data_9H2D
# 
_entry.id   9H2D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9H2D         pdb_00009h2d 10.2210/pdb9h2d/pdb 
WWPDB D_1292142380 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        9H2D 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              el@mbg.au.dk 
_pdbx_contact_author.name_first         Esben 
_pdbx_contact_author.name_last          Lorentzen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6493-7220 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lorentzen, E.'  1 ? 
'Zacharia, N.K.' 2 ? 
'Bhogaraju, S.'  3 ? 
# 
_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                     
'Intraflagellar transport protein IFT172 contains a C-terminal ubiquitin-binding U-box-like domain involved in ciliary signaling' 
_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 'Lorentzen, E.'  1 ? 
primary 'Zacharia, N.K.' 2 ? 
primary 'Bhogaraju, S.'  3 ? 
# 
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 'Intraflagellar transport protein 172 homolog'        30519.646 2   ? ? ? ? 
2 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   2   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                        35.453    1   ? ? ? ? 
4 water       nat water                                                 18.015    177 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;APANPQNFNIYKRIFTDMVSSPGTNCAEAYHSWADLRDVLFNLCENLVKSSEANSPAHEEFKTMLLIAHYYATRSAAQSV
KQLETVAARLSVSLLRHTQLLPVDKAFYEAGIAAKAVGWDNMAFIFLNRFLDLTDAIEEGTLDGLDHSDFQDTDIPFEVP
LPAKQHVPEAEREEVRDWVLTVSMDQRLEQVLPRDERGAYEASLVAASTGVRALPCLITGYPILRNKIEFKRPGKAANKD
NWNKFLMAIKTSHSPVCQDVLKFISQWCGGLP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;APANPQNFNIYKRIFTDMVSSPGTNCAEAYHSWADLRDVLFNLCENLVKSSEANSPAHEEFKTMLLIAHYYATRSAAQSV
KQLETVAARLSVSLLRHTQLLPVDKAFYEAGIAAKAVGWDNMAFIFLNRFLDLTDAIEEGTLDGLDHSDFQDTDIPFEVP
LPAKQHVPEAEREEVRDWVLTVSMDQRLEQVLPRDERGAYEASLVAASTGVRALPCLITGYPILRNKIEFKRPGKAANKD
NWNKFLMAIKTSHSPVCQDVLKFISQWCGGLP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
3 'CHLORIDE ION'                                        CL  
4 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PRO n 
1 3   ALA n 
1 4   ASN n 
1 5   PRO n 
1 6   GLN n 
1 7   ASN n 
1 8   PHE n 
1 9   ASN n 
1 10  ILE n 
1 11  TYR n 
1 12  LYS n 
1 13  ARG n 
1 14  ILE n 
1 15  PHE n 
1 16  THR n 
1 17  ASP n 
1 18  MET n 
1 19  VAL n 
1 20  SER n 
1 21  SER n 
1 22  PRO n 
1 23  GLY n 
1 24  THR n 
1 25  ASN n 
1 26  CYS n 
1 27  ALA n 
1 28  GLU n 
1 29  ALA n 
1 30  TYR n 
1 31  HIS n 
1 32  SER n 
1 33  TRP n 
1 34  ALA n 
1 35  ASP n 
1 36  LEU n 
1 37  ARG n 
1 38  ASP n 
1 39  VAL n 
1 40  LEU n 
1 41  PHE n 
1 42  ASN n 
1 43  LEU n 
1 44  CYS n 
1 45  GLU n 
1 46  ASN n 
1 47  LEU n 
1 48  VAL n 
1 49  LYS n 
1 50  SER n 
1 51  SER n 
1 52  GLU n 
1 53  ALA n 
1 54  ASN n 
1 55  SER n 
1 56  PRO n 
1 57  ALA n 
1 58  HIS n 
1 59  GLU n 
1 60  GLU n 
1 61  PHE n 
1 62  LYS n 
1 63  THR n 
1 64  MET n 
1 65  LEU n 
1 66  LEU n 
1 67  ILE n 
1 68  ALA n 
1 69  HIS n 
1 70  TYR n 
1 71  TYR n 
1 72  ALA n 
1 73  THR n 
1 74  ARG n 
1 75  SER n 
1 76  ALA n 
1 77  ALA n 
1 78  GLN n 
1 79  SER n 
1 80  VAL n 
1 81  LYS n 
1 82  GLN n 
1 83  LEU n 
1 84  GLU n 
1 85  THR n 
1 86  VAL n 
1 87  ALA n 
1 88  ALA n 
1 89  ARG n 
1 90  LEU n 
1 91  SER n 
1 92  VAL n 
1 93  SER n 
1 94  LEU n 
1 95  LEU n 
1 96  ARG n 
1 97  HIS n 
1 98  THR n 
1 99  GLN n 
1 100 LEU n 
1 101 LEU n 
1 102 PRO n 
1 103 VAL n 
1 104 ASP n 
1 105 LYS n 
1 106 ALA n 
1 107 PHE n 
1 108 TYR n 
1 109 GLU n 
1 110 ALA n 
1 111 GLY n 
1 112 ILE n 
1 113 ALA n 
1 114 ALA n 
1 115 LYS n 
1 116 ALA n 
1 117 VAL n 
1 118 GLY n 
1 119 TRP n 
1 120 ASP n 
1 121 ASN n 
1 122 MET n 
1 123 ALA n 
1 124 PHE n 
1 125 ILE n 
1 126 PHE n 
1 127 LEU n 
1 128 ASN n 
1 129 ARG n 
1 130 PHE n 
1 131 LEU n 
1 132 ASP n 
1 133 LEU n 
1 134 THR n 
1 135 ASP n 
1 136 ALA n 
1 137 ILE n 
1 138 GLU n 
1 139 GLU n 
1 140 GLY n 
1 141 THR n 
1 142 LEU n 
1 143 ASP n 
1 144 GLY n 
1 145 LEU n 
1 146 ASP n 
1 147 HIS n 
1 148 SER n 
1 149 ASP n 
1 150 PHE n 
1 151 GLN n 
1 152 ASP n 
1 153 THR n 
1 154 ASP n 
1 155 ILE n 
1 156 PRO n 
1 157 PHE n 
1 158 GLU n 
1 159 VAL n 
1 160 PRO n 
1 161 LEU n 
1 162 PRO n 
1 163 ALA n 
1 164 LYS n 
1 165 GLN n 
1 166 HIS n 
1 167 VAL n 
1 168 PRO n 
1 169 GLU n 
1 170 ALA n 
1 171 GLU n 
1 172 ARG n 
1 173 GLU n 
1 174 GLU n 
1 175 VAL n 
1 176 ARG n 
1 177 ASP n 
1 178 TRP n 
1 179 VAL n 
1 180 LEU n 
1 181 THR n 
1 182 VAL n 
1 183 SER n 
1 184 MET n 
1 185 ASP n 
1 186 GLN n 
1 187 ARG n 
1 188 LEU n 
1 189 GLU n 
1 190 GLN n 
1 191 VAL n 
1 192 LEU n 
1 193 PRO n 
1 194 ARG n 
1 195 ASP n 
1 196 GLU n 
1 197 ARG n 
1 198 GLY n 
1 199 ALA n 
1 200 TYR n 
1 201 GLU n 
1 202 ALA n 
1 203 SER n 
1 204 LEU n 
1 205 VAL n 
1 206 ALA n 
1 207 ALA n 
1 208 SER n 
1 209 THR n 
1 210 GLY n 
1 211 VAL n 
1 212 ARG n 
1 213 ALA n 
1 214 LEU n 
1 215 PRO n 
1 216 CYS n 
1 217 LEU n 
1 218 ILE n 
1 219 THR n 
1 220 GLY n 
1 221 TYR n 
1 222 PRO n 
1 223 ILE n 
1 224 LEU n 
1 225 ARG n 
1 226 ASN n 
1 227 LYS n 
1 228 ILE n 
1 229 GLU n 
1 230 PHE n 
1 231 LYS n 
1 232 ARG n 
1 233 PRO n 
1 234 GLY n 
1 235 LYS n 
1 236 ALA n 
1 237 ALA n 
1 238 ASN n 
1 239 LYS n 
1 240 ASP n 
1 241 ASN n 
1 242 TRP n 
1 243 ASN n 
1 244 LYS n 
1 245 PHE n 
1 246 LEU n 
1 247 MET n 
1 248 ALA n 
1 249 ILE n 
1 250 LYS n 
1 251 THR n 
1 252 SER n 
1 253 HIS n 
1 254 SER n 
1 255 PRO n 
1 256 VAL n 
1 257 CYS n 
1 258 GLN n 
1 259 ASP n 
1 260 VAL n 
1 261 LEU n 
1 262 LYS n 
1 263 PHE n 
1 264 ILE n 
1 265 SER n 
1 266 GLN n 
1 267 TRP n 
1 268 CYS n 
1 269 GLY n 
1 270 GLY n 
1 271 LEU n 
1 272 PRO 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                   272 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'IFT172, KIAA1179' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                               ?     'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                              ?     'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                            ?     'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                       ?     'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                                        ?     'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                              ?     'C3 H7 N O2 S'   121.158 
EPE non-polymer         . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 
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 
# 
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   ALA 1   1471 1471 ALA ALA A . n 
A 1 2   PRO 2   1472 1472 PRO PRO A . n 
A 1 3   ALA 3   1473 1473 ALA ALA A . n 
A 1 4   ASN 4   1474 1474 ASN ASN A . n 
A 1 5   PRO 5   1475 1475 PRO PRO A . n 
A 1 6   GLN 6   1476 1476 GLN GLN A . n 
A 1 7   ASN 7   1477 1477 ASN ASN A . n 
A 1 8   PHE 8   1478 1478 PHE PHE A . n 
A 1 9   ASN 9   1479 1479 ASN ASN A . n 
A 1 10  ILE 10  1480 1480 ILE ILE A . n 
A 1 11  TYR 11  1481 1481 TYR TYR A . n 
A 1 12  LYS 12  1482 1482 LYS LYS A . n 
A 1 13  ARG 13  1483 1483 ARG ARG A . n 
A 1 14  ILE 14  1484 1484 ILE ILE A . n 
A 1 15  PHE 15  1485 1485 PHE PHE A . n 
A 1 16  THR 16  1486 1486 THR THR A . n 
A 1 17  ASP 17  1487 1487 ASP ASP A . n 
A 1 18  MET 18  1488 1488 MET MET A . n 
A 1 19  VAL 19  1489 1489 VAL VAL A . n 
A 1 20  SER 20  1490 1490 SER SER A . n 
A 1 21  SER 21  1491 1491 SER SER A . n 
A 1 22  PRO 22  1492 1492 PRO PRO A . n 
A 1 23  GLY 23  1493 1493 GLY GLY A . n 
A 1 24  THR 24  1494 1494 THR THR A . n 
A 1 25  ASN 25  1495 1495 ASN ASN A . n 
A 1 26  CYS 26  1496 1496 CYS CYS A . n 
A 1 27  ALA 27  1497 1497 ALA ALA A . n 
A 1 28  GLU 28  1498 1498 GLU GLU A . n 
A 1 29  ALA 29  1499 1499 ALA ALA A . n 
A 1 30  TYR 30  1500 1500 TYR TYR A . n 
A 1 31  HIS 31  1501 1501 HIS HIS A . n 
A 1 32  SER 32  1502 1502 SER SER A . n 
A 1 33  TRP 33  1503 1503 TRP TRP A . n 
A 1 34  ALA 34  1504 1504 ALA ALA A . n 
A 1 35  ASP 35  1505 1505 ASP ASP A . n 
A 1 36  LEU 36  1506 1506 LEU LEU A . n 
A 1 37  ARG 37  1507 1507 ARG ARG A . n 
A 1 38  ASP 38  1508 1508 ASP ASP A . n 
A 1 39  VAL 39  1509 1509 VAL VAL A . n 
A 1 40  LEU 40  1510 1510 LEU LEU A . n 
A 1 41  PHE 41  1511 1511 PHE PHE A . n 
A 1 42  ASN 42  1512 1512 ASN ASN A . n 
A 1 43  LEU 43  1513 1513 LEU LEU A . n 
A 1 44  CYS 44  1514 1514 CYS CYS A . n 
A 1 45  GLU 45  1515 1515 GLU GLU A . n 
A 1 46  ASN 46  1516 1516 ASN ASN A . n 
A 1 47  LEU 47  1517 1517 LEU LEU A . n 
A 1 48  VAL 48  1518 1518 VAL VAL A . n 
A 1 49  LYS 49  1519 1519 LYS LYS A . n 
A 1 50  SER 50  1520 1520 SER SER A . n 
A 1 51  SER 51  1521 1521 SER SER A . n 
A 1 52  GLU 52  1522 1522 GLU GLU A . n 
A 1 53  ALA 53  1523 1523 ALA ALA A . n 
A 1 54  ASN 54  1524 1524 ASN ASN A . n 
A 1 55  SER 55  1525 1525 SER SER A . n 
A 1 56  PRO 56  1526 1526 PRO PRO A . n 
A 1 57  ALA 57  1527 1527 ALA ALA A . n 
A 1 58  HIS 58  1528 1528 HIS HIS A . n 
A 1 59  GLU 59  1529 1529 GLU GLU A . n 
A 1 60  GLU 60  1530 1530 GLU GLU A . n 
A 1 61  PHE 61  1531 1531 PHE PHE A . n 
A 1 62  LYS 62  1532 1532 LYS LYS A . n 
A 1 63  THR 63  1533 1533 THR THR A . n 
A 1 64  MET 64  1534 1534 MET MET A . n 
A 1 65  LEU 65  1535 1535 LEU LEU A . n 
A 1 66  LEU 66  1536 1536 LEU LEU A . n 
A 1 67  ILE 67  1537 1537 ILE ILE A . n 
A 1 68  ALA 68  1538 1538 ALA ALA A . n 
A 1 69  HIS 69  1539 1539 HIS HIS A . n 
A 1 70  TYR 70  1540 1540 TYR TYR A . n 
A 1 71  TYR 71  1541 1541 TYR TYR A . n 
A 1 72  ALA 72  1542 1542 ALA ALA A . n 
A 1 73  THR 73  1543 1543 THR THR A . n 
A 1 74  ARG 74  1544 1544 ARG ARG A . n 
A 1 75  SER 75  1545 1545 SER SER A . n 
A 1 76  ALA 76  1546 1546 ALA ALA A . n 
A 1 77  ALA 77  1547 1547 ALA ALA A . n 
A 1 78  GLN 78  1548 1548 GLN GLN A . n 
A 1 79  SER 79  1549 1549 SER SER A . n 
A 1 80  VAL 80  1550 1550 VAL VAL A . n 
A 1 81  LYS 81  1551 1551 LYS LYS A . n 
A 1 82  GLN 82  1552 1552 GLN GLN A . n 
A 1 83  LEU 83  1553 1553 LEU LEU A . n 
A 1 84  GLU 84  1554 1554 GLU GLU A . n 
A 1 85  THR 85  1555 1555 THR THR A . n 
A 1 86  VAL 86  1556 1556 VAL VAL A . n 
A 1 87  ALA 87  1557 1557 ALA ALA A . n 
A 1 88  ALA 88  1558 1558 ALA ALA A . n 
A 1 89  ARG 89  1559 1559 ARG ARG A . n 
A 1 90  LEU 90  1560 1560 LEU LEU A . n 
A 1 91  SER 91  1561 1561 SER SER A . n 
A 1 92  VAL 92  1562 1562 VAL VAL A . n 
A 1 93  SER 93  1563 1563 SER SER A . n 
A 1 94  LEU 94  1564 1564 LEU LEU A . n 
A 1 95  LEU 95  1565 1565 LEU LEU A . n 
A 1 96  ARG 96  1566 1566 ARG ARG A . n 
A 1 97  HIS 97  1567 1567 HIS HIS A . n 
A 1 98  THR 98  1568 1568 THR THR A . n 
A 1 99  GLN 99  1569 1569 GLN GLN A . n 
A 1 100 LEU 100 1570 1570 LEU LEU A . n 
A 1 101 LEU 101 1571 1571 LEU LEU A . n 
A 1 102 PRO 102 1572 1572 PRO PRO A . n 
A 1 103 VAL 103 1573 1573 VAL VAL A . n 
A 1 104 ASP 104 1574 1574 ASP ASP A . n 
A 1 105 LYS 105 1575 1575 LYS LYS A . n 
A 1 106 ALA 106 1576 1576 ALA ALA A . n 
A 1 107 PHE 107 1577 1577 PHE PHE A . n 
A 1 108 TYR 108 1578 1578 TYR TYR A . n 
A 1 109 GLU 109 1579 1579 GLU GLU A . n 
A 1 110 ALA 110 1580 1580 ALA ALA A . n 
A 1 111 GLY 111 1581 1581 GLY GLY A . n 
A 1 112 ILE 112 1582 1582 ILE ILE A . n 
A 1 113 ALA 113 1583 1583 ALA ALA A . n 
A 1 114 ALA 114 1584 1584 ALA ALA A . n 
A 1 115 LYS 115 1585 1585 LYS LYS A . n 
A 1 116 ALA 116 1586 1586 ALA ALA A . n 
A 1 117 VAL 117 1587 1587 VAL VAL A . n 
A 1 118 GLY 118 1588 1588 GLY GLY A . n 
A 1 119 TRP 119 1589 1589 TRP TRP A . n 
A 1 120 ASP 120 1590 1590 ASP ASP A . n 
A 1 121 ASN 121 1591 1591 ASN ASN A . n 
A 1 122 MET 122 1592 1592 MET MET A . n 
A 1 123 ALA 123 1593 1593 ALA ALA A . n 
A 1 124 PHE 124 1594 1594 PHE PHE A . n 
A 1 125 ILE 125 1595 1595 ILE ILE A . n 
A 1 126 PHE 126 1596 1596 PHE PHE A . n 
A 1 127 LEU 127 1597 1597 LEU LEU A . n 
A 1 128 ASN 128 1598 1598 ASN ASN A . n 
A 1 129 ARG 129 1599 1599 ARG ARG A . n 
A 1 130 PHE 130 1600 1600 PHE PHE A . n 
A 1 131 LEU 131 1601 1601 LEU LEU A . n 
A 1 132 ASP 132 1602 1602 ASP ASP A . n 
A 1 133 LEU 133 1603 1603 LEU LEU A . n 
A 1 134 THR 134 1604 1604 THR THR A . n 
A 1 135 ASP 135 1605 1605 ASP ASP A . n 
A 1 136 ALA 136 1606 1606 ALA ALA A . n 
A 1 137 ILE 137 1607 1607 ILE ILE A . n 
A 1 138 GLU 138 1608 1608 GLU GLU A . n 
A 1 139 GLU 139 1609 1609 GLU GLU A . n 
A 1 140 GLY 140 1610 1610 GLY GLY A . n 
A 1 141 THR 141 1611 1611 THR THR A . n 
A 1 142 LEU 142 1612 1612 LEU LEU A . n 
A 1 143 ASP 143 1613 1613 ASP ASP A . n 
A 1 144 GLY 144 1614 1614 GLY GLY A . n 
A 1 145 LEU 145 1615 1615 LEU LEU A . n 
A 1 146 ASP 146 1616 1616 ASP ASP A . n 
A 1 147 HIS 147 1617 1617 HIS HIS A . n 
A 1 148 SER 148 1618 1618 SER SER A . n 
A 1 149 ASP 149 1619 1619 ASP ASP A . n 
A 1 150 PHE 150 1620 1620 PHE PHE A . n 
A 1 151 GLN 151 1621 1621 GLN GLN A . n 
A 1 152 ASP 152 1622 1622 ASP ASP A . n 
A 1 153 THR 153 1623 1623 THR THR A . n 
A 1 154 ASP 154 1624 1624 ASP ASP A . n 
A 1 155 ILE 155 1625 1625 ILE ILE A . n 
A 1 156 PRO 156 1626 1626 PRO PRO A . n 
A 1 157 PHE 157 1627 1627 PHE PHE A . n 
A 1 158 GLU 158 1628 1628 GLU GLU A . n 
A 1 159 VAL 159 1629 1629 VAL VAL A . n 
A 1 160 PRO 160 1630 1630 PRO PRO A . n 
A 1 161 LEU 161 1631 1631 LEU LEU A . n 
A 1 162 PRO 162 1632 1632 PRO PRO A . n 
A 1 163 ALA 163 1633 1633 ALA ALA A . n 
A 1 164 LYS 164 1634 1634 LYS LYS A . n 
A 1 165 GLN 165 1635 1635 GLN GLN A . n 
A 1 166 HIS 166 1636 1636 HIS HIS A . n 
A 1 167 VAL 167 1637 1637 VAL VAL A . n 
A 1 168 PRO 168 1638 1638 PRO PRO A . n 
A 1 169 GLU 169 1639 1639 GLU GLU A . n 
A 1 170 ALA 170 1640 1640 ALA ALA A . n 
A 1 171 GLU 171 1641 1641 GLU GLU A . n 
A 1 172 ARG 172 1642 1642 ARG ARG A . n 
A 1 173 GLU 173 1643 1643 GLU GLU A . n 
A 1 174 GLU 174 1644 1644 GLU GLU A . n 
A 1 175 VAL 175 1645 1645 VAL VAL A . n 
A 1 176 ARG 176 1646 1646 ARG ARG A . n 
A 1 177 ASP 177 1647 1647 ASP ASP A . n 
A 1 178 TRP 178 1648 1648 TRP TRP A . n 
A 1 179 VAL 179 1649 1649 VAL VAL A . n 
A 1 180 LEU 180 1650 1650 LEU LEU A . n 
A 1 181 THR 181 1651 1651 THR THR A . n 
A 1 182 VAL 182 1652 1652 VAL VAL A . n 
A 1 183 SER 183 1653 1653 SER SER A . n 
A 1 184 MET 184 1654 1654 MET MET A . n 
A 1 185 ASP 185 1655 1655 ASP ASP A . n 
A 1 186 GLN 186 1656 ?    ?   ?   A . n 
A 1 187 ARG 187 1657 ?    ?   ?   A . n 
A 1 188 LEU 188 1658 1658 LEU LEU A . n 
A 1 189 GLU 189 1659 1659 GLU GLU A . n 
A 1 190 GLN 190 1660 1660 GLN GLN A . n 
A 1 191 VAL 191 1661 1661 VAL VAL A . n 
A 1 192 LEU 192 1662 1662 LEU LEU A . n 
A 1 193 PRO 193 1663 1663 PRO PRO A . n 
A 1 194 ARG 194 1664 1664 ARG ARG A . n 
A 1 195 ASP 195 1665 1665 ASP ASP A . n 
A 1 196 GLU 196 1666 1666 GLU GLU A . n 
A 1 197 ARG 197 1667 1667 ARG ARG A . n 
A 1 198 GLY 198 1668 1668 GLY GLY A . n 
A 1 199 ALA 199 1669 1669 ALA ALA A . n 
A 1 200 TYR 200 1670 1670 TYR TYR A . n 
A 1 201 GLU 201 1671 1671 GLU GLU A . n 
A 1 202 ALA 202 1672 1672 ALA ALA A . n 
A 1 203 SER 203 1673 1673 SER SER A . n 
A 1 204 LEU 204 1674 1674 LEU LEU A . n 
A 1 205 VAL 205 1675 1675 VAL VAL A . n 
A 1 206 ALA 206 1676 1676 ALA ALA A . n 
A 1 207 ALA 207 1677 1677 ALA ALA A . n 
A 1 208 SER 208 1678 1678 SER SER A . n 
A 1 209 THR 209 1679 1679 THR THR A . n 
A 1 210 GLY 210 1680 1680 GLY GLY A . n 
A 1 211 VAL 211 1681 1681 VAL VAL A . n 
A 1 212 ARG 212 1682 1682 ARG ARG A . n 
A 1 213 ALA 213 1683 1683 ALA ALA A . n 
A 1 214 LEU 214 1684 1684 LEU LEU A . n 
A 1 215 PRO 215 1685 1685 PRO PRO A . n 
A 1 216 CYS 216 1686 1686 CYS CYS A . n 
A 1 217 LEU 217 1687 1687 LEU LEU A . n 
A 1 218 ILE 218 1688 1688 ILE ILE A . n 
A 1 219 THR 219 1689 1689 THR THR A . n 
A 1 220 GLY 220 1690 1690 GLY GLY A . n 
A 1 221 TYR 221 1691 1691 TYR TYR A . n 
A 1 222 PRO 222 1692 1692 PRO PRO A . n 
A 1 223 ILE 223 1693 1693 ILE ILE A . n 
A 1 224 LEU 224 1694 1694 LEU LEU A . n 
A 1 225 ARG 225 1695 1695 ARG ARG A . n 
A 1 226 ASN 226 1696 1696 ASN ASN A . n 
A 1 227 LYS 227 1697 1697 LYS LYS A . n 
A 1 228 ILE 228 1698 1698 ILE ILE A . n 
A 1 229 GLU 229 1699 1699 GLU GLU A . n 
A 1 230 PHE 230 1700 1700 PHE PHE A . n 
A 1 231 LYS 231 1701 1701 LYS LYS A . n 
A 1 232 ARG 232 1702 1702 ARG ARG A . n 
A 1 233 PRO 233 1703 1703 PRO PRO A . n 
A 1 234 GLY 234 1704 1704 GLY GLY A . n 
A 1 235 LYS 235 1705 1705 LYS LYS A . n 
A 1 236 ALA 236 1706 1706 ALA ALA A . n 
A 1 237 ALA 237 1707 1707 ALA ALA A . n 
A 1 238 ASN 238 1708 1708 ASN ASN A . n 
A 1 239 LYS 239 1709 1709 LYS LYS A . n 
A 1 240 ASP 240 1710 1710 ASP ASP A . n 
A 1 241 ASN 241 1711 1711 ASN ASN A . n 
A 1 242 TRP 242 1712 1712 TRP TRP A . n 
A 1 243 ASN 243 1713 1713 ASN ASN A . n 
A 1 244 LYS 244 1714 1714 LYS LYS A . n 
A 1 245 PHE 245 1715 1715 PHE PHE A . n 
A 1 246 LEU 246 1716 1716 LEU LEU A . n 
A 1 247 MET 247 1717 1717 MET MET A . n 
A 1 248 ALA 248 1718 1718 ALA ALA A . n 
A 1 249 ILE 249 1719 1719 ILE ILE A . n 
A 1 250 LYS 250 1720 1720 LYS LYS A . n 
A 1 251 THR 251 1721 1721 THR THR A . n 
A 1 252 SER 252 1722 1722 SER SER A . n 
A 1 253 HIS 253 1723 1723 HIS HIS A . n 
A 1 254 SER 254 1724 1724 SER SER A . n 
A 1 255 PRO 255 1725 1725 PRO PRO A . n 
A 1 256 VAL 256 1726 1726 VAL VAL A . n 
A 1 257 CYS 257 1727 1727 CYS CYS A . n 
A 1 258 GLN 258 1728 1728 GLN GLN A . n 
A 1 259 ASP 259 1729 1729 ASP ASP A . n 
A 1 260 VAL 260 1730 1730 VAL VAL A . n 
A 1 261 LEU 261 1731 1731 LEU LEU A . n 
A 1 262 LYS 262 1732 1732 LYS LYS A . n 
A 1 263 PHE 263 1733 1733 PHE PHE A . n 
A 1 264 ILE 264 1734 1734 ILE ILE A . n 
A 1 265 SER 265 1735 1735 SER SER A . n 
A 1 266 GLN 266 1736 1736 GLN GLN A . n 
A 1 267 TRP 267 1737 1737 TRP TRP A . n 
