -13.087 4.587   34.107  1.00 37.48  ? 296 VAL   A C    1 
ATOM   2275 O  O    . VAL   A 1 296 ? -12.056 4.442   34.767  1.00 39.83  ? 296 VAL   A O    1 
ATOM   2276 C  CB   . VAL   A 1 296 ? -13.608 6.798   32.971  1.00 44.39  ? 296 VAL   A CB   1 
ATOM   2277 C  CG1  . VAL   A 1 296 ? -12.842 7.512   34.058  1.00 42.95  ? 296 VAL   A CG1  1 
ATOM   2278 C  CG2  . VAL   A 1 296 ? -13.483 7.540   31.653  1.00 40.32  ? 296 VAL   A CG2  1 
ATOM   2279 N  N    . VAL   A 1 297 ? -14.252 4.067   34.504  1.00 39.95  ? 297 VAL   A N    1 
ATOM   2280 C  CA   . VAL   A 1 297 ? -14.344 3.337   35.777  1.00 46.46  ? 297 VAL   A CA   1 
ATOM   2281 C  C    . VAL   A 1 297 ? -13.378 2.162   35.786  1.00 44.71  ? 297 VAL   A C    1 
ATOM   2282 O  O    . VAL   A 1 297 ? -12.667 1.926   36.774  1.00 44.01  ? 297 VAL   A O    1 
ATOM   2283 C  CB   . VAL   A 1 297 ? -15.791 2.864   36.042  1.00 41.99  ? 297 VAL   A CB   1 
ATOM   2284 C  CG1  . VAL   A 1 297 ? -15.832 1.956   37.254  1.00 44.13  ? 297 VAL   A CG1  1 
ATOM   2285 C  CG2  . VAL   A 1 297 ? -16.713 4.036   36.234  1.00 40.05  ? 297 VAL   A CG2  1 
ATOM   2286 N  N    . ARG   A 1 298 ? -13.335 1.420   34.671  1.00 42.12  ? 298 ARG   A N    1 
ATOM   2287 C  CA   . ARG   A 1 298 ? -12.527 0.213   34.553  1.00 41.85  ? 298 ARG   A CA   1 
ATOM   2288 C  C    . ARG   A 1 298 ? -11.029 0.508   34.616  1.00 43.80  ? 298 ARG   A C    1 
ATOM   2289 O  O    . ARG   A 1 298 ? -10.280 -0.244  35.248  1.00 49.53  ? 298 ARG   A O    1 
ATOM   2290 C  CB   . ARG   A 1 298 ? -12.889 -0.499  33.246  1.00 49.94  ? 298 ARG   A CB   1 
ATOM   2291 C  CG   . ARG   A 1 298 ? -12.118 -1.779  32.953  1.00 55.09  ? 298 ARG   A CG   1 
ATOM   2292 C  CD   . ARG   A 1 298 ? -12.857 -2.656  31.953  1.00 56.35  ? 298 ARG   A CD   1 
ATOM   2293 N  NE   . ARG   A 1 298 ? -12.951 -2.050  30.635  1.00 63.13  ? 298 ARG   A NE   1 
ATOM   2294 C  CZ   . ARG   A 1 298 ? -14.016 -1.391  30.197  1.00 62.98  ? 298 ARG   A CZ   1 
ATOM   2295 N  NH1  . ARG   A 1 298 ? -15.059 -1.242  31.005  1.00 60.83  ? 298 ARG   A NH1  1 
ATOM   2296 N  NH2  . ARG   A 1 298 ? -14.027 -0.873  28.966  1.00 57.31  ? 298 ARG   A NH2  1 
ATOM   2297 N  N    . GLN   A 1 299 ? -10.566 1.582   33.960  1.00 39.14  ? 299 GLN   A N    1 
ATOM   2298 C  CA   . GLN   A 1 299 ? -9.136  1.885   33.913  1.00 41.92  ? 299 GLN   A CA   1 
ATOM   2299 C  C    . GLN   A 1 299 ? -8.648  2.595   35.172  1.00 46.98  ? 299 GLN   A C    1 
ATOM   2300 O  O    . GLN   A 1 299 ? -7.473  2.472   35.542  1.00 52.22  ? 299 GLN   A O    1 
ATOM   2301 C  CB   . GLN   A 1 299 ? -8.806  2.748   32.681  1.00 46.23  ? 299 GLN   A CB   1 
ATOM   2302 C  CG   . GLN   A 1 299 ? -7.297  3.073   32.497  1.00 41.00  ? 299 GLN   A CG   1 
ATOM   2303 C  CD   . GLN   A 1 299 ? -6.972  3.814   31.203  1.00 46.25  ? 299 GLN   A CD   1 
ATOM   2304 O  OE1  . GLN   A 1 299 ? -5.836  4.252   31.002  1.00 47.69  ? 299 GLN   A OE1  1 
ATOM   2305 N  NE2  . GLN   A 1 299 ? -7.965  3.962   30.322  1.00 45.93  ? 299 GLN   A NE2  1 
ATOM   2306 N  N    . CYS   A 1 300 ? -9.514  3.350   35.837  1.00 46.26  ? 300 CYS   A N    1 
ATOM   2307 C  CA   . CYS   A 1 300 ? -9.115  4.002   37.075  1.00 47.42  ? 300 CYS   A CA   1 
ATOM   2308 C  C    . CYS   A 1 300 ? -9.219  3.082   38.290  1.00 43.84  ? 300 CYS   A C    1 
ATOM   2309 O  O    . CYS   A 1 300 ? -8.589  3.362   39.314  1.00 47.71  ? 300 CYS   A O    1 
ATOM   2310 C  CB   . CYS   A 1 300 ? -9.949  5.268   37.253  1.00 46.87  ? 300 CYS   A CB   1 
ATOM   2311 S  SG   . CYS   A 1 300 ? -9.638  6.408   35.863  1.00 45.49  ? 300 CYS   A SG   1 
ATOM   2312 N  N    . SER   A 1 301 ? -9.974  1.991   38.201  1.00 43.76  ? 301 SER   A N    1 
ATOM   2313 C  CA   . SER   A 1 301 ? -10.002 0.997   39.274  1.00 49.68  ? 301 SER   A CA   1 
ATOM   2314 C  C    . SER   A 1 301 ? -9.854  -0.422  38.710  1.00 44.86  ? 301 SER   A C    1 
ATOM   2315 O  O    . SER   A 1 301 ? -10.814 -1.030  38.238  1.00 44.66  ? 301 SER   A O    1 
ATOM   2316 C  CB   . SER   A 1 301 ? -11.293 1.119   40.105  1.00 51.84  ? 301 SER   A CB   1 
ATOM   2317 O  OG   . SER   A 1 301 ? -11.482 2.436   40.615  1.00 50.48  ? 301 SER   A OG   1 
HETATM 2318 C  C10  . YXY   B 2 1   ? -13.596 2.761   -7.343  1.00 52.11  ? 1   YXY   B C10  1 
HETATM 2319 C  C02  . YXY   B 2 1   ? -13.744 0.188   -5.553  1.00 58.11  ? 1   YXY   B C02  1 
HETATM 2320 O  O03  . YXY   B 2 1   ? -12.591 0.265   -5.280  1.00 57.20  ? 1   YXY   B O03  1 
HETATM 2321 C  C04  . YXY   B 2 1   ? -14.149 0.262   -7.034  1.00 63.83  ? 1   YXY   B C04  1 
HETATM 2322 C  C05  . YXY   B 2 1   ? -12.958 -0.198  -7.866  1.00 65.57  ? 1   YXY   B C05  1 
HETATM 2323 C  C06  . YXY   B 2 1   ? -12.175 0.958   -8.480  1.00 58.31  ? 1   YXY   B C06  1 
HETATM 2324 C  C07  . YXY   B 2 1   ? -12.198 2.269   -7.700  1.00 53.64  ? 1   YXY   B C07  1 
HETATM 2325 F  F08  . YXY   B 2 1   ? -11.574 3.196   -8.468  1.00 54.09  ? 1   YXY   B F08  1 
HETATM 2326 F  F09  . YXY   B 2 1   ? -11.486 2.120   -6.546  1.00 56.33  ? 1   YXY   B F09  1 
HETATM 2327 C  C11  . YXY   B 2 1   ? -14.639 1.656   -7.466  1.00 62.05  ? 1   YXY   B C11  1 
HETATM 2328 N  N    . CHG   B 2 2   ? -14.760 -0.003  -4.521  1.00 57.90  ? 2   CHG   B N    1 
HETATM 2329 C  CA   . CHG   B 2 2   ? -14.407 -0.075  -3.112  1.00 53.27  ? 2   CHG   B CA   1 
HETATM 2330 C  C    . CHG   B 2 2   ? -13.251 -1.068  -2.942  1.00 52.79  ? 2   CHG   B C    1 
HETATM 2331 O  O    . CHG   B 2 2   ? -13.387 -2.223  -3.169  1.00 55.46  ? 2   CHG   B O    1 
HETATM 2332 C  C1   . CHG   B 2 2   ? -15.666 -0.278  -2.240  1.00 52.28  ? 2   CHG   B C1   1 
HETATM 2333 C  C2   . CHG   B 2 2   ? -15.397 -1.009  -0.926  1.00 49.29  ? 2   CHG   B C2   1 
HETATM 2334 C  C3   . CHG   B 2 2   ? -16.652 -0.905  -0.054  1.00 44.62  ? 2   CHG   B C3   1 
HETATM 2335 C  C4   . CHG   B 2 2   ? -17.947 -1.365  -0.729  1.00 41.76  ? 2   CHG   B C4   1 
HETATM 2336 C  C5   . CHG   B 2 2   ? -18.094 -0.844  -2.160  1.00 52.15  ? 2   CHG   B C5   1 
HETATM 2337 C  C6   . CHG   B 2 2   ? -16.810 -0.952  -2.995  1.00 55.36  ? 2   CHG   B C6   1 
HETATM 2338 C  C    . FP9   B 2 3   ? -10.523 -2.271  -1.391  1.00 44.06  ? 3   FP9   B C    1 
HETATM 2339 N  N    . FP9   B 2 3   ? -11.962 -0.498  -2.551  1.00 50.93  ? 3   FP9   B N    1 
HETATM 2340 O  O    . FP9   B 2 3   ? -9.534  -2.521  -0.779  1.00 41.11  ? 3   FP9   B O    1 
HETATM 2341 C  CA   . FP9   B 2 3   ? -10.578 -1.181  -2.338  1.00 46.03  ? 3   FP9   B CA   1 
HETATM 2342 C  CB   . FP9   B 2 3   ? -9.624  0.010   -1.995  1.00 43.84  ? 3   FP9   B CB   1 
HETATM 2343 C  CD   . FP9   B 2 3   ? -11.772 0.769   -2.309  1.00 48.73  ? 3   FP9   B CD   1 
HETATM 2344 F  FD   . FP9   B 2 3   ? -10.019 0.936   -4.010  1.00 54.82  ? 3   FP9   B FD   1 
HETATM 2345 C  CG   . FP9   B 2 3   ? -10.181 0.998   -2.584  1.00 49.71  ? 3   FP9   B CG   1 
HETATM 2346 C  C    . 005   B 2 4   ? -11.742 -3.023  1.947   1.00 40.31  ? 4   005   B C    1 
HETATM 2347 N  N    . 005   B 2 4   ? -11.708 -3.083  -1.239  1.00 43.10  ? 4   005   B N    1 
HETATM 2348 O  O    . 005   B 2 4   ? -10.598 -3.094  2.217   1.00 40.88  ? 4   005   B O    1 
HETATM 2349 C  CA   . 005   B 2 4   ? -12.447 -4.015  1.016   1.00 42.91  ? 4   005   B CA   1 
HETATM 2350 C  CD   . 005   B 2 4   ? -10.448 -5.634  -1.901  1.00 50.41  ? 4   005   B CD   1 
HETATM 2351 C  CG   . 005   B 2 4   ? -10.727 -5.258  -0.446  1.00 48.42  ? 4   005   B CG   1 
HETATM 2352 C  CH   . 005   B 2 4   ? -9.953  -6.262  -4.535  1.00 52.35  ? 4   005   B CH   1 
HETATM 2353 C  CB1  . 005   B 2 4   ? -11.897 -4.268  -0.402  1.00 47.94  ? 4   005   B CB1  1 
HETATM 2354 O  OB2  . 005   B 2 4   ? -13.724 -3.497  0.776   1.00 41.25  ? 4   005   B OB2  1 
HETATM 2355 C  CE1  . 005   B 2 4   ? -11.476 -5.569  -2.843  1.00 53.84  ? 4   005   B CE1  1 
HETATM 2356 C  CE2  . 005   B 2 4   ? -9.171  -6.011  -2.271  1.00 49.44  ? 4   005   B CE2  1 
HETATM 2357 C  CZ1  . 005   B 2 4   ? -11.230 -5.884  -4.167  1.00 51.58  ? 4   005   B CZ1  1 
HETATM 2358 C  CZ2  . 005   B 2 4   ? -8.930  -6.320  -3.598  1.00 51.66  ? 4   005   B CZ2  1 
HETATM 2359 C  C21  . A1L3F B 2 5   ? -9.836  1.812   3.924   1.00 42.02  ? 5   A1L3F B C21  1 
HETATM 2360 C  C22  . A1L3F B 2 5   ? -9.230  1.929   2.685   1.00 40.56  ? 5   A1L3F B C22  1 
HETATM 2361 C  C24  . A1L3F B 2 5   ? -9.543  1.075   1.638   1.00 39.04  ? 5   A1L3F B C24  1 
HETATM 2362 C  C18  . A1L3F B 2 5   ? -12.085 -1.022  3.510   1.00 44.65  ? 5   A1L3F B C18  1 
HETATM 2363 C  C19  . A1L3F B 2 5   ? -11.047 0.020   3.143   1.00 45.01  ? 5   A1L3F B C19  1 
HETATM 2364 C  C25  . A1L3F B 2 5   ? -10.484 0.084   1.878   1.00 41.64  ? 5   A1L3F B C25  1 
HETATM 2365 N  N17  . A1L3F B 2 5   ? -12.567 -1.980  2.533   1.00 43.58  ? 5   A1L3F B N17  1 
HETATM 2366 N  N20  . A1L3F B 2 5   ? -10.726 0.865   4.118   1.00 42.21  ? 5   A1L3F B N20  1 
HETATM 2367 CL CL23 . A1L3F B 2 5   ? -8.028  3.212   2.469   1.00 35.82  ? 5   A1L3F B CL23 1 
HETATM 2368 O  O    . HOH   C 3 .   ? -16.976 -2.379  27.883  1.00 57.45  ? 401 HOH   A O    1 
HETATM 2369 O  O    . HOH   C 3 .   ? -0.190  -20.651 6.527   1.00 68.67  ? 402 HOH   A O    1 
HETATM 2370 O  O    . HOH   C 3 .   ? -9.250  -23.293 4.691   1.00 80.58  ? 403 HOH   A O    1 
HETATM 2371 O  O    . HOH   C 3 .   ? -23.581 9.837   9.058   1.00 51.56  ? 404 HOH   A O    1 
HETATM 2372 O  O    . HOH   C 3 .   ? -21.106 7.433   25.923  1.00 31.11  ? 405 HOH   A O    1 
HETATM 2373 O  O    . HOH   C 3 .   ? -20.893 -18.944 14.015  1.00 50.97  ? 406 HOH   A O    1 
HETATM 2374 O  O    . HOH   C 3 .   ? -5.518  -15.604 10.875  1.00 48.85  ? 407 HOH   A O    1 
HETATM 2375 O  O    . HOH   C 3 .   ? -25.257 -12.919 10.795  1.00 49.62  ? 408 HOH   A O    1 
HETATM 2376 O  O    . HOH   C 3 .   ? -27.307 -8.765  2.170   1.00 49.17  ? 409 HOH   A O    1 
HETATM 2377 O  O    . HOH   C 3 .   ? -14.684 -0.962  26.695  1.00 58.59  ? 410 HOH   A O    1 
HETATM 2378 O  O    . HOH   C 3 .   ? -13.830 10.220  26.300  1.00 40.74  ? 411 HOH   A O    1 
HETATM 2379 O  O    . HOH   C 3 .   ? -23.285 12.952  25.793  1.00 39.22  ? 412 HOH   A O    1 
HETATM 2380 O  O    . HOH   C 3 .   ? -17.901 11.232  3.100   1.00 54.37  ? 413 HOH   A O    1 
HETATM 2381 O  O    . HOH   C 3 .   ? -18.196 8.663   23.118  1.00 47.91  ? 414 HOH   A O    1 
HETATM 2382 O  O    . HOH   C 3 .   ? -15.673 -17.627 -8.304  1.00 47.22  ? 415 HOH   A O    1 
HETATM 2383 O  O    . HOH   C 3 .   ? -1.325  6.228   41.290  1.00 42.14  ? 416 HOH   A O    1 
HETATM 2384 O  O    . HOH   C 3 .   ? -22.960 9.148   -4.954  1.00 53.63  ? 417 HOH   A O    1 
HETATM 2385 O  O    . HOH   C 3 .   ? -10.216 -8.133  13.453  1.00 32.15  ? 418 HOH   A O    1 
HETATM 2386 O  O    . HOH   C 3 .   ? -27.144 -2.067  5.997   1.00 35.61  ? 419 HOH   A O    1 
HETATM 2387 O  O    . HOH   C 3 .   ? -18.111 20.413  42.938  1.00 42.24  ? 420 HOH   A O    1 
HETATM 2388 O  O    . HOH   C 3 .   ? -17.634 16.544  47.379  1.00 39.81  ? 421 HOH   A O    1 
HETATM 2389 O  O    . HOH   C 3 .   ? -12.061 -14.164 29.917  1.00 50.69  ? 422 HOH   A O    1 
HETATM 2390 O  O    . HOH   C 3 .   ? -14.114 3.171   -0.001  1.00 47.07  ? 423 HOH   A O    1 
HETATM 2391 O  O    . HOH   C 3 .   ? -28.538 -6.045  12.067  1.00 52.82  ? 424 HOH   A O    1 
HETATM 2392 O  O    . HOH   C 3 .   ? -16.891 11.009  11.260  1.00 42.56  ? 425 HOH   A O    1 
HETATM 2393 O  O    . HOH   C 3 .   ? -11.210 10.788  22.301  1.00 43.13  ? 426 HOH   A O    1 
HETATM 2394 O  O    . HOH   C 3 .   ? -9.201  25.465  39.534  1.00 58.27  ? 427 HOH   A O    1 
HETATM 2395 O  O    . HOH   C 3 .   ? -4.858  -25.935 7.384   1.00 84.31  ? 428 HOH   A O    1 
HETATM 2396 O  O    . HOH   C 3 .   ? -14.141 6.831   15.919  1.00 55.11  ? 429 HOH   A O    1 
HETATM 2397 O  O    . HOH   C 3 .   ? -6.306  12.942  27.749  1.00 36.45  ? 430 HOH   A O    1 
HETATM 2398 O  O    . HOH   C 3 .   ? -4.273  2.337   1.701   1.00 46.28  ? 431 HOH   A O    1 
HETATM 2399 O  O    . HOH   C 3 .   ? 0.864   15.035  25.005  1.00 38.30  ? 432 HOH   A O    1 
HETATM 2400 O  O    . HOH   C 3 .   ? -25.906 11.920  18.366  1.00 47.58  ? 433 HOH   A O    1 
HETATM 2401 O  O    . HOH   C 3 .   ? -22.524 0.524   28.110  1.00 52.12  ? 434 HOH   A O    1 
HETATM 2402 O  O    . HOH   C 3 .   ? -19.547 -10.041 26.306  1.00 51.25  ? 435 HOH   A O    1 
HETATM 2403 O  O    . HOH   C 3 .   ? -7.783  -11.613 24.301  1.00 29.48  ? 436 HOH   A O    1 
HETATM 2404 O  O    . HOH   C 3 .   ? -3.631  -1.184  -1.267  1.00 50.98  ? 437 HOH   A O    1 
HETATM 2405 O  O    . HOH   C 3 .   ? -19.906 -26.617 -4.821  1.00 59.26  ? 438 HOH   A O    1 
HETATM 2406 O  O    . HOH   C 3 .   ? -20.188 -5.097  1.531   1.00 32.76  ? 439 HOH   A O    1 
HETATM 2407 O  O    . HOH   C 3 .   ? -20.978 2.855   9.353   1.00 38.21  ? 440 HOH   A O    1 
HETATM 2408 O  O    . HOH   C 3 .   ? -32.269 -5.220  9.349   1.00 49.89  ? 441 HOH   A O    1 
HETATM 2409 O  O    . HOH   C 3 .   ? -9.088  -2.634  27.366  1.00 30.00  ? 442 HOH   A O    1 
HETATM 2410 O  O    . HOH   C 3 .   ? -16.277 33.371  32.944  1.00 42.94  ? 443 HOH   A O    1 
HETATM 2411 O  O    . HOH   C 3 .   ? -20.156 30.035  33.209  1.00 59.96  ? 444 HOH   A O    1 
HETATM 2412 O  O    . HOH   C 3 .   ? -14.558 -16.856 25.775  1.00 48.37  ? 445 HOH   A O    1 
HETATM 2413 O  O    . HOH   C 3 .   ? -14.710 20.978  22.009  1.00 41.76  ? 446 HOH   A O    1 
HETATM 2414 O  O    . HOH   C 3 .   ? -1.740  14.192  32.965  1.00 48.52  ? 447 HOH   A O    1 
HETATM 2415 O  O    . HOH   C 3 .   ? -4.652  -31.337 3.728   1.00 60.08  ? 448 HOH   A O    1 
HETATM 2416 O  O    . HOH   C 3 .   ? -27.450 -5.662  -4.185  1.00 47.25  ? 449 HOH   A O    1 
HETATM 2417 O  O    . HOH   C 3 .   ? -4.536  4.483   36.040  1.00 42.71  ? 450 HOH   A O    1 
HETATM 2418 O  O    . HOH   C 3 .   ? -7.270  14.434  42.848  1.00 50.13  ? 451 HOH   A O    1 
HETATM 2419 O  O    . HOH   C 3 .   ? -16.792 3.105   -1.084  1.00 55.39  ? 452 HOH   A O    1 
HETATM 2420 O  O    . HOH   C 3 .   ? -2.018  21.772  32.022  1.00 60.97  ? 453 HOH   A O    1 
HETATM 2421 O  O    . HOH   C 3 .   ? -12.167 -21.776 23.284  1.00 47.64  ? 454 HOH   A O    1 
HETATM 2422 O  O    . HOH   C 3 .   ? -28.004 -9.853  19.000  1.00 43.74  ? 455 HOH   A O    1 
HETATM 2423 O  O    . HOH   C 3 .   ? -7.847  -8.461  -7.661  1.00 53.39  ? 456 HOH   A O    1 
HETATM 2424 O  O    . HOH   C 3 .   ? -18.627 -7.417  25.851  1.00 62.23  ? 457 HOH   A O    1 
HETATM 2425 O  O    . HOH   C 3 .   ? -29.293 -7.781  -4.255  1.00 56.85  ? 458 HOH   A O    1 
HETATM 2426 O  O    . HOH   C 3 .   ? -20.331 -18.516 21.865  1.00 49.67  ? 459 HOH   A O    1 
HETATM 2427 O  O    . HOH   C 3 .   ? -15.095 21.904  40.069  1.00 48.66  ? 460 HOH   A O    1 
HETATM 2428 O  O    . HOH   C 3 .   ? -31.838 -7.833  9.976   1.00 46.84  ? 461 HOH   A O    1 
HETATM 2429 O  O    . HOH   C 3 .   ? -13.315 1.196   0.708   1.00 42.47  ? 462 HOH   A O    1 
HETATM 2430 O  O    . HOH   C 3 .   ? -11.062 -1.189  27.746  1.00 44.59  ? 463 HOH   A O    1 
HETATM 2431 O  O    . HOH   C 3 .   ? -26.483 -14.935 -12.396 1.00 57.80  ? 464 HOH   A O    1 
HETATM 2432 O  O    . HOH   C 3 .   ? -29.460 -0.428  -4.568  1.00 45.87  ? 465 HOH   A O    1 
HETATM 2433 O  O    . HOH   C 3 .   ? -3.845  12.041  23.175  1.00 42.06  ? 466 HOH   A O    1 
HETATM 2434 O  O    . HOH   C 3 .   ? -26.697 -1.560  0.441   1.00 37.98  ? 467 HOH   A O    1 
HETATM 2435 O  O    . HOH   C 3 .   ? -28.880 16.494  36.928  1.00 48.31  ? 468 HOH   A O    1 
HETATM 2436 O  O    . HOH   C 3 .   ? -31.311 -11.440 5.549   1.00 52.95  ? 469 HOH   A O    1 
HETATM 2437 O  O    . HOH   C 3 .   ? -28.195 32.719  16.717  1.00 47.09  ? 470 HOH   A O    1 
HETATM 2438 O  O    . HOH   C 3 .   ? -2.049  -23.455 1.963   1.00 62.03  ? 471 HOH   A O    1 
HETATM 2439 O  O    . HOH   C 3 .   ? -13.309 -2.921  36.992  1.00 38.18  ? 472 HOH   A O    1 
HETATM 2440 O  O    . HOH   C 3 .   ? 1.213   -5.040  8.460   1.00 54.94  ? 473 HOH   A O    1 
HETATM 2441 O  O    . HOH   C 3 .   ? -1.910  -10.554 -1.259  1.00 55.09  ? 474 HOH   A O    1 
HETATM 2442 O  O    . HOH   C 3 .   ? -10.434 9.230   43.542  1.00 51.86  ? 475 HOH   A O    1 
HETATM 2443 O  O    . HOH   C 3 .   ? -4.006  25.684  23.013  1.00 68.30  ? 476 HOH   A O    1 
HETATM 2444 O  O    . HOH   C 3 .   ? -18.347 19.456  16.671  1.00 48.20  ? 477 HOH   A O    1 
HETATM 2445 O  O    . HOH   C 3 .   ? 1.110   19.395  32.566  1.00 33.90  ? 478 HOH   A O    1 
HETATM 2446 O  O    . HOH   C 3 .   ? -9.115  -11.751 26.289  1.00 37.97  ? 479 HOH   A O    1 
HETATM 2447 O  O    . HOH   C 3 .   ? -29.796 -3.638  0.565   1.00 59.95  ? 480 HOH   A O    1 
HETATM 2448 O  O    . HOH   C 3 .   ? -23.683 10.576  19.990  1.00 46.43  ? 481 HOH   A O    1 
HETATM 2449 O  O    . HOH   C 3 .   ? -10.136 12.239  43.266  1.00 48.25  ? 482 HOH   A O    1 
HETATM 2450 O  O    . HOH   C 3 .   ? -5.086  4.684   2.914   1.00 40.66  ? 483 HOH   A O    1 
HETATM 2451 O  O    . HOH   C 3 .   ? -26.117 3.270   25.438  1.00 29.08  ? 484 HOH   A O    1 
HETATM 2452 O  O    . HOH   C 3 .   ? -1.535  11.142  23.325  1.00 42.78  ? 485 HOH   A O    1 
HETATM 2453 O  O    . HOH   C 3 .   ? -25.821 30.467  25.530  1.00 40.89  ? 486 HOH   A O    1 
HETATM 2454 O  O    . HOH   C 3 .   ? -14.666 -21.506 -12.053 1.00 49.00  ? 487 HOH   A O    1 
HETATM 2455 O  O    . HOH   C 3 .   ? 1.797   -6.757  6.094   1.00 47.11  ? 488 HOH   A O    1 
HETATM 2456 O  O    . HOH   C 3 .   ? -13.475 -5.196  34.762  1.00 44.37  ? 489 HOH   A O    1 
HETATM 2457 O  O    . HOH   C 3 .   ? -16.571 24.124  15.115  1.00 53.91  ? 490 HOH   A O    1 
HETATM 2458 O  O    . HOH   C 3 .   ? -13.369 21.217  49.116  1.00 66.12  ? 491 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    . SER   A 1   ? 0.4682 0.4015 0.4244 0.0181  -0.0251 -0.0216 1   SER   A N    
2    C  CA   . SER   A 1   ? 0.5308 0.4723 0.4963 0.0165  -0.0213 -0.0213 1   SER   A CA   
3    C  C    . SER   A 1   ? 0.6193 0.5734 0.5986 0.0159  -0.0190 -0.0194 1   SER   A C    
4    O  O    . SER   A 1   ? 0.5692 0.5251 0.5486 0.0164  -0.0183 -0.0183 1   SER   A O    
5    C  CB   . SER   A 1   ? 0.5304 0.4713 0.5001 0.0171  -0.0258 -0.0223 1   SER   A CB   
6    O  OG   . SER   A 1   ? 0.6410 0.5699 0.5974 0.0178  -0.0272 -0.0241 1   SER   A OG   
7    N  N    . GLY   A 2   ? 0.5441 0.5058 0.5338 0.0151  -0.0180 -0.0191 2   GLY   A N    
8    C  CA   . GLY   A 2   ? 0.5523 0.5252 0.5545 0.0147  -0.0157 -0.0173 2   GLY   A CA   
9    C  C    . GLY   A 2   ? 0.6269 0.6030 0.6282 0.0132  -0.0092 -0.0170 2   GLY   A C    
10   O  O    . GLY   A 2   ? 0.6102 0.5808 0.6017 0.0122  -0.0062 -0.0178 2   GLY   A O    
11   N  N    . PHE   A 3   ? 0.6347 0.6201 0.6468 0.0128  -0.0070 -0.0158 3   PHE   A N    
12   C  CA   . PHE   A 3   ? 0.6187 0.6080 0.6313 0.0116  -0.0015 -0.0156 3   PHE   A CA   
13   C  C    . PHE   A 3   ? 0.6386 0.6369 0.6620 0.0119  -0.0004 -0.0138 3   PHE   A C    
14   O  O    . PHE   A 3   ? 0.6734 0.6769 0.7047 0.0120  0.0000  -0.0135 3   PHE   A O    
15   C  CB   . PHE   A 3   ? 0.6056 0.5948 0.6171 0.0110  0.0009  -0.0171 3   PHE   A CB   
16   C  CG   . PHE   A 3   ? 0.6053 0.5969 0.6142 0.0097  0.0064  -0.0175 3   PHE   A CG   
17   C  CD1  . PHE   A 3   ? 0.5915 0.5773 0.5897 0.0084  0.0086  -0.0183 3   PHE   A CD1  
18   C  CD2  . PHE   A 3   ? 0.5845 0.5844 0.6015 0.0094  0.0093  -0.0169 3   PHE   A CD2  
19   C  CE1  . PHE   A 3   ? 0.5500 0.5394 0.5470 0.0065  0.0137  -0.0184 3   PHE   A CE1  
20   C  CE2  . PHE   A 3   ? 0.5680 0.5712 0.5836 0.0079  0.0139  -0.0173 3   PHE   A CE2  
21   C  CZ   . PHE   A 3   ? 0.5463 0.5449 0.5525 0.0063  0.0162  -0.0179 3   PHE   A CZ   
22   N  N    . ARG   A 4   ? 0.6429 0.6417 0.6651 0.0124  0.0000  -0.0127 4   ARG   A N    
23   C  CA   . ARG   A 4   ? 0.5850 0.5909 0.6150 0.0133  0.0013  -0.0110 4   ARG   A CA   
24   C  C    . ARG   A 4   ? 0.5911 0.5980 0.6187 0.0118  0.0055  -0.0109 4   ARG   A C    
25   O  O    . ARG   A 4   ? 0.5954 0.5976 0.6149 0.0100  0.0072  -0.0119 4   ARG   A O    
26   C  CB   . ARG   A 4   ? 0.5728 0.5784 0.6026 0.0156  -0.0014 -0.0097 4   ARG   A CB   
27   C  CG   . ARG   A 4   ? 0.5681 0.5734 0.6005 0.0172  -0.0061 -0.0097 4   ARG   A CG   
28   C  CD   . ARG   A 4   ? 0.6434 0.6554 0.6867 0.0166  -0.0068 -0.0090 4   ARG   A CD   
29   N  NE   . ARG   A 4   ? 0.7081 0.7288 0.7615 0.0178  -0.0059 -0.0069 4   ARG   A NE   
30   C  CZ   . ARG   A 4   ? 0.6930 0.7189 0.7532 0.0195  -0.0087 -0.0055 4   ARG   A CZ   
31   N  NH1  . ARG   A 4   ? 0.7340 0.7681 0.8031 0.0205  -0.0069 -0.0033 4   ARG   A NH1  
32   N  NH2  . ARG   A 4   ? 0.6441 0.6672 0.7025 0.0202  -0.0132 -0.0062 4   ARG   A NH2  
33   N  N    . LYS   A 5   ? 0.5617 0.5749 0.5964 0.0125  0.0071  -0.0097 5   LYS   A N    
34   C  CA   . LYS   A 5   ? 0.5489 0.5624 0.5810 0.0114  0.0099  -0.0095 5   LYS   A CA   
35   C  C    . LYS   A 5   ? 0.5763 0.5839 0.6006 0.0120  0.0084  -0.0087 5   LYS   A C    
36   O  O    . LYS   A 5   ? 0.4936 0.5022 0.5200 0.0149  0.0065  -0.0075 5   LYS   A O    
37   C  CB   . LYS   A 5   ? 0.4273 0.4475 0.4674 0.0124  0.0115  -0.0084 5   LYS   A CB   
38   C  CG   . LYS   A 5   ? 0.4561 0.4808 0.5014 0.0116  0.0135  -0.0094 5   LYS   A CG   
39   C  CD   . LYS   A 5   ? 0.5344 0.5639 0.5850 0.0125  0.0152  -0.0086 5   LYS   A CD   
40   C  CE   . LYS   A 5   ? 0.5873 0.6213 0.6444 0.0131  0.0160  -0.0092 5   LYS   A CE   
41   N  NZ   . LYS   A 5   ? 0.6126 0.6467 0.6681 0.0119  0.0172  -0.0113 5   LYS   A NZ   
42   N  N    . MET   A 6   ? 0.5280 0.5294 0.5428 0.0095  0.0092  -0.0095 6   MET   A N    
43   C  CA   . MET   A 6   ? 0.4935 0.4874 0.4989 0.0096  0.0078  -0.0089 6   MET   A CA   
44   C  C    . MET   A 6   ? 0.5124 0.5066 0.5163 0.0078  0.0098  -0.0082 6   MET   A C    
45   O  O    . MET   A 6   ? 0.5448 0.5435 0.5523 0.0051  0.0126  -0.0086 6   MET   A O    
46   C  CB   . MET   A 6   ? 0.4938 0.4789 0.4880 0.0074  0.0073  -0.0098 6   MET   A CB   
47   C  CG   . MET   A 6   ? 0.5843 0.5655 0.5762 0.0100  0.0038  -0.0104 6   MET   A CG   
48   S  SD   . MET   A 6   ? 0.5897 0.5594 0.5670 0.0074  0.0037  -0.0115 6   MET   A SD   
49   C  CE   . MET   A 6   ? 0.4713 0.4410 0.4518 0.0104  -0.0001 -0.0126 6   MET   A CE   
50   N  N    . ALA   A 7   ? 0.4317 0.4208 0.4300 0.0097  0.0078  -0.0072 7   ALA   A N    
51   C  CA   . ALA   A 7   ? 0.4712 0.4567 0.4641 0.0075  0.0086  -0.0066 7   ALA   A CA   
52   C  C    . ALA   A 7   ? 0.4933 0.4670 0.4721 0.0053  0.0070  -0.0066 7   ALA   A C    
53   O  O    . ALA   A 7   ? 0.5011 0.4692 0.4742 0.0072  0.0048  -0.0070 7   ALA   A O    
54   C  CB   . ALA   A 7   ? 0.4448 0.4316 0.4400 0.0114  0.0074  -0.0054 7   ALA   A CB   
55   N  N    . PHE   A 8   ? 0.4891 0.4586 0.4617 0.0012  0.0079  -0.0062 8   PHE   A N    
56   C  CA   . PHE   A 8   ? 0.4695 0.4261 0.4272 -0.0010 0.0062  -0.0059 8   PHE   A CA   
57   C  C    . PHE   A 8   ? 0.4995 0.4485 0.4502 0.0044  0.0021  -0.0053 8   PHE   A C    
58   O  O    . PHE   A 8   ? 0.5333 0.4874 0.4906 0.0089  0.0014  -0.0049 8   PHE   A O    
59   C  CB   . PHE   A 8   ? 0.5435 0.4974 0.4967 -0.0071 0.0076  -0.0052 8   PHE   A CB   
60   C  CG   . PHE   A 8   ? 0.5907 0.5520 0.5495 -0.0124 0.0117  -0.0058 8   PHE   A CG   
61   C  CD1  . PHE   A 8   ? 0.6577 0.6146 0.6095 -0.0159 0.0133  -0.0061 8   PHE   A CD1  
62   C  CD2  . PHE   A 8   ? 0.5545 0.5273 0.5253 -0.0134 0.0141  -0.0060 8   PHE   A CD2  
63   C  CE1  . PHE   A 8   ? 0.6681 0.6326 0.6251 -0.0201 0.0176  -0.0066 8   PHE   A CE1  
64   C  CE2  . PHE   A 8   ? 0.6178 0.5984 0.5940 -0.0174 0.0178  -0.0066 8   PHE   A CE2  
65   C  CZ   . PHE   A 8   ? 0.6667 0.6435 0.6362 -0.0207 0.0198  -0.0069 8   PHE   A CZ   
66   N  N    . PRO   A 9   ? 0.5363 0.4730 0.4734 0.0046  -0.0005 -0.0054 9   PRO   A N    
67   C  CA   . PRO   A 9   ? 0.5203 0.4477 0.4479 0.0096  -0.0045 -0.0050 9   PRO   A CA   
68   C  C    . PRO   A 9   ? 0.4912 0.4157 0.4157 0.0084  -0.0047 -0.0040 9   PRO   A C    
69   O  O    . PRO   A 9   ? 0.4639 0.3851 0.3844 0.0019  -0.0034 -0.0035 9   PRO   A O    
70   C  CB   . PRO   A 9   ? 0.4978 0.4108 0.4092 0.0080  -0.0068 -0.0053 9   PRO   A CB   
71   C  CG   . PRO   A 9   ? 0.4991 0.4171 0.4155 0.0056  -0.0046 -0.0063 9   PRO   A CG   
72   C  CD   . PRO   A 9   ? 0.5020 0.4325 0.4314 0.0014  -0.0001 -0.0061 9   PRO   A CD   
73   N  N    . SER   A 10  ? 0.4704 0.3965 0.3971 0.0148  -0.0065 -0.0035 10  SER   A N    
74   C  CA   . SER   A 10  ? 0.5135 0.4385 0.4394 0.0146  -0.0066 -0.0027 10  SER   A CA   
75   C  C    . SER   A 10  ? 0.5165 0.4251 0.4248 0.0158  -0.0106 -0.0022 10  SER   A C    
76   O  O    . SER   A 10  ? 0.5123 0.4177 0.4177 0.0153  -0.0114 -0.0015 10  SER   A O    
77   C  CB   . SER   A 10  ? 0.4500 0.3858 0.3878 0.0208  -0.0057 -0.0023 10  SER   A CB   
78   O  OG   . SER   A 10  ? 0.4326 0.3673 0.3684 0.0285  -0.0078 -0.0022 10  SER   A OG   
79   N  N    . GLY   A 11  ? 0.5279 0.4253 0.4236 0.0176  -0.0135 -0.0026 11  GLY   A N    
80   C  CA   . GLY   A 11  ? 0.5168 0.3979 0.3948 0.0205  -0.0178 -0.0023 11  GLY   A CA   
81   C  C    . GLY   A 11  ? 0.5472 0.4185 0.4158 0.0135  -0.0186 -0.0014 11  GLY   A C    
82   O  O    . GLY   A 11  ? 0.5615 0.4239 0.4212 0.0163  -0.0215 -0.0009 11  GLY   A O    
83   N  N    . LYS   A 12  ? 0.5400 0.4131 0.4107 0.0044  -0.0160 -0.0012 12  LYS   A N    
84   C  CA   . LYS   A 12  ? 0.5692 0.4338 0.4316 -0.0034 -0.0169 -0.0002 12  LYS   A CA   
85   C  C    . LYS   A 12  ? 0.5801 0.4509 0.4502 -0.0028 -0.0168 0.0002  12  LYS   A C    
86   O  O    . LYS   A 12  ? 0.6033 0.4624 0.4622 -0.0042 -0.0202 0.0009  12  LYS   A O    
87   C  CB   . LYS   A 12  ? 0.5687 0.4380 0.4351 -0.0130 -0.0131 0.0001  12  LYS   A CB   
88   C  CG   . LYS   A 12  ? 0.5455 0.4019 0.3973 -0.0151 -0.0142 0.0001  12  LYS   A CG   
89   C  CD   . LYS   A 12  ? 0.6292 0.4917 0.4857 -0.0232 -0.0096 0.0003  12  LYS   A CD   
90   C  CE   . LYS   A 12  ? 0.6213 0.4694 0.4617 -0.0246 -0.0108 0.0003  12  LYS   A CE   
91   N  NZ   . LYS   A 12  ? 0.7343 0.5868 0.5769 -0.0329 -0.0060 0.0008  12  LYS   A NZ   
92   N  N    . VAL   A 13  ? 0.6401 0.5279 0.5281 0.0000  -0.0135 -0.0002 13  VAL   A N    
93   C  CA   . VAL   A 13  ? 0.6328 0.5269 0.5285 0.0010  -0.0133 0.0001  13  VAL   A CA   
94   C  C    . VAL   A 13  ? 0.5715 0.4607 0.4623 0.0106  -0.0160 0.0002  13  VAL   A C    
95   O  O    . VAL   A 13  ? 0.6364 0.5226 0.5250 0.0116  -0.0177 0.0006  13  VAL   A O    
96   C  CB   . VAL   A 13  ? 0.6087 0.5216 0.5242 -0.0001 -0.0086 -0.0005 13  VAL   A CB   
97   C  CG1  . VAL   A 13  ? 0.5486 0.4673 0.4713 0.0005  -0.0086 -0.0003 13  VAL   A CG1  
98   C  CG2  . VAL   A 13  ? 0.5502 0.4679 0.4695 -0.0086 -0.0056 -0.0007 13  VAL   A CG2  
99   N  N    . GLU   A 14  ? 0.5132 0.4014 0.4017 0.0179  -0.0167 -0.0002 14  GLU   A N    
100  C  CA   . GLU   A 14  ? 0.5445 0.4287 0.4279 0.0275  -0.0189 0.0000  14  GLU   A CA   
101  C  C    . GLU   A 14  ? 0.6359 0.5013 0.5000 0.0278  -0.0237 0.0005  14  GLU   A C    
102  O  O    . GLU   A 14  ? 0.6080 0.4708 0.4698 0.0313  -0.0250 0.0009  14  GLU   A O    
103  C  CB   . GLU   A 14  ? 0.5030 0.3889 0.3862 0.0346  -0.0193 -0.0005 14  GLU   A CB   
104  C  CG   . GLU   A 14  ? 0.5081 0.4119 0.4100 0.0354  -0.0152 -0.0007 14  GLU   A CG   
105  C  CD   . GLU   A 14  ? 0.4804 0.3862 0.3827 0.0412  -0.0162 -0.0013 14  GLU   A CD   
106  O  OE1  . GLU   A 14  ? 0.5306 0.4453 0.4429 0.0387  -0.0142 -0.0018 14  GLU   A OE1  
107  O  OE2  . GLU   A 14  ? 0.4964 0.3950 0.3892 0.0487  -0.0191 -0.0013 14  GLU   A OE2  
108  N  N    . GLY   A 15  ? 0.6402 0.4912 0.4894 0.0239  -0.0266 0.0004  15  GLY   A N    
109  C  CA   . GLY   A 15  ? 0.6183 0.4496 0.4476 0.0234  -0.0317 0.0008  15  GLY   A CA   
110  C  C    . GLY   A 15  ? 0.6610 0.4899 0.4902 0.0159  -0.0325 0.0016  15  GLY   A C    
111  O  O    . GLY   A 15  ? 0.7113 0.5228 0.5237 0.0128  -0.0370 0.0021  15  GLY   A O    
112  N  N    . CYS   A 16  ? 0.6241 0.4697 0.4715 0.0128  -0.0286 0.0016  16  CYS   A N    
113  C  CA   . CYS   A 16  ? 0.6750 0.5200 0.5239 0.0070  -0.0297 0.0021  16  CYS   A CA   
114  C  C    . CYS   A 16  ? 0.7028 0.5566 0.5612 0.0133  -0.0288 0.0019  16  CYS   A C    
115  O  O    . CYS   A 16  ? 0.7226 0.5760 0.5825 0.0094  -0.0302 0.0022  16  CYS   A O    
116  C  CB   . CYS   A 16  ? 0.6546 0.5104 0.5152 -0.0038 -0.0264 0.0022  16  CYS   A CB   
117  S  SG   . CYS   A 16  ? 0.7061 0.5531 0.5566 -0.0117 -0.0263 0.0026  16  CYS   A SG   
118  N  N    . MET   A 17  ? 0.6529 0.5143 0.5174 0.0227  -0.0266 0.0017  17  MET   A N    
119  C  CA   . MET   A 17  ? 0.6714 0.5414 0.5450 0.0283  -0.0250 0.0018  17  MET   A CA   
120  C  C    . MET   A 17  ? 0.7477 0.6034 0.6057 0.0362  -0.0290 0.0021  17  MET   A C    
121  O  O    . MET   A 17  ? 0.7752 0.6220 0.6218 0.0429  -0.0308 0.0021  17  MET   A O    
122  C  CB   . MET   A 17  ? 0.6053 0.4921 0.4947 0.0335  -0.0200 0.0017  17  MET   A CB   
123  C  CG   . MET   A 17  ? 0.5623 0.4613 0.4650 0.0263  -0.0165 0.0012  17  MET   A CG   
124  S  SD   . MET   A 17  ? 0.5166 0.4232 0.4294 0.0171  -0.0153 0.0010  17  MET   A SD   
125  C  CE   . MET   A 17  ? 0.6232 0.5307 0.5379 0.0233  -0.0161 0.0013  17  MET   A CE   
126  N  N    . VAL   A 18  ? 0.7047 0.5580 0.5620 0.0358  -0.0306 0.0023  18  VAL   A N    
127  C  CA   . VAL   A 18  ? 0.7785 0.6170 0.6201 0.0430  -0.0347 0.0026  18  VAL   A CA   
128  C  C    . VAL   A 18  ? 0.7099 0.5575 0.5606 0.0488  -0.0322 0.0028  18  VAL   A C    
129  O  O    . VAL   A 18  ? 0.6454 0.5090 0.5135 0.0458  -0.0281 0.0028  18  VAL   A O    
130  C  CB   . VAL   A 18  ? 0.7810 0.6016 0.6070 0.0364  -0.0409 0.0027  18  VAL   A CB   
131  C  CG1  . VAL   A 18  ? 0.7669 0.5755 0.5805 0.0315  -0.0437 0.0027  18  VAL   A CG1  
132  C  CG2  . VAL   A 18  ? 0.7383 0.5679 0.5766 0.0267  -0.0403 0.0026  18  VAL   A CG2  
133  N  N    . GLN   A 19  ? 0.7492 0.5854 0.5867 0.0575  -0.0347 0.0031  19  GLN   A N    
134  C  CA   . GLN   A 19  ? 0.7429 0.5833 0.5841 0.0638  -0.0331 0.0035  19  GLN   A CA   
135  C  C    . GLN   A 19  ? 0.7875 0.6143 0.6179 0.0607  -0.0385 0.0033  19  GLN   A C    
136  O  O    . GLN   A 19  ? 0.8952 0.7033 0.7069 0.0607  -0.0442 0.0032  19  GLN   A O    
137  C  CB   . GLN   A 19  ? 0.7898 0.6272 0.6234 0.0766  -0.0318 0.0041  19  GLN   A CB   
138  C  CG   . GLN   A 19  ? 0.8268 0.6663 0.6612 0.0841  -0.0299 0.0048  19  GLN   A CG   