A 1 268 CYS 268 1738 1738 CYS CYS A . n 
A 1 269 GLY 269 1739 1739 GLY GLY A . n 
A 1 270 GLY 270 1740 1740 GLY GLY A . n 
A 1 271 LEU 271 1741 1741 LEU LEU A . n 
A 1 272 PRO 272 1742 1742 PRO PRO A . n 
B 1 1   ALA 1   1471 ?    ?   ?   B . n 
B 1 2   PRO 2   1472 ?    ?   ?   B . n 
B 1 3   ALA 3   1473 ?    ?   ?   B . n 
B 1 4   ASN 4   1474 ?    ?   ?   B . n 
B 1 5   PRO 5   1475 ?    ?   ?   B . n 
B 1 6   GLN 6   1476 ?    ?   ?   B . n 
B 1 7   ASN 7   1477 1477 ASN ASN B . n 
B 1 8   PHE 8   1478 1478 PHE PHE B . n 
B 1 9   ASN 9   1479 1479 ASN ASN B . n 
B 1 10  ILE 10  1480 1480 ILE ILE B . n 
B 1 11  TYR 11  1481 1481 TYR TYR B . n 
B 1 12  LYS 12  1482 1482 LYS LYS B . n 
B 1 13  ARG 13  1483 1483 ARG ARG B . n 
B 1 14  ILE 14  1484 1484 ILE ILE B . n 
B 1 15  PHE 15  1485 1485 PHE PHE B . n 
B 1 16  THR 16  1486 1486 THR THR B . n 
B 1 17  ASP 17  1487 1487 ASP ASP B . n 
B 1 18  MET 18  1488 1488 MET MET B . n 
B 1 19  VAL 19  1489 1489 VAL VAL B . n 
B 1 20  SER 20  1490 1490 SER SER B . n 
B 1 21  SER 21  1491 1491 SER SER B . n 
B 1 22  PRO 22  1492 1492 PRO PRO B . n 
B 1 23  GLY 23  1493 1493 GLY GLY B . n 
B 1 24  THR 24  1494 1494 THR THR B . n 
B 1 25  ASN 25  1495 1495 ASN ASN B . n 
B 1 26  CYS 26  1496 1496 CYS CYS B . n 
B 1 27  ALA 27  1497 1497 ALA ALA B . n 
B 1 28  GLU 28  1498 1498 GLU GLU B . n 
B 1 29  ALA 29  1499 1499 ALA ALA B . n 
B 1 30  TYR 30  1500 1500 TYR TYR B . n 
B 1 31  HIS 31  1501 1501 HIS HIS B . n 
B 1 32  SER 32  1502 1502 SER SER B . n 
B 1 33  TRP 33  1503 1503 TRP TRP B . n 
B 1 34  ALA 34  1504 1504 ALA ALA B . n 
B 1 35  ASP 35  1505 1505 ASP ASP B . n 
B 1 36  LEU 36  1506 1506 LEU LEU B . n 
B 1 37  ARG 37  1507 1507 ARG ARG B . n 
B 1 38  ASP 38  1508 1508 ASP ASP B . n 
B 1 39  VAL 39  1509 1509 VAL VAL B . n 
B 1 40  LEU 40  1510 1510 LEU LEU B . n 
B 1 41  PHE 41  1511 1511 PHE PHE B . n 
B 1 42  ASN 42  1512 1512 ASN ASN B . n 
B 1 43  LEU 43  1513 1513 LEU LEU B . n 
B 1 44  CYS 44  1514 1514 CYS CYS B . n 
B 1 45  GLU 45  1515 1515 GLU GLU B . n 
B 1 46  ASN 46  1516 1516 ASN ASN B . n 
B 1 47  LEU 47  1517 1517 LEU LEU B . n 
B 1 48  VAL 48  1518 1518 VAL VAL B . n 
B 1 49  LYS 49  1519 ?    ?   ?   B . n 
B 1 50  SER 50  1520 ?    ?   ?   B . n 
B 1 51  SER 51  1521 ?    ?   ?   B . n 
B 1 52  GLU 52  1522 ?    ?   ?   B . n 
B 1 53  ALA 53  1523 ?    ?   ?   B . n 
B 1 54  ASN 54  1524 ?    ?   ?   B . n 
B 1 55  SER 55  1525 1525 SER SER B . n 
B 1 56  PRO 56  1526 1526 PRO PRO B . n 
B 1 57  ALA 57  1527 1527 ALA ALA B . n 
B 1 58  HIS 58  1528 1528 HIS HIS B . n 
B 1 59  GLU 59  1529 1529 GLU GLU B . n 
B 1 60  GLU 60  1530 1530 GLU GLU B . n 
B 1 61  PHE 61  1531 1531 PHE PHE B . n 
B 1 62  LYS 62  1532 1532 LYS LYS B . n 
B 1 63  THR 63  1533 1533 THR THR B . n 
B 1 64  MET 64  1534 1534 MET MET B . n 
B 1 65  LEU 65  1535 1535 LEU LEU B . n 
B 1 66  LEU 66  1536 1536 LEU LEU B . n 
B 1 67  ILE 67  1537 1537 ILE ILE B . n 
B 1 68  ALA 68  1538 1538 ALA ALA B . n 
B 1 69  HIS 69  1539 1539 HIS HIS B . n 
B 1 70  TYR 70  1540 1540 TYR TYR B . n 
B 1 71  TYR 71  1541 1541 TYR TYR B . n 
B 1 72  ALA 72  1542 1542 ALA ALA B . n 
B 1 73  THR 73  1543 1543 THR THR B . n 
B 1 74  ARG 74  1544 1544 ARG ARG B . n 
B 1 75  SER 75  1545 1545 SER SER B . n 
B 1 76  ALA 76  1546 1546 ALA ALA B . n 
B 1 77  ALA 77  1547 1547 ALA ALA B . n 
B 1 78  GLN 78  1548 1548 GLN GLN B . n 
B 1 79  SER 79  1549 1549 SER SER B . n 
B 1 80  VAL 80  1550 1550 VAL VAL B . n 
B 1 81  LYS 81  1551 1551 LYS LYS B . n 
B 1 82  GLN 82  1552 1552 GLN GLN B . n 
B 1 83  LEU 83  1553 1553 LEU LEU B . n 
B 1 84  GLU 84  1554 1554 GLU GLU B . n 
B 1 85  THR 85  1555 1555 THR THR B . n 
B 1 86  VAL 86  1556 1556 VAL VAL B . n 
B 1 87  ALA 87  1557 1557 ALA ALA B . n 
B 1 88  ALA 88  1558 1558 ALA ALA B . n 
B 1 89  ARG 89  1559 1559 ARG ARG B . n 
B 1 90  LEU 90  1560 1560 LEU LEU B . n 
B 1 91  SER 91  1561 1561 SER SER B . n 
B 1 92  VAL 92  1562 1562 VAL VAL B . n 
B 1 93  SER 93  1563 1563 SER SER B . n 
B 1 94  LEU 94  1564 1564 LEU LEU B . n 
B 1 95  LEU 95  1565 1565 LEU LEU B . n 
B 1 96  ARG 96  1566 1566 ARG ARG B . n 
B 1 97  HIS 97  1567 1567 HIS HIS B . n 
B 1 98  THR 98  1568 1568 THR THR B . n 
B 1 99  GLN 99  1569 1569 GLN GLN B . n 
B 1 100 LEU 100 1570 1570 LEU LEU B . n 
B 1 101 LEU 101 1571 1571 LEU LEU B . n 
B 1 102 PRO 102 1572 1572 PRO PRO B . n 
B 1 103 VAL 103 1573 1573 VAL VAL B . n 
B 1 104 ASP 104 1574 1574 ASP ASP B . n 
B 1 105 LYS 105 1575 1575 LYS LYS B . n 
B 1 106 ALA 106 1576 1576 ALA ALA B . n 
B 1 107 PHE 107 1577 1577 PHE PHE B . n 
B 1 108 TYR 108 1578 1578 TYR TYR B . n 
B 1 109 GLU 109 1579 1579 GLU GLU B . n 
B 1 110 ALA 110 1580 1580 ALA ALA B . n 
B 1 111 GLY 111 1581 1581 GLY GLY B . n 
B 1 112 ILE 112 1582 1582 ILE ILE B . n 
B 1 113 ALA 113 1583 1583 ALA ALA B . n 
B 1 114 ALA 114 1584 1584 ALA ALA B . n 
B 1 115 LYS 115 1585 1585 LYS LYS B . n 
B 1 116 ALA 116 1586 1586 ALA ALA B . n 
B 1 117 VAL 117 1587 1587 VAL VAL B . n 
B 1 118 GLY 118 1588 1588 GLY GLY B . n 
B 1 119 TRP 119 1589 1589 TRP TRP B . n 
B 1 120 ASP 120 1590 1590 ASP ASP B . n 
B 1 121 ASN 121 1591 1591 ASN ASN B . n 
B 1 122 MET 122 1592 1592 MET MET B . n 
B 1 123 ALA 123 1593 1593 ALA ALA B . n 
B 1 124 PHE 124 1594 1594 PHE PHE B . n 
B 1 125 ILE 125 1595 1595 ILE ILE B . n 
B 1 126 PHE 126 1596 1596 PHE PHE B . n 
B 1 127 LEU 127 1597 1597 LEU LEU B . n 
B 1 128 ASN 128 1598 1598 ASN ASN B . n 
B 1 129 ARG 129 1599 1599 ARG ARG B . n 
B 1 130 PHE 130 1600 1600 PHE PHE B . n 
B 1 131 LEU 131 1601 1601 LEU LEU B . n 
B 1 132 ASP 132 1602 1602 ASP ASP B . n 
B 1 133 LEU 133 1603 1603 LEU LEU B . n 
B 1 134 THR 134 1604 1604 THR THR B . n 
B 1 135 ASP 135 1605 1605 ASP ASP B . n 
B 1 136 ALA 136 1606 1606 ALA ALA B . n 
B 1 137 ILE 137 1607 1607 ILE ILE B . n 
B 1 138 GLU 138 1608 1608 GLU GLU B . n 
B 1 139 GLU 139 1609 1609 GLU GLU B . n 
B 1 140 GLY 140 1610 1610 GLY GLY B . n 
B 1 141 THR 141 1611 1611 THR THR B . n 
B 1 142 LEU 142 1612 1612 LEU LEU B . n 
B 1 143 ASP 143 1613 1613 ASP ASP B . n 
B 1 144 GLY 144 1614 1614 GLY GLY B . n 
B 1 145 LEU 145 1615 1615 LEU LEU B . n 
B 1 146 ASP 146 1616 1616 ASP ASP B . n 
B 1 147 HIS 147 1617 1617 HIS HIS B . n 
B 1 148 SER 148 1618 1618 SER SER B . n 
B 1 149 ASP 149 1619 1619 ASP ASP B . n 
B 1 150 PHE 150 1620 1620 PHE PHE B . n 
B 1 151 GLN 151 1621 1621 GLN GLN B . n 
B 1 152 ASP 152 1622 1622 ASP ASP B . n 
B 1 153 THR 153 1623 1623 THR THR B . n 
B 1 154 ASP 154 1624 1624 ASP ASP B . n 
B 1 155 ILE 155 1625 1625 ILE ILE B . n 
B 1 156 PRO 156 1626 1626 PRO PRO B . n 
B 1 157 PHE 157 1627 1627 PHE PHE B . n 
B 1 158 GLU 158 1628 1628 GLU GLU B . n 
B 1 159 VAL 159 1629 1629 VAL VAL B . n 
B 1 160 PRO 160 1630 1630 PRO PRO B . n 
B 1 161 LEU 161 1631 1631 LEU LEU B . n 
B 1 162 PRO 162 1632 1632 PRO PRO B . n 
B 1 163 ALA 163 1633 1633 ALA ALA B . n 
B 1 164 LYS 164 1634 1634 LYS LYS B . n 
B 1 165 GLN 165 1635 1635 GLN GLN B . n 
B 1 166 HIS 166 1636 1636 HIS HIS B . n 
B 1 167 VAL 167 1637 1637 VAL VAL B . n 
B 1 168 PRO 168 1638 1638 PRO PRO B . n 
B 1 169 GLU 169 1639 1639 GLU GLU B . n 
B 1 170 ALA 170 1640 1640 ALA ALA B . n 
B 1 171 GLU 171 1641 1641 GLU GLU B . n 
B 1 172 ARG 172 1642 1642 ARG ARG B . n 
B 1 173 GLU 173 1643 1643 GLU GLU B . n 
B 1 174 GLU 174 1644 1644 GLU GLU B . n 
B 1 175 VAL 175 1645 1645 VAL VAL B . n 
B 1 176 ARG 176 1646 1646 ARG ARG B . n 
B 1 177 ASP 177 1647 1647 ASP ASP B . n 
B 1 178 TRP 178 1648 1648 TRP TRP B . n 
B 1 179 VAL 179 1649 1649 VAL VAL B . n 
B 1 180 LEU 180 1650 1650 LEU LEU B . n 
B 1 181 THR 181 1651 1651 THR THR B . n 
B 1 182 VAL 182 1652 1652 VAL VAL B . n 
B 1 183 SER 183 1653 1653 SER SER B . n 
B 1 184 MET 184 1654 1654 MET MET B . n 
B 1 185 ASP 185 1655 1655 ASP ASP B . n 
B 1 186 GLN 186 1656 1656 GLN GLN B . n 
B 1 187 ARG 187 1657 1657 ARG ARG B . n 
B 1 188 LEU 188 1658 1658 LEU LEU B . n 
B 1 189 GLU 189 1659 1659 GLU GLU B . n 
B 1 190 GLN 190 1660 1660 GLN GLN B . n 
B 1 191 VAL 191 1661 1661 VAL VAL B . n 
B 1 192 LEU 192 1662 1662 LEU LEU B . n 
B 1 193 PRO 193 1663 1663 PRO PRO B . n 
B 1 194 ARG 194 1664 1664 ARG ARG B . n 
B 1 195 ASP 195 1665 1665 ASP ASP B . n 
B 1 196 GLU 196 1666 1666 GLU GLU B . n 
B 1 197 ARG 197 1667 1667 ARG ARG B . n 
B 1 198 GLY 198 1668 1668 GLY GLY B . n 
B 1 199 ALA 199 1669 1669 ALA ALA B . n 
B 1 200 TYR 200 1670 1670 TYR TYR B . n 
B 1 201 GLU 201 1671 1671 GLU GLU B . n 
B 1 202 ALA 202 1672 1672 ALA ALA B . n 
B 1 203 SER 203 1673 1673 SER SER B . n 
B 1 204 LEU 204 1674 1674 LEU LEU B . n 
B 1 205 VAL 205 1675 1675 VAL VAL B . n 
B 1 206 ALA 206 1676 1676 ALA ALA B . n 
B 1 207 ALA 207 1677 1677 ALA ALA B . n 
B 1 208 SER 208 1678 1678 SER SER B . n 
B 1 209 THR 209 1679 1679 THR THR B . n 
B 1 210 GLY 210 1680 1680 GLY GLY B . n 
B 1 211 VAL 211 1681 1681 VAL VAL B . n 
B 1 212 ARG 212 1682 1682 ARG ARG B . n 
B 1 213 ALA 213 1683 1683 ALA ALA B . n 
B 1 214 LEU 214 1684 1684 LEU LEU B . n 
B 1 215 PRO 215 1685 1685 PRO PRO B . n 
B 1 216 CYS 216 1686 1686 CYS CYS B . n 
B 1 217 LEU 217 1687 1687 LEU LEU B . n 
B 1 218 ILE 218 1688 1688 ILE ILE B . n 
B 1 219 THR 219 1689 1689 THR THR B . n 
B 1 220 GLY 220 1690 1690 GLY GLY B . n 
B 1 221 TYR 221 1691 1691 TYR TYR B . n 
B 1 222 PRO 222 1692 1692 PRO PRO B . n 
B 1 223 ILE 223 1693 1693 ILE ILE B . n 
B 1 224 LEU 224 1694 1694 LEU LEU B . n 
B 1 225 ARG 225 1695 1695 ARG ARG B . n 
B 1 226 ASN 226 1696 1696 ASN ASN B . n 
B 1 227 LYS 227 1697 1697 LYS LYS B . n 
B 1 228 ILE 228 1698 1698 ILE ILE B . n 
B 1 229 GLU 229 1699 1699 GLU GLU B . n 
B 1 230 PHE 230 1700 1700 PHE PHE B . n 
B 1 231 LYS 231 1701 1701 LYS LYS B . n 
B 1 232 ARG 232 1702 1702 ARG ARG B . n 
B 1 233 PRO 233 1703 1703 PRO PRO B . n 
B 1 234 GLY 234 1704 1704 GLY GLY B . n 
B 1 235 LYS 235 1705 1705 LYS LYS B . n 
B 1 236 ALA 236 1706 1706 ALA ALA B . n 
B 1 237 ALA 237 1707 1707 ALA ALA B . n 
B 1 238 ASN 238 1708 1708 ASN ASN B . n 
B 1 239 LYS 239 1709 1709 LYS LYS B . n 
B 1 240 ASP 240 1710 1710 ASP ASP B . n 
B 1 241 ASN 241 1711 1711 ASN ASN B . n 
B 1 242 TRP 242 1712 1712 TRP TRP B . n 
B 1 243 ASN 243 1713 1713 ASN ASN B . n 
B 1 244 LYS 244 1714 1714 LYS LYS B . n 
B 1 245 PHE 245 1715 1715 PHE PHE B . n 
B 1 246 LEU 246 1716 1716 LEU LEU B . n 
B 1 247 MET 247 1717 1717 MET MET B . n 
B 1 248 ALA 248 1718 1718 ALA ALA B . n 
B 1 249 ILE 249 1719 1719 ILE ILE B . n 
B 1 250 LYS 250 1720 1720 LYS LYS B . n 
B 1 251 THR 251 1721 1721 THR THR B . n 
B 1 252 SER 252 1722 1722 SER SER B . n 
B 1 253 HIS 253 1723 1723 HIS HIS B . n 
B 1 254 SER 254 1724 1724 SER SER B . n 
B 1 255 PRO 255 1725 1725 PRO PRO B . n 
B 1 256 VAL 256 1726 1726 VAL VAL B . n 
B 1 257 CYS 257 1727 1727 CYS CYS B . n 
B 1 258 GLN 258 1728 1728 GLN GLN B . n 
B 1 259 ASP 259 1729 1729 ASP ASP B . n 
B 1 260 VAL 260 1730 1730 VAL VAL B . n 
B 1 261 LEU 261 1731 1731 LEU LEU B . n 
B 1 262 LYS 262 1732 1732 LYS LYS B . n 
B 1 263 PHE 263 1733 1733 PHE PHE B . n 
B 1 264 ILE 264 1734 1734 ILE ILE B . n 
B 1 265 SER 265 1735 1735 SER SER B . n 
B 1 266 GLN 266 1736 1736 GLN GLN B . n 
B 1 267 TRP 267 1737 1737 TRP TRP B . n 
B 1 268 CYS 268 1738 1738 CYS CYS B . n 
B 1 269 GLY 269 1739 1739 GLY GLY B . n 
B 1 270 GLY 270 1740 1740 GLY GLY B . n 
B 1 271 LEU 271 1741 1741 LEU LEU B . n 
B 1 272 PRO 272 1742 ?    ?   ?   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 CL  ? ? CL  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 EPE ? ? EPE ? ? '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 2 EPE 1  1801 1   EPE EPE A . 
D 3 CL  1  1802 1   CL  CL  A . 
E 2 EPE 1  1801 1   EPE EPE B . 
F 4 HOH 1  1901 71  HOH HOH A . 
F 4 HOH 2  1902 76  HOH HOH A . 
F 4 HOH 3  1903 66  HOH HOH A . 
F 4 HOH 4  1904 154 HOH HOH A . 
F 4 HOH 5  1905 182 HOH HOH A . 
F 4 HOH 6  1906 190 HOH HOH A . 
F 4 HOH 7  1907 195 HOH HOH A . 
F 4 HOH 8  1908 22  HOH HOH A . 
F 4 HOH 9  1909 15  HOH HOH A . 
F 4 HOH 10 1910 35  HOH HOH A . 
F 4 HOH 11 1911 83  HOH HOH A . 
F 4 HOH 12 1912 52  HOH HOH A . 
F 4 HOH 13 1913 110 HOH HOH A . 
F 4 HOH 14 1914 7   HOH HOH A . 
F 4 HOH 15 1915 144 HOH HOH A . 
F 4 HOH 16 1916 192 HOH HOH A . 
F 4 HOH 17 1917 10  HOH HOH A . 
F 4 HOH 18 1918 17  HOH HOH A . 
F 4 HOH 19 1919 137 HOH HOH A . 
F 4 HOH 20 1920 119 HOH HOH A . 
F 4 HOH 21 1921 183 HOH HOH A . 
F 4 HOH 22 1922 13  HOH HOH A . 
F 4 HOH 23 1923 30  HOH HOH A . 
F 4 HOH 24 1924 61  HOH HOH A . 
F 4 HOH 25 1925 12  HOH HOH A . 
F 4 HOH 26 1926 20  HOH HOH A . 
F 4 HOH 27 1927 3   HOH HOH A . 
F 4 HOH 28 1928 18  HOH HOH A . 
F 4 HOH 29 1929 99  HOH HOH A . 
F 4 HOH 30 1930 44  HOH HOH A . 
F 4 HOH 31 1931 174 HOH HOH A . 
F 4 HOH 32 1932 82  HOH HOH A . 
F 4 HOH 33 1933 78  HOH HOH A . 
F 4 HOH 34 1934 91  HOH HOH A . 
F 4 HOH 35 1935 70  HOH HOH A . 
F 4 HOH 36 1936 38  HOH HOH A . 
F 4 HOH 37 1937 211 HOH HOH A . 
F 4 HOH 38 1938 53  HOH HOH A . 
F 4 HOH 39 1939 51  HOH HOH A . 
F 4 HOH 40 1940 98  HOH HOH A . 
F 4 HOH 41 1941 77  HOH HOH A . 
F 4 HOH 42 1942 1   HOH HOH A . 
F 4 HOH 43 1943 33  HOH HOH A . 
F 4 HOH 44 1944 186 HOH HOH A . 
F 4 HOH 45 1945 138 HOH HOH A . 
F 4 HOH 46 1946 184 HOH HOH A . 
F 4 HOH 47 1947 19  HOH HOH A . 
F 4 HOH 48 1948 11  HOH HOH A . 
F 4 HOH 49 1949 208 HOH HOH A . 
F 4 HOH 50 1950 135 HOH HOH A . 
F 4 HOH 51 1951 187 HOH HOH A . 
F 4 HOH 52 1952 176 HOH HOH A . 
F 4 HOH 53 1953 34  HOH HOH A . 
F 4 HOH 54 1954 24  HOH HOH A . 
F 4 HOH 55 1955 81  HOH HOH A . 
F 4 HOH 56 1956 105 HOH HOH A . 
F 4 HOH 57 1957 74  HOH HOH A . 
F 4 HOH 58 1958 212 HOH HOH A . 
F 4 HOH 59 1959 80  HOH HOH A . 
F 4 HOH 60 1960 194 HOH HOH A . 
F 4 HOH 61 1961 168 HOH HOH A . 
F 4 HOH 62 1962 28  HOH HOH A . 
F 4 HOH 63 1963 108 HOH HOH A . 
F 4 HOH 64 1964 172 HOH HOH A . 
F 4 HOH 65 1965 94  HOH HOH A . 
F 4 HOH 66 1966 193 HOH HOH A . 
F 4 HOH 67 1967 32  HOH HOH A . 
F 4 HOH 68 1968 139 HOH HOH A . 
F 4 HOH 69 1969 96  HOH HOH A . 
F 4 HOH 70 1970 29  HOH HOH A . 
F 4 HOH 71 1971 185 HOH HOH A . 
F 4 HOH 72 1972 143 HOH HOH A . 
F 4 HOH 73 1973 126 HOH HOH A . 
F 4 HOH 74 1974 179 HOH HOH A . 
F 4 HOH 75 1975 160 HOH HOH A . 
F 4 HOH 76 1976 64  HOH HOH A . 
F 4 HOH 77 1977 198 HOH HOH A . 
F 4 HOH 78 1978 47  HOH HOH A . 
F 4 HOH 79 1979 140 HOH HOH A . 
F 4 HOH 80 1980 197 HOH HOH A . 
F 4 HOH 81 1981 188 HOH HOH A . 
F 4 HOH 82 1982 191 HOH HOH A . 
F 4 HOH 83 1983 127 HOH HOH A . 
F 4 HOH 84 1984 153 HOH HOH A . 
F 4 HOH 85 1985 97  HOH HOH A . 
F 4 HOH 86 1986 162 HOH HOH A . 
F 4 HOH 87 1987 145 HOH HOH A . 
F 4 HOH 88 1988 158 HOH HOH A . 
F 4 HOH 89 1989 65  HOH HOH A . 
F 4 HOH 90 1990 189 HOH HOH A . 
F 4 HOH 91 1991 112 HOH HOH A . 
F 4 HOH 92 1992 131 HOH HOH A . 
G 4 HOH 1  1901 48  HOH HOH B . 
G 4 HOH 2  1902 21  HOH HOH B . 
G 4 HOH 3  1903 84  HOH HOH B . 
G 4 HOH 4  1904 9   HOH HOH B . 
G 4 HOH 5  1905 2   HOH HOH B . 
G 4 HOH 6  1906 117 HOH HOH B . 
G 4 HOH 7  1907 90  HOH HOH B . 
G 4 HOH 8  1908 6   HOH HOH B . 
G 4 HOH 9  1909 40  HOH HOH B . 
G 4 HOH 10 1910 5   HOH HOH B . 
G 4 HOH 11 1911 132 HOH HOH B . 
G 4 HOH 12 1912 41  HOH HOH B . 
G 4 HOH 13 1913 104 HOH HOH B . 
G 4 HOH 14 1914 141 HOH HOH B . 
G 4 HOH 15 1915 39  HOH HOH B . 
G 4 HOH 16 1916 4   HOH HOH B . 
G 4 HOH 17 1917 25  HOH HOH B . 
G 4 HOH 18 1918 93  HOH HOH B . 
G 4 HOH 19 1919 50  HOH HOH B . 
G 4 HOH 20 1920 43  HOH HOH B . 
G 4 HOH 21 1921 60  HOH HOH B . 
G 4 HOH 22 1922 201 HOH HOH B . 
G 4 HOH 23 1923 62  HOH HOH B . 
G 4 HOH 24 1924 136 HOH HOH B . 
G 4 HOH 25 1925 14  HOH HOH B . 
G 4 HOH 26 1926 73  HOH HOH B . 
G 4 HOH 27 1927 173 HOH HOH B . 
G 4 HOH 28 1928 161 HOH HOH B . 
G 4 HOH 29 1929 58  HOH HOH B . 
G 4 HOH 30 1930 31  HOH HOH B . 
G 4 HOH 31 1931 122 HOH HOH B . 
G 4 HOH 32 1932 167 HOH HOH B . 
G 4 HOH 33 1933 79  HOH HOH B . 
G 4 HOH 34 1934 49  HOH HOH B . 
G 4 HOH 35 1935 23  HOH HOH B . 
G 4 HOH 36 1936 55  HOH HOH B . 
G 4 HOH 37 1937 26  HOH HOH B . 
G 4 HOH 38 1938 123 HOH HOH B . 
G 4 HOH 39 1939 45  HOH HOH B . 
G 4 HOH 40 1940 202 HOH HOH B . 
G 4 HOH 41 1941 95  HOH HOH B . 
G 4 HOH 42 1942 27  HOH HOH B . 
G 4 HOH 43 1943 203 HOH HOH B . 
G 4 HOH 44 1944 8   HOH HOH B . 
G 4 HOH 45 1945 85  HOH HOH B . 
G 4 HOH 46 1946 121 HOH HOH B . 
G 4 HOH 47 1947 210 HOH HOH B . 
G 4 HOH 48 1948 205 HOH HOH B . 
G 4 HOH 49 1949 63  HOH HOH B . 
G 4 HOH 50 1950 101 HOH HOH B . 
G 4 HOH 51 1951 56  HOH HOH B . 
G 4 HOH 52 1952 163 HOH HOH B . 
G 4 HOH 53 1953 125 HOH HOH B . 
G 4 HOH 54 1954 67  HOH HOH B . 
G 4 HOH 55 1955 148 HOH HOH B . 
G 4 HOH 56 1956 72  HOH HOH B . 
G 4 HOH 57 1957 157 HOH HOH B . 
G 4 HOH 58 1958 59  HOH HOH B . 
G 4 HOH 59 1959 207 HOH HOH B . 
G 4 HOH 60 1960 113 HOH HOH B . 
G 4 HOH 61 1961 170 HOH HOH B . 
G 4 HOH 62 1962 69  HOH HOH B . 
G 4 HOH 63 1963 165 HOH HOH B . 
G 4 HOH 64 1964 166 HOH HOH B . 
G 4 HOH 65 1965 109 HOH HOH B . 
G 4 HOH 66 1966 115 HOH HOH B . 
G 4 HOH 67 1967 57  HOH HOH B . 
G 4 HOH 68 1968 116 HOH HOH B . 
G 4 HOH 69 1969 209 HOH HOH B . 
G 4 HOH 70 1970 133 HOH HOH B . 
G 4 HOH 71 1971 159 HOH HOH B . 
G 4 HOH 72 1972 178 HOH HOH B . 
G 4 HOH 73 1973 130 HOH HOH B . 
G 4 HOH 74 1974 180 HOH HOH B . 
G 4 HOH 75 1975 68  HOH HOH B . 
G 4 HOH 76 1976 103 HOH HOH B . 
G 4 HOH 77 1977 100 HOH HOH B . 
G 4 HOH 78 1978 152 HOH HOH B . 
G 4 HOH 79 1979 204 HOH HOH B . 
G 4 HOH 80 1980 87  HOH HOH B . 
G 4 HOH 81 1981 149 HOH HOH B . 
G 4 HOH 82 1982 206 HOH HOH B . 
G 4 HOH 83 1983 124 HOH HOH B . 
G 4 HOH 84 1984 151 HOH HOH B . 
G 4 HOH 85 1985 106 HOH HOH B . 
# 
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 B PHE 1478 ? CG  ? B PHE 8   CG  
2  1 Y 1 B PHE 1478 ? CD1 ? B PHE 8   CD1 
3  1 Y 1 B PHE 1478 ? CD2 ? B PHE 8   CD2 
4  1 Y 1 B PHE 1478 ? CE1 ? B PHE 8   CE1 
5  1 Y 1 B PHE 1478 ? CE2 ? B PHE 8   CE2 
6  1 Y 1 B PHE 1478 ? CZ  ? B PHE 8   CZ  
7  1 Y 1 B HIS 1528 ? CG  ? B HIS 58  CG  
8  1 Y 1 B HIS 1528 ? ND1 ? B HIS 58  ND1 
9  1 Y 1 B HIS 1528 ? CD2 ? B HIS 58  CD2 
10 1 Y 1 B HIS 1528 ? CE1 ? B HIS 58  CE1 
11 1 Y 1 B HIS 1528 ? NE2 ? B HIS 58  NE2 
12 1 Y 1 B LYS 1551 ? CG  ? B LYS 81  CG  
13 1 Y 1 B LYS 1551 ? CD  ? B LYS 81  CD  
14 1 Y 1 B LYS 1551 ? CE  ? B LYS 81  CE  
15 1 Y 1 B LYS 1551 ? NZ  ? B LYS 81  NZ  
16 1 Y 1 B GLU 1609 ? CG  ? B GLU 139 CG  
17 1 Y 1 B GLU 1609 ? CD  ? B GLU 139 CD  
18 1 Y 1 B GLU 1609 ? OE1 ? B GLU 139 OE1 
19 1 Y 1 B GLU 1609 ? OE2 ? B GLU 139 OE2 
20 1 Y 1 B LEU 1612 ? CG  ? B LEU 142 CG  
21 1 Y 1 B LEU 1612 ? CD1 ? B LEU 142 CD1 
22 1 Y 1 B LEU 1612 ? CD2 ? B LEU 142 CD2 
23 1 Y 1 B GLN 1621 ? CG  ? B GLN 151 CG  
24 1 Y 1 B GLN 1621 ? CD  ? B GLN 151 CD  
25 1 Y 1 B GLN 1621 ? OE1 ? B GLN 151 OE1 
26 1 Y 1 B GLN 1621 ? NE2 ? B GLN 151 NE2 
27 1 Y 1 B GLU 1628 ? CG  ? B GLU 158 CG  
28 1 Y 1 B GLU 1628 ? CD  ? B GLU 158 CD  
29 1 Y 1 B GLU 1628 ? OE1 ? B GLU 158 OE1 
30 1 Y 1 B GLU 1628 ? OE2 ? B GLU 158 OE2 
31 1 Y 1 B LYS 1634 ? CG  ? B LYS 164 CG  
32 1 Y 1 B LYS 1634 ? CD  ? B LYS 164 CD  
33 1 Y 1 B LYS 1634 ? CE  ? B LYS 164 CE  
34 1 Y 1 B LYS 1634 ? NZ  ? B LYS 164 NZ  
35 1 Y 1 B GLU 1639 ? CG  ? B GLU 169 CG  
36 1 Y 1 B GLU 1639 ? CD  ? B GLU 169 CD  
37 1 Y 1 B GLU 1639 ? OE1 ? B GLU 169 OE1 
38 1 Y 1 B GLU 1639 ? OE2 ? B GLU 169 OE2 
39 1 Y 1 B ASP 1655 ? CG  ? B ASP 185 CG  
40 1 Y 1 B ASP 1655 ? OD1 ? B ASP 185 OD1 
41 1 Y 1 B ASP 1655 ? OD2 ? B ASP 185 OD2 
42 1 Y 1 B GLN 1656 ? CG  ? B GLN 186 CG  
43 1 Y 1 B GLN 1656 ? CD  ? B GLN 186 CD  
44 1 Y 1 B GLN 1656 ? OE1 ? B GLN 186 OE1 
45 1 Y 1 B GLN 1656 ? NE2 ? B GLN 186 NE2 
46 1 Y 1 B ARG 1657 ? CG  ? B ARG 187 CG  
47 1 Y 1 B ARG 1657 ? CD  ? B ARG 187 CD  
48 1 Y 1 B ARG 1657 ? NE  ? B ARG 187 NE  
49 1 Y 1 B ARG 1657 ? CZ  ? B ARG 187 CZ  
50 1 Y 1 B ARG 1657 ? NH1 ? B ARG 187 NH1 
51 1 Y 1 B ARG 1657 ? NH2 ? B ARG 187 NH2 
52 1 Y 1 B LEU 1658 ? CG  ? B LEU 188 CG  
53 1 Y 1 B LEU 1658 ? CD1 ? B LEU 188 CD1 
54 1 Y 1 B LEU 1658 ? CD2 ? B LEU 188 CD2 
55 1 Y 1 B GLU 1659 ? CG  ? B GLU 189 CG  
56 1 Y 1 B GLU 1659 ? CD  ? B GLU 189 CD  
57 1 Y 1 B GLU 1659 ? OE1 ? B GLU 189 OE1 
58 1 Y 1 B GLU 1659 ? OE2 ? B GLU 189 OE2 
59 1 Y 1 B GLN 1660 ? CG  ? B GLN 190 CG  
60 1 Y 1 B GLN 1660 ? CD  ? B GLN 190 CD  
61 1 Y 1 B GLN 1660 ? OE1 ? B GLN 190 OE1 
62 1 Y 1 B GLN 1660 ? NE2 ? B GLN 190 NE2 
63 1 Y 1 B ARG 1682 ? CG  ? B ARG 212 CG  
64 1 Y 1 B ARG 1682 ? CD  ? B ARG 212 CD  
65 1 Y 1 B ARG 1682 ? NE  ? B ARG 212 NE  
66 1 Y 1 B ARG 1682 ? CZ  ? B ARG 212 CZ  
67 1 Y 1 B ARG 1682 ? NH1 ? B ARG 212 NH1 
68 1 Y 1 B ARG 1682 ? NH2 ? B ARG 212 NH2 
69 1 Y 1 B LYS 1701 ? CG  ? B LYS 231 CG  
70 1 Y 1 B LYS 1701 ? CD  ? B LYS 231 CD  
71 1 Y 1 B LYS 1701 ? CE  ? B LYS 231 CE  
72 1 Y 1 B LYS 1701 ? NZ  ? B LYS 231 NZ  
73 1 Y 1 B ARG 1702 ? CG  ? B ARG 232 CG  
74 1 Y 1 B ARG 1702 ? CD  ? B ARG 232 CD  
75 1 Y 1 B ARG 1702 ? NE  ? B ARG 232 NE  
76 1 Y 1 B ARG 1702 ? CZ  ? B ARG 232 CZ  
77 1 Y 1 B ARG 1702 ? NH1 ? B ARG 232 NH1 
78 1 Y 1 B ARG 1702 ? NH2 ? B ARG 232 NH2 
79 1 Y 1 B LYS 1732 ? CG  ? B LYS 262 CG  
80 1 Y 1 B LYS 1732 ? CD  ? B LYS 262 CD  
81 1 Y 1 B LYS 1732 ? CE  ? B LYS 262 CE  
82 1 Y 1 B LYS 1732 ? NZ  ? B LYS 262 NZ  
83 1 Y 1 B LEU 1741 ? CG  ? B LEU 271 CG  
84 1 Y 1 B LEU 1741 ? CD1 ? B LEU 271 CD1 
85 1 Y 1 B LEU 1741 ? CD2 ? B LEU 271 CD2 
# 
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    ? ? ? '(1.14_3260: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? pointless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.42 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H2D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.967 
_cell.length_a_esd                 ? 
_cell.length_b                     90.507 
_cell.length_b_esd                 ? 
_cell.length_c                     67.423 
_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                         9H2D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9H2D 
_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             2.37 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.15 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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 Sodium phosphate dibasic dihydrate, 20% w/v Polyethylene glycol 3350, pH 9.1' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 PILATUS3 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         2015-11-24 
_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   1.006 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.006 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H2D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.07 
_reflns.d_resolution_low                               46.573 
_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                                     34038 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    2.07 
_reflns_shell.d_res_low                                     2.10 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1631 
_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                               6.4 
_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                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.483 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.777 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               65 
_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                                 9H2D 
_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                            2.097 
_refine.ls_d_res_low                             46.573 
_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                     32557 
_refine.ls_number_reflns_R_free                  1564 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.14 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1917 
_refine.ls_R_factor_R_free                       0.2383 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1893 
_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                          1.33 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_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                 31.07 
_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                            0.29 
_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        4128 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.number_atoms_solvent             177 
_refine_hist.number_atoms_total               4306 
_refine_hist.d_res_high                       2.097 
_refine_hist.d_res_low                        46.573 
# 
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' ? 0.008 ? 4327 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.952 ? 5904 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.682 ? 3509 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050 ? 661  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 768  ? 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' 2.0972 2.1649 . . 134 2602 92.00  . . . . 0.3525 . . . . . . . . . . . 0.3478 
'X-RAY DIFFRACTION' 2.1649 2.2423 . . 146 2827 100.00 . . . . 0.3193 . . . . . . . . . . . 0.3907 
'X-RAY DIFFRACTION' 2.2423 2.3321 . . 140 2821 100.00 . . . . 0.2883 . . . . . . . . . . . 0.3584 
'X-RAY DIFFRACTION' 2.3321 2.4382 . . 151 2799 100.00 . . . . 0.2641 . . . . . . . . . . . 0.3666 
'X-RAY DIFFRACTION' 2.4382 2.5668 . . 152 2835 100.00 . . . . 0.2441 . . . . . . . . . . . 0.3015 
'X-RAY DIFFRACTION' 2.5668 2.7276 . . 128 2830 100.00 . . . . 0.2152 . . . . . . . . . . . 0.2905 
'X-RAY DIFFRACTION' 2.7276 2.9381 . . 142 2858 100.00 . . . . 0.2048 . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 2.9381 3.2337 . . 126 2838 100.00 . . . . 0.2010 . . . . . . . . . . . 0.3002 
'X-RAY DIFFRACTION' 3.2337 3.7015 . . 139 2850 100.00 . . . . 0.1806 . . . . . . . . . . . 0.2396 
'X-RAY DIFFRACTION' 3.7015 4.6628 . . 149 2850 100.00 . . . . 0.1404 . . . . . . . . . . . 0.1910 
'X-RAY DIFFRACTION' 4.6628 46.573 . . 157 2883 100.00 . . . . 0.1522 . . . . . . . . . . . 0.1742 
# 
_struct.entry_id                     9H2D 
_struct.title                        'Human IFT172 C-terminal U-box domain crystal structure' 
_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        9H2D 
_struct_keywords.text            
'Cilia, intraflagellar transport, IFT172, intracellular trafficking, U-box, ubiquitin, PROTEIN TRANSPORT' 
_struct_keywords.pdbx_keywords   'PROTEIN TRANSPORT' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IF172_HUMAN 
_struct_ref.pdbx_db_accession          Q9UG01 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;APANPQNFNIYKRIFTDMVSSPGTNCAEAYHSWADLRDVLFNLCENLVKSSEANSPAHEEFKTMLLIAHYYATRSAAQSV
KQLETVAARLSVSLLRHTQLLPVDKAFYEAGIAAKAVGWDNMAFIFLNRFLDLTDAIEEGTLDGLDHSDFQDTDIPFEVP
LPAKQHVPEAEREEVRDWVLTVSMDQRLEQVLPRDERGAYEASLVAASTGVRALPCLITGYPILRNKIEFKRPGKAANKD
NWNKFLMAIKTSHSPVCQDVLKFISQWCGGLP
;
_struct_ref.pdbx_align_begin           1471 
# 
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 9H2D A 1 ? 272 ? Q9UG01 1471 ? 1742 ? 1471 1742 
2 1 9H2D B 1 ? 272 ? Q9UG01 1471 ? 1742 ? 1471 1742 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,F 
2 1 B,E,G   
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 ASN A 7   ? SER A 20  ? ASN A 1477 SER A 1490 1 ? 14 
HELX_P HELX_P2  AA2 CYS A 26  ? GLU A 28  ? CYS A 1496 GLU A 1498 5 ? 3  
HELX_P HELX_P3  AA3 ALA A 29  ? SER A 51  ? ALA A 1499 SER A 1521 1 ? 23 
HELX_P HELX_P4  AA4 SER A 55  ? SER A 79  ? SER A 1525 SER A 1549 1 ? 25 
HELX_P HELX_P5  AA5 VAL A 80  ? GLN A 82  ? VAL A 1550 GLN A 1552 5 ? 3  
HELX_P HELX_P6  AA6 LEU A 83  ? LEU A 95  ? LEU A 1553 LEU A 1565 1 ? 13 
HELX_P HELX_P7  AA7 ARG A 96  ? THR A 98  ? ARG A 1566 THR A 1568 5 ? 3  
HELX_P HELX_P8  AA8 PRO A 102 ? VAL A 117 ? PRO A 1572 VAL A 1587 1 ? 16 
HELX_P HELX_P9  AA9 TRP A 119 ? GLY A 140 ? TRP A 1589 GLY A 1610 1 ? 22 
HELX_P HELX_P10 AB1 HIS A 147 ? GLN A 151 ? HIS A 1617 GLN A 1621 5 ? 5  
HELX_P HELX_P11 AB2 PRO A 168 ? SER A 183 ? PRO A 1638 SER A 1653 1 ? 16 
HELX_P HELX_P12 AB3 LYS A 239 ? HIS A 253 ? LYS A 1709 HIS A 1723 1 ? 15 
HELX_P HELX_P13 AB4 SER A 254 ? GLY A 269 ? SER A 1724 GLY A 1739 1 ? 16 
HELX_P HELX_P14 AB5 PHE B 8   ? SER B 20  ? PHE B 1478 SER B 1490 1 ? 13 
HELX_P HELX_P15 AB6 CYS B 26  ? GLU B 28  ? CYS B 1496 GLU B 1498 5 ? 3  
HELX_P HELX_P16 AB7 ALA B 29  ? VAL B 48  ? ALA B 1499 VAL B 1518 1 ? 20 
HELX_P HELX_P17 AB8 PRO B 56  ? SER B 79  ? PRO B 1526 SER B 1549 1 ? 24 
HELX_P HELX_P18 AB9 VAL B 80  ? GLN B 82  ? VAL B 1550 GLN B 1552 5 ? 3  
HELX_P HELX_P19 AC1 LEU B 83  ? LEU B 95  ? LEU B 1553 LEU B 1565 1 ? 13 
HELX_P HELX_P20 AC2 ARG B 96  ? THR B 98  ? ARG B 1566 THR B 1568 5 ? 3  
HELX_P HELX_P21 AC3 PRO B 102 ? VAL B 117 ? PRO B 1572 VAL B 1587 1 ? 16 
HELX_P HELX_P22 AC4 TRP B 119 ? GLY B 140 ? TRP B 1589 GLY B 1610 1 ? 22 
HELX_P HELX_P23 AC5 HIS B 147 ? GLN B 151 ? HIS B 1617 GLN B 1621 5 ? 5  
HELX_P HELX_P24 AC6 PRO B 168 ? ASP B 185 ? PRO B 1638 ASP B 1655 1 ? 18 
HELX_P HELX_P25 AC7 LYS B 239 ? HIS B 253 ? LYS B 1709 HIS B 1723 1 ? 15 
HELX_P HELX_P26 AC8 SER B 254 ? GLY B 269 ? SER B 1724 GLY B 1739 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
# 
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 
AA2 1 2 ? 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 LYS A 227 ? GLU A 229 ? LYS A 1697 GLU A 1699 
AA1 2 ALA A 236 ? ASN A 238 ? ALA A 1706 ASN A 1708 
AA2 1 LYS B 227 ? GLU B 229 ? LYS B 1697 GLU B 1699 
AA2 2 ALA B 236 ? ASN B 238 ? ALA B 1706 ASN B 1708 
# 
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 N ILE A 228 ? N ILE A 1698 O ALA A 237 ? O ALA A 1707 
AA2 1 2 N ILE B 228 ? N ILE B 1698 O ALA B 237 ? O ALA B 1707 
# 
_pdbx_entry_details.entry_id                   9H2D 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LEU 
_pdbx_validate_close_contact.auth_seq_id_1    1650 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    1653 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    ASN 
_pdbx_validate_symm_contact.auth_seq_id_1     1477 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     1958 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 1474 ? ? -118.05 74.01   
2  1 ASN A 1495 ? ? -97.01  57.53   
3  1 GLN A 1660 ? ? -108.90 74.56   
4  1 SER A 1678 ? ? -59.19  -73.31  
5  1 PHE B 1478 ? ? 115.03  -126.19 
6  1 PHE B 1478 ? ? 115.03  -134.69 
7  1 ASN B 1479 ? B -22.06  -65.42  
8  1 ASN B 1495 ? ? -96.08  58.14   
9  1 ASP B 1665 ? ? -101.05 -168.70 
10 1 SER B 1678 ? ? -59.69  -72.83  
11 1 SER B 1724 ? ? -46.49  107.69  
# 
_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         -0.8411 
_pdbx_refine_tls.origin_y         -23.3209 
_pdbx_refine_tls.origin_z         17.3765 
_pdbx_refine_tls.T[1][1]          0.3300 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0158 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.1808 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2290 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0044 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.7060 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.2881 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.1199 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4937 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.4107 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.3594 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.7332 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0095 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0110 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0163 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.1413 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0320 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0400 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1625 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0520 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0318 
_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 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1992 ? 6.08 . 
2 1 O ? B HOH 1985 ? 5.94 . 
# 
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 GLN 1656 ? A GLN 186 
2  1 Y 1 A ARG 1657 ? A ARG 187 
3  1 Y 1 B ALA 1471 ? B ALA 1   
4  1 Y 1 B PRO 1472 ? B PRO 2   
5  1 Y 1 B ALA 1473 ? B ALA 3   
6  1 Y 1 B ASN 1474 ? B ASN 4   
7  1 Y 1 B PRO 1475 ? B PRO 5   
8  1 Y 1 B GLN 1476 ? B GLN 6   
9  1 Y 1 B LYS 1519 ? B LYS 49  
10 1 Y 1 B SER 1520 ? B SER 50  
11 1 Y 1 B SER 1521 ? B SER 51  
12 1 Y 1 B GLU 1522 ? B GLU 52  
13 1 Y 1 B ALA 1523 ? B ALA 53  
14 1 Y 1 B ASN 1524 ? B ASN 54  
15 1 Y 1 B PRO 1742 ? B PRO 272 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
EPE N1   N  N N 89  
EPE C2   C  N N 90  
EPE C3   C  N N 91  
EPE N4   N  N N 92  
EPE C5   C  N N 93  
EPE C6   C  N N 94  
EPE C7   C  N N 95  
EPE C8   C  N N 96  
EPE O8   O  N N 97  
EPE C9   C  N N 98  
EPE C10  C  N N 99  
EPE S    S  N N 100 
EPE O1S  O  N N 101 
EPE O2S  O  N N 102 
EPE O3S  O  N N 103 
EPE H21  H  N N 104 
EPE H22  H  N N 105 
EPE H31  H  N N 106 
EPE H32  H  N N 107 
EPE H51  H  N N 108 
EPE H52  H  N N 109 
EPE H61  H  N N 110 
EPE H62  H  N N 111 
EPE H71  H  N N 112 
EPE H72  H  N N 113 
EPE H81  H  N N 114 
EPE H82  H  N N 115 
EPE HO8  H  N N 116 
EPE H91  H  N N 117 
EPE H92  H  N N 118 
EPE H101 H  N N 119 
EPE H102 H  N N 120 
EPE HOS3 H  N N 121 
GLN N    N  N N 122 
GLN CA   C  N S 123 
GLN C    C  N N 124 
GLN O    O  N N 125 
GLN CB   C  N N 126 
GLN CG   C  N N 127 
GLN CD   C  N N 128 
GLN OE1  O  N N 129 
GLN NE2  N  N N 130 
GLN OXT  O  N N 131 
GLN H    H  N N 132 
GLN H2   H  N N 133 
GLN HA   H  N N 134 
GLN HB2  H  N N 135 
GLN HB3  H  N N 136 
GLN HG2  H  N N 137 
GLN HG3  H  N N 138 
GLN HE21 H  N N 139 
GLN HE22 H  N N 140 
GLN HXT  H  N N 141 
GLU N    N  N N 142 
GLU CA   C  N S 143 
GLU C    C  N N 144 
GLU O    O  N N 145 
GLU CB   C  N N 146 
GLU CG   C  N N 147 
GLU CD   C  N N 148 
GLU OE1  O  N N 149 
GLU OE2  O  N N 150 
GLU OXT  O  N N 151 
GLU H    H  N N 152 
GLU H2   H  N N 153 
GLU HA   H  N N 154 
GLU HB2  H  N N 155 
GLU HB3  H  N N 156 
GLU HG2  H  N N 157 
GLU HG3  H  N N 158 
GLU HE2  H  N N 159 
GLU HXT  H  N N 160 
GLY N    N  N N 161 
GLY CA   C  N N 162 
GLY C    C  N N 163 
GLY O    O  N N 164 
GLY OXT  O  N N 165 
GLY H    H  N N 166 
GLY H2   H  N N 167 
GLY HA2  H  N N 168 
GLY HA3  H  N N 169 
GLY HXT  H  N N 170 
HIS N    N  N N 171 
HIS CA   C  N S 172 
HIS C    C  N N 173 
HIS O    O  N N 174 
HIS CB   C  N N 175 
HIS CG   C  Y N 176 
HIS ND1  N  Y N 177 
HIS CD2  C  Y N 178 
HIS CE1  C  Y N 179 
HIS NE2  N  Y N 180 
HIS OXT  O  N N 181 
HIS H    H  N N 182 
HIS H2   H  N N 183 
HIS HA   H  N N 184 
HIS HB2  H  N N 185 
HIS HB3  H  N N 186 
HIS HD1  H  N N 187 
HIS HD2  H  N N 188 
HIS HE1  H  N N 189 
HIS HE2  H  N N 190 
HIS HXT  H  N N 191 
HOH O    O  N N 192 
HOH H1   H  N N 193 
HOH H2   H  N N 194 
ILE N    N  N N 195 
ILE CA   C  N S 196 
ILE C    C  N N 197 
ILE O    O  N N 198 
ILE CB   C  N S 199 
ILE CG1  C  N N 200 
ILE CG2  C  N N 201 
ILE CD1  C  N N 202 
ILE OXT  O  N N 203 
ILE H    H  N N 204 
ILE H2   H  N N 205 
ILE HA   H  N N 206 
ILE HB   H  N N 207 
ILE HG12 H  N N 208 
ILE HG13 H  N N 209 
ILE HG21 H  N N 210 
ILE HG22 H  N N 211 
ILE HG23 H  N N 212 
ILE HD11 H  N N 213 
ILE HD12 H  N N 214 
ILE HD13 H  N N 215 
ILE HXT  H  N N 216 
LEU N    N  N N 217 
LEU CA   C  N S 218 
LEU C    C  N N 219 
LEU O    O  N N 220 
LEU CB   C  N N 221 
LEU CG   C  N N 222 
LEU CD1  C  N N 223 
LEU CD2  C  N N 224 
LEU OXT  O  N N 225 
LEU H    H  N N 226 
LEU H2   H  N N 227 
LEU HA   H  N N 228 
LEU HB2  H  N N 229 
LEU HB3  H  N N 230 
LEU HG   H  N N 231 
LEU HD11 H  N N 232 
LEU HD12 H  N N 233 
LEU HD13 H  N N 234 
LEU HD21 H  N N 235 
LEU HD22 H  N N 236 
LEU HD23 H  N N 237 
LEU HXT  H  N N 238 
LYS N    N  N N 239 
LYS CA   C  N S 240 
LYS C    C  N N 241 
LYS O    O  N N 242 
LYS CB   C  N N 243 
LYS CG   C  N N 244 
LYS CD   C  N N 245 
LYS CE   C  N N 246 
LYS NZ   N  N N 247 
LYS OXT  O  N N 248 
LYS H    H  N N 249 
LYS H2   H  N N 250 
LYS HA   H  N N 251 
LYS HB2  H  N N 252 
LYS HB3  H  N N 253 
LYS HG2  H  N N 254 
LYS HG3  H  N N 255 
LYS HD2  H  N N 256 
LYS HD3  H  N N 257 
LYS HE2  H  N N 258 
LYS HE3  H  N N 259 
LYS HZ1  H  N N 260 
LYS HZ2  H  N N 261 
LYS HZ3  H  N N 262 
LYS HXT  H  N N 263 
MET N    N  N N 264 
MET CA   C  N S 265 
MET C    C  N N 266 
MET O    O  N N 267 
MET CB   C  N N 268 
MET CG   C  N N 269 
MET SD   S  N N 270 
MET CE   C  N N 271 
MET OXT  O  N N 272 
MET H    H  N N 273 
MET H2   H  N N 274 
MET HA   H  N N 275 
MET HB2  H  N N 276 
MET HB3  H  N N 277 
MET HG2  H  N N 278 
MET HG3  H  N N 279 
MET HE1  H  N N 280 
MET HE2  H  N N 281 
MET HE3  H  N N 282 
MET HXT  H  N N 283 
PHE N    N  N N 284 
PHE CA   C  N S 285 
PHE C    C  N N 286 
PHE O    O  N N 287 
PHE CB   C  N N 288 
PHE CG   C  Y N 289 
PHE CD1  C  Y N 290 
PHE CD2  C  Y N 291 
PHE CE1  C  Y N 292 
PHE CE2  C  Y N 293 
PHE CZ   C  Y N 294 
PHE OXT  O  N N 295 
PHE H    H  N N 296 
PHE H2   H  N N 297 
PHE HA   H  N N 298 
PHE HB2  H  N N 299 
PHE HB3  H  N N 300 
PHE HD1  H  N N 301 
PHE HD2  H  N N 302 
PHE HE1  H  N N 303 
PHE HE2  H  N N 304 
PHE HZ   H  N N 305 
PHE HXT  H  N N 306 
PRO N    N  N N 307 
PRO CA   C  N S 308 
PRO C    C  N N 309 