139  C  CD   . GLN   A 19  ? 0.8223 0.6641 0.6534 0.0964  -0.0269 0.0056  19  GLN   A CD   
140  O  OE1  . GLN   A 19  ? 0.8152 0.6573 0.6437 0.0993  -0.0267 0.0054  19  GLN   A OE1  
141  N  NE2  . GLN   A 19  ? 0.7935 0.6381 0.6254 0.1036  -0.0242 0.0065  19  GLN   A NE2  
142  N  N    . VAL   A 20  ? 0.7067 0.5419 0.5480 0.0580  -0.0373 0.0032  20  VAL   A N    
143  C  CA   . VAL   A 20  ? 0.7446 0.5687 0.5778 0.0545  -0.0427 0.0028  20  VAL   A CA   
144  C  C    . VAL   A 20  ? 0.7466 0.5722 0.5806 0.0625  -0.0414 0.0030  20  VAL   A C    
145  O  O    . VAL   A 20  ? 0.7338 0.5750 0.5826 0.0653  -0.0357 0.0034  20  VAL   A O    
146  C  CB   . VAL   A 20  ? 0.7601 0.5923 0.6052 0.0420  -0.0435 0.0022  20  VAL   A CB   
147  C  CG1  . VAL   A 20  ? 0.7593 0.5811 0.5971 0.0387  -0.0496 0.0018  20  VAL   A CG1  
148  C  CG2  . VAL   A 20  ? 0.7399 0.5690 0.5820 0.0339  -0.0446 0.0022  20  VAL   A CG2  
149  N  N    . THR   A 21  ? 0.8213 0.6294 0.6383 0.0663  -0.0470 0.0030  21  THR   A N    
150  C  CA   . THR   A 21  ? 0.8032 0.6096 0.6175 0.0747  -0.0463 0.0032  21  THR   A CA   
151  C  C    . THR   A 21  ? 0.8317 0.6245 0.6363 0.0711  -0.0534 0.0025  21  THR   A C    
152  O  O    . THR   A 21  ? 0.8500 0.6257 0.6389 0.0681  -0.0601 0.0022  21  THR   A O    
153  C  CB   . THR   A 21  ? 0.7258 0.5234 0.5261 0.0875  -0.0450 0.0040  21  THR   A CB   
154  O  OG1  . THR   A 21  ? 0.6794 0.4890 0.4884 0.0899  -0.0394 0.0046  21  THR   A OG1  
155  C  CG2  . THR   A 21  ? 0.8615 0.6616 0.6626 0.0961  -0.0420 0.0047  21  THR   A CG2  
156  N  N    . CYS   A 22  ? 0.8153 0.6154 0.6290 0.0712  -0.0524 0.0022  22  CYS   A N    
157  C  CA   . CYS   A 22  ? 0.8611 0.6490 0.6660 0.0693  -0.0593 0.0014  22  CYS   A CA   
158  C  C    . CYS   A 22  ? 0.8700 0.6573 0.6726 0.0795  -0.0570 0.0017  22  CYS   A C    
159  O  O    . CYS   A 22  ? 0.8932 0.6965 0.7117 0.0802  -0.0513 0.0019  22  CYS   A O    
160  C  CB   . CYS   A 22  ? 0.8282 0.6262 0.6479 0.0572  -0.0615 0.0003  22  CYS   A CB   
161  S  SG   . CYS   A 22  ? 0.9234 0.7068 0.7334 0.0529  -0.0715 -0.0008 22  CYS   A SG   
162  N  N    . GLY   A 23  ? 0.9311 0.6992 0.7131 0.0875  -0.0613 0.0019  23  GLY   A N    
163  C  CA   . GLY   A 23  ? 0.8581 0.6251 0.6357 0.0990  -0.0575 0.0026  23  GLY   A CA   
164  C  C    . GLY   A 23  ? 0.9579 0.7378 0.7430 0.1056  -0.0487 0.0041  23  GLY   A C    
165  O  O    . GLY   A 23  ? 0.9212 0.6969 0.6989 0.1084  -0.0482 0.0045  23  GLY   A O    
166  N  N    . THR   A 24  ? 1.1165 0.9122 0.9163 0.1079  -0.0418 0.0049  24  THR   A N    
167  C  CA   . THR   A 24  ? 1.0690 0.8782 0.8774 0.1137  -0.0334 0.0065  24  THR   A CA   
168  C  C    . THR   A 24  ? 1.0848 0.9148 0.9160 0.1054  -0.0286 0.0064  24  THR   A C    
169  O  O    . THR   A 24  ? 1.0867 0.9302 0.9282 0.1087  -0.0217 0.0077  24  THR   A O    
170  C  CB   . THR   A 24  ? 1.0344 0.8443 0.8400 0.1237  -0.0286 0.0079  24  THR   A CB   
171  O  OG1  . THR   A 24  ? 1.0116 0.8297 0.8291 0.1194  -0.0276 0.0075  24  THR   A OG1  
172  C  CG2  . THR   A 24  ? 1.0019 0.7899 0.7833 0.1326  -0.0334 0.0078  24  THR   A CG2  
173  N  N    . THR   A 25  ? 0.9372 0.7704 0.7765 0.0949  -0.0323 0.0050  25  THR   A N    
174  C  CA   . THR   A 25  ? 0.9025 0.7539 0.7617 0.0870  -0.0283 0.0047  25  THR   A CA   
175  C  C    . THR   A 25  ? 0.7679 0.6189 0.6254 0.0837  -0.0288 0.0047  25  THR   A C    
176  O  O    . THR   A 25  ? 0.7764 0.6146 0.6225 0.0799  -0.0348 0.0039  25  THR   A O    
177  C  CB   . THR   A 25  ? 0.8625 0.7181 0.7308 0.0780  -0.0317 0.0031  25  THR   A CB   
178  O  OG1  . THR   A 25  ? 0.8529 0.7062 0.7199 0.0823  -0.0321 0.0030  25  THR   A OG1  
179  C  CG2  . THR   A 25  ? 0.7578 0.6321 0.6461 0.0709  -0.0272 0.0028  25  THR   A CG2  
180  N  N    . THR   A 26  ? 0.7332 0.5966 0.6005 0.0856  -0.0229 0.0056  26  THR   A N    
181  C  CA   . THR   A 26  ? 0.7823 0.6473 0.6502 0.0822  -0.0230 0.0054  26  THR   A CA   
182  C  C    . THR   A 26  ? 0.6953 0.5777 0.5828 0.0742  -0.0193 0.0050  26  THR   A C    
183  O  O    . THR   A 26  ? 0.6298 0.5257 0.5303 0.0760  -0.0139 0.0057  26  THR   A O    
184  C  CB   . THR   A 26  ? 0.7580 0.6221 0.6198 0.0915  -0.0200 0.0066  26  THR   A CB   
185  O  OG1  . THR   A 26  ? 0.7507 0.6326 0.6285 0.0937  -0.0130 0.0077  26  THR   A OG1  
186  C  CG2  . THR   A 26  ? 0.8276 0.6774 0.6718 0.1016  -0.0219 0.0072  26  THR   A CG2  
187  N  N    . LEU   A 27  ? 0.6373 0.5186 0.5261 0.0652  -0.0223 0.0039  27  LEU   A N    
188  C  CA   . LEU   A 27  ? 0.6495 0.5453 0.5542 0.0578  -0.0192 0.0034  27  LEU   A CA   
189  C  C    . LEU   A 27  ? 0.6041 0.4944 0.5031 0.0524  -0.0216 0.0030  27  LEU   A C    
190  O  O    . LEU   A 27  ? 0.6088 0.4835 0.4916 0.0532  -0.0262 0.0030  27  LEU   A O    
191  C  CB   . LEU   A 27  ? 0.6118 0.5155 0.5279 0.0509  -0.0195 0.0024  27  LEU   A CB   
192  C  CG   . LEU   A 27  ? 0.5953 0.4896 0.5046 0.0454  -0.0256 0.0014  27  LEU   A CG   
193  C  CD1  . LEU   A 27  ? 0.5680 0.4582 0.4741 0.0368  -0.0287 0.0009  27  LEU   A CD1  
194  C  CD2  . LEU   A 27  ? 0.5673 0.4729 0.4903 0.0420  -0.0246 0.0004  27  LEU   A CD2  
195  N  N    . ASN   A 28  ? 0.6411 0.5433 0.5524 0.0470  -0.0184 0.0027  28  ASN   A N    
196  C  CA   . ASN   A 28  ? 0.5756 0.4737 0.4823 0.0421  -0.0198 0.0024  28  ASN   A CA   
197  C  C    . ASN   A 28  ? 0.5927 0.4857 0.4967 0.0322  -0.0235 0.0017  28  ASN   A C    
198  O  O    . ASN   A 28  ? 0.5135 0.4138 0.4269 0.0275  -0.0234 0.0011  28  ASN   A O    
199  C  CB   . ASN   A 28  ? 0.5941 0.5065 0.5145 0.0404  -0.0150 0.0023  28  ASN   A CB   
200  C  CG   . ASN   A 28  ? 0.5350 0.4563 0.4625 0.0486  -0.0108 0.0032  28  ASN   A CG   
201  O  OD1  . ASN   A 28  ? 0.4705 0.3879 0.3913 0.0549  -0.0107 0.0038  28  ASN   A OD1  
202  N  ND2  . ASN   A 28  ? 0.4494 0.3833 0.3909 0.0482  -0.0072 0.0033  28  ASN   A ND2  
203  N  N    . GLY   A 29  ? 0.6040 0.4844 0.4949 0.0291  -0.0270 0.0018  29  GLY   A N    
204  C  CA   . GLY   A 29  ? 0.6067 0.4834 0.4958 0.0185  -0.0299 0.0015  29  GLY   A CA   
205  C  C    . GLY   A 29  ? 0.6010 0.4777 0.4889 0.0132  -0.0286 0.0016  29  GLY   A C    
206  O  O    . GLY   A 29  ? 0.6023 0.4772 0.4863 0.0183  -0.0273 0.0018  29  GLY   A O    
207  N  N    . LEU   A 30  ? 0.6446 0.5231 0.5355 0.0027  -0.0293 0.0015  30  LEU   A N    
208  C  CA   . LEU   A 30  ? 0.5852 0.4629 0.4741 -0.0039 -0.0281 0.0018  30  LEU   A CA   
209  C  C    . LEU   A 30  ? 0.6315 0.4914 0.5034 -0.0104 -0.0335 0.0025  30  LEU   A C    
210  O  O    . LEU   A 30  ? 0.6194 0.4797 0.4933 -0.0188 -0.0355 0.0028  30  LEU   A O    
211  C  CB   . LEU   A 30  ? 0.5500 0.4453 0.4565 -0.0110 -0.0236 0.0013  30  LEU   A CB   
212  C  CG   . LEU   A 30  ? 0.5796 0.4763 0.4857 -0.0173 -0.0211 0.0015  30  LEU   A CG   
213  C  CD1  . LEU   A 30  ? 0.5274 0.4260 0.4338 -0.0108 -0.0182 0.0012  30  LEU   A CD1  
214  C  CD2  . LEU   A 30  ? 0.5238 0.4354 0.4443 -0.0256 -0.0175 0.0011  30  LEU   A CD2  
215  N  N    . TRP   A 31  ? 0.6636 0.5082 0.5189 -0.0069 -0.0360 0.0029  31  TRP   A N    
216  C  CA   . TRP   A 31  ? 0.7140 0.5384 0.5500 -0.0121 -0.0417 0.0037  31  TRP   A CA   
217  C  C    . TRP   A 31  ? 0.7131 0.5367 0.5474 -0.0213 -0.0401 0.0043  31  TRP   A C    
218  O  O    . TRP   A 31  ? 0.7316 0.5559 0.5646 -0.0182 -0.0375 0.0041  31  TRP   A O    
219  C  CB   . TRP   A 31  ? 0.7325 0.5394 0.5498 -0.0021 -0.0456 0.0037  31  TRP   A CB   
220  C  CG   . TRP   A 31  ? 0.7738 0.5564 0.5676 -0.0058 -0.0522 0.0044  31  TRP   A CG   
221  C  CD1  . TRP   A 31  ? 0.8253 0.5992 0.6128 -0.0168 -0.0561 0.0053  31  TRP   A CD1  
222  C  CD2  . TRP   A 31  ? 0.7808 0.5447 0.5541 0.0019  -0.0561 0.0043  31  TRP   A CD2  
223  N  NE1  . TRP   A 31  ? 0.8334 0.5829 0.5968 -0.0169 -0.0623 0.0059  31  TRP   A NE1  
224  C  CE2  . TRP   A 31  ? 0.8251 0.5678 0.5790 -0.0051 -0.0624 0.0052  31  TRP   A CE2  
225  C  CE3  . TRP   A 31  ? 0.7415 0.5047 0.5111 0.0139  -0.0549 0.0036  31  TRP   A CE3  
226  C  CZ2  . TRP   A 31  ? 0.8779 0.5977 0.6078 0.0001  -0.0677 0.0052  31  TRP   A CZ2  
227  C  CZ3  . TRP   A 31  ? 0.7900 0.5321 0.5369 0.0194  -0.0600 0.0035  31  TRP   A CZ3  
228  C  CH2  . TRP   A 31  ? 0.8938 0.6138 0.6205 0.0128  -0.0664 0.0042  31  TRP   A CH2  
229  N  N    . LEU   A 32  ? 0.6913 0.5134 0.5254 -0.0327 -0.0416 0.0052  32  LEU   A N    
230  C  CA   . LEU   A 32  ? 0.6903 0.5125 0.5232 -0.0427 -0.0395 0.0061  32  LEU   A CA   
231  C  C    . LEU   A 32  ? 0.7613 0.5676 0.5801 -0.0525 -0.0450 0.0075  32  LEU   A C    
232  O  O    . LEU   A 32  ? 0.7575 0.5688 0.5832 -0.0583 -0.0468 0.0078  32  LEU   A O    
233  C  CB   . LEU   A 32  ? 0.7114 0.5568 0.5664 -0.0482 -0.0332 0.0057  32  LEU   A CB   
234  C  CG   . LEU   A 32  ? 0.6712 0.5344 0.5423 -0.0414 -0.0271 0.0044  32  LEU   A CG   
235  C  CD1  . LEU   A 32  ? 0.5839 0.4672 0.4743 -0.0478 -0.0225 0.0041  32  LEU   A CD1  
236  C  CD2  . LEU   A 32  ? 0.6261 0.4850 0.4908 -0.0384 -0.0249 0.0043  32  LEU   A CD2  
237  N  N    . ASP   A 33  ? 0.8007 0.5879 0.5999 -0.0547 -0.0478 0.0085  33  ASP   A N    
238  C  CA   . ASP   A 33  ? 0.8392 0.6062 0.6202 -0.0631 -0.0542 0.0100  33  ASP   A CA   
239  C  C    . ASP   A 33  ? 0.8848 0.6396 0.6562 -0.0559 -0.0607 0.0094  33  ASP   A C    
240  O  O    . ASP   A 33  ? 0.8275 0.5782 0.5937 -0.0433 -0.0612 0.0083  33  ASP   A O    
241  C  CB   . ASP   A 33  ? 0.8014 0.5788 0.5932 -0.0776 -0.0523 0.0114  33  ASP   A CB   
242  C  CG   . ASP   A 33  ? 0.7722 0.5637 0.5746 -0.0826 -0.0448 0.0118  33  ASP   A CG   
243  O  OD1  . ASP   A 33  ? 0.7889 0.5754 0.5845 -0.0764 -0.0429 0.0112  33  ASP   A OD1  
244  O  OD2  . ASP   A 33  ? 0.6625 0.4698 0.4795 -0.0921 -0.0409 0.0125  33  ASP   A OD2  
245  N  N    . ASP   A 34  ? 0.9335 0.6822 0.7018 -0.0630 -0.0657 0.0102  34  ASP   A N    
246  C  CA   . ASP   A 34  ? 0.9556 0.6920 0.7139 -0.0561 -0.0721 0.0096  34  ASP   A CA   
247  C  C    . ASP   A 34  ? 0.9579 0.7127 0.7359 -0.0539 -0.0705 0.0086  34  ASP   A C    
248  O  O    . ASP   A 34  ? 1.0228 0.7697 0.7958 -0.0547 -0.0763 0.0086  34  ASP   A O    
249  C  CB   . ASP   A 34  ? 1.0602 0.7730 0.7980 -0.0644 -0.0804 0.0111  34  ASP   A CB   
250  C  CG   . ASP   A 34  ? 1.0577 0.7790 0.8058 -0.0805 -0.0803 0.0126  34  ASP   A CG   
251  O  OD1  . ASP   A 34  ? 1.0458 0.7905 0.8152 -0.0852 -0.0733 0.0126  34  ASP   A OD1  
252  O  OD2  . ASP   A 34  ? 1.1077 0.8124 0.8423 -0.0884 -0.0875 0.0139  34  ASP   A OD2  
253  N  N    . VAL   A 35  ? 0.8663 0.6447 0.6658 -0.0513 -0.0631 0.0077  35  VAL   A N    
254  C  CA   . VAL   A 35  ? 0.7929 0.5890 0.6111 -0.0489 -0.0612 0.0066  35  VAL   A CA   
255  C  C    . VAL   A 35  ? 0.7470 0.5544 0.5743 -0.0367 -0.0559 0.0053  35  VAL   A C    
256  O  O    . VAL   A 35  ? 0.7537 0.5657 0.5830 -0.0344 -0.0513 0.0053  35  VAL   A O    
257  C  CB   . VAL   A 35  ? 0.7968 0.6126 0.6345 -0.0603 -0.0576 0.0069  35  VAL   A CB   
258  C  CG1  . VAL   A 35  ? 0.7843 0.6154 0.6386 -0.0577 -0.0572 0.0057  35  VAL   A CG1  
259  C  CG2  . VAL   A 35  ? 0.7684 0.5736 0.5971 -0.0737 -0.0622 0.0086  35  VAL   A CG2  
260  N  N    . VAL   A 36  ? 0.7266 0.5376 0.5584 -0.0288 -0.0568 0.0044  36  VAL   A N    
261  C  CA   . VAL   A 36  ? 0.7235 0.5447 0.5636 -0.0174 -0.0520 0.0035  36  VAL   A CA   
262  C  C    . VAL   A 36  ? 0.7312 0.5720 0.5918 -0.0178 -0.0488 0.0027  36  VAL   A C    
263  O  O    . VAL   A 36  ? 0.7135 0.5517 0.5737 -0.0172 -0.0526 0.0023  36  VAL   A O    
264  C  CB   . VAL   A 36  ? 0.7367 0.5424 0.5609 -0.0057 -0.0554 0.0034  36  VAL   A CB   
265  C  CG1  . VAL   A 36  ? 0.6947 0.5141 0.5307 0.0047  -0.0502 0.0027  36  VAL   A CG1  
266  C  CG2  . VAL   A 36  ? 0.7765 0.5651 0.5819 -0.0031 -0.0576 0.0039  36  VAL   A CG2  
267  N  N    . TYR   A 37  ? 0.7003 0.5596 0.5777 -0.0185 -0.0422 0.0022  37  TYR   A N    
268  C  CA   . TYR   A 37  ? 0.6130 0.4917 0.5102 -0.0200 -0.0389 0.0013  37  TYR   A CA   
269  C  C    . TYR   A 37  ? 0.5898 0.4752 0.4933 -0.0090 -0.0357 0.0006  37  TYR   A C    
270  O  O    . TYR   A 37  ? 0.5673 0.4528 0.4690 -0.0028 -0.0326 0.0009  37  TYR   A O    
271  C  CB   . TYR   A 37  ? 0.6438 0.5378 0.5545 -0.0271 -0.0335 0.0012  37  TYR   A CB   
272  C  CG   . TYR   A 37  ? 0.6358 0.5257 0.5423 -0.0389 -0.0354 0.0021  37  TYR   A CG   
273  C  CD1  . TYR   A 37  ? 0.5786 0.4541 0.4699 -0.0415 -0.0367 0.0032  37  TYR   A CD1  
274  C  CD2  . TYR   A 37  ? 0.6331 0.5336 0.5507 -0.0473 -0.0359 0.0019  37  TYR   A CD2  
275  C  CE1  . TYR   A 37  ? 0.6771 0.5479 0.5635 -0.0527 -0.0383 0.0044  37  TYR   A CE1  
276  C  CE2  . TYR   A 37  ? 0.6743 0.5719 0.5886 -0.0587 -0.0373 0.0031  37  TYR   A CE2  
277  C  CZ   . TYR   A 37  ? 0.7318 0.6141 0.6301 -0.0617 -0.0384 0.0045  37  TYR   A CZ   
278  O  OH   . TYR   A 37  ? 0.7969 0.6754 0.6909 -0.0736 -0.0395 0.0060  37  TYR   A OH   
279  N  N    . CYS   A 38  ? 0.6471 0.5385 0.5581 -0.0069 -0.0366 -0.0001 38  CYS   A N    
280  C  CA   . CYS   A 38  ? 0.5661 0.4638 0.4829 0.0030  -0.0335 -0.0005 38  CYS   A CA   
281  C  C    . CYS   A 38  ? 0.5110 0.4211 0.4417 0.0017  -0.0330 -0.0015 38  CYS   A C    
282  O  O    . CYS   A 38  ? 0.5057 0.4179 0.4400 -0.0057 -0.0361 -0.0021 38  CYS   A O    
283  C  CB   . CYS   A 38  ? 0.5943 0.4757 0.4948 0.0118  -0.0369 0.0001  38  CYS   A CB   
284  S  SG   . CYS   A 38  ? 0.6138 0.4809 0.5029 0.0117  -0.0447 -0.0002 38  CYS   A SG   
285  N  N    . PRO   A 39  ? 0.4916 0.4106 0.4309 0.0086  -0.0292 -0.0019 39  PRO   A N    
286  C  CA   . PRO   A 39  ? 0.5349 0.4633 0.4851 0.0089  -0.0293 -0.0030 39  PRO   A CA   
287  C  C    . PRO   A 39  ? 0.5614 0.4777 0.5016 0.0110  -0.0354 -0.0032 39  PRO   A C    
288  O  O    . PRO   A 39  ? 0.5888 0.4901 0.5139 0.0163  -0.0381 -0.0024 39  PRO   A O    
289  C  CB   . PRO   A 39  ? 0.5618 0.4984 0.5193 0.0167  -0.0240 -0.0029 39  PRO   A CB   
290  C  CG   . PRO   A 39  ? 0.5123 0.4500 0.4688 0.0173  -0.0202 -0.0020 39  PRO   A CG   
291  C  CD   . PRO   A 39  ? 0.4743 0.3964 0.4148 0.0159  -0.0243 -0.0012 39  PRO   A CD   
292  N  N    . ARG   A 40  ? 0.5460 0.4688 0.4944 0.0072  -0.0379 -0.0045 40  ARG   A N    
293  C  CA   . ARG   A 40  ? 0.6277 0.5385 0.5664 0.0076  -0.0449 -0.0048 40  ARG   A CA   
294  C  C    . ARG   A 40  ? 0.6675 0.5714 0.5999 0.0180  -0.0452 -0.0048 40  ARG   A C    
295  O  O    . ARG   A 40  ? 0.6275 0.5167 0.5467 0.0205  -0.0510 -0.0047 40  ARG   A O    
296  C  CB   . ARG   A 40  ? 0.6013 0.5216 0.5512 0.0000  -0.0482 -0.0062 40  ARG   A CB   
297  C  CG   . ARG   A 40  ? 0.5585 0.4935 0.5232 0.0032  -0.0457 -0.0078 40  ARG   A CG   
298  C  CD   . ARG   A 40  ? 0.5137 0.4551 0.4864 -0.0028 -0.0507 -0.0093 40  ARG   A CD   
299  N  NE   . ARG   A 40  ? 0.4990 0.4572 0.4877 -0.0011 -0.0475 -0.0110 40  ARG   A NE   
300  C  CZ   . ARG   A 40  ? 0.5225 0.4905 0.5216 -0.0049 -0.0508 -0.0127 40  ARG   A CZ   
301  N  NH1  . ARG   A 40  ? 0.5243 0.4875 0.5203 -0.0115 -0.0575 -0.0128 40  ARG   A NH1  
302  N  NH2  . ARG   A 40  ? 0.5125 0.4948 0.5249 -0.0022 -0.0478 -0.0144 40  ARG   A NH2  
303  N  N    . HIS   A 41  ? 0.6576 0.5712 0.5983 0.0241  -0.0392 -0.0047 41  HIS   A N    
304  C  CA   . HIS   A 41  ? 0.6006 0.5081 0.5352 0.0338  -0.0386 -0.0043 41  HIS   A CA   
305  C  C    . HIS   A 41  ? 0.6791 0.5726 0.5978 0.0406  -0.0385 -0.0027 41  HIS   A C    
306  O  O    . HIS   A 41  ? 0.7182 0.6071 0.6313 0.0493  -0.0367 -0.0019 41  HIS   A O    
307  C  CB   . HIS   A 41  ? 0.5367 0.4583 0.4846 0.0373  -0.0324 -0.0044 41  HIS   A CB   
308  C  CG   . HIS   A 41  ? 0.5982 0.5280 0.5521 0.0374  -0.0261 -0.0034 41  HIS   A CG   
309  N  ND1  . HIS   A 41  ? 0.5833 0.5271 0.5509 0.0314  -0.0231 -0.0042 41  HIS   A ND1  
310  C  CD2  . HIS   A 41  ? 0.6059 0.5328 0.5548 0.0434  -0.0223 -0.0018 41  HIS   A CD2  
311  C  CE1  . HIS   A 41  ? 0.5464 0.4941 0.5161 0.0333  -0.0182 -0.0031 41  HIS   A CE1  
312  N  NE2  . HIS   A 41  ? 0.5922 0.5304 0.5514 0.0404  -0.0177 -0.0016 41  HIS   A NE2  
313  N  N    . VAL   A 42  ? 0.6740 0.5602 0.5847 0.0369  -0.0403 -0.0021 42  VAL   A N    
314  C  CA   . VAL   A 42  ? 0.7608 0.6314 0.6541 0.0435  -0.0416 -0.0009 42  VAL   A CA   
315  C  C    . VAL   A 42  ? 0.7256 0.5802 0.6041 0.0480  -0.0476 -0.0011 42  VAL   A C    
316  O  O    . VAL   A 42  ? 0.7360 0.5796 0.6014 0.0571  -0.0474 -0.0002 42  VAL   A O    
317  C  CB   . VAL   A 42  ? 0.6936 0.5576 0.5795 0.0382  -0.0434 -0.0005 42  VAL   A CB   
318  C  CG1  . VAL   A 42  ? 0.6432 0.4976 0.5225 0.0298  -0.0508 -0.0011 42  VAL   A CG1  
319  C  CG2  . VAL   A 42  ? 0.6859 0.5374 0.5563 0.0467  -0.0430 0.0007  42  VAL   A CG2  
320  N  N    . ILE   A 43  ? 0.7188 0.5720 0.5993 0.0419  -0.0532 -0.0024 43  ILE   A N    
321  C  CA   . ILE   A 43  ? 0.7748 0.6117 0.6409 0.0453  -0.0601 -0.0028 43  ILE   A CA   
322  C  C    . ILE   A 43  ? 0.8137 0.6521 0.6811 0.0537  -0.0582 -0.0030 43  ILE   A C    
323  O  O    . ILE   A 43  ? 0.9316 0.7548 0.7844 0.0593  -0.0629 -0.0031 43  ILE   A O    
324  C  CB   . ILE   A 43  ? 0.7928 0.6283 0.6613 0.0351  -0.0673 -0.0040 43  ILE   A CB   
325  C  CG1  . ILE   A 43  ? 0.7897 0.6429 0.6775 0.0310  -0.0660 -0.0055 43  ILE   A CG1  
326  C  CG2  . ILE   A 43  ? 0.8315 0.6674 0.7004 0.0258  -0.0681 -0.0035 43  ILE   A CG2  
327  C  CD1  . ILE   A 43  ? 0.7743 0.6306 0.6681 0.0198  -0.0721 -0.0066 43  ILE   A CD1  
328  N  N    . CYS   A 44  ? 0.8418 0.6968 0.7247 0.0550  -0.0515 -0.0030 44  CYS   A N    
329  C  CA   . CYS   A 44  ? 0.8795 0.7365 0.7646 0.0616  -0.0499 -0.0033 44  CYS   A CA   
330  C  C    . CYS   A 44  ? 0.9179 0.7685 0.7931 0.0725  -0.0452 -0.0015 44  CYS   A C    
331  O  O    . CYS   A 44  ? 0.8469 0.7020 0.7235 0.0748  -0.0397 0.0000  44  CYS   A O    
332  C  CB   . CYS   A 44  ? 0.8478 0.7244 0.7531 0.0580  -0.0452 -0.0041 44  CYS   A CB   
333  S  SG   . CYS   A 44  ? 0.9112 0.7977 0.8296 0.0466  -0.0499 -0.0063 44  CYS   A SG   
334  N  N    . THR   A 45  ? 1.0279 0.8686 0.8935 0.0794  -0.0472 -0.0015 45  THR   A N    
335  C  CA   . THR   A 45  ? 1.1410 0.9796 1.0008 0.0896  -0.0413 0.0003  45  THR   A CA   
336  C  C    . THR   A 45  ? 1.2189 1.0742 1.0954 0.0892  -0.0347 0.0006  45  THR   A C    
337  O  O    . THR   A 45  ? 1.1740 1.0410 1.0650 0.0821  -0.0353 -0.0008 45  THR   A O    
338  C  CB   . THR   A 45  ? 1.1997 1.0205 1.0416 0.0974  -0.0456 0.0003  45  THR   A CB   
339  O  OG1  . THR   A 45  ? 1.2272 1.0507 1.0748 0.0968  -0.0474 -0.0010 45  THR   A OG1  
340  C  CG2  . THR   A 45  ? 1.1782 0.9820 1.0048 0.0954  -0.0543 -0.0007 45  THR   A CG2  
341  N  N    . SER   A 46  ? 1.4562 1.3124 1.3302 0.0971  -0.0285 0.0026  46  SER   A N    
342  C  CA   . SER   A 46  ? 1.4108 1.2812 1.2991 0.0968  -0.0222 0.0032  46  SER   A CA   
343  C  C    . SER   A 46  ? 1.3241 1.1938 1.2151 0.0962  -0.0254 0.0016  46  SER   A C    
344  O  O    . SER   A 46  ? 1.3402 1.2224 1.2456 0.0918  -0.0235 0.0007  46  SER   A O    
345  C  CB   . SER   A 46  ? 1.3738 1.2446 1.2580 0.1050  -0.0150 0.0061  46  SER   A CB   
346  O  OG   . SER   A 46  ? 1.3932 1.2478 1.2589 0.1133  -0.0169 0.0069  46  SER   A OG   
347  N  N    . GLU   A 47  ? 1.2363 1.0908 1.1128 0.1008  -0.0307 0.0010  47  GLU   A N    
348  C  CA   . GLU   A 47  ? 1.2158 1.0687 1.0937 0.1012  -0.0340 -0.0006 47  GLU   A CA   
349  C  C    . GLU   A 47  ? 1.1629 1.0219 1.0510 0.0925  -0.0404 -0.0036 47  GLU   A C    
350  O  O    . GLU   A 47  ? 1.0796 0.9444 0.9758 0.0911  -0.0418 -0.0052 47  GLU   A O    
351  N  N    . ASP   A 48  ? 1.1569 1.0148 1.0446 0.0867  -0.0443 -0.0042 48  ASP   A N    
352  C  CA   . ASP   A 48  ? 1.1930 1.0575 1.0906 0.0778  -0.0501 -0.0066 48  ASP   A CA   
353  C  C    . ASP   A 48  ? 1.1807 1.0651 1.0983 0.0719  -0.0454 -0.0073 48  ASP   A C    
354  O  O    . ASP   A 48  ? 1.1723 1.0651 1.1005 0.0661  -0.0490 -0.0095 48  ASP   A O    
355  C  CB   . ASP   A 48  ? 1.1566 1.0140 1.0477 0.0725  -0.0551 -0.0067 48  ASP   A CB   
356  C  CG   . ASP   A 48  ? 1.2244 1.0605 1.0941 0.0782  -0.0605 -0.0063 48  ASP   A CG   
357  O  OD1  . ASP   A 48  ? 1.2850 1.1119 1.1457 0.0854  -0.0619 -0.0064 48  ASP   A OD1  
358  O  OD2  . ASP   A 48  ? 1.2021 1.0296 1.0631 0.0755  -0.0637 -0.0058 48  ASP   A OD2  
359  N  N    . MET   A 49  ? 1.1427 1.0349 1.0656 0.0732  -0.0377 -0.0055 49  MET   A N    
360  C  CA   . MET   A 49  ? 1.1227 1.0321 1.0628 0.0668  -0.0340 -0.0061 49  MET   A CA   
361  C  C    . MET   A 49  ? 1.0869 1.0062 1.0383 0.0669  -0.0328 -0.0076 49  MET   A C    
362  O  O    . MET   A 49  ? 0.9486 0.8817 0.9134 0.0630  -0.0289 -0.0080 49  MET   A O    
363  C  CB   . MET   A 49  ? 1.0427 0.9566 0.9845 0.0681  -0.0269 -0.0038 49  MET   A CB   
364  C  CG   . MET   A 49  ? 1.0218 0.9301 0.9566 0.0655  -0.0284 -0.0030 49  MET   A CG   
365  S  SD   . MET   A 49  ? 1.0350 0.9448 0.9675 0.0696  -0.0213 -0.0003 49  MET   A SD   
366  C  CE   . MET   A 49  ? 0.8041 0.7120 0.7345 0.0627  -0.0243 -0.0007 49  MET   A CE   
367  N  N    . LEU   A 50  ? 1.1410 1.0535 1.0871 0.0713  -0.0363 -0.0086 50  LEU   A N    
368  C  CA   . LEU   A 50  ? 1.1448 1.0660 1.1008 0.0718  -0.0355 -0.0102 50  LEU   A CA   
369  C  C    . LEU   A 50  ? 1.0773 1.0084 1.0447 0.0649  -0.0405 -0.0131 50  LEU   A C    
370  O  O    . LEU   A 50  ? 0.9837 0.9290 0.9645 0.0602  -0.0376 -0.0139 50  LEU   A O    
371  C  CB   . LEU   A 50  ? 1.1451 1.0546 1.0903 0.0796  -0.0374 -0.0102 50  LEU   A CB   
372  C  CG   . LEU   A 50  ? 1.2809 1.1953 1.2315 0.0829  -0.0344 -0.0107 50  LEU   A CG   
373  C  CD1  . LEU   A 50  ? 1.2961 1.1959 1.2319 0.0914  -0.0336 -0.0091 50  LEU   A CD1  
374  C  CD2  . LEU   A 50  ? 1.0780 1.0026 1.0407 0.0796  -0.0384 -0.0140 50  LEU   A CD2  
375  N  N    . ASN   A 51  ? 1.0582 0.9819 1.0200 0.0641  -0.0482 -0.0147 51  ASN   A N    
376  C  CA   . ASN   A 51  ? 0.9820 0.9122 0.9512 0.0562  -0.0538 -0.0166 51  ASN   A CA   
377  C  C    . ASN   A 51  ? 0.9925 0.9089 0.9487 0.0545  -0.0586 -0.0156 51  ASN   A C    
378  O  O    . ASN   A 51  ? 1.0497 0.9508 0.9919 0.0599  -0.0628 -0.0154 51  ASN   A O    
379  C  CB   . ASN   A 51  ? 1.0906 1.0253 1.0661 0.0562  -0.0598 -0.0196 51  ASN   A CB   
380  C  CG   . ASN   A 51  ? 1.0558 1.0067 1.0471 0.0476  -0.0620 -0.0215 51  ASN   A CG   
381  O  OD1  . ASN   A 51  ? 1.0082 0.9625 1.0021 0.0407  -0.0614 -0.0207 51  ASN   A OD1  
382  N  ND2  . ASN   A 51  ? 1.1411 1.1018 1.1425 0.0482  -0.0645 -0.0242 51  ASN   A ND2  
383  N  N    . PRO   A 52  ? 0.9504 0.8703 0.9093 0.0475  -0.0583 -0.0149 52  PRO   A N    
384  C  CA   . PRO   A 52  ? 0.8456 0.7516 0.7918 0.0449  -0.0643 -0.0143 52  PRO   A CA   
385  C  C    . PRO   A 52  ? 0.7472 0.6598 0.7016 0.0354  -0.0705 -0.0160 52  PRO   A C    
386  O  O    . PRO   A 52  ? 0.7866 0.7152 0.7557 0.0289  -0.0675 -0.0165 52  PRO   A O    
387  C  CB   . PRO   A 52  ? 0.8333 0.7369 0.7748 0.0442  -0.0590 -0.0119 52  PRO   A CB   
388  C  CG   . PRO   A 52  ? 0.8892 0.8087 0.8444 0.0446  -0.0504 -0.0115 52  PRO   A CG   
389  C  CD   . PRO   A 52  ? 0.9104 0.8423 0.8790 0.0435  -0.0514 -0.0138 52  PRO   A CD   
390  N  N    . ASN   A 53  ? 0.7408 0.6414 0.6858 0.0344  -0.0791 -0.0167 53  ASN   A N    
391  C  CA   . ASN   A 53  ? 0.7312 0.6358 0.6817 0.0241  -0.0851 -0.0175 53  ASN   A CA   
392  C  C    . ASN   A 53  ? 0.7650 0.6598 0.7051 0.0198  -0.0847 -0.0153 53  ASN   A C    
393  O  O    . ASN   A 53  ? 0.7922 0.6678 0.7148 0.0218  -0.0898 -0.0145 53  ASN   A O    
394  C  CB   . ASN   A 53  ? 0.6804 0.5766 0.6260 0.0240  -0.0951 -0.0193 53  ASN   A CB   
395  C  CG   . ASN   A 53  ? 0.7245 0.6345 0.6848 0.0134  -0.1001 -0.0208 53  ASN   A CG   
396  O  OD1  . ASN   A 53  ? 0.8378 0.7525 0.8020 0.0045  -0.0993 -0.0197 53  ASN   A OD1  
397  N  ND2  . ASN   A 53  ? 0.6051 0.5225 0.5741 0.0144  -0.1049 -0.0233 53  ASN   A ND2  
398  N  N    . TYR   A 54  ? 0.7545 0.6617 0.7046 0.0144  -0.0785 -0.0145 54  TYR   A N    
399  C  CA   . TYR   A 54  ? 0.7705 0.6690 0.7108 0.0115  -0.0768 -0.0124 54  TYR   A CA   
400  C  C    . TYR   A 54  ? 0.8210 0.7070 0.7514 0.0043  -0.0853 -0.0121 54  TYR   A C    
401  O  O    . TYR   A 54  ? 0.8147 0.6820 0.7270 0.0066  -0.0879 -0.0108 54  TYR   A O    
402  C  CB   . TYR   A 54  ? 0.6874 0.6025 0.6415 0.0060  -0.0696 -0.0119 54  TYR   A CB   
403  C  CG   . TYR   A 54  ? 0.6276 0.5500 0.5865 0.0131  -0.0611 -0.0114 54  TYR   A CG   
404  C  CD1  . TYR   A 54  ? 0.6252 0.5377 0.5727 0.0185  -0.0574 -0.0095 54  TYR   A CD1  
405  C  CD2  . TYR   A 54  ? 0.5638 0.5024 0.5380 0.0146  -0.0572 -0.0128 54  TYR   A CD2  
406  C  CE1  . TYR   A 54  ? 0.5470 0.4664 0.4994 0.0243  -0.0500 -0.0089 54  TYR   A CE1  
407  C  CE2  . TYR   A 54  ? 0.5560 0.5001 0.5339 0.0204  -0.0499 -0.0122 54  TYR   A CE2  
408  C  CZ   . TYR   A 54  ? 0.5870 0.5217 0.5543 0.0249  -0.0464 -0.0102 54  TYR   A CZ   
409  O  OH   . TYR   A 54  ? 0.6227 0.5633 0.5942 0.0301  -0.0395 -0.0094 54  TYR   A OH   
410  N  N    . GLU   A 55  ? 1.0060 0.9021 0.9479 -0.0046 -0.0897 -0.0133 55  GLU   A N    
411  C  CA   . GLU   A 55  ? 1.0011 0.8863 0.9348 -0.0131 -0.0980 -0.0128 55  GLU   A CA   
412  C  C    . GLU   A 55  ? 1.0472 0.9099 0.9617 -0.0070 -0.1060 -0.0131 55  GLU   A C    
413  O  O    . GLU   A 55  ? 1.1470 0.9914 1.0448 -0.0095 -0.1112 -0.0119 55  GLU   A O    
414  C  CB   . GLU   A 55  ? 1.0189 0.9214 0.9705 -0.0233 -0.1012 -0.0141 55  GLU   A CB   
415  C  CG   . GLU   A 55  ? 1.1220 1.0256 1.0774 -0.0210 -0.1085 -0.0163 55  GLU   A CG   
416  C  CD   . GLU   A 55  ? 1.2319 1.1535 1.2054 -0.0316 -0.1122 -0.0175 55  GLU   A CD   
417  O  OE1  . GLU   A 55  ? 1.2377 1.1705 1.2202 -0.0410 -0.1087 -0.0164 55  GLU   A OE1  
418  O  OE2  . GLU   A 55  ? 1.2081 1.1325 1.1866 -0.0303 -0.1186 -0.0196 55  GLU   A OE2  
419  N  N    . ASP   A 56  ? 0.8892 0.7515 0.8040 0.0016  -0.1070 -0.0146 56  ASP   A N    
420  C  CA   . ASP   A 56  ? 0.8315 0.6717 0.7269 0.0087  -0.1141 -0.0148 56  ASP   A CA   
421  C  C    . ASP   A 56  ? 0.8461 0.6695 0.7227 0.0172  -0.1103 -0.0130 56  ASP   A C    
422  O  O    . ASP   A 56  ? 0.9382 0.7399 0.7947 0.0200  -0.1166 -0.0124 56  ASP   A O    
423  C  CB   . ASP   A 56  ? 0.8459 0.6903 0.7462 0.0161  -0.1153 -0.0168 56  ASP   A CB   
424  C  CG   . ASP   A 56  ? 0.7775 0.6301 0.6890 0.0092  -0.1233 -0.0190 56  ASP   A CG   
425  O  OD1  . ASP   A 56  ? 0.7747 0.6284 0.6889 -0.0015 -0.1282 -0.0186 56  ASP   A OD1  
426  O  OD2  . ASP   A 56  ? 0.7552 0.6128 0.6725 0.0144  -0.1249 -0.0209 56  ASP   A OD2  
427  N  N    . LEU   A 57  ? 0.8240 0.6574 0.7069 0.0216  -0.1005 -0.0120 57  LEU   A N    
428  C  CA   . LEU   A 57  ? 0.8799 0.7007 0.7476 0.0290  -0.0961 -0.0102 57  LEU   A CA   
429  C  C    . LEU   A 57  ? 0.9052 0.7163 0.7631 0.0227  -0.0983 -0.0088 57  LEU   A C    
430  O  O    . LEU   A 57  ? 0.8983 0.6919 0.7376 0.0288  -0.0990 -0.0076 57  LEU   A O    
431  C  CB   . LEU   A 57  ? 0.8307 0.6668 0.7100 0.0339  -0.0854 -0.0095 57  LEU   A CB   
432  C  CG   . LEU   A 57  ? 0.8326 0.6722 0.7149 0.0429  -0.0826 -0.0102 57  LEU   A CG   
433  C  CD1  . LEU   A 57  ? 0.8512 0.7088 0.7487 0.0445  -0.0728 -0.0097 57  LEU   A CD1  
434  C  CD2  . LEU   A 57  ? 0.8388 0.6578 0.6993 0.0534  -0.0834 -0.0090 57  LEU   A CD2  
435  N  N    . LEU   A 58  ? 0.8913 0.7133 0.7610 0.0109  -0.0992 -0.0089 58  LEU   A N    
436  C  CA   . LEU   A 58  ? 0.8789 0.6912 0.7388 0.0044  -0.1010 -0.0074 58  LEU   A CA   
437  C  C    . LEU   A 58  ? 0.9122 0.7025 0.7539 0.0014  -0.1119 -0.0074 58  LEU   A C    
438  O  O    . LEU   A 58  ? 0.9589 0.7318 0.7831 0.0013  -0.1143 -0.0061 58  LEU   A O    
439  C  CB   . LEU   A 58  ? 0.8889 0.7198 0.7667 -0.0072 -0.0976 -0.0072 58  LEU   A CB   
440  C  CG   . LEU   A 58  ? 0.9103 0.7337 0.7802 -0.0155 -0.0984 -0.0056 58  LEU   A CG   
441  C  CD1  . LEU   A 58  ? 0.8946 0.7005 0.7450 -0.0077 -0.0967 -0.0043 58  LEU   A CD1  
442  C  CD2  . LEU   A 58  ? 0.7997 0.6450 0.6890 -0.0230 -0.0914 -0.0054 58  LEU   A CD2  
443  N  N    . ILE   A 59  ? 0.8908 0.6804 0.7352 -0.0006 -0.1190 -0.0089 59  ILE   A N    
444  C  CA   . ILE   A 59  ? 0.8836 0.6505 0.7093 -0.0025 -0.1301 -0.0090 59  ILE   A CA   
445  C  C    . ILE   A 59  ? 0.9685 0.7120 0.7697 0.0101  -0.1312 -0.0084 59  ILE   A C    
446  O  O    . ILE   A 59  ? 1.0232 0.7446 0.8039 0.0093  -0.1377 -0.0076 59  ILE   A O    
447  C  CB   . ILE   A 59  ? 0.8252 0.5969 0.6594 -0.0056 -0.1374 -0.0109 59  ILE   A CB   
448  C  CG1  . ILE   A 59  ? 0.7763 0.5703 0.6334 -0.0190 -0.1372 -0.0112 59  ILE   A CG1  
449  C  CG2  . ILE   A 59  ? 0.7941 0.5390 0.6059 -0.0046 -0.1495 -0.0112 59  ILE   A CG2  
450  C  CD1  . ILE   A 59  ? 0.7685 0.5733 0.6390 -0.0212 -0.1426 -0.0134 59  ILE   A CD1  
451  N  N    . ARG   A 60  ? 1.0656 0.8132 0.8680 0.0219  -0.1248 -0.0087 60  ARG   A N    
452  C  CA   . ARG   A 60  ? 1.0611 0.7889 0.8415 0.0347  -0.1245 -0.0080 60  ARG   A CA   
453  C  C    . ARG   A 60  ? 1.1075 0.8249 0.8750 0.0352  -0.1223 -0.0064 60  ARG   A C    
454  O  O    . ARG   A 60  ? 1.1470 0.8412 0.8910 0.0412  -0.1271 -0.0059 60  ARG   A O    
455  C  CB   . ARG   A 60  ? 1.1224 0.8609 0.9099 0.0458  -0.1157 -0.0081 60  ARG   A CB   
456  C  CG   . ARG   A 60  ? 1.1342 0.8814 0.9324 0.0479  -0.1171 -0.0098 60  ARG   A CG   
457  C  CD   . ARG   A 60  ? 1.2237 0.9492 1.0028 0.0537  -0.1262 -0.0107 60  ARG   A CD   
458  N  NE   . ARG   A 60  ? 1.2627 0.9672 1.0180 0.0643  -0.1257 -0.0094 60  ARG   A NE   
459  C  CZ   . ARG   A 60  ? 1.2652 0.9452 0.9977 0.0692  -0.1342 -0.0098 60  ARG   A CZ   
460  N  NH1  . ARG   A 60  ? 1.2708 0.9331 0.9821 0.0795  -0.1328 -0.0087 60  ARG   A NH1  
461  N  NH2  . ARG   A 60  ? 1.2640 0.9372 0.9949 0.0639  -0.1444 -0.0115 60  ARG   A NH2  
462  N  N    . LYS   A 61  ? 1.0639 0.7977 0.8457 0.0292  -0.1156 -0.0056 61  LYS   A N    
463  C  CA   . LYS   A 61  ? 1.0992 0.8264 0.8715 0.0299  -0.1124 -0.0042 61  LYS   A CA   
464  C  C    . LYS   A 61  ? 1.1155 0.8336 0.8817 0.0176  -0.1190 -0.0036 61  LYS   A C    
465  O  O    . LYS   A 61  ? 1.0827 0.8087 0.8602 0.0062  -0.1230 -0.0041 61  LYS   A O    
466  C  CB   . LYS   A 61  ? 1.0513 0.8007 0.8420 0.0307  -0.1013 -0.0036 61  LYS   A CB   
467  C  CG   . LYS   A 61  ? 0.9816 0.7438 0.7827 0.0400  -0.0944 -0.0040 61  LYS   A CG   
468  C  CD   . LYS   A 61  ? 1.0018 0.7523 0.7872 0.0536  -0.0912 -0.0030 61  LYS   A CD   
469  C  CE   . LYS   A 61  ? 0.9545 0.7197 0.7520 0.0613  -0.0832 -0.0030 61  LYS   A CE   
470  N  NZ   . LYS   A 61  ? 0.9511 0.7231 0.7587 0.0588  -0.0859 -0.0044 61  LYS   A NZ   