PRO O    O  N N 310 
PRO CB   C  N N 311 
PRO CG   C  N N 312 
PRO CD   C  N N 313 
PRO OXT  O  N N 314 
PRO H    H  N N 315 
PRO HA   H  N N 316 
PRO HB2  H  N N 317 
PRO HB3  H  N N 318 
PRO HG2  H  N N 319 
PRO HG3  H  N N 320 
PRO HD2  H  N N 321 
PRO HD3  H  N N 322 
PRO HXT  H  N N 323 
SER N    N  N N 324 
SER CA   C  N S 325 
SER C    C  N N 326 
SER O    O  N N 327 
SER CB   C  N N 328 
SER OG   O  N N 329 
SER OXT  O  N N 330 
SER H    H  N N 331 
SER H2   H  N N 332 
SER HA   H  N N 333 
SER HB2  H  N N 334 
SER HB3  H  N N 335 
SER HG   H  N N 336 
SER HXT  H  N N 337 
THR N    N  N N 338 
THR CA   C  N S 339 
THR C    C  N N 340 
THR O    O  N N 341 
THR CB   C  N R 342 
THR OG1  O  N N 343 
THR CG2  C  N N 344 
THR OXT  O  N N 345 
THR H    H  N N 346 
THR H2   H  N N 347 
THR HA   H  N N 348 
THR HB   H  N N 349 
THR HG1  H  N N 350 
THR HG21 H  N N 351 
THR HG22 H  N N 352 
THR HG23 H  N N 353 
THR HXT  H  N N 354 
TRP N    N  N N 355 
TRP CA   C  N S 356 
TRP C    C  N N 357 
TRP O    O  N N 358 
TRP CB   C  N N 359 
TRP CG   C  Y N 360 
TRP CD1  C  Y N 361 
TRP CD2  C  Y N 362 
TRP NE1  N  Y N 363 
TRP CE2  C  Y N 364 
TRP CE3  C  Y N 365 
TRP CZ2  C  Y N 366 
TRP CZ3  C  Y N 367 
TRP CH2  C  Y N 368 
TRP OXT  O  N N 369 
TRP H    H  N N 370 
TRP H2   H  N N 371 
TRP HA   H  N N 372 
TRP HB2  H  N N 373 
TRP HB3  H  N N 374 
TRP HD1  H  N N 375 
TRP HE1  H  N N 376 
TRP HE3  H  N N 377 
TRP HZ2  H  N N 378 
TRP HZ3  H  N N 379 
TRP HH2  H  N N 380 
TRP HXT  H  N N 381 
TYR N    N  N N 382 
TYR CA   C  N S 383 
TYR C    C  N N 384 
TYR O    O  N N 385 
TYR CB   C  N N 386 
TYR CG   C  Y N 387 
TYR CD1  C  Y N 388 
TYR CD2  C  Y N 389 
TYR CE1  C  Y N 390 
TYR CE2  C  Y N 391 
TYR CZ   C  Y N 392 
TYR OH   O  N N 393 
TYR OXT  O  N N 394 
TYR H    H  N N 395 
TYR H2   H  N N 396 
TYR HA   H  N N 397 
TYR HB2  H  N N 398 
TYR HB3  H  N N 399 
TYR HD1  H  N N 400 
TYR HD2  H  N N 401 
TYR HE1  H  N N 402 
TYR HE2  H  N N 403 
TYR HH   H  N N 404 
TYR HXT  H  N N 405 
VAL N    N  N N 406 
VAL CA   C  N S 407 
VAL C    C  N N 408 
VAL O    O  N N 409 
VAL CB   C  N N 410 
VAL CG1  C  N N 411 
VAL CG2  C  N N 412 
VAL OXT  O  N N 413 
VAL H    H  N N 414 
VAL H2   H  N N 415 
VAL HA   H  N N 416 
VAL HB   H  N N 417 
VAL HG11 H  N N 418 
VAL HG12 H  N N 419 
VAL HG13 H  N N 420 
VAL HG21 H  N N 421 
VAL HG22 H  N N 422 
VAL HG23 H  N N 423 
VAL HXT  H  N N 424 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EPE N1  C2   sing N N 83  
EPE N1  C6   sing N N 84  
EPE N1  C9   sing N N 85  
EPE C2  C3   sing N N 86  
EPE C2  H21  sing N N 87  
EPE C2  H22  sing N N 88  
EPE C3  N4   sing N N 89  
EPE C3  H31  sing N N 90  
EPE C3  H32  sing N N 91  
EPE N4  C5   sing N N 92  
EPE N4  C7   sing N N 93  
EPE C5  C6   sing N N 94  
EPE C5  H51  sing N N 95  
EPE C5  H52  sing N N 96  
EPE C6  H61  sing N N 97  
EPE C6  H62  sing N N 98  
EPE C7  C8   sing N N 99  
EPE C7  H71  sing N N 100 
EPE C7  H72  sing N N 101 
EPE C8  O8   sing N N 102 
EPE C8  H81  sing N N 103 
EPE C8  H82  sing N N 104 
EPE O8  HO8  sing N N 105 
EPE C9  C10  sing N N 106 
EPE C9  H91  sing N N 107 
EPE C9  H92  sing N N 108 
EPE C10 S    sing N N 109 
EPE C10 H101 sing N N 110 
EPE C10 H102 sing N N 111 
EPE S   O1S  doub N N 112 
EPE S   O2S  doub N N 113 
EPE S   O3S  sing N N 114 
EPE O3S HOS3 sing N N 115 
GLN N   CA   sing N N 116 
GLN N   H    sing N N 117 
GLN N   H2   sing N N 118 
GLN CA  C    sing N N 119 
GLN CA  CB   sing N N 120 
GLN CA  HA   sing N N 121 
GLN C   O    doub N N 122 
GLN C   OXT  sing N N 123 
GLN CB  CG   sing N N 124 
GLN CB  HB2  sing N N 125 
GLN CB  HB3  sing N N 126 
GLN CG  CD   sing N N 127 
GLN CG  HG2  sing N N 128 
GLN CG  HG3  sing N N 129 
GLN CD  OE1  doub N N 130 
GLN CD  NE2  sing N N 131 
GLN NE2 HE21 sing N N 132 
GLN NE2 HE22 sing N N 133 
GLN OXT HXT  sing N N 134 
GLU N   CA   sing N N 135 
GLU N   H    sing N N 136 
GLU N   H2   sing N N 137 
GLU CA  C    sing N N 138 
GLU CA  CB   sing N N 139 
GLU CA  HA   sing N N 140 
GLU C   O    doub N N 141 
GLU C   OXT  sing N N 142 
GLU CB  CG   sing N N 143 
GLU CB  HB2  sing N N 144 
GLU CB  HB3  sing N N 145 
GLU CG  CD   sing N N 146 
GLU CG  HG2  sing N N 147 
GLU CG  HG3  sing N N 148 
GLU CD  OE1  doub N N 149 
GLU CD  OE2  sing N N 150 
GLU OE2 HE2  sing N N 151 
GLU OXT HXT  sing N N 152 
GLY N   CA   sing N N 153 
GLY N   H    sing N N 154 
GLY N   H2   sing N N 155 
GLY CA  C    sing N N 156 
GLY CA  HA2  sing N N 157 
GLY CA  HA3  sing N N 158 
GLY C   O    doub N N 159 
GLY C   OXT  sing N N 160 
GLY OXT HXT  sing N N 161 
HIS N   CA   sing N N 162 
HIS N   H    sing N N 163 
HIS N   H2   sing N N 164 
HIS CA  C    sing N N 165 
HIS CA  CB   sing N N 166 
HIS CA  HA   sing N N 167 
HIS C   O    doub N N 168 
HIS C   OXT  sing N N 169 
HIS CB  CG   sing N N 170 
HIS CB  HB2  sing N N 171 
HIS CB  HB3  sing N N 172 
HIS CG  ND1  sing Y N 173 
HIS CG  CD2  doub Y N 174 
HIS ND1 CE1  doub Y N 175 
HIS ND1 HD1  sing N N 176 
HIS CD2 NE2  sing Y N 177 
HIS CD2 HD2  sing N N 178 
HIS CE1 NE2  sing Y N 179 
HIS CE1 HE1  sing N N 180 
HIS NE2 HE2  sing N N 181 
HIS OXT HXT  sing N N 182 
HOH O   H1   sing N N 183 
HOH O   H2   sing N N 184 
ILE N   CA   sing N N 185 
ILE N   H    sing N N 186 
ILE N   H2   sing N N 187 
ILE CA  C    sing N N 188 
ILE CA  CB   sing N N 189 
ILE CA  HA   sing N N 190 
ILE C   O    doub N N 191 
ILE C   OXT  sing N N 192 
ILE CB  CG1  sing N N 193 
ILE CB  CG2  sing N N 194 
ILE CB  HB   sing N N 195 
ILE CG1 CD1  sing N N 196 
ILE CG1 HG12 sing N N 197 
ILE CG1 HG13 sing N N 198 
ILE CG2 HG21 sing N N 199 
ILE CG2 HG22 sing N N 200 
ILE CG2 HG23 sing N N 201 
ILE CD1 HD11 sing N N 202 
ILE CD1 HD12 sing N N 203 
ILE CD1 HD13 sing N N 204 
ILE OXT HXT  sing N N 205 
LEU N   CA   sing N N 206 
LEU N   H    sing N N 207 
LEU N   H2   sing N N 208 
LEU CA  C    sing N N 209 
LEU CA  CB   sing N N 210 
LEU CA  HA   sing N N 211 
LEU C   O    doub N N 212 
LEU C   OXT  sing N N 213 
LEU CB  CG   sing N N 214 
LEU CB  HB2  sing N N 215 
LEU CB  HB3  sing N N 216 
LEU CG  CD1  sing N N 217 
LEU CG  CD2  sing N N 218 
LEU CG  HG   sing N N 219 
LEU CD1 HD11 sing N N 220 
LEU CD1 HD12 sing N N 221 
LEU CD1 HD13 sing N N 222 
LEU CD2 HD21 sing N N 223 
LEU CD2 HD22 sing N N 224 
LEU CD2 HD23 sing N N 225 
LEU OXT HXT  sing N N 226 
LYS N   CA   sing N N 227 
LYS N   H    sing N N 228 
LYS N   H2   sing N N 229 
LYS CA  C    sing N N 230 
LYS CA  CB   sing N N 231 
LYS CA  HA   sing N N 232 
LYS C   O    doub N N 233 
LYS C   OXT  sing N N 234 
LYS CB  CG   sing N N 235 
LYS CB  HB2  sing N N 236 
LYS CB  HB3  sing N N 237 
LYS CG  CD   sing N N 238 
LYS CG  HG2  sing N N 239 
LYS CG  HG3  sing N N 240 
LYS CD  CE   sing N N 241 
LYS CD  HD2  sing N N 242 
LYS CD  HD3  sing N N 243 
LYS CE  NZ   sing N N 244 
LYS CE  HE2  sing N N 245 
LYS CE  HE3  sing N N 246 
LYS NZ  HZ1  sing N N 247 
LYS NZ  HZ2  sing N N 248 
LYS NZ  HZ3  sing N N 249 
LYS OXT HXT  sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
PHE N   CA   sing N N 270 
PHE N   H    sing N N 271 
PHE N   H2   sing N N 272 
PHE CA  C    sing N N 273 
PHE CA  CB   sing N N 274 
PHE CA  HA   sing N N 275 
PHE C   O    doub N N 276 
PHE C   OXT  sing N N 277 
PHE CB  CG   sing N N 278 
PHE CB  HB2  sing N N 279 
PHE CB  HB3  sing N N 280 
PHE CG  CD1  doub Y N 281 
PHE CG  CD2  sing Y N 282 
PHE CD1 CE1  sing Y N 283 
PHE CD1 HD1  sing N N 284 
PHE CD2 CE2  doub Y N 285 
PHE CD2 HD2  sing N N 286 
PHE CE1 CZ   doub Y N 287 
PHE CE1 HE1  sing N N 288 
PHE CE2 CZ   sing Y N 289 
PHE CE2 HE2  sing N N 290 
PHE CZ  HZ   sing N N 291 
PHE OXT HXT  sing N N 292 
PRO N   CA   sing N N 293 
PRO N   CD   sing N N 294 
PRO N   H    sing N N 295 
PRO CA  C    sing N N 296 
PRO CA  CB   sing N N 297 
PRO CA  HA   sing N N 298 
PRO C   O    doub N N 299 
PRO C   OXT  sing N N 300 
PRO CB  CG   sing N N 301 
PRO CB  HB2  sing N N 302 
PRO CB  HB3  sing N N 303 
PRO CG  CD   sing N N 304 
PRO CG  HG2  sing N N 305 
PRO CG  HG3  sing N N 306 
PRO CD  HD2  sing N N 307 
PRO CD  HD3  sing N N 308 
PRO OXT HXT  sing N N 309 
SER N   CA   sing N N 310 
SER N   H    sing N N 311 
SER N   H2   sing N N 312 
SER CA  C    sing N N 313 
SER CA  CB   sing N N 314 
SER CA  HA   sing N N 315 
SER C   O    doub N N 316 
SER C   OXT  sing N N 317 
SER CB  OG   sing N N 318 
SER CB  HB2  sing N N 319 
SER CB  HB3  sing N N 320 
SER OG  HG   sing N N 321 
SER OXT HXT  sing N N 322 
THR N   CA   sing N N 323 
THR N   H    sing N N 324 
THR N   H2   sing N N 325 
THR CA  C    sing N N 326 
THR CA  CB   sing N N 327 
THR CA  HA   sing N N 328 
THR C   O    doub N N 329 
THR C   OXT  sing N N 330 
THR CB  OG1  sing N N 331 
THR CB  CG2  sing N N 332 
THR CB  HB   sing N N 333 
THR OG1 HG1  sing N N 334 
THR CG2 HG21 sing N N 335 
THR CG2 HG22 sing N N 336 
THR CG2 HG23 sing N N 337 
THR OXT HXT  sing N N 338 
TRP N   CA   sing N N 339 
TRP N   H    sing N N 340 
TRP N   H2   sing N N 341 
TRP CA  C    sing N N 342 
TRP CA  CB   sing N N 343 
TRP CA  HA   sing N N 344 
TRP C   O    doub N N 345 
TRP C   OXT  sing N N 346 
TRP CB  CG   sing N N 347 
TRP CB  HB2  sing N N 348 
TRP CB  HB3  sing N N 349 
TRP CG  CD1  doub Y N 350 
TRP CG  CD2  sing Y N 351 
TRP CD1 NE1  sing Y N 352 
TRP CD1 HD1  sing N N 353 
TRP CD2 CE2  doub Y N 354 
TRP CD2 CE3  sing Y N 355 
TRP NE1 CE2  sing Y N 356 
TRP NE1 HE1  sing N N 357 
TRP CE2 CZ2  sing Y N 358 
TRP CE3 CZ3  doub Y N 359 
TRP CE3 HE3  sing N N 360 
TRP CZ2 CH2  doub Y N 361 
TRP CZ2 HZ2  sing N N 362 
TRP CZ3 CH2  sing Y N 363 
TRP CZ3 HZ3  sing N N 364 
TRP CH2 HH2  sing N N 365 
TRP OXT HXT  sing N N 366 
TYR N   CA   sing N N 367 
TYR N   H    sing N N 368 
TYR N   H2   sing N N 369 
TYR CA  C    sing N N 370 
TYR CA  CB   sing N N 371 
TYR CA  HA   sing N N 372 
TYR C   O    doub N N 373 
TYR C   OXT  sing N N 374 
TYR CB  CG   sing N N 375 
TYR CB  HB2  sing N N 376 
TYR CB  HB3  sing N N 377 
TYR CG  CD1  doub Y N 378 
TYR CG  CD2  sing Y N 379 
TYR CD1 CE1  sing Y N 380 
TYR CD1 HD1  sing N N 381 
TYR CD2 CE2  doub Y N 382 
TYR CD2 HD2  sing N N 383 
TYR CE1 CZ   doub Y N 384 
TYR CE1 HE1  sing N N 385 
TYR CE2 CZ   sing Y N 386 
TYR CE2 HE2  sing N N 387 
TYR CZ  OH   sing N N 388 
TYR OH  HH   sing N N 389 
TYR OXT HXT  sing N N 390 
VAL N   CA   sing N N 391 
VAL N   H    sing N N 392 
VAL N   H2   sing N N 393 
VAL CA  C    sing N N 394 
VAL CA  CB   sing N N 395 
VAL CA  HA   sing N N 396 
VAL C   O    doub N N 397 
VAL C   OXT  sing N N 398 
VAL CB  CG1  sing N N 399 
VAL CB  CG2  sing N N 400 
VAL CB  HB   sing N N 401 
VAL CG1 HG11 sing N N 402 
VAL CG1 HG12 sing N N 403 
VAL CG1 HG13 sing N N 404 
VAL CG2 HG21 sing N N 405 
VAL CG2 HG22 sing N N 406 
VAL CG2 HG23 sing N N 407 
VAL OXT HXT  sing N N 408 
# 
_pdbx_audit_support.funding_organization   'Novo Nordisk Foundation' 
_pdbx_audit_support.country                Denmark 
_pdbx_audit_support.grant_number           NNF23OC0085823 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H2D 
_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]   0.021292 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002774 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011049 
_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]   0.014957 
_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 
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   . ALA A 1 1   ? 42.140  -17.455 19.433  1.00 95.58  ? 1471 ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 41.028  -18.220 18.871  1.00 110.19 ? 1471 ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 41.175  -19.715 19.163  1.00 107.07 ? 1471 ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 41.996  -20.394 18.529  1.00 122.96 ? 1471 ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 40.927  -17.979 17.367  1.00 122.25 ? 1471 ALA A CB  1 
ATOM   6    N  N   . PRO A 1 2   ? 40.395  -20.223 20.149  1.00 79.01  ? 1472 PRO A N   1 
ATOM   7    C  CA  . PRO A 1 2   ? 40.449  -21.653 20.484  1.00 78.76  ? 1472 PRO A CA  1 
ATOM   8    C  C   . PRO A 1 2   ? 39.261  -22.433 19.946  1.00 77.37  ? 1472 PRO A C   1 
ATOM   9    O  O   . PRO A 1 2   ? 38.198  -21.859 19.693  1.00 78.10  ? 1472 PRO A O   1 
ATOM   10   C  CB  . PRO A 1 2   ? 40.444  -21.637 22.015  1.00 78.31  ? 1472 PRO A CB  1 
ATOM   11   C  CG  . PRO A 1 2   ? 39.506  -20.504 22.324  1.00 86.45  ? 1472 PRO A CG  1 
ATOM   12   C  CD  . PRO A 1 2   ? 39.691  -19.466 21.198  1.00 91.06  ? 1472 PRO A CD  1 
ATOM   13   N  N   . ALA A 1 3   ? 39.422  -23.741 19.787  1.00 76.60  ? 1473 ALA A N   1 
ATOM   14   C  CA  . ALA A 1 3   ? 38.339  -24.568 19.294  1.00 74.49  ? 1473 ALA A CA  1 
ATOM   15   C  C   . ALA A 1 3   ? 37.370  -24.916 20.413  1.00 72.19  ? 1473 ALA A C   1 
ATOM   16   O  O   . ALA A 1 3   ? 37.733  -25.000 21.590  1.00 72.61  ? 1473 ALA A O   1 
ATOM   17   C  CB  . ALA A 1 3   ? 38.866  -25.849 18.657  1.00 75.82  ? 1473 ALA A CB  1 
ATOM   18   N  N   . ASN A 1 4   ? 36.121  -25.126 20.024  1.00 69.85  ? 1474 ASN A N   1 
ATOM   19   C  CA  . ASN A 1 4   ? 35.048  -25.532 20.929  1.00 69.97  ? 1474 ASN A CA  1 
ATOM   20   C  C   . ASN A 1 4   ? 34.538  -26.893 20.479  1.00 66.83  ? 1474 ASN A C   1 
ATOM   21   O  O   . ASN A 1 4   ? 33.458  -26.990 19.887  1.00 74.76  ? 1474 ASN A O   1 
ATOM   22   C  CB  . ASN A 1 4   ? 33.925  -24.497 20.939  1.00 65.51  ? 1474 ASN A CB  1 
ATOM   23   C  CG  . ASN A 1 4   ? 34.420  -23.132 21.333  1.00 68.64  ? 1474 ASN A CG  1 
ATOM   24   O  OD1 . ASN A 1 4   ? 34.952  -22.386 20.501  1.00 76.23  ? 1474 ASN A OD1 1 
ATOM   25   N  ND2 . ASN A 1 4   ? 34.305  -22.811 22.621  1.00 66.28  ? 1474 ASN A ND2 1 
ATOM   26   N  N   . PRO A 1 5   ? 35.303  -27.963 20.723  1.00 68.47  ? 1475 PRO A N   1 
ATOM   27   C  CA  . PRO A 1 5   ? 34.940  -29.261 20.128  1.00 68.24  ? 1475 PRO A CA  1 
ATOM   28   C  C   . PRO A 1 5   ? 33.549  -29.756 20.506  1.00 65.48  ? 1475 PRO A C   1 
ATOM   29   O  O   . PRO A 1 5   ? 32.940  -30.475 19.707  1.00 64.75  ? 1475 PRO A O   1 
ATOM   30   C  CB  . PRO A 1 5   ? 36.045  -30.213 20.629  1.00 70.23  ? 1475 PRO A CB  1 
ATOM   31   C  CG  . PRO A 1 5   ? 36.840  -29.449 21.631  1.00 74.24  ? 1475 PRO A CG  1 
ATOM   32   C  CD  . PRO A 1 5   ? 36.634  -27.999 21.361  1.00 70.75  ? 1475 PRO A CD  1 
ATOM   33   N  N   . GLN A 1 6   ? 33.015  -29.387 21.670  1.00 64.22  ? 1476 GLN A N   1 
ATOM   34   C  CA  . GLN A 1 6   ? 31.673  -29.826 22.062  1.00 71.32  ? 1476 GLN A CA  1 
ATOM   35   C  C   . GLN A 1 6   ? 30.567  -28.824 21.720  1.00 67.84  ? 1476 GLN A C   1 
ATOM   36   O  O   . GLN A 1 6   ? 29.381  -29.141 21.913  1.00 58.04  ? 1476 GLN A O   1 
ATOM   37   C  CB  . GLN A 1 6   ? 31.645  -30.157 23.558  1.00 75.46  ? 1476 GLN A CB  1 
ATOM   38   C  CG  . GLN A 1 6   ? 32.229  -31.546 23.865  1.00 83.72  ? 1476 GLN A CG  1 
ATOM   39   C  CD  . GLN A 1 6   ? 32.927  -31.618 25.216  1.00 85.40  ? 1476 GLN A CD  1 
ATOM   40   O  OE1 . GLN A 1 6   ? 33.746  -30.758 25.555  1.00 68.70  ? 1476 GLN A OE1 1 
ATOM   41   N  NE2 . GLN A 1 6   ? 32.598  -32.651 25.998  1.00 86.22  ? 1476 GLN A NE2 1 
ATOM   42   N  N   . ASN A 1 7   ? 30.922  -27.639 21.201  1.00 60.41  ? 1477 ASN A N   1 
ATOM   43   C  CA  . ASN A 1 7   ? 29.986  -26.634 20.694  1.00 58.86  ? 1477 ASN A CA  1 
ATOM   44   C  C   . ASN A 1 7   ? 29.199  -25.939 21.793  1.00 57.37  ? 1477 ASN A C   1 
ATOM   45   O  O   . ASN A 1 7   ? 28.102  -25.451 21.540  1.00 55.71  ? 1477 ASN A O   1 
ATOM   46   C  CB  . ASN A 1 7   ? 29.003  -27.230 19.683  1.00 58.34  ? 1477 ASN A CB  1 
ATOM   47   C  CG  . ASN A 1 7   ? 29.629  -27.480 18.342  1.00 63.35  ? 1477 ASN A CG  1 
ATOM   48   O  OD1 . ASN A 1 7   ? 30.643  -26.867 17.995  1.00 60.67  ? 1477 ASN A OD1 1 
ATOM   49   N  ND2 . ASN A 1 7   ? 29.017  -28.374 17.561  1.00 58.31  ? 1477 ASN A ND2 1 
ATOM   50   N  N   . PHE A 1 8   ? 29.734  -25.902 23.016  1.00 65.60  ? 1478 PHE A N   1 
ATOM   51   C  CA  . PHE A 1 8   ? 29.072  -25.207 24.119  1.00 62.44  ? 1478 PHE A CA  1 
ATOM   52   C  C   . PHE A 1 8   ? 28.655  -23.785 23.735  1.00 56.32  ? 1478 PHE A C   1 
ATOM   53   O  O   . PHE A 1 8   ? 27.522  -23.370 23.995  1.00 54.71  ? 1478 PHE A O   1 
ATOM   54   C  CB  . PHE A 1 8   ? 30.002  -25.196 25.342  1.00 62.79  ? 1478 PHE A CB  1 
ATOM   55   C  CG  . PHE A 1 8   ? 30.252  -26.566 25.933  1.00 67.91  ? 1478 PHE A CG  1 
ATOM   56   C  CD1 . PHE A 1 8   ? 31.347  -26.800 26.740  1.00 64.73  ? 1478 PHE A CD1 1 
ATOM   57   C  CD2 . PHE A 1 8   ? 29.376  -27.616 25.692  1.00 80.13  ? 1478 PHE A CD2 1 
ATOM   58   C  CE1 . PHE A 1 8   ? 31.574  -28.060 27.283  1.00 78.10  ? 1478 PHE A CE1 1 
ATOM   59   C  CE2 . PHE A 1 8   ? 29.602  -28.875 26.229  1.00 72.84  ? 1478 PHE A CE2 1 
ATOM   60   C  CZ  . PHE A 1 8   ? 30.696  -29.094 27.024  1.00 76.63  ? 1478 PHE A CZ  1 
ATOM   61   N  N   . ASN A 1 9   ? 29.563  -23.027 23.104  1.00 57.83  ? 1479 ASN A N   1 
ATOM   62   C  CA  . ASN A 1 9   ? 29.265  -21.638 22.768  1.00 57.58  ? 1479 ASN A CA  1 
ATOM   63   C  C   . ASN A 1 9   ? 28.104  -21.547 21.792  1.00 55.96  ? 1479 ASN A C   1 
ATOM   64   O  O   . ASN A 1 9   ? 27.194  -20.730 21.976  1.00 63.36  ? 1479 ASN A O   1 
ATOM   65   C  CB  . ASN A 1 9   ? 30.513  -20.935 22.209  1.00 61.37  ? 1479 ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 9   ? 31.184  -21.699 21.057  1.00 63.72  ? 1479 ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 9   ? 30.994  -22.906 20.878  1.00 64.17  ? 1479 ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 9   ? 31.974  -20.981 20.270  1.00 62.62  ? 1479 ASN A ND2 1 
ATOM   69   N  N   . ILE A 1 10  ? 28.093  -22.410 20.777  1.00 56.01  ? 1480 ILE A N   1 
ATOM   70   C  CA  . ILE A 1 10  ? 27.046  -22.368 19.762  1.00 54.68  ? 1480 ILE A CA  1 
ATOM   71   C  C   . ILE A 1 10  ? 25.682  -22.613 20.396  1.00 54.93  ? 1480 ILE A C   1 
ATOM   72   O  O   . ILE A 1 10  ? 24.715  -21.880 20.156  1.00 54.80  ? 1480 ILE A O   1 
ATOM   73   C  CB  . ILE A 1 10  ? 27.337  -23.397 18.655  1.00 55.28  ? 1480 ILE A CB  1 
ATOM   74   C  CG1 . ILE A 1 10  ? 28.709  -23.148 18.020  1.00 68.92  ? 1480 ILE A CG1 1 
ATOM   75   C  CG2 . ILE A 1 10  ? 26.224  -23.397 17.605  1.00 53.96  ? 1480 ILE A CG2 1 
ATOM   76   C  CD1 . ILE A 1 10  ? 28.762  -21.980 17.061  1.00 58.19  ? 1480 ILE A CD1 1 
ATOM   77   N  N   . TYR A 1 11  ? 25.580  -23.667 21.198  1.00 65.60  ? 1481 TYR A N   1 
ATOM   78   C  CA  . TYR A 1 11  ? 24.282  -24.034 21.741  1.00 61.55  ? 1481 TYR A CA  1 
ATOM   79   C  C   . TYR A 1 11  ? 23.807  -23.016 22.762  1.00 52.54  ? 1481 TYR A C   1 
ATOM   80   O  O   . TYR A 1 11  ? 22.622  -22.673 22.793  1.00 48.20  ? 1481 TYR A O   1 
ATOM   81   C  CB  . TYR A 1 11  ? 24.354  -25.429 22.339  1.00 50.30  ? 1481 TYR A CB  1 
ATOM   82   C  CG  . TYR A 1 11  ? 24.396  -26.495 21.282  1.00 51.43  ? 1481 TYR A CG  1 
ATOM   83   C  CD1 . TYR A 1 11  ? 23.330  -26.671 20.418  1.00 49.25  ? 1481 TYR A CD1 1 
ATOM   84   C  CD2 . TYR A 1 11  ? 25.491  -27.346 21.158  1.00 52.09  ? 1481 TYR A CD2 1 
ATOM   85   C  CE1 . TYR A 1 11  ? 23.347  -27.654 19.447  1.00 49.87  ? 1481 TYR A CE1 1 
ATOM   86   C  CE2 . TYR A 1 11  ? 25.520  -28.341 20.184  1.00 52.41  ? 1481 TYR A CE2 1 
ATOM   87   C  CZ  . TYR A 1 11  ? 24.449  -28.496 19.334  1.00 51.64  ? 1481 TYR A CZ  1 
ATOM   88   O  OH  . TYR A 1 11  ? 24.452  -29.478 18.370  1.00 51.50  ? 1481 TYR A OH  1 
ATOM   89   N  N   . LYS A 1 12  ? 24.721  -22.509 23.597  1.00 59.21  ? 1482 LYS A N   1 
ATOM   90   C  CA  . LYS A 1 12  ? 24.337  -21.460 24.532  1.00 56.09  ? 1482 LYS A CA  1 
ATOM   91   C  C   . LYS A 1 12  ? 23.812  -20.245 23.776  1.00 53.10  ? 1482 LYS A C   1 
ATOM   92   O  O   . LYS A 1 12  ? 22.796  -19.651 24.160  1.00 48.91  ? 1482 LYS A O   1 
ATOM   93   C  CB  . LYS A 1 12  ? 25.530  -21.084 25.416  1.00 52.08  ? 1482 LYS A CB  1 
ATOM   94   C  CG  . LYS A 1 12  ? 25.200  -20.088 26.535  1.00 75.23  ? 1482 LYS A CG  1 
ATOM   95   C  CD  . LYS A 1 12  ? 26.165  -20.214 27.735  1.00 86.59  ? 1482 LYS A CD  1 
ATOM   96   C  CE  . LYS A 1 12  ? 25.933  -19.112 28.801  1.00 86.64  ? 1482 LYS A CE  1 
ATOM   97   N  NZ  . LYS A 1 12  ? 27.138  -18.834 29.687  1.00 70.08  ? 1482 LYS A NZ  1 
ATOM   98   N  N   A ARG A 1 13  ? 24.479  -19.893 22.670  0.47 52.37  ? 1483 ARG A N   1 
ATOM   99   N  N   B ARG A 1 13  ? 24.475  -19.870 22.685  0.53 51.96  ? 1483 ARG A N   1 
ATOM   100  C  CA  A ARG A 1 13  ? 24.078  -18.743 21.868  0.47 55.04  ? 1483 ARG A CA  1 
ATOM   101  C  CA  B ARG A 1 13  ? 24.065  -18.669 21.973  0.53 55.27  ? 1483 ARG A CA  1 
ATOM   102  C  C   A ARG A 1 13  ? 22.685  -18.934 21.285  0.47 53.49  ? 1483 ARG A C   1 
ATOM   103  C  C   B ARG A 1 13  ? 22.696  -18.841 21.329  0.53 54.27  ? 1483 ARG A C   1 
ATOM   104  O  O   A ARG A 1 13  ? 21.858  -18.016 21.318  0.47 48.56  ? 1483 ARG A O   1 
ATOM   105  O  O   B ARG A 1 13  ? 21.890  -17.907 21.325  0.53 49.29  ? 1483 ARG A O   1 
ATOM   106  C  CB  A ARG A 1 13  ? 25.102  -18.507 20.752  0.47 53.15  ? 1483 ARG A CB  1 
ATOM   107  C  CB  B ARG A 1 13  ? 25.113  -18.294 20.932  0.53 52.93  ? 1483 ARG A CB  1 
ATOM   108  C  CG  A ARG A 1 13  ? 24.984  -17.165 20.042  0.47 61.15  ? 1483 ARG A CG  1 
ATOM   109  C  CG  B ARG A 1 13  ? 26.307  -17.578 21.521  0.53 60.54  ? 1483 ARG A CG  1 
ATOM   110  C  CD  A ARG A 1 13  ? 26.316  -16.782 19.393  0.47 78.88  ? 1483 ARG A CD  1 
ATOM   111  C  CD  B ARG A 1 13  ? 26.938  -16.683 20.469  0.53 78.72  ? 1483 ARG A CD  1 
ATOM   112  N  NE  A ARG A 1 13  ? 27.423  -16.897 20.345  0.47 78.63  ? 1483 ARG A NE  1 
ATOM   113  N  NE  B ARG A 1 13  ? 26.619  -17.187 19.138  0.53 80.64  ? 1483 ARG A NE  1 
ATOM   114  C  CZ  A ARG A 1 13  ? 28.693  -17.123 20.019  0.47 76.40  ? 1483 ARG A CZ  1 
ATOM   115  C  CZ  B ARG A 1 13  ? 27.418  -17.966 18.419  0.53 75.04  ? 1483 ARG A CZ  1 
ATOM   116  N  NH1 A ARG A 1 13  ? 29.053  -17.264 18.749  0.47 84.23  ? 1483 ARG A NH1 1 
ATOM   117  N  NH1 B ARG A 1 13  ? 27.025  -18.385 17.228  0.53 56.79  ? 1483 ARG A NH1 1 
ATOM   118  N  NH2 A ARG A 1 13  ? 29.607  -17.215 20.975  0.47 60.41  ? 1483 ARG A NH2 1 
ATOM   119  N  NH2 B ARG A 1 13  ? 28.609  -18.318 18.888  0.53 83.68  ? 1483 ARG A NH2 1 
ATOM   120  N  N   A ILE A 1 14  ? 22.415  -20.103 20.708  0.47 48.69  ? 1484 ILE A N   1 
ATOM   121  N  N   B ILE A 1 14  ? 22.416  -20.012 20.764  0.53 48.71  ? 1484 ILE A N   1 
ATOM   122  C  CA  A ILE A 1 14  ? 21.112  -20.284 20.077  0.47 49.64  ? 1484 ILE A CA  1 
ATOM   123  C  CA  B ILE A 1 14  ? 21.126  -20.178 20.108  0.53 49.57  ? 1484 ILE A CA  1 
ATOM   124  C  C   A ILE A 1 14  ? 20.005  -20.296 21.127  0.47 53.38  ? 1484 ILE A C   1 
ATOM   125  C  C   B ILE A 1 14  ? 20.007  -20.262 21.143  0.53 53.87  ? 1484 ILE A C   1 
ATOM   126  O  O   A ILE A 1 14  ? 18.925  -19.742 20.900  0.47 49.45  ? 1484 ILE A O   1 
ATOM   127  O  O   B ILE A 1 14  ? 18.918  -19.723 20.925  0.53 49.48  ? 1484 ILE A O   1 
ATOM   128  C  CB  A ILE A 1 14  ? 21.081  -21.545 19.197  0.47 52.32  ? 1484 ILE A CB  1 
ATOM   129  C  CB  B ILE A 1 14  ? 21.137  -21.383 19.155  0.53 52.62  ? 1484 ILE A CB  1 
ATOM   130  C  CG1 A ILE A 1 14  ? 21.029  -22.812 20.050  0.47 46.63  ? 1484 ILE A CG1 1 
ATOM   131  C  CG1 B ILE A 1 14  ? 21.793  -20.982 17.838  0.53 59.56  ? 1484 ILE A CG1 1 
ATOM   132  C  CG2 A ILE A 1 14  ? 22.271  -21.561 18.245  0.47 56.81  ? 1484 ILE A CG2 1 
ATOM   133  C  CG2 B ILE A 1 14  ? 19.731  -21.837 18.843  0.53 45.56  ? 1484 ILE A CG2 1 
ATOM   134  C  CD1 A ILE A 1 14  ? 20.051  -23.833 19.529  0.47 57.97  ? 1484 ILE A CD1 1 
ATOM   135  C  CD1 B ILE A 1 14  ? 23.072  -21.704 17.538  0.53 62.25  ? 1484 ILE A CD1 1 
ATOM   136  N  N   . PHE A 1 15  ? 20.265  -20.881 22.303  1.00 49.90  ? 1485 PHE A N   1 
ATOM   137  C  CA  . PHE A 1 15  ? 19.310  -20.775 23.407  1.00 50.44  ? 1485 PHE A CA  1 
ATOM   138  C  C   . PHE A 1 15  ? 19.011  -19.306 23.721  1.00 44.77  ? 1485 PHE A C   1 
ATOM   139  O  O   . PHE A 1 15  ? 17.847  -18.878 23.731  1.00 51.73  ? 1485 PHE A O   1 
ATOM   140  C  CB  . PHE A 1 15  ? 19.846  -21.489 24.654  1.00 45.14  ? 1485 PHE A CB  1 
ATOM   141  C  CG  . PHE A 1 15  ? 18.977  -21.314 25.889  1.00 44.33  ? 1485 PHE A CG  1 
ATOM   142  C  CD1 . PHE A 1 15  ? 17.909  -22.160 26.133  1.00 48.49  ? 1485 PHE A CD1 1 
ATOM   143  C  CD2 . PHE A 1 15  ? 19.251  -20.322 26.812  1.00 47.64  ? 1485 PHE A CD2 1 
ATOM   144  C  CE1 . PHE A 1 15  ? 17.124  -22.004 27.274  1.00 53.77  ? 1485 PHE A CE1 1 
ATOM   145  C  CE2 . PHE A 1 15  ? 18.491  -20.152 27.941  1.00 44.33  ? 1485 PHE A CE2 1 
ATOM   146  C  CZ  . PHE A 1 15  ? 17.414  -20.982 28.182  1.00 45.93  ? 1485 PHE A CZ  1 
ATOM   147  N  N   . THR A 1 16  ? 20.064  -18.523 23.970  1.00 48.19  ? 1486 THR A N   1 
ATOM   148  C  CA  . THR A 1 16  ? 19.896  -17.115 24.327  1.00 51.76  ? 1486 THR A CA  1 
ATOM   149  C  C   . THR A 1 16  ? 19.107  -16.363 23.264  1.00 57.72  ? 1486 THR A C   1 
ATOM   150  O  O   . THR A 1 16  ? 18.123  -15.681 23.565  1.00 60.95  ? 1486 THR A O   1 
ATOM   151  C  CB  . THR A 1 16  ? 21.260  -16.469 24.504  1.00 61.80  ? 1486 THR A CB  1 
ATOM   152  O  OG1 . THR A 1 16  ? 22.030  -17.208 25.463  1.00 65.33  ? 1486 THR A OG1 1 
ATOM   153  C  CG2 . THR A 1 16  ? 21.121  -15.008 24.941  1.00 61.60  ? 1486 THR A CG2 1 
ATOM   154  N  N   . ASP A 1 17  ? 19.506  -16.500 22.008  1.00 46.41  ? 1487 ASP A N   1 
ATOM   155  C  CA  . ASP A 1 17  ? 18.791  -15.837 20.930  1.00 47.90  ? 1487 ASP A CA  1 
ATOM   156  C  C   . ASP A 1 17  ? 17.334  -16.263 20.891  1.00 54.45  ? 1487 ASP A C   1 
ATOM   157  O  O   . ASP A 1 17  ? 16.440  -15.432 20.705  1.00 47.94  ? 1487 ASP A O   1 
ATOM   158  C  CB  . ASP A 1 17  ? 19.483  -16.125 19.601  1.00 51.12  ? 1487 ASP A CB  1 
ATOM   159  C  CG  . ASP A 1 17  ? 20.808  -15.354 19.452  1.00 63.77  ? 1487 ASP A CG  1 
ATOM   160  O  OD1 . ASP A 1 17  ? 21.011  -14.360 20.190  1.00 69.24  ? 1487 ASP A OD1 1 
ATOM   161  O  OD2 . ASP A 1 17  ? 21.653  -15.756 18.620  1.00 72.47  ? 1487 ASP A OD2 1 
ATOM   162  N  N   . MET A 1 18  ? 17.071  -17.561 21.053  1.00 58.49  ? 1488 MET A N   1 
ATOM   163  C  CA  . MET A 1 18  ? 15.718  -18.046 20.910  1.00 42.25  ? 1488 MET A CA  1 
ATOM   164  C  C   . MET A 1 18  ? 14.816  -17.486 22.003  1.00 49.01  ? 1488 MET A C   1 
ATOM   165  O  O   . MET A 1 18  ? 13.672  -17.118 21.739  1.00 40.84  ? 1488 MET A O   1 
ATOM   166  C  CB  . MET A 1 18  ? 15.704  -19.576 20.915  1.00 51.09  ? 1488 MET A CB  1 
ATOM   167  C  CG  . MET A 1 18  ? 14.292  -20.129 20.821  1.00 50.23  ? 1488 MET A CG  1 
ATOM   168  S  SD  . MET A 1 18  ? 13.427  -19.701 19.281  1.00 58.15  ? 1488 MET A SD  1 
ATOM   169  C  CE  . MET A 1 18  ? 11.767  -20.300 19.683  1.00 53.85  ? 1488 MET A CE  1 
ATOM   170  N  N   . VAL A 1 19  ? 15.301  -17.431 23.243  1.00 47.96  ? 1489 VAL A N   1 
ATOM   171  C  CA  . VAL A 1 19  ? 14.417  -16.983 24.317  1.00 44.47  ? 1489 VAL A CA  1 
ATOM   172  C  C   . VAL A 1 19  ? 14.275  -15.470 24.368  1.00 56.35  ? 1489 VAL A C   1 
ATOM   173  O  O   . VAL A 1 19  ? 13.373  -14.955 25.055  1.00 43.46  ? 1489 VAL A O   1 
ATOM   174  C  CB  . VAL A 1 19  ? 14.930  -17.458 25.685  1.00 46.30  ? 1489 VAL A CB  1 
ATOM   175  C  CG1 . VAL A 1 19  ? 14.971  -18.974 25.728  1.00 42.88  ? 1489 VAL A CG1 1 
ATOM   176  C  CG2 . VAL A 1 19  ? 16.340  -16.865 25.936  1.00 47.37  ? 1489 VAL A CG2 1 
ATOM   177  N  N   . SER A 1 20  ? 15.127  -14.736 23.654  1.00 43.00  ? 1490 SER A N   1 
ATOM   178  C  CA  . SER A 1 20  ? 14.945  -13.304 23.489  1.00 53.34  ? 1490 SER A CA  1 
ATOM   179  C  C   . SER A 1 20  ? 14.298  -12.949 22.155  1.00 52.73  ? 1490 SER A C   1 
ATOM   180  O  O   . SER A 1 20  ? 14.161  -11.764 21.849  1.00 58.25  ? 1490 SER A O   1 
ATOM   181  C  CB  . SER A 1 20  ? 16.284  -12.575 23.639  1.00 49.74  ? 1490 SER A CB  1 
ATOM   182  O  OG  . SER A 1 20  ? 17.085  -12.831 22.509  1.00 58.46  ? 1490 SER A OG  1 
ATOM   183  N  N   . SER A 1 21  ? 13.900  -13.942 21.353  1.00 56.28  ? 1491 SER A N   1 
ATOM   184  C  CA  . SER A 1 21  ? 13.332  -13.640 20.048  1.00 51.19  ? 1491 SER A CA  1 
ATOM   185  C  C   . SER A 1 21  ? 11.845  -13.288 20.188  1.00 53.94  ? 1491 SER A C   1 
ATOM   186  O  O   . SER A 1 21  ? 11.195  -13.674 21.169  1.00 49.50  ? 1491 SER A O   1 
ATOM   187  C  CB  . SER A 1 21  ? 13.522  -14.818 19.087  1.00 42.20  ? 1491 SER A CB  1 
ATOM   188  O  OG  . SER A 1 21  ? 13.008  -16.043 19.611  1.00 56.06  ? 1491 SER A OG  1 
ATOM   189  N  N   . PRO A 1 22  ? 11.308  -12.483 19.271  1.00 55.18  ? 1492 PRO A N   1 
ATOM   190  C  CA  . PRO A 1 22  ? 9.895   -12.098 19.356  1.00 48.20  ? 1492 PRO A CA  1 
ATOM   191  C  C   . PRO A 1 22  ? 8.966   -13.159 18.791  1.00 59.04  ? 1492 PRO A C   1 
ATOM   192  O  O   . PRO A 1 22  ? 9.371   -14.053 18.044  1.00 53.93  ? 1492 PRO A O   1 
ATOM   193  C  CB  . PRO A 1 22  ? 9.827   -10.813 18.521  1.00 64.74  ? 1492 PRO A CB  1 
ATOM   194  C  CG  . PRO A 1 22  ? 10.900  -10.987 17.504  1.00 66.48  ? 1492 PRO A CG  1 
ATOM   195  C  CD  . PRO A 1 22  ? 12.013  -11.750 18.199  1.00 60.13  ? 1492 PRO A CD  1 
ATOM   196  N  N   . GLY A 1 23  ? 7.690   -13.028 19.159  1.00 59.64  ? 1493 GLY A N   1 
ATOM   197  C  CA  . GLY A 1 23  ? 6.648   -13.851 18.576  1.00 57.70  ? 1493 GLY A CA  1 
ATOM   198  C  C   . GLY A 1 23  ? 6.687   -15.293 19.015  1.00 59.90  ? 1493 GLY A C   1 
ATOM   199  O  O   . GLY A 1 23  ? 6.308   -16.181 18.244  1.00 71.84  ? 1493 GLY A O   1 
ATOM   200  N  N   . THR A 1 24  ? 7.159   -15.556 20.228  1.00 48.01  ? 1494 THR A N   1 
ATOM   201  C  CA  . THR A 1 24  ? 7.355   -16.924 20.687  1.00 44.95  ? 1494 THR A CA  1 
ATOM   202  C  C   . THR A 1 24  ? 6.329   -17.360 21.720  1.00 46.20  ? 1494 THR A C   1 
ATOM   203  O  O   . THR A 1 24  ? 6.365   -18.525 22.146  1.00 40.68  ? 1494 THR A O   1 
ATOM   204  C  CB  . THR A 1 24  ? 8.777   -17.102 21.246  1.00 47.01  ? 1494 THR A CB  1 
ATOM   205  O  OG1 . THR A 1 24  ? 9.023   -16.148 22.300  1.00 48.96  ? 1494 THR A OG1 1 
ATOM   206  C  CG2 . THR A 1 24  ? 9.822   -16.931 20.125  1.00 42.42  ? 1494 THR A CG2 1 
ATOM   207  N  N   . ASN A 1 25  ? 5.422   -16.466 22.136  1.00 39.30  ? 1495 ASN A N   1 
ATOM   208  C  CA  . ASN A 1 25  ? 4.385   -16.791 23.122  1.00 52.13  ? 1495 ASN A CA  1 
ATOM   209  C  C   . ASN A 1 25  ? 3.063   -17.147 22.438  1.00 53.68  ? 1495 ASN A C   1 
ATOM   210  O  O   . ASN A 1 25  ? 2.047   -16.494 22.665  1.00 55.94  ? 1495 ASN A O   1 
ATOM   211  C  CB  . ASN A 1 25  ? 4.184   -15.618 24.085  1.00 37.52  ? 1495 ASN A CB  1 
ATOM   212  C  CG  . ASN A 1 25  ? 3.204   -15.924 25.203  1.00 44.06  ? 1495 ASN A CG  1 
ATOM   213  O  OD1 . ASN A 1 25  ? 3.174   -17.028 25.740  1.00 46.72  ? 1495 ASN A OD1 1 
ATOM   214  N  ND2 . ASN A 1 25  ? 2.363   -14.945 25.537  1.00 51.23  ? 1495 ASN A ND2 1 
ATOM   215  N  N   . CYS A 1 26  ? 3.075   -18.157 21.566  1.00 58.09  ? 1496 CYS A N   1 
ATOM   216  C  CA  . CYS A 1 26  ? 1.840   -18.615 20.924  1.00 52.70  ? 1496 CYS A CA  1 
ATOM   217  C  C   . CYS A 1 26  ? 2.022   -20.081 20.558  1.00 49.68  ? 1496 CYS A C   1 
ATOM   218  O  O   . CYS A 1 26  ? 3.152   -20.580 20.496  1.00 47.27  ? 1496 CYS A O   1 
ATOM   219  C  CB  . CYS A 1 26  ? 1.486   -17.848 19.646  1.00 44.38  ? 1496 CYS A CB  1 
ATOM   220  S  SG  . CYS A 1 26  ? 2.866   -17.721 18.512  1.00 57.22  ? 1496 CYS A SG  1 
ATOM   221  N  N   . ALA A 1 27  ? 0.893   -20.764 20.312  1.00 33.84  ? 1497 ALA A N   1 
ATOM   222  C  CA  . ALA A 1 27  ? 0.921   -22.169 19.892  1.00 37.58  ? 1497 ALA A CA  1 
ATOM   223  C  C   . ALA A 1 27  ? 1.757   -22.362 18.635  1.00 40.55  ? 1497 ALA A C   1 
ATOM   224  O  O   . ALA A 1 27  ? 2.486   -23.350 18.506  1.00 42.90  ? 1497 ALA A O   1 
ATOM   225  C  CB  . ALA A 1 27  ? -0.505  -22.684 19.656  1.00 45.32  ? 1497 ALA A CB  1 
ATOM   226  N  N   . GLU A 1 28  ? 1.680   -21.408 17.709  1.00 45.77  ? 1498 GLU A N   1 
ATOM   227  C  CA  . GLU A 1 28  ? 2.351   -21.532 16.424  1.00 50.09  ? 1498 GLU A CA  1 
ATOM   228  C  C   . GLU A 1 28  ? 3.866   -21.593 16.565  1.00 58.07  ? 1498 GLU A C   1 
ATOM   229  O  O   . GLU A 1 28  ? 4.552   -21.991 15.619  1.00 45.49  ? 1498 GLU A O   1 
ATOM   230  C  CB  . GLU A 1 28  ? 1.967   -20.344 15.529  1.00 65.71  ? 1498 GLU A CB  1 
ATOM   231  C  CG  . GLU A 1 28  ? 0.478   -20.300 15.118  1.00 84.78  ? 1498 GLU A CG  1 
ATOM   232  C  CD  . GLU A 1 28  ? -0.460  -19.814 16.230  1.00 82.76  ? 1498 GLU A CD  1 
ATOM   233  O  OE1 . GLU A 1 28  ? 0.021   -19.241 17.226  1.00 86.56  ? 1498 GLU A OE1 1 
ATOM   234  O  OE2 . GLU A 1 28  ? -1.688  -20.014 16.107  1.00 92.32  ? 1498 GLU A OE2 1 
ATOM   235  N  N   . ALA A 1 29  ? 4.401   -21.219 17.719  1.00 49.67  ? 1499 ALA A N   1 
ATOM   236  C  CA  . ALA A 1 29  ? 5.836   -21.279 17.928  1.00 54.90  ? 1499 ALA A CA  1 
ATOM   237  C  C   . ALA A 1 29  ? 6.319   -22.660 18.353  1.00 46.50  ? 1499 ALA A C   1 
ATOM   238  O  O   . ALA A 1 29  ? 7.534   -22.825 18.526  1.00 51.82  ? 1499 ALA A O   1 
ATOM   239  C  CB  . ALA A 1 29  ? 6.259   -20.232 18.971  1.00 45.70  ? 1499 ALA A CB  1 
ATOM   240  N  N   . TYR A 1 30  ? 5.413   -23.645 18.476  1.00 45.46  ? 1500 TYR A N   1 
ATOM   241  C  CA  . TYR A 1 30  ? 5.763   -24.921 19.097  1.00 45.48  ? 1500 TYR A CA  1 
ATOM   242  C  C   . TYR A 1 30  ? 7.031   -25.516 18.496  1.00 38.57  ? 1500 TYR A C   1 
ATOM   243  O  O   . TYR A 1 30  ? 7.980   -25.829 19.219  1.00 48.65  ? 1500 TYR A O   1 
ATOM   244  C  CB  . TYR A 1 30  ? 4.613   -25.938 18.985  1.00 40.63  ? 1500 TYR A CB  1 
ATOM   245  C  CG  . TYR A 1 30  ? 5.061   -27.279 19.522  1.00 44.15  ? 1500 TYR A CG  1 
ATOM   246  C  CD1 . TYR A 1 30  ? 5.152   -27.494 20.893  1.00 38.50  ? 1500 TYR A CD1 1 
ATOM   247  C  CD2 . TYR A 1 30  ? 5.481   -28.303 18.664  1.00 34.74  ? 1500 TYR A CD2 1 
ATOM   248  C  CE1 . TYR A 1 30  ? 5.629   -28.688 21.385  1.00 41.57  ? 1500 TYR A CE1 1 
ATOM   249  C  CE2 . TYR A 1 30  ? 5.942   -29.515 19.159  1.00 36.39  ? 1500 TYR A CE2 1 
ATOM   250  C  CZ  . TYR A 1 30  ? 6.018   -29.691 20.517  1.00 37.94  ? 1500 TYR A CZ  1 
ATOM   251  O  OH  . TYR A 1 30  ? 6.473   -30.862 21.026  1.00 37.71  ? 1500 TYR A OH  1 
ATOM   252  N  N   . HIS A 1 31  ? 7.086   -25.616 17.167  1.00 39.23  ? 1501 HIS A N   1 
ATOM   253  C  CA  . HIS A 1 31  ? 8.170   -26.348 16.521  1.00 53.48  ? 1501 HIS A CA  1 
ATOM   254  C  C   . HIS A 1 31  ? 9.510   -25.661 16.688  1.00 54.93  ? 1501 HIS A C   1 
ATOM   255  O  O   . HIS A 1 31  ? 10.534  -26.344 16.680  1.00 42.99  ? 1501 HIS A O   1 
ATOM   256  C  CB  . HIS A 1 31  ? 7.859   -26.540 15.037  1.00 53.51  ? 1501 HIS A CB  1 
ATOM   257  C  CG  . HIS A 1 31  ? 6.744   -27.510 14.791  1.00 68.64  ? 1501 HIS A CG  1 
ATOM   258  N  ND1 . HIS A 1 31  ? 6.932   -28.878 14.782  1.00 60.83  ? 1501 HIS A ND1 1 
ATOM   259  C  CD2 . HIS A 1 31  ? 5.416   -27.309 14.596  1.00 61.99  ? 1501 HIS A CD2 1 
ATOM   260  C  CE1 . HIS A 1 31  ? 5.771   -29.476 14.564  1.00 73.00  ? 1501 HIS A CE1 1 
ATOM   261  N  NE2 . HIS A 1 31  ? 4.836   -28.547 14.444  1.00 60.08  ? 1501 HIS A NE2 1 
ATOM   262  N  N   . SER A 1 32  ? 9.524   -24.345 16.918  1.00 42.48  ? 1502 SER A N   1 
ATOM   263  C  CA  . SER A 1 32  ? 10.794  -23.693 17.162  1.00 49.52  ? 1502 SER A CA  1 
ATOM   264  C  C   . SER A 1 32  ? 11.283  -24.012 18.558  1.00 46.74  ? 1502 SER A C   1 
ATOM   265  O  O   . SER A 1 32  ? 12.467  -24.293 18.758  1.00 41.26  ? 1502 SER A O   1 
ATOM   266  C  CB  . SER A 1 32  ? 10.654  -22.177 16.976  1.00 56.64  ? 1502 SER A CB  1 
ATOM   267  O  OG  . SER A 1 32  ? 10.325  -21.858 15.634  1.00 60.44  ? 1502 SER A OG  1 
ATOM   268  N  N   . TRP A 1 33  ? 10.369  -24.064 19.517  1.00 36.98  ? 1503 TRP A N   1 
ATOM   269  C  CA  . TRP A 1 33  ? 10.752  -24.439 20.873  1.00 45.17  ? 1503 TRP A CA  1 
ATOM   270  C  C   . TRP A 1 33  ? 11.138  -25.919 20.934  1.00 37.28  ? 1503 TRP A C   1 
ATOM   271  O  O   . TRP A 1 33  ? 12.194  -26.280 21.469  1.00 45.21  ? 1503 TRP A O   1 
ATOM   272  C  CB  . TRP A 1 33  ? 9.591   -24.139 21.837  1.00 38.10  ? 1503 TRP A CB  1 
ATOM   273  C  CG  . TRP A 1 33  ? 9.343   -22.666 22.171  1.00 55.58  ? 1503 TRP A CG  1 
ATOM   274  C  CD1 . TRP A 1 33  ? 8.168   -21.970 22.018  1.00 46.94  ? 1503 TRP A CD1 1 
ATOM   275  C  CD2 . TRP A 1 33  ? 10.274  -21.741 22.763  1.00 54.23  ? 1503 TRP A CD2 1 
ATOM   276  N  NE1 . TRP A 1 33  ? 8.316   -20.675 22.476  1.00 40.24  ? 1503 TRP A NE1 1 
ATOM   277  C  CE2 . TRP A 1 33  ? 9.594   -20.510 22.937  1.00 54.94  ? 1503 TRP A CE2 1 
ATOM   278  C  CE3 . TRP A 1 33  ? 11.606  -21.836 23.166  1.00 50.00  ? 1503 TRP A CE3 1 
ATOM   279  C  CZ2 . TRP A 1 33  ? 10.211  -19.390 23.484  1.00 44.02  ? 1503 TRP A CZ2 1 
ATOM   280  C  CZ3 . TRP A 1 33  ? 12.213  -20.727 23.712  1.00 50.38  ? 1503 TRP A CZ3 1 
ATOM   281  C  CH2 . TRP A 1 33  ? 11.512  -19.519 23.868  1.00 40.77  ? 1503 TRP A CH2 1 
ATOM   282  N  N   . ALA A 1 34  ? 10.313  -26.782 20.333  1.00 44.25  ? 1504 ALA A N   1 
ATOM   283  C  CA  . ALA A 1 34  ? 10.594  -28.212 20.321  1.00 47.45  ? 1504 ALA A CA  1 
ATOM   284  C  C   . ALA A 1 34  ? 11.969  -28.485 19.712  1.00 47.93  ? 1504 ALA A C   1 
ATOM   285  O  O   . ALA A 1 34  ? 12.789  -29.198 20.305  1.00 50.38  ? 1504 ALA A O   1 
ATOM   286  C  CB  . ALA A 1 34  ? 9.483   -28.952 19.571  1.00 36.54  ? 1504 ALA A CB  1 
ATOM   287  N  N   . ASP A 1 35  ? 12.256  -27.852 18.564  1.00 48.61  ? 1505 ASP A N   1 
ATOM   288  C  CA  . ASP A 1 35  ? 13.577  -27.918 17.939  1.00 50.03  ? 1505 ASP A CA  1 
ATOM   289  C  C   . ASP A 1 35  ? 14.682  -27.550 18.919  1.00 58.42  ? 1505 ASP A C   1 
ATOM   290  O  O   . ASP A 1 35  ? 15.643  -28.310 19.099  1.00 51.73  ? 1505 ASP A O   1 
ATOM   291  C  CB  . ASP A 1 35  ? 13.656  -26.987 16.720  1.00 41.55  ? 1505 ASP A CB  1 
ATOM   292  C  CG  . ASP A 1 35  ? 12.966  -27.571 15.495  1.00 48.51  ? 1505 ASP A CG  1 
ATOM   293  O  OD1 . ASP A 1 35  ? 12.427  -28.676 15.613  1.00 43.96  ? 1505 ASP A OD1 1 
ATOM   294  O  OD2 . ASP A 1 35  ? 12.952  -26.936 14.423  1.00 51.21  ? 1505 ASP A OD2 1 
ATOM   295  N  N   . LEU A 1 36  ? 14.576  -26.382 19.559  1.00 52.50  ? 1506 LEU A N   1 
ATOM   296  C  CA  . LEU A 1 36  ? 15.593  -26.032 20.544  1.00 44.10  ? 1506 LEU A CA  1 
ATOM   297  C  C   . LEU A 1 36  ? 15.684  -27.129 21.593  1.00 45.17  ? 1506 LEU A C   1 
ATOM   298  O  O   . LEU A 1 36  ? 16.766  -27.663 21.856  1.00 44.34  ? 1506 LEU A O   1 
ATOM   299  C  CB  . LEU A 1 36  ? 15.272  -24.691 21.186  1.00 40.46  ? 1506 LEU A CB  1 
ATOM   300  C  CG  . LEU A 1 36  ? 16.077  -24.182 22.393  1.00 59.86  ? 1506 LEU A CG  1 
ATOM   301  C  CD1 . LEU A 1 36  ? 17.528  -23.839 22.031  1.00 46.39  ? 1506 LEU A CD1 1 
ATOM   302  C  CD2 . LEU A 1 36  ? 15.397  -22.951 23.014  1.00 40.64  ? 1506 LEU A CD2 1 
ATOM   303  N  N   . ARG A 1 37  ? 14.522  -27.541 22.124  1.00 44.31  ? 1507 ARG A N   1 
ATOM   304  C  CA  . ARG A 1 37  ? 14.476  -28.630 23.095  1.00 40.30  ? 1507 ARG A CA  1 
ATOM   305  C  C   . ARG A 1 37  ? 15.254  -29.832 22.584  1.00 44.29  ? 1507 ARG A C   1 
ATOM   306  O  O   . ARG A 1 37  ? 16.139  -30.359 23.269  1.00 44.79  ? 1507 ARG A O   1 