471  N  N    . SER   A 62  ? 1.2857 0.9878 1.0341 0.0200  -0.1197 -0.0025 62  SER   A N    
472  C  CA   . SER   A 62  ? 1.2576 0.9477 0.9963 0.0092  -0.1255 -0.0017 62  SER   A CA   
473  C  C    . SER   A 62  ? 1.2305 0.9224 0.9672 0.0100  -0.1193 -0.0005 62  SER   A C    
474  O  O    . SER   A 62  ? 1.2349 0.9399 0.9806 0.0175  -0.1105 -0.0005 62  SER   A O    
475  C  CB   . SER   A 62  ? 1.2273 0.8873 0.9388 0.0115  -0.1365 -0.0017 62  SER   A CB   
476  O  OG   . SER   A 62  ? 1.2078 0.8652 0.9203 0.0121  -0.1424 -0.0030 62  SER   A OG   
477  N  N    . ASN   A 63  ? 1.1379 0.8154 0.8618 0.0018  -0.1243 0.0004  63  ASN   A N    
478  C  CA   . ASN   A 63  ? 1.0877 0.7665 0.8096 0.0009  -0.1192 0.0014  63  ASN   A CA   
479  C  C    . ASN   A 63  ? 1.0829 0.7537 0.7920 0.0161  -0.1153 0.0014  63  ASN   A C    
480  O  O    . ASN   A 63  ? 1.0121 0.6943 0.7289 0.0188  -0.1078 0.0017  63  ASN   A O    
481  C  CB   . ASN   A 63  ? 1.0490 0.7091 0.7550 -0.0097 -0.1264 0.0025  63  ASN   A CB   
482  C  CG   . ASN   A 63  ? 1.0592 0.7356 0.7828 -0.0253 -0.1241 0.0034  63  ASN   A CG   
483  O  OD1  . ASN   A 63  ? 1.0603 0.7623 0.8078 -0.0273 -0.1164 0.0030  63  ASN   A OD1  
484  N  ND2  . ASN   A 63  ? 0.9978 0.6587 0.7088 -0.0362 -0.1306 0.0046  63  ASN   A ND2  
485  N  N    . HIS   A 64  ? 1.1357 0.7867 0.8248 0.0262  -0.1204 0.0009  64  HIS   A N    
486  C  CA   . HIS   A 64  ? 1.1473 0.7900 0.8228 0.0411  -0.1170 0.0010  64  HIS   A CA   
487  C  C    . HIS   A 64  ? 1.0550 0.7179 0.7469 0.0508  -0.1079 0.0007  64  HIS   A C    
488  O  O    . HIS   A 64  ? 1.0391 0.7029 0.7268 0.0618  -0.1027 0.0009  64  HIS   A O    
489  C  CB   . HIS   A 64  ? 1.1572 0.7702 0.8035 0.0491  -0.1257 0.0006  64  HIS   A CB   
490  C  CG   . HIS   A 64  ? 1.1377 0.7457 0.7826 0.0496  -0.1312 -0.0001 64  HIS   A CG   
491  N  ND1  . HIS   A 64  ? 1.1848 0.7915 0.8345 0.0365  -0.1381 -0.0003 64  HIS   A ND1  
492  C  CD2  . HIS   A 64  ? 1.1424 0.7461 0.7811 0.0617  -0.1308 -0.0008 64  HIS   A CD2  
493  C  CE1  . HIS   A 64  ? 1.1998 0.8015 0.8465 0.0407  -0.1422 -0.0012 64  HIS   A CE1  
494  N  NE2  . HIS   A 64  ? 1.1995 0.7985 0.8388 0.0560  -0.1379 -0.0015 64  HIS   A NE2  
495  N  N    . ASN   A 65  ? 1.0538 0.7330 0.7644 0.0469  -0.1061 0.0002  65  ASN   A N    
496  C  CA   . ASN   A 65  ? 1.0118 0.7087 0.7371 0.0554  -0.0981 0.0000  65  ASN   A CA   
497  C  C    . ASN   A 65  ? 1.0494 0.7680 0.7931 0.0549  -0.0885 0.0005  65  ASN   A C    
498  O  O    . ASN   A 65  ? 1.0121 0.7432 0.7650 0.0632  -0.0814 0.0007  65  ASN   A O    
499  C  CB   . ASN   A 65  ? 0.9998 0.7073 0.7395 0.0505  -0.0995 -0.0009 65  ASN   A CB   
500  C  CG   . ASN   A 65  ? 1.0773 0.7649 0.7997 0.0544  -0.1080 -0.0016 65  ASN   A CG   
501  O  OD1  . ASN   A 65  ? 1.1556 0.8269 0.8656 0.0476  -0.1170 -0.0018 65  ASN   A OD1  
502  N  ND2  . ASN   A 65  ? 0.9833 0.6715 0.7044 0.0652  -0.1054 -0.0018 65  ASN   A ND2  
503  N  N    . PHE   A 66  ? 1.0088 0.7317 0.7577 0.0452  -0.0881 0.0008  66  PHE   A N    
504  C  CA   . PHE   A 66  ? 0.9705 0.7130 0.7364 0.0437  -0.0798 0.0012  66  PHE   A CA   
505  C  C    . PHE   A 66  ? 1.0401 0.7723 0.7921 0.0486  -0.0792 0.0018  66  PHE   A C    
506  O  O    . PHE   A 66  ? 1.1099 0.8244 0.8456 0.0442  -0.0853 0.0020  66  PHE   A O    
507  C  CB   . PHE   A 66  ? 0.9903 0.7468 0.7731 0.0295  -0.0791 0.0011  66  PHE   A CB   
508  C  CG   . PHE   A 66  ? 0.9537 0.7197 0.7495 0.0238  -0.0810 0.0003  66  PHE   A CG   
509  C  CD1  . PHE   A 66  ? 0.8991 0.6841 0.7131 0.0273  -0.0751 -0.0002 66  PHE   A CD1  
510  C  CD2  . PHE   A 66  ? 0.9821 0.7382 0.7721 0.0145  -0.0889 0.0001  66  PHE   A CD2  
511  C  CE1  . PHE   A 66  ? 0.9399 0.7334 0.7655 0.0225  -0.0772 -0.0012 66  PHE   A CE1  
512  C  CE2  . PHE   A 66  ? 1.0199 0.7858 0.8227 0.0094  -0.0911 -0.0008 66  PHE   A CE2  
513  C  CZ   . PHE   A 66  ? 1.0151 0.7997 0.8355 0.0138  -0.0852 -0.0016 66  PHE   A CZ   
514  N  N    . LEU   A 67  ? 1.0275 0.7708 0.7862 0.0572  -0.0720 0.0021  67  LEU   A N    
515  C  CA   . LEU   A 67  ? 1.0363 0.7707 0.7820 0.0644  -0.0713 0.0025  67  LEU   A CA   
516  C  C    . LEU   A 67  ? 1.0381 0.7909 0.8002 0.0620  -0.0644 0.0027  67  LEU   A C    
517  O  O    . LEU   A 67  ? 0.8817 0.6511 0.6578 0.0679  -0.0576 0.0029  67  LEU   A O    
518  C  CB   . LEU   A 67  ? 1.0650 0.7929 0.7998 0.0793  -0.0701 0.0026  67  LEU   A CB   
519  C  CG   . LEU   A 67  ? 1.1961 0.8974 0.9048 0.0838  -0.0784 0.0023  67  LEU   A CG   
520  C  CD1  . LEU   A 67  ? 1.2118 0.9113 0.9133 0.0989  -0.0752 0.0026  67  LEU   A CD1  
521  C  CD2  . LEU   A 67  ? 1.2594 0.9420 0.9494 0.0811  -0.0840 0.0022  67  LEU   A CD2  
522  N  N    . VAL   A 68  ? 1.1593 0.9077 0.9183 0.0535  -0.0664 0.0027  68  VAL   A N    
523  C  CA   . VAL   A 68  ? 1.0705 0.8338 0.8429 0.0502  -0.0609 0.0028  68  VAL   A CA   
524  C  C    . VAL   A 68  ? 1.1172 0.8727 0.8772 0.0601  -0.0604 0.0029  68  VAL   A C    
525  O  O    . VAL   A 68  ? 1.1457 0.8811 0.8853 0.0606  -0.0660 0.0028  68  VAL   A O    
526  C  CB   . VAL   A 68  ? 1.1246 0.8871 0.8994 0.0362  -0.0630 0.0030  68  VAL   A CB   
527  C  CG1  . VAL   A 68  ? 1.0353 0.8157 0.8265 0.0327  -0.0565 0.0030  68  VAL   A CG1  
528  C  CG2  . VAL   A 68  ? 1.0660 0.8317 0.8482 0.0273  -0.0656 0.0028  68  VAL   A CG2  
529  N  N    . GLN   A 69  ? 1.0575 0.8289 0.8300 0.0676  -0.0539 0.0030  69  GLN   A N    
530  C  CA   . GLN   A 69  ? 1.1077 0.8744 0.8704 0.0788  -0.0531 0.0030  69  GLN   A CA   
531  C  C    . GLN   A 69  ? 1.1567 0.9215 0.9168 0.0751  -0.0535 0.0027  69  GLN   A C    
532  O  O    . GLN   A 69  ? 1.2430 0.9910 0.9840 0.0803  -0.0577 0.0024  69  GLN   A O    
533  C  CB   . GLN   A 69  ? 1.1798 0.9654 0.9579 0.0875  -0.0461 0.0035  69  GLN   A CB   
534  C  CG   . GLN   A 69  ? 1.1501 0.9351 0.9216 0.1001  -0.0443 0.0036  69  GLN   A CG   
535  C  CD   . GLN   A 69  ? 1.1812 0.9460 0.9294 0.1101  -0.0491 0.0035  69  GLN   A CD   
536  O  OE1  . GLN   A 69  ? 1.2197 0.9702 0.9511 0.1145  -0.0530 0.0029  69  GLN   A OE1  
537  N  NE2  . GLN   A 69  ? 1.2702 1.0323 1.0158 0.1141  -0.0490 0.0039  69  GLN   A NE2  
538  N  N    . ALA   A 70  ? 1.0315 0.8123 0.8094 0.0667  -0.0495 0.0027  70  ALA   A N    
539  C  CA   . ALA   A 70  ? 1.1083 0.8899 0.8859 0.0642  -0.0488 0.0024  70  ALA   A CA   
540  C  C    . ALA   A 70  ? 1.1419 0.9268 0.9176 0.0770  -0.0468 0.0022  70  ALA   A C    
541  O  O    . ALA   A 70  ? 1.2362 1.0325 1.0210 0.0848  -0.0430 0.0026  70  ALA   A O    
542  C  CB   . ALA   A 70  ? 1.0644 0.8250 0.8228 0.0571  -0.0551 0.0023  70  ALA   A CB   
543  N  N    . GLY   A 71  ? 0.9518 0.7272 0.7160 0.0793  -0.0493 0.0017  71  GLY   A N    
544  C  CA   . GLY   A 71  ? 0.9873 0.7643 0.7477 0.0923  -0.0484 0.0013  71  GLY   A CA   
545  C  C    . GLY   A 71  ? 1.1643 0.9275 0.9078 0.1029  -0.0515 0.0014  71  GLY   A C    
546  O  O    . GLY   A 71  ? 1.1361 0.9094 0.8860 0.1127  -0.0479 0.0018  71  GLY   A O    
547  N  N    . ASN   A 72  ? 1.1666 0.9060 0.8878 0.1009  -0.0583 0.0011  72  ASN   A N    
548  C  CA   . ASN   A 72  ? 1.1799 0.9028 0.8827 0.1095  -0.0623 0.0010  72  ASN   A CA   
549  C  C    . ASN   A 72  ? 1.2319 0.9389 0.9243 0.0995  -0.0677 0.0013  72  ASN   A C    
550  O  O    . ASN   A 72  ? 1.2349 0.9313 0.9200 0.0894  -0.0715 0.0012  72  ASN   A O    
551  C  CB   . ASN   A 72  ? 1.2354 0.9412 0.9161 0.1206  -0.0667 0.0001  72  ASN   A CB   
552  C  CG   . ASN   A 72  ? 1.2296 0.9521 0.9209 0.1319  -0.0617 -0.0001 72  ASN   A CG   
553  O  OD1  . ASN   A 72  ? 1.1753 0.9173 0.8839 0.1364  -0.0556 0.0006  72  ASN   A OD1  
554  N  ND2  . ASN   A 72  ? 1.2563 0.9712 0.9371 0.1363  -0.0645 -0.0011 72  ASN   A ND2  
555  N  N    . VAL   A 73  ? 1.2838 0.9900 0.9761 0.1020  -0.0679 0.0016  73  VAL   A N    
556  C  CA   . VAL   A 73  ? 1.3205 1.0123 1.0035 0.0939  -0.0734 0.0018  73  VAL   A CA   
557  C  C    . VAL   A 73  ? 1.3848 1.0485 1.0415 0.0906  -0.0821 0.0015  73  VAL   A C    
558  O  O    . VAL   A 73  ? 1.4409 1.0847 1.0752 0.1000  -0.0872 0.0011  73  VAL   A O    
559  C  CB   . VAL   A 73  ? 1.2933 0.9847 0.9749 0.1017  -0.0731 0.0020  73  VAL   A CB   
560  C  CG1  . VAL   A 73  ? 1.2787 0.9935 0.9856 0.0976  -0.0667 0.0026  73  VAL   A CG1  
561  C  CG2  . VAL   A 73  ? 1.2884 0.9835 0.9668 0.1172  -0.0696 0.0019  73  VAL   A CG2  
562  N  N    . GLN   A 74  ? 1.4423 1.1042 1.1013 0.0770  -0.0838 0.0018  74  GLN   A N    
563  C  CA   . GLN   A 74  ? 1.5126 1.1499 1.1508 0.0685  -0.0920 0.0021  74  GLN   A CA   
564  C  C    . GLN   A 74  ? 1.5230 1.1682 1.1747 0.0517  -0.0918 0.0029  74  GLN   A C    
565  O  O    . GLN   A 74  ? 1.5854 1.2173 1.2267 0.0412  -0.0962 0.0035  74  GLN   A O    
566  C  CB   . GLN   A 74  ? 1.5613 1.1829 1.1820 0.0693  -0.0952 0.0018  74  GLN   A CB   
567  C  CG   . GLN   A 74  ? 1.5313 1.1363 1.1300 0.0849  -0.0985 0.0008  74  GLN   A CG   
568  C  CD   . GLN   A 74  ? 1.5711 1.1545 1.1480 0.0832  -0.1040 0.0005  74  GLN   A CD   
569  O  OE1  . GLN   A 74  ? 1.7204 1.3025 1.2995 0.0701  -0.1046 0.0012  74  GLN   A OE1  
570  N  NE2  . GLN   A 74  ? 1.5583 1.1245 1.1134 0.0967  -0.1080 -0.0005 74  GLN   A NE2  
571  N  N    . LEU   A 75  ? 1.3358 1.0028 1.0107 0.0490  -0.0867 0.0031  75  LEU   A N    
572  C  CA   . LEU   A 75  ? 1.2726 0.9482 0.9609 0.0342  -0.0867 0.0037  75  LEU   A CA   
573  C  C    . LEU   A 75  ? 1.1735 0.8372 0.8534 0.0324  -0.0929 0.0037  75  LEU   A C    
574  O  O    . LEU   A 75  ? 1.1327 0.8023 0.8176 0.0403  -0.0915 0.0033  75  LEU   A O    
575  C  CB   . LEU   A 75  ? 1.2206 0.9260 0.9383 0.0316  -0.0781 0.0036  75  LEU   A CB   
576  C  CG   . LEU   A 75  ? 1.0868 0.8061 0.8173 0.0259  -0.0727 0.0038  75  LEU   A CG   
577  C  CD1  . LEU   A 75  ? 0.9935 0.7050 0.7191 0.0116  -0.0757 0.0046  75  LEU   A CD1  
578  C  CD2  . LEU   A 75  ? 1.0982 0.8148 0.8216 0.0358  -0.0708 0.0033  75  LEU   A CD2  
579  N  N    . ARG   A 76  ? 1.1552 0.8016 0.8216 0.0220  -0.0999 0.0044  76  ARG   A N    
580  C  CA   . ARG   A 76  ? 1.2376 0.8700 0.8939 0.0187  -0.1073 0.0045  76  ARG   A CA   
581  C  C    . ARG   A 76  ? 1.1642 0.8134 0.8414 0.0048  -0.1060 0.0050  76  ARG   A C    
582  O  O    . ARG   A 76  ? 1.1274 0.7782 0.8080 -0.0081 -0.1064 0.0059  76  ARG   A O    
583  C  CB   . ARG   A 76  ? 1.2686 0.8697 0.8955 0.0159  -0.1167 0.0050  76  ARG   A CB   
584  C  CG   . ARG   A 76  ? 1.3329 0.9156 0.9371 0.0298  -0.1185 0.0043  76  ARG   A CG   
585  C  CD   . ARG   A 76  ? 1.3747 0.9353 0.9567 0.0402  -0.1255 0.0036  76  ARG   A CD   
586  N  NE   . ARG   A 76  ? 1.1991 0.7737 0.7942 0.0477  -0.1222 0.0030  76  ARG   A NE   
587  C  CZ   . ARG   A 76  ? 1.2195 0.8092 0.8245 0.0604  -0.1149 0.0024  76  ARG   A CZ   
588  N  NH1  . ARG   A 76  ? 1.2656 0.8659 0.8808 0.0662  -0.1123 0.0021  76  ARG   A NH1  
589  N  NH2  . ARG   A 76  ? 1.2577 0.8521 0.8627 0.0671  -0.1104 0.0023  76  ARG   A NH2  
590  N  N    . VAL   A 77  ? 1.1283 0.7902 0.8192 0.0077  -0.1045 0.0043  77  VAL   A N    
591  C  CA   . VAL   A 77  ? 1.0700 0.7500 0.7821 -0.0038 -0.1031 0.0044  77  VAL   A CA   
592  C  C    . VAL   A 77  ? 1.0967 0.7604 0.7973 -0.0153 -0.1123 0.0051  77  VAL   A C    
593  O  O    . VAL   A 77  ? 1.0520 0.7006 0.7400 -0.0120 -0.1193 0.0047  77  VAL   A O    
594  C  CB   . VAL   A 77  ? 1.0628 0.7597 0.7913 0.0034  -0.0992 0.0034  77  VAL   A CB   
595  C  CG1  . VAL   A 77  ? 0.9758 0.6953 0.7291 -0.0073 -0.0963 0.0033  77  VAL   A CG1  
596  C  CG2  . VAL   A 77  ? 0.9988 0.7068 0.7335 0.0157  -0.0913 0.0030  77  VAL   A CG2  
597  N  N    . ILE   A 78  ? 1.0727 0.7387 0.7771 -0.0289 -0.1124 0.0063  78  ILE   A N    
598  C  CA   . ILE   A 78  ? 1.0539 0.7067 0.7496 -0.0423 -0.1205 0.0074  78  ILE   A CA   
599  C  C    . ILE   A 78  ? 1.0031 0.6754 0.7211 -0.0516 -0.1203 0.0073  78  ILE   A C    
600  O  O    . ILE   A 78  ? 0.9566 0.6193 0.6691 -0.0612 -0.1280 0.0079  78  ILE   A O    
601  C  CB   . ILE   A 78  ? 1.1281 0.7745 0.8170 -0.0529 -0.1200 0.0091  78  ILE   A CB   
602  C  CG1  . ILE   A 78  ? 1.0994 0.7261 0.7658 -0.0432 -0.1206 0.0090  78  ILE   A CG1  
603  C  CG2  . ILE   A 78  ? 1.2041 0.8369 0.8841 -0.0682 -0.1281 0.0107  78  ILE   A CG2  
604  C  CD1  . ILE   A 78  ? 1.1434 0.7598 0.7994 -0.0534 -0.1212 0.0107  78  ILE   A CD1  
605  N  N    . GLY   A 79  ? 1.0746 0.7739 0.8172 -0.0490 -0.1121 0.0064  79  GLY   A N    
606  C  CA   . GLY   A 79  ? 1.0561 0.7752 0.8204 -0.0566 -0.1116 0.0059  79  GLY   A CA   
607  C  C    . GLY   A 79  ? 1.0437 0.7872 0.8295 -0.0485 -0.1031 0.0045  79  GLY   A C    
608  O  O    . GLY   A 79  ? 1.0539 0.8015 0.8403 -0.0396 -0.0968 0.0043  79  GLY   A O    
609  N  N    . HIS   A 80  ? 0.9887 0.7481 0.7920 -0.0518 -0.1034 0.0036  80  HIS   A N    
610  C  CA   . HIS   A 80  ? 0.9242 0.7065 0.7481 -0.0451 -0.0959 0.0023  80  HIS   A CA   
611  C  C    . HIS   A 80  ? 0.9195 0.7221 0.7649 -0.0546 -0.0958 0.0017  80  HIS   A C    
612  O  O    . HIS   A 80  ? 0.8651 0.6627 0.7087 -0.0640 -0.1028 0.0021  80  HIS   A O    
613  C  CB   . HIS   A 80  ? 0.8754 0.6508 0.6925 -0.0311 -0.0970 0.0011  80  HIS   A CB   
614  C  CG   . HIS   A 80  ? 0.9389 0.7077 0.7532 -0.0318 -0.1048 0.0002  80  HIS   A CG   
615  N  ND1  . HIS   A 80  ? 0.9310 0.6748 0.7234 -0.0325 -0.1142 0.0006  80  HIS   A ND1  
616  C  CD2  . HIS   A 80  ? 0.9704 0.7533 0.8001 -0.0316 -0.1051 -0.0011 80  HIS   A CD2  
617  C  CE1  . HIS   A 80  ? 1.0002 0.7433 0.7952 -0.0329 -0.1201 -0.0004 80  HIS   A CE1  
618  N  NE2  . HIS   A 80  ? 1.0496 0.8164 0.8671 -0.0322 -0.1147 -0.0015 80  HIS   A NE2  
619  N  N    . SER   A 81  ? 0.8524 0.6780 0.7182 -0.0517 -0.0880 0.0007  81  SER   A N    
620  C  CA   . SER   A 81  ? 0.7982 0.6465 0.6864 -0.0595 -0.0860 0.0000  81  SER   A CA   
621  C  C    . SER   A 81  ? 0.8064 0.6741 0.7112 -0.0512 -0.0780 -0.0014 81  SER   A C    
622  O  O    . SER   A 81  ? 0.8358 0.7022 0.7370 -0.0435 -0.0726 -0.0012 81  SER   A O    
623  C  CB   . SER   A 81  ? 0.8300 0.6851 0.7235 -0.0727 -0.0840 0.0016  81  SER   A CB   
624  O  OG   . SER   A 81  ? 0.7785 0.6591 0.6954 -0.0787 -0.0794 0.0009  81  SER   A OG   
625  N  N    . MET   A 82  ? 0.7242 0.6095 0.6468 -0.0528 -0.0776 -0.0028 82  MET   A N    
626  C  CA   . MET   A 82  ? 0.6991 0.6027 0.6376 -0.0458 -0.0705 -0.0042 82  MET   A CA   
627  C  C    . MET   A 82  ? 0.6902 0.6169 0.6491 -0.0540 -0.0659 -0.0046 82  MET   A C    
628  O  O    . MET   A 82  ? 0.6979 0.6355 0.6684 -0.0591 -0.0690 -0.0056 82  MET   A O    
629  C  CB   . MET   A 82  ? 0.7027 0.6056 0.6425 -0.0374 -0.0737 -0.0059 82  MET   A CB   
630  C  CG   . MET   A 82  ? 0.6650 0.5840 0.6188 -0.0296 -0.0668 -0.0072 82  MET   A CG   
631  S  SD   . MET   A 82  ? 0.6737 0.5976 0.6346 -0.0234 -0.0706 -0.0094 82  MET   A SD   
632  C  CE   . MET   A 82  ? 0.7949 0.6922 0.7330 -0.0196 -0.0799 -0.0089 82  MET   A CE   
633  N  N    . GLN   A 83  ? 0.7001 0.6347 0.6636 -0.0549 -0.0586 -0.0040 83  GLN   A N    
634  C  CA   . GLN   A 83  ? 0.7110 0.6678 0.6933 -0.0608 -0.0531 -0.0045 83  GLN   A CA   
635  C  C    . GLN   A 83  ? 0.6800 0.6501 0.6739 -0.0516 -0.0473 -0.0062 83  GLN   A C    
636  O  O    . GLN   A 83  ? 0.6041 0.5707 0.5935 -0.0451 -0.0428 -0.0058 83  GLN   A O    
637  C  CB   . GLN   A 83  ? 0.6885 0.6448 0.6676 -0.0681 -0.0489 -0.0027 83  GLN   A CB   
638  C  CG   . GLN   A 83  ? 0.7247 0.7023 0.7213 -0.0768 -0.0445 -0.0028 83  GLN   A CG   
639  C  CD   . GLN   A 83  ? 0.7381 0.7164 0.7319 -0.0830 -0.0390 -0.0011 83  GLN   A CD   
640  O  OE1  . GLN   A 83  ? 0.7473 0.7114 0.7273 -0.0798 -0.0379 -0.0001 83  GLN   A OE1  
641  N  NE2  . GLN   A 83  ? 0.5954 0.5904 0.6023 -0.0915 -0.0356 -0.0008 83  GLN   A NE2  
642  N  N    . ASN   A 84  ? 0.7832 0.7673 0.7911 -0.0507 -0.0481 -0.0080 84  ASN   A N    
643  C  CA   . ASN   A 84  ? 0.8111 0.8120 0.8334 -0.0449 -0.0423 -0.0097 84  ASN   A CA   
644  C  C    . ASN   A 84  ? 0.7916 0.7862 0.8079 -0.0347 -0.0383 -0.0096 84  ASN   A C    
645  O  O    . ASN   A 84  ? 0.8067 0.8106 0.8297 -0.0328 -0.0319 -0.0097 84  ASN   A O    
646  C  CB   . ASN   A 84  ? 0.8106 0.8290 0.8459 -0.0515 -0.0365 -0.0097 84  ASN   A CB   
647  C  CG   . ASN   A 84  ? 0.8451 0.8757 0.8913 -0.0607 -0.0394 -0.0101 84  ASN   A CG   
648  O  OD1  . ASN   A 84  ? 0.9455 0.9787 0.9922 -0.0702 -0.0382 -0.0086 84  ASN   A OD1  
649  N  ND2  . ASN   A 84  ? 0.8951 0.9331 0.9499 -0.0580 -0.0432 -0.0120 84  ASN   A ND2  
650  N  N    . CYS   A 85  ? 0.5871 0.5660 0.5906 -0.0280 -0.0421 -0.0092 85  CYS   A N    
651  C  CA   . CYS   A 85  ? 0.5639 0.5362 0.5611 -0.0181 -0.0388 -0.0089 85  CYS   A CA   
652  C  C    . CYS   A 85  ? 0.5837 0.5431 0.5675 -0.0171 -0.0373 -0.0070 85  CYS   A C    
653  O  O    . CYS   A 85  ? 0.4817 0.4386 0.4624 -0.0097 -0.0336 -0.0065 85  CYS   A O    
654  C  CB   . CYS   A 85  ? 0.5453 0.5327 0.5556 -0.0138 -0.0322 -0.0099 85  CYS   A CB   
655  S  SG   . CYS   A 85  ? 0.5608 0.5626 0.5858 -0.0113 -0.0330 -0.0124 85  CYS   A SG   
656  N  N    . VAL   A 86  ? 0.6360 0.5872 0.6116 -0.0245 -0.0401 -0.0059 86  VAL   A N    
657  C  CA   . VAL   A 86  ? 0.6349 0.5711 0.5952 -0.0227 -0.0400 -0.0043 86  VAL   A CA   
658  C  C    . VAL   A 86  ? 0.6762 0.5941 0.6206 -0.0256 -0.0475 -0.0035 86  VAL   A C    
659  O  O    . VAL   A 86  ? 0.6461 0.5649 0.5930 -0.0324 -0.0523 -0.0038 86  VAL   A O    
660  C  CB   . VAL   A 86  ? 0.6530 0.5943 0.6157 -0.0281 -0.0353 -0.0035 86  VAL   A CB   
661  C  CG1  . VAL   A 86  ? 0.5802 0.5389 0.5581 -0.0252 -0.0284 -0.0044 86  VAL   A CG1  
662  C  CG2  . VAL   A 86  ? 0.6759 0.6188 0.6398 -0.0399 -0.0375 -0.0029 86  VAL   A CG2  
663  N  N    . LEU   A 87  ? 0.7755 0.6768 0.7034 -0.0201 -0.0489 -0.0025 87  LEU   A N    
664  C  CA   . LEU   A 87  ? 0.8366 0.7176 0.7461 -0.0225 -0.0559 -0.0016 87  LEU   A CA   
665  C  C    . LEU   A 87  ? 0.8941 0.7683 0.7954 -0.0283 -0.0549 -0.0002 87  LEU   A C    
666  O  O    . LEU   A 87  ? 0.9119 0.7905 0.8150 -0.0251 -0.0495 0.0000  87  LEU   A O    
667  C  CB   . LEU   A 87  ? 0.8430 0.7082 0.7373 -0.0115 -0.0585 -0.0014 87  LEU   A CB   
668  C  CG   . LEU   A 87  ? 0.8988 0.7569 0.7889 -0.0089 -0.0646 -0.0022 87  LEU   A CG   
669  C  CD1  . LEU   A 87  ? 0.8514 0.7274 0.7596 -0.0073 -0.0619 -0.0036 87  LEU   A CD1  
670  C  CD2  . LEU   A 87  ? 0.8966 0.7375 0.7691 0.0022  -0.0665 -0.0018 87  LEU   A CD2  
671  N  N    . LYS   A 88  ? 0.8323 0.6954 0.7242 -0.0370 -0.0606 0.0006  88  LYS   A N    
672  C  CA   . LYS   A 88  ? 0.8077 0.6608 0.6885 -0.0432 -0.0608 0.0020  88  LYS   A CA   
673  C  C    . LYS   A 88  ? 0.8290 0.6563 0.6862 -0.0412 -0.0685 0.0028  88  LYS   A C    
674  O  O    . LYS   A 88  ? 0.8282 0.6468 0.6797 -0.0471 -0.0753 0.0030  88  LYS   A O    
675  C  CB   . LYS   A 88  ? 0.7030 0.5666 0.5940 -0.0567 -0.0601 0.0027  88  LYS   A CB   
676  C  CG   . LYS   A 88  ? 0.7035 0.5917 0.6162 -0.0578 -0.0524 0.0018  88  LYS   A CG   
677  C  CD   . LYS   A 88  ? 0.7315 0.6297 0.6525 -0.0706 -0.0505 0.0028  88  LYS   A CD   
678  C  CE   . LYS   A 88  ? 0.7143 0.6152 0.6402 -0.0791 -0.0560 0.0028  88  LYS   A CE   
679  N  NZ   . LYS   A 88  ? 0.6954 0.6077 0.6303 -0.0917 -0.0535 0.0040  88  LYS   A NZ   
680  N  N    . LEU   A 89  ? 0.8217 0.6367 0.6650 -0.0326 -0.0676 0.0031  89  LEU   A N    
681  C  CA   . LEU   A 89  ? 0.8403 0.6301 0.6597 -0.0279 -0.0745 0.0035  89  LEU   A CA   
682  C  C    . LEU   A 89  ? 0.8406 0.6153 0.6447 -0.0345 -0.0768 0.0048  89  LEU   A C    
683  O  O    . LEU   A 89  ? 0.7932 0.5633 0.5900 -0.0292 -0.0739 0.0050  89  LEU   A O    
684  C  CB   . LEU   A 89  ? 0.8011 0.5870 0.6144 -0.0131 -0.0723 0.0029  89  LEU   A CB   
685  C  CG   . LEU   A 89  ? 0.7479 0.5486 0.5759 -0.0060 -0.0688 0.0019  89  LEU   A CG   
686  C  CD1  . LEU   A 89  ? 0.7566 0.5504 0.5753 0.0081  -0.0672 0.0018  89  LEU   A CD1  
687  C  CD2  . LEU   A 89  ? 0.8129 0.6119 0.6426 -0.0097 -0.0744 0.0013  89  LEU   A CD2  
688  N  N    . LYS   A 90  ? 0.8558 0.6229 0.6549 -0.0463 -0.0822 0.0058  90  LYS   A N    
689  C  CA   . LYS   A 90  ? 0.8423 0.5900 0.6225 -0.0532 -0.0863 0.0072  90  LYS   A CA   
690  C  C    . LYS   A 90  ? 0.9258 0.6491 0.6814 -0.0425 -0.0909 0.0071  90  LYS   A C    
691  O  O    . LYS   A 90  ? 0.9646 0.6771 0.7110 -0.0357 -0.0959 0.0064  90  LYS   A O    
692  C  CB   . LYS   A 90  ? 0.9022 0.6437 0.6800 -0.0666 -0.0928 0.0083  90  LYS   A CB   
693  C  CG   . LYS   A 90  ? 0.9756 0.6944 0.7319 -0.0752 -0.0981 0.0102  90  LYS   A CG   
694  C  CD   . LYS   A 90  ? 0.9885 0.7150 0.7496 -0.0826 -0.0919 0.0114  90  LYS   A CD   
695  C  CE   . LYS   A 90  ? 1.0147 0.7645 0.7986 -0.0955 -0.0877 0.0121  90  LYS   A CE   
696  N  NZ   . LYS   A 90  ? 0.9793 0.7361 0.7669 -0.1027 -0.0813 0.0135  90  LYS   A NZ   
697  N  N    . VAL   A 91  ? 0.9582 0.6727 0.7026 -0.0404 -0.0891 0.0076  91  VAL   A N    
698  C  CA   . VAL   A 91  ? 1.0035 0.6969 0.7254 -0.0290 -0.0926 0.0072  91  VAL   A CA   
699  C  C    . VAL   A 91  ? 1.0302 0.7010 0.7301 -0.0354 -0.0975 0.0084  91  VAL   A C    
700  O  O    . VAL   A 91  ? 1.0120 0.6847 0.7150 -0.0488 -0.0973 0.0098  91  VAL   A O    
701  C  CB   . VAL   A 91  ? 0.9901 0.6955 0.7196 -0.0165 -0.0855 0.0062  91  VAL   A CB   
702  C  CG1  . VAL   A 91  ? 0.9567 0.6766 0.7003 -0.0079 -0.0826 0.0051  91  VAL   A CG1  
703  C  CG2  . VAL   A 91  ? 0.9283 0.6517 0.6740 -0.0226 -0.0783 0.0065  91  VAL   A CG2  
704  N  N    . ASP   A 92  ? 1.0508 0.6997 0.7275 -0.0253 -0.1019 0.0080  92  ASP   A N    
705  C  CA   . ASP   A 92  ? 1.1067 0.7294 0.7580 -0.0298 -0.1080 0.0090  92  ASP   A CA   
706  C  C    . ASP   A 92  ? 1.1624 0.7888 0.8145 -0.0316 -0.1029 0.0094  92  ASP   A C    
707  O  O    . ASP   A 92  ? 1.1214 0.7429 0.7698 -0.0442 -0.1036 0.0109  92  ASP   A O    
708  C  CB   . ASP   A 92  ? 1.0973 0.6946 0.7226 -0.0172 -0.1148 0.0082  92  ASP   A CB   
709  C  CG   . ASP   A 92  ? 1.1966 0.8021 0.8251 -0.0003 -0.1097 0.0067  92  ASP   A CG   
710  O  OD1  . ASP   A 92  ? 1.1627 0.7944 0.8153 0.0014  -0.1014 0.0062  92  ASP   A OD1  
711  O  OD2  . ASP   A 92  ? 1.2519 0.8378 0.8588 0.0111  -0.1141 0.0059  92  ASP   A OD2  
712  N  N    . THR   A 93  ? 1.2097 0.8453 0.8669 -0.0194 -0.0978 0.0082  93  THR   A N    
713  C  CA   . THR   A 93  ? 1.1846 0.8236 0.8423 -0.0193 -0.0934 0.0082  93  THR   A CA   
714  C  C    . THR   A 93  ? 1.1355 0.8022 0.8202 -0.0268 -0.0850 0.0085  93  THR   A C    
715  O  O    . THR   A 93  ? 1.1230 0.8114 0.8291 -0.0237 -0.0802 0.0077  93  THR   A O    
716  C  CB   . THR   A 93  ? 1.2549 0.8919 0.9064 -0.0026 -0.0921 0.0067  93  THR   A CB   
717  O  OG1  . THR   A 93  ? 1.2388 0.8808 0.8926 -0.0024 -0.0880 0.0065  93  THR   A OG1  
718  C  CG2  . THR   A 93  ? 1.2333 0.8900 0.9031 0.0073  -0.0876 0.0056  93  THR   A CG2  
719  N  N    . ALA   A 94  ? 1.0626 0.7272 0.7450 -0.0366 -0.0835 0.0096  94  ALA   A N    
720  C  CA   . ALA   A 94  ? 0.9738 0.6620 0.6782 -0.0424 -0.0754 0.0098  94  ALA   A CA   
721  C  C    . ALA   A 94  ? 0.9709 0.6657 0.6782 -0.0319 -0.0710 0.0085  94  ALA   A C    
722  O  O    . ALA   A 94  ? 0.9183 0.5954 0.6065 -0.0261 -0.0741 0.0082  94  ALA   A O    
723  C  CB   . ALA   A 94  ? 1.0159 0.6986 0.7156 -0.0576 -0.0754 0.0117  94  ALA   A CB   
724  N  N    . ASN   A 95  ? 0.9156 0.6355 0.6468 -0.0295 -0.0640 0.0077  95  ASN   A N    
725  C  CA   . ASN   A 95  ? 0.8513 0.5799 0.5882 -0.0188 -0.0601 0.0064  95  ASN   A CA   
726  C  C    . ASN   A 95  ? 0.9105 0.6291 0.6356 -0.0213 -0.0599 0.0067  95  ASN   A C    
727  O  O    . ASN   A 95  ? 0.9576 0.6813 0.6878 -0.0320 -0.0568 0.0076  95  ASN   A O    
728  C  CB   . ASN   A 95  ? 0.8137 0.5702 0.5781 -0.0186 -0.0529 0.0058  95  ASN   A CB   
729  C  CG   . ASN   A 95  ? 0.8381 0.6051 0.6104 -0.0065 -0.0495 0.0045  95  ASN   A CG   
730  O  OD1  . ASN   A 95  ? 0.8700 0.6251 0.6285 0.0020  -0.0521 0.0039  95  ASN   A OD1  
731  N  ND2  . ASN   A 95  ? 0.7920 0.5816 0.5868 -0.0057 -0.0438 0.0040  95  ASN   A ND2  
732  N  N    . PRO   A 96  ? 0.9067 0.6105 0.6151 -0.0115 -0.0633 0.0058  96  PRO   A N    
733  C  CA   . PRO   A 96  ? 0.8669 0.5619 0.5647 -0.0127 -0.0631 0.0058  96  PRO   A CA   
734  C  C    . PRO   A 96  ? 0.8994 0.6159 0.6172 -0.0138 -0.0559 0.0053  96  PRO   A C    
735  O  O    . PRO   A 96  ? 0.8217 0.5349 0.5354 -0.0206 -0.0543 0.0059  96  PRO   A O    
736  C  CB   . PRO   A 96  ? 0.8978 0.5780 0.5786 0.0012  -0.0676 0.0045  96  PRO   A CB   
737  C  CG   . PRO   A 96  ? 0.9372 0.6277 0.6281 0.0107  -0.0672 0.0037  96  PRO   A CG   
738  C  CD   . PRO   A 96  ? 0.8794 0.5739 0.5775 0.0015  -0.0673 0.0048  96  PRO   A CD   
739  N  N    . LYS   A 97  ? 0.8513 0.5892 0.5900 -0.0076 -0.0517 0.0044  97  LYS   A N    
740  C  CA   . LYS   A 97  ? 0.7974 0.5551 0.5547 -0.0075 -0.0455 0.0037  97  LYS   A CA   
741  C  C    . LYS   A 97  ? 0.7822 0.5582 0.5590 -0.0173 -0.0403 0.0044  97  LYS   A C    
742  O  O    . LYS   A 97  ? 0.7402 0.5352 0.5354 -0.0159 -0.0351 0.0036  97  LYS   A O    
743  C  CB   . LYS   A 97  ? 0.7708 0.5402 0.5384 0.0054  -0.0441 0.0023  97  LYS   A CB   
744  C  CG   . LYS   A 97  ? 0.8407 0.5938 0.5898 0.0159  -0.0489 0.0015  97  LYS   A CG   
745  C  CD   . LYS   A 97  ? 0.8898 0.6568 0.6506 0.0280  -0.0469 0.0003  97  LYS   A CD   
746  C  CE   . LYS   A 97  ? 0.8592 0.6329 0.6266 0.0352  -0.0468 0.0003  97  LYS   A CE   
747  N  NZ   . LYS   A 97  ? 0.8099 0.6017 0.5936 0.0445  -0.0432 -0.0004 97  LYS   A NZ   
748  N  N    . THR   A 98  ? 0.7809 0.5514 0.5540 -0.0271 -0.0419 0.0057  98  THR   A N    
749  C  CA   . THR   A 98  ? 0.7590 0.5468 0.5498 -0.0367 -0.0371 0.0063  98  THR   A CA   
750  C  C    . THR   A 98  ? 0.7764 0.5706 0.5715 -0.0416 -0.0323 0.0064  98  THR   A C    
751  O  O    . THR   A 98  ? 0.8072 0.5864 0.5864 -0.0472 -0.0337 0.0074  98  THR   A O    
752  C  CB   . THR   A 98  ? 0.7415 0.5213 0.5263 -0.0475 -0.0401 0.0078  98  THR   A CB   
753  O  OG1  . THR   A 98  ? 0.7564 0.5328 0.5400 -0.0432 -0.0443 0.0076  98  THR   A OG1  
754  C  CG2  . THR   A 98  ? 0.7458 0.5447 0.5491 -0.0574 -0.0347 0.0084  98  THR   A CG2  
755  N  N    . PRO   A 99  ? 0.7057 0.5202 0.5201 -0.0396 -0.0267 0.0054  99  PRO   A N    
756  C  CA   . PRO   A 99  ? 0.7348 0.5556 0.5533 -0.0447 -0.0220 0.0055  99  PRO   A CA   
757  C  C    . PRO   A 99  ? 0.7161 0.5437 0.5408 -0.0570 -0.0190 0.0069  99  PRO   A C    
758  O  O    . PRO   A 99  ? 0.7435 0.5749 0.5735 -0.0609 -0.0204 0.0075  99  PRO   A O    
759  C  CB   . PRO   A 99  ? 0.7217 0.5617 0.5591 -0.0376 -0.0177 0.0040  99  PRO   A CB   
760  C  CG   . PRO   A 99  ? 0.6939 0.5444 0.5437 -0.0350 -0.0181 0.0037  99  PRO   A CG   
761  C  CD   . PRO   A 99  ? 0.6859 0.5184 0.5192 -0.0333 -0.0244 0.0043  99  PRO   A CD   
762  N  N    . LYS   A 100 ? 0.7567 0.5863 0.5808 -0.0629 -0.0150 0.0075  100 LYS   A N    
763  C  CA   . LYS   A 100 ? 0.7464 0.5895 0.5824 -0.0730 -0.0103 0.0085  100 LYS   A CA   
764  C  C    . LYS   A 100 ? 0.7588 0.6245 0.6178 -0.0687 -0.0070 0.0070  100 LYS   A C    
765  O  O    . LYS   A 100 ? 0.7191 0.5926 0.5858 -0.0604 -0.0052 0.0054  100 LYS   A O    
766  C  CB   . LYS   A 100 ? 0.6951 0.5376 0.5268 -0.0787 -0.0057 0.0092  100 LYS   A CB   
767  C  CG   . LYS   A 100 ? 0.7641 0.6200 0.6065 -0.0895 -0.0007 0.0105  100 LYS   A CG   
768  C  CD   . LYS   A 100 ? 0.8413 0.6899 0.6782 -0.0982 -0.0045 0.0125  100 LYS   A CD   
769  C  CE   . LYS   A 100 ? 0.9079 0.7690 0.7540 -0.1103 0.0004  0.0142  100 LYS   A CE   
770  N  NZ   . LYS   A 100 ? 0.9196 0.8067 0.7898 -0.1081 0.0056  0.0127  100 LYS   A NZ   
771  N  N    . TYR   A 101 ? 0.7292 0.6043 0.5983 -0.0739 -0.0069 0.0074  101 TYR   A N    
772  C  CA   . TYR   A 101 ? 0.6643 0.5583 0.5531 -0.0693 -0.0049 0.0060  101 TYR   A CA   
773  C  C    . TYR   A 101 ? 0.6357 0.5443 0.5375 -0.0782 -0.0020 0.0066  101 TYR   A C    
774  O  O    . TYR   A 101 ? 0.6194 0.5231 0.5152 -0.0881 -0.0024 0.0083  101 TYR   A O    
775  C  CB   . TYR   A 101 ? 0.7106 0.5993 0.5977 -0.0618 -0.0100 0.0053  101 TYR   A CB   
776  C  CG   . TYR   A 101 ? 0.6888 0.5694 0.5699 -0.0676 -0.0148 0.0065  101 TYR   A CG   
777  C  CD1  . TYR   A 101 ? 0.6076 0.5019 0.5031 -0.0716 -0.0143 0.0063  101 TYR   A CD1  
778  C  CD2  . TYR   A 101 ? 0.7163 0.5748 0.5768 -0.0689 -0.0204 0.0076  101 TYR   A CD2  
779  C  CE1  . TYR   A 101 ? 0.6085 0.4951 0.4985 -0.0771 -0.0195 0.0073  101 TYR   A CE1  
780  C  CE2  . TYR   A 101 ? 0.7203 0.5699 0.5742 -0.0743 -0.0255 0.0086  101 TYR   A CE2  
781  C  CZ   . TYR   A 101 ? 0.6687 0.5325 0.5376 -0.0786 -0.0251 0.0085  101 TYR   A CZ   
782  O  OH   . TYR   A 101 ? 0.6853 0.5397 0.5473 -0.0843 -0.0308 0.0095  101 TYR   A OH   
783  N  N    . LYS   A 102 ? 0.7096 0.6364 0.6297 -0.0744 0.0005  0.0051  102 LYS   A N    
784  C  CA   . LYS   A 102 ? 0.6422 0.5854 0.5771 -0.0807 0.0029  0.0051  102 LYS   A CA   
785  C  C    . LYS   A 102 ? 0.6540 0.6116 0.6049 -0.0733 0.0033  0.0031  102 LYS   A C    
786  O  O    . LYS   A 102 ? 0.6748 0.6330 0.6275 -0.0643 0.0039  0.0019  102 LYS   A O    
787  C  CB   . LYS   A 102 ? 0.6336 0.5868 0.5735 -0.0873 0.0092  0.0057  102 LYS   A CB   
788  C  CG   . LYS   A 102 ? 0.7985 0.7711 0.7549 -0.0938 0.0124  0.0057  102 LYS   A CG   
789  C  CD   . LYS   A 102 ? 0.8107 0.7803 0.7656 -0.1025 0.0080  0.0072  102 LYS   A CD   
790  C  CE   . LYS   A 102 ? 0.8680 0.8569 0.8381 -0.1113 0.0117  0.0078  102 LYS   A CE   
791  N  NZ   . LYS   A 102 ? 0.8884 0.8740 0.8577 -0.1190 0.0062  0.0090  102 LYS   A NZ   
792  N  N    . PHE   A 103 ? 0.5880 0.5557 0.5493 -0.0772 0.0023  0.0030  103 PHE   A N    
793  C  CA   . PHE   A 103 ? 0.5844 0.5656 0.5605 -0.0710 0.0025  0.0011  103 PHE   A CA   
794  C  C    . PHE   A 103 ? 0.5524 0.5535 0.5442 -0.0730 0.0084  0.0002  103 PHE   A C    
795  O  O    . PHE   A 103 ? 0.6311 0.6385 0.6256 -0.0817 0.0108  0.0011  103 PHE   A O    
796  C  CB   . PHE   A 103 ? 0.5196 0.4989 0.4968 -0.0731 -0.0029 0.0013  103 PHE   A CB   
797  C  CG   . PHE   A 103 ? 0.5156 0.4750 0.4767 -0.0698 -0.0089 0.0020  103 PHE   A CG   
798  C  CD1  . PHE   A 103 ? 0.4913 0.4392 0.4416 -0.0629 -0.0089 0.0021  103 PHE   A CD1  
799  C  CD2  . PHE   A 103 ? 0.4959 0.4478 0.4522 -0.0733 -0.0148 0.0027  103 PHE   A CD2  
800  C  CE1  . PHE   A 103 ? 0.5062 0.4360 0.4411 -0.0590 -0.0142 0.0027  103 PHE   A CE1  
801  C  CE2  . PHE   A 103 ? 0.5150 0.4472 0.4548 -0.0696 -0.0204 0.0033  103 PHE   A CE2  
802  C  CZ   . PHE   A 103 ? 0.5408 0.4622 0.4699 -0.0621 -0.0199 0.0032  103 PHE   A CZ   
803  N  N    . VAL   A 104 ? 0.4649 0.4757 0.4665 -0.0650 0.0109  -0.0017 104 VAL   A N    
804  C  CA   . VAL   A 104 ? 0.5102 0.5378 0.5245 -0.0649 0.0166  -0.0029 104 VAL   A CA   
805  C  C    . VAL   A 104 ? 0.4578 0.4967 0.4848 -0.0576 0.0165  -0.0050 104 VAL   A C    
806  O  O    . VAL   A 104 ? 0.4567 0.4903 0.4818 -0.0500 0.0149  -0.0056 104 VAL   A O    
807  C  CB   . VAL   A 104 ? 0.5120 0.5358 0.5205 -0.0625 0.0205  -0.0029 104 VAL   A CB   
808  C  CG1  . VAL   A 104 ? 0.5485 0.5884 0.5692 -0.0601 0.0259  -0.0045 104 VAL   A CG1  
809  C  CG2  . VAL   A 104 ? 0.5228 0.5364 0.5187 -0.0703 0.0213  -0.0009 104 VAL   A CG2  
810  N  N    . ARG   A 105 ? 0.4753 0.5301 0.5155 -0.0599 0.0182  -0.0060 105 ARG   A N    
811  C  CA   . ARG   A 105 ? 0.4794 0.5454 0.5314 -0.0527 0.0187  -0.0082 105 ARG   A CA   
812  C  C    . ARG   A 105 ? 0.4704 0.5443 0.5269 -0.0493 0.0242  -0.0094 105 ARG   A C    
813  O  O    . ARG   A 105 ? 0.4661 0.5517 0.5290 -0.0530 0.0283  -0.0097 105 ARG   A O    
814  C  CB   . ARG   A 105 ? 0.4088 0.4877 0.4725 -0.0554 0.0172  -0.0091 105 ARG   A CB   
815  C  CG   . ARG   A 105 ? 0.4331 0.5183 0.5054 -0.0471 0.0158  -0.0113 105 ARG   A CG   
816  C  CD   . ARG   A 105 ? 0.4271 0.5233 0.5099 -0.0487 0.0130  -0.0124 105 ARG   A CD   
817  N  NE   . ARG   A 105 ? 0.4876 0.5875 0.5763 -0.0401 0.0117  -0.0145 105 ARG   A NE   
818  C  CZ   . ARG   A 105 ? 0.5291 0.6202 0.6140 -0.0359 0.0069  -0.0146 105 ARG   A CZ   
819  N  NH1  . ARG   A 105 ? 0.5106 0.5890 0.5859 -0.0392 0.0026  -0.0129 105 ARG   A NH1  
820  N  NH2  . ARG   A 105 ? 0.4666 0.5611 0.5565 -0.0283 0.0063  -0.0163 105 ARG   A NH2  
821  N  N    . ILE   A 106 ? 0.4773 0.5451 0.5303 -0.0423 0.0243  -0.0099 106 ILE   A N    
822  C  CA   . ILE   A 106 ? 0.5031 0.5771 0.5601 -0.0380 0.0284  -0.0112 106 ILE   A CA   
823  C  C    . ILE   A 106 ? 0.4843 0.5726 0.5541 -0.0339 0.0296  -0.0134 106 ILE   A C    
824  O  O    . ILE   A 106 ? 0.4851 0.5791 0.5614 -0.0339 0.0272  -0.0141 106 ILE   A O    
825  C  CB   . ILE   A 106 ? 0.4903 0.5533 0.5402 -0.0320 0.0273  -0.0111 106 ILE   A CB   
826  C  CG1  . ILE   A 106 ? 0.4963 0.5582 0.5498 -0.0259 0.0240  -0.0116 106 ILE   A CG1  
827  C  CG2  . ILE   A 106 ? 0.4723 0.5215 0.5092 -0.0352 0.0261  -0.0092 106 ILE   A CG2  
828  C  CD1  . ILE   A 106 ? 0.4792 0.5344 0.5293 -0.0198 0.0235  -0.0115 106 ILE   A CD1  
829  N  N    . GLN   A 107 ? 0.4779 0.5707 0.5501 -0.0299 0.0330  -0.0147 107 GLN   A N    
830  C  CA   . GLN   A 107 ? 0.4932 0.5990 0.5756 -0.0258 0.0352  -0.0170 107 GLN   A CA   
831  C  C    . GLN   A 107 ? 0.4477 0.5488 0.5290 -0.0182 0.0345  -0.0180 107 GLN   A C    
832  O  O    . GLN   A 107 ? 0.4113 0.5013 0.4846 -0.0171 0.0337  -0.0169 107 GLN   A O    
833  C  CB   . GLN   A 107 ? 0.5454 0.6602 0.6297 -0.0289 0.0404  -0.0174 107 GLN   A CB   
834  C  CG   . GLN   A 107 ? 0.6184 0.7498 0.7144 -0.0265 0.0427  -0.0196 107 GLN   A CG   
835  C  CD   . GLN   A 107 ? 0.6146 0.7560 0.7188 -0.0312 0.0412  -0.0194 107 GLN   A CD   
836  O  OE1  . GLN   A 107 ? 0.6871 0.8344 0.7989 -0.0276 0.0384  -0.0210 107 GLN   A OE1  
837  N  NE2  . GLN   A 107 ? 0.6147 0.7581 0.7174 -0.0396 0.0431  -0.0176 107 GLN   A NE2  
838  N  N    . PRO   A 108 ? 0.4168 0.5255 0.5057 -0.0129 0.0343  -0.0200 108 PRO   A N    
839  C  CA   . PRO   A 108 ? 0.4730 0.5766 0.5604 -0.0064 0.0336  -0.0208 108 PRO   A CA   
840  C  C    . PRO   A 108 ? 0.5529 0.6535 0.6352 -0.0060 0.0366  -0.0209 108 PRO   A C    
841  O  O    . PRO   A 108 ? 0.5538 0.6608 0.6368 -0.0083 0.0402  -0.0215 108 PRO   A O    
842  C  CB   . PRO   A 108 ? 0.4647 0.5778 0.5605 -0.0015 0.0334  -0.0232 108 PRO   A CB   
843  C  CG   . PRO   A 108 ? 0.4818 0.6017 0.5831 -0.0046 0.0318  -0.0232 108 PRO   A CG   
844  C  CD   . PRO   A 108 ? 0.4734 0.5943 0.5722 -0.0123 0.0337  -0.0216 108 PRO   A CD   
845  N  N    . GLY   A 109 ? 0.5316 0.6222 0.6084 -0.0032 0.0351  -0.0203 109 GLY   A N    
846  C  CA   . GLY   A 109 ? 0.4625 0.5482 0.5334 -0.0028 0.0369  -0.0203 109 GLY   A CA   
847  C  C    . GLY   A 109 ? 0.5010 0.5774 0.5635 -0.0069 0.0364  -0.0183 109 GLY   A C    
848  O  O    . GLY   A 109 ? 0.4906 0.5587 0.5474 -0.0054 0.0354  -0.0178 109 GLY   A O    
849  N  N    . GLN   A 110 ? 0.5608 0.6379 0.6219 -0.0122 0.0367  -0.0171 110 GLN   A N    
850  C  CA   . GLN   A 110 ? 0.5418 0.6086 0.5935 -0.0160 0.0357  -0.0152 110 GLN   A CA   
851  C  C    . GLN   A 110 ? 0.6172 0.6748 0.6656 -0.0133 0.0318  -0.0141 110 GLN   A C    
852  O  O    . GLN   A 110 ? 0.5758 0.6351 0.6291 -0.0102 0.0297  -0.0142 110 GLN   A O    
853  C  CB   . GLN   A 110 ? 0.5470 0.6159 0.5977 -0.0227 0.0364  -0.0142 110 GLN   A CB   
854  C  CG   . GLN   A 110 ? 0.6521 0.7259 0.7013 -0.0269 0.0410  -0.0143 110 GLN   A CG   
855  C  CD   . GLN   A 110 ? 0.7230 0.7945 0.7674 -0.0348 0.0413  -0.0124 110 GLN   A CD   
856  O  OE1  . GLN   A 110 ? 0.6898 0.7609 0.7358 -0.0375 0.0385  -0.0116 110 GLN   A OE1  
857  N  NE2  . GLN   A 110 ? 0.7540 0.8228 0.7914 -0.0388 0.0447  -0.0117 110 GLN   A NE2  
858  N  N    . THR   A 111 ? 0.6274 0.6749 0.6667 -0.0141 0.0308  -0.0130 111 THR   A N    
859  C  CA   . THR   A 111 ? 0.5606 0.6003 0.5968 -0.0105 0.0276  -0.0121 111 THR   A CA   
860  C  C    . THR   A 111 ? 0.5786 0.6094 0.6064 -0.0131 0.0254  -0.0104 111 THR   A C    
861  O  O    . THR   A 111 ? 0.6632 0.6914 0.6854 -0.0182 0.0263  -0.0099 111 THR   A O    
862  C  CB   . THR   A 111 ? 0.5408 0.5763 0.5735 -0.0082 0.0278  -0.0125 111 THR   A CB   
863  O  OG1  . THR   A 111 ? 0.6115 0.6432 0.6449 -0.0040 0.0250  -0.0118 111 THR   A OG1  
864  C  CG2  . THR   A 111 ? 0.5285 0.5558 0.5506 -0.0117 0.0280  -0.0118 111 THR   A CG2  
865  N  N    . PHE   A 112 ? 0.5415 0.5671 0.5677 -0.0096 0.0225  -0.0095 112 PHE   A N    
866  C  CA   . PHE   A 112 ? 0.4973 0.5129 0.5139 -0.0111 0.0199  -0.0081 112 PHE   A CA   
867  C  C    . PHE   A 112 ? 0.5005 0.5108 0.5150 -0.0056 0.0174  -0.0073 112 PHE   A C    
868  O  O    . PHE   A 112 ? 0.4984 0.5137 0.5202 -0.0015 0.0176  -0.0076 112 PHE   A O    
869  C  CB   . PHE   A 112 ? 0.4879 0.5040 0.5047 -0.0139 0.0188  -0.0076 112 PHE   A CB   
870  C  CG   . PHE   A 112 ? 0.5193 0.5419 0.5449 -0.0103 0.0182  -0.0080 112 PHE   A CG   
871  C  CD1  . PHE   A 112 ? 0.4746 0.5081 0.5101 -0.0105 0.0203  -0.0094 112 PHE   A CD1  
872  C  CD2  . PHE   A 112 ? 0.5053 0.5227 0.5284 -0.0063 0.0155  -0.0071 112 PHE   A CD2  
873  C  CE1  . PHE   A 112 ? 0.4126 0.4508 0.4549 -0.0070 0.0195  -0.0099 112 PHE   A CE1  
874  C  CE2  . PHE   A 112 ? 0.4566 0.4788 0.4864 -0.0030 0.0151  -0.0073 112 PHE   A CE2  
875  C  CZ   . PHE   A 112 ? 0.4928 0.5251 0.5321 -0.0035 0.0169  -0.0088 112 PHE   A CZ   
876  N  N    . SER   A 113 ? 0.4721 0.4722 0.4762 -0.0057 0.0151  -0.0063 113 SER   A N    
877  C  CA   . SER   A 113 ? 0.4367 0.4321 0.4383 -0.0002 0.0126  -0.0055 113 SER   A CA   
878  C  C    . SER   A 113 ? 0.4750 0.4681 0.4752 0.0018  0.0108  -0.0046 113 SER   A C    
879  O  O    . SER   A 113 ? 0.4682 0.4574 0.4636 -0.0018 0.0099  -0.0043 113 SER   A O    
880  C  CB   . SER   A 113 ? 0.4167 0.4018 0.4069 0.0001  0.0106  -0.0051 113 SER   A CB   
881  O  OG   . SER   A 113 ? 0.5205 0.5073 0.5122 0.0002  0.0116  -0.0059 113 SER   A OG   
882  N  N    . VAL   A 114 ? 0.4764 0.4716 0.4806 0.0075  0.0103  -0.0040 114 VAL   A N    
883  C  CA   . VAL   A 114 ? 0.4084 0.4010 0.4107 0.0106  0.0088  -0.0031 114 VAL   A CA   
884  C  C    . VAL   A 114 ? 0.3815 0.3671 0.3765 0.0159  0.0068  -0.0021 114 VAL   A C    
885  O  O    . VAL   A 114 ? 0.3318 0.3207 0.3304 0.0192  0.0072  -0.0019 114 VAL   A O    
886  C  CB   . VAL   A 114 ? 0.4622 0.4637 0.4753 0.0132  0.0105  -0.0032 114 VAL   A CB   
887  C  CG1  . VAL   A 114 ? 0.4309 0.4291 0.4413 0.0179  0.0092  -0.0020 114 VAL   A CG1  
888  C  CG2  . VAL   A 114 ? 0.4259 0.4336 0.4449 0.0086  0.0119  -0.0044 114 VAL   A CG2  
889  N  N    . LEU   A 115 ? 0.3840 0.3599 0.3684 0.0166  0.0042  -0.0015 115 LEU   A N    
890  C  CA   . LEU   A 115 ? 0.4306 0.3996 0.4071 0.0228  0.0021  -0.0006 115 LEU   A CA   
891  C  C    . LEU   A 115 ? 0.4379 0.4081 0.4162 0.0276  0.0022  0.0003  115 LEU   A C    
892  O  O    . LEU   A 115 ? 0.4040 0.3681 0.3763 0.0265  0.0005  0.0003  115 LEU   A O    
893  C  CB   . LEU   A 115 ? 0.3689 0.3238 0.3298 0.0211  -0.0012 -0.0006 115 LEU   A CB   
894  C  CG   . LEU   A 115 ? 0.4183 0.3650 0.3693 0.0283  -0.0037 0.0000  115 LEU   A CG   
895  C  CD1  . LEU   A 115 ? 0.4122 0.3636 0.3672 0.0319  -0.0032 -0.0001 115 LEU   A CD1  
896  C  CD2  . LEU   A 115 ? 0.4460 0.3764 0.3795 0.0269  -0.0076 0.0001  115 LEU   A CD2  
897  N  N    . ALA   A 116 ? 0.4333 0.4111 0.4194 0.0328  0.0041  0.0010  116 ALA   A N    
898  C  CA   . ALA   A 116 ? 0.4981 0.4774 0.4859 0.0376  0.0049  0.0020  116 ALA   A CA   
899  C  C    . ALA   A 116 ? 0.4587 0.4280 0.4340 0.0435  0.0025  0.0028  116 ALA   A C    
900  O  O    . ALA   A 116 ? 0.4674 0.4342 0.4383 0.0468  0.0015  0.0030  116 ALA   A O    
901  C  CB   . ALA   A 116 ? 0.3738 0.3646 0.3740 0.0404  0.0080  0.0029  116 ALA   A CB   
902  N  N    . CYS   A 117 ? 0.3955 0.3584 0.3644 0.0451  0.0012  0.0031  117 CYS   A N    
903  C  CA   . CYS   A 117 ? 0.4965 0.4470 0.4507 0.0501  -0.0018 0.0036  117 CYS   A CA   
904  C  C    . CYS   A 117 ? 0.5563 0.5058 0.5089 0.0560  -0.0011 0.0046  117 CYS   A C    
905  O  O    . CYS   A 117 ? 0.5311 0.4811 0.4862 0.0534  -0.0011 0.0044  117 CYS   A O    
906  C  CB   . CYS   A 117 ? 0.4936 0.4315 0.4358 0.0447  -0.0058 0.0027  117 CYS   A CB   
907  S  SG   . CYS   A 117 ? 0.5908 0.5252 0.5292 0.0390  -0.0071 0.0019  117 CYS   A SG   
908  N  N    . TYR   A 118 ? 0.5746 0.5222 0.5221 0.0643  -0.0006 0.0057  118 TYR   A N    
909  C  CA   . TYR   A 118 ? 0.5552 0.5005 0.4988 0.0711  0.0003  0.0068  118 TYR   A CA   
910  C  C    . TYR   A 118 ? 0.5669 0.4978 0.4929 0.0773  -0.0032 0.0069  118 TYR   A C    
911  O  O    . TYR   A 118 ? 0.5827 0.5127 0.5049 0.0813  -0.0037 0.0070  118 TYR   A O    
912  C  CB   . TYR   A 118 ? 0.5014 0.4600 0.4569 0.0758  0.0053  0.0084  118 TYR   A CB   
913  C  CG   . TYR   A 118 ? 0.5478 0.5189 0.5192 0.0695  0.0081  0.0083  118 TYR   A CG   
914  C  CD1  . TYR   A 118 ? 0.5512 0.5290 0.5302 0.0653  0.0084  0.0076  118 TYR   A CD1  
915  C  CD2  . TYR   A 118 ? 0.4959 0.4709 0.4734 0.0679  0.0100  0.0085  118 TYR   A CD2  
916  C  CE1  . TYR   A 118 ? 0.4958 0.4835 0.4878 0.0599  0.0105  0.0073  118 TYR   A CE1  
917  C  CE2  . TYR   A 118 ? 0.5015 0.4867 0.4923 0.0625  0.0121  0.0082  118 TYR   A CE2  
918  C  CZ   . TYR   A 118 ? 0.5338 0.5252 0.5317 0.0586  0.0124  0.0076  118 TYR   A CZ   
919  O  OH   . TYR   A 118 ? 0.5519 0.5522 0.5615 0.0537  0.0142  0.0071  118 TYR   A OH   
920  N  N    . ASN   A 119 ? 0.6026 0.5217 0.5172 0.0781  -0.0062 0.0067  119 ASN   A N    
921  C  CA   . ASN   A 119 ? 0.6596 0.5622 0.5550 0.0840  -0.0103 0.0066  119 ASN   A CA   
922  C  C    . ASN   A 119 ? 0.6859 0.5787 0.5718 0.0800  -0.0145 0.0055  119 ASN   A C    
923  O  O    . ASN   A 119 ? 0.6577 0.5413 0.5311 0.0862  -0.0167 0.0055  119 ASN   A O    
924  C  CB   . ASN   A 119 ? 0.6080 0.5130 0.5006 0.0953  -0.0076 0.0079  119 ASN   A CB   
925  C  CG   . ASN   A 119 ? 0.6668 0.5762 0.5630 0.1000  -0.0042 0.0092  119 ASN   A CG   
926  O  OD1  . ASN   A 119 ? 0.8079 0.7065 0.6942 0.1010  -0.0068 0.0090  119 ASN   A OD1  
927  N  ND2  . ASN   A 119 ? 0.6380 0.5632 0.5484 0.1025  0.0014  0.0106  119 ASN   A ND2  
928  N  N    . GLY   A 120 ? 0.7354 0.6299 0.6267 0.0699  -0.0154 0.0046  120 GLY   A N    
929  C  CA   . GLY   A 120 ? 0.7541 0.6389 0.6363 0.0645  -0.0191 0.0038  120 GLY   A CA   
930  C  C    . GLY   A 120 ? 0.7194 0.6096 0.6052 0.0654  -0.0177 0.0036  120 GLY   A C    
931  O  O    . GLY   A 120 ? 0.7154 0.5968 0.5928 0.0611  -0.0206 0.0029  120 GLY   A O    
932  N  N    . SER   A 121 ? 0.6205 0.5243 0.5181 0.0707  -0.0136 0.0042  121 SER   A N    
933  C  CA   . SER   A 121 ? 0.6136 0.5227 0.5149 0.0719  -0.0129 0.0039  121 SER   A CA   
934  C  C    . SER   A 121 ? 0.6432 0.5677 0.5626 0.0656  -0.0092 0.0037  121 SER   A C    
935  O  O    . SER   A 121 ? 0.6023 0.5384 0.5346 0.0653  -0.0056 0.0044  121 SER   A O    
936  C  CB   . SER   A 121 ? 0.5693 0.4823 0.4702 0.0826  -0.0116 0.0046  121 SER   A CB   
937  O  OG   . SER   A 121 ? 0.7199 0.6167 0.6015 0.0890  -0.0157 0.0044  121 SER   A OG   
938  N  N    . PRO   A 122 ? 0.5724 0.4966 0.4923 0.0606  -0.0101 0.0028  122 PRO   A N    
939  C  CA   . PRO   A 122 ? 0.5164 0.4542 0.4522 0.0553  -0.0069 0.0026  122 PRO   A CA   
940  C  C    . PRO   A 122 ? 0.5194 0.4704 0.4670 0.0611  -0.0041 0.0033  122 PRO   A C    
941  O  O    . PRO   A 122 ? 0.5159 0.4653 0.4590 0.0675  -0.0054 0.0035  122 PRO   A O    
942  C  CB   . PRO   A 122 ? 0.5886 0.5200 0.5182 0.0501  -0.0090 0.0015  122 PRO   A CB   
943  C  CG   . PRO   A 122 ? 0.5892 0.5028 0.4999 0.0503  -0.0133 0.0013  122 PRO   A CG   
944  C  CD   . PRO   A 122 ? 0.6144 0.5230 0.5186 0.0570  -0.0144 0.0020  122 PRO   A CD   
945  N  N    . SER   A 123 ? 0.4572 0.4209 0.4198 0.0585  -0.0005 0.0038  123 SER   A N    
946  C  CA   . SER   A 123 ? 0.4980 0.4750 0.4734 0.0622  0.0023  0.0048  123 SER   A CA   
947  C  C    . SER   A 123 ? 0.5131 0.4984 0.4990 0.0574  0.0030  0.0042  123 SER   A C    
948  O  O    . SER   A 123 ? 0.4440 0.4368 0.4364 0.0606  0.0033  0.0046  123 SER   A O    
949  C  CB   . SER   A 123 ? 0.5332 0.5178 0.5170 0.0634  0.0057  0.0061  123 SER   A CB   
950  O  OG   . SER   A 123 ? 0.6505 0.6285 0.6249 0.0698  0.0053  0.0070  123 SER   A OG   
951  N  N    . GLY   A 124 ? 0.4820 0.4667 0.4700 0.0501  0.0033  0.0031  124 GLY   A N    
952  C  CA   . GLY   A 124 ? 0.4466 0.4380 0.4434 0.0458  0.0040  0.0024  124 GLY   A CA   
953  C  C    . GLY   A 124 ? 0.4343 0.4225 0.4296 0.0384  0.0041  0.0011  124 GLY   A C    
954  O  O    . GLY   A 124 ? 0.4602 0.4434 0.4505 0.0362  0.0040  0.0009  124 GLY   A O    
955  N  N    . VAL   A 125 ? 0.4232 0.4146 0.4229 0.0348  0.0043  0.0001  125 VAL   A N    
956  C  CA   . VAL   A 125 ? 0.4400 0.4291 0.4381 0.0281  0.0049  -0.0011 125 VAL   A CA   
957  C  C    . VAL   A 125 ? 0.3628 0.3611 0.3723 0.0257  0.0068  -0.0017 125 VAL   A C    
958  O  O    . VAL   A 125 ? 0.3452 0.3476 0.3596 0.0277  0.0063  -0.0016 125 VAL   A O    
959  C  CB   . VAL   A 125 ? 0.4276 0.4059 0.4132 0.0262  0.0024  -0.0019 125 VAL   A CB   
960  C  CG1  . VAL   A 125 ? 0.3994 0.3783 0.3854 0.0289  0.0008  -0.0022 125 VAL   A CG1  
961  C  CG2  . VAL   A 125 ? 0.3895 0.3653 0.3725 0.0192  0.0035  -0.0028 125 VAL   A CG2  
962  N  N    . TYR   A 126 ? 0.3086 0.3104 0.3225 0.0216  0.0088  -0.0023 126 TYR   A N    
963  C  CA   . TYR   A 126 ? 0.3944 0.4038 0.4178 0.0197  0.0106  -0.0031 126 TYR   A CA   
964  C  C    . TYR   A 126 ? 0.4292 0.4387 0.4517 0.0146  0.0121  -0.0044 126 TYR   A C    
965  O  O    . TYR   A 126 ? 0.4011 0.4068 0.4184 0.0125  0.0120  -0.0044 126 TYR   A O    
966  C  CB   . TYR   A 126 ? 0.4610 0.4782 0.4943 0.0223  0.0120  -0.0021 126 TYR   A CB   
967  C  CG   . TYR   A 126 ? 0.4240 0.4411 0.4569 0.0235  0.0129  -0.0014 126 TYR   A CG   
968  C  CD1  . TYR   A 126 ? 0.4296 0.4489 0.4652 0.0207  0.0141  -0.0024 126 TYR   A CD1  
969  C  CD2  . TYR   A 126 ? 0.4094 0.4239 0.4388 0.0280  0.0122  0.0000  126 TYR   A CD2  
970  C  CE1  . TYR   A 126 ? 0.4245 0.4431 0.4593 0.0220  0.0142  -0.0019 126 TYR   A CE1  
971  C  CE2  . TYR   A 126 ? 0.4612 0.4742 0.4890 0.0295  0.0126  0.0006  126 TYR   A CE2  
972  C  CZ   . TYR   A 126 ? 0.4878 0.5025 0.5182 0.0263  0.0134  -0.0004 126 TYR   A CZ   
973  O  OH   . TYR   A 126 ? 0.4788 0.4915 0.5071 0.0281  0.0132  0.0000  126 TYR   A OH   
974  N  N    . GLN   A 127 ? 0.4353 0.4493 0.4631 0.0127  0.0134  -0.0054 127 GLN   A N    
975  C  CA   . GLN   A 127 ? 0.4417 0.4574 0.4696 0.0085  0.0153  -0.0067 127 GLN   A CA   
976  C  C    . GLN   A 127 ? 0.4490 0.4725 0.4859 0.0090  0.0170  -0.0072 127 GLN   A C    
977  O  O    . GLN   A 127 ? 0.4963 0.5237 0.5396 0.0116  0.0170  -0.0069 127 GLN   A O    
978  C  CB   . GLN   A 127 ? 0.4579 0.4726 0.4839 0.0066  0.0157  -0.0079 127 GLN   A CB   
979  C  CG   . GLN   A 127 ? 0.5058 0.5223 0.5306 0.0025  0.0182  -0.0091 127 GLN   A CG   
980  C  CD   . GLN   A 127 ? 0.5394 0.5485 0.5538 -0.0012 0.0181  -0.0089 127 GLN   A CD   
981  O  OE1  . GLN   A 127 ? 0.5656 0.5688 0.5740 -0.0012 0.0163  -0.0078 127 GLN   A OE1  
982  N  NE2  . GLN   A 127 ? 0.5649 0.5739 0.5764 -0.0043 0.0202  -0.0098 127 GLN   A NE2  
983  N  N    . CYS   A 128 ? 0.4867 0.5121 0.5237 0.0063  0.0181  -0.0078 128 CYS   A N    
984  C  CA   . CYS   A 128 ? 0.4480 0.4802 0.4925 0.0069  0.0193  -0.0085 128 CYS   A CA   
985  C  C    . CYS   A 128 ? 0.4741 0.5108 0.5201 0.0034  0.0213  -0.0101 128 CYS   A C    
986  O  O    . CYS   A 128 ? 0.4622 0.4964 0.5029 -0.0003 0.0218  -0.0102 128 CYS   A O    
987  C  CB   . CYS   A 128 ? 0.4877 0.5185 0.5312 0.0079  0.0182  -0.0076 128 CYS   A CB   
988  S  SG   . CYS   A 128 ? 0.6467 0.6755 0.6911 0.0133  0.0170  -0.0058 128 CYS   A SG   
989  N  N    . ALA   A 129 ? 0.5161 0.5597 0.5692 0.0047  0.0224  -0.0113 129 ALA   A N    
990  C  CA   . ALA   A 129 ? 0.4993 0.5492 0.5553 0.0021  0.0244  -0.0129 129 ALA   A CA   
991  C  C    . ALA   A 129 ? 0.4835 0.5383 0.5445 0.0026  0.0239  -0.0133 129 ALA   A C    
992  O  O    . ALA   A 129 ? 0.4672 0.5214 0.5306 0.0061  0.0225  -0.0129 129 ALA   A O    
993  C  CB   . ALA   A 129 ? 0.4976 0.5515 0.5568 0.0036  0.0261  -0.0145 129 ALA   A CB   
994  N  N    . MET   A 130 ? 0.4508 0.5107 0.5132 -0.0009 0.0249  -0.0141 130 MET   A N    
995  C  CA   . MET   A 130 ? 0.4987 0.5646 0.5668 -0.0006 0.0241  -0.0149 130 MET   A CA   
996  C  C    . MET   A 130 ? 0.4963 0.5702 0.5714 0.0027  0.0255  -0.0170 130 MET   A C    
997  O  O    . MET   A 130 ? 0.5067 0.5865 0.5839 0.0015  0.0279  -0.0183 130 MET   A O    
998  C  CB   . MET   A 130 ? 0.4954 0.5646 0.5632 -0.0062 0.0243  -0.0149 130 MET   A CB   
999  C  CG   . MET   A 130 ? 0.4594 0.5359 0.5340 -0.0061 0.0230  -0.0160 130 MET   A CG   
1000 S  SD   . MET   A 130 ? 0.4247 0.4929 0.4959 -0.0032 0.0188  -0.0148 130 MET   A SD   
1001 C  CE   . MET   A 130 ? 0.4139 0.4709 0.4743 -0.0076 0.0175  -0.0125 130 MET   A CE   
1002 N  N    . ARG   A 131 ? 0.5177 0.5910 0.5956 0.0071  0.0239  -0.0172 131 ARG   A N    
1003 C  CA   . ARG   A 131 ? 0.5177 0.5961 0.6006 0.0111  0.0245  -0.0190 131 ARG   A CA   
1004 C  C    . ARG   A 131 ? 0.5508 0.6389 0.6397 0.0108  0.0247  -0.0210 131 ARG   A C    
1005 O  O    . ARG   A 131 ? 0.5081 0.5987 0.5978 0.0072  0.0240  -0.0207 131 ARG   A O    
1006 C  CB   . ARG   A 131 ? 0.5575 0.6307 0.6401 0.0154  0.0226  -0.0183 131 ARG   A CB   
1007 C  CG   . ARG   A 131 ? 0.6065 0.6725 0.6849 0.0158  0.0226  -0.0164 131 ARG   A CG   
1008 C  CD   . ARG   A 131 ? 0.6082 0.6742 0.6877 0.0181  0.0233  -0.0174 131 ARG   A CD   
1009 N  NE   . ARG   A 131 ? 0.5814 0.6428 0.6575 0.0169  0.0235  -0.0162 131 ARG   A NE   
1010 C  CZ   . ARG   A 131 ? 0.5850 0.6457 0.6606 0.0177  0.0239  -0.0171 131 ARG   A CZ   
1011 N  NH1  . ARG   A 131 ? 0.6169 0.6811 0.6946 0.0200  0.0244  -0.0192 131 ARG   A NH1  
1012 N  NH2  . ARG   A 131 ? 0.6256 0.6818 0.6980 0.0165  0.0235  -0.0161 131 ARG   A NH2  
1013 N  N    . PRO   A 132 ? 0.6148 0.7084 0.7078 0.0145  0.0255  -0.0231 132 PRO   A N    
1014 C  CA   . PRO   A 132 ? 0.6133 0.7179 0.7129 0.0148  0.0258  -0.0253 132 PRO   A CA   
1015 C  C    . PRO   A 132 ? 0.6173 0.7226 0.7198 0.0172  0.0226  -0.0258 132 PRO   A C    
1016 O  O    . PRO   A 132 ? 0.6238 0.7378 0.7320 0.0161  0.0219  -0.0270 132 PRO   A O    
1017 C  CB   . PRO   A 132 ? 0.6263 0.7350 0.7275 0.0190  0.0276  -0.0275 132 PRO   A CB   
1018 C  CG   . PRO   A 132 ? 0.6418 0.7414 0.7365 0.0190  0.0285  -0.0263 132 PRO   A CG   
1019 C  CD   . PRO   A 132 ? 0.6600 0.7506 0.7514 0.0183  0.0262  -0.0239 132 PRO   A CD   
1020 N  N    . ASN   A 133 ? 0.5790 0.6757 0.6781 0.0206  0.0206  -0.0248 133 ASN   A N    
1021 C  CA   . ASN   A 133 ? 0.5984 0.6927 0.6977 0.0221  0.0174  -0.0245 133 ASN   A CA   
1022 C  C    . ASN   A 133 ? 0.5965 0.6869 0.6927 0.0176  0.0161  -0.0226 133 ASN   A C    
1023 O  O    . ASN   A 133 ? 0.5460 0.6327 0.6408 0.0187  0.0132  -0.0221 133 ASN   A O    
1024 C  CB   . ASN   A 133 ? 0.6477 0.7332 0.7431 0.0268  0.0162  -0.0237 133 ASN   A CB   
1025 C  CG   . ASN   A 133 ? 0.6344 0.7120 0.7247 0.0255  0.0176  -0.0212 133 ASN   A CG   
1026 O  OD1  . ASN   A 133 ? 0.5392 0.6164 0.6278 0.0215  0.0189  -0.0201 133 ASN   A OD1  
1027 N  ND2  . ASN   A 133 ? 0.6107 0.6817 0.6983 0.0289  0.0171  -0.0201 133 ASN   A ND2  
1028 N  N    . PHE   A 134 ? 0.5951 0.6851 0.6890 0.0127  0.0180  -0.0214 134 PHE   A N    
1029 C  CA   . PHE   A 134 ? 0.5989 0.6841 0.6884 0.0080  0.0168  -0.0196 134 PHE   A CA   
1030 C  C    . PHE   A 134 ? 0.5984 0.6721 0.6809 0.0103  0.0149  -0.0175 134 PHE   A C    
1031 O  O    . PHE   A 134 ? 0.5622 0.6306 0.6404 0.0086  0.0126  -0.0163 134 PHE   A O    
1032 C  CB   . PHE   A 134 ? 0.5378 0.6290 0.6313 0.0051  0.0145  -0.0204 134 PHE   A CB   
1033 C  CG   . PHE   A 134 ? 0.5927 0.6953 0.6922 0.0008  0.0169  -0.0216 134 PHE   A CG   
1034 C  CD1  . PHE   A 134 ? 0.5711 0.6726 0.6672 -0.0052 0.0188  -0.0202 134 PHE   A CD1  
1035 C  CD2  . PHE   A 134 ? 0.6386 0.7530 0.7468 0.0031  0.0174  -0.0241 134 PHE   A CD2  
1036 C  CE1  . PHE   A 134 ? 0.5744 0.6868 0.6759 -0.0094 0.0216  -0.0210 134 PHE   A CE1  
1037 C  CE2  . PHE   A 134 ? 0.6319 0.7583 0.7461 -0.0006 0.0202  -0.0251 134 PHE   A CE2  
1038 C  CZ   . PHE   A 134 ? 0.6012 0.7267 0.7122 -0.0071 0.0225  -0.0234 134 PHE   A CZ   
1039 N  N    . THR   A 135 ? 0.5575 0.6273 0.6386 0.0142  0.0160  -0.0169 135 THR   A N    
1040 C  CA   . THR   A 135 ? 0.5197 0.5803 0.5948 0.0161  0.0153  -0.0146 135 THR   A CA   
1041 C  C    . THR   A 135 ? 0.4917 0.5497 0.5638 0.0143  0.0173  -0.0135 135 THR   A C    
1042 O  O    . THR   A 135 ? 0.5141 0.5766 0.5886 0.0123  0.0191  -0.0146 135 THR   A O    
1043 C  CB   . THR   A 135 ? 0.5607 0.6189 0.6365 0.0214  0.0151  -0.0144 135 THR   A CB   
1044 O  OG1  . THR   A 135 ? 0.6092 0.6688 0.6870 0.0224  0.0171  -0.0146 135 THR   A OG1  
1045 C  CG2  . THR   A 135 ? 0.5666 0.6288 0.6462 0.0237  0.0134  -0.0163 135 THR   A CG2  
1046 N  N    . ILE   A 136 ? 0.5071 0.5578 0.5740 0.0155  0.0168  -0.0115 136 ILE   A N    
1047 C  CA   . ILE   A 136 ? 0.5313 0.5796 0.5960 0.0149  0.0181  -0.0105 136 ILE   A CA   
1048 C  C    . ILE   A 136 ? 0.5047 0.5498 0.5693 0.0189  0.0182  -0.0089 136 ILE   A C    
1049 O  O    . ILE   A 136 ? 0.5381 0.5804 0.6012 0.0217  0.0174  -0.0078 136 ILE   A O    
1050 C  CB   . ILE   A 136 ? 0.5487 0.5918 0.6066 0.0116  0.0174  -0.0095 136 ILE   A CB   
1051 C  CG1  . ILE   A 136 ? 0.4619 0.4978 0.5137 0.0136  0.0154  -0.0078 136 ILE   A CG1  
1052 C  CG2  . ILE   A 136 ? 0.5185 0.5647 0.5764 0.0067  0.0175  -0.0106 136 ILE   A CG2  
1053 C  CD1  . ILE   A 136 ? 0.4088 0.4379 0.4527 0.0116  0.0145  -0.0068 136 ILE   A CD1  
1054 N  N    . LYS   A 137 ? 0.5123 0.5581 0.5785 0.0191  0.0193  -0.0086 137 LYS   A N    
1055 C  CA   . LYS   A 137 ? 0.5489 0.5927 0.6158 0.0220  0.0196  -0.0067 137 LYS   A CA   
1056 C  C    . LYS   A 137 ? 0.5661 0.6059 0.6283 0.0217  0.0191  -0.0051 137 LYS   A C    
1057 O  O    . LYS   A 137 ? 0.5695 0.6091 0.6311 0.0201  0.0191  -0.0052 137 LYS   A O    
1058 C  CB   . LYS   A 137 ? 0.5850 0.6312 0.6561 0.0221  0.0203  -0.0072 137 LYS   A CB   
1059 C  CG   . LYS   A 137 ? 0.5580 0.6072 0.6324 0.0229  0.0204  -0.0091 137 LYS   A CG   
1060 C  CD   . LYS   A 137 ? 0.5379 0.5874 0.6147 0.0232  0.0206  -0.0095 137 LYS   A CD   
1061 C  CE   . LYS   A 137 ? 0.6687 0.7201 0.7475 0.0250  0.0205  -0.0115 137 LYS   A CE   
1062 N  NZ   . LYS   A 137 ? 0.6784 0.7283 0.7573 0.0277  0.0200  -0.0108 137 LYS   A NZ   
1063 N  N    . GLY   A 138 ? 0.5613 0.5973 0.6194 0.0237  0.0184  -0.0038 138 GLY   A N    
1064 C  CA   . GLY   A 138 ? 0.5438 0.5757 0.5967 0.0244  0.0177  -0.0025 138 GLY   A CA   
1065 C  C    . GLY   A 138 ? 0.4983 0.5299 0.5519 0.0285  0.0184  -0.0002 138 GLY   A C    
1066 O  O    . GLY   A 138 ? 0.4269 0.4619 0.4858 0.0299  0.0197  0.0005  138 GLY   A O    
1067 N  N    . SER   A 139 ? 0.4711 0.4987 0.5190 0.0305  0.0176  0.0009  139 SER   A N    
1068 C  CA   . SER   A 139 ? 0.4685 0.4963 0.5163 0.0351  0.0185  0.0032  139 SER   A CA   
1069 C  C    . SER   A 139 ? 0.4737 0.4944 0.5121 0.0379  0.0172  0.0036  139 SER   A C    
1070 O  O    . SER   A 139 ? 0.5828 0.5987 0.6146 0.0380  0.0155  0.0034  139 SER   A O    
1071 C  CB   . SER   A 139 ? 0.4880 0.5188 0.5385 0.0357  0.0185  0.0040  139 SER   A CB   
1072 O  OG   . SER   A 139 ? 0.5086 0.5416 0.5605 0.0402  0.0199  0.0064  139 SER   A OG   
1073 N  N    . PHE   A 140 ? 0.4854 0.5042 0.5223 0.0403  0.0176  0.0041  140 PHE   A N    
1074 C  CA   . PHE   A 140 ? 0.5139 0.5247 0.5410 0.0430  0.0159  0.0044  140 PHE   A CA   
1075 C  C    . PHE   A 140 ? 0.5415 0.5518 0.5676 0.0486  0.0177  0.0063  140 PHE   A C    
1076 O  O    . PHE   A 140 ? 0.5419 0.5559 0.5735 0.0488  0.0195  0.0067  140 PHE   A O    
1077 C  CB   . PHE   A 140 ? 0.4985 0.5058 0.5230 0.0396  0.0137  0.0025  140 PHE   A CB   
1078 C  CG   . PHE   A 140 ? 0.5092 0.5174 0.5345 0.0338  0.0125  0.0008  140 PHE   A CG   
1079 C  CD1  . PHE   A 140 ? 0.5404 0.5417 0.5571 0.0324  0.0103  0.0007  140 PHE   A CD1  
1080 C  CD2  . PHE   A 140 ? 0.4761 0.4913 0.5096 0.0301  0.0136  -0.0005 140 PHE   A CD2  
1081 C  CE1  . PHE   A 140 ? 0.5222 0.5239 0.5389 0.0267  0.0096  -0.0007 140 PHE   A CE1  
1082 C  CE2  . PHE   A 140 ? 0.5322 0.5484 0.5660 0.0251  0.0131  -0.0020 140 PHE   A CE2  
1083 C  CZ   . PHE   A 140 ? 0.4836 0.4932 0.5091 0.0231  0.0113  -0.0019 140 PHE   A CZ   
1084 N  N    . LEU   A 141 ? 0.5063 0.5113 0.5244 0.0534  0.0173  0.0076  141 LEU   A N    
1085 C  CA   . LEU   A 141 ? 0.5227 0.5258 0.5375 0.0593  0.0191  0.0094  141 LEU   A CA   
1086 C  C    . LEU   A 141 ? 0.5470 0.5396 0.5508 0.0610  0.0162  0.0087  141 LEU   A C    
1087 O  O    . LEU   A 141 ? 0.5557 0.5440 0.5565 0.0568  0.0130  0.0067  141 LEU   A O    
1088 C  CB   . LEU   A 141 ? 0.5109 0.5162 0.5245 0.0646  0.0210  0.0115  141 LEU   A CB   
1089 C  CG   . LEU   A 141 ? 0.5235 0.5399 0.5487 0.0632  0.0237  0.0126  141 LEU   A CG   
1090 C  CD1  . LEU   A 141 ? 0.6095 0.6283 0.6330 0.0689  0.0250  0.0144  141 LEU   A CD1  
1091 C  CD2  . LEU   A 141 ? 0.4615 0.4841 0.4952 0.0620  0.0268  0.0139  141 LEU   A CD2  
1092 N  N    . ASN   A 142 ? 0.5153 0.5038 0.5129 0.0673  0.0175  0.0103  142 ASN   A N    
1093 C  CA   . ASN   A 142 ? 0.5273 0.5045 0.5129 0.0704  0.0146  0.0099  142 ASN   A CA   
1094 C  C    . ASN   A 142 ? 0.5442 0.5123 0.5187 0.0713  0.0111  0.0092  142 ASN   A C    
1095 O  O    . ASN   A 142 ? 0.5619 0.5310 0.5345 0.0748  0.0122  0.0102  142 ASN   A O    
1096 C  CB   . ASN   A 142 ? 0.5801 0.5558 0.5619 0.0776  0.0177  0.0121  142 ASN   A CB   
1097 C  CG   . ASN   A 142 ? 0.6503 0.6331 0.6414 0.0764  0.0210  0.0129  142 ASN   A CG   
1098 O  OD1  . ASN   A 142 ? 0.6386 0.6212 0.6327 0.0725  0.0194  0.0113  142 ASN   A OD1  
1099 N  ND2  . ASN   A 142 ? 0.7452 0.7352 0.7415 0.0794  0.0258  0.0154  142 ASN   A ND2  
1100 N  N    . GLY   A 143 ? 0.5607 0.5201 0.5282 0.0680  0.0066  0.0075  143 GLY   A N    
1101 C  CA   . GLY   A 143 ? 0.5789 0.5293 0.5363 0.0668  0.0027  0.0067  143 GLY   A CA   
1102 C  C    . GLY   A 143 ? 0.5467 0.5020 0.5099 0.0602  0.0023  0.0057  143 GLY   A C    
1103 O  O    . GLY   A 143 ? 0.5489 0.4967 0.5033 0.0597  -0.0004 0.0053  143 GLY   A O    
1104 N  N    . SER   A 144 ? 0.5085 0.4751 0.4850 0.0555  0.0048  0.0052  144 SER   A N    
1105 C  CA   . SER   A 144 ? 0.5239 0.4937 0.5046 0.0487  0.0040  0.0039  144 SER   A CA   
1106 C  C    . SER   A 144 ? 0.5579 0.5229 0.5354 0.0425  0.0006  0.0023  144 SER   A C    
1107 O  O    . SER   A 144 ? 0.5454 0.5115 0.5241 0.0365  -0.0002 0.0014  144 SER   A O    
1108 C  CB   . SER   A 144 ? 0.5302 0.5128 0.5252 0.0461  0.0076  0.0037  144 SER   A CB   
1109 O  OG   . SER   A 144 ? 0.5491 0.5358 0.5500 0.0461  0.0087  0.0035  144 SER   A OG   
1110 N  N    . CYS   A 145 ? 0.5100 0.4703 0.4838 0.0435  -0.0015 0.0021  145 CYS   A N    
1111 C  CA   . CYS   A 145 ? 0.5249 0.4810 0.4960 0.0375  -0.0053 0.0008  145 CYS   A CA   
1112 C  C    . CYS   A 145 ? 0.5124 0.4575 0.4714 0.0348  -0.0088 0.0008  145 CYS   A C    
1113 O  O    . CYS   A 145 ? 0.5085 0.4446 0.4568 0.0398  -0.0098 0.0017  145 CYS   A O    
1114 C  CB   . CYS   A 145 ? 0.5647 0.5169 0.5333 0.0399  -0.0075 0.0005  145 CYS   A CB   
1115 S  SG   . CYS   A 145 ? 0.5657 0.5057 0.5206 0.0497  -0.0086 0.0020  145 CYS   A SG   
1116 N  N    . GLY   A 146 ? 0.5153 0.4617 0.4765 0.0267  -0.0104 -0.0002 146 GLY   A N    
1117 C  CA   . GLY   A 146 ? 0.5433 0.4802 0.4942 0.0226  -0.0132 -0.0001 146 GLY   A CA   
1118 C  C    . GLY   A 146 ? 0.5457 0.4869 0.4995 0.0206  -0.0104 0.0000  146 GLY   A C    
1119 O  O    . GLY   A 146 ? 0.5535 0.4874 0.4994 0.0158  -0.0124 0.0000  146 GLY   A O    
1120 N  N    . SER   A 147 ? 0.4789 0.4306 0.4427 0.0239  -0.0062 0.0001  147 SER   A N    
1121 C  CA   . SER   A 147 ? 0.4358 0.3918 0.4029 0.0218  -0.0040 0.0000  147 SER   A CA   
1122 C  C    . SER   A 147 ? 0.4719 0.4345 0.4459 0.0136  -0.0030 -0.0011 147 SER   A C    
1123 O  O    . SER   A 147 ? 0.4813 0.4506 0.4631 0.0108  -0.0026 -0.0018 147 SER   A O    
1124 C  CB   . SER   A 147 ? 0.4460 0.4118 0.4228 0.0269  -0.0003 0.0004  147 SER   A CB   
1125 O  OG   . SER   A 147 ? 0.4845 0.4455 0.4553 0.0345  -0.0007 0.0016  147 SER   A OG   
1126 N  N    . VAL   A 148 ? 0.4345 0.3951 0.4054 0.0099  -0.0026 -0.0012 148 VAL   A N    
1127 C  CA   . VAL   A 148 ? 0.4569 0.4219 0.4315 0.0018  -0.0017 -0.0019 148 VAL   A CA   
1128 C  C    . VAL   A 148 ? 0.4605 0.4341 0.4428 0.0006  0.0020  -0.0025 148 VAL   A C    
1129 O  O    . VAL   A 148 ? 0.3976 0.3714 0.3801 0.0052  0.0029  -0.0022 148 VAL   A O    
1130 C  CB   . VAL   A 148 ? 0.4320 0.3846 0.3934 -0.0038 -0.0049 -0.0014 148 VAL   A CB   
1131 C  CG1  . VAL   A 148 ? 0.4938 0.4367 0.4468 -0.0027 -0.0092 -0.0009 148 VAL   A CG1  
1132 C  CG2  . VAL   A 148 ? 0.3894 0.3329 0.3404 -0.0020 -0.0055 -0.0009 148 VAL   A CG2  