ATOM   307  C  CB  . ARG A 1 37  ? 13.027  -29.026 23.374  1.00 38.91  ? 1507 ARG A CB  1 
ATOM   308  C  CG  . ARG A 1 37  ? 12.840  -30.122 24.452  1.00 46.65  ? 1507 ARG A CG  1 
ATOM   309  C  CD  . ARG A 1 37  ? 11.427  -30.693 24.366  1.00 47.47  ? 1507 ARG A CD  1 
ATOM   310  N  NE  . ARG A 1 37  ? 11.230  -31.273 23.050  1.00 49.04  ? 1507 ARG A NE  1 
ATOM   311  C  CZ  . ARG A 1 37  ? 10.067  -31.431 22.444  1.00 39.80  ? 1507 ARG A CZ  1 
ATOM   312  N  NH1 . ARG A 1 37  ? 8.937   -31.052 23.040  1.00 36.92  ? 1507 ARG A NH1 1 
ATOM   313  N  NH2 . ARG A 1 37  ? 10.042  -31.965 21.229  1.00 38.71  ? 1507 ARG A NH2 1 
ATOM   314  N  N   . ASP A 1 38  ? 14.985  -30.211 21.338  1.00 40.70  ? 1508 ASP A N   1 
ATOM   315  C  CA  . ASP A 1 38  ? 15.552  -31.436 20.821  1.00 41.53  ? 1508 ASP A CA  1 
ATOM   316  C  C   . ASP A 1 38  ? 17.077  -31.321 20.701  1.00 53.60  ? 1508 ASP A C   1 
ATOM   317  O  O   . ASP A 1 38  ? 17.805  -32.209 21.172  1.00 45.84  ? 1508 ASP A O   1 
ATOM   318  C  CB  . ASP A 1 38  ? 14.863  -31.783 19.493  1.00 41.12  ? 1508 ASP A CB  1 
ATOM   319  C  CG  . ASP A 1 38  ? 13.379  -32.235 19.689  1.00 50.57  ? 1508 ASP A CG  1 
ATOM   320  O  OD1 . ASP A 1 38  ? 12.965  -32.475 20.851  1.00 40.24  ? 1508 ASP A OD1 1 
ATOM   321  O  OD2 . ASP A 1 38  ? 12.627  -32.344 18.693  1.00 47.92  ? 1508 ASP A OD2 1 
ATOM   322  N  N   . VAL A 1 39  ? 17.586  -30.193 20.185  1.00 46.59  ? 1509 VAL A N   1 
ATOM   323  C  CA  . VAL A 1 39  ? 19.033  -30.107 20.029  1.00 44.71  ? 1509 VAL A CA  1 
ATOM   324  C  C   . VAL A 1 39  ? 19.684  -30.114 21.399  1.00 49.47  ? 1509 VAL A C   1 
ATOM   325  O  O   . VAL A 1 39  ? 20.708  -30.788 21.611  1.00 52.95  ? 1509 VAL A O   1 
ATOM   326  C  CB  . VAL A 1 39  ? 19.459  -28.914 19.154  1.00 54.48  ? 1509 VAL A CB  1 
ATOM   327  C  CG1 . VAL A 1 39  ? 18.843  -29.044 17.768  1.00 47.24  ? 1509 VAL A CG1 1 
ATOM   328  C  CG2 . VAL A 1 39  ? 19.106  -27.566 19.795  1.00 44.89  ? 1509 VAL A CG2 1 
ATOM   329  N  N   . LEU A 1 40  ? 19.042  -29.465 22.379  1.00 46.32  ? 1510 LEU A N   1 
ATOM   330  C  CA  . LEU A 1 40  ? 19.650  -29.457 23.702  1.00 46.19  ? 1510 LEU A CA  1 
ATOM   331  C  C   . LEU A 1 40  ? 19.647  -30.872 24.283  1.00 54.93  ? 1510 LEU A C   1 
ATOM   332  O  O   . LEU A 1 40  ? 20.640  -31.314 24.892  1.00 46.69  ? 1510 LEU A O   1 
ATOM   333  C  CB  . LEU A 1 40  ? 18.930  -28.453 24.601  1.00 44.15  ? 1510 LEU A CB  1 
ATOM   334  C  CG  . LEU A 1 40  ? 19.157  -26.971 24.180  1.00 50.84  ? 1510 LEU A CG  1 
ATOM   335  C  CD1 . LEU A 1 40  ? 18.350  -25.976 25.027  1.00 47.77  ? 1510 LEU A CD1 1 
ATOM   336  C  CD2 . LEU A 1 40  ? 20.626  -26.558 24.182  1.00 45.74  ? 1510 LEU A CD2 1 
ATOM   337  N  N   . PHE A 1 41  ? 18.572  -31.625 24.029  1.00 44.51  ? 1511 PHE A N   1 
ATOM   338  C  CA  . PHE A 1 41  ? 18.529  -32.996 24.515  1.00 44.98  ? 1511 PHE A CA  1 
ATOM   339  C  C   . PHE A 1 41  ? 19.664  -33.786 23.893  1.00 48.03  ? 1511 PHE A C   1 
ATOM   340  O  O   . PHE A 1 41  ? 20.415  -34.490 24.590  1.00 53.29  ? 1511 PHE A O   1 
ATOM   341  C  CB  . PHE A 1 41  ? 17.177  -33.639 24.200  1.00 43.86  ? 1511 PHE A CB  1 
ATOM   342  C  CG  . PHE A 1 41  ? 17.084  -35.075 24.612  1.00 51.88  ? 1511 PHE A CG  1 
ATOM   343  C  CD1 . PHE A 1 41  ? 17.030  -35.422 25.951  1.00 47.90  ? 1511 PHE A CD1 1 
ATOM   344  C  CD2 . PHE A 1 41  ? 17.099  -36.080 23.665  1.00 66.40  ? 1511 PHE A CD2 1 
ATOM   345  C  CE1 . PHE A 1 41  ? 16.966  -36.754 26.341  1.00 53.16  ? 1511 PHE A CE1 1 
ATOM   346  C  CE2 . PHE A 1 41  ? 17.039  -37.407 24.048  1.00 65.61  ? 1511 PHE A CE2 1 
ATOM   347  C  CZ  . PHE A 1 41  ? 16.973  -37.740 25.389  1.00 54.28  ? 1511 PHE A CZ  1 
ATOM   348  N  N   . ASN A 1 42  ? 19.843  -33.631 22.576  1.00 53.33  ? 1512 ASN A N   1 
ATOM   349  C  CA  . ASN A 1 42  ? 20.895  -34.380 21.923  1.00 48.06  ? 1512 ASN A CA  1 
ATOM   350  C  C   . ASN A 1 42  ? 22.246  -33.986 22.505  1.00 65.76  ? 1512 ASN A C   1 
ATOM   351  O  O   . ASN A 1 42  ? 23.095  -34.853 22.780  1.00 54.11  ? 1512 ASN A O   1 
ATOM   352  C  CB  . ASN A 1 42  ? 20.834  -34.158 20.415  1.00 53.47  ? 1512 ASN A CB  1 
ATOM   353  C  CG  . ASN A 1 42  ? 21.903  -34.937 19.669  1.00 71.83  ? 1512 ASN A CG  1 
ATOM   354  O  OD1 . ASN A 1 42  ? 22.893  -34.366 19.173  1.00 67.67  ? 1512 ASN A OD1 1 
ATOM   355  N  ND2 . ASN A 1 42  ? 21.720  -36.255 19.597  1.00 56.24  ? 1512 ASN A ND2 1 
ATOM   356  N  N   . LEU A 1 43  ? 22.426  -32.686 22.789  1.00 55.59  ? 1513 LEU A N   1 
ATOM   357  C  CA  . LEU A 1 43  ? 23.693  -32.242 23.355  1.00 55.09  ? 1513 LEU A CA  1 
ATOM   358  C  C   . LEU A 1 43  ? 23.919  -32.889 24.709  1.00 51.19  ? 1513 LEU A C   1 
ATOM   359  O  O   . LEU A 1 43  ? 25.027  -33.361 25.005  1.00 54.60  ? 1513 LEU A O   1 
ATOM   360  C  CB  . LEU A 1 43  ? 23.726  -30.722 23.459  1.00 54.11  ? 1513 LEU A CB  1 
ATOM   361  C  CG  . LEU A 1 43  ? 24.863  -30.135 24.271  1.00 51.53  ? 1513 LEU A CG  1 
ATOM   362  C  CD1 . LEU A 1 43  ? 26.257  -30.322 23.602  1.00 53.50  ? 1513 LEU A CD1 1 
ATOM   363  C  CD2 . LEU A 1 43  ? 24.544  -28.662 24.496  1.00 50.79  ? 1513 LEU A CD2 1 
ATOM   364  N  N   . CYS A 1 44  ? 22.869  -32.963 25.531  1.00 49.96  ? 1514 CYS A N   1 
ATOM   365  C  CA  . CYS A 1 44  ? 23.078  -33.520 26.856  1.00 57.77  ? 1514 CYS A CA  1 
ATOM   366  C  C   . CYS A 1 44  ? 23.333  -35.010 26.739  1.00 51.61  ? 1514 CYS A C   1 
ATOM   367  O  O   . CYS A 1 44  ? 24.202  -35.552 27.440  1.00 57.26  ? 1514 CYS A O   1 
ATOM   368  C  CB  . CYS A 1 44  ? 21.845  -33.265 27.723  1.00 58.41  ? 1514 CYS A CB  1 
ATOM   369  S  SG  . CYS A 1 44  ? 21.608  -31.571 28.246  1.00 56.87  ? 1514 CYS A SG  1 
ATOM   370  N  N   . GLU A 1 45  ? 22.779  -35.606 25.680  1.00 55.34  ? 1515 GLU A N   1 
ATOM   371  C  CA  . GLU A 1 45  ? 22.994  -37.017 25.397  1.00 69.64  ? 1515 GLU A CA  1 
ATOM   372  C  C   . GLU A 1 45  ? 24.451  -37.278 25.056  1.00 69.67  ? 1515 GLU A C   1 
ATOM   373  O  O   . GLU A 1 45  ? 24.970  -38.368 25.322  1.00 67.52  ? 1515 GLU A O   1 
ATOM   374  C  CB  . GLU A 1 45  ? 22.070  -37.442 24.249  1.00 73.94  ? 1515 GLU A CB  1 
ATOM   375  C  CG  . GLU A 1 45  ? 21.711  -38.912 24.220  1.00 93.11  ? 1515 GLU A CG  1 
ATOM   376  C  CD  . GLU A 1 45  ? 20.311  -39.155 23.675  1.00 93.85  ? 1515 GLU A CD  1 
ATOM   377  O  OE1 . GLU A 1 45  ? 19.984  -38.630 22.580  1.00 85.93  ? 1515 GLU A OE1 1 
ATOM   378  O  OE2 . GLU A 1 45  ? 19.540  -39.870 24.354  1.00 90.78  ? 1515 GLU A OE2 1 
ATOM   379  N  N   . ASN A 1 46  ? 25.138  -36.275 24.518  1.00 60.79  ? 1516 ASN A N   1 
ATOM   380  C  CA  . ASN A 1 46  ? 26.532  -36.477 24.186  1.00 66.92  ? 1516 ASN A CA  1 
ATOM   381  C  C   . ASN A 1 46  ? 27.433  -36.132 25.358  1.00 65.37  ? 1516 ASN A C   1 
ATOM   382  O  O   . ASN A 1 46  ? 28.440  -36.821 25.575  1.00 74.15  ? 1516 ASN A O   1 
ATOM   383  C  CB  . ASN A 1 46  ? 26.897  -35.648 22.950  1.00 61.62  ? 1516 ASN A CB  1 
ATOM   384  C  CG  . ASN A 1 46  ? 26.172  -36.124 21.696  1.00 73.42  ? 1516 ASN A CG  1 
ATOM   385  O  OD1 . ASN A 1 46  ? 25.744  -37.277 21.614  1.00 83.11  ? 1516 ASN A OD1 1 
ATOM   386  N  ND2 . ASN A 1 46  ? 26.034  -35.239 20.714  1.00 70.68  ? 1516 ASN A ND2 1 
ATOM   387  N  N   . LEU A 1 47  ? 27.010  -35.199 26.217  1.00 65.43  ? 1517 LEU A N   1 
ATOM   388  C  CA  . LEU A 1 47  ? 27.867  -34.825 27.336  1.00 69.53  ? 1517 LEU A CA  1 
ATOM   389  C  C   . LEU A 1 47  ? 28.094  -36.007 28.268  1.00 78.39  ? 1517 LEU A C   1 
ATOM   390  O  O   . LEU A 1 47  ? 29.244  -36.349 28.586  1.00 100.09 ? 1517 LEU A O   1 
ATOM   391  C  CB  . LEU A 1 47  ? 27.270  -33.629 28.074  1.00 70.41  ? 1517 LEU A CB  1 
ATOM   392  C  CG  . LEU A 1 47  ? 27.276  -32.373 27.201  1.00 64.77  ? 1517 LEU A CG  1 
ATOM   393  C  CD1 . LEU A 1 47  ? 26.786  -31.154 27.958  1.00 62.62  ? 1517 LEU A CD1 1 
ATOM   394  C  CD2 . LEU A 1 47  ? 28.686  -32.165 26.657  1.00 80.77  ? 1517 LEU A CD2 1 
ATOM   395  N  N   . VAL A 1 48  ? 27.015  -36.716 28.619  1.00 81.09  ? 1518 VAL A N   1 
ATOM   396  C  CA  . VAL A 1 48  ? 27.137  -37.869 29.508  1.00 94.09  ? 1518 VAL A CA  1 
ATOM   397  C  C   . VAL A 1 48  ? 28.029  -38.933 28.878  1.00 99.46  ? 1518 VAL A C   1 
ATOM   398  O  O   . VAL A 1 48  ? 28.826  -39.580 29.571  1.00 101.03 ? 1518 VAL A O   1 
ATOM   399  C  CB  . VAL A 1 48  ? 25.747  -38.441 29.867  1.00 87.86  ? 1518 VAL A CB  1 
ATOM   400  C  CG1 . VAL A 1 48  ? 24.836  -37.366 30.496  1.00 59.65  ? 1518 VAL A CG1 1 
ATOM   401  C  CG2 . VAL A 1 48  ? 25.079  -39.069 28.647  1.00 96.12  ? 1518 VAL A CG2 1 
ATOM   402  N  N   . LYS A 1 49  ? 27.950  -39.103 27.548  1.00 95.54  ? 1519 LYS A N   1 
ATOM   403  C  CA  . LYS A 1 49  ? 28.822  -40.084 26.913  1.00 100.20 ? 1519 LYS A CA  1 
ATOM   404  C  C   . LYS A 1 49  ? 30.271  -39.613 26.956  1.00 111.19 ? 1519 LYS A C   1 
ATOM   405  O  O   . LYS A 1 49  ? 31.178  -40.394 27.273  1.00 117.44 ? 1519 LYS A O   1 
ATOM   406  C  CB  . LYS A 1 49  ? 28.388  -40.348 25.469  1.00 88.52  ? 1519 LYS A CB  1 
ATOM   407  C  CG  . LYS A 1 49  ? 27.072  -41.085 25.296  1.00 89.65  ? 1519 LYS A CG  1 
ATOM   408  C  CD  . LYS A 1 49  ? 26.778  -41.299 23.813  1.00 94.93  ? 1519 LYS A CD  1 
ATOM   409  C  CE  . LYS A 1 49  ? 25.312  -41.665 23.562  1.00 104.21 ? 1519 LYS A CE  1 
ATOM   410  N  NZ  . LYS A 1 49  ? 25.063  -42.125 22.156  1.00 101.31 ? 1519 LYS A NZ  1 
ATOM   411  N  N   . SER A 1 50  ? 30.502  -38.327 26.683  1.00 111.76 ? 1520 SER A N   1 
ATOM   412  C  CA  . SER A 1 50  ? 31.863  -37.837 26.536  1.00 120.60 ? 1520 SER A CA  1 
ATOM   413  C  C   . SER A 1 50  ? 32.574  -37.711 27.869  1.00 130.41 ? 1520 SER A C   1 
ATOM   414  O  O   . SER A 1 50  ? 33.774  -37.419 27.883  1.00 136.55 ? 1520 SER A O   1 
ATOM   415  C  CB  . SER A 1 50  ? 31.872  -36.488 25.808  1.00 118.82 ? 1520 SER A CB  1 
ATOM   416  O  OG  . SER A 1 50  ? 31.681  -36.659 24.412  1.00 119.23 ? 1520 SER A OG  1 
ATOM   417  N  N   . SER A 1 51  ? 31.859  -37.932 28.972  1.00 130.82 ? 1521 SER A N   1 
ATOM   418  C  CA  . SER A 1 51  ? 32.373  -37.927 30.335  1.00 142.57 ? 1521 SER A CA  1 
ATOM   419  C  C   . SER A 1 51  ? 32.727  -36.531 30.827  1.00 138.36 ? 1521 SER A C   1 
ATOM   420  O  O   . SER A 1 51  ? 33.284  -36.396 31.923  1.00 151.51 ? 1521 SER A O   1 
ATOM   421  C  CB  . SER A 1 51  ? 33.585  -38.859 30.491  1.00 154.32 ? 1521 SER A CB  1 
ATOM   422  O  OG  . SER A 1 51  ? 33.652  -39.420 31.792  1.00 155.94 ? 1521 SER A OG  1 
ATOM   423  N  N   . GLU A 1 52  ? 32.426  -35.483 30.061  1.00 125.59 ? 1522 GLU A N   1 
ATOM   424  C  CA  . GLU A 1 52  ? 32.441  -34.147 30.646  1.00 127.54 ? 1522 GLU A CA  1 
ATOM   425  C  C   . GLU A 1 52  ? 31.137  -33.835 31.376  1.00 127.57 ? 1522 GLU A C   1 
ATOM   426  O  O   . GLU A 1 52  ? 30.859  -32.665 31.679  1.00 122.22 ? 1522 GLU A O   1 
ATOM   427  C  CB  . GLU A 1 52  ? 32.735  -33.084 29.579  1.00 118.43 ? 1522 GLU A CB  1 
ATOM   428  C  CG  . GLU A 1 52  ? 33.413  -31.796 30.114  1.00 116.99 ? 1522 GLU A CG  1 
ATOM   429  C  CD  . GLU A 1 52  ? 34.516  -32.048 31.158  1.00 114.81 ? 1522 GLU A CD  1 
ATOM   430  O  OE1 . GLU A 1 52  ? 34.699  -31.190 32.058  1.00 101.95 ? 1522 GLU A OE1 1 
ATOM   431  O  OE2 . GLU A 1 52  ? 35.213  -33.089 31.072  1.00 106.32 ? 1522 GLU A OE2 1 
ATOM   432  N  N   . ALA A 1 53  ? 30.352  -34.871 31.669  1.00 121.99 ? 1523 ALA A N   1 
ATOM   433  C  CA  . ALA A 1 53  ? 29.121  -34.712 32.423  1.00 116.29 ? 1523 ALA A CA  1 
ATOM   434  C  C   . ALA A 1 53  ? 29.399  -34.139 33.809  1.00 113.72 ? 1523 ALA A C   1 
ATOM   435  O  O   . ALA A 1 53  ? 30.450  -34.379 34.411  1.00 121.12 ? 1523 ALA A O   1 
ATOM   436  C  CB  . ALA A 1 53  ? 28.404  -36.057 32.548  1.00 115.53 ? 1523 ALA A CB  1 
ATOM   437  N  N   . ASN A 1 54  ? 28.442  -33.356 34.298  1.00 104.64 ? 1524 ASN A N   1 
ATOM   438  C  CA  . ASN A 1 54  ? 28.332  -32.814 35.649  1.00 106.01 ? 1524 ASN A CA  1 
ATOM   439  C  C   . ASN A 1 54  ? 29.298  -31.662 35.906  1.00 97.16  ? 1524 ASN A C   1 
ATOM   440  O  O   . ASN A 1 54  ? 29.311  -31.119 37.021  1.00 91.77  ? 1524 ASN A O   1 
ATOM   441  C  CB  . ASN A 1 54  ? 28.497  -33.903 36.720  1.00 108.56 ? 1524 ASN A CB  1 
ATOM   442  C  CG  . ASN A 1 54  ? 27.350  -34.897 36.696  1.00 105.98 ? 1524 ASN A CG  1 
ATOM   443  O  OD1 . ASN A 1 54  ? 27.166  -35.624 35.718  1.00 105.92 ? 1524 ASN A OD1 1 
ATOM   444  N  ND2 . ASN A 1 54  ? 26.545  -34.903 37.755  1.00 103.03 ? 1524 ASN A ND2 1 
ATOM   445  N  N   . SER A 1 55  ? 30.100  -31.265 34.921  1.00 102.68 ? 1525 SER A N   1 
ATOM   446  C  CA  . SER A 1 55  ? 30.705  -29.948 34.935  1.00 99.87  ? 1525 SER A CA  1 
ATOM   447  C  C   . SER A 1 55  ? 29.598  -28.898 34.887  1.00 103.54 ? 1525 SER A C   1 
ATOM   448  O  O   . SER A 1 55  ? 28.495  -29.167 34.396  1.00 97.70  ? 1525 SER A O   1 
ATOM   449  C  CB  . SER A 1 55  ? 31.663  -29.775 33.758  1.00 102.54 ? 1525 SER A CB  1 
ATOM   450  O  OG  . SER A 1 55  ? 30.960  -29.749 32.531  1.00 106.73 ? 1525 SER A OG  1 
ATOM   451  N  N   . PRO A 1 56  ? 29.854  -27.704 35.427  1.00 103.49 ? 1526 PRO A N   1 
ATOM   452  C  CA  . PRO A 1 56  ? 28.808  -26.667 35.430  1.00 101.88 ? 1526 PRO A CA  1 
ATOM   453  C  C   . PRO A 1 56  ? 28.242  -26.375 34.049  1.00 100.09 ? 1526 PRO A C   1 
ATOM   454  O  O   . PRO A 1 56  ? 27.122  -25.863 33.956  1.00 103.95 ? 1526 PRO A O   1 
ATOM   455  C  CB  . PRO A 1 56  ? 29.525  -25.446 36.020  1.00 102.26 ? 1526 PRO A CB  1 
ATOM   456  C  CG  . PRO A 1 56  ? 30.587  -26.038 36.899  1.00 102.31 ? 1526 PRO A CG  1 
ATOM   457  C  CD  . PRO A 1 56  ? 31.036  -27.304 36.210  1.00 101.91 ? 1526 PRO A CD  1 
ATOM   458  N  N   . ALA A 1 57  ? 28.979  -26.664 32.974  1.00 98.50  ? 1527 ALA A N   1 
ATOM   459  C  CA  . ALA A 1 57  ? 28.416  -26.482 31.642  1.00 92.26  ? 1527 ALA A CA  1 
ATOM   460  C  C   . ALA A 1 57  ? 27.392  -27.566 31.321  1.00 98.24  ? 1527 ALA A C   1 
ATOM   461  O  O   . ALA A 1 57  ? 26.332  -27.267 30.760  1.00 98.78  ? 1527 ALA A O   1 
ATOM   462  C  CB  . ALA A 1 57  ? 29.525  -26.469 30.594  1.00 96.72  ? 1527 ALA A CB  1 
ATOM   463  N  N   . HIS A 1 58  ? 27.672  -28.826 31.684  1.00 90.10  ? 1528 HIS A N   1 
ATOM   464  C  CA  . HIS A 1 58  ? 26.644  -29.860 31.567  1.00 86.66  ? 1528 HIS A CA  1 
ATOM   465  C  C   . HIS A 1 58  ? 25.390  -29.475 32.346  1.00 80.31  ? 1528 HIS A C   1 
ATOM   466  O  O   . HIS A 1 58  ? 24.273  -29.550 31.821  1.00 76.14  ? 1528 HIS A O   1 
ATOM   467  C  CB  . HIS A 1 58  ? 27.166  -31.220 32.041  1.00 86.56  ? 1528 HIS A CB  1 
ATOM   468  C  CG  . HIS A 1 58  ? 26.232  -32.361 31.743  1.00 90.99  ? 1528 HIS A CG  1 
ATOM   469  N  ND1 . HIS A 1 58  ? 26.113  -33.464 32.563  1.00 95.67  ? 1528 HIS A ND1 1 
ATOM   470  C  CD2 . HIS A 1 58  ? 25.369  -32.568 30.718  1.00 92.12  ? 1528 HIS A CD2 1 
ATOM   471  C  CE1 . HIS A 1 58  ? 25.224  -34.302 32.055  1.00 90.98  ? 1528 HIS A CE1 1 
ATOM   472  N  NE2 . HIS A 1 58  ? 24.757  -33.782 30.934  1.00 89.44  ? 1528 HIS A NE2 1 
ATOM   473  N  N   . GLU A 1 59  ? 25.558  -29.040 33.599  1.00 66.20  ? 1529 GLU A N   1 
ATOM   474  C  CA  . GLU A 1 59  ? 24.394  -28.762 34.422  1.00 75.27  ? 1529 GLU A CA  1 
ATOM   475  C  C   . GLU A 1 59  ? 23.643  -27.539 33.918  1.00 75.11  ? 1529 GLU A C   1 
ATOM   476  O  O   . GLU A 1 59  ? 22.407  -27.523 33.923  1.00 60.38  ? 1529 GLU A O   1 
ATOM   477  C  CB  . GLU A 1 59  ? 24.807  -28.603 35.886  1.00 78.69  ? 1529 GLU A CB  1 
ATOM   478  C  CG  . GLU A 1 59  ? 25.272  -29.915 36.510  1.00 89.36  ? 1529 GLU A CG  1 
ATOM   479  C  CD  . GLU A 1 59  ? 24.138  -30.696 37.166  1.00 98.95  ? 1529 GLU A CD  1 
ATOM   480  O  OE1 . GLU A 1 59  ? 24.372  -31.872 37.530  1.00 107.83 ? 1529 GLU A OE1 1 
ATOM   481  O  OE2 . GLU A 1 59  ? 23.017  -30.141 37.304  1.00 96.22  ? 1529 GLU A OE2 1 
ATOM   482  N  N   . GLU A 1 60  ? 24.359  -26.531 33.421  1.00 56.08  ? 1530 GLU A N   1 
ATOM   483  C  CA  . GLU A 1 60  ? 23.642  -25.394 32.873  1.00 70.24  ? 1530 GLU A CA  1 
ATOM   484  C  C   . GLU A 1 60  ? 22.948  -25.768 31.573  1.00 59.82  ? 1530 GLU A C   1 
ATOM   485  O  O   . GLU A 1 60  ? 21.873  -25.245 31.284  1.00 53.24  ? 1530 GLU A O   1 
ATOM   486  C  CB  . GLU A 1 60  ? 24.576  -24.193 32.664  1.00 91.81  ? 1530 GLU A CB  1 
ATOM   487  C  CG  . GLU A 1 60  ? 23.827  -22.923 32.235  1.00 96.98  ? 1530 GLU A CG  1 
ATOM   488  C  CD  . GLU A 1 60  ? 24.752  -21.768 31.870  1.00 96.24  ? 1530 GLU A CD  1 
ATOM   489  O  OE1 . GLU A 1 60  ? 25.741  -22.001 31.128  1.00 96.61  ? 1530 GLU A OE1 1 
ATOM   490  O  OE2 . GLU A 1 60  ? 24.462  -20.623 32.286  1.00 86.35  ? 1530 GLU A OE2 1 
ATOM   491  N  N   . PHE A 1 61  ? 23.516  -26.684 30.785  1.00 50.14  ? 1531 PHE A N   1 
ATOM   492  C  CA  . PHE A 1 61  ? 22.785  -27.113 29.599  1.00 55.07  ? 1531 PHE A CA  1 
ATOM   493  C  C   . PHE A 1 61  ? 21.575  -27.964 29.957  1.00 49.76  ? 1531 PHE A C   1 
ATOM   494  O  O   . PHE A 1 61  ? 20.592  -27.968 29.216  1.00 51.65  ? 1531 PHE A O   1 
ATOM   495  C  CB  . PHE A 1 61  ? 23.699  -27.845 28.627  1.00 50.01  ? 1531 PHE A CB  1 
ATOM   496  C  CG  . PHE A 1 61  ? 24.497  -26.906 27.749  1.00 56.06  ? 1531 PHE A CG  1 
ATOM   497  C  CD1 . PHE A 1 61  ? 23.845  -25.978 26.937  1.00 56.32  ? 1531 PHE A CD1 1 
ATOM   498  C  CD2 . PHE A 1 61  ? 25.882  -26.942 27.737  1.00 52.57  ? 1531 PHE A CD2 1 
ATOM   499  C  CE1 . PHE A 1 61  ? 24.550  -25.102 26.133  1.00 50.96  ? 1531 PHE A CE1 1 
ATOM   500  C  CE2 . PHE A 1 61  ? 26.608  -26.059 26.935  1.00 59.96  ? 1531 PHE A CE2 1 
ATOM   501  C  CZ  . PHE A 1 61  ? 25.944  -25.145 26.126  1.00 56.19  ? 1531 PHE A CZ  1 
ATOM   502  N  N   . LYS A 1 62  ? 21.644  -28.721 31.051  1.00 52.52  ? 1532 LYS A N   1 
ATOM   503  C  CA  . LYS A 1 62  ? 20.456  -29.426 31.528  1.00 59.12  ? 1532 LYS A CA  1 
ATOM   504  C  C   . LYS A 1 62  ? 19.379  -28.422 31.912  1.00 54.54  ? 1532 LYS A C   1 
ATOM   505  O  O   . LYS A 1 62  ? 18.199  -28.601 31.585  1.00 54.72  ? 1532 LYS A O   1 
ATOM   506  C  CB  . LYS A 1 62  ? 20.805  -30.348 32.706  1.00 58.26  ? 1532 LYS A CB  1 
ATOM   507  C  CG  . LYS A 1 62  ? 21.521  -31.661 32.314  1.00 65.71  ? 1532 LYS A CG  1 
ATOM   508  C  CD  . LYS A 1 62  ? 22.006  -32.445 33.542  1.00 78.73  ? 1532 LYS A CD  1 
ATOM   509  C  CE  . LYS A 1 62  ? 21.960  -33.961 33.310  1.00 94.63  ? 1532 LYS A CE  1 
ATOM   510  N  NZ  . LYS A 1 62  ? 22.424  -34.750 34.496  1.00 92.92  ? 1532 LYS A NZ  1 
ATOM   511  N  N   . THR A 1 63  ? 19.775  -27.336 32.586  1.00 53.46  ? 1533 THR A N   1 
ATOM   512  C  CA  . THR A 1 63  ? 18.798  -26.305 32.921  1.00 57.70  ? 1533 THR A CA  1 
ATOM   513  C  C   . THR A 1 63  ? 18.215  -25.671 31.664  1.00 44.64  ? 1533 THR A C   1 
ATOM   514  O  O   . THR A 1 63  ? 17.007  -25.440 31.578  1.00 49.21  ? 1533 THR A O   1 
ATOM   515  C  CB  . THR A 1 63  ? 19.436  -25.253 33.822  1.00 65.75  ? 1533 THR A CB  1 
ATOM   516  O  OG1 . THR A 1 63  ? 19.833  -25.873 35.056  1.00 65.44  ? 1533 THR A OG1 1 
ATOM   517  C  CG2 . THR A 1 63  ? 18.459  -24.131 34.113  1.00 50.15  ? 1533 THR A CG2 1 
ATOM   518  N  N   . MET A 1 64  ? 19.059  -25.375 30.681  1.00 51.19  ? 1534 MET A N   1 
ATOM   519  C  CA  . MET A 1 64  ? 18.551  -24.826 29.428  1.00 50.14  ? 1534 MET A CA  1 
ATOM   520  C  C   . MET A 1 64  ? 17.588  -25.803 28.755  1.00 48.58  ? 1534 MET A C   1 
ATOM   521  O  O   . MET A 1 64  ? 16.591  -25.390 28.147  1.00 42.66  ? 1534 MET A O   1 
ATOM   522  C  CB  . MET A 1 64  ? 19.717  -24.468 28.500  1.00 45.18  ? 1534 MET A CB  1 
ATOM   523  C  CG  . MET A 1 64  ? 20.417  -23.152 28.851  1.00 49.88  ? 1534 MET A CG  1 
ATOM   524  S  SD  . MET A 1 64  ? 21.896  -22.838 27.837  1.00 57.35  ? 1534 MET A SD  1 
ATOM   525  C  CE  . MET A 1 64  ? 23.218  -23.323 28.925  1.00 72.70  ? 1534 MET A CE  1 
ATOM   526  N  N   . LEU A 1 65  ? 17.901  -27.105 28.811  1.00 53.36  ? 1535 LEU A N   1 
ATOM   527  C  CA  . LEU A 1 65  ? 16.990  -28.117 28.286  1.00 46.60  ? 1535 LEU A CA  1 
ATOM   528  C  C   . LEU A 1 65  ? 15.656  -28.070 29.014  1.00 45.73  ? 1535 LEU A C   1 
ATOM   529  O  O   . LEU A 1 65  ? 14.591  -28.124 28.392  1.00 40.78  ? 1535 LEU A O   1 
ATOM   530  C  CB  . LEU A 1 65  ? 17.607  -29.504 28.410  1.00 50.07  ? 1535 LEU A CB  1 
ATOM   531  C  CG  . LEU A 1 65  ? 16.711  -30.695 28.056  1.00 48.69  ? 1535 LEU A CG  1 
ATOM   532  C  CD1 . LEU A 1 65  ? 16.193  -30.574 26.626  1.00 42.25  ? 1535 LEU A CD1 1 
ATOM   533  C  CD2 . LEU A 1 65  ? 17.528  -32.006 28.252  1.00 44.28  ? 1535 LEU A CD2 1 
ATOM   534  N  N   . LEU A 1 66  ? 15.699  -27.990 30.339  1.00 42.23  ? 1536 LEU A N   1 
ATOM   535  C  CA  . LEU A 1 66  ? 14.461  -27.942 31.104  1.00 46.41  ? 1536 LEU A CA  1 
ATOM   536  C  C   . LEU A 1 66  ? 13.637  -26.732 30.707  1.00 50.41  ? 1536 LEU A C   1 
ATOM   537  O  O   . LEU A 1 66  ? 12.414  -26.836 30.529  1.00 40.92  ? 1536 LEU A O   1 
ATOM   538  C  CB  . LEU A 1 66  ? 14.762  -27.913 32.600  1.00 45.86  ? 1536 LEU A CB  1 
ATOM   539  C  CG  . LEU A 1 66  ? 13.539  -27.754 33.497  1.00 41.86  ? 1536 LEU A CG  1 
ATOM   540  C  CD1 . LEU A 1 66  ? 12.610  -28.903 33.276  1.00 42.13  ? 1536 LEU A CD1 1 
ATOM   541  C  CD2 . LEU A 1 66  ? 13.992  -27.732 34.939  1.00 51.94  ? 1536 LEU A CD2 1 
ATOM   542  N  N   . ILE A 1 67  ? 14.307  -25.582 30.526  1.00 44.15  ? 1537 ILE A N   1 
ATOM   543  C  CA  . ILE A 1 67  ? 13.618  -24.352 30.148  1.00 49.96  ? 1537 ILE A CA  1 
ATOM   544  C  C   . ILE A 1 67  ? 12.987  -24.493 28.769  1.00 43.06  ? 1537 ILE A C   1 
ATOM   545  O  O   . ILE A 1 67  ? 11.832  -24.104 28.559  1.00 47.74  ? 1537 ILE A O   1 
ATOM   546  C  CB  . ILE A 1 67  ? 14.585  -23.151 30.187  1.00 49.76  ? 1537 ILE A CB  1 
ATOM   547  C  CG1 . ILE A 1 67  ? 14.800  -22.661 31.624  1.00 56.05  ? 1537 ILE A CG1 1 
ATOM   548  C  CG2 . ILE A 1 67  ? 14.054  -22.023 29.310  1.00 40.52  ? 1537 ILE A CG2 1 
ATOM   549  C  CD1 . ILE A 1 67  ? 16.159  -21.969 31.867  1.00 44.40  ? 1537 ILE A CD1 1 
ATOM   550  N  N   . ALA A 1 68  ? 13.744  -25.030 27.800  1.00 40.44  ? 1538 ALA A N   1 
ATOM   551  C  CA  . ALA A 1 68  ? 13.184  -25.223 26.463  1.00 46.34  ? 1538 ALA A CA  1 
ATOM   552  C  C   . ALA A 1 68  ? 11.993  -26.179 26.513  1.00 42.41  ? 1538 ALA A C   1 
ATOM   553  O  O   . ALA A 1 68  ? 11.032  -26.024 25.760  1.00 37.50  ? 1538 ALA A O   1 
ATOM   554  C  CB  . ALA A 1 68  ? 14.240  -25.762 25.492  1.00 39.71  ? 1538 ALA A CB  1 
ATOM   555  N  N   . HIS A 1 69  ? 12.047  -27.179 27.390  1.00 38.56  ? 1539 HIS A N   1 
ATOM   556  C  CA  . HIS A 1 69  ? 10.915  -28.088 27.528  1.00 37.99  ? 1539 HIS A CA  1 
ATOM   557  C  C   . HIS A 1 69  ? 9.687   -27.353 28.076  1.00 45.26  ? 1539 HIS A C   1 
ATOM   558  O  O   . HIS A 1 69  ? 8.580   -27.508 27.549  1.00 41.66  ? 1539 HIS A O   1 
ATOM   559  C  CB  . HIS A 1 69  ? 11.305  -29.261 28.420  1.00 38.69  ? 1539 HIS A CB  1 
ATOM   560  C  CG  . HIS A 1 69  ? 10.137  -29.891 29.105  1.00 42.31  ? 1539 HIS A CG  1 
ATOM   561  N  ND1 . HIS A 1 69  ? 9.222   -30.667 28.432  1.00 37.85  ? 1539 HIS A ND1 1 
ATOM   562  C  CD2 . HIS A 1 69  ? 9.723   -29.842 30.393  1.00 40.71  ? 1539 HIS A CD2 1 
ATOM   563  C  CE1 . HIS A 1 69  ? 8.307   -31.092 29.286  1.00 45.33  ? 1539 HIS A CE1 1 
ATOM   564  N  NE2 . HIS A 1 69  ? 8.587   -30.600 30.480  1.00 42.65  ? 1539 HIS A NE2 1 
ATOM   565  N  N   . TYR A 1 70  ? 9.876   -26.501 29.094  1.00 45.86  ? 1540 TYR A N   1 
ATOM   566  C  CA  . TYR A 1 70  ? 8.762   -25.675 29.593  1.00 41.88  ? 1540 TYR A CA  1 
ATOM   567  C  C   . TYR A 1 70  ? 8.161   -24.834 28.471  1.00 37.86  ? 1540 TYR A C   1 
ATOM   568  O  O   . TYR A 1 70  ? 6.945   -24.809 28.287  1.00 41.05  ? 1540 TYR A O   1 
ATOM   569  C  CB  . TYR A 1 70  ? 9.222   -24.749 30.721  1.00 37.84  ? 1540 TYR A CB  1 
ATOM   570  C  CG  . TYR A 1 70  ? 9.483   -25.414 32.053  1.00 38.54  ? 1540 TYR A CG  1 
ATOM   571  C  CD1 . TYR A 1 70  ? 8.872   -26.618 32.396  1.00 43.15  ? 1540 TYR A CD1 1 
ATOM   572  C  CD2 . TYR A 1 70  ? 10.318  -24.816 32.985  1.00 39.37  ? 1540 TYR A CD2 1 
ATOM   573  C  CE1 . TYR A 1 70  ? 9.100   -27.218 33.639  1.00 39.29  ? 1540 TYR A CE1 1 
ATOM   574  C  CE2 . TYR A 1 70  ? 10.566  -25.404 34.218  1.00 45.11  ? 1540 TYR A CE2 1 
ATOM   575  C  CZ  . TYR A 1 70  ? 9.946   -26.604 34.544  1.00 40.36  ? 1540 TYR A CZ  1 
ATOM   576  O  OH  . TYR A 1 70  ? 10.192  -27.181 35.772  1.00 43.64  ? 1540 TYR A OH  1 
ATOM   577  N  N   . TYR A 1 71  ? 9.001   -24.151 27.692  1.00 38.85  ? 1541 TYR A N   1 
ATOM   578  C  CA  . TYR A 1 71  ? 8.465   -23.336 26.602  1.00 38.68  ? 1541 TYR A CA  1 
ATOM   579  C  C   . TYR A 1 71  ? 7.734   -24.171 25.550  1.00 35.72  ? 1541 TYR A C   1 
ATOM   580  O  O   . TYR A 1 71  ? 6.681   -23.758 25.047  1.00 47.14  ? 1541 TYR A O   1 
ATOM   581  C  CB  . TYR A 1 71  ? 9.575   -22.540 25.931  1.00 36.85  ? 1541 TYR A CB  1 
ATOM   582  C  CG  . TYR A 1 71  ? 9.919   -21.224 26.606  1.00 51.74  ? 1541 TYR A CG  1 
ATOM   583  C  CD1 . TYR A 1 71  ? 9.004   -20.169 26.662  1.00 47.24  ? 1541 TYR A CD1 1 
ATOM   584  C  CD2 . TYR A 1 71  ? 11.165  -21.035 27.186  1.00 38.24  ? 1541 TYR A CD2 1 
ATOM   585  C  CE1 . TYR A 1 71  ? 9.338   -18.969 27.288  1.00 37.75  ? 1541 TYR A CE1 1 
ATOM   586  C  CE2 . TYR A 1 71  ? 11.499  -19.848 27.798  1.00 54.04  ? 1541 TYR A CE2 1 
ATOM   587  C  CZ  . TYR A 1 71  ? 10.579  -18.821 27.852  1.00 43.36  ? 1541 TYR A CZ  1 
ATOM   588  O  OH  . TYR A 1 71  ? 10.949  -17.653 28.456  1.00 48.27  ? 1541 TYR A OH  1 
ATOM   589  N  N   . ALA A 1 72  ? 8.301   -25.321 25.152  1.00 45.55  ? 1542 ALA A N   1 
ATOM   590  C  CA  . ALA A 1 72  ? 7.633   -26.139 24.141  1.00 41.40  ? 1542 ALA A CA  1 
ATOM   591  C  C   . ALA A 1 72  ? 6.302   -26.676 24.651  1.00 38.35  ? 1542 ALA A C   1 
ATOM   592  O  O   . ALA A 1 72  ? 5.315   -26.722 23.909  1.00 34.48  ? 1542 ALA A O   1 
ATOM   593  C  CB  . ALA A 1 72  ? 8.515   -27.305 23.707  1.00 43.89  ? 1542 ALA A CB  1 
ATOM   594  N  N   . THR A 1 73  ? 6.286   -27.138 25.896  1.00 35.21  ? 1543 THR A N   1 
ATOM   595  C  CA  . THR A 1 73  ? 5.067   -27.638 26.494  1.00 37.92  ? 1543 THR A CA  1 
ATOM   596  C  C   . THR A 1 73  ? 4.058   -26.513 26.611  1.00 53.83  ? 1543 THR A C   1 
ATOM   597  O  O   . THR A 1 73  ? 2.856   -26.743 26.468  1.00 38.95  ? 1543 THR A O   1 
ATOM   598  C  CB  . THR A 1 73  ? 5.353   -28.254 27.869  1.00 38.33  ? 1543 THR A CB  1 
ATOM   599  O  OG1 . THR A 1 73  ? 6.465   -29.151 27.774  1.00 39.23  ? 1543 THR A OG1 1 
ATOM   600  C  CG2 . THR A 1 73  ? 4.117   -29.014 28.397  1.00 44.92  ? 1543 THR A CG2 1 
ATOM   601  N  N   . ARG A 1 74  ? 4.540   -25.281 26.830  1.00 49.02  ? 1544 ARG A N   1 
ATOM   602  C  CA  . ARG A 1 74  ? 3.643   -24.136 26.875  1.00 42.55  ? 1544 ARG A CA  1 
ATOM   603  C  C   . ARG A 1 74  ? 2.972   -23.909 25.528  1.00 36.48  ? 1544 ARG A C   1 
ATOM   604  O  O   . ARG A 1 74  ? 1.755   -23.717 25.464  1.00 41.61  ? 1544 ARG A O   1 
ATOM   605  C  CB  . ARG A 1 74  ? 4.384   -22.882 27.339  1.00 35.01  ? 1544 ARG A CB  1 
ATOM   606  C  CG  . ARG A 1 74  ? 3.438   -21.655 27.533  1.00 35.02  ? 1544 ARG A CG  1 
ATOM   607  C  CD  . ARG A 1 74  ? 4.222   -20.428 27.929  1.00 35.56  ? 1544 ARG A CD  1 
ATOM   608  N  NE  . ARG A 1 74  ? 4.935   -19.891 26.775  1.00 37.23  ? 1544 ARG A NE  1 
ATOM   609  C  CZ  . ARG A 1 74  ? 5.669   -18.781 26.792  1.00 36.16  ? 1544 ARG A CZ  1 
ATOM   610  N  NH1 . ARG A 1 74  ? 5.789   -18.059 27.909  1.00 39.67  ? 1544 ARG A NH1 1 
ATOM   611  N  NH2 . ARG A 1 74  ? 6.277   -18.403 25.687  1.00 36.29  ? 1544 ARG A NH2 1 
ATOM   612  N  N   . SER A 1 75  ? 3.741   -23.930 24.440  1.00 36.81  ? 1545 SER A N   1 
ATOM   613  C  CA  . SER A 1 75  ? 3.095   -23.753 23.141  1.00 33.82  ? 1545 SER A CA  1 
ATOM   614  C  C   . SER A 1 75  ? 2.094   -24.869 22.856  1.00 41.36  ? 1545 SER A C   1 
ATOM   615  O  O   . SER A 1 75  ? 0.983   -24.602 22.359  1.00 49.31  ? 1545 SER A O   1 
ATOM   616  C  CB  . SER A 1 75  ? 4.126   -23.674 22.033  1.00 34.02  ? 1545 SER A CB  1 
ATOM   617  O  OG  . SER A 1 75  ? 4.932   -22.520 22.196  1.00 40.48  ? 1545 SER A OG  1 
ATOM   618  N  N   . ALA A 1 76  ? 2.451   -26.120 23.191  1.00 37.07  ? 1546 ALA A N   1 
ATOM   619  C  CA  . ALA A 1 76  ? 1.485   -27.210 23.049  1.00 35.36  ? 1546 ALA A CA  1 
ATOM   620  C  C   . ALA A 1 76  ? 0.205   -26.911 23.826  1.00 43.77  ? 1546 ALA A C   1 
ATOM   621  O  O   . ALA A 1 76  ? -0.900  -27.000 23.284  1.00 40.80  ? 1546 ALA A O   1 
ATOM   622  C  CB  . ALA A 1 76  ? 2.090   -28.541 23.507  1.00 36.18  ? 1546 ALA A CB  1 
ATOM   623  N  N   . ALA A 1 77  ? 0.340   -26.539 25.100  1.00 41.34  ? 1547 ALA A N   1 
ATOM   624  C  CA  . ALA A 1 77  ? -0.828  -26.249 25.921  1.00 33.72  ? 1547 ALA A CA  1 
ATOM   625  C  C   . ALA A 1 77  ? -1.662  -25.104 25.340  1.00 42.73  ? 1547 ALA A C   1 
ATOM   626  O  O   . ALA A 1 77  ? -2.893  -25.126 25.419  1.00 45.22  ? 1547 ALA A O   1 
ATOM   627  C  CB  . ALA A 1 77  ? -0.392  -25.932 27.355  1.00 36.08  ? 1547 ALA A CB  1 
ATOM   628  N  N   . GLN A 1 78  ? -1.010  -24.087 24.774  1.00 48.77  ? 1548 GLN A N   1 
ATOM   629  C  CA  . GLN A 1 78  ? -1.714  -23.002 24.107  1.00 41.45  ? 1548 GLN A CA  1 
ATOM   630  C  C   . GLN A 1 78  ? -2.470  -23.485 22.883  1.00 53.80  ? 1548 GLN A C   1 
ATOM   631  O  O   . GLN A 1 78  ? -3.315  -22.744 22.361  1.00 44.41  ? 1548 GLN A O   1 
ATOM   632  C  CB  . GLN A 1 78  ? -0.737  -21.878 23.682  1.00 33.64  ? 1548 GLN A CB  1 
ATOM   633  C  CG  . GLN A 1 78  ? -0.112  -21.149 24.862  1.00 35.11  ? 1548 GLN A CG  1 
ATOM   634  C  CD  . GLN A 1 78  ? 1.057   -20.262 24.465  1.00 45.54  ? 1548 GLN A CD  1 
ATOM   635  O  OE1 . GLN A 1 78  ? 1.647   -20.428 23.394  1.00 36.21  ? 1548 GLN A OE1 1 
ATOM   636  N  NE2 . GLN A 1 78  ? 1.375   -19.296 25.320  1.00 38.38  ? 1548 GLN A NE2 1 
ATOM   637  N  N   . SER A 1 79  ? -2.187  -24.696 22.401  1.00 38.84  ? 1549 SER A N   1 
ATOM   638  C  CA  . SER A 1 79  ? -2.922  -25.139 21.219  1.00 43.17  ? 1549 SER A CA  1 
ATOM   639  C  C   . SER A 1 79  ? -4.365  -25.584 21.501  1.00 43.04  ? 1549 SER A C   1 
ATOM   640  O  O   . SER A 1 79  ? -5.168  -25.571 20.562  1.00 44.75  ? 1549 SER A O   1 
ATOM   641  C  CB  . SER A 1 79  ? -2.200  -26.304 20.521  1.00 45.75  ? 1549 SER A CB  1 
ATOM   642  O  OG  . SER A 1 79  ? -2.367  -27.530 21.240  1.00 47.49  ? 1549 SER A OG  1 
ATOM   643  N  N   . VAL A 1 80  ? -4.737  -25.975 22.731  1.00 46.09  ? 1550 VAL A N   1 
ATOM   644  C  CA  . VAL A 1 80  ? -6.122  -26.390 23.023  1.00 41.91  ? 1550 VAL A CA  1 
ATOM   645  C  C   . VAL A 1 80  ? -6.668  -25.664 24.250  1.00 45.88  ? 1550 VAL A C   1 
ATOM   646  O  O   . VAL A 1 80  ? -5.993  -25.546 25.281  1.00 45.23  ? 1550 VAL A O   1 
ATOM   647  C  CB  . VAL A 1 80  ? -6.274  -27.916 23.229  1.00 44.17  ? 1550 VAL A CB  1 
ATOM   648  C  CG1 . VAL A 1 80  ? -6.113  -28.675 21.915  1.00 59.32  ? 1550 VAL A CG1 1 
ATOM   649  C  CG2 . VAL A 1 80  ? -5.289  -28.423 24.241  1.00 54.43  ? 1550 VAL A CG2 1 
ATOM   650  N  N   . LYS A 1 81  ? -7.939  -25.259 24.159  1.00 51.54  ? 1551 LYS A N   1 
ATOM   651  C  CA  . LYS A 1 81  ? -8.542  -24.414 25.186  1.00 46.36  ? 1551 LYS A CA  1 
ATOM   652  C  C   . LYS A 1 81  ? -8.415  -25.029 26.575  1.00 48.89  ? 1551 LYS A C   1 
ATOM   653  O  O   . LYS A 1 81  ? -8.108  -24.326 27.552  1.00 42.66  ? 1551 LYS A O   1 
ATOM   654  C  CB  . LYS A 1 81  ? -10.014 -24.167 24.841  1.00 50.45  ? 1551 LYS A CB  1 
ATOM   655  C  CG  . LYS A 1 81  ? -10.764 -23.385 25.885  1.00 53.91  ? 1551 LYS A CG  1 
ATOM   656  C  CD  . LYS A 1 81  ? -10.283 -21.943 25.937  1.00 50.54  ? 1551 LYS A CD  1 
ATOM   657  C  CE  . LYS A 1 81  ? -11.193 -21.099 26.840  1.00 71.97  ? 1551 LYS A CE  1 
ATOM   658  N  NZ  . LYS A 1 81  ? -10.828 -19.656 26.740  1.00 81.82  ? 1551 LYS A NZ  1 
ATOM   659  N  N   A GLN A 1 82  ? -8.608  -26.343 26.678  0.53 36.77  ? 1552 GLN A N   1 
ATOM   660  N  N   B GLN A 1 82  ? -8.602  -26.349 26.682  0.47 36.98  ? 1552 GLN A N   1 
ATOM   661  C  CA  A GLN A 1 82  ? -8.663  -27.000 27.975  0.53 45.51  ? 1552 GLN A CA  1 
ATOM   662  C  CA  B GLN A 1 82  ? -8.655  -26.986 27.994  0.47 45.42  ? 1552 GLN A CA  1 
ATOM   663  C  C   A GLN A 1 82  ? -7.310  -27.070 28.693  0.53 44.64  ? 1552 GLN A C   1 
ATOM   664  C  C   B GLN A 1 82  ? -7.310  -27.022 28.718  0.47 44.87  ? 1552 GLN A C   1 
ATOM   665  O  O   A GLN A 1 82  ? -7.280  -27.513 29.850  0.53 48.37  ? 1552 GLN A O   1 
ATOM   666  O  O   B GLN A 1 82  ? -7.283  -27.396 29.899  0.47 48.38  ? 1552 GLN A O   1 
ATOM   667  C  CB  A GLN A 1 82  ? -9.246  -28.402 27.798  0.53 48.11  ? 1552 GLN A CB  1 
ATOM   668  C  CB  B GLN A 1 82  ? -9.208  -28.410 27.869  0.47 48.11  ? 1552 GLN A CB  1 
ATOM   669  C  CG  A GLN A 1 82  ? -8.581  -29.189 26.662  0.53 55.63  ? 1552 GLN A CG  1 
ATOM   670  C  CG  B GLN A 1 82  ? -8.233  -29.407 27.231  0.47 50.73  ? 1552 GLN A CG  1 
ATOM   671  C  CD  A GLN A 1 82  ? -9.363  -29.137 25.348  0.53 59.41  ? 1552 GLN A CD  1 
ATOM   672  C  CD  B GLN A 1 82  ? -8.919  -30.687 26.792  0.47 48.38  ? 1552 GLN A CD  1 
ATOM   673  O  OE1 A GLN A 1 82  ? -9.823  -28.068 24.901  0.53 35.32  ? 1552 GLN A OE1 1 
ATOM   674  O  OE1 B GLN A 1 82  ? -8.722  -31.745 27.388  0.47 50.58  ? 1552 GLN A OE1 1 
ATOM   675  N  NE2 A GLN A 1 82  ? -9.522  -30.308 24.724  0.53 50.20  ? 1552 GLN A NE2 1 
ATOM   676  N  NE2 B GLN A 1 82  ? -9.739  -30.593 25.753  0.47 44.32  ? 1552 GLN A NE2 1 
ATOM   677  N  N   . LEU A 1 83  ? -6.203  -26.654 28.064  1.00 41.91  ? 1553 LEU A N   1 
ATOM   678  C  CA  . LEU A 1 83  ? -4.904  -26.559 28.735  1.00 44.15  ? 1553 LEU A CA  1 
ATOM   679  C  C   . LEU A 1 83  ? -4.472  -25.115 29.045  1.00 42.25  ? 1553 LEU A C   1 
ATOM   680  O  O   . LEU A 1 83  ? -3.315  -24.904 29.427  1.00 39.42  ? 1553 LEU A O   1 
ATOM   681  C  CB  . LEU A 1 83  ? -3.808  -27.257 27.895  1.00 40.18  ? 1553 LEU A CB  1 
ATOM   682  C  CG  . LEU A 1 83  ? -4.075  -28.760 27.672  1.00 44.47  ? 1553 LEU A CG  1 
ATOM   683  C  CD1 . LEU A 1 83  ? -2.996  -29.402 26.782  1.00 34.38  ? 1553 LEU A CD1 1 
ATOM   684  C  CD2 . LEU A 1 83  ? -4.207  -29.496 29.000  1.00 38.68  ? 1553 LEU A CD2 1 
ATOM   685  N  N   A GLU A 1 84  ? -5.359  -24.132 28.834  0.43 40.98  ? 1554 GLU A N   1 
ATOM   686  N  N   B GLU A 1 84  ? -5.369  -24.131 28.942  0.57 40.50  ? 1554 GLU A N   1 
ATOM   687  C  CA  A GLU A 1 84  ? -5.038  -22.734 29.115  0.43 43.47  ? 1554 GLU A CA  1 
ATOM   688  C  CA  B GLU A 1 84  ? -5.001  -22.740 29.211  0.57 44.11  ? 1554 GLU A CA  1 
ATOM   689  C  C   A GLU A 1 84  ? -4.292  -22.573 30.439  0.43 40.22  ? 1554 GLU A C   1 
ATOM   690  C  C   B GLU A 1 84  ? -4.290  -22.582 30.558  0.57 39.92  ? 1554 GLU A C   1 
ATOM   691  O  O   A GLU A 1 84  ? -3.212  -21.974 30.495  0.43 45.28  ? 1554 GLU A O   1 
ATOM   692  O  O   B GLU A 1 84  ? -3.225  -21.959 30.640  0.57 41.15  ? 1554 GLU A O   1 
ATOM   693  C  CB  A GLU A 1 84  ? -6.334  -21.901 29.128  0.43 41.85  ? 1554 GLU A CB  1 
ATOM   694  C  CB  B GLU A 1 84  ? -6.252  -21.839 29.151  0.57 43.09  ? 1554 GLU A CB  1 
ATOM   695  C  CG  A GLU A 1 84  ? -6.241  -20.562 28.388  0.43 45.52  ? 1554 GLU A CG  1 
ATOM   696  C  CG  B GLU A 1 84  ? -7.435  -22.330 29.966  0.57 41.38  ? 1554 GLU A CG  1 
ATOM   697  C  CD  A GLU A 1 84  ? -7.604  -19.939 28.108  0.43 46.63  ? 1554 GLU A CD  1 
ATOM   698  C  CD  B GLU A 1 84  ? -8.636  -21.380 29.954  0.57 52.82  ? 1554 GLU A CD  1 
ATOM   699  O  OE1 A GLU A 1 84  ? -8.484  -20.006 28.993  0.43 46.70  ? 1554 GLU A OE1 1 
ATOM   700  O  OE1 B GLU A 1 84  ? -8.638  -20.403 29.174  0.57 46.88  ? 1554 GLU A OE1 1 
ATOM   701  O  OE2 A GLU A 1 84  ? -7.801  -19.393 27.001  0.43 45.44  ? 1554 GLU A OE2 1 
ATOM   702  O  OE2 B GLU A 1 84  ? -9.579  -21.619 30.741  0.57 54.40  ? 1554 GLU A OE2 1 
ATOM   703  N  N   A THR A 1 85  ? -4.846  -23.142 31.512  0.43 40.69  ? 1555 THR A N   1 
ATOM   704  N  N   B THR A 1 85  ? -4.857  -23.150 31.628  0.57 39.75  ? 1555 THR A N   1 
ATOM   705  C  CA  A THR A 1 85  ? -4.245  -22.989 32.832  0.43 37.06  ? 1555 THR A CA  1 
ATOM   706  C  CA  B THR A 1 85  ? -4.225  -23.012 32.938  0.57 37.12  ? 1555 THR A CA  1 
ATOM   707  C  C   A THR A 1 85  ? -2.837  -23.583 32.879  0.43 45.53  ? 1555 THR A C   1 
ATOM   708  C  C   B THR A 1 85  ? -2.821  -23.609 32.932  0.57 46.25  ? 1555 THR A C   1 
ATOM   709  O  O   A THR A 1 85  ? -1.925  -22.993 33.473  0.43 46.63  ? 1555 THR A O   1 
ATOM   710  O  O   B THR A 1 85  ? -1.893  -23.041 33.524  0.57 44.62  ? 1555 THR A O   1 
ATOM   711  C  CB  A THR A 1 85  ? -5.150  -23.634 33.876  0.43 39.29  ? 1555 THR A CB  1 
ATOM   712  C  CB  B THR A 1 85  ? -5.077  -23.670 34.015  0.57 38.27  ? 1555 THR A CB  1 
ATOM   713  O  OG1 A THR A 1 85  ? -6.421  -22.954 33.888  0.43 54.97  ? 1555 THR A OG1 1 
ATOM   714  O  OG1 B THR A 1 85  ? -5.393  -25.008 33.621  0.57 37.72  ? 1555 THR A OG1 1 
ATOM   715  C  CG2 A THR A 1 85  ? -4.532  -23.537 35.244  0.43 40.50  ? 1555 THR A CG2 1 
ATOM   716  C  CG2 B THR A 1 85  ? -6.393  -22.865 34.247  0.57 51.17  ? 1555 THR A CG2 1 
ATOM   717  N  N   . VAL A 1 86  ? -2.643  -24.748 32.253  1.00 44.99  ? 1556 VAL A N   1 
ATOM   718  C  CA  . VAL A 1 86  ? -1.309  -25.330 32.156  1.00 36.21  ? 1556 VAL A CA  1 
ATOM   719  C  C   . VAL A 1 86  ? -0.361  -24.325 31.518  1.00 36.58  ? 1556 VAL A C   1 
ATOM   720  O  O   . VAL A 1 86  ? 0.679   -23.988 32.092  1.00 40.71  ? 1556 VAL A O   1 
ATOM   721  C  CB  . VAL A 1 86  ? -1.334  -26.648 31.370  1.00 35.86  ? 1556 VAL A CB  1 
ATOM   722  C  CG1 . VAL A 1 86  ? 0.126   -27.080 31.030  1.00 35.72  ? 1556 VAL A CG1 1 
ATOM   723  C  CG2 . VAL A 1 86  ? -2.064  -27.729 32.169  1.00 58.58  ? 1556 VAL A CG2 1 
ATOM   724  N  N   . ALA A 1 87  ? -0.764  -23.750 30.376  1.00 40.06  ? 1557 ALA A N   1 
ATOM   725  C  CA  . ALA A 1 87  ? 0.111   -22.771 29.744  1.00 45.66  ? 1557 ALA A CA  1 
ATOM   726  C  C   . ALA A 1 87  ? 0.393   -21.621 30.709  1.00 47.70  ? 1557 ALA A C   1 
ATOM   727  O  O   . ALA A 1 87  ? 1.549   -21.186 30.866  1.00 45.13  ? 1557 ALA A O   1 
ATOM   728  C  CB  . ALA A 1 87  ? -0.506  -22.267 28.437  1.00 42.54  ? 1557 ALA A CB  1 
ATOM   729  N  N   . ALA A 1 88  ? -0.631  -21.193 31.451  1.00 36.18  ? 1558 ALA A N   1 
ATOM   730  C  CA  . ALA A 1 88  ? -0.410  -20.058 32.333  1.00 39.53  ? 1558 ALA A CA  1 
ATOM   731  C  C   . ALA A 1 88  ? 0.580   -20.443 33.410  1.00 40.14  ? 1558 ALA A C   1 
ATOM   732  O  O   . ALA A 1 88  ? 1.511   -19.680 33.703  1.00 40.88  ? 1558 ALA A O   1 
ATOM   733  C  CB  . ALA A 1 88  ? -1.729  -19.554 32.946  1.00 41.44  ? 1558 ALA A CB  1 
ATOM   734  N  N   A ARG A 1 89  ? 0.445   -21.643 33.973  0.55 39.08  ? 1559 ARG A N   1 
ATOM   735  N  N   B ARG A 1 89  ? 0.421   -21.648 33.982  0.45 38.74  ? 1559 ARG A N   1 
ATOM   736  C  CA  A ARG A 1 89  ? 1.355   -21.984 35.054  0.55 38.06  ? 1559 ARG A CA  1 
ATOM   737  C  CA  B ARG A 1 89  ? 1.325   -22.084 35.043  0.45 38.04  ? 1559 ARG A CA  1 