1133 N  N    . GLY   A 149 ? 0.4208 0.4018 0.4096 -0.0055 0.0039  -0.0033 149 GLY   A N    
1134 C  CA   . GLY   A 149 ? 0.4272 0.4155 0.4221 -0.0071 0.0072  -0.0040 149 GLY   A CA   
1135 C  C    . GLY   A 149 ? 0.4900 0.4747 0.4790 -0.0144 0.0077  -0.0039 149 GLY   A C    
1136 O  O    . GLY   A 149 ? 0.4578 0.4407 0.4443 -0.0197 0.0064  -0.0036 149 GLY   A O    
1137 N  N    . PHE   A 150 ? 0.4571 0.4409 0.4438 -0.0148 0.0094  -0.0041 150 PHE   A N    
1138 C  CA   . PHE   A 150 ? 0.5023 0.4798 0.4803 -0.0211 0.0097  -0.0036 150 PHE   A CA   
1139 C  C    . PHE   A 150 ? 0.5462 0.5283 0.5269 -0.0219 0.0131  -0.0044 150 PHE   A C    
1140 O  O    . PHE   A 150 ? 0.5012 0.4871 0.4869 -0.0168 0.0138  -0.0051 150 PHE   A O    
1141 C  CB   . PHE   A 150 ? 0.4587 0.4203 0.4212 -0.0204 0.0060  -0.0026 150 PHE   A CB   
1142 C  CG   . PHE   A 150 ? 0.4674 0.4248 0.4269 -0.0127 0.0047  -0.0026 150 PHE   A CG   
1143 C  CD1  . PHE   A 150 ? 0.4703 0.4297 0.4337 -0.0060 0.0033  -0.0025 150 PHE   A CD1  
1144 C  CD2  . PHE   A 150 ? 0.4485 0.4000 0.4009 -0.0121 0.0046  -0.0028 150 PHE   A CD2  
1145 C  CE1  . PHE   A 150 ? 0.4509 0.4081 0.4127 0.0008  0.0023  -0.0024 150 PHE   A CE1  
1146 C  CE2  . PHE   A 150 ? 0.4558 0.4045 0.4063 -0.0052 0.0030  -0.0029 150 PHE   A CE2  
1147 C  CZ   . PHE   A 150 ? 0.4857 0.4380 0.4415 0.0012  0.0019  -0.0026 150 PHE   A CZ   
1148 N  N    . ASN   A 151 ? 0.5063 0.4875 0.4831 -0.0285 0.0150  -0.0041 151 ASN   A N    
1149 C  CA   . ASN   A 151 ? 0.6107 0.5897 0.5831 -0.0296 0.0172  -0.0044 151 ASN   A CA   
1150 C  C    . ASN   A 151 ? 0.6259 0.5894 0.5818 -0.0330 0.0150  -0.0032 151 ASN   A C    
1151 O  O    . ASN   A 151 ? 0.5922 0.5510 0.5426 -0.0389 0.0141  -0.0021 151 ASN   A O    
1152 C  CB   . ASN   A 151 ? 0.6089 0.5992 0.5890 -0.0341 0.0219  -0.0051 151 ASN   A CB   
1153 C  CG   . ASN   A 151 ? 0.5560 0.5589 0.5494 -0.0292 0.0240  -0.0067 151 ASN   A CG   
1154 O  OD1  . ASN   A 151 ? 0.5557 0.5692 0.5594 -0.0296 0.0252  -0.0073 151 ASN   A OD1  
1155 N  ND2  . ASN   A 151 ? 0.5444 0.5455 0.5371 -0.0247 0.0240  -0.0074 151 ASN   A ND2  
1156 N  N    . ILE   A 152 ? 0.6227 0.5777 0.5706 -0.0292 0.0136  -0.0034 152 ILE   A N    
1157 C  CA   . ILE   A 152 ? 0.7242 0.6643 0.6557 -0.0325 0.0121  -0.0025 152 ILE   A CA   
1158 C  C    . ILE   A 152 ? 0.7646 0.7060 0.6943 -0.0353 0.0157  -0.0029 152 ILE   A C    
1159 O  O    . ILE   A 152 ? 0.7316 0.6698 0.6585 -0.0309 0.0151  -0.0037 152 ILE   A O    
1160 C  CB   . ILE   A 152 ? 0.6564 0.5842 0.5776 -0.0262 0.0074  -0.0025 152 ILE   A CB   
1161 C  CG1  . ILE   A 152 ? 0.6103 0.5364 0.5322 -0.0227 0.0041  -0.0020 152 ILE   A CG1  
1162 C  CG2  . ILE   A 152 ? 0.6690 0.5799 0.5715 -0.0298 0.0056  -0.0016 152 ILE   A CG2  
1163 C  CD1  . ILE   A 152 ? 0.5880 0.5043 0.5013 -0.0153 0.0000  -0.0021 152 ILE   A CD1  
1164 N  N    . ASP   A 153 ? 0.8356 0.7823 0.7673 -0.0424 0.0196  -0.0023 153 ASP   A N    
1165 C  CA   . ASP   A 153 ? 0.9284 0.8753 0.8564 -0.0456 0.0236  -0.0024 153 ASP   A CA   
1166 C  C    . ASP   A 153 ? 0.9656 0.8999 0.8785 -0.0532 0.0237  -0.0006 153 ASP   A C    
1167 O  O    . ASP   A 153 ? 1.0672 0.9996 0.9785 -0.0584 0.0225  0.0007  153 ASP   A O    
1168 C  CB   . ASP   A 153 ? 0.9267 0.8909 0.8691 -0.0475 0.0288  -0.0032 153 ASP   A CB   
1169 C  CG   . ASP   A 153 ? 0.9545 0.9288 0.9093 -0.0400 0.0289  -0.0051 153 ASP   A CG   
1170 O  OD1  . ASP   A 153 ? 0.9822 0.9507 0.9334 -0.0346 0.0268  -0.0059 153 ASP   A OD1  
1171 O  OD2  . ASP   A 153 ? 0.8842 0.8719 0.8523 -0.0396 0.0307  -0.0058 153 ASP   A OD2  
1172 N  N    . TYR   A 154 ? 0.9294 0.8540 0.8303 -0.0538 0.0247  -0.0005 154 TYR   A N    
1173 C  CA   . TYR   A 154 ? 0.9614 0.8738 0.8472 -0.0616 0.0255  0.0014  154 TYR   A CA   
1174 C  C    . TYR   A 154 ? 0.9369 0.8356 0.8118 -0.0634 0.0201  0.0027  154 TYR   A C    
1175 O  O    . TYR   A 154 ? 0.8655 0.7619 0.7371 -0.0714 0.0206  0.0045  154 TYR   A O    
1176 C  CB   . TYR   A 154 ? 0.8458 0.7704 0.7391 -0.0697 0.0316  0.0025  154 TYR   A CB   
1177 N  N    . ASP   A 155 ? 0.8471 0.7373 0.7173 -0.0556 0.0148  0.0018  155 ASP   A N    
1178 C  CA   . ASP   A 155 ? 0.8501 0.7237 0.7059 -0.0553 0.0091  0.0027  155 ASP   A CA   
1179 C  C    . ASP   A 155 ? 0.8583 0.7362 0.7207 -0.0569 0.0070  0.0033  155 ASP   A C    
1180 O  O    . ASP   A 155 ? 0.7685 0.6341 0.6211 -0.0546 0.0018  0.0037  155 ASP   A O    
1181 C  CB   . ASP   A 155 ? 0.7968 0.6535 0.6333 -0.0626 0.0091  0.0044  155 ASP   A CB   
1182 C  CG   . ASP   A 155 ? 0.8310 0.6690 0.6510 -0.0630 0.0030  0.0055  155 ASP   A CG   
1183 O  OD1  . ASP   A 155 ? 0.8092 0.6379 0.6220 -0.0546 -0.0018 0.0043  155 ASP   A OD1  
1184 O  OD2  . ASP   A 155 ? 0.8412 0.6742 0.6557 -0.0716 0.0028  0.0074  155 ASP   A OD2  
1185 N  N    . CYS   A 156 ? 0.8353 0.7302 0.7139 -0.0603 0.0108  0.0033  156 CYS   A N    
1186 C  CA   . CYS   A 156 ? 0.7457 0.6452 0.6305 -0.0635 0.0092  0.0040  156 CYS   A CA   
1187 C  C    . CYS   A 156 ? 0.7411 0.6553 0.6430 -0.0563 0.0093  0.0024  156 CYS   A C    
1188 O  O    . CYS   A 156 ? 0.6544 0.5828 0.5693 -0.0540 0.0133  0.0012  156 CYS   A O    
1189 C  CB   . CYS   A 156 ? 0.6942 0.6011 0.5832 -0.0741 0.0133  0.0054  156 CYS   A CB   
1190 S  SG   . CYS   A 156 ? 0.7228 0.6370 0.6208 -0.0793 0.0113  0.0062  156 CYS   A SG   
1191 N  N    . VAL   A 157 ? 0.7042 0.6138 0.6047 -0.0525 0.0047  0.0024  157 VAL   A N    
1192 C  CA   . VAL   A 157 ? 0.6260 0.5476 0.5409 -0.0460 0.0045  0.0012  157 VAL   A CA   
1193 C  C    . VAL   A 157 ? 0.6240 0.5590 0.5518 -0.0513 0.0065  0.0013  157 VAL   A C    
1194 O  O    . VAL   A 157 ? 0.5991 0.5292 0.5226 -0.0566 0.0039  0.0024  157 VAL   A O    
1195 C  CB   . VAL   A 157 ? 0.6326 0.5436 0.5398 -0.0394 -0.0008 0.0013  157 VAL   A CB   
1196 C  CG1  . VAL   A 157 ? 0.5190 0.4423 0.4406 -0.0331 -0.0006 0.0003  157 VAL   A CG1  
1197 C  CG2  . VAL   A 157 ? 0.6513 0.5509 0.5471 -0.0332 -0.0030 0.0009  157 VAL   A CG2  
1198 N  N    . SER   A 158 ? 0.6054 0.5572 0.5489 -0.0495 0.0106  0.0001  158 SER   A N    
1199 C  CA   . SER   A 158 ? 0.5644 0.5309 0.5220 -0.0529 0.0125  -0.0003 158 SER   A CA   
1200 C  C    . SER   A 158 ? 0.5285 0.5002 0.4946 -0.0457 0.0103  -0.0013 158 SER   A C    
1201 O  O    . SER   A 158 ? 0.5122 0.4920 0.4871 -0.0395 0.0121  -0.0026 158 SER   A O    
1202 C  CB   . SER   A 158 ? 0.5151 0.4960 0.4833 -0.0548 0.0182  -0.0012 158 SER   A CB   
1203 O  OG   . SER   A 158 ? 0.6805 0.6587 0.6422 -0.0628 0.0208  0.0001  158 SER   A OG   
1204 N  N    . PHE   A 159 ? 0.5507 0.5168 0.5134 -0.0466 0.0062  -0.0007 159 PHE   A N    
1205 C  CA   . PHE   A 159 ? 0.4972 0.4676 0.4670 -0.0401 0.0043  -0.0015 159 PHE   A CA   
1206 C  C    . PHE   A 159 ? 0.4798 0.4673 0.4659 -0.0414 0.0070  -0.0027 159 PHE   A C    
1207 O  O    . PHE   A 159 ? 0.5290 0.5224 0.5190 -0.0487 0.0077  -0.0024 159 PHE   A O    
1208 C  CB   . PHE   A 159 ? 0.4649 0.4225 0.4244 -0.0402 -0.0011 -0.0006 159 PHE   A CB   
1209 C  CG   . PHE   A 159 ? 0.4906 0.4318 0.4345 -0.0359 -0.0040 0.0001  159 PHE   A CG   
1210 C  CD1  . PHE   A 159 ? 0.4695 0.4105 0.4144 -0.0266 -0.0039 -0.0004 159 PHE   A CD1  
1211 C  CD2  . PHE   A 159 ? 0.5647 0.4910 0.4933 -0.0410 -0.0067 0.0013  159 PHE   A CD2  
1212 C  CE1  . PHE   A 159 ? 0.4380 0.3657 0.3697 -0.0219 -0.0065 0.0000  159 PHE   A CE1  
1213 C  CE2  . PHE   A 159 ? 0.5724 0.4835 0.4862 -0.0360 -0.0096 0.0017  159 PHE   A CE2  
1214 C  CZ   . PHE   A 159 ? 0.5067 0.4191 0.4226 -0.0261 -0.0095 0.0010  159 PHE   A CZ   
1215 N  N    . CYS   A 160 ? 0.4486 0.4445 0.4442 -0.0346 0.0085  -0.0039 160 CYS   A N    
1216 C  CA   . CYS   A 160 ? 0.4320 0.4431 0.4421 -0.0344 0.0104  -0.0052 160 CYS   A CA   
1217 C  C    . CYS   A 160 ? 0.4923 0.5052 0.5074 -0.0278 0.0082  -0.0059 160 CYS   A C    
1218 O  O    . CYS   A 160 ? 0.4473 0.4697 0.4719 -0.0284 0.0080  -0.0069 160 CYS   A O    
1219 C  CB   . CYS   A 160 ? 0.4017 0.4231 0.4196 -0.0332 0.0153  -0.0064 160 CYS   A CB   
1220 S  SG   . CYS   A 160 ? 0.4415 0.4600 0.4586 -0.0248 0.0162  -0.0068 160 CYS   A SG   
1221 N  N    . TYR   A 161 ? 0.4406 0.4450 0.4497 -0.0216 0.0065  -0.0054 161 TYR   A N    
1222 C  CA   . TYR   A 161 ? 0.4936 0.5002 0.5075 -0.0150 0.0054  -0.0058 161 TYR   A CA   
1223 C  C    . TYR   A 161 ? 0.4377 0.4313 0.4406 -0.0116 0.0015  -0.0047 161 TYR   A C    
1224 O  O    . TYR   A 161 ? 0.4747 0.4588 0.4679 -0.0100 0.0007  -0.0037 161 TYR   A O    
1225 C  CB   . TYR   A 161 ? 0.4612 0.4734 0.4812 -0.0094 0.0084  -0.0063 161 TYR   A CB   
1226 C  CG   . TYR   A 161 ? 0.4325 0.4476 0.4577 -0.0033 0.0080  -0.0066 161 TYR   A CG   
1227 C  CD1  . TYR   A 161 ? 0.4152 0.4385 0.4488 -0.0036 0.0079  -0.0078 161 TYR   A CD1  
1228 C  CD2  . TYR   A 161 ? 0.4265 0.4366 0.4484 0.0028  0.0077  -0.0056 161 TYR   A CD2  
1229 C  CE1  . TYR   A 161 ? 0.4769 0.5017 0.5142 0.0020  0.0074  -0.0080 161 TYR   A CE1  
1230 C  CE2  . TYR   A 161 ? 0.3863 0.3988 0.4125 0.0081  0.0078  -0.0056 161 TYR   A CE2  
1231 C  CZ   . TYR   A 161 ? 0.4307 0.4497 0.4639 0.0076  0.0076  -0.0068 161 TYR   A CZ   
1232 O  OH   . TYR   A 161 ? 0.4060 0.4262 0.4423 0.0128  0.0075  -0.0068 161 TYR   A OH   
1233 N  N    . MET   A 162 ? 0.4620 0.4547 0.4657 -0.0101 -0.0012 -0.0049 162 MET   A N    
1234 C  CA   . MET   A 162 ? 0.5145 0.4969 0.5097 -0.0040 -0.0040 -0.0040 162 MET   A CA   
1235 C  C    . MET   A 162 ? 0.4297 0.4187 0.4329 0.0024  -0.0026 -0.0045 162 MET   A C    
1236 O  O    . MET   A 162 ? 0.3708 0.3687 0.3833 0.0014  -0.0021 -0.0057 162 MET   A O    
1237 C  CB   . MET   A 162 ? 0.4475 0.4196 0.4335 -0.0064 -0.0091 -0.0036 162 MET   A CB   
1238 C  CG   . MET   A 162 ? 0.4846 0.4430 0.4577 0.0003  -0.0116 -0.0025 162 MET   A CG   
1239 S  SD   . MET   A 162 ? 0.5071 0.4478 0.4636 -0.0022 -0.0183 -0.0018 162 MET   A SD   
1240 C  CE   . MET   A 162 ? 0.4255 0.3745 0.3917 -0.0081 -0.0205 -0.0029 162 MET   A CE   
1241 N  N    . HIS   A 163 ? 0.4417 0.4264 0.4411 0.0091  -0.0019 -0.0036 163 HIS   A N    
1242 C  CA   . HIS   A 163 ? 0.4768 0.4668 0.4827 0.0148  -0.0002 -0.0036 163 HIS   A CA   
1243 C  C    . HIS   A 163 ? 0.4469 0.4302 0.4474 0.0181  -0.0034 -0.0034 163 HIS   A C    
1244 O  O    . HIS   A 163 ? 0.4222 0.3940 0.4111 0.0194  -0.0065 -0.0026 163 HIS   A O    
1245 C  CB   . HIS   A 163 ? 0.4752 0.4651 0.4808 0.0203  0.0024  -0.0025 163 HIS   A CB   
1246 C  CG   . HIS   A 163 ? 0.4878 0.4838 0.5007 0.0251  0.0046  -0.0022 163 HIS   A CG   
1247 N  ND1  . HIS   A 163 ? 0.4819 0.4875 0.5053 0.0235  0.0065  -0.0034 163 HIS   A ND1  
1248 C  CD2  . HIS   A 163 ? 0.4905 0.4839 0.5010 0.0314  0.0055  -0.0008 163 HIS   A CD2  
1249 C  CE1  . HIS   A 163 ? 0.4915 0.4991 0.5181 0.0283  0.0080  -0.0028 163 HIS   A CE1  
1250 N  NE2  . HIS   A 163 ? 0.5368 0.5376 0.5562 0.0329  0.0078  -0.0011 163 HIS   A NE2  
1251 N  N    . HIS   A 164 ? 0.4067 0.3963 0.4147 0.0198  -0.0029 -0.0043 164 HIS   A N    
1252 C  CA   . HIS   A 164 ? 0.5007 0.4842 0.5040 0.0234  -0.0059 -0.0043 164 HIS   A CA   
1253 C  C    . HIS   A 164 ? 0.5253 0.5104 0.5309 0.0304  -0.0035 -0.0036 164 HIS   A C    
1254 O  O    . HIS   A 164 ? 0.4976 0.4741 0.4945 0.0358  -0.0043 -0.0023 164 HIS   A O    
1255 C  CB   . HIS   A 164 ? 0.4672 0.4552 0.4758 0.0190  -0.0087 -0.0060 164 HIS   A CB   
1256 C  CG   . HIS   A 164 ? 0.4235 0.4073 0.4274 0.0123  -0.0122 -0.0062 164 HIS   A CG   
1257 N  ND1  . HIS   A 164 ? 0.4565 0.4323 0.4538 0.0111  -0.0175 -0.0065 164 HIS   A ND1  
1258 C  CD2  . HIS   A 164 ? 0.4372 0.4230 0.4416 0.0061  -0.0113 -0.0061 164 HIS   A CD2  
1259 C  CE1  . HIS   A 164 ? 0.5078 0.4811 0.5020 0.0040  -0.0198 -0.0063 164 HIS   A CE1  
1260 N  NE2  . HIS   A 164 ? 0.4637 0.4429 0.4620 0.0008  -0.0158 -0.0061 164 HIS   A NE2  
1261 N  N    . MET   A 165 ? 0.4667 0.4619 0.4830 0.0304  -0.0005 -0.0043 165 MET   A N    
1262 C  CA   . MET   A 165 ? 0.5082 0.5044 0.5267 0.0357  0.0009  -0.0040 165 MET   A CA   
1263 C  C    . MET   A 165 ? 0.5094 0.5145 0.5371 0.0361  0.0050  -0.0039 165 MET   A C    
1264 O  O    . MET   A 165 ? 0.5154 0.5280 0.5502 0.0319  0.0060  -0.0051 165 MET   A O    
1265 C  CB   . MET   A 165 ? 0.4692 0.4660 0.4895 0.0354  -0.0023 -0.0057 165 MET   A CB   
1266 C  CG   . MET   A 165 ? 0.4524 0.4600 0.4834 0.0308  -0.0022 -0.0079 165 MET   A CG   
1267 S  SD   . MET   A 165 ? 0.4834 0.4924 0.5166 0.0298  -0.0071 -0.0102 165 MET   A SD   
1268 C  CE   . MET   A 165 ? 0.6008 0.6015 0.6278 0.0377  -0.0081 -0.0096 165 MET   A CE   
1269 N  N    . GLU   A 166 ? 0.4711 0.4748 0.4979 0.0410  0.0075  -0.0022 166 GLU   A N    
1270 C  CA   . GLU   A 166 ? 0.5070 0.5179 0.5420 0.0413  0.0106  -0.0021 166 GLU   A CA   
1271 C  C    . GLU   A 166 ? 0.5436 0.5553 0.5810 0.0430  0.0096  -0.0034 166 GLU   A C    
1272 O  O    . GLU   A 166 ? 0.5359 0.5415 0.5676 0.0457  0.0072  -0.0035 166 GLU   A O    
1273 C  CB   . GLU   A 166 ? 0.4864 0.4965 0.5205 0.0449  0.0138  0.0005  166 GLU   A CB   
1274 C  CG   . GLU   A 166 ? 0.4805 0.4972 0.5226 0.0443  0.0166  0.0008  166 GLU   A CG   
1275 C  CD   . GLU   A 166 ? 0.5109 0.5285 0.5536 0.0465  0.0197  0.0036  166 GLU   A CD   
1276 O  OE1  . GLU   A 166 ? 0.4604 0.4782 0.5044 0.0489  0.0217  0.0051  166 GLU   A OE1  
1277 O  OE2  . GLU   A 166 ? 0.4902 0.5085 0.5320 0.0457  0.0199  0.0042  166 GLU   A OE2  
1278 N  N    . LEU   A 167 ? 0.5596 0.5780 0.6046 0.0417  0.0110  -0.0045 167 LEU   A N    
1279 C  CA   . LEU   A 167 ? 0.5625 0.5816 0.6096 0.0438  0.0099  -0.0059 167 LEU   A CA   
1280 C  C    . LEU   A 167 ? 0.5903 0.6071 0.6367 0.0474  0.0125  -0.0041 167 LEU   A C    
1281 O  O    . LEU   A 167 ? 0.5719 0.5889 0.6186 0.0475  0.0154  -0.0018 167 LEU   A O    
1282 C  CB   . LEU   A 167 ? 0.5661 0.5935 0.6211 0.0406  0.0093  -0.0086 167 LEU   A CB   
1283 C  CG   . LEU   A 167 ? 0.5395 0.5709 0.5965 0.0363  0.0071  -0.0105 167 LEU   A CG   
1284 C  CD1  . LEU   A 167 ? 0.5563 0.5968 0.6212 0.0344  0.0072  -0.0131 167 LEU   A CD1  
1285 C  CD2  . LEU   A 167 ? 0.6217 0.6479 0.6736 0.0370  0.0033  -0.0109 167 LEU   A CD2  
1286 N  N    . PRO   A 168 ? 0.6704 0.6845 0.7155 0.0504  0.0115  -0.0048 168 PRO   A N    
1287 C  CA   . PRO   A 168 ? 0.6780 0.6892 0.7219 0.0532  0.0141  -0.0028 168 PRO   A CA   
1288 C  C    . PRO   A 168 ? 0.6968 0.7136 0.7473 0.0506  0.0164  -0.0026 168 PRO   A C    
1289 O  O    . PRO   A 168 ? 0.7309 0.7465 0.7813 0.0511  0.0193  0.0000  168 PRO   A O    
1290 C  CB   . PRO   A 168 ? 0.7007 0.7078 0.7417 0.0565  0.0117  -0.0045 168 PRO   A CB   
1291 C  CG   . PRO   A 168 ? 0.7012 0.7119 0.7448 0.0548  0.0077  -0.0077 168 PRO   A CG   
1292 C  CD   . PRO   A 168 ? 0.6759 0.6879 0.7190 0.0518  0.0075  -0.0071 168 PRO   A CD   
1293 N  N    . THR   A 169 ? 0.6412 0.6640 0.6973 0.0477  0.0152  -0.0052 169 THR   A N    
1294 C  CA   . THR   A 169 ? 0.6539 0.6812 0.7153 0.0451  0.0169  -0.0053 169 THR   A CA   
1295 C  C    . THR   A 169 ? 0.6146 0.6435 0.6770 0.0428  0.0190  -0.0030 169 THR   A C    
1296 O  O    . THR   A 169 ? 0.6361 0.6673 0.7020 0.0410  0.0203  -0.0023 169 THR   A O    
1297 C  CB   . THR   A 169 ? 0.6749 0.7085 0.7410 0.0429  0.0153  -0.0086 169 THR   A CB   
1298 O  OG1  . THR   A 169 ? 0.7799 0.8167 0.8498 0.0408  0.0167  -0.0088 169 THR   A OG1  
1299 C  CG2  . THR   A 169 ? 0.6182 0.6544 0.6844 0.0403  0.0143  -0.0094 169 THR   A CG2  
1300 N  N    . GLY   A 170 ? 0.5626 0.5896 0.6214 0.0432  0.0190  -0.0018 170 GLY   A N    
1301 C  CA   . GLY   A 170 ? 0.5638 0.5923 0.6233 0.0417  0.0205  0.0000  170 GLY   A CA   
1302 C  C    . GLY   A 170 ? 0.4918 0.5239 0.5534 0.0380  0.0196  -0.0017 170 GLY   A C    
1303 O  O    . GLY   A 170 ? 0.4770 0.5106 0.5395 0.0366  0.0206  -0.0005 170 GLY   A O    
1304 N  N    . VAL   A 171 ? 0.4645 0.4986 0.5272 0.0363  0.0178  -0.0043 171 VAL   A N    
1305 C  CA   . VAL   A 171 ? 0.5396 0.5767 0.6032 0.0325  0.0172  -0.0056 171 VAL   A CA   
1306 C  C    . VAL   A 171 ? 0.5395 0.5733 0.5982 0.0320  0.0152  -0.0058 171 VAL   A C    
1307 O  O    . VAL   A 171 ? 0.4831 0.5124 0.5378 0.0349  0.0140  -0.0053 171 VAL   A O    
1308 C  CB   . VAL   A 171 ? 0.4956 0.5385 0.5644 0.0303  0.0171  -0.0083 171 VAL   A CB   
1309 C  CG1  . VAL   A 171 ? 0.5378 0.5822 0.6100 0.0312  0.0184  -0.0082 171 VAL   A CG1  
1310 C  CG2  . VAL   A 171 ? 0.5598 0.6043 0.6293 0.0310  0.0152  -0.0102 171 VAL   A CG2  
1311 N  N    . HIS   A 172 ? 0.5078 0.5430 0.5660 0.0281  0.0146  -0.0067 172 HIS   A N    
1312 C  CA   . HIS   A 172 ? 0.4638 0.4940 0.5156 0.0267  0.0128  -0.0062 172 HIS   A CA   
1313 C  C    . HIS   A 172 ? 0.4808 0.5141 0.5341 0.0224  0.0111  -0.0081 172 HIS   A C    
1314 O  O    . HIS   A 172 ? 0.4456 0.4850 0.5035 0.0191  0.0123  -0.0094 172 HIS   A O    
1315 C  CB   . HIS   A 172 ? 0.4540 0.4816 0.5024 0.0258  0.0137  -0.0048 172 HIS   A CB   
1316 C  CG   . HIS   A 172 ? 0.5188 0.5450 0.5669 0.0299  0.0154  -0.0027 172 HIS   A CG   
1317 N  ND1  . HIS   A 172 ? 0.5034 0.5335 0.5563 0.0297  0.0173  -0.0022 172 HIS   A ND1  
1318 C  CD2  . HIS   A 172 ? 0.5045 0.5261 0.5482 0.0343  0.0154  -0.0009 172 HIS   A CD2  
1319 C  CE1  . HIS   A 172 ? 0.4915 0.5205 0.5440 0.0332  0.0185  -0.0001 172 HIS   A CE1  
1320 N  NE2  . HIS   A 172 ? 0.4848 0.5088 0.5316 0.0363  0.0177  0.0008  172 HIS   A NE2  
1321 N  N    . ALA   A 173 ? 0.4688 0.4979 0.5180 0.0225  0.0082  -0.0083 173 ALA   A N    
1322 C  CA   . ALA   A 173 ? 0.4707 0.5034 0.5220 0.0181  0.0061  -0.0099 173 ALA   A CA   
1323 C  C    . ALA   A 173 ? 0.4391 0.4640 0.4821 0.0151  0.0035  -0.0090 173 ALA   A C    
1324 O  O    . ALA   A 173 ? 0.4100 0.4257 0.4447 0.0181  0.0021  -0.0075 173 ALA   A O    
1325 C  CB   . ALA   A 173 ? 0.4773 0.5125 0.5321 0.0203  0.0040  -0.0114 173 ALA   A CB   
1326 N  N    . GLY   A 174 ? 0.4294 0.4581 0.4743 0.0091  0.0028  -0.0098 174 GLY   A N    
1327 C  CA   . GLY   A 174 ? 0.4538 0.4746 0.4903 0.0052  0.0001  -0.0089 174 GLY   A CA   
1328 C  C    . GLY   A 174 ? 0.4817 0.5086 0.5224 -0.0020 -0.0008 -0.0099 174 GLY   A C    
1329 O  O    . GLY   A 174 ? 0.4416 0.4793 0.4920 -0.0031 -0.0002 -0.0116 174 GLY   A O    
1330 N  N    . THR   A 175 ? 0.4948 0.5147 0.5277 -0.0070 -0.0022 -0.0089 175 THR   A N    
1331 C  CA   . THR   A 175 ? 0.5043 0.5271 0.5385 -0.0148 -0.0040 -0.0091 175 THR   A CA   
1332 C  C    . THR   A 175 ? 0.4982 0.5190 0.5281 -0.0204 -0.0019 -0.0081 175 THR   A C    
1333 O  O    . THR   A 175 ? 0.4609 0.4740 0.4833 -0.0181 -0.0007 -0.0071 175 THR   A O    
1334 C  CB   . THR   A 175 ? 0.4955 0.5077 0.5214 -0.0159 -0.0098 -0.0085 175 THR   A CB   
1335 O  OG1  . THR   A 175 ? 0.4112 0.4085 0.4230 -0.0151 -0.0114 -0.0068 175 THR   A OG1  
1336 C  CG2  . THR   A 175 ? 0.4793 0.4911 0.5071 -0.0095 -0.0120 -0.0094 175 THR   A CG2  
1337 N  N    . ASP   A 176 ? 0.4808 0.5082 0.5149 -0.0280 -0.0016 -0.0084 176 ASP   A N    
1338 C  CA   . ASP   A 176 ? 0.5014 0.5231 0.5279 -0.0345 -0.0008 -0.0070 176 ASP   A CA   
1339 C  C    . ASP   A 176 ? 0.5090 0.5141 0.5215 -0.0359 -0.0060 -0.0055 176 ASP   A C    
1340 O  O    . ASP   A 176 ? 0.5101 0.5088 0.5191 -0.0311 -0.0096 -0.0056 176 ASP   A O    
1341 C  CB   . ASP   A 176 ? 0.5424 0.5763 0.5774 -0.0425 0.0015  -0.0073 176 ASP   A CB   
1342 C  CG   . ASP   A 176 ? 0.5207 0.5595 0.5610 -0.0470 -0.0023 -0.0077 176 ASP   A CG   
1343 O  OD1  . ASP   A 176 ? 0.4992 0.5270 0.5318 -0.0471 -0.0077 -0.0070 176 ASP   A OD1  
1344 O  OD2  . ASP   A 176 ? 0.5505 0.6046 0.6027 -0.0508 -0.0001 -0.0086 176 ASP   A OD2  
1345 N  N    . LEU   A 177 ? 0.5230 0.5200 0.5263 -0.0423 -0.0065 -0.0041 177 LEU   A N    
1346 C  CA   . LEU   A 177 ? 0.4984 0.4781 0.4866 -0.0441 -0.0118 -0.0027 177 LEU   A CA   
1347 C  C    . LEU   A 177 ? 0.5122 0.4917 0.5008 -0.0520 -0.0160 -0.0024 177 LEU   A C    
1348 O  O    . LEU   A 177 ? 0.5980 0.5620 0.5732 -0.0542 -0.0212 -0.0012 177 LEU   A O    
1349 C  CB   . LEU   A 177 ? 0.4833 0.4511 0.4584 -0.0464 -0.0111 -0.0014 177 LEU   A CB   
1350 C  CG   . LEU   A 177 ? 0.4688 0.4283 0.4363 -0.0377 -0.0104 -0.0013 177 LEU   A CG   
1351 C  CD1  . LEU   A 177 ? 0.5418 0.4901 0.5009 -0.0313 -0.0149 -0.0011 177 LEU   A CD1  
1352 C  CD2  . LEU   A 177 ? 0.4518 0.4242 0.4312 -0.0322 -0.0053 -0.0024 177 LEU   A CD2  
1353 N  N    . GLU   A 178 ? 0.5212 0.5171 0.5244 -0.0563 -0.0143 -0.0033 178 GLU   A N    
1354 C  CA   . GLU   A 178 ? 0.5909 0.5890 0.5974 -0.0622 -0.0190 -0.0033 178 GLU   A CA   
1355 C  C    . GLU   A 178 ? 0.6818 0.6834 0.6944 -0.0553 -0.0221 -0.0050 178 GLU   A C    
1356 O  O    . GLU   A 178 ? 0.6831 0.6886 0.7007 -0.0590 -0.0262 -0.0055 178 GLU   A O    
1357 C  CB   . GLU   A 178 ? 0.5592 0.5742 0.5786 -0.0709 -0.0158 -0.0034 178 GLU   A CB   
1358 C  CG   . GLU   A 178 ? 0.5972 0.6068 0.6087 -0.0786 -0.0131 -0.0014 178 GLU   A CG   
1359 C  CD   . GLU   A 178 ? 0.6439 0.6677 0.6657 -0.0890 -0.0109 -0.0008 178 GLU   A CD   
1360 O  OE1  . GLU   A 178 ? 0.5730 0.6152 0.6111 -0.0886 -0.0092 -0.0023 178 GLU   A OE1  
1361 O  OE2  . GLU   A 178 ? 0.7839 0.8000 0.7968 -0.0976 -0.0108 0.0014  178 GLU   A OE2  
1362 N  N    . GLY   A 179 ? 0.7353 0.7356 0.7476 -0.0455 -0.0200 -0.0058 179 GLY   A N    
1363 C  CA   . GLY   A 179 ? 0.6796 0.6798 0.6944 -0.0384 -0.0228 -0.0070 179 GLY   A CA   
1364 C  C    . GLY   A 179 ? 0.6442 0.6611 0.6744 -0.0342 -0.0194 -0.0090 179 GLY   A C    
1365 O  O    . GLY   A 179 ? 0.6915 0.7069 0.7218 -0.0260 -0.0193 -0.0097 179 GLY   A O    
1366 N  N    . ASN   A 180 ? 0.5735 0.6061 0.6162 -0.0395 -0.0168 -0.0098 180 ASN   A N    
1367 C  CA   . ASN   A 180 ? 0.5397 0.5873 0.5962 -0.0352 -0.0149 -0.0120 180 ASN   A CA   
1368 C  C    . ASN   A 180 ? 0.4979 0.5471 0.5557 -0.0276 -0.0101 -0.0125 180 ASN   A C    
1369 O  O    . ASN   A 180 ? 0.4828 0.5311 0.5380 -0.0284 -0.0059 -0.0116 180 ASN   A O    
1370 C  CB   . ASN   A 180 ? 0.5737 0.6386 0.6432 -0.0420 -0.0127 -0.0128 180 ASN   A CB   
1371 C  CG   . ASN   A 180 ? 0.6159 0.6817 0.6869 -0.0494 -0.0181 -0.0125 180 ASN   A CG   
1372 O  OD1  . ASN   A 180 ? 0.6130 0.6857 0.6918 -0.0479 -0.0217 -0.0142 180 ASN   A OD1  
1373 N  ND2  . ASN   A 180 ? 0.6410 0.6984 0.7036 -0.0574 -0.0193 -0.0104 180 ASN   A ND2  
1374 N  N    . PHE   A 181 ? 0.5394 0.5902 0.6006 -0.0203 -0.0109 -0.0138 181 PHE   A N    
1375 C  CA   . PHE   A 181 ? 0.5097 0.5617 0.5723 -0.0133 -0.0069 -0.0142 181 PHE   A CA   
1376 C  C    . PHE   A 181 ? 0.4468 0.5128 0.5196 -0.0148 -0.0020 -0.0153 181 PHE   A C    
1377 O  O    . PHE   A 181 ? 0.4286 0.5071 0.5111 -0.0178 -0.0019 -0.0168 181 PHE   A O    
1378 C  CB   . PHE   A 181 ? 0.4751 0.5265 0.5396 -0.0059 -0.0089 -0.0154 181 PHE   A CB   
1379 C  CG   . PHE   A 181 ? 0.5204 0.5567 0.5732 -0.0011 -0.0114 -0.0139 181 PHE   A CG   
1380 C  CD1  . PHE   A 181 ? 0.5090 0.5402 0.5577 0.0045  -0.0083 -0.0129 181 PHE   A CD1  
1381 C  CD2  . PHE   A 181 ? 0.5342 0.5617 0.5803 -0.0019 -0.0170 -0.0137 181 PHE   A CD2  
1382 C  CE1  . PHE   A 181 ? 0.4711 0.4896 0.5094 0.0095  -0.0100 -0.0115 181 PHE   A CE1  
1383 C  CE2  . PHE   A 181 ? 0.5105 0.5238 0.5449 0.0034  -0.0191 -0.0124 181 PHE   A CE2  
1384 C  CZ   . PHE   A 181 ? 0.4855 0.4948 0.5161 0.0093  -0.0152 -0.0113 181 PHE   A CZ   
1385 N  N    . TYR   A 182 ? 0.4996 0.5636 0.5700 -0.0123 0.0020  -0.0147 182 TYR   A N    
1386 C  CA   . TYR   A 182 ? 0.4955 0.5706 0.5743 -0.0106 0.0063  -0.0161 182 TYR   A CA   
1387 C  C    . TYR   A 182 ? 0.5163 0.5960 0.6011 -0.0040 0.0054  -0.0179 182 TYR   A C    
1388 O  O    . TYR   A 182 ? 0.4906 0.5619 0.5706 0.0011  0.0036  -0.0174 182 TYR   A O    
1389 C  CB   . TYR   A 182 ? 0.4647 0.5345 0.5383 -0.0091 0.0097  -0.0150 182 TYR   A CB   
1390 C  CG   . TYR   A 182 ? 0.4769 0.5436 0.5453 -0.0156 0.0110  -0.0137 182 TYR   A CG   
1391 C  CD1  . TYR   A 182 ? 0.4624 0.5390 0.5361 -0.0202 0.0144  -0.0144 182 TYR   A CD1  
1392 C  CD2  . TYR   A 182 ? 0.4664 0.5200 0.5236 -0.0172 0.0089  -0.0118 182 TYR   A CD2  
1393 C  CE1  . TYR   A 182 ? 0.5198 0.5928 0.5877 -0.0265 0.0157  -0.0130 182 TYR   A CE1  
1394 C  CE2  . TYR   A 182 ? 0.4738 0.5231 0.5248 -0.0232 0.0097  -0.0106 182 TYR   A CE2  
1395 C  CZ   . TYR   A 182 ? 0.5545 0.6133 0.6107 -0.0281 0.0131  -0.0111 182 TYR   A CZ   
1396 O  OH   . TYR   A 182 ? 0.5700 0.6238 0.6191 -0.0344 0.0142  -0.0097 182 TYR   A OH   
1397 N  N    . GLY   A 183 ? 0.5578 0.6506 0.6525 -0.0039 0.0067  -0.0200 183 GLY   A N    
1398 C  CA   . GLY   A 183 ? 0.5523 0.6491 0.6520 0.0024  0.0056  -0.0220 183 GLY   A CA   
1399 C  C    . GLY   A 183 ? 0.5151 0.6108 0.6156 0.0033  0.0005  -0.0227 183 GLY   A C    
1400 O  O    . GLY   A 183 ? 0.5297 0.6225 0.6278 -0.0016 -0.0025 -0.0218 183 GLY   A O    
1401 N  N    . PRO   A 184 ? 0.4732 0.5701 0.5763 0.0097  -0.0011 -0.0244 184 PRO   A N    
1402 C  CA   . PRO   A 184 ? 0.4882 0.5855 0.5930 0.0111  -0.0063 -0.0256 184 PRO   A CA   
1403 C  C    . PRO   A 184 ? 0.5338 0.6160 0.6281 0.0130  -0.0098 -0.0239 184 PRO   A C    
1404 O  O    . PRO   A 184 ? 0.5897 0.6697 0.6836 0.0151  -0.0145 -0.0249 184 PRO   A O    
1405 C  CB   . PRO   A 184 ? 0.4843 0.5869 0.5940 0.0181  -0.0060 -0.0281 184 PRO   A CB   
1406 C  CG   . PRO   A 184 ? 0.4889 0.5844 0.5932 0.0215  -0.0022 -0.0268 184 PRO   A CG   
1407 C  CD   . PRO   A 184 ? 0.5245 0.6203 0.6274 0.0159  0.0014  -0.0250 184 PRO   A CD   
1408 N  N    . PHE   A 185 ? 0.5201 0.5919 0.6057 0.0125  -0.0078 -0.0215 185 PHE   A N    
1409 C  CA   . PHE   A 185 ? 0.5253 0.5830 0.6005 0.0166  -0.0097 -0.0198 185 PHE   A CA   
1410 C  C    . PHE   A 185 ? 0.5029 0.5527 0.5717 0.0136  -0.0146 -0.0191 185 PHE   A C    
1411 O  O    . PHE   A 185 ? 0.4984 0.5527 0.5701 0.0072  -0.0164 -0.0193 185 PHE   A O    
1412 C  CB   . PHE   A 185 ? 0.5425 0.5939 0.6120 0.0175  -0.0056 -0.0176 185 PHE   A CB   
1413 C  CG   . PHE   A 185 ? 0.5392 0.5970 0.6142 0.0199  -0.0013 -0.0183 185 PHE   A CG   
1414 C  CD1  . PHE   A 185 ? 0.5791 0.6372 0.6559 0.0257  -0.0013 -0.0193 185 PHE   A CD1  
1415 C  CD2  . PHE   A 185 ? 0.5088 0.5712 0.5863 0.0164  0.0023  -0.0179 185 PHE   A CD2  
1416 C  CE1  . PHE   A 185 ? 0.5556 0.6181 0.6363 0.0278  0.0020  -0.0199 185 PHE   A CE1  
1417 C  CE2  . PHE   A 185 ? 0.5618 0.6289 0.6434 0.0188  0.0056  -0.0186 185 PHE   A CE2  
1418 C  CZ   . PHE   A 185 ? 0.5485 0.6155 0.6317 0.0244  0.0054  -0.0196 185 PHE   A CZ   
1419 N  N    . VAL   A 186 ? 0.5698 0.6071 0.6290 0.0185  -0.0169 -0.0181 186 VAL   A N    
1420 C  CA   . VAL   A 186 ? 0.5639 0.5908 0.6146 0.0176  -0.0222 -0.0175 186 VAL   A CA   
1421 C  C    . VAL   A 186 ? 0.5224 0.5348 0.5603 0.0223  -0.0213 -0.0151 186 VAL   A C    
1422 O  O    . VAL   A 186 ? 0.5319 0.5434 0.5690 0.0271  -0.0173 -0.0142 186 VAL   A O    
1423 C  CB   . VAL   A 186 ? 0.5467 0.5744 0.5996 0.0204  -0.0274 -0.0195 186 VAL   A CB   
1424 C  CG1  . VAL   A 186 ? 0.4902 0.5321 0.5551 0.0147  -0.0295 -0.0217 186 VAL   A CG1  
1425 C  CG2  . VAL   A 186 ? 0.5285 0.5568 0.5827 0.0278  -0.0253 -0.0203 186 VAL   A CG2  
1426 N  N    . ASP   A 187 ? 0.5451 0.5463 0.5728 0.0207  -0.0252 -0.0140 187 ASP   A N    
1427 C  CA   . ASP   A 187 ? 0.5420 0.5299 0.5570 0.0251  -0.0242 -0.0118 187 ASP   A CA   
1428 C  C    . ASP   A 187 ? 0.5784 0.5560 0.5850 0.0319  -0.0273 -0.0118 187 ASP   A C    
1429 O  O    . ASP   A 187 ? 0.5616 0.5267 0.5568 0.0330  -0.0316 -0.0111 187 ASP   A O    
1430 C  CB   . ASP   A 187 ? 0.4882 0.4680 0.4946 0.0204  -0.0262 -0.0105 187 ASP   A CB   
1431 C  CG   . ASP   A 187 ? 0.5021 0.4788 0.5066 0.0149  -0.0328 -0.0115 187 ASP   A CG   
1432 O  OD1  . ASP   A 187 ? 0.5650 0.5471 0.5758 0.0147  -0.0359 -0.0133 187 ASP   A OD1  
1433 O  OD2  . ASP   A 187 ? 0.5018 0.4699 0.4978 0.0108  -0.0352 -0.0104 187 ASP   A OD2  
1434 N  N    . ARG   A 188 ? 0.6157 0.5978 0.6273 0.0367  -0.0252 -0.0125 188 ARG   A N    
1435 C  CA   . ARG   A 188 ? 0.6953 0.6678 0.6988 0.0439  -0.0268 -0.0122 188 ARG   A CA   
1436 C  C    . ARG   A 188 ? 0.7014 0.6758 0.7062 0.0490  -0.0209 -0.0109 188 ARG   A C    
1437 O  O    . ARG   A 188 ? 0.6473 0.6320 0.6616 0.0468  -0.0167 -0.0110 188 ARG   A O    
1438 C  CB   . ARG   A 188 ? 0.7191 0.6942 0.7266 0.0442  -0.0320 -0.0148 188 ARG   A CB   
1439 C  CG   . ARG   A 188 ? 0.7902 0.7655 0.7984 0.0379  -0.0380 -0.0160 188 ARG   A CG   
1440 C  CD   . ARG   A 188 ? 0.7992 0.7718 0.8066 0.0392  -0.0448 -0.0181 188 ARG   A CD   
1441 N  NE   . ARG   A 188 ? 0.9175 0.9027 0.9371 0.0401  -0.0446 -0.0205 188 ARG   A NE   
1442 C  CZ   . ARG   A 188 ? 0.9349 0.9353 0.9681 0.0344  -0.0449 -0.0223 188 ARG   A CZ   
1443 N  NH1  . ARG   A 188 ? 0.8366 0.8414 0.8731 0.0265  -0.0452 -0.0217 188 ARG   A NH1  
1444 N  NH2  . ARG   A 188 ? 0.9330 0.9438 0.9759 0.0367  -0.0449 -0.0246 188 ARG   A NH2  
1445 N  N    . GLN   A 189 ? 0.8038 0.7674 0.7983 0.0557  -0.0204 -0.0094 189 GLN   A N    
1446 C  CA   . GLN   A 189 ? 0.7854 0.7503 0.7810 0.0604  -0.0152 -0.0080 189 GLN   A CA   
1447 C  C    . GLN   A 189 ? 0.7596 0.7268 0.7591 0.0626  -0.0171 -0.0101 189 GLN   A C    
1448 O  O    . GLN   A 189 ? 0.7737 0.7319 0.7652 0.0680  -0.0188 -0.0099 189 GLN   A O    
1449 C  CB   . GLN   A 189 ? 0.7777 0.7314 0.7612 0.0665  -0.0130 -0.0053 189 GLN   A CB   
1450 C  CG   . GLN   A 189 ? 0.7667 0.7244 0.7534 0.0692  -0.0064 -0.0031 189 GLN   A CG   
1451 C  CD   . GLN   A 189 ? 0.7173 0.6852 0.7132 0.0648  -0.0024 -0.0024 189 GLN   A CD   
1452 O  OE1  . GLN   A 189 ? 0.6790 0.6452 0.6716 0.0643  -0.0011 -0.0010 189 GLN   A OE1  
1453 N  NE2  . GLN   A 189 ? 0.6758 0.6533 0.6823 0.0619  -0.0007 -0.0036 189 GLN   A NE2  
1454 N  N    . THR   A 190 ? 0.7338 0.7128 0.7452 0.0585  -0.0172 -0.0122 190 THR   A N    
1455 C  CA   . THR   A 190 ? 0.7359 0.7194 0.7527 0.0606  -0.0183 -0.0143 190 THR   A CA   
1456 C  C    . THR   A 190 ? 0.7231 0.7164 0.7490 0.0590  -0.0132 -0.0141 190 THR   A C    
1457 O  O    . THR   A 190 ? 0.7452 0.7438 0.7753 0.0550  -0.0102 -0.0132 190 THR   A O    
1458 C  CB   . THR   A 190 ? 0.7380 0.7272 0.7606 0.0578  -0.0242 -0.0175 190 THR   A CB   
1459 O  OG1  . THR   A 190 ? 0.6474 0.6469 0.6787 0.0509  -0.0236 -0.0181 190 THR   A OG1  
1460 C  CG2  . THR   A 190 ? 0.7068 0.6847 0.7194 0.0595  -0.0301 -0.0177 190 THR   A CG2  
1461 N  N    . ALA   A 191 ? 0.7133 0.7076 0.7412 0.0624  -0.0126 -0.0151 191 ALA   A N    
1462 C  CA   . ALA   A 191 ? 0.6892 0.6912 0.7245 0.0611  -0.0085 -0.0151 191 ALA   A CA   
1463 C  C    . ALA   A 191 ? 0.6822 0.6968 0.7283 0.0565  -0.0096 -0.0178 191 ALA   A C    
1464 O  O    . ALA   A 191 ? 0.7643 0.7831 0.8141 0.0566  -0.0137 -0.0205 191 ALA   A O    
1465 C  CB   . ALA   A 191 ? 0.6126 0.6105 0.6454 0.0661  -0.0083 -0.0155 191 ALA   A CB   
1466 N  N    . GLN   A 192 ? 0.6465 0.6673 0.6976 0.0524  -0.0059 -0.0169 192 GLN   A N    
1467 C  CA   . GLN   A 192 ? 0.7395 0.7719 0.7998 0.0477  -0.0062 -0.0190 192 GLN   A CA   
1468 C  C    . GLN   A 192 ? 0.7850 0.8234 0.8507 0.0468  -0.0021 -0.0190 192 GLN   A C    
1469 O  O    . GLN   A 192 ? 0.7587 0.7940 0.8220 0.0461  0.0013  -0.0166 192 GLN   A O    
1470 C  CB   . GLN   A 192 ? 0.6550 0.6880 0.7147 0.0425  -0.0068 -0.0181 192 GLN   A CB   
1471 C  CG   . GLN   A 192 ? 0.6801 0.7075 0.7348 0.0425  -0.0118 -0.0184 192 GLN   A CG   
1472 C  CD   . GLN   A 192 ? 0.6325 0.6584 0.6847 0.0372  -0.0127 -0.0173 192 GLN   A CD   
1473 O  OE1  . GLN   A 192 ? 0.6278 0.6616 0.6859 0.0319  -0.0110 -0.0177 192 GLN   A OE1  
1474 N  NE2  . GLN   A 192 ? 0.6550 0.6696 0.6973 0.0387  -0.0154 -0.0160 192 GLN   A NE2  
1475 N  N    . ALA   A 193 ? 0.7332 0.7802 0.8059 0.0470  -0.0027 -0.0218 193 ALA   A N    
1476 C  CA   . ALA   A 193 ? 0.8264 0.8773 0.9025 0.0474  0.0004  -0.0222 193 ALA   A CA   
1477 C  C    . ALA   A 193 ? 0.8067 0.8672 0.8892 0.0425  0.0025  -0.0229 193 ALA   A C    
1478 O  O    . ALA   A 193 ? 0.7417 0.8109 0.8299 0.0404  0.0010  -0.0250 193 ALA   A O    
1479 C  CB   . ALA   A 193 ? 0.8554 0.9082 0.9333 0.0522  -0.0014 -0.0249 193 ALA   A CB   
1480 N  N    . ALA   A 194 ? 0.7642 0.8231 0.8456 0.0405  0.0058  -0.0211 194 ALA   A N    
1481 C  CA   . ALA   A 194 ? 0.7421 0.8089 0.8286 0.0374  0.0082  -0.0221 194 ALA   A CA   
1482 C  C    . ALA   A 194 ? 0.7418 0.8129 0.8316 0.0409  0.0084  -0.0245 194 ALA   A C    
1483 O  O    . ALA   A 194 ? 0.7351 0.8005 0.8218 0.0452  0.0075  -0.0246 194 ALA   A O    
1484 C  CB   . ALA   A 194 ? 0.6704 0.7333 0.7541 0.0349  0.0110  -0.0196 194 ALA   A CB   
1485 N  N    . GLY   A 195 ? 0.7424 0.8228 0.8376 0.0391  0.0097  -0.0264 195 GLY   A N    
1486 C  CA   . GLY   A 195 ? 0.6912 0.7759 0.7889 0.0428  0.0101  -0.0289 195 GLY   A CA   
1487 C  C    . GLY   A 195 ? 0.6443 0.7248 0.7391 0.0428  0.0125  -0.0281 195 GLY   A C    
1488 O  O    . GLY   A 195 ? 0.6034 0.6766 0.6942 0.0410  0.0135  -0.0254 195 GLY   A O    
1489 N  N    . THR   A 196 ? 0.6381 0.7232 0.7348 0.0453  0.0132  -0.0305 196 THR   A N    
1490 C  CA   . THR   A 196 ? 0.6159 0.6967 0.7094 0.0452  0.0150  -0.0300 196 THR   A CA   
1491 C  C    . THR   A 196 ? 0.6314 0.7143 0.7254 0.0399  0.0176  -0.0285 196 THR   A C    
1492 O  O    . THR   A 196 ? 0.6224 0.7132 0.7202 0.0369  0.0187  -0.0290 196 THR   A O    
1493 C  CB   . THR   A 196 ? 0.5919 0.6764 0.6859 0.0497  0.0150  -0.0332 196 THR   A CB   
1494 O  OG1  . THR   A 196 ? 0.6722 0.7693 0.7724 0.0490  0.0163  -0.0353 196 THR   A OG1  
1495 C  CG2  . THR   A 196 ? 0.6824 0.7624 0.7740 0.0555  0.0120  -0.0346 196 THR   A CG2  
1496 N  N    . ASP   A 197 ? 0.7108 0.7863 0.8008 0.0384  0.0183  -0.0264 197 ASP   A N    
1497 C  CA   . ASP   A 197 ? 0.6978 0.7734 0.7870 0.0338  0.0202  -0.0249 197 ASP   A CA   
1498 C  C    . ASP   A 197 ? 0.6252 0.7027 0.7136 0.0342  0.0217  -0.0265 197 ASP   A C    
1499 O  O    . ASP   A 197 ? 0.6197 0.6909 0.7045 0.0343  0.0216  -0.0257 197 ASP   A O    
1500 C  CB   . ASP   A 197 ? 0.6768 0.7442 0.7627 0.0322  0.0198  -0.0218 197 ASP   A CB   
1501 C  CG   . ASP   A 197 ? 0.7105 0.7779 0.7954 0.0278  0.0210  -0.0202 197 ASP   A CG   
1502 O  OD1  . ASP   A 197 ? 0.7163 0.7894 0.8026 0.0255  0.0222  -0.0212 197 ASP   A OD1  
1503 O  OD2  . ASP   A 197 ? 0.6877 0.7496 0.7703 0.0267  0.0209  -0.0178 197 ASP   A OD2  
1504 N  N    . THR   A 198 ? 0.5636 0.6500 0.6552 0.0346  0.0232  -0.0288 198 THR   A N    
1505 C  CA   . THR   A 198 ? 0.6176 0.7059 0.7075 0.0355  0.0250  -0.0304 198 THR   A CA   
1506 C  C    . THR   A 198 ? 0.5812 0.6651 0.6675 0.0312  0.0264  -0.0285 198 THR   A C    
1507 O  O    . THR   A 198 ? 0.5843 0.6688 0.6711 0.0269  0.0270  -0.0268 198 THR   A O    
1508 C  CB   . THR   A 198 ? 0.5229 0.6233 0.6176 0.0362  0.0271  -0.0329 198 THR   A CB   
1509 O  OG1  . THR   A 198 ? 0.5731 0.6792 0.6713 0.0310  0.0283  -0.0316 198 THR   A OG1  
1510 C  CG2  . THR   A 198 ? 0.5356 0.6404 0.6337 0.0416  0.0253  -0.0352 198 THR   A CG2  
1511 N  N    . THR   A 199 ? 0.5230 0.6013 0.6048 0.0326  0.0263  -0.0289 199 THR   A N    
1512 C  CA   . THR   A 199 ? 0.5628 0.6361 0.6406 0.0291  0.0269  -0.0274 199 THR   A CA   
1513 C  C    . THR   A 199 ? 0.5704 0.6496 0.6475 0.0273  0.0301  -0.0285 199 THR   A C    
1514 O  O    . THR   A 199 ? 0.5099 0.5956 0.5883 0.0300  0.0319  -0.0308 199 THR   A O    
1515 C  CB   . THR   A 199 ? 0.5308 0.5953 0.6039 0.0311  0.0249  -0.0274 199 THR   A CB   
1516 O  OG1  . THR   A 199 ? 0.5035 0.5640 0.5777 0.0333  0.0225  -0.0267 199 THR   A OG1  
1517 C  CG2  . THR   A 199 ? 0.5115 0.5698 0.5814 0.0275  0.0243  -0.0252 199 THR   A CG2  
1518 N  N    . ILE   A 200 ? 0.5515 0.6284 0.6262 0.0227  0.0310  -0.0267 200 ILE   A N    
1519 C  CA   . ILE   A 200 ? 0.5323 0.6144 0.6059 0.0198  0.0343  -0.0271 200 ILE   A CA   
1520 C  C    . ILE   A 200 ? 0.4907 0.5689 0.5582 0.0213  0.0355  -0.0282 200 ILE   A C    
1521 O  O    . ILE   A 200 ? 0.4547 0.5250 0.5165 0.0194  0.0347  -0.0271 200 ILE   A O    
1522 C  CB   . ILE   A 200 ? 0.4794 0.5593 0.5515 0.0144  0.0344  -0.0248 200 ILE   A CB   
1523 C  CG1  . ILE   A 200 ? 0.5730 0.6545 0.6495 0.0136  0.0326  -0.0237 200 ILE   A CG1  
1524 C  CG2  . ILE   A 200 ? 0.4505 0.5360 0.5215 0.0106  0.0380  -0.0250 200 ILE   A CG2  
1525 C  CD1  . ILE   A 200 ? 0.5774 0.6506 0.6520 0.0139  0.0297  -0.0216 200 ILE   A CD1  
1526 N  N    . THR   A 201 ? 0.4746 0.5581 0.5428 0.0252  0.0373  -0.0307 201 THR   A N    
1527 C  CA   . THR   A 201 ? 0.5010 0.5795 0.5623 0.0282  0.0379  -0.0321 201 THR   A CA   
1528 C  C    . THR   A 201 ? 0.4108 0.4861 0.4659 0.0244  0.0402  -0.0312 201 THR   A C    
1529 O  O    . THR   A 201 ? 0.4087 0.4743 0.4568 0.0249  0.0385  -0.0310 201 THR   A O    
1530 C  CB   . THR   A 201 ? 0.5405 0.6269 0.6035 0.0333  0.0401  -0.0350 201 THR   A CB   
1531 O  OG1  . THR   A 201 ? 0.4494 0.5387 0.5179 0.0367  0.0377  -0.0359 201 THR   A OG1  
1532 C  CG2  . THR   A 201 ? 0.4821 0.5612 0.5365 0.0375  0.0399  -0.0367 201 THR   A CG2  
1533 N  N    . VAL   A 202 ? 0.4037 0.4865 0.4611 0.0204  0.0436  -0.0305 202 VAL   A N    
1534 C  CA   . VAL   A 202 ? 0.4208 0.4999 0.4712 0.0169  0.0462  -0.0296 202 VAL   A CA   
1535 C  C    . VAL   A 202 ? 0.3945 0.4621 0.4396 0.0140  0.0428  -0.0275 202 VAL   A C    
1536 O  O    . VAL   A 202 ? 0.3856 0.4456 0.4224 0.0131  0.0431  -0.0272 202 VAL   A O    
1537 C  CB   . VAL   A 202 ? 0.4571 0.5467 0.5113 0.0123  0.0504  -0.0289 202 VAL   A CB   
1538 C  CG1  . VAL   A 202 ? 0.4345 0.5260 0.4943 0.0082  0.0484  -0.0271 202 VAL   A CG1  
1539 C  CG2  . VAL   A 202 ? 0.4689 0.5547 0.5144 0.0089  0.0539  -0.0281 202 VAL   A CG2  
1540 N  N    . ASN   A 203 ? 0.4620 0.5279 0.5115 0.0132  0.0395  -0.0262 203 ASN   A N    
1541 C  CA   . ASN   A 203 ? 0.4588 0.5150 0.5040 0.0113  0.0363  -0.0244 203 ASN   A CA   
1542 C  C    . ASN   A 203 ? 0.4707 0.5191 0.5129 0.0147  0.0330  -0.0249 203 ASN   A C    
1543 O  O    . ASN   A 203 ? 0.4396 0.4797 0.4755 0.0137  0.0312  -0.0243 203 ASN   A O    
1544 C  CB   . ASN   A 203 ? 0.4334 0.4908 0.4838 0.0094  0.0343  -0.0226 203 ASN   A CB   
1545 C  CG   . ASN   A 203 ? 0.4349 0.4960 0.4853 0.0049  0.0365  -0.0215 203 ASN   A CG   
1546 O  OD1  . ASN   A 203 ? 0.3967 0.4644 0.4479 0.0033  0.0399  -0.0223 203 ASN   A OD1  
1547 N  ND2  . ASN   A 203 ? 0.4870 0.5437 0.5363 0.0027  0.0343  -0.0196 203 ASN   A ND2  
1548 N  N    . VAL   A 204 ? 0.4413 0.4914 0.4874 0.0185  0.0316  -0.0261 204 VAL   A N    
1549 C  CA   . VAL   A 204 ? 0.4428 0.4847 0.4855 0.0211  0.0281  -0.0266 204 VAL   A CA   
1550 C  C    . VAL   A 204 ? 0.4310 0.4671 0.4649 0.0219  0.0288  -0.0278 204 VAL   A C    
1551 O  O    . VAL   A 204 ? 0.4328 0.4602 0.4617 0.0214  0.0257  -0.0273 204 VAL   A O    
1552 C  CB   . VAL   A 204 ? 0.4542 0.4979 0.5004 0.0252  0.0270  -0.0280 204 VAL   A CB   
1553 C  CG1  . VAL   A 204 ? 0.4390 0.4730 0.4809 0.0271  0.0229  -0.0282 204 VAL   A CG1  
1554 C  CG2  . VAL   A 204 ? 0.4535 0.5020 0.5073 0.0246  0.0264  -0.0267 204 VAL   A CG2  
1555 N  N    . LEU   A 205 ? 0.4203 0.4618 0.4522 0.0230  0.0330  -0.0294 205 LEU   A N    
1556 C  CA   . LEU   A 205 ? 0.4171 0.4536 0.4396 0.0242  0.0346  -0.0306 205 LEU   A CA   
1557 C  C    . LEU   A 205 ? 0.4118 0.4417 0.4282 0.0203  0.0343  -0.0290 205 LEU   A C    
1558 O  O    . LEU   A 205 ? 0.4328 0.4529 0.4408 0.0212  0.0321  -0.0295 205 LEU   A O    
1559 C  CB   . LEU   A 205 ? 0.3736 0.4196 0.3967 0.0258  0.0402  -0.0322 205 LEU   A CB   
1560 C  CG   . LEU   A 205 ? 0.3464 0.3976 0.3735 0.0313  0.0401  -0.0343 205 LEU   A CG   
1561 C  CD1  . LEU   A 205 ? 0.3449 0.4093 0.3764 0.0324  0.0455  -0.0356 205 LEU   A CD1  
1562 C  CD2  . LEU   A 205 ? 0.4055 0.4464 0.4238 0.0361  0.0375  -0.0361 205 LEU   A CD2  
1563 N  N    . ALA   A 206 ? 0.4489 0.4832 0.4685 0.0159  0.0360  -0.0273 206 ALA   A N    
1564 C  CA   . ALA   A 206 ? 0.4455 0.4726 0.4583 0.0124  0.0353  -0.0258 206 ALA   A CA   
1565 C  C    . ALA   A 206 ? 0.4844 0.5030 0.4963 0.0127  0.0297  -0.0249 206 ALA   A C    
1566 O  O    . ALA   A 206 ? 0.4139 0.4234 0.4176 0.0124  0.0277  -0.0248 206 ALA   A O    
1567 C  CB   . ALA   A 206 ? 0.4557 0.4882 0.4717 0.0078  0.0376  -0.0241 206 ALA   A CB   
1568 N  N    . TRP   A 207 ? 0.4714 0.4931 0.4917 0.0135  0.0271  -0.0242 207 TRP   A N    
1569 C  CA   . TRP   A 207 ? 0.4663 0.4820 0.4876 0.0138  0.0220  -0.0232 207 TRP   A CA   
1570 C  C    . TRP   A 207 ? 0.4953 0.5035 0.5114 0.0164  0.0189  -0.0246 207 TRP   A C    
1571 O  O    . TRP   A 207 ? 0.5176 0.5188 0.5310 0.0160  0.0148  -0.0240 207 TRP   A O    
1572 C  CB   . TRP   A 207 ? 0.4732 0.4944 0.5043 0.0141  0.0207  -0.0220 207 TRP   A CB   
1573 C  CG   . TRP   A 207 ? 0.4317 0.4486 0.4654 0.0146  0.0160  -0.0209 207 TRP   A CG   
1574 C  CD1  . TRP   A 207 ? 0.4202 0.4343 0.4541 0.0131  0.0132  -0.0193 207 TRP   A CD1  
1575 C  CD2  . TRP   A 207 ? 0.3992 0.4146 0.4357 0.0165  0.0134  -0.0213 207 TRP   A CD2  
1576 N  NE1  . TRP   A 207 ? 0.3696 0.3819 0.4075 0.0137  0.0094  -0.0185 207 TRP   A NE1  
1577 C  CE2  . TRP   A 207 ? 0.4151 0.4275 0.4543 0.0154  0.0094  -0.0196 207 TRP   A CE2  
1578 C  CE3  . TRP   A 207 ? 0.4564 0.4726 0.4932 0.0190  0.0140  -0.0229 207 TRP   A CE3  
1579 C  CZ2  . TRP   A 207 ? 0.4471 0.4571 0.4893 0.0159  0.0060  -0.0192 207 TRP   A CZ2  
1580 C  CZ3  . TRP   A 207 ? 0.4490 0.4612 0.4874 0.0200  0.0104  -0.0227 207 TRP   A CZ3  
1581 C  CH2  . TRP   A 207 ? 0.4591 0.4683 0.5004 0.0180  0.0065  -0.0207 207 TRP   A CH2  
1582 N  N    . LEU   A 208 ? 0.4634 0.4727 0.4778 0.0193  0.0207  -0.0266 208 LEU   A N    
1583 C  CA   . LEU   A 208 ? 0.5142 0.5146 0.5210 0.0221  0.0178  -0.0282 208 LEU   A CA   
1584 C  C    . LEU   A 208 ? 0.5350 0.5282 0.5310 0.0216  0.0185  -0.0287 208 LEU   A C    
1585 O  O    . LEU   A 208 ? 0.5756 0.5594 0.5660 0.0217  0.0141  -0.0288 208 LEU   A O    
1586 C  CB   . LEU   A 208 ? 0.4306 0.4334 0.4370 0.0261  0.0196  -0.0303 208 LEU   A CB   
1587 C  CG   . LEU   A 208 ? 0.4325 0.4386 0.4476 0.0267  0.0173  -0.0296 208 LEU   A CG   
1588 C  CD1  . LEU   A 208 ? 0.4534 0.4636 0.4694 0.0308  0.0193  -0.0316 208 LEU   A CD1  
1589 C  CD2  . LEU   A 208 ? 0.4925 0.4896 0.5065 0.0262  0.0111  -0.0289 208 LEU   A CD2  
1590 N  N    . TYR   A 209 ? 0.4998 0.4972 0.4926 0.0209  0.0240  -0.0291 209 TYR   A N    
1591 C  CA   . TYR   A 209 ? 0.5344 0.5243 0.5159 0.0200  0.0251  -0.0293 209 TYR   A CA   
1592 C  C    . TYR   A 209 ? 0.5858 0.5688 0.5654 0.0174  0.0207  -0.0277 209 TYR   A C    
1593 O  O    . TYR   A 209 ? 0.5514 0.5240 0.5217 0.0181  0.0176  -0.0282 209 TYR   A O    
1594 C  CB   . TYR   A 209 ? 0.4701 0.4669 0.4502 0.0180  0.0318  -0.0290 209 TYR   A CB   
1595 C  CG   . TYR   A 209 ? 0.4558 0.4565 0.4328 0.0213  0.0364  -0.0308 209 TYR   A CG   
1596 C  CD1  . TYR   A 209 ? 0.5267 0.5181 0.4921 0.0248  0.0360  -0.0325 209 TYR   A CD1  
1597 C  CD2  . TYR   A 209 ? 0.4367 0.4504 0.4220 0.0214  0.0410  -0.0311 209 TYR   A CD2  
1598 C  CE1  . TYR   A 209 ? 0.5357 0.5308 0.4976 0.0288  0.0405  -0.0344 209 TYR   A CE1  
1599 C  CE2  . TYR   A 209 ? 0.5183 0.5371 0.5013 0.0251  0.0455  -0.0330 209 TYR   A CE2  
1600 C  CZ   . TYR   A 209 ? 0.5349 0.5444 0.5060 0.0290  0.0455  -0.0346 209 TYR   A CZ   
1601 O  OH   . TYR   A 209 ? 0.4828 0.4974 0.4511 0.0335  0.0501  -0.0365 209 TYR   A OH   
1602 N  N    . ALA   A 210 ? 0.5522 0.5410 0.5403 0.0147  0.0201  -0.0259 210 ALA   A N    
1603 C  CA   . ALA   A 210 ? 0.5514 0.5349 0.5388 0.0131  0.0158  -0.0244 210 ALA   A CA   
1604 C  C    . ALA   A 210 ? 0.5974 0.5746 0.5850 0.0149  0.0096  -0.0249 210 ALA   A C    
1605 O  O    . ALA   A 210 ? 0.5691 0.5386 0.5513 0.0147  0.0056  -0.0247 210 ALA   A O    
1606 C  CB   . ALA   A 210 ? 0.5635 0.5547 0.5606 0.0111  0.0161  -0.0226 210 ALA   A CB   
1607 N  N    . ALA   A 211 ? 0.6293 0.6094 0.6227 0.0167  0.0084  -0.0254 211 ALA   A N    
1608 C  CA   . ALA   A 211 ? 0.6772 0.6516 0.6716 0.0177  0.0023  -0.0256 211 ALA   A CA   
1609 C  C    . ALA   A 211 ? 0.6840 0.6469 0.6662 0.0194  -0.0003 -0.0274 211 ALA   A C    
1610 O  O    . ALA   A 211 ? 0.7286 0.6846 0.7087 0.0191  -0.0061 -0.0273 211 ALA   A O    
1611 C  CB   . ALA   A 211 ? 0.6176 0.5960 0.6188 0.0190  0.0020  -0.0259 211 ALA   A CB   
1612 N  N    . VAL   A 212 ? 0.6052 0.5661 0.5793 0.0216  0.0038  -0.0292 212 VAL   A N    
1613 C  CA   . VAL   A 212 ? 0.6676 0.6168 0.6284 0.0238  0.0019  -0.0309 212 VAL   A CA   
1614 C  C    . VAL   A 212 ? 0.7180 0.6606 0.6716 0.0222  0.0003  -0.0303 212 VAL   A C    
1615 O  O    . VAL   A 212 ? 0.7066 0.6382 0.6522 0.0232  -0.0050 -0.0311 212 VAL   A O    
1616 C  CB   . VAL   A 212 ? 0.6104 0.5606 0.5644 0.0268  0.0078  -0.0327 212 VAL   A CB   
1617 C  CG1  . VAL   A 212 ? 0.6040 0.5410 0.5435 0.0302  0.0055  -0.0347 212 VAL   A CG1  
1618 C  CG2  . VAL   A 212 ? 0.5847 0.5435 0.5471 0.0286  0.0099  -0.0332 212 VAL   A CG2  
1619 N  N    . ILE   A 213 ? 0.6598 0.6080 0.6156 0.0196  0.0043  -0.0289 213 ILE   A N    
1620 C  CA   . ILE   A 213 ? 0.6532 0.5945 0.6009 0.0182  0.0031  -0.0283 213 ILE   A CA   
1621 C  C    . ILE   A 213 ? 0.7026 0.6407 0.6542 0.0177  -0.0042 -0.0276 213 ILE   A C    
1622 O  O    . ILE   A 213 ? 0.6393 0.5679 0.5820 0.0180  -0.0079 -0.0279 213 ILE   A O    
1623 C  CB   . ILE   A 213 ? 0.6606 0.6084 0.6096 0.0152  0.0090  -0.0269 213 ILE   A CB   
1624 C  CG1  . ILE   A 213 ? 0.6094 0.5618 0.5553 0.0154  0.0163  -0.0276 213 ILE   A CG1  
1625 C  CG2  . ILE   A 213 ? 0.7326 0.6719 0.6719 0.0138  0.0075  -0.0262 213 ILE   A CG2  
1626 C  CD1  . ILE   A 213 ? 0.5252 0.4859 0.4749 0.0118  0.0218  -0.0261 213 ILE   A CD1  
1627 N  N    . ASN   A 214 ? 0.7199 0.6658 0.6846 0.0170  -0.0064 -0.0265 214 ASN   A N    
1628 C  CA   . ASN   A 214 ? 0.7231 0.6695 0.6944 0.0163  -0.0125 -0.0253 214 ASN   A CA   
1629 C  C    . ASN   A 214 ? 0.7114 0.6522 0.6832 0.0173  -0.0192 -0.0261 214 ASN   A C    
1630 O  O    . ASN   A 214 ? 0.7215 0.6620 0.6976 0.0167  -0.0249 -0.0253 214 ASN   A O    
1631 C  CB   . ASN   A 214 ? 0.6825 0.6408 0.6678 0.0149  -0.0109 -0.0233 214 ASN   A CB   
1632 C  CG   . ASN   A 214 ? 0.6286 0.5903 0.6136 0.0137  -0.0075 -0.0221 214 ASN   A CG   
1633 O  OD1  . ASN   A 214 ? 0.6724 0.6349 0.6602 0.0136  -0.0105 -0.0210 214 ASN   A OD1  
1634 N  ND2  . ASN   A 214 ? 0.5862 0.5499 0.5674 0.0129  -0.0015 -0.0224 214 ASN   A ND2  
1635 N  N    . GLY   A 215 ? 0.7337 0.6704 0.7013 0.0188  -0.0190 -0.0276 215 GLY   A N    
1636 C  CA   . GLY   A 215 ? 0.6988 0.6280 0.6648 0.0194  -0.0259 -0.0285 215 GLY   A CA   
1637 C  C    . GLY   A 215 ? 0.8074 0.7388 0.7785 0.0197  -0.0262 -0.0287 215 GLY   A C    
1638 O  O    . GLY   A 215 ? 0.8677 0.7897 0.8323 0.0210  -0.0307 -0.0302 215 GLY   A O    
1639 N  N    . ASP   A 216 ? 0.8101 0.7524 0.7915 0.0188  -0.0218 -0.0274 216 ASP   A N    
1640 C  CA   . ASP   A 216 ? 0.7935 0.7380 0.7802 0.0190  -0.0222 -0.0274 216 ASP   A CA   
1641 C  C    . ASP   A 216 ? 0.7824 0.7236 0.7603 0.0225  -0.0179 -0.0296 216 ASP   A C    
1642 O  O    . ASP   A 216 ? 0.7664 0.7142 0.7445 0.0233  -0.0114 -0.0299 216 ASP   A O    
1643 C  CB   . ASP   A 216 ? 0.7466 0.7035 0.7469 0.0170  -0.0193 -0.0252 216 ASP   A CB   
1644 C  CG   . ASP   A 216 ? 0.7451 0.7060 0.7549 0.0142  -0.0235 -0.0229 216 ASP   A CG   
1645 O  OD1  . ASP   A 216 ? 0.7499 0.7044 0.7573 0.0134  -0.0296 -0.0230 216 ASP   A OD1  
1646 O  OD2  . ASP   A 216 ? 0.7353 0.7060 0.7549 0.0129  -0.0208 -0.0209 216 ASP   A OD2  
1647 N  N    . ARG   A 217 ? 0.9523 0.8836 0.9227 0.0246  -0.0219 -0.0313 217 ARG   A N    
1648 C  CA   . ARG   A 217 ? 0.9268 0.8540 0.8876 0.0289  -0.0184 -0.0337 217 ARG   A CA   
1649 C  C    . ARG   A 217 ? 0.8967 0.8202 0.8574 0.0307  -0.0211 -0.0345 217 ARG   A C    
1650 O  O    . ARG   A 217 ? 0.9691 0.8878 0.9206 0.0352  -0.0191 -0.0368 217 ARG   A O    
1651 C  CB   . ARG   A 217 ? 1.0154 0.9303 0.9608 0.0315  -0.0199 -0.0357 217 ARG   A CB   
1652 C  CG   . ARG   A 217 ? 1.0553 0.9724 0.9959 0.0314  -0.0147 -0.0356 217 ARG   A CG   
1653 C  CD   . ARG   A 217 ? 1.0667 0.9694 0.9916 0.0338  -0.0178 -0.0374 217 ARG   A CD   
1654 N  NE   . ARG   A 217 ? 1.0697 0.9656 0.9955 0.0313  -0.0261 -0.0366 217 ARG   A NE   
1655 C  CZ   . ARG   A 217 ? 1.0820 0.9640 0.9977 0.0329  -0.0330 -0.0381 217 ARG   A CZ   
1656 N  NH1  . ARG   A 217 ? 1.0512 0.9241 0.9546 0.0374  -0.0323 -0.0404 217 ARG   A NH1  
1657 N  NH2  . ARG   A 217 ? 1.0475 0.9252 0.9659 0.0304  -0.0407 -0.0374 217 ARG   A NH2  
1658 N  N    . TRP   A 218 ? 0.8604 0.7854 0.8303 0.0275  -0.0254 -0.0327 218 TRP   A N    
1659 C  CA   . TRP   A 218 ? 0.8395 0.7578 0.8068 0.0289  -0.0290 -0.0334 218 TRP   A CA   
1660 C  C    . TRP   A 218 ? 0.8291 0.7526 0.7960 0.0330  -0.0232 -0.0348 218 TRP   A C    
1661 O  O    . TRP   A 218 ? 0.8564 0.7715 0.8145 0.0370  -0.0247 -0.0368 218 TRP   A O    
1662 C  CB   . TRP   A 218 ? 0.8918 0.8124 0.8701 0.0240  -0.0338 -0.0307 218 TRP   A CB   
1663 C  CG   . TRP   A 218 ? 0.8723 0.8070 0.8644 0.0216  -0.0292 -0.0283 218 TRP   A CG   
1664 C  CD1  . TRP   A 218 ? 0.8153 0.7593 0.8175 0.0182  -0.0281 -0.0260 218 TRP   A CD1  
1665 C  CD2  . TRP   A 218 ? 0.8463 0.7863 0.8425 0.0230  -0.0256 -0.0282 218 TRP   A CD2  
1666 N  NE1  . TRP   A 218 ? 0.8073 0.7616 0.8192 0.0173  -0.0240 -0.0244 218 TRP   A NE1  
1667 C  CE2  . TRP   A 218 ? 0.8148 0.7670 0.8234 0.0201  -0.0224 -0.0257 218 TRP   A CE2  
1668 C  CE3  . TRP   A 218 ? 0.8548 0.7900 0.8448 0.0270  -0.0250 -0.0301 218 TRP   A CE3  
1669 C  CZ2  . TRP   A 218 ? 0.8033 0.7625 0.8181 0.0207  -0.0188 -0.0249 218 TRP   A CZ2  
1670 C  CZ3  . TRP   A 218 ? 0.8587 0.8014 0.8553 0.0277  -0.0214 -0.0295 218 TRP   A CZ3  
1671 C  CH2  . TRP   A 218 ? 0.8090 0.7634 0.8178 0.0245  -0.0184 -0.0269 218 TRP   A CH2  
1672 N  N    . PHE   A 219 ? 0.8272 0.7640 0.8029 0.0324  -0.0168 -0.0338 219 PHE   A N    
1673 C  CA   . PHE   A 219 ? 0.7654 0.7090 0.7423 0.0361  -0.0114 -0.0351 219 PHE   A CA   
1674 C  C    . PHE   A 219 ? 0.7326 0.6738 0.6986 0.0413  -0.0075 -0.0379 219 PHE   A C    
1675 O  O    . PHE   A 219 ? 0.7203 0.6683 0.6872 0.0450  -0.0027 -0.0393 219 PHE   A O    
1676 C  CB   . PHE   A 219 ? 0.6985 0.6567 0.6877 0.0335  -0.0063 -0.0332 219 PHE   A CB   
1677 C  CG   . PHE   A 219 ? 0.6954 0.6584 0.6852 0.0314  -0.0030 -0.0325 219 PHE   A CG   
1678 C  CD1  . PHE   A 219 ? 0.6919 0.6527 0.6839 0.0275  -0.0064 -0.0307 219 PHE   A CD1  
1679 C  CD2  . PHE   A 219 ? 0.6293 0.5989 0.6172 0.0333  0.0034  -0.0336 219 PHE   A CD2  
1680 C  CE1  . PHE   A 219 ? 0.6456 0.6091 0.6365 0.0260  -0.0038 -0.0301 219 PHE   A CE1  
1681 C  CE2  . PHE   A 219 ? 0.6267 0.5992 0.6138 0.0309  0.0062  -0.0328 219 PHE   A CE2  
1682 C  CZ   . PHE   A 219 ? 0.6389 0.6075 0.6268 0.0274  0.0025  -0.0311 219 PHE   A CZ   
1683 N  N    . LEU   A 220 ? 0.7997 0.7320 0.7555 0.0420  -0.0092 -0.0388 220 LEU   A N    
1684 C  CA   . LEU   A 220 ? 0.8204 0.7505 0.7652 0.0471  -0.0049 -0.0413 220 LEU   A CA   
1685 C  C    . LEU   A 220 ? 0.8756 0.7954 0.8103 0.0528  -0.0078 -0.0438 220 LEU   A C    
1686 O  O    . LEU   A 220 ? 0.8741 0.7809 0.8030 0.0524  -0.0151 -0.0440 220 LEU   A O    
1687 C  CB   . LEU   A 220 ? 0.7886 0.7120 0.7249 0.0460  -0.0053 -0.0413 220 LEU   A CB   
1688 C  CG   . LEU   A 220 ? 0.7610 0.6950 0.7059 0.0412  -0.0013 -0.0392 220 LEU   A CG   
1689 C  CD1  . LEU   A 220 ? 0.7327 0.6599 0.6676 0.0407  -0.0009 -0.0393 220 LEU   A CD1  
1690 C  CD2  . LEU   A 220 ? 0.6274 0.5762 0.5798 0.0417  0.0066  -0.0390 220 LEU   A CD2  
1691 N  N    . ASN   A 221 ? 0.9110 0.8366 0.8437 0.0581  -0.0025 -0.0457 221 ASN   A N    
1692 C  CA   . ASN   A 221 ? 0.9836 0.9008 0.9073 0.0645  -0.0048 -0.0482 221 ASN   A CA   
1693 C  C    . ASN   A 221 ? 1.0759 0.9887 0.9858 0.0711  -0.0011 -0.0509 221 ASN   A C    
1694 O  O    . ASN   A 221 ? 0.9177 0.8388 0.8279 0.0710  0.0055  -0.0508 221 ASN   A O    
1695 C  CB   . ASN   A 221 ? 0.9166 0.8438 0.8487 0.0668  -0.0021 -0.0486 221 ASN   A CB   
1696 C  CG   . ASN   A 221 ? 0.8859 0.8293 0.8234 0.0693  0.0067  -0.0494 221 ASN   A CG   
1697 O  OD1  . ASN   A 221 ? 0.8593 0.8086 0.7974 0.0673  0.0114  -0.0488 221 ASN   A OD1  
1698 N  ND2  . ASN   A 221 ? 0.8687 0.8191 0.8099 0.0737  0.0088  -0.0508 221 ASN   A ND2  
1699 N  N    . ARG   A 222 ? 1.3445 1.2438 1.2419 0.0768  -0.0054 -0.0533 222 ARG   A N    
1700 C  CA   . ARG   A 222 ? 1.4181 1.3120 1.3009 0.0847  -0.0023 -0.0562 222 ARG   A CA   
1701 C  C    . ARG   A 222 ? 1.3997 1.3071 1.2863 0.0908  0.0048  -0.0579 222 ARG   A C    
1702 O  O    . ARG   A 222 ? 1.4130 1.3179 1.2882 0.0984  0.0082  -0.0605 222 ARG   A O    
1703 C  CB   . ARG   A 222 ? 1.4527 1.3254 1.3199 0.0885  -0.0106 -0.0580 222 ARG   A CB   
1704 C  CG   . ARG   A 222 ? 1.4506 1.3135 1.3200 0.0808  -0.0189 -0.0557 222 ARG   A CG   
1705 C  CD   . ARG   A 222 ? 1.5357 1.3953 1.4006 0.0778  -0.0185 -0.0549 222 ARG   A CD   
1706 N  NE   . ARG   A 222 ? 1.4795 1.3539 1.3580 0.0716  -0.0135 -0.0524 222 ARG   A NE   
1707 C  CZ   . ARG   A 222 ? 1.4354 1.3116 1.3239 0.0642  -0.0176 -0.0498 222 ARG   A CZ   
1708 N  NH1  . ARG   A 222 ? 1.3853 1.2506 1.2731 0.0614  -0.0265 -0.0491 222 ARG   A NH1  
1709 N  NH2  . ARG   A 222 ? 1.4213 1.3101 1.3203 0.0596  -0.0128 -0.0477 222 ARG   A NH2  
1710 N  N    . PHE   A 223 ? 1.1127 1.0347 1.0147 0.0880  0.0073  -0.0567 223 PHE   A N    
1711 C  CA   . PHE   A 223 ? 1.0197 0.9540 0.9244 0.0945  0.0134  -0.0587 223 PHE   A CA   
1712 C  C    . PHE   A 223 ? 0.9686 0.9212 0.8828 0.0919  0.0222  -0.0576 223 PHE   A C    
1713 O  O    . PHE   A 223 ? 0.8941 0.8486 0.8120 0.0851  0.0234  -0.0552 223 PHE   A O    
1714 C  CB   . PHE   A 223 ? 1.0033 0.9438 0.9179 0.0951  0.0116  -0.0587 223 PHE   A CB   
1715 C  CG   . PHE   A 223 ? 1.0542 0.9780 0.9625 0.0954  0.0027  -0.0589 223 PHE   A CG   
1716 C  CD1  . PHE   A 223 ? 1.0939 0.9985 0.9886 0.0956  -0.0038 -0.0593 223 PHE   A CD1  
1717 C  CD2  . PHE   A 223 ? 1.0376 0.9646 0.9520 0.0969  0.0010  -0.0592 223 PHE   A CD2  
1718 C  CE1  . PHE   A 223 ? 1.1414 1.0311 1.0308 0.0950  -0.0120 -0.0593 223 PHE   A CE1  
1719 C  CE2  . PHE   A 223 ? 1.0455 0.9568 0.9533 0.0970  -0.0068 -0.0593 223 PHE   A CE2  
1720 C  CZ   . PHE   A 223 ? 1.0868 0.9796 0.9823 0.0958  -0.0133 -0.0592 223 PHE   A CZ   
1721 N  N    . THR   A 224 ? 0.9276 0.8937 0.8458 0.0973  0.0281  -0.0593 224 THR   A N    
1722 C  CA   . THR   A 224 ? 0.8876 0.8737 0.8183 0.0942  0.0361  -0.0581 224 THR   A CA   
1723 C  C    . THR   A 224 ? 0.8890 0.8886 0.8306 0.0975  0.0376  -0.0592 224 THR   A C    
1724 O  O    . THR   A 224 ? 0.9204 0.9124 0.8590 0.1020  0.0324  -0.0608 224 THR   A O    
1725 C  CB   . THR   A 224 ? 0.8297 0.8201 0.7527 0.0975  0.0433  -0.0590 224 THR   A CB   
1726 O  OG1  . THR   A 224 ? 0.7692 0.7762 0.7039 0.0913  0.0499  -0.0568 224 THR   A OG1  
1727 C  CG2  . THR   A 224 ? 0.8175 0.8120 0.7349 0.1081  0.0464  -0.0624 224 THR   A CG2  
1728 N  N    . THR   A 225 ? 0.8622 0.8811 0.8164 0.0951  0.0441  -0.0584 225 THR   A N    
1729 C  CA   . THR   A 225 ? 0.7935 0.8264 0.7583 0.0987  0.0457  -0.0598 225 THR   A CA   
1730 C  C    . THR   A 225 ? 0.7274 0.7812 0.7024 0.0969  0.0541  -0.0592 225 THR   A C    
1731 O  O    . THR   A 225 ? 0.6773 0.7336 0.6500 0.0932  0.0589  -0.0579 225 THR   A O    
1732 C  CB   . THR   A 225 ? 0.8172 0.8491 0.7917 0.0939  0.0404  -0.0581 225 THR   A CB   
1733 O  OG1  . THR   A 225 ? 0.8287 0.8683 0.8085 0.0997  0.0399  -0.0602 225 THR   A OG1  
1734 C  CG2  . THR   A 225 ? 0.6955 0.7377 0.6825 0.0842  0.0429  -0.0548 225 THR   A CG2  
1735 N  N    . THR   A 226 ? 0.7850 0.8537 0.7715 0.0993  0.0557  -0.0603 226 THR   A N    
1736 C  CA   . THR   A 226 ? 0.7593 0.8498 0.7579 0.0979  0.0628  -0.0600 226 THR   A CA   
1737 C  C    . THR   A 226 ? 0.7262 0.8253 0.7396 0.0898  0.0614  -0.0576 226 THR   A C    
1738 O  O    . THR   A 226 ? 0.7053 0.7956 0.7201 0.0880  0.0553  -0.0569 226 THR   A O    
1739 C  CB   . THR   A 226 ? 0.7524 0.8532 0.7520 0.1083  0.0648  -0.0636 226 THR   A CB   
1740 O  OG1  . THR   A 226 ? 0.7608 0.8540 0.7459 0.1158  0.0670  -0.0657 226 THR   A OG1  
1741 C  CG2  . THR   A 226 ? 0.7723 0.8975 0.7868 0.1071  0.0713  -0.0635 226 THR   A CG2  
1742 N  N    . LEU   A 227 ? 0.6341 0.7497 0.6578 0.0844  0.0671  -0.0560 227 LEU   A N    
1743 C  CA   . LEU   A 227 ? 0.6326 0.7574 0.6700 0.0777  0.0659  -0.0541 227 LEU   A CA   
1744 C  C    . LEU   A 227 ? 0.6645 0.7940 0.7086 0.0833  0.0622  -0.0563 227 LEU   A C    
1745 O  O    . LEU   A 227 ? 0.6672 0.7895 0.7137 0.0809  0.0568  -0.0553 227 LEU   A O    
1746 C  CB   . LEU   A 227 ? 0.5970 0.7400 0.6442 0.0721  0.0727  -0.0526 227 LEU   A CB   
1747 C  CG   . LEU   A 227 ? 0.5690 0.7071 0.6134 0.0626  0.0747  -0.0492 227 LEU   A CG   
1748 C  CD1  . LEU   A 227 ? 0.6304 0.7854 0.6815 0.0581  0.0822  -0.0479 227 LEU   A CD1  
1749 C  CD2  . LEU   A 227 ? 0.5412 0.6735 0.5907 0.0558  0.0696  -0.0469 227 LEU   A CD2  
1750 N  N    . ASN   A 228 ? 0.6859 0.8275 0.7325 0.0912  0.0652  -0.0592 228 ASN   A N    
1751 C  CA   . ASN   A 228 ? 0.7156 0.8618 0.7676 0.0975  0.0616  -0.0617 228 ASN   A CA   
1752 C  C    . ASN   A 228 ? 0.7727 0.8988 0.8146 0.1014  0.0543  -0.0625 228 ASN   A C    
1753 O  O    . ASN   A 228 ? 0.7723 0.8971 0.8187 0.1024  0.0497  -0.0629 228 ASN   A O    
1754 C  CB   . ASN   A 228 ? 0.6878 0.8483 0.7415 0.1069  0.0658  -0.0651 228 ASN   A CB   
1755 C  CG   . ASN   A 228 ? 0.6214 0.8050 0.6883 0.1028  0.0727  -0.0642 228 ASN   A CG   
1756 O  OD1  . ASN   A 228 ? 0.5652 0.7535 0.6400 0.0928  0.0738  -0.0611 228 ASN   A OD1  
1757 N  ND2  . ASN   A 228 ? 0.5901 0.7883 0.6593 0.1105  0.0775  -0.0668 228 ASN   A ND2  
1758 N  N    . ASP   A 229 ? 0.9618 1.0718 0.9897 0.1034  0.0529  -0.0628 229 ASP   A N    
1759 C  CA   . ASP   A 229 ? 0.9950 1.0856 1.0128 0.1066  0.0458  -0.0635 229 ASP   A CA   
1760 C  C    . ASP   A 229 ? 0.9603 1.0405 0.9799 0.0975  0.0416  -0.0600 229 ASP   A C    
1761 O  O    . ASP   A 229 ? 0.9632 1.0349 0.9824 0.0978  0.0362  -0.0598 229 ASP   A O    
1762 C  CB   . ASP   A 229 ? 1.0662 1.1434 1.0680 0.1126  0.0454  -0.0653 229 ASP   A CB   
1763 C  CG   . ASP   A 229 ? 1.1042 1.1910 1.1034 0.1232  0.0491  -0.0690 229 ASP   A CG   
1764 O  OD1  . ASP   A 229 ? 1.1589 1.2519 1.1627 0.1292  0.0474  -0.0712 229 ASP   A OD1  
1765 O  OD2  . ASP   A 229 ? 1.2012 1.2899 1.1940 0.1258  0.0540  -0.0697 229 ASP   A OD2  
1766 N  N    . PHE   A 230 ? 0.7808 0.8618 0.8020 0.0896  0.0442  -0.0573 230 PHE   A N    
1767 C  CA   . PHE   A 230 ? 0.6886 0.7629 0.7133 0.0813  0.0409  -0.0540 230 PHE   A CA   
1768 C  C    . PHE   A 230 ? 0.7201 0.8049 0.7574 0.0788  0.0403  -0.0532 230 PHE   A C    
1769 O  O    . PHE   A 230 ? 0.7271 0.8044 0.7660 0.0759  0.0359  -0.0515 230 PHE   A O    
1770 C  CB   . PHE   A 230 ? 0.6184 0.6931 0.6427 0.0740  0.0441  -0.0515 230 PHE   A CB   
1771 C  CG   . PHE   A 230 ? 0.6014 0.6741 0.6319 0.0658  0.0418  -0.0482 230 PHE   A CG   
1772 C  CD1  . PHE   A 230 ? 0.6108 0.6686 0.6357 0.0631  0.0369  -0.0466 230 PHE   A CD1  
1773 C  CD2  . PHE   A 230 ? 0.5653 0.6510 0.6071 0.0611  0.0444  -0.0467 230 PHE   A CD2  
1774 C  CE1  . PHE   A 230 ? 0.5683 0.6249 0.5990 0.0563  0.0350  -0.0436 230 PHE   A CE1  
1775 C  CE2  . PHE   A 230 ? 0.5748 0.6576 0.6209 0.0544  0.0422  -0.0439 230 PHE   A CE2  
1776 C  CZ   . PHE   A 230 ? 0.5401 0.6087 0.5807 0.0524  0.0377  -0.0424 230 PHE   A CZ   
1777 N  N    . ASN   A 231 ? 0.7010 0.8032 0.7474 0.0798  0.0447  -0.0541 231 ASN   A N    
1778 C  CA   . ASN   A 231 ? 0.6356 0.7479 0.6940 0.0766  0.0440  -0.0532 231 ASN   A CA   
1779 C  C    . ASN   A 231 ? 0.7693 0.8771 0.8276 0.0824  0.0391  -0.0550 231 ASN   A C    
1780 O  O    . ASN   A 231 ? 0.8051 0.9107 0.8681 0.0791  0.0360  -0.0534 231 ASN   A O    
1781 C  CB   . ASN   A 231 ? 0.6042 0.7365 0.6725 0.0758  0.0496  -0.0538 231 ASN   A CB   
1782 C  CG   . ASN   A 231 ? 0.5553 0.6919 0.6269 0.0665  0.0534  -0.0507 231 ASN   A CG   
1783 O  OD1  . ASN   A 231 ? 0.5405 0.6660 0.6083 0.0608  0.0513  -0.0482 231 ASN   A OD1  
1784 N  ND2  . ASN   A 231 ? 0.5166 0.6693 0.5950 0.0650  0.0588  -0.0510 231 ASN   A ND2  
1785 N  N    . LEU   A 232 ? 0.7205 0.8257 0.7722 0.0913  0.0383  -0.0582 232 LEU   A N    
1786 C  CA   . LEU   A 232 ? 0.6949 0.7923 0.7433 0.0973  0.0331  -0.0600 232 LEU   A CA   
1787 C  C    . LEU   A 232 ? 0.7401 0.8200 0.7828 0.0931  0.0279  -0.0575 232 LEU   A C    
1788 O  O    . LEU   A 232 ? 0.7170 0.7930 0.7614 0.0936  0.0242  -0.0572 232 LEU   A O    
1789 C  CB   . LEU   A 232 ? 0.7325 0.8258 0.7710 0.1075  0.0326  -0.0637 232 LEU   A CB   
1790 C  CG   . LEU   A 232 ? 0.8066 0.9155 0.8509 0.1157  0.0347  -0.0672 232 LEU   A CG   
1791 C  CD1  . LEU   A 232 ? 0.7914 0.9221 0.8483 0.1121  0.0412  -0.0667 232 LEU   A CD1  
1792 C  CD2  . LEU   A 232 ? 0.7895 0.8914 0.8214 0.1260  0.0342  -0.0707 232 LEU   A CD2  
1793 N  N    . VAL   A 233 ? 0.7626 0.8317 0.7982 0.0891  0.0276  -0.0558 233 VAL   A N    
1794 C  CA   . VAL   A 233 ? 0.7375 0.7917 0.7691 0.0842  0.0231  -0.0531 233 VAL   A CA   
1795 C  C    . VAL   A 233 ? 0.8200 0.8795 0.8612 0.0759  0.0240  -0.0497 233 VAL   A C    
1796 O  O    . VAL   A 233 ? 0.8709 0.9231 0.9128 0.0731  0.0206  -0.0477 233 VAL   A O    
1797 C  CB   . VAL   A 233 ? 0.8231 0.8645 0.8440 0.0833  0.0220  -0.0527 233 VAL   A CB   
1798 C  CG1  . VAL   A 233 ? 0.7961 0.8231 0.8137 0.0781  0.0171  -0.0499 233 VAL   A CG1  
1799 C  CG2  . VAL   A 233 ? 0.7748 0.8101 0.7847 0.0922  0.0212  -0.0562 233 VAL   A CG2  
1800 N  N    . ALA   A 234 ? 0.8832 0.9547 0.9310 0.0719  0.0286  -0.0489 234 ALA   A N    
1801 C  CA   . ALA   A 234 ? 0.8983 0.9745 0.9543 0.0647  0.0292  -0.0459 234 ALA   A CA   
1802 C  C    . ALA   A 234 ? 0.9119 0.9923 0.9744 0.0659  0.0272  -0.0460 234 ALA   A C    
1803 O  O    . ALA   A 234 ? 0.8993 0.9749 0.9639 0.0619  0.0250  -0.0435 234 ALA   A O    
1804 C  CB   . ALA   A 234 ? 0.7930 0.8813 0.8540 0.0608  0.0343  -0.0454 234 ALA   A CB   
1805 N  N    . MET   A 235 ? 0.8054 0.8940 0.8703 0.0723  0.0277  -0.0490 235 MET   A N    
1806 C  CA   . MET   A 235 ? 0.7948 0.8884 0.8658 0.0743  0.0258  -0.0497 235 MET   A CA   
1807 C  C    . MET   A 235 ? 0.8148 0.8940 0.8802 0.0754  0.0209  -0.0487 235 MET   A C    
1808 O  O    . MET   A 235 ? 0.8212 0.9000 0.8906 0.0730  0.0192  -0.0471 235 MET   A O    
1809 C  CB   . MET   A 235 ? 0.8750 0.9791 0.9486 0.0820  0.0265  -0.0535 235 MET   A CB   
1810 C  CG   . MET   A 235 ? 1.0353 1.1417 1.1141 0.0837  0.0233  -0.0538 235 MET   A CG   
1811 S  SD   . MET   A 235 ? 1.3281 1.4477 1.4122 0.0927  0.0227  -0.0582 235 MET   A SD   
1812 C  CE   . MET   A 235 ? 1.1218 1.2332 1.2058 0.0935  0.0172  -0.0575 235 MET   A CE   
1813 N  N    . LYS   A 236 ? 0.7729 0.8402 0.8286 0.0797  0.0184  -0.0499 236 LYS   A N    
1814 C  CA   . LYS   A 236 ? 0.8063 0.8596 0.8562 0.0805  0.0138  -0.0489 236 LYS   A CA   
1815 C  C    . LYS   A 236 ? 0.7492 0.7971 0.8012 0.0727  0.0132  -0.0448 236 LYS   A C    
1816 O  O    . LYS   A 236 ? 0.8121 0.8569 0.8658 0.0716  0.0114  -0.0432 236 LYS   A O    
1817 C  CB   . LYS   A 236 ? 0.8103 0.8498 0.8482 0.0850  0.0109  -0.0504 236 LYS   A CB   
1818 C  CG   . LYS   A 236 ? 0.8448 0.8861 0.8779 0.0946  0.0103  -0.0548 236 LYS   A CG   
1819 C  CD   . LYS   A 236 ? 0.9253 0.9648 0.9576 0.1003  0.0071  -0.0565 236 LYS   A CD   
1820 C  CE   . LYS   A 236 ? 0.9394 0.9819 0.9671 0.1105  0.0066  -0.0611 236 LYS   A CE   
1821 N  NZ   . LYS   A 236 ? 0.8245 0.8623 0.8498 0.1158  0.0027  -0.0625 236 LYS   A NZ   
1822 N  N    . TYR   A 237 ? 0.7204 0.7685 0.7729 0.0675  0.0151  -0.0430 237 TYR   A N    
1823 C  CA   . TYR   A 237 ? 0.6998 0.7438 0.7544 0.0607  0.0148  -0.0392 237 TYR   A CA   
1824 C  C    . TYR   A 237 ? 0.6277 0.6827 0.6910 0.0565  0.0175  -0.0377 237 TYR   A C    
1825 O  O    . TYR   A 237 ? 0.5676 0.6208 0.6328 0.0511  0.0178  -0.0348 237 TYR   A O    
1826 C  CB   . TYR   A 237 ? 0.6699 0.7070 0.7194 0.0578  0.0145  -0.0382 237 TYR   A CB   
1827 C  CG   . TYR   A 237 ? 0.7028 0.7265 0.7426 0.0608  0.0108  -0.0392 237 TYR   A CG   
1828 C  CD1  . TYR   A 237 ? 0.6644 0.6772 0.7015 0.0579  0.0073  -0.0367 237 TYR   A CD1  
1829 C  CD2  . TYR   A 237 ? 0.7410 0.7630 0.7741 0.0668  0.0107  -0.0425 237 TYR   A CD2  
1830 C  CE1  . TYR   A 237 ? 0.6516 0.6513 0.6795 0.0599  0.0034  -0.0374 237 TYR   A CE1  
1831 C  CE2  . TYR   A 237 ? 0.6658 0.6737 0.6886 0.0697  0.0067  -0.0435 237 TYR   A CE2  
1832 C  CZ   . TYR   A 237 ? 0.6768 0.6733 0.6970 0.0659  0.0028  -0.0408 237 TYR   A CZ   
1833 O  OH   . TYR   A 237 ? 0.7097 0.6914 0.7192 0.0681  -0.0016 -0.0416 237 TYR   A OH   
1834 N  N    . ASN   A 238 ? 0.5718 0.6379 0.6405 0.0591  0.0191  -0.0397 238 ASN   A N    
1835 C  CA   . ASN   A 238 ? 0.5709 0.6465 0.6474 0.0553  0.0209  -0.0385 238 ASN   A CA   
1836 C  C    . ASN   A 238 ? 0.5811 0.6591 0.6587 0.0494  0.0235  -0.0366 238 ASN   A C    
1837 O  O    . ASN   A 238 ? 0.5563 0.6337 0.6363 0.0447  0.0236  -0.0340 238 ASN   A O    
1838 C  CB   . ASN   A 238 ? 0.6292 0.7002 0.7070 0.0541  0.0186  -0.0364 238 ASN   A CB   
1839 C  CG   . ASN   A 238 ? 0.6251 0.6956 0.7025 0.0599  0.0161  -0.0385 238 ASN   A CG   
1840 O  OD1  . ASN   A 238 ? 0.5912 0.6714 0.6741 0.0618  0.0164  -0.0402 238 ASN   A OD1  
1841 N  ND2  . ASN   A 238 ? 0.6234 0.6824 0.6942 0.0625  0.0134  -0.0383 238 ASN   A ND2  
1842 N  N    . TYR   A 239 ? 0.6048 0.6844 0.6795 0.0501  0.0256  -0.0380 239 TYR   A N    
1843 C  CA   . TYR   A 239 ? 0.4896 0.5733 0.5651 0.0453  0.0287  -0.0369 239 TYR   A CA   
1844 C  C    . TYR   A 239 ? 0.4643 0.5621 0.5461 0.0450  0.0320  -0.0382 239 TYR   A C    
1845 O  O    . TYR   A 239 ? 0.5099 0.6148 0.5943 0.0500  0.0324  -0.0408 239 TYR   A O    
1846 C  CB   . TYR   A 239 ? 0.5800 0.6573 0.6479 0.0460  0.0294  -0.0374 239 TYR   A CB   
1847 C  CG   . TYR   A 239 ? 0.4893 0.5546 0.5523 0.0432  0.0268  -0.0352 239 TYR   A CG   
1848 C  CD1  . TYR   A 239 ? 0.5538 0.6123 0.6171 0.0430  0.0234  -0.0337 239 TYR   A CD1  
1849 C  CD2  . TYR   A 239 ? 0.4975 0.5592 0.5562 0.0403  0.0278  -0.0344 239 TYR   A CD2  
1850 C  CE1  . TYR   A 239 ? 0.6186 0.6679 0.6788 0.0400  0.0211  -0.0315 239 TYR   A CE1  
1851 C  CE2  . TYR   A 239 ? 0.5681 0.6200 0.6232 0.0376  0.0251  -0.0325 239 TYR   A CE2  
1852 C  CZ   . TYR   A 239 ? 0.5526 0.5990 0.6091 0.0373  0.0218  -0.0309 239 TYR   A CZ   
1853 O  OH   . TYR   A 239 ? 0.5032 0.5415 0.5574 0.0344  0.0192  -0.0289 239 TYR   A OH   
1854 N  N    . GLU   A 240 ? 0.4964 0.5982 0.5806 0.0392  0.0342  -0.0364 240 GLU   A N    
1855 C  CA   . GLU   A 240 ? 0.5840 0.6992 0.6739 0.0375  0.0377  -0.0373 240 GLU   A CA   
1856 C  C    . GLU   A 240 ? 0.5398 0.6595 0.6269 0.0406  0.0412  -0.0394 240 GLU   A C    
1857 O  O    . GLU   A 240 ? 0.4718 0.5828 0.5511 0.0409  0.0416  -0.0391 240 GLU   A O    
1858 C  CB   . GLU   A 240 ? 0.5745 0.6901 0.6652 0.0299  0.0390  -0.0346 240 GLU   A CB   
1859 C  CG   . GLU   A 240 ? 0.5112 0.6401 0.6076 0.0268  0.0426  -0.0350 240 GLU   A CG   
1860 C  CD   . GLU   A 240 ? 0.6144 0.7522 0.7195 0.0272  0.0408  -0.0356 240 GLU   A CD   
1861 O  OE1  . GLU   A 240 ? 0.5820 0.7136 0.6871 0.0292  0.0369  -0.0353 240 GLU   A OE1  
1862 O  OE2  . GLU   A 240 ? 0.5857 0.7367 0.6974 0.0256  0.0433  -0.0365 240 GLU   A OE2  
1863 N  N    . PRO   A 241 ? 0.5286 0.6619 0.6218 0.0432  0.0437  -0.0415 241 PRO   A N    
1864 C  CA   . PRO   A 241 ? 0.5841 0.7225 0.6744 0.0470  0.0476  -0.0435 241 PRO   A CA   
1865 C  C    . PRO   A 241 ? 0.5645 0.7041 0.6519 0.0411  0.0519  -0.0417 241 PRO   A C    
1866 O  O    . PRO   A 241 ? 0.6009 0.7443 0.6923 0.0342  0.0530  -0.0395 241 PRO   A O    
1867 C  CB   . PRO   A 241 ? 0.5604 0.7153 0.6600 0.0507  0.0491  -0.0459 241 PRO   A CB   
1868 C  CG   . PRO   A 241 ? 0.6276 0.7814 0.7322 0.0513  0.0444  -0.0458 241 PRO   A CG   
1869 C  CD   . PRO   A 241 ? 0.5783 0.7230 0.6811 0.0440  0.0427  -0.0424 241 PRO   A CD   
1870 N  N    . LEU   A 242 ? 0.5384 0.6738 0.6179 0.0441  0.0542  -0.0427 242 LEU   A N    
1871 C  CA   . LEU   A 242 ? 0.5602 0.6933 0.6341 0.0391  0.0580  -0.0410 242 LEU   A CA   
1872 C  C    . LEU   A 242 ? 0.5001 0.6491 0.5790 0.0383  0.0642  -0.0416 242 LEU   A C    
1873 O  O    . LEU   A 242 ? 0.4911 0.6489 0.5720 0.0448  0.0663  -0.0442 242 LEU   A O    
1874 C  CB   . LEU   A 242 ? 0.5396 0.6587 0.6013 0.0425  0.0571  -0.0416 242 LEU   A CB   
1875 C  CG   . LEU   A 242 ? 0.5553 0.6662 0.6095 0.0368  0.0585  -0.0394 242 LEU   A CG   
1876 C  CD1  . LEU   A 242 ? 0.4879 0.5915 0.5438 0.0313  0.0544  -0.0368 242 LEU   A CD1  
1877 C  CD2  . LEU   A 242 ? 0.6036 0.7019 0.6456 0.0409  0.0578  -0.0404 242 LEU   A CD2  
1878 N  N    . THR   A 243 ? 0.5134 0.6661 0.5938 0.0304  0.0671  -0.0392 243 THR   A N    
1879 C  CA   . THR   A 243 ? 0.5010 0.6687 0.5860 0.0279  0.0735  -0.0390 243 THR   A CA   
1880 C  C    . THR   A 243 ? 0.4820 0.6435 0.5561 0.0264  0.0779  -0.0381 243 THR   A C    
1881 O  O    . THR   A 243 ? 0.5092 0.6544 0.5725 0.0263  0.0756  -0.0374 243 THR   A O    
1882 C  CB   . THR   A 243 ? 0.5041 0.6803 0.5979 0.0192  0.0738  -0.0367 243 THR   A CB   
1883 O  OG1  . THR   A 243 ? 0.5063 0.6696 0.5925 0.0123  0.0727  -0.0338 243 THR   A OG1  
1884 C  CG2  . THR   A 243 ? 0.4669 0.6472 0.5702 0.0206  0.0688  -0.0374 243 THR   A CG2  
1885 N  N    . GLN   A 244 ? 0.5707 0.7457 0.6477 0.0254  0.0846  -0.0382 244 GLN   A N    
1886 C  CA   . GLN   A 244 ? 0.5964 0.7662 0.6628 0.0228  0.0896  -0.0368 244 GLN   A CA   
1887 C  C    . GLN   A 244 ? 0.4981 0.6595 0.5607 0.0130  0.0888  -0.0334 244 GLN   A C    
1888 O  O    . GLN   A 244 ? 0.5061 0.6547 0.5564 0.0112  0.0898  -0.0322 244 GLN   A O    
1889 C  CB   . GLN   A 244 ? 0.5124 0.7002 0.5835 0.0237  0.0975  -0.0374 244 GLN   A CB   
1890 C  CG   . GLN   A 244 ? 0.5250 0.7074 0.5844 0.0211  0.1034  -0.0359 244 GLN   A CG   
1891 C  CD   . GLN   A 244 ? 0.5472 0.7120 0.5914 0.0281  0.1015  -0.0374 244 GLN   A CD   
1892 O  OE1  . GLN   A 244 ? 0.6534 0.8180 0.6967 0.0372  0.0998  -0.0404 244 GLN   A OE1  
1893 N  NE2  . GLN   A 244 ? 0.5615 0.7105 0.5933 0.0239  0.1010  -0.0355 244 GLN   A NE2  
1894 N  N    . ASP   A 245 ? 0.4464 0.6136 0.5183 0.0069  0.0867  -0.0319 245 ASP   A N    
1895 C  CA   . ASP   A 245 ? 0.4928 0.6500 0.5599 -0.0017 0.0850  -0.0288 245 ASP   A CA   
1896 C  C    . ASP   A 245 ? 0.5187 0.6565 0.5763 0.0002  0.0792  -0.0286 245 ASP   A C    
1897 O  O    . ASP   A 245 ? 0.4453 0.5707 0.4928 -0.0039 0.0789  -0.0267 245 ASP   A O    
1898 C  CB   . ASP   A 245 ? 0.5205 0.6872 0.5991 -0.0076 0.0831  -0.0275 245 ASP   A CB   
1899 C  CG   . ASP   A 245 ? 0.5643 0.7508 0.6529 -0.0106 0.0887  -0.0274 245 ASP   A CG   
1900 O  OD1  . ASP   A 245 ? 0.7219 0.9110 0.8062 -0.0154 0.0944  -0.0257 245 ASP   A OD1  
1901 O  OD2  . ASP   A 245 ? 0.6613 0.8613 0.7620 -0.0075 0.0876  -0.0291 245 ASP   A OD2  
1902 N  N    . HIS   A 246 ? 0.5054 0.6405 0.5663 0.0063  0.0744  -0.0305 246 HIS   A N    
1903 C  CA   . HIS   A 246 ? 0.4907 0.6090 0.5434 0.0088  0.0693  -0.0304 246 HIS   A CA   
1904 C  C    . HIS   A 246 ? 0.4993 0.6079 0.5396 0.0118  0.0711  -0.0311 246 HIS   A C    
1905 O  O    . HIS   A 246 ? 0.4769 0.5712 0.5080 0.0102  0.0684  -0.0300 246 HIS   A O    
1906 C  CB   . HIS   A 246 ? 0.5106 0.6289 0.5687 0.0151  0.0647  -0.0324 246 HIS   A CB   
1907 C  CG   . HIS   A 246 ? 0.5007 0.6271 0.5698 0.0131  0.0624  -0.0319 246 HIS   A CG   
1908 N  ND1  . HIS   A 246 ? 0.4942 0.6258 0.5701 0.0187  0.0599  -0.0339 246 HIS   A ND1  
1909 C  CD2  . HIS   A 246 ? 0.5029 0.6318 0.5762 0.0065  0.0617  -0.0298 246 HIS   A CD2  
1910 C  CE1  . HIS   A 246 ? 0.4903 0.6274 0.5743 0.0156  0.0579  -0.0331 246 HIS   A CE1  
1911 N  NE2  . HIS   A 246 ? 0.4679 0.6035 0.5505 0.0082  0.0589  -0.0306 246 HIS   A NE2  
1912 N  N    . VAL   A 247 ? 0.4946 0.6104 0.5342 0.0167  0.0754  -0.0331 247 VAL   A N    
1913 C  CA   . VAL   A 247 ? 0.5048 0.6104 0.5314 0.0201  0.0770  -0.0338 247 VAL   A CA   
1914 C  C    . VAL   A 247 ? 0.5656 0.6670 0.5841 0.0136  0.0808  -0.0315 247 VAL   A C    
1915 O  O    . VAL   A 247 ? 0.5973 0.6837 0.6037 0.0134  0.0791  -0.0310 247 VAL   A O    
1916 C  CB   . VAL   A 247 ? 0.4994 0.6135 0.5261 0.0278  0.0808  -0.0366 247 VAL   A CB   
1917 C  CG1  . VAL   A 247 ? 0.5069 0.6106 0.5189 0.0309  0.0834  -0.0372 247 VAL   A CG1  
1918 C  CG2  . VAL   A 247 ? 0.4822 0.5955 0.5132 0.0346  0.0759  -0.0390 247 VAL   A CG2  
1919 N  N    . ASP   A 248 ? 0.5655 0.6795 0.5905 0.0078  0.0857  -0.0299 248 ASP   A N    
1920 C  CA   . ASP   A 248 ? 0.5276 0.6373 0.5452 0.0002  0.0891  -0.0272 248 ASP   A CA   
1921 C  C    . ASP   A 248 ? 0.5773 0.6700 0.5873 -0.0035 0.0834  -0.0255 248 ASP   A C    
1922 O  O    . ASP   A 248 ? 0.6034 0.6822 0.6002 -0.0032 0.0830  -0.0251 248 ASP   A O    
1923 C  CB   . ASP   A 248 ? 0.5444 0.6698 0.5726 -0.0069 0.0931  -0.0254 248 ASP   A CB   
1924 C  CG   . ASP   A 248 ? 0.5542 0.6975 0.5890 -0.0045 0.1001  -0.0265 248 ASP   A CG   
1925 O  OD1  . ASP   A 248 ? 0.6155 0.7567 0.6420 0.0007  0.1040  -0.0278 248 ASP   A OD1  
1926 O  OD2  . ASP   A 248 ? 0.5148 0.6745 0.5629 -0.0077 0.1017  -0.0261 248 ASP   A OD2  
1927 N  N    . ILE   A 249 ? 0.5612 0.6548 0.5792 -0.0063 0.0787  -0.0247 249 ILE   A N    
1928 C  CA   . ILE   A 249 ? 0.4994 0.5794 0.5114 -0.0104 0.0740  -0.0228 249 ILE   A CA   
1929 C  C    . ILE   A 249 ? 0.4970 0.5625 0.5012 -0.0053 0.0689  -0.0239 249 ILE   A C    
1930 O  O    . ILE   A 249 ? 0.4835 0.5363 0.4800 -0.0077 0.0654  -0.0225 249 ILE   A O    
1931 C  CB   . ILE   A 249 ? 0.5390 0.6248 0.5618 -0.0137 0.0707  -0.0218 249 ILE   A CB   
1932 C  CG1  . ILE   A 249 ? 0.5655 0.6410 0.5820 -0.0202 0.0682  -0.0193 249 ILE   A CG1  
1933 C  CG2  . ILE   A 249 ? 0.5692 0.6544 0.5986 -0.0078 0.0654  -0.0234 249 ILE   A CG2  
1934 C  CD1  . ILE   A 249 ? 0.5043 0.5861 0.5299 -0.0246 0.0661  -0.0180 249 ILE   A CD1  
1935 N  N    . LEU   A 250 ? 0.5430 0.6097 0.5486 0.0016  0.0681  -0.0262 250 LEU   A N    
1936 C  CA   . LEU   A 250 ? 0.5796 0.6324 0.5766 0.0060  0.0637  -0.0273 250 LEU   A CA   
1937 C  C    . LEU   A 250 ? 0.5402 0.5846 0.5234 0.0071  0.0667  -0.0276 250 LEU   A C    
1938 O  O    . LEU   A 250 ? 0.5236 0.5550 0.4980 0.0103  0.0627  -0.0284 250 LEU   A O    
1939 C  CB   . LEU   A 250 ? 0.5580 0.6141 0.5612 0.0127  0.0610  -0.0296 250 LEU   A CB   
1940 C  CG   . LEU   A 250 ? 0.4760 0.5342 0.4892 0.0120  0.0561  -0.0290 250 LEU   A CG   
1941 C  CD1  . LEU   A 250 ? 0.4293 0.4936 0.4500 0.0177  0.0547  -0.0310 250 LEU   A CD1  
1942 C  CD2  . LEU   A 250 ? 0.4535 0.4984 0.4619 0.0111  0.0504  -0.0278 250 LEU   A CD2  
1943 N  N    . GLY   A 251 ? 0.5039 0.5549 0.4848 0.0041  0.0733  -0.0268 251 GLY   A N    
1944 C  CA   . GLY   A 251 ? 0.5661 0.6098 0.5335 0.0047  0.0773  -0.0268 251 GLY   A CA   
1945 C  C    . GLY   A 251 ? 0.5694 0.5943 0.5231 0.0042  0.0729  -0.0263 251 GLY   A C    
1946 O  O    . GLY   A 251 ? 0.6231 0.6379 0.5677 0.0094  0.0708  -0.0279 251 GLY   A O    
1947 N  N    . PRO   A 252 ? 0.5749 0.5942 0.5261 -0.0020 0.0712  -0.0240 252 PRO   A N    
1948 C  CA   . PRO   A 252 ? 0.5851 0.5865 0.5230 -0.0021 0.0667  -0.0236 252 PRO   A CA   
1949 C  C    . PRO   A 252 ? 0.5762 0.5693 0.5141 0.0033  0.0594  -0.0253 252 PRO   A C    
1950 O  O    . PRO   A 252 ? 0.5769 0.5564 0.5028 0.0057  0.0564  -0.0260 252 PRO   A O    
1951 C  CB   . PRO   A 252 ? 0.5892 0.5884 0.5279 -0.0089 0.0652  -0.0211 252 PRO   A CB   
1952 C  CG   . PRO   A 252 ? 0.6529 0.6665 0.5994 -0.0137 0.0715  -0.0198 252 PRO   A CG   
1953 C  CD   . PRO   A 252 ? 0.6212 0.6490 0.5800 -0.0089 0.0732  -0.0218 252 PRO   A CD   
1954 N  N    . LEU   A 253 ? 0.5930 0.5940 0.5438 0.0053  0.0564  -0.0260 253 LEU   A N    
1955 C  CA   . LEU   A 253 ? 0.5697 0.5637 0.5215 0.0097  0.0495  -0.0273 253 LEU   A CA   
1956 C  C    . LEU   A 253 ? 0.5695 0.5598 0.5152 0.0158  0.0499  -0.0297 253 LEU   A C    
1957 O  O    . LEU   A 253 ? 0.5426 0.5204 0.4799 0.0185  0.0450  -0.0306 253 LEU   A O    
1958 C  CB   . LEU   A 253 ? 0.5387 0.5417 0.5051 0.0097  0.0468  -0.0271 253 LEU   A CB   
1959 C  CG   . LEU   A 253 ? 0.5721 0.5772 0.5445 0.0049  0.0450  -0.0249 253 LEU   A CG   
1960 C  CD1  . LEU   A 253 ? 0.4608 0.4749 0.4470 0.0061  0.0428  -0.0249 253 LEU   A CD1  
1961 C  CD2  . LEU   A 253 ? 0.5548 0.5471 0.5196 0.0039  0.0399  -0.0240 253 LEU   A CD2  
1962 N  N    . SER   A 254 ? 0.5691 0.5701 0.5187 0.0182  0.0552  -0.0308 254 SER   A N    
1963 C  CA   . SER   A 254 ? 0.5982 0.5953 0.5396 0.0244  0.0565  -0.0331 254 SER   A CA   
1964 C  C    . SER   A 254 ? 0.5800 0.5643 0.5048 0.0245  0.0579  -0.0330 254 SER   A C    
1965 O  O    . SER   A 254 ? 0.6321 0.6057 0.5467 0.0295  0.0554  -0.0348 254 SER   A O    
1966 C  CB   . SER   A 254 ? 0.5800 0.5920 0.5277 0.0268  0.0632  -0.0341 254 SER   A CB   
1967 O  OG   . SER   A 254 ? 0.5688 0.5866 0.5134 0.0230  0.0705  -0.0327 254 SER   A OG   
1968 N  N    . ALA   A 255 ? 0.6130 0.5972 0.5339 0.0189  0.0617  -0.0309 255 ALA   A N    
1969 C  CA   . ALA   A 255 ? 0.6166 0.5877 0.5207 0.0185  0.0631  -0.0306 255 ALA   A CA   
1970 C  C    . ALA   A 255 ? 0.6316 0.5860 0.5276 0.0194  0.0548  -0.0309 255 ALA   A C    
1971 O  O    . ALA   A 255 ? 0.6367 0.5789 0.5207 0.0238  0.0523  -0.0325 255 ALA   A O    
1972 C  CB   . ALA   A 255 ? 0.6173 0.5923 0.5197 0.0115  0.0688  -0.0280 255 ALA   A CB   
1973 N  N    . GLN   A 256 ? 0.6498 0.6036 0.5522 0.0153  0.0502  -0.0294 256 GLN   A N    
1974 C  CA   . GLN   A 256 ? 0.6820 0.6227 0.5797 0.0161  0.0419  -0.0296 256 GLN   A CA   
1975 C  C    . GLN   A 256 ? 0.7123 0.6476 0.6098 0.0216  0.0362  -0.0318 256 GLN   A C    
1976 O  O    . GLN   A 256 ? 0.7719 0.6933 0.6586 0.0239  0.0312  -0.0327 256 GLN   A O    
1977 C  CB   . GLN   A 256 ? 0.6448 0.5904 0.5537 0.0121  0.0385  -0.0279 256 GLN   A CB   
1978 C  CG   . GLN   A 256 ? 0.6962 0.6298 0.6004 0.0121  0.0309  -0.0276 256 GLN   A CG   
1979 C  CD   . GLN   A 256 ? 0.8289 0.7673 0.7421 0.0084  0.0288  -0.0258 256 GLN   A CD   
1980 O  OE1  . GLN   A 256 ? 0.8593 0.8086 0.7809 0.0053  0.0331  -0.0246 256 GLN   A OE1  
1981 N  NE2  . GLN   A 256 ? 0.8418 0.7721 0.7530 0.0090  0.0220  -0.0256 256 GLN   A NE2  
1982 N  N    . THR   A 257 ? 0.6440 0.5894 0.5532 0.0238  0.0364  -0.0326 257 THR   A N    
1983 C  CA   . THR   A 257 ? 0.6865 0.6262 0.5962 0.0282  0.0301  -0.0344 257 THR   A CA   
1984 C  C    . THR   A 257 ? 0.6754 0.6092 0.5742 0.0339  0.0318  -0.0367 257 THR   A C    
1985 O  O    . THR   A 257 ? 0.6610 0.5848 0.5549 0.0374  0.0257  -0.0382 257 THR   A O    
1986 C  CB   . THR   A 257 ? 0.6217 0.5728 0.5475 0.0280  0.0286  -0.0341 257 THR   A CB   
1987 O  OG1  . THR   A 257 ? 0.6488 0.6136 0.5814 0.0278  0.0358  -0.0341 257 THR   A OG1  
1988 C  CG2  . THR   A 257 ? 0.6146 0.5678 0.5493 0.0236  0.0248  -0.0321 257 THR   A CG2  
1989 N  N    . GLY   A 258 ? 0.6408 0.5805 0.5355 0.0350  0.0399  -0.0370 258 GLY   A N    
1990 C  CA   . GLY   A 258 ? 0.6254 0.5615 0.5108 0.0413  0.0422  -0.0393 258 GLY   A CA   
1991 C  C    . GLY   A 258 ? 0.6178 0.5616 0.5123 0.0455  0.0413  -0.0408 258 GLY   A C    
1992 O  O    . GLY   A 258 ? 0.6635 0.5988 0.5497 0.0514  0.0386  -0.0431 258 GLY   A O    
1993 N  N    . ILE   A 259 ? 0.6099 0.5684 0.5203 0.0427  0.0430  -0.0398 259 ILE   A N    
1994 C  CA   . ILE   A 259 ? 0.5951 0.5606 0.5143 0.0465  0.0417  -0.0412 259 ILE   A CA   
1995 C  C    . ILE   A 259 ? 0.6160 0.5998 0.5459 0.0458  0.0492  -0.0409 259 ILE   A C    
1996 O  O    . ILE   A 259 ? 0.6176 0.6105 0.5576 0.0401  0.0509  -0.0389 259 ILE   A O    
1997 C  CB   . ILE   A 259 ? 0.5695 0.5335 0.4985 0.0439  0.0344  -0.0403 259 ILE   A CB   
1998 C  CG1  . ILE   A 259 ? 0.5949 0.5423 0.5148 0.0439  0.0267  -0.0405 259 ILE   A CG1  
1999 C  CG2  . ILE   A 259 ? 0.6605 0.6301 0.5967 0.0479  0.0332  -0.0418 259 ILE   A CG2  
2000 C  CD1  . ILE   A 259 ? 0.5960 0.5431 0.5259 0.0401  0.0203  -0.0390 259 ILE   A CD1  
2001 N  N    . ALA   A 260 ? 0.6222 0.6113 0.5499 0.0518  0.0533  -0.0430 260 ALA   A N    
2002 C  CA   . ALA   A 260 ? 0.6397 0.6474 0.5781 0.0518  0.0602  -0.0430 260 ALA   A CA   
2003 C  C    . ALA   A 260 ? 0.6587 0.6760 0.6129 0.0495  0.0574  -0.0423 260 ALA   A C    
2004 O  O    . ALA   A 260 ? 0.6953 0.7054 0.6512 0.0508  0.0507  -0.0428 260 ALA   A O    
2005 C  CB   . ALA   A 260 ? 0.7149 0.7259 0.6479 0.0602  0.0640  -0.0457 260 ALA   A CB   
2006 N  N    . VAL   A 261 ? 0.6738 0.7071 0.6394 0.0459  0.0624  -0.0412 261 VAL   A N    
2007 C  CA   . VAL   A 261 ? 0.5857 0.6275 0.5655 0.0432  0.0598  -0.0404 261 VAL   A CA   
2008 C  C    . VAL   A 261 ? 0.5947 0.6370 0.5775 0.0499  0.0565  -0.0427 261 VAL   A C    
2009 O  O    . VAL   A 261 ? 0.5779 0.6146 0.5643 0.0495  0.0505  -0.0424 261 VAL   A O    
2010 C  CB   . VAL   A 261 ? 0.5055 0.5644 0.4962 0.0386  0.0657  -0.0390 261 VAL   A CB   
2011 C  CG1  . VAL   A 261 ? 0.5531 0.6210 0.5577 0.0375  0.0630  -0.0388 261 VAL   A CG1  
2012 C  CG2  . VAL   A 261 ? 0.4573 0.5131 0.4449 0.0309  0.0673  -0.0363 261 VAL   A CG2  
2013 N  N    . LEU   A 262 ? 0.6153 0.6635 0.5955 0.0565  0.0604  -0.0451 262 LEU   A N    
2014 C  CA   . LEU   A 262 ? 0.6240 0.6720 0.6053 0.0637  0.0574  -0.0477 262 LEU   A CA   
2015 C  C    . LEU   A 262 ? 0.6522 0.6813 0.6235 0.0663  0.0499  -0.0484 262 LEU   A C    
2016 O  O    . LEU   A 262 ? 0.6269 0.6529 0.6006 0.0693  0.0452  -0.0495 262 LEU   A O    
2017 C  CB   . LEU   A 262 ? 0.5730 0.6295 0.5510 0.0710  0.0631  -0.0502 262 LEU   A CB   
2018 C  CG   . LEU   A 262 ? 0.5559 0.6335 0.5460 0.0686  0.0703  -0.0496 262 LEU   A CG   
2019 C  CD1  . LEU   A 262 ? 0.5022 0.5902 0.4908 0.0769  0.0757  -0.0523 262 LEU   A CD1  
2020 C  CD2  . LEU   A 262 ? 0.5573 0.6440 0.5622 0.0649  0.0676  -0.0487 262 LEU   A CD2  
2021 N  N    . ASP   A 263 ? 0.6625 0.6785 0.6221 0.0651  0.0485  -0.0480 263 ASP   A N    
2022 C  CA   . ASP   A 263 ? 0.6892 0.6877 0.6404 0.0666  0.0407  -0.0485 263 ASP   A CA   
2023 C  C    . ASP   A 263 ? 0.6240 0.6211 0.5846 0.0607  0.0353  -0.0462 263 ASP   A C    
2024 O  O    . ASP   A 263 ? 0.5728 0.5627 0.5335 0.0622  0.0295  -0.0467 263 ASP   A O    
2025 C  CB   . ASP   A 263 ? 0.7249 0.7097 0.6617 0.0664  0.0398  -0.0484 263 ASP   A CB   
2026 C  CG   . ASP   A 263 ? 0.6960 0.6789 0.6208 0.0737  0.0443  -0.0509 263 ASP   A CG   
2027 O  OD1  . ASP   A 263 ? 0.6535 0.6483 0.5828 0.0784  0.0488  -0.0524 263 ASP   A OD1  
2028 O  OD2  . ASP   A 263 ? 0.7316 0.7012 0.6423 0.0750  0.0430  -0.0513 263 ASP   A OD2  
2029 N  N    . MET   A 264 ? 0.6467 0.6504 0.6146 0.0539  0.0374  -0.0437 264 MET   A N    
2030 C  CA   . MET   A 264 ? 0.5855 0.5903 0.5633 0.0488  0.0334  -0.0416 264 MET   A CA   
2031 C  C    . MET   A 264 ? 0.5478 0.5621 0.5361 0.0506  0.0334  -0.0421 264 MET   A C    
2032 O  O    . MET   A 264 ? 0.5388 0.5496 0.5317 0.0494  0.0286  -0.0412 264 MET   A O    
2033 C  CB   . MET   A 264 ? 0.5341 0.5438 0.5161 0.0422  0.0360  -0.0391 264 MET   A CB   
2034 C  CG   . MET   A 264 ? 0.5054 0.5129 0.4941 0.0375  0.0314  -0.0369 264 MET   A CG   
2035 S  SD   . MET   A 264 ? 0.5782 0.5686 0.5582 0.0375  0.0239  -0.0367 264 MET   A SD   
2036 C  CE   . MET   A 264 ? 0.5135 0.4993 0.4863 0.0334  0.0254  -0.0354 264 MET   A CE   
2037 N  N    . CYS   A 265 ? 0.5521 0.5786 0.5441 0.0536  0.0388  -0.0434 265 CYS   A N    
2038 C  CA   . CYS   A 265 ? 0.5260 0.5608 0.5266 0.0565  0.0385  -0.0444 265 CYS   A CA   
2039 C  C    . CYS   A 265 ? 0.5880 0.6125 0.5823 0.0626  0.0336  -0.0465 265 CYS   A C    
2040 O  O    . CYS   A 265 ? 0.6152 0.6417 0.6150 0.0643  0.0311  -0.0468 265 CYS   A O    
2041 C  CB   . CYS   A 265 ? 0.4934 0.5438 0.4991 0.0590  0.0450  -0.0458 265 CYS   A CB   
2042 S  SG   . CYS   A 265 ? 0.6378 0.7007 0.6522 0.0510  0.0501  -0.0431 265 CYS   A SG   
2043 N  N    . ALA   A 266 ? 0.6250 0.6376 0.6065 0.0662  0.0319  -0.0479 266 ALA   A N    
2044 C  CA   . ALA   A 266 ? 0.6578 0.6583 0.6316 0.0716  0.0265  -0.0498 266 ALA   A CA   
2045 C  C    . ALA   A 266 ? 0.6650 0.6531 0.6381 0.0669  0.0195  -0.0478 266 ALA   A C    
2046 O  O    . ALA   A 266 ? 0.6628 0.6436 0.6345 0.0689  0.0147  -0.0482 266 ALA   A O    
2047 C  CB   . ALA   A 266 ? 0.6827 0.6746 0.6421 0.0781  0.0272  -0.0523 266 ALA   A CB   
2048 N  N    . SER   A 267 ? 0.6748 0.6601 0.6484 0.0609  0.0188  -0.0455 267 SER   A N    
2049 C  CA   . SER   A 267 ? 0.6539 0.6311 0.6299 0.0559  0.0128  -0.0433 267 SER   A CA   
2050 C  C    . SER   A 267 ? 0.6567 0.6428 0.6455 0.0529  0.0128  -0.0415 267 SER   A C    
2051 O  O    . SER   A 267 ? 0.6643 0.6445 0.6548 0.0519  0.0080  -0.0406 267 SER   A O    
2052 C  CB   . SER   A 267 ? 0.6305 0.6045 0.6048 0.0509  0.0123  -0.0415 267 SER   A CB   
2053 O  OG   . SER   A 267 ? 0.6472 0.6075 0.6086 0.0530  0.0090  -0.0428 267 SER   A OG   
2054 N  N    . LEU   A 268 ? 0.6008 0.6005 0.5980 0.0513  0.0181  -0.0409 268 LEU   A N    
2055 C  CA   . LEU   A 268 ? 0.6107 0.6185 0.6191 0.0489  0.0183  -0.0393 268 LEU   A CA   
2056 C  C    . LEU   A 268 ? 0.6024 0.6092 0.6108 0.0539  0.0165  -0.0410 268 LEU   A C    
2057 O  O    . LEU   A 268 ? 0.6307 0.6345 0.6429 0.0522  0.0132  -0.0396 268 LEU   A O    
2058 C  CB   . LEU   A 268 ? 0.5486 0.5704 0.5646 0.0466  0.0240  -0.0387 268 LEU   A CB   
2059 C  CG   . LEU   A 268 ? 0.5325 0.5633 0.5596 0.0444  0.0246  -0.0373 268 LEU   A CG   
2060 C  CD1  . LEU   A 268 ? 0.5837 0.6085 0.6139 0.0408  0.0203  -0.0348 268 LEU   A CD1  
2061 C  CD2  . LEU   A 268 ? 0.5510 0.5923 0.5833 0.0407  0.0292  -0.0363 268 LEU   A CD2  
2062 N  N    . LYS   A 269 ? 0.5939 0.6025 0.5972 0.0602  0.0187  -0.0440 269 LYS   A N    
2063 C  CA   . LYS   A 269 ? 0.6785 0.6848 0.6800 0.0660  0.0166  -0.0460 269 LYS   A CA   
2064 C  C    . LYS   A 269 ? 0.7158 0.7062 0.7106 0.0657  0.0098  -0.0454 269 LYS   A C    
2065 O  O    . LYS   A 269 ? 0.7492 0.7378 0.7474 0.0653  0.0071  -0.0445 269 LYS   A O    
2066 C  CB   . LYS   A 269 ? 0.6915 0.7005 0.6864 0.0737  0.0195  -0.0495 269 LYS   A CB   
2067 C  CG   . LYS   A 269 ? 0.6816 0.6859 0.6721 0.0807  0.0166  -0.0519 269 LYS   A CG   
2068 C  CD   . LYS   A 269 ? 0.7458 0.7454 0.7246 0.0889  0.0174  -0.0553 269 LYS   A CD   
2069 C  CE   . LYS   A 269 ? 0.7881 0.8047 0.7721 0.0940  0.0238  -0.0575 269 LYS   A CE   
2070 N  NZ   . LYS   A 269 ? 0.8396 0.8526 0.8120 0.1034  0.0250  -0.0611 269 LYS   A NZ   
2071 N  N    . GLU   A 270 ? 0.8322 0.8107 0.8171 0.0657  0.0069  -0.0457 270 GLU   A N    
2072 C  CA   . GLU   A 270 ? 0.9136 0.8770 0.8927 0.0642  0.0000  -0.0448 270 GLU   A CA   
2073 C  C    . GLU   A 270 ? 0.8939 0.8592 0.8829 0.0568  -0.0019 -0.0411 270 GLU   A C    
2074 O  O    . GLU   A 270 ? 0.8873 0.8457 0.8763 0.0555  -0.0060 -0.0400 270 GLU   A O    
2075 C  CB   . GLU   A 270 ? 0.9058 0.8565 0.8734 0.0645  -0.0032 -0.0456 270 GLU   A CB   
2076 C  CG   . GLU   A 270 ? 0.8854 0.8297 0.8403 0.0728  -0.0029 -0.0492 270 GLU   A CG   
2077 C  CD   . GLU   A 270 ? 0.9468 0.8799 0.8945 0.0771  -0.0079 -0.0506 270 GLU   A CD   
2078 O  OE1  . GLU   A 270 ? 0.9768 0.8956 0.9189 0.0741  -0.0144 -0.0495 270 GLU   A OE1  
2079 O  OE2  . GLU   A 270 ? 1.0893 1.0279 1.0372 0.0833  -0.0056 -0.0528 270 GLU   A OE2  
2080 N  N    . LEU   A 271 ? 0.7486 0.7231 0.7454 0.0521  0.0013  -0.0392 271 LEU   A N    
2081 C  CA   . LEU   A 271 ? 0.6549 0.6317 0.6605 0.0458  -0.0001 -0.0358 271 LEU   A CA   
2082 C  C    . LEU   A 271 ? 0.6687 0.6525 0.6823 0.0459  0.0013  -0.0349 271 LEU   A C    
2083 O  O    . LEU   A 271 ? 0.7083 0.6910 0.7271 0.0418  -0.0008 -0.0322 271 LEU   A O    
2084 C  CB   . LEU   A 271 ? 0.6243 0.6080 0.6341 0.0419  0.0029  -0.0345 271 LEU   A CB   
2085 C  CG   . LEU   A 271 ? 0.6608 0.6422 0.6745 0.0360  0.0000  -0.0316 271 LEU   A CG   
2086 C  CD1  . LEU   A 271 ? 0.5954 0.5635 0.6012 0.0355  -0.0058 -0.0318 271 LEU   A CD1  
2087 C  CD2  . LEU   A 271 ? 0.5632 0.5511 0.5788 0.0339  0.0036  -0.0311 271 LEU   A CD2  
2088 N  N    . LEU   A 272 ? 0.6524 0.6435 0.6670 0.0506  0.0047  -0.0371 272 LEU   A N    
2089 C  CA   . LEU   A 272 ? 0.6284 0.6246 0.6489 0.0517  0.0053  -0.0367 272 LEU   A CA   
2090 C  C    . LEU   A 272 ? 0.6708 0.6562 0.6847 0.0552  0.0011  -0.0377 272 LEU   A C    
2091 O  O    . LEU   A 272 ? 0.7432 0.7279 0.7606 0.0541  -0.0001 -0.0362 272 LEU   A O    
2092 C  CB   . LEU   A 272 ? 0.5947 0.6038 0.6198 0.0553  0.0101  -0.0387 272 LEU   A CB   
2093 C  CG   . LEU   A 272 ? 0.5981 0.6182 0.6308 0.0508  0.0142  -0.0372 272 LEU   A CG   
2094 C  CD1  . LEU   A 272 ? 0.6192 0.6524 0.6583 0.0531  0.0182  -0.0386 272 LEU   A CD1  
2095 C  CD2  . LEU   A 272 ? 0.6118 0.6309 0.6500 0.0449  0.0128  -0.0337 272 LEU   A CD2  
2096 N  N    . GLN   A 273 ? 0.6686 0.6446 0.6719 0.0595  -0.0012 -0.0401 273 GLN   A N    
2097 C  CA   . GLN   A 273 ? 0.6870 0.6518 0.6821 0.0638  -0.0053 -0.0415 273 GLN   A CA   
2098 C  C    . GLN   A 273 ? 0.6806 0.6312 0.6712 0.0591  -0.0110 -0.0391 273 GLN   A C    
2099 O  O    . GLN   A 273 ? 0.7743 0.7178 0.7630 0.0589  -0.0140 -0.0382 273 GLN   A O    
2100 C  CB   . GLN   A 273 ? 0.7419 0.7024 0.7264 0.0716  -0.0054 -0.0455 273 GLN   A CB   
2101 C  CG   . GLN   A 273 ? 0.6962 0.6714 0.6853 0.0768  0.0002  -0.0481 273 GLN   A CG   
2102 C  CD   . GLN   A 273 ? 0.7615 0.7342 0.7408 0.0837  0.0013  -0.0515 273 GLN   A CD   
2103 O  OE1  . GLN   A 273 ? 0.8634 0.8227 0.8320 0.0842  -0.0022 -0.0520 273 GLN   A OE1  
2104 N  NE2  . GLN   A 273 ? 0.7569 0.7426 0.7397 0.0891  0.0061  -0.0540 273 GLN   A NE2  
2105 N  N    . ASN   A 274 ? 0.7197 0.6657 0.7082 0.0552  -0.0128 -0.0381 274 ASN   A N    
2106 C  CA   . ASN   A 274 ? 0.6942 0.6276 0.6790 0.0503  -0.0186 -0.0359 274 ASN   A CA   
2107 C  C    . ASN   A 274 ? 0.6762 0.6160 0.6720 0.0425  -0.0182 -0.0319 274 ASN   A C    
2108 O  O    . ASN   A 274 ? 0.6787 0.6107 0.6739 0.0375  -0.0227 -0.0296 274 ASN   A O    
2109 C  CB   . ASN   A 274 ? 0.7070 0.6290 0.6806 0.0518  -0.0223 -0.0377 274 ASN   A CB   
2110 C  CG   . ASN   A 274 ? 0.7379 0.6556 0.7005 0.0606  -0.0216 -0.0419 274 ASN   A CG   
2111 O  OD1  . ASN   A 274 ? 0.8289 0.7503 0.7884 0.0638  -0.0186 -0.0439 274 ASN   A OD1  
2112 N  ND2  . ASN   A 274 ? 0.7790 0.6891 0.7352 0.0648  -0.0240 -0.0432 274 ASN   A ND2  
2113 N  N    . GLY   A 275 ? 0.7326 0.6865 0.7381 0.0414  -0.0129 -0.0312 275 GLY   A N    
2114 C  CA   . GLY   A 275 ? 0.7013 0.6620 0.7170 0.0351  -0.0121 -0.0276 275 GLY   A CA   
2115 C  C    . GLY   A 275 ? 0.7569 0.7139 0.7716 0.0312  -0.0148 -0.0267 275 GLY   A C    
2116 O  O    . GLY   A 275 ? 0.7961 0.7440 0.8016 0.0330  -0.0178 -0.0286 275 GLY   A O    
2117 N  N    . MET   A 276 ? 0.8210 0.7848 0.8448 0.0262  -0.0141 -0.0237 276 MET   A N    
2118 C  CA   . MET   A 276 ? 0.8691 0.8319 0.8933 0.0230  -0.0162 -0.0229 276 MET   A CA   
2119 C  C    . MET   A 276 ? 0.9213 0.8742 0.9435 0.0190  -0.0227 -0.0213 276 MET   A C    
2120 O  O    . MET   A 276 ? 0.9514 0.9032 0.9743 0.0163  -0.0253 -0.0207 276 MET   A O    
2121 C  CB   . MET   A 276 ? 0.8403 0.8145 0.8747 0.0198  -0.0131 -0.0205 276 MET   A CB   
2122 C  CG   . MET   A 276 ? 0.7235 0.7043 0.7574 0.0219  -0.0087 -0.0221 276 MET   A CG   
2123 S  SD   . MET   A 276 ? 0.6576 0.6481 0.7015 0.0179  -0.0069 -0.0190 276 MET   A SD   
2124 C  CE   . MET   A 276 ? 0.5327 0.5316 0.5766 0.0204  -0.0009 -0.0206 276 MET   A CE   
2125 N  N    . ASN   A 277 ? 0.9554 0.9008 0.9749 0.0185  -0.0256 -0.0207 277 ASN   A N    
2126 C  CA   . ASN   A 277 ? 1.0864 1.0214 1.1033 0.0141  -0.0323 -0.0191 277 ASN   A CA   
2127 C  C    . ASN   A 277 ? 1.0082 0.9500 1.0359 0.0077  -0.0337 -0.0156 277 ASN   A C    
2128 O  O    . ASN   A 277 ? 1.0166 0.9524 1.0428 0.0044  -0.0391 -0.0151 277 ASN   A O    
2129 C  CB   . ASN   A 277 ? 1.0820 1.0043 1.0864 0.0167  -0.0368 -0.0221 277 ASN   A CB   
2130 C  CG   . ASN   A 277 ? 1.1196 1.0297 1.1123 0.0210  -0.0390 -0.0243 277 ASN   A CG   
2131 O  OD1  . ASN   A 277 ? 1.1820 1.0820 1.1713 0.0180  -0.0440 -0.0230 277 ASN   A OD1  
2132 N  ND2  . ASN   A 277 ? 1.1469 1.0580 1.1333 0.0280  -0.0353 -0.0277 277 ASN   A ND2  
2133 N  N    . GLY   A 278 ? 0.9536 0.9078 0.9918 0.0063  -0.0290 -0.0133 278 GLY   A N    
2134 C  CA   . GLY   A 278 ? 0.9482 0.9097 0.9971 0.0009  -0.0300 -0.0098 278 GLY   A CA   
2135 C  C    . GLY   A 278 ? 0.8840 0.8490 0.9348 0.0003  -0.0313 -0.0103 278 GLY   A C    
2136 O  O    . GLY   A 278 ? 0.9191 0.8891 0.9781 -0.0040 -0.0334 -0.0077 278 GLY   A O    
2137 N  N    . ARG   A 279 ? 0.7999 0.7624 0.8433 0.0044  -0.0302 -0.0135 279 ARG   A N    
2138 C  CA   . ARG   A 279 ? 0.7974 0.7628 0.8417 0.0041  -0.0309 -0.0140 279 ARG   A CA   
2139 C  C    . ARG   A 279 ? 0.7969 0.7714 0.8431 0.0071  -0.0245 -0.0147 279 ARG   A C    
2140 O  O    . ARG   A 279 ? 0.7638 0.7428 0.8114 0.0091  -0.0199 -0.0149 279 ARG   A O    
2141 C  CB   . ARG   A 279 ? 0.9193 0.8725 0.9521 0.0056  -0.0358 -0.0168 279 ARG   A CB   
2142 C  CG   . ARG   A 279 ? 0.9284 0.8731 0.9492 0.0106  -0.0345 -0.0201 279 ARG   A CG   
2143 C  CD   . ARG   A 279 ? 1.0150 0.9455 1.0242 0.0114  -0.0408 -0.0222 279 ARG   A CD   
2144 N  NE   . ARG   A 279 ? 1.0721 0.9944 1.0692 0.0169  -0.0397 -0.0254 279 ARG   A NE   
2145 C  CZ   . ARG   A 279 ? 1.0619 0.9742 1.0497 0.0200  -0.0415 -0.0272 279 ARG   A CZ   
2146 N  NH1  . ARG   A 279 ? 1.0842 0.9820 1.0601 0.0212  -0.0474 -0.0290 279 ARG   A NH1  
2147 N  NH2  . ARG   A 279 ? 0.9938 0.9106 0.9809 0.0243  -0.0361 -0.0285 279 ARG   A NH2  
2148 N  N    . THR   A 280 ? 0.7504 0.7274 0.7967 0.0070  -0.0247 -0.0151 280 THR   A N    
2149 C  CA   . THR   A 280 ? 0.6571 0.6435 0.7075 0.0081  -0.0195 -0.0146 280 THR   A CA   
2150 C  C    . THR   A 280 ? 0.6073 0.5907 0.6493 0.0106  -0.0181 -0.0171 280 THR   A C    
2151 O  O    . THR   A 280 ? 0.6239 0.6006 0.6603 0.0104  -0.0220 -0.0181 280 THR   A O    
2152 C  CB   . THR   A 280 ? 0.6254 0.6192 0.6855 0.0053  -0.0207 -0.0117 280 THR   A CB   
2153 O  OG1  . THR   A 280 ? 0.6478 0.6373 0.7060 0.0039  -0.0260 -0.0120 280 THR   A OG1  
2154 C  CG2  . THR   A 280 ? 0.6206 0.6179 0.6891 0.0025  -0.0215 -0.0088 280 THR   A CG2  
2155 N  N    . ILE   A 281 ? 0.6054 0.5934 0.6462 0.0128  -0.0125 -0.0180 281 ILE   A N    
2156 C  CA   . ILE   A 281 ? 0.6316 0.6183 0.6652 0.0144  -0.0101 -0.0198 281 ILE   A CA   
2157 C  C    . ILE   A 281 ? 0.6133 0.6068 0.6516 0.0132  -0.0079 -0.0182 281 ILE   A C    
2158 O  O    . ILE   A 281 ? 0.5064 0.5074 0.5507 0.0131  -0.0044 -0.0170 281 ILE   A O    
2159 C  CB   . ILE   A 281 ? 0.5969 0.5845 0.6259 0.0173  -0.0054 -0.0219 281 ILE   A CB   
2160 C  CG1  . ILE   A 281 ? 0.6343 0.6155 0.6590 0.0194  -0.0075 -0.0235 281 ILE   A CG1  
2161 C  CG2  . ILE   A 281 ? 0.5225 0.5076 0.5431 0.0185  -0.0031 -0.0236 281 ILE   A CG2  
2162 C  CD1  . ILE   A 281 ? 0.6254 0.6087 0.6462 0.0231  -0.0030 -0.0257 281 ILE   A CD1  
2163 N  N    . LEU   A 282 ? 0.7064 0.6965 0.7411 0.0126  -0.0104 -0.0183 282 LEU   A N    
2164 C  CA   . LEU   A 282 ? 0.6330 0.6275 0.6698 0.0120  -0.0090 -0.0170 282 LEU   A CA   
2165 C  C    . LEU   A 282 ? 0.6005 0.6033 0.6484 0.0110  -0.0089 -0.0143 282 LEU   A C    
2166 O  O    . LEU   A 282 ? 0.6180 0.6261 0.6684 0.0113  -0.0058 -0.0133 282 LEU   A O    
2167 C  CB   . LEU   A 282 ? 0.5923 0.5884 0.6242 0.0128  -0.0037 -0.0180 282 LEU   A CB   
2168 C  CG   . LEU   A 282 ? 0.6583 0.6470 0.6786 0.0135  -0.0031 -0.0199 282 LEU   A CG   
2169 C  CD1  . LEU   A 282 ? 0.6546 0.6465 0.6718 0.0131  0.0024  -0.0202 282 LEU   A CD1  
2170 C  CD2  . LEU   A 282 ? 0.7113 0.6941 0.7277 0.0131  -0.0077 -0.0197 282 LEU   A CD2  
2171 N  N    . GLY   A 283 ? 0.5181 0.5215 0.5721 0.0096  -0.0125 -0.0131 283 GLY   A N    
2172 C  CA   . GLY   A 283 ? 0.5204 0.5317 0.5846 0.0086  -0.0125 -0.0103 283 GLY   A CA   
2173 C  C    . GLY   A 283 ? 0.5401 0.5566 0.6093 0.0088  -0.0086 -0.0091 283 GLY   A C    
2174 O  O    . GLY   A 283 ? 0.5622 0.5852 0.6394 0.0081  -0.0079 -0.0066 283 GLY   A O    
2175 N  N    . SER   A 284 ? 0.4894 0.5035 0.5541 0.0100  -0.0059 -0.0109 284 SER   A N    
2176 C  CA   . SER   A 284 ? 0.4793 0.4969 0.5475 0.0106  -0.0027 -0.0102 284 SER   A CA   
2177 C  C    . SER   A 284 ? 0.5605 0.5728 0.6268 0.0104  -0.0047 -0.0111 284 SER   A C    
2178 O  O    . SER   A 284 ? 0.5727 0.5781 0.6321 0.0110  -0.0069 -0.0132 284 SER   A O    
2179 C  CB   . SER   A 284 ? 0.4393 0.4590 0.5041 0.0125  0.0017  -0.0117 284 SER   A CB   
2180 O  OG   . SER   A 284 ? 0.5053 0.5279 0.5697 0.0125  0.0032  -0.0112 284 SER   A OG   
2181 N  N    . ALA   A 285 ? 0.5500 0.5643 0.6211 0.0099  -0.0041 -0.0094 285 ALA   A N    
2182 C  CA   . ALA   A 285 ? 0.4993 0.5074 0.5671 0.0102  -0.0057 -0.0103 285 ALA   A CA   
2183 C  C    . ALA   A 285 ? 0.4829 0.4918 0.5480 0.0134  -0.0022 -0.0121 285 ALA   A C    
2184 O  O    . ALA   A 285 ? 0.5462 0.5500 0.6080 0.0146  -0.0033 -0.0130 285 ALA   A O    
2185 C  CB   . ALA   A 285 ? 0.5110 0.5191 0.5845 0.0073  -0.0078 -0.0074 285 ALA   A CB   
2186 N  N    . LEU   A 286 ? 0.4797 0.4946 0.5458 0.0149  0.0016  -0.0126 286 LEU   A N    
2187 C  CA   . LEU   A 286 ? 0.4846 0.5014 0.5483 0.0178  0.0047  -0.0146 286 LEU   A CA   
2188 C  C    . LEU   A 286 ? 0.5537 0.5718 0.6131 0.0189  0.0066  -0.0168 286 LEU   A C    
2189 O  O    . LEU   A 286 ? 0.5020 0.5192 0.5598 0.0173  0.0058  -0.0166 286 LEU   A O    
2190 C  CB   . LEU   A 286 ? 0.4919 0.5150 0.5611 0.0182  0.0075  -0.0130 286 LEU   A CB   
2191 C  CG   . LEU   A 286 ? 0.5955 0.6178 0.6687 0.0171  0.0065  -0.0103 286 LEU   A CG   
2192 C  CD1  . LEU   A 286 ? 0.5265 0.5548 0.6043 0.0175  0.0094  -0.0084 286 LEU   A CD1  
2193 C  CD2  . LEU   A 286 ? 0.5208 0.5374 0.5909 0.0187  0.0052  -0.0112 286 LEU   A CD2  
2194 N  N    . LEU   A 287 ? 0.4955 0.5158 0.5528 0.0215  0.0092  -0.0190 287 LEU   A N    
2195 C  CA   . LEU   A 287 ? 0.4206 0.4435 0.4743 0.0223  0.0119  -0.0210 287 LEU   A CA   
2196 C  C    . LEU   A 287 ? 0.4784 0.5081 0.5358 0.0207  0.0148  -0.0199 287 LEU   A C    
2197 O  O    . LEU   A 287 ? 0.4877 0.5221 0.5494 0.0214  0.0162  -0.0195 287 LEU   A O    
2198 C  CB   . LEU   A 287 ? 0.4026 0.4261 0.4532 0.0260  0.0133  -0.0238 287 LEU   A CB   
2199 C  CG   . LEU   A 287 ? 0.4753 0.4900 0.5204 0.0278  0.0099  -0.0249 287 LEU   A CG   
2200 C  CD1  . LEU   A 287 ? 0.4906 0.5052 0.5332 0.0324  0.0105  -0.0273 287 LEU   A CD1  
2201 C  CD2  . LEU   A 287 ? 0.5245 0.5339 0.5626 0.0275  0.0090  -0.0260 287 LEU   A CD2  
2202 N  N    . GLU   A 288 ? 0.4490 0.4782 0.5039 0.0187  0.0153  -0.0195 288 GLU   A N    
2203 C  CA   . GLU   A 288 ? 0.4151 0.4485 0.4720 0.0169  0.0171  -0.0182 288 GLU   A CA   
2204 C  C    . GLU   A 288 ? 0.4482 0.4860 0.5033 0.0166  0.0207  -0.0197 288 GLU   A C    
2205 O  O    . GLU   A 288 ? 0.5169 0.5532 0.5669 0.0167  0.0219  -0.0212 288 GLU   A O    
2206 C  CB   . GLU   A 288 ? 0.3816 0.4112 0.4360 0.0149  0.0153  -0.0168 288 GLU   A CB   
2207 C  CG   . GLU   A 288 ? 0.4298 0.4571 0.4877 0.0147  0.0119  -0.0150 288 GLU   A CG   
2208 C  CD   . GLU   A 288 ? 0.5360 0.5668 0.5987 0.0142  0.0121  -0.0125 288 GLU   A CD   
2209 O  OE1  . GLU   A 288 ? 0.4851 0.5196 0.5491 0.0145  0.0145  -0.0123 288 GLU   A OE1  
2210 O  OE2  . GLU   A 288 ? 0.5341 0.5640 0.5992 0.0137  0.0096  -0.0109 288 GLU   A OE2  
2211 N  N    . ASP   A 289 ? 0.4563 0.4996 0.5154 0.0161  0.0223  -0.0191 289 ASP   A N    
2212 C  CA   . ASP   A 289 ? 0.4457 0.4948 0.5049 0.0155  0.0254  -0.0204 289 ASP   A CA   
2213 C  C    . ASP   A 289 ? 0.5220 0.5727 0.5807 0.0122  0.0265  -0.0191 289 ASP   A C    
2214 O  O    . ASP   A 289 ? 0.5209 0.5773 0.5812 0.0110  0.0287  -0.0197 289 ASP   A O    
2215 C  CB   . ASP   A 289 ? 0.4840 0.5389 0.5484 0.0182  0.0260  -0.0216 289 ASP   A CB   
2216 C  CG   . ASP   A 289 ? 0.5556 0.6113 0.6244 0.0184  0.0247  -0.0200 289 ASP   A CG   
2217 O  OD1  . ASP   A 289 ? 0.5548 0.6064 0.6234 0.0175  0.0231  -0.0179 289 ASP   A OD1  
2218 O  OD2  . ASP   A 289 ? 0.5345 0.5953 0.6070 0.0200  0.0254  -0.0210 289 ASP   A OD2  
2219 N  N    . GLU   A 290 ? 0.5416 0.5871 0.5978 0.0109  0.0247  -0.0172 290 GLU   A N    
2220 C  CA   . GLU   A 290 ? 0.5088 0.5537 0.5630 0.0083  0.0250  -0.0159 290 GLU   A CA   
2221 C  C    . GLU   A 290 ? 0.4957 0.5349 0.5423 0.0059  0.0250  -0.0156 290 GLU   A C    
2222 O  O    . GLU   A 290 ? 0.5144 0.5497 0.5575 0.0045  0.0239  -0.0141 290 GLU   A O    
2223 C  CB   . GLU   A 290 ? 0.5374 0.5808 0.5942 0.0095  0.0229  -0.0140 290 GLU   A CB   
2224 C  CG   . GLU   A 290 ? 0.5704 0.6186 0.6326 0.0109  0.0233  -0.0140 290 GLU   A CG   
2225 C  CD   . GLU   A 290 ? 0.5889 0.6353 0.6517 0.0118  0.0220  -0.0120 290 GLU   A CD   
2226 O  OE1  . GLU   A 290 ? 0.6072 0.6563 0.6735 0.0133  0.0221  -0.0120 290 GLU   A OE1  
2227 O  OE2  . GLU   A 290 ? 0.5770 0.6190 0.6361 0.0114  0.0209  -0.0106 290 GLU   A OE2  
2228 N  N    . PHE   A 291 ? 0.5276 0.5652 0.5703 0.0057  0.0261  -0.0169 291 PHE   A N    
2229 C  CA   . PHE   A 291 ? 0.5388 0.5712 0.5731 0.0032  0.0270  -0.0169 291 PHE   A CA   
2230 C  C    . PHE   A 291 ? 0.4855 0.5228 0.5186 0.0015  0.0310  -0.0182 291 PHE   A C    
2231 O  O    . PHE   A 291 ? 0.4746 0.5150 0.5094 0.0038  0.0323  -0.0198 291 PHE   A O    
2232 C  CB   . PHE   A 291 ? 0.5076 0.5328 0.5367 0.0046  0.0246  -0.0172 291 PHE   A CB   
2233 C  CG   . PHE   A 291 ? 0.4577 0.4798 0.4892 0.0063  0.0207  -0.0160 291 PHE   A CG   
2234 C  CD1  . PHE   A 291 ? 0.4599 0.4770 0.4872 0.0055  0.0188  -0.0146 291 PHE   A CD1  
2235 C  CD2  . PHE   A 291 ? 0.4931 0.5169 0.5305 0.0087  0.0189  -0.0161 291 PHE   A CD2  
2236 C  CE1  . PHE   A 291 ? 0.5291 0.5449 0.5593 0.0075  0.0154  -0.0135 291 PHE   A CE1  
2237 C  CE2  . PHE   A 291 ? 0.5177 0.5400 0.5582 0.0098  0.0156  -0.0147 291 PHE   A CE2  
2238 C  CZ   . PHE   A 291 ? 0.5208 0.5398 0.5582 0.0094  0.0140  -0.0134 291 PHE   A CZ   
2239 N  N    . THR   A 292 ? 0.4607 0.4986 0.4907 -0.0025 0.0330  -0.0174 292 THR   A N    
2240 C  CA   . THR   A 292 ? 0.5239 0.5675 0.5532 -0.0045 0.0374  -0.0184 292 THR   A CA   
2241 C  C    . THR   A 292 ? 0.5289 0.5666 0.5494 -0.0043 0.0388  -0.0191 292 THR   A C    
2242 O  O    . THR   A 292 ? 0.5410 0.5691 0.5549 -0.0035 0.0360  -0.0187 292 THR   A O    
2243 C  CB   . THR   A 292 ? 0.4853 0.5313 0.5138 -0.0099 0.0392  -0.0171 292 THR   A CB   
2244 O  OG1  . THR   A 292 ? 0.5138 0.5493 0.5333 -0.0124 0.0372  -0.0155 292 THR   A OG1  
2245 C  CG2  . THR   A 292 ? 0.4771 0.5300 0.5143 -0.0099 0.0381  -0.0168 292 THR   A CG2  
2246 N  N    . PRO   A 293 ? 0.4881 0.5314 0.5082 -0.0045 0.0431  -0.0202 293 PRO   A N    
2247 C  CA   . PRO   A 293 ? 0.4880 0.5249 0.4978 -0.0050 0.0451  -0.0206 293 PRO   A CA   
2248 C  C    . PRO   A 293 ? 0.5493 0.5766 0.5498 -0.0092 0.0442  -0.0188 293 PRO   A C    
2249 O  O    . PRO   A 293 ? 0.5166 0.5332 0.5080 -0.0081 0.0420  -0.0188 293 PRO   A O    
2250 C  CB   . PRO   A 293 ? 0.4907 0.5380 0.5030 -0.0061 0.0509  -0.0214 293 PRO   A CB   
2251 C  CG   . PRO   A 293 ? 0.5162 0.5741 0.5402 -0.0030 0.0506  -0.0226 293 PRO   A CG   
2252 C  CD   . PRO   A 293 ? 0.4682 0.5244 0.4969 -0.0042 0.0464  -0.0213 293 PRO   A CD   
2253 N  N    . PHE   A 294 ? 0.5991 0.6293 0.6011 -0.0140 0.0453  -0.0173 294 PHE   A N    
2254 C  CA   . PHE   A 294 ? 0.5976 0.6176 0.5897 -0.0181 0.0441  -0.0155 294 PHE   A CA   
2255 C  C    . PHE   A 294 ? 0.5915 0.6016 0.5802 -0.0152 0.0384  -0.0152 294 PHE   A C    
2256 O  O    . PHE   A 294 ? 0.5469 0.5458 0.5247 -0.0156 0.0368  -0.0147 294 PHE   A O    
2257 C  CB   . PHE   A 294 ? 0.6205 0.6453 0.6157 -0.0236 0.0453  -0.0140 294 PHE   A CB   
2258 C  CG   . PHE   A 294 ? 0.7777 0.7917 0.7609 -0.0288 0.0450  -0.0121 294 PHE   A CG   
2259 C  CD1  . PHE   A 294 ? 0.8228 0.8299 0.7947 -0.0308 0.0477  -0.0119 294 PHE   A CD1  
2260 C  CD2  . PHE   A 294 ? 0.7683 0.7777 0.7500 -0.0313 0.0418  -0.0106 294 PHE   A CD2  
2261 C  CE1  . PHE   A 294 ? 0.8219 0.8177 0.7814 -0.0356 0.0473  -0.0101 294 PHE   A CE1  
2262 C  CE2  . PHE   A 294 ? 0.8467 0.8446 0.8159 -0.0360 0.0411  -0.0090 294 PHE   A CE2  
2263 C  CZ   . PHE   A 294 ? 0.8943 0.8852 0.8523 -0.0382 0.0438  -0.0087 294 PHE   A CZ   
2264 N  N    . ASP   A 295 ? 0.5432 0.5574 0.5410 -0.0122 0.0355  -0.0153 295 ASP   A N    
2265 C  CA   . ASP   A 295 ? 0.5477 0.5546 0.5438 -0.0092 0.0305  -0.0149 295 ASP   A CA   
2266 C  C    . ASP   A 295 ? 0.5546 0.5549 0.5451 -0.0063 0.0288  -0.0159 295 ASP   A C    
2267 O  O    . ASP   A 295 ? 0.5481 0.5391 0.5312 -0.0057 0.0256  -0.0155 295 ASP   A O    
2268 C  CB   . ASP   A 295 ? 0.5316 0.5451 0.5388 -0.0061 0.0285  -0.0148 295 ASP   A CB   
2269 C  CG   . ASP   A 295 ? 0.5835 0.6026 0.5957 -0.0084 0.0294  -0.0139 295 ASP   A CG   
2270 O  OD1  . ASP   A 295 ? 0.6200 0.6376 0.6272 -0.0128 0.0311  -0.0132 295 ASP   A OD1  
2271 O  OD2  . ASP   A 295 ? 0.6118 0.6363 0.6324 -0.0059 0.0283  -0.0140 295 ASP   A OD2  
2272 N  N    . VAL   A 296 ? 0.5711 0.5757 0.5647 -0.0041 0.0305  -0.0175 296 VAL   A N    
2273 C  CA   . VAL   A 296 ? 0.5726 0.5702 0.5607 -0.0012 0.0284  -0.0186 296 VAL   A CA   
2274 C  C    . VAL   A 296 ? 0.4873 0.4751 0.4618 -0.0031 0.0294  -0.0186 296 VAL   A C    
2275 O  O    . VAL   A 296 ? 0.5225 0.5008 0.4901 -0.0016 0.0255  -0.0187 296 VAL   A O    
2276 C  CB   . VAL   A 296 ? 0.5635 0.5667 0.5564 0.0017  0.0300  -0.0204 296 VAL   A CB   
2277 C  CG1  . VAL   A 296 ? 0.5504 0.5450 0.5365 0.0046  0.0271  -0.0216 296 VAL   A CG1  
2278 C  CG2  . VAL   A 296 ? 0.5054 0.5164 0.5102 0.0036  0.0285  -0.0203 296 VAL   A CG2  
2279 N  N    . VAL   A 297 ? 0.5191 0.5092 0.4897 -0.0066 0.0344  -0.0182 297 VAL   A N    
2280 C  CA   . VAL   A 297 ? 0.6096 0.5897 0.5661 -0.0087 0.0360  -0.0180 297 VAL   A CA   
2281 C  C    . VAL   A 297 ? 0.5936 0.5629 0.5422 -0.0100 0.0319  -0.0167 297 VAL   A C    
2282 O  O    . VAL   A 297 ? 0.5923 0.5501 0.5298 -0.0087 0.0294  -0.0171 297 VAL   A O    
2283 C  CB   . VAL   A 297 ? 0.5516 0.5375 0.5064 -0.0132 0.0426  -0.0173 297 VAL   A CB   
2284 C  CG1  . VAL   A 297 ? 0.5877 0.5622 0.5270 -0.0161 0.0443  -0.0165 297 VAL   A CG1  
2285 C  CG2  . VAL   A 297 ? 0.5216 0.5176 0.4826 -0.0108 0.0467  -0.0189 297 VAL   A CG2  
2286 N  N    . ARG   A 298 ? 0.5581 0.5305 0.5117 -0.0120 0.0308  -0.0154 298 ARG   A N    
2287 C  CA   . ARG   A 298 ? 0.5608 0.5231 0.5064 -0.0129 0.0271  -0.0142 298 ARG   A CA   
2288 C  C    . ARG   A 298 ? 0.5872 0.5441 0.5328 -0.0080 0.0211  -0.0148 298 ARG   A C    
2289 O  O    . ARG   A 298 ? 0.6673 0.6128 0.6019 -0.0073 0.0179  -0.0147 298 ARG   A O    
2290 C  CB   . ARG   A 298 ? 0.6595 0.6269 0.6111 -0.0154 0.0272  -0.0128 298 ARG   A CB   
2291 C  CG   . ARG   A 298 ? 0.7309 0.6880 0.6741 -0.0158 0.0232  -0.0116 298 ARG   A CG   
2292 C  CD   . ARG   A 298 ? 0.7456 0.7052 0.6904 -0.0199 0.0244  -0.0101 298 ARG   A CD   
2293 N  NE   . ARG   A 298 ? 0.8230 0.7939 0.7818 -0.0179 0.0241  -0.0101 298 ARG   A NE   
2294 C  CZ   . ARG   A 298 ? 0.8139 0.7964 0.7826 -0.0197 0.0277  -0.0105 298 ARG   A CZ   
2295 N  NH1  . ARG   A 298 ? 0.7862 0.7718 0.7531 -0.0232 0.0322  -0.0107 298 ARG   A NH1  
2296 N  NH2  . ARG   A 298 ? 0.7354 0.7264 0.7155 -0.0175 0.0269  -0.0106 298 ARG   A NH2  
2297 N  N    . GLN   A 299 ? 0.5216 0.4864 0.4792 -0.0045 0.0193  -0.0155 299 GLN   A N    
2298 C  CA   . GLN   A 299 ? 0.5572 0.5189 0.5167 -0.0005 0.0137  -0.0158 299 GLN   A CA   
2299 C  C    . GLN   A 299 ? 0.6253 0.5806 0.5791 0.0017  0.0116  -0.0173 299 GLN   A C    
2300 O  O    . GLN   A 299 ? 0.6948 0.6439 0.6454 0.0042  0.0065  -0.0176 299 GLN   A O    
2301 C  CB   . GLN   A 299 ? 0.6032 0.5756 0.5776 0.0017  0.0127  -0.0156 299 GLN   A CB   
2302 C  CG   . GLN   A 299 ? 0.5359 0.5074 0.5145 0.0053  0.0072  -0.0155 299 GLN   A CG   
2303 C  CD   . GLN   A 299 ? 0.5944 0.5761 0.5869 0.0069  0.0068  -0.0147 299 GLN   A CD   
2304 O  OE1  . GLN   A 299 ? 0.6102 0.5934 0.6082 0.0093  0.0030  -0.0145 299 GLN   A OE1  
2305 N  NE2  . GLN   A 299 ? 0.5860 0.5748 0.5842 0.0054  0.0105  -0.0144 299 GLN   A NE2  
2306 N  N    . CYS   A 300 ? 0.6163 0.5730 0.5685 0.0012  0.0151  -0.0184 300 CYS   A N    
2307 C  CA   . CYS   A 300 ? 0.6360 0.5850 0.5807 0.0035  0.0130  -0.0199 300 CYS   A CA   
2308 C  C    . CYS   A 300 ? 0.6003 0.5369 0.5286 0.0021  0.0136  -0.0200 300 CYS   A C    
2309 O  O    . CYS   A 300 ? 0.6551 0.5823 0.5752 0.0045  0.0102  -0.0212 300 CYS   A O    
2310 C  CB   . CYS   A 300 ? 0.6256 0.5806 0.5747 0.0045  0.0163  -0.0212 300 CYS   A CB   
2311 S  SG   . CYS   A 300 ? 0.5983 0.5652 0.5648 0.0064  0.0145  -0.0211 300 CYS   A SG   
2312 N  N    . SER   A 301 ? 0.6016 0.5369 0.5243 -0.0017 0.0174  -0.0187 301 SER   A N    
2313 C  CA   . SER   A 301 ? 0.6866 0.6086 0.5925 -0.0034 0.0177  -0.0184 301 SER   A CA   
2314 C  C    . SER   A 301 ? 0.6283 0.5461 0.5300 -0.0061 0.0168  -0.0167 301 SER   A C    
2315 O  O    . SER   A 301 ? 0.6242 0.5460 0.5266 -0.0105 0.0211  -0.0154 301 SER   A O    
2316 C  CB   . SER   A 301 ? 0.7163 0.6382 0.6152 -0.0061 0.0245  -0.0185 301 SER   A CB   
2317 O  OG   . SER   A 301 ? 0.6970 0.6222 0.5987 -0.0029 0.0255  -0.0202 301 SER   A OG   
2318 C  C10  . YXY   B 1   ? 0.6950 0.6307 0.6542 0.0839  0.0000  0.0037  1   YXY   B C10  
2319 C  C02  . YXY   B 1   ? 0.7717 0.7072 0.7291 0.0759  -0.0053 0.0024  1   YXY   B C02  
2320 O  O03  . YXY   B 1   ? 0.7589 0.6974 0.7170 0.0782  -0.0005 0.0045  1   YXY   B O03  
2321 C  C04  . YXY   B 1   ? 0.8513 0.7756 0.7982 0.0814  -0.0081 0.0022  1   YXY   B C04  
2322 C  C05  . YXY   B 1   ? 0.8804 0.7958 0.8150 0.0892  -0.0051 0.0048  1   YXY   B C05  
2323 C  C06  . YXY   B 1   ? 0.7870 0.7053 0.7233 0.0938  0.0010  0.0070  1   YXY   B C06  
2324 C  C07  . YXY   B 1   ? 0.7182 0.6499 0.6698 0.0892  0.0045  0.0069  1   YXY   B C07  
2325 F  F08  . YXY   B 1   ? 0.7247 0.6557 0.6747 0.0935  0.0090  0.0090  1   YXY   B F08  
2326 F  F09  . YXY   B 1   ? 0.7466 0.6875 0.7061 0.0859  0.0076  0.0077  1   YXY   B F09  
2327 C  C11  . YXY   B 1   ? 0.8251 0.7539 0.7786 0.0819  -0.0070 0.0014  1   YXY   B C11  
2328 N  N    . CHG   B 2   ? 0.7640 0.7061 0.7299 0.0682  -0.0085 0.0001  2   CHG   B N    
2329 C  CA   . CHG   B 2   ? 0.6995 0.6509 0.6738 0.0632  -0.0058 0.0002  2   CHG   B CA   
2330 C  C    . CHG   B 2   ? 0.6981 0.6439 0.6640 0.0661  -0.0043 0.0022  2   CHG   B C    
2331 O  O    . CHG   B 2   ? 0.7386 0.6746 0.6942 0.0667  -0.0081 0.0020  2   CHG   B O    
2332 C  C1   . CHG   B 2   ? 0.6825 0.6397 0.6642 0.0555  -0.0094 -0.0022 2   CHG   B C1   
2333 C  C2   . CHG   B 2   ? 0.6429 0.6033 0.6266 0.0505  -0.0086 -0.0020 2   CHG   B C2   
2334 C  C3   . CHG   B 2   ? 0.5778 0.5466 0.5708 0.0429  -0.0107 -0.0042 2   CHG   B C3   
2335 C  C4   . CHG   B 2   ? 0.5440 0.5085 0.5343 0.0406  -0.0166 -0.0059 2   CHG   B C4   
2336 C  C5   . CHG   B 2   ? 0.6789 0.6377 0.6648 0.0466  -0.0184 -0.0061 2   CHG   B C5   
2337 C  C6   . CHG   B 2   ? 0.7263 0.6756 0.7016 0.0543  -0.0159 -0.0038 2   CHG   B C6   
2338 C  C    . FP9   B 3   ? 0.5877 0.5363 0.5502 0.0697  0.0022  0.0058  3   FP9   B C    
2339 N  N    . FP9   B 3   ? 0.6705 0.6231 0.6414 0.0687  0.0016  0.0042  3   FP9   B N    
2340 O  O    . FP9   B 3   ? 0.5490 0.5006 0.5123 0.0710  0.0046  0.0069  3   FP9   B O    
2341 C  CA   . FP9   B 3   ? 0.6108 0.5616 0.5764 0.0728  0.0045  0.0064  3   FP9   B CA   
2342 C  CB   . FP9   B 3   ? 0.5756 0.5378 0.5521 0.0735  0.0105  0.0081  3   FP9   B CB   
2343 C  CD   . FP9   B 3   ? 0.6360 0.5981 0.6173 0.0678  0.0054  0.0046  3   FP9   B CD   
2344 F  FD   . FP9   B 3   ? 0.7194 0.6741 0.6893 0.0799  0.0111  0.0089  3   FP9   B FD   
2345 C  CG   . FP9   B 3   ? 0.6484 0.6120 0.6284 0.0734  0.0109  0.0077  3   FP9   B CG   
2346 C  C    . 005   B 4   ? 0.5322 0.4916 0.5076 0.0518  -0.0012 0.0024  4   005   B C    
2347 N  N    . 005   B 4   ? 0.5792 0.5213 0.5370 0.0649  -0.0035 0.0038  4   005   B N    
2348 O  O    . 005   B 4   ? 0.5394 0.5000 0.5140 0.0552  0.0015  0.0038  4   005   B O    
2349 C  CA   . 005   B 4   ? 0.5735 0.5202 0.5366 0.0527  -0.0064 0.0019  4   005   B CA   
2350 C  CD   . 005   B 4   ? 0.6898 0.6075 0.6179 0.0745  -0.0077 0.0055  4   005   B CD   
2351 C  CG   . 005   B 4   ? 0.6566 0.5857 0.5976 0.0666  -0.0065 0.0046  4   005   B CG   
2352 C  CH   . 005   B 4   ? 0.7299 0.6259 0.6331 0.0898  -0.0096 0.0071  4   005   B CH   
2353 C  CB1  . 005   B 4   ? 0.6440 0.5811 0.5963 0.0609  -0.0068 0.0031  4   005   B CB1  
2354 O  OB2  . 005   B 4   ? 0.5494 0.4996 0.5185 0.0485  -0.0084 0.0003  4   005   B OB2  
2355 C  CE1  . 005   B 4   ? 0.7367 0.6480 0.6609 0.0740  -0.0115 0.0045  4   005   B CE1  
2356 C  CE2  . 005   B 4   ? 0.6812 0.5955 0.6019 0.0825  -0.0050 0.0073  4   005   B CE2  
2357 C  CZ1  . 005   B 4   ? 0.7161 0.6161 0.6276 0.0816  -0.0127 0.0053  4   005   B CZ1  
2358 C  CZ2  . 005   B 4   ? 0.7169 0.6208 0.6253 0.0902  -0.0057 0.0082  4   005   B CZ2  
2359 C  C21  . A1L3F B 5   ? 0.5256 0.5260 0.5448 0.0495  0.0143  0.0042  5   A1L3F B C21  
2360 C  C22  . A1L3F B 5   ? 0.5098 0.5066 0.5246 0.0552  0.0157  0.0060  5   A1L3F B C22  
2361 C  C24  . A1L3F B 5   ? 0.4973 0.4845 0.5014 0.0587  0.0134  0.0061  5   A1L3F B C24  
2362 C  C18  . A1L3F B 5   ? 0.5721 0.5531 0.5712 0.0447  0.0040  0.0012  5   A1L3F B C18  
2363 C  C19  . A1L3F B 5   ? 0.5733 0.5596 0.5775 0.0493  0.0082  0.0028  5   A1L3F B C19  
2364 C  C25  . A1L3F B 5   ? 0.5341 0.5155 0.5327 0.0556  0.0091  0.0044  5   A1L3F B C25  
2365 N  N17  . A1L3F B 5   ? 0.5660 0.5361 0.5540 0.0465  0.0000  0.0011  5   A1L3F B N17  
2366 N  N20  . A1L3F B 5   ? 0.5315 0.5269 0.5454 0.0467  0.0108  0.0027  5   A1L3F B N20  
2367 CL CL23 . A1L3F B 5   ? 0.4448 0.4490 0.4672 0.0577  0.0207  0.0085  5   A1L3F B CL23 
2368 O  O    . HOH   C .   ? 0.7328 0.7340 0.7161 -0.0307 0.0323  -0.0085 401 HOH   A O    
2369 O  O    . HOH   C .   ? 1.0220 0.8099 0.7772 0.1302  -0.0438 0.0015  402 HOH   A O    
2370 O  O    . HOH   C .   ? 1.2168 0.9214 0.9235 0.0625  -0.0736 0.0026  403 HOH   A O    
2371 O  O    . HOH   C .   ? 0.5912 0.6787 0.6890 0.0271  0.0098  -0.0246 404 HOH   A O    
2372 O  O    . HOH   C .   ? 0.3478 0.4293 0.4051 -0.0029 0.0441  -0.0219 405 HOH   A O    
2373 O  O    . HOH   C .   ? 0.7482 0.5871 0.6012 -0.0740 -0.0424 0.0084  406 HOH   A O    
2374 O  O    . HOH   C .   ? 0.7189 0.5715 0.5658 0.0593  -0.0287 0.0020  407 HOH   A O    
2375 O  O    . HOH   C .   ? 0.6574 0.6068 0.6209 -0.0719 -0.0320 0.0009  408 HOH   A O    
2376 O  O    . HOH   C .   ? 0.6336 0.6029 0.6320 -0.0334 -0.0548 -0.0100 409 HOH   A O    
2377 O  O    . HOH   C .   ? 0.7437 0.7454 0.7371 -0.0177 0.0261  -0.0097 410 HOH   A O    
2378 O  O    . HOH   C .   ? 0.4887 0.5265 0.5329 0.0103  0.0256  -0.0195 411 HOH   A O    
2379 O  O    . HOH   C .   ? 0.4379 0.5417 0.5104 0.0210  0.0461  -0.0319 412 HOH   A O    
2380 O  O    . HOH   C .   ? 0.6574 0.6890 0.7195 0.0467  0.0085  -0.0125 413 HOH   A O    
2381 O  O    . HOH   C .   ? 0.5635 0.6308 0.6260 0.0058  0.0330  -0.0202 414 HOH   A O    
2382 O  O    . HOH   C .   ? 0.7779 0.4959 0.5205 0.0786  -0.0873 -0.0006 415 HOH   A O    
2383 O  O    . HOH   C .   ? 0.5884 0.4947 0.5181 0.0202  -0.0316 -0.0262 416 HOH   A O    
2384 O  O    . HOH   C .   ? 0.6707 0.6661 0.7008 0.0665  -0.0216 -0.0204 417 HOH   A O    
2385 O  O    . HOH   C .   ? 0.4420 0.3862 0.3934 0.0182  -0.0048 0.0000  418 HOH   A O    
2386 O  O    . HOH   C .   ? 0.4114 0.4641 0.4776 -0.0189 -0.0201 -0.0160 419 HOH   A O    
2387 O  O    . HOH   C .   ? 0.5851 0.5329 0.4868 0.0660  0.0344  -0.0484 420 HOH   A O    
2388 O  O    . HOH   C .   ? 0.5790 0.4985 0.4350 0.0575  0.0455  -0.0447 421 HOH   A O    
2389 O  O    . HOH   C .   ? 0.7493 0.5955 0.5811 -0.0385 -0.0013 0.0006  422 HOH   A O    
2390 O  O    . HOH   C .   ? 0.5958 0.5840 0.6087 0.0528  0.0050  -0.0009 423 HOH   A O    
2391 O  O    . HOH   C .   ? 0.6286 0.6901 0.6884 -0.0624 -0.0074 -0.0085 424 HOH   A O    
2392 O  O    . HOH   C .   ? 0.4930 0.5509 0.5732 0.0277  0.0183  -0.0148 425 HOH   A O    
2393 O  O    . HOH   C .   ? 0.5125 0.5523 0.5739 0.0137  0.0193  -0.0141 426 HOH   A O    
2394 O  O    . HOH   C .   ? 0.8017 0.6875 0.7249 0.0459  -0.0299 -0.0424 427 HOH   A O    
2395 O  O    . HOH   C .   ? 1.2923 0.9630 0.9484 0.0942  -0.0781 0.0002  428 HOH   A O    
2396 O  O    . HOH   C .   ? 0.6597 0.7086 0.7254 0.0139  0.0209  -0.0107 429 HOH   A O    
2397 O  O    . HOH   C .   ? 0.4419 0.4541 0.4890 0.0125  0.0028  -0.0150 430 HOH   A O    
2398 O  O    . HOH   C .   ? 0.5770 0.5859 0.5954 0.0706  0.0284  0.0155  431 HOH   A O    
2399 O  O    . HOH   C .   ? 0.4433 0.4765 0.5355 0.0057  -0.0124 -0.0021 432 HOH   A O    
2400 O  O    . HOH   C .   ? 0.5221 0.6536 0.6323 0.0210  0.0333  -0.0321 433 HOH   A O    
2401 O  O    . HOH   C .   ? 0.6308 0.6936 0.6559 -0.0374 0.0509  -0.0122 434 HOH   A O    
2402 O  O    . HOH   C .   ? 0.6877 0.6399 0.6198 -0.0670 0.0223  0.0019  435 HOH   A O    
2403 O  O    . HOH   C .   ? 0.4480 0.3377 0.3345 0.0027  -0.0104 -0.0030 436 HOH   A O    
2404 O  O    . HOH   C .   ? 0.6606 0.6393 0.6370 0.0921  0.0256  0.0173  437 HOH   A O    
2405 O  O    . HOH   C .   ? 1.0055 0.5986 0.6476 0.0106  -0.1470 0.0014  438 HOH   A O    
2406 O  O    . HOH   C .   ? 0.4351 0.3922 0.4175 0.0160  -0.0280 -0.0070 439 HOH   A O    
2407 O  O    . HOH   C .   ? 0.4444 0.4971 0.5101 0.0072  0.0064  -0.0139 440 HOH   A O    
2408 O  O    . HOH   C .   ? 0.5671 0.6651 0.6636 -0.0666 -0.0199 -0.0133 441 HOH   A O    
2410 O  O    . HOH   C .   ? 0.6092 0.4993 0.5232 0.0876  -0.0231 -0.0549 443 HOH   A O    
2411 O  O    . HOH   C .   ? 0.7934 0.7492 0.7356 0.0967  0.0057  -0.0584 444 HOH   A O    
2412 O  O    . HOH   C .   ? 0.7267 0.5601 0.5510 -0.0539 -0.0097 0.0054  445 HOH   A O    
2413 O  O    . HOH   C .   ? 0.5017 0.5283 0.5567 0.0354  0.0130  -0.0265 446 HOH   A O    
2414 O  O    . HOH   C .   ? 0.6111 0.5915 0.6410 0.0110  -0.0229 -0.0177 447 HOH   A O    
2415 O  O    . HOH   C .   ? 1.0705 0.6156 0.5969 0.1253  -0.1130 -0.0019 448 HOH   A O    
2416 O  O    . HOH   C .   ? 0.6183 0.5690 0.6080 0.0062  -0.0700 -0.0169 449 HOH   A O    
2417 O  O    . HOH   C .   ? 0.5705 0.5192 0.5331 0.0118  -0.0070 -0.0193 450 HOH   A O    
2418 O  O    . HOH   C .   ? 0.6951 0.5976 0.6120 0.0281  -0.0132 -0.0346 451 HOH   A O    
2419 O  O    . HOH   C .   ? 0.7023 0.6875 0.7146 0.0507  -0.0039 -0.0054 452 HOH   A O    
2420 O  O    . HOH   C .   ? 0.7756 0.7341 0.8069 0.0066  -0.0357 -0.0182 453 HOH   A O    
2421 O  O    . HOH   C .   ? 0.7713 0.5210 0.5177 -0.0376 -0.0376 0.0063  454 HOH   A O    
2422 O  O    . HOH   C .   ? 0.5367 0.5717 0.5536 -0.0986 0.0117  0.0020  455 HOH   A O    
2423 O  O    . HOH   C .   ? 0.7729 0.6304 0.6254 0.1196  -0.0104 0.0106  456 HOH   A O    
2424 O  O    . HOH   C .   ? 0.8110 0.7855 0.7678 -0.0519 0.0246  -0.0020 457 HOH   A O    
2425 O  O    . HOH   C .   ? 0.7434 0.6870 0.7297 -0.0108 -0.0845 -0.0170 458 HOH   A O    
2426 O  O    . HOH   C .   ? 0.7314 0.5799 0.5760 -0.0935 -0.0151 0.0116  459 HOH   A O    
2427 O  O    . HOH   C .   ? 0.6616 0.5997 0.5874 0.0576  0.0122  -0.0457 460 HOH   A O    
2428 O  O    . HOH   C .   ? 0.5455 0.6165 0.6178 -0.0820 -0.0238 -0.0082 461 HOH   A O    
2429 O  O    . HOH   C .   ? 0.5428 0.5244 0.5463 0.0516  0.0038  0.0004  462 HOH   A O    
2430 O  O    . HOH   C .   ? 0.5774 0.5592 0.5575 -0.0074 0.0172  -0.0097 463 HOH   A O    
2431 O  O    . HOH   C .   ? 0.8784 0.6277 0.6899 0.0266  -0.1391 -0.0135 464 HOH   A O    
2432 O  O    . HOH   C .   ? 0.5665 0.5706 0.6056 0.0206  -0.0630 -0.0255 465 HOH   A O    
2433 O  O    . HOH   C .   ? 0.4970 0.5301 0.5711 0.0131  0.0045  -0.0062 466 HOH   A O    
2434 O  O    . HOH   C .   ? 0.4612 0.4778 0.5040 0.0048  -0.0381 -0.0181 467 HOH   A O    
2435 O  O    . HOH   C .   ? 0.5639 0.6908 0.5810 0.0543  0.0891  -0.0453 468 HOH   A O    
2436 O  O    . HOH   C .   ? 0.6638 0.6628 0.6853 -0.0832 -0.0571 -0.0060 469 HOH   A O    
2437 O  O    . HOH   C .   ? 0.5814 0.6111 0.5966 0.1349  -0.0062 -0.0693 470 HOH   A O    
2438 O  O    . HOH   C .   ? 0.9863 0.7014 0.6692 0.1444  -0.0604 0.0017  471 HOH   A O    
2439 O  O    . HOH   C .   ? 0.5391 0.4694 0.4420 -0.0240 0.0308  -0.0113 472 HOH   A O    
2440 O  O    . HOH   C .   ? 0.6982 0.6999 0.6895 0.0851  0.0127  0.0115  473 HOH   A O    
2441 O  O    . HOH   C .   ? 0.7721 0.6725 0.6485 0.1256  0.0014  0.0129  474 HOH   A O    
2442 O  O    . HOH   C .   ? 0.7205 0.6326 0.6174 0.0192  0.0141  -0.0304 475 HOH   A O    
2443 O  O    . HOH   C .   ? 0.8530 0.8303 0.9117 0.0043  -0.0185 -0.0074 476 HOH   A O    
2444 O  O    . HOH   C .   ? 0.5672 0.6220 0.6423 0.0422  0.0177  -0.0278 477 HOH   A O    
2445 O  O    . HOH   C .   ? 0.4224 0.3949 0.4709 0.0014  -0.0430 -0.0143 478 HOH   A O    
2446 O  O    . HOH   C .   ? 0.5607 0.4438 0.4382 -0.0095 -0.0068 -0.0028 479 HOH   A O    
2447 O  O    . HOH   C .   ? 0.7320 0.7600 0.7860 -0.0162 -0.0514 -0.0195 480 HOH   A O    
2448 O  O    . HOH   C .   ? 0.5189 0.6310 0.6140 0.0132  0.0354  -0.0275 481 HOH   A O    
2449 O  O    . HOH   C .   ? 0.6714 0.5847 0.5773 0.0263  0.0075  -0.0336 482 HOH   A O    
2450 O  O    . HOH   C .   ? 0.4959 0.5161 0.5329 0.0601  0.0290  0.0139  483 HOH   A O    
2451 O  O    . HOH   C .   ? 0.3051 0.4224 0.3776 -0.0302 0.0539  -0.0178 484 HOH   A O    
2452 O  O    . HOH   C .   ? 0.5027 0.5400 0.5826 0.0136  0.0004  -0.0034 485 HOH   A O    
2453 O  O    . HOH   C .   ? 0.5075 0.5381 0.5078 0.1163  0.0137  -0.0648 486 HOH   A O    
2454 O  O    . HOH   C .   ? 0.8685 0.4860 0.5073 0.1112  -0.1129 -0.0013 487 HOH   A O    
2455 O  O    . HOH   C .   ? 0.6119 0.5988 0.5794 0.1019  0.0131  0.0132  488 HOH   A O    
2456 O  O    . HOH   C .   ? 0.6186 0.5457 0.5214 -0.0304 0.0270  -0.0080 489 HOH   A O    
2457 O  O    . HOH   C .   ? 0.6576 0.6765 0.7143 0.0495  0.0082  -0.0264 490 HOH   A O    
2458 O  O    . HOH   C .   ? 0.9499 0.7948 0.7675 0.0727  0.0026  -0.0526 491 HOH   A O    
# 