ATOM   738  C  C   A ARG A 1 89  ? 2.775   -22.114 34.526  0.55 40.80  ? 1559 ARG A C   1 
ATOM   739  C  C   B ARG A 1 89  ? 2.753   -22.119 34.523  0.45 40.43  ? 1559 ARG A C   1 
ATOM   740  O  O   A ARG A 1 89  ? 3.730   -21.709 35.206  0.55 40.23  ? 1559 ARG A O   1 
ATOM   741  O  O   B ARG A 1 89  ? 3.688   -21.678 35.208  0.45 41.09  ? 1559 ARG A O   1 
ATOM   742  C  CB  A ARG A 1 89  ? 0.876   -23.249 35.764  0.55 44.87  ? 1559 ARG A CB  1 
ATOM   743  C  CB  B ARG A 1 89  ? 0.904   -23.462 35.586  0.45 42.88  ? 1559 ARG A CB  1 
ATOM   744  C  CG  A ARG A 1 89  ? -0.436  -23.026 36.565  0.55 39.74  ? 1559 ARG A CG  1 
ATOM   745  C  CG  B ARG A 1 89  ? -0.010  -23.477 36.869  0.45 50.90  ? 1559 ARG A CG  1 
ATOM   746  C  CD  A ARG A 1 89  ? -1.007  -24.322 37.148  0.55 41.83  ? 1559 ARG A CD  1 
ATOM   747  C  CD  B ARG A 1 89  ? -0.360  -24.940 37.325  0.45 48.36  ? 1559 ARG A CD  1 
ATOM   748  N  NE  A ARG A 1 89  ? -1.915  -24.957 36.200  0.55 54.04  ? 1559 ARG A NE  1 
ATOM   749  N  NE  B ARG A 1 89  ? -0.324  -25.209 38.778  0.45 56.21  ? 1559 ARG A NE  1 
ATOM   750  C  CZ  A ARG A 1 89  ? -2.549  -26.118 36.376  0.55 52.93  ? 1559 ARG A CZ  1 
ATOM   751  C  CZ  B ARG A 1 89  ? -0.018  -26.395 39.337  0.45 49.57  ? 1559 ARG A CZ  1 
ATOM   752  N  NH1 A ARG A 1 89  ? -2.391  -26.845 37.486  0.55 44.78  ? 1559 ARG A NH1 1 
ATOM   753  N  NH1 B ARG A 1 89  ? 0.313   -27.432 38.588  0.45 40.67  ? 1559 ARG A NH1 1 
ATOM   754  N  NH2 A ARG A 1 89  ? -3.353  -26.549 35.419  0.55 38.52  ? 1559 ARG A NH2 1 
ATOM   755  N  NH2 B ARG A 1 89  ? -0.017  -26.547 40.658  0.45 42.33  ? 1559 ARG A NH2 1 
ATOM   756  N  N   . LEU A 1 90  ? 2.932   -22.557 33.274  1.00 41.25  ? 1560 LEU A N   1 
ATOM   757  C  CA  . LEU A 1 90  ? 4.281   -22.631 32.738  1.00 48.18  ? 1560 LEU A CA  1 
ATOM   758  C  C   . LEU A 1 90  ? 4.899   -21.237 32.676  1.00 37.89  ? 1560 LEU A C   1 
ATOM   759  O  O   . LEU A 1 90  ? 6.017   -21.049 33.161  1.00 45.39  ? 1560 LEU A O   1 
ATOM   760  C  CB  . LEU A 1 90  ? 4.307   -23.357 31.390  1.00 40.81  ? 1560 LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 90  ? 4.142   -24.900 31.523  1.00 39.40  ? 1560 LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 90  ? 3.631   -25.530 30.240  1.00 35.70  ? 1560 LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 90  ? 5.434   -25.577 31.967  1.00 36.92  ? 1560 LEU A CD2 1 
ATOM   764  N  N   . SER A 1 91  ? 4.145   -20.206 32.285  1.00 42.69  ? 1561 SER A N   1 
ATOM   765  C  CA  . SER A 1 91  ? 4.879   -18.939 32.274  1.00 43.39  ? 1561 SER A CA  1 
ATOM   766  C  C   . SER A 1 91  ? 5.123   -18.425 33.683  1.00 43.46  ? 1561 SER A C   1 
ATOM   767  O  O   . SER A 1 91  ? 6.198   -17.891 33.961  1.00 45.03  ? 1561 SER A O   1 
ATOM   768  C  CB  . SER A 1 91  ? 4.186   -17.880 31.429  1.00 37.50  ? 1561 SER A CB  1 
ATOM   769  O  OG  . SER A 1 91  ? 3.830   -18.372 30.148  1.00 43.16  ? 1561 SER A OG  1 
ATOM   770  N  N   . VAL A 1 92  ? 4.278   -18.791 34.636  1.00 50.59  ? 1562 VAL A N   1 
ATOM   771  C  CA  . VAL A 1 92  ? 4.589   -18.413 36.008  1.00 48.43  ? 1562 VAL A CA  1 
ATOM   772  C  C   . VAL A 1 92  ? 5.866   -19.110 36.447  1.00 46.77  ? 1562 VAL A C   1 
ATOM   773  O  O   . VAL A 1 92  ? 6.786   -18.467 36.972  1.00 46.79  ? 1562 VAL A O   1 
ATOM   774  C  CB  . VAL A 1 92  ? 3.405   -18.702 36.957  1.00 49.86  ? 1562 VAL A CB  1 
ATOM   775  C  CG1 . VAL A 1 92  ? 3.807   -18.357 38.390  1.00 41.26  ? 1562 VAL A CG1 1 
ATOM   776  C  CG2 . VAL A 1 92  ? 2.214   -17.881 36.515  1.00 43.47  ? 1562 VAL A CG2 1 
ATOM   777  N  N   . SER A 1 93  ? 5.991   -20.419 36.155  1.00 47.31  ? 1563 SER A N   1 
ATOM   778  C  CA  . SER A 1 93  ? 7.167   -21.088 36.701  1.00 40.66  ? 1563 SER A CA  1 
ATOM   779  C  C   . SER A 1 93  ? 8.419   -20.627 36.003  1.00 44.28  ? 1563 SER A C   1 
ATOM   780  O  O   . SER A 1 93  ? 9.480   -20.597 36.635  1.00 45.79  ? 1563 SER A O   1 
ATOM   781  C  CB  . SER A 1 93  ? 7.102   -22.619 36.569  1.00 41.30  ? 1563 SER A CB  1 
ATOM   782  O  OG  . SER A 1 93  ? 5.845   -23.172 36.848  1.00 45.27  ? 1563 SER A OG  1 
ATOM   783  N  N   . LEU A 1 94  ? 8.293   -20.121 34.769  1.00 49.02  ? 1564 LEU A N   1 
ATOM   784  C  CA  . LEU A 1 94  ? 9.495   -19.694 34.089  1.00 40.03  ? 1564 LEU A CA  1 
ATOM   785  C  C   . LEU A 1 94  ? 10.111  -18.486 34.783  1.00 55.13  ? 1564 LEU A C   1 
ATOM   786  O  O   . LEU A 1 94  ? 11.294  -18.200 34.570  1.00 49.87  ? 1564 LEU A O   1 
ATOM   787  C  CB  . LEU A 1 94  ? 9.185   -19.416 32.620  1.00 42.89  ? 1564 LEU A CB  1 
ATOM   788  C  CG  . LEU A 1 94  ? 9.341   -20.647 31.716  1.00 41.16  ? 1564 LEU A CG  1 
ATOM   789  C  CD1 . LEU A 1 94  ? 8.561   -20.475 30.419  1.00 38.83  ? 1564 LEU A CD1 1 
ATOM   790  C  CD2 . LEU A 1 94  ? 10.832  -20.960 31.421  1.00 39.28  ? 1564 LEU A CD2 1 
ATOM   791  N  N   . LEU A 1 95  ? 9.354   -17.811 35.658  1.00 49.19  ? 1565 LEU A N   1 
ATOM   792  C  CA  . LEU A 1 95  ? 9.916   -16.669 36.372  1.00 42.67  ? 1565 LEU A CA  1 
ATOM   793  C  C   . LEU A 1 95  ? 11.103  -17.080 37.234  1.00 49.95  ? 1565 LEU A C   1 
ATOM   794  O  O   . LEU A 1 95  ? 11.969  -16.247 37.519  1.00 51.91  ? 1565 LEU A O   1 
ATOM   795  C  CB  . LEU A 1 95  ? 8.838   -15.987 37.220  1.00 42.63  ? 1565 LEU A CB  1 
ATOM   796  C  CG  . LEU A 1 95  ? 7.711   -15.347 36.395  1.00 50.04  ? 1565 LEU A CG  1 
ATOM   797  C  CD1 . LEU A 1 95  ? 6.580   -14.816 37.291  1.00 49.02  ? 1565 LEU A CD1 1 
ATOM   798  C  CD2 . LEU A 1 95  ? 8.275   -14.238 35.495  1.00 44.40  ? 1565 LEU A CD2 1 
ATOM   799  N  N   . ARG A 1 96  ? 11.167  -18.347 37.673  1.00 56.89  ? 1566 ARG A N   1 
ATOM   800  C  CA  . ARG A 1 96  ? 12.329  -18.743 38.475  1.00 56.86  ? 1566 ARG A CA  1 
ATOM   801  C  C   . ARG A 1 96  ? 13.601  -18.885 37.638  1.00 54.13  ? 1566 ARG A C   1 
ATOM   802  O  O   . ARG A 1 96  ? 14.709  -18.905 38.194  1.00 52.21  ? 1566 ARG A O   1 
ATOM   803  C  CB  . ARG A 1 96  ? 12.041  -20.045 39.252  1.00 57.71  ? 1566 ARG A CB  1 
ATOM   804  C  CG  . ARG A 1 96  ? 12.097  -21.364 38.456  1.00 59.04  ? 1566 ARG A CG  1 
ATOM   805  C  CD  . ARG A 1 96  ? 11.872  -22.626 39.350  1.00 59.48  ? 1566 ARG A CD  1 
ATOM   806  N  NE  . ARG A 1 96  ? 10.516  -22.720 39.904  1.00 43.78  ? 1566 ARG A NE  1 
ATOM   807  C  CZ  . ARG A 1 96  ? 9.541   -23.461 39.382  1.00 45.29  ? 1566 ARG A CZ  1 
ATOM   808  N  NH1 . ARG A 1 96  ? 9.769   -24.186 38.291  1.00 51.70  ? 1566 ARG A NH1 1 
ATOM   809  N  NH2 . ARG A 1 96  ? 8.323   -23.461 39.932  1.00 49.91  ? 1566 ARG A NH2 1 
ATOM   810  N  N   . HIS A 1 97  ? 13.484  -18.919 36.317  1.00 50.06  ? 1567 HIS A N   1 
ATOM   811  C  CA  . HIS A 1 97  ? 14.643  -19.087 35.462  1.00 43.90  ? 1567 HIS A CA  1 
ATOM   812  C  C   . HIS A 1 97  ? 15.062  -17.795 34.788  1.00 57.23  ? 1567 HIS A C   1 
ATOM   813  O  O   . HIS A 1 97  ? 15.817  -17.841 33.811  1.00 53.98  ? 1567 HIS A O   1 
ATOM   814  C  CB  . HIS A 1 97  ? 14.347  -20.161 34.424  1.00 47.64  ? 1567 HIS A CB  1 
ATOM   815  C  CG  . HIS A 1 97  ? 14.103  -21.507 35.030  1.00 57.88  ? 1567 HIS A CG  1 
ATOM   816  N  ND1 . HIS A 1 97  ? 15.079  -22.194 35.721  1.00 49.62  ? 1567 HIS A ND1 1 
ATOM   817  C  CD2 . HIS A 1 97  ? 12.992  -22.280 35.077  1.00 43.35  ? 1567 HIS A CD2 1 
ATOM   818  C  CE1 . HIS A 1 97  ? 14.581  -23.336 36.163  1.00 44.40  ? 1567 HIS A CE1 1 
ATOM   819  N  NE2 . HIS A 1 97  ? 13.321  -23.417 35.777  1.00 49.17  ? 1567 HIS A NE2 1 
ATOM   820  N  N   . THR A 1 98  ? 14.623  -16.639 35.315  1.00 44.95  ? 1568 THR A N   1 
ATOM   821  C  CA  . THR A 1 98  ? 14.949  -15.346 34.705  1.00 55.59  ? 1568 THR A CA  1 
ATOM   822  C  C   . THR A 1 98  ? 16.413  -14.934 34.857  1.00 47.19  ? 1568 THR A C   1 
ATOM   823  O  O   . THR A 1 98  ? 16.788  -13.891 34.316  1.00 60.60  ? 1568 THR A O   1 
ATOM   824  C  CB  . THR A 1 98  ? 14.090  -14.229 35.280  1.00 45.15  ? 1568 THR A CB  1 
ATOM   825  O  OG1 . THR A 1 98  ? 14.034  -14.361 36.703  1.00 47.67  ? 1568 THR A OG1 1 
ATOM   826  C  CG2 . THR A 1 98  ? 12.718  -14.321 34.716  1.00 50.63  ? 1568 THR A CG2 1 
ATOM   827  N  N   . GLN A 1 99  ? 17.247  -15.673 35.582  1.00 55.18  ? 1569 GLN A N   1 
ATOM   828  C  CA  . GLN A 1 99  ? 18.671  -15.430 35.400  1.00 69.32  ? 1569 GLN A CA  1 
ATOM   829  C  C   . GLN A 1 99  ? 19.152  -15.850 34.015  1.00 53.25  ? 1569 GLN A C   1 
ATOM   830  O  O   . GLN A 1 99  ? 20.274  -15.503 33.634  1.00 49.61  ? 1569 GLN A O   1 
ATOM   831  C  CB  . GLN A 1 99  ? 19.489  -16.124 36.487  1.00 74.44  ? 1569 GLN A CB  1 
ATOM   832  C  CG  . GLN A 1 99  ? 20.119  -15.127 37.444  1.00 87.64  ? 1569 GLN A CG  1 
ATOM   833  C  CD  . GLN A 1 99  ? 20.424  -15.707 38.815  1.00 96.18  ? 1569 GLN A CD  1 
ATOM   834  O  OE1 . GLN A 1 99  ? 20.171  -16.884 39.079  1.00 87.84  ? 1569 GLN A OE1 1 
ATOM   835  N  NE2 . GLN A 1 99  ? 20.975  -14.874 39.699  1.00 100.61 ? 1569 GLN A NE2 1 
ATOM   836  N  N   . LEU A 1 100 ? 18.322  -16.555 33.247  1.00 50.95  ? 1570 LEU A N   1 
ATOM   837  C  CA  . LEU A 1 100 ? 18.679  -17.012 31.911  1.00 54.16  ? 1570 LEU A CA  1 
ATOM   838  C  C   . LEU A 1 100 ? 17.734  -16.547 30.808  1.00 61.40  ? 1570 LEU A C   1 
ATOM   839  O  O   . LEU A 1 100 ? 17.921  -16.969 29.657  1.00 45.06  ? 1570 LEU A O   1 
ATOM   840  C  CB  . LEU A 1 100 ? 18.726  -18.546 31.883  1.00 45.93  ? 1570 LEU A CB  1 
ATOM   841  C  CG  . LEU A 1 100 ? 19.847  -19.175 32.692  1.00 49.20  ? 1570 LEU A CG  1 
ATOM   842  C  CD1 . LEU A 1 100 ? 19.481  -20.604 33.085  1.00 48.77  ? 1570 LEU A CD1 1 
ATOM   843  C  CD2 . LEU A 1 100 ? 21.139  -19.119 31.875  1.00 61.36  ? 1570 LEU A CD2 1 
ATOM   844  N  N   . LEU A 1 101 ? 16.727  -15.718 31.118  1.00 55.00  ? 1571 LEU A N   1 
ATOM   845  C  CA  . LEU A 1 101 ? 15.696  -15.227 30.207  1.00 51.06  ? 1571 LEU A CA  1 
ATOM   846  C  C   . LEU A 1 101 ? 15.606  -13.710 30.287  1.00 54.07  ? 1571 LEU A C   1 
ATOM   847  O  O   . LEU A 1 101 ? 15.836  -13.143 31.356  1.00 56.62  ? 1571 LEU A O   1 
ATOM   848  C  CB  . LEU A 1 101 ? 14.319  -15.813 30.548  1.00 53.08  ? 1571 LEU A CB  1 
ATOM   849  C  CG  . LEU A 1 101 ? 14.255  -17.314 30.706  1.00 54.19  ? 1571 LEU A CG  1 
ATOM   850  C  CD1 . LEU A 1 101 ? 12.904  -17.709 31.233  1.00 58.54  ? 1571 LEU A CD1 1 
ATOM   851  C  CD2 . LEU A 1 101 ? 14.527  -17.949 29.354  1.00 58.93  ? 1571 LEU A CD2 1 
ATOM   852  N  N   . PRO A 1 102 ? 15.254  -13.033 29.187  1.00 58.58  ? 1572 PRO A N   1 
ATOM   853  C  CA  . PRO A 1 102 ? 15.001  -11.579 29.266  1.00 48.91  ? 1572 PRO A CA  1 
ATOM   854  C  C   . PRO A 1 102 ? 13.878  -11.347 30.258  1.00 49.44  ? 1572 PRO A C   1 
ATOM   855  O  O   . PRO A 1 102 ? 12.742  -11.790 30.051  1.00 48.08  ? 1572 PRO A O   1 
ATOM   856  C  CB  . PRO A 1 102 ? 14.580  -11.198 27.838  1.00 44.89  ? 1572 PRO A CB  1 
ATOM   857  C  CG  . PRO A 1 102 ? 14.865  -12.419 26.976  1.00 46.56  ? 1572 PRO A CG  1 
ATOM   858  C  CD  . PRO A 1 102 ? 14.805  -13.600 27.902  1.00 56.49  ? 1572 PRO A CD  1 
ATOM   859  N  N   . VAL A 1 103 ? 14.212  -10.682 31.362  1.00 52.67  ? 1573 VAL A N   1 
ATOM   860  C  CA  . VAL A 1 103 ? 13.332  -10.744 32.524  1.00 55.01  ? 1573 VAL A CA  1 
ATOM   861  C  C   . VAL A 1 103 ? 12.072  -9.907  32.314  1.00 47.05  ? 1573 VAL A C   1 
ATOM   862  O  O   . VAL A 1 103 ? 10.990  -10.236 32.841  1.00 50.71  ? 1573 VAL A O   1 
ATOM   863  C  CB  . VAL A 1 103 ? 14.136  -10.296 33.762  1.00 51.95  ? 1573 VAL A CB  1 
ATOM   864  C  CG1 . VAL A 1 103 ? 14.581  -8.833  33.625  1.00 48.05  ? 1573 VAL A CG1 1 
ATOM   865  C  CG2 . VAL A 1 103 ? 13.351  -10.534 35.050  1.00 60.83  ? 1573 VAL A CG2 1 
ATOM   866  N  N   . ASP A 1 104 ? 12.151  -8.882  31.473  1.00 51.01  ? 1574 ASP A N   1 
ATOM   867  C  CA  . ASP A 1 104 ? 10.950  -8.115  31.160  1.00 53.17  ? 1574 ASP A CA  1 
ATOM   868  C  C   . ASP A 1 104 ? 9.961   -8.967  30.381  1.00 44.11  ? 1574 ASP A C   1 
ATOM   869  O  O   . ASP A 1 104 ? 8.761   -8.989  30.694  1.00 49.11  ? 1574 ASP A O   1 
ATOM   870  C  CB  . ASP A 1 104 ? 11.319  -6.843  30.396  1.00 50.41  ? 1574 ASP A CB  1 
ATOM   871  C  CG  . ASP A 1 104 ? 12.218  -7.119  29.211  1.00 68.61  ? 1574 ASP A CG  1 
ATOM   872  O  OD1 . ASP A 1 104 ? 13.066  -8.032  29.317  1.00 61.87  ? 1574 ASP A OD1 1 
ATOM   873  O  OD2 . ASP A 1 104 ? 12.079  -6.420  28.181  1.00 68.44  ? 1574 ASP A OD2 1 
ATOM   874  N  N   . LYS A 1 105 ? 10.447  -9.671  29.360  1.00 46.13  ? 1575 LYS A N   1 
ATOM   875  C  CA  . LYS A 1 105 ? 9.601   -10.617 28.640  1.00 59.74  ? 1575 LYS A CA  1 
ATOM   876  C  C   . LYS A 1 105 ? 8.959   -11.617 29.590  1.00 47.16  ? 1575 LYS A C   1 
ATOM   877  O  O   . LYS A 1 105 ? 7.755   -11.869 29.521  1.00 45.94  ? 1575 LYS A O   1 
ATOM   878  C  CB  . LYS A 1 105 ? 10.408  -11.364 27.576  1.00 62.32  ? 1575 LYS A CB  1 
ATOM   879  C  CG  . LYS A 1 105 ? 9.527   -12.246 26.679  1.00 60.69  ? 1575 LYS A CG  1 
ATOM   880  C  CD  . LYS A 1 105 ? 10.313  -13.331 25.939  1.00 49.96  ? 1575 LYS A CD  1 
ATOM   881  C  CE  . LYS A 1 105 ? 10.465  -14.577 26.835  1.00 43.15  ? 1575 LYS A CE  1 
ATOM   882  N  NZ  . LYS A 1 105 ? 10.948  -15.818 26.119  1.00 45.88  ? 1575 LYS A NZ  1 
ATOM   883  N  N   . ALA A 1 106 ? 9.754   -12.179 30.499  1.00 54.44  ? 1576 ALA A N   1 
ATOM   884  C  CA  . ALA A 1 106 ? 9.260   -13.257 31.354  1.00 57.37  ? 1576 ALA A CA  1 
ATOM   885  C  C   . ALA A 1 106 ? 8.115   -12.791 32.222  1.00 42.82  ? 1576 ALA A C   1 
ATOM   886  O  O   . ALA A 1 106 ? 7.111   -13.508 32.378  1.00 42.21  ? 1576 ALA A O   1 
ATOM   887  C  CB  . ALA A 1 106 ? 10.381  -13.791 32.238  1.00 41.84  ? 1576 ALA A CB  1 
ATOM   888  N  N   . PHE A 1 107 ? 8.252   -11.597 32.809  1.00 45.98  ? 1577 PHE A N   1 
ATOM   889  C  CA  . PHE A 1 107 ? 7.174   -11.089 33.662  1.00 47.84  ? 1577 PHE A CA  1 
ATOM   890  C  C   . PHE A 1 107 ? 5.983   -10.635 32.842  1.00 44.57  ? 1577 PHE A C   1 
ATOM   891  O  O   . PHE A 1 107 ? 4.830   -10.841 33.248  1.00 44.36  ? 1577 PHE A O   1 
ATOM   892  C  CB  . PHE A 1 107 ? 7.671   -9.961  34.564  1.00 43.99  ? 1577 PHE A CB  1 
ATOM   893  C  CG  . PHE A 1 107 ? 8.363   -10.459 35.807  1.00 49.71  ? 1577 PHE A CG  1 
ATOM   894  C  CD1 . PHE A 1 107 ? 7.636   -10.804 36.936  1.00 47.92  ? 1577 PHE A CD1 1 
ATOM   895  C  CD2 . PHE A 1 107 ? 9.737   -10.620 35.832  1.00 46.48  ? 1577 PHE A CD2 1 
ATOM   896  C  CE1 . PHE A 1 107 ? 8.272   -11.278 38.079  1.00 45.30  ? 1577 PHE A CE1 1 
ATOM   897  C  CE2 . PHE A 1 107 ? 10.385  -11.089 36.973  1.00 53.22  ? 1577 PHE A CE2 1 
ATOM   898  C  CZ  . PHE A 1 107 ? 9.657   -11.422 38.095  1.00 45.77  ? 1577 PHE A CZ  1 
ATOM   899  N  N   . TYR A 1 108 ? 6.226   -10.022 31.684  1.00 46.35  ? 1578 TYR A N   1 
ATOM   900  C  CA  . TYR A 1 108 ? 5.108   -9.661  30.820  1.00 51.36  ? 1578 TYR A CA  1 
ATOM   901  C  C   . TYR A 1 108 ? 4.254   -10.877 30.524  1.00 44.58  ? 1578 TYR A C   1 
ATOM   902  O  O   . TYR A 1 108 ? 3.027   -10.853 30.664  1.00 43.54  ? 1578 TYR A O   1 
ATOM   903  C  CB  . TYR A 1 108 ? 5.626   -9.059  29.521  1.00 42.10  ? 1578 TYR A CB  1 
ATOM   904  C  CG  . TYR A 1 108 ? 4.555   -8.781  28.503  1.00 43.29  ? 1578 TYR A CG  1 
ATOM   905  C  CD1 . TYR A 1 108 ? 3.634   -7.747  28.705  1.00 47.90  ? 1578 TYR A CD1 1 
ATOM   906  C  CD2 . TYR A 1 108 ? 4.453   -9.541  27.336  1.00 46.32  ? 1578 TYR A CD2 1 
ATOM   907  C  CE1 . TYR A 1 108 ? 2.656   -7.482  27.792  1.00 42.33  ? 1578 TYR A CE1 1 
ATOM   908  C  CE2 . TYR A 1 108 ? 3.476   -9.271  26.400  1.00 50.17  ? 1578 TYR A CE2 1 
ATOM   909  C  CZ  . TYR A 1 108 ? 2.578   -8.227  26.646  1.00 50.98  ? 1578 TYR A CZ  1 
ATOM   910  O  OH  . TYR A 1 108 ? 1.591   -7.931  25.748  1.00 54.79  ? 1578 TYR A OH  1 
ATOM   911  N  N   . GLU A 1 109 ? 4.910   -11.960 30.115  1.00 49.66  ? 1579 GLU A N   1 
ATOM   912  C  CA  . GLU A 1 109 ? 4.201   -13.161 29.695  1.00 40.75  ? 1579 GLU A CA  1 
ATOM   913  C  C   . GLU A 1 109 ? 3.485   -13.814 30.865  1.00 38.92  ? 1579 GLU A C   1 
ATOM   914  O  O   . GLU A 1 109 ? 2.335   -14.255 30.725  1.00 43.51  ? 1579 GLU A O   1 
ATOM   915  C  CB  . GLU A 1 109 ? 5.186   -14.128 29.033  1.00 41.64  ? 1579 GLU A CB  1 
ATOM   916  C  CG  . GLU A 1 109 ? 5.504   -13.744 27.626  1.00 41.16  ? 1579 GLU A CG  1 
ATOM   917  C  CD  . GLU A 1 109 ? 6.509   -14.647 26.968  1.00 46.24  ? 1579 GLU A CD  1 
ATOM   918  O  OE1 . GLU A 1 109 ? 7.122   -15.497 27.658  1.00 50.64  ? 1579 GLU A OE1 1 
ATOM   919  O  OE2 . GLU A 1 109 ? 6.681   -14.501 25.743  1.00 48.75  ? 1579 GLU A OE2 1 
ATOM   920  N  N   . ALA A 1 110 ? 4.151   -13.906 32.020  1.00 43.84  ? 1580 ALA A N   1 
ATOM   921  C  CA  . ALA A 1 110 ? 3.474   -14.433 33.196  1.00 41.09  ? 1580 ALA A CA  1 
ATOM   922  C  C   . ALA A 1 110 ? 2.231   -13.603 33.536  1.00 41.72  ? 1580 ALA A C   1 
ATOM   923  O  O   . ALA A 1 110 ? 1.152   -14.159 33.802  1.00 44.42  ? 1580 ALA A O   1 
ATOM   924  C  CB  . ALA A 1 110 ? 4.446   -14.481 34.375  1.00 40.34  ? 1580 ALA A CB  1 
ATOM   925  N  N   . GLY A 1 111 ? 2.352   -12.272 33.493  1.00 43.05  ? 1581 GLY A N   1 
ATOM   926  C  CA  . GLY A 1 111 ? 1.235   -11.418 33.875  1.00 49.87  ? 1581 GLY A CA  1 
ATOM   927  C  C   . GLY A 1 111 ? 0.066   -11.504 32.914  1.00 40.89  ? 1581 GLY A C   1 
ATOM   928  O  O   . GLY A 1 111 ? -1.084  -11.601 33.333  1.00 50.84  ? 1581 GLY A O   1 
ATOM   929  N  N   . ILE A 1 112 ? 0.351   -11.484 31.613  1.00 49.29  ? 1582 ILE A N   1 
ATOM   930  C  CA  . ILE A 1 112 ? -0.698  -11.592 30.606  1.00 42.90  ? 1582 ILE A CA  1 
ATOM   931  C  C   . ILE A 1 112 ? -1.411  -12.946 30.708  1.00 50.63  ? 1582 ILE A C   1 
ATOM   932  O  O   . ILE A 1 112 ? -2.646  -13.020 30.644  1.00 46.67  ? 1582 ILE A O   1 
ATOM   933  C  CB  . ILE A 1 112 ? -0.088  -11.364 29.210  1.00 53.33  ? 1582 ILE A CB  1 
ATOM   934  C  CG1 . ILE A 1 112 ? 0.340   -9.904  29.049  1.00 57.07  ? 1582 ILE A CG1 1 
ATOM   935  C  CG2 . ILE A 1 112 ? -1.047  -11.769 28.121  1.00 71.67  ? 1582 ILE A CG2 1 
ATOM   936  C  CD1 . ILE A 1 112 ? -0.759  -8.999  28.642  1.00 53.53  ? 1582 ILE A CD1 1 
ATOM   937  N  N   . ALA A 1 113 ? -0.654  -14.039 30.856  1.00 47.68  ? 1583 ALA A N   1 
ATOM   938  C  CA  . ALA A 1 113 ? -1.294  -15.350 30.966  1.00 44.63  ? 1583 ALA A CA  1 
ATOM   939  C  C   . ALA A 1 113 ? -2.168  -15.429 32.215  1.00 39.17  ? 1583 ALA A C   1 
ATOM   940  O  O   . ALA A 1 113 ? -3.329  -15.879 32.162  1.00 41.67  ? 1583 ALA A O   1 
ATOM   941  C  CB  . ALA A 1 113 ? -0.227  -16.455 30.981  1.00 37.39  ? 1583 ALA A CB  1 
ATOM   942  N  N   . ALA A 1 114 ? -1.629  -14.963 33.347  1.00 44.23  ? 1584 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 114 ? -2.397  -14.921 34.581  1.00 50.16  ? 1584 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 114 ? -3.687  -14.137 34.396  1.00 54.95  ? 1584 ALA A C   1 
ATOM   945  O  O   . ALA A 1 114 ? -4.765  -14.591 34.801  1.00 43.02  ? 1584 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 114 ? -1.560  -14.306 35.699  1.00 40.93  ? 1584 ALA A CB  1 
ATOM   947  N  N   . LYS A 1 115 ? -3.593  -12.947 33.790  1.00 60.87  ? 1585 LYS A N   1 
ATOM   948  C  CA  . LYS A 1 115 ? -4.787  -12.121 33.605  1.00 60.63  ? 1585 LYS A CA  1 
ATOM   949  C  C   . LYS A 1 115 ? -5.821  -12.836 32.752  1.00 54.66  ? 1585 LYS A C   1 
ATOM   950  O  O   . LYS A 1 115 ? -7.018  -12.807 33.062  1.00 55.18  ? 1585 LYS A O   1 
ATOM   951  C  CB  . LYS A 1 115 ? -4.417  -10.777 32.972  1.00 54.95  ? 1585 LYS A CB  1 
ATOM   952  C  CG  . LYS A 1 115 ? -5.590  -9.823  32.809  1.00 48.58  ? 1585 LYS A CG  1 
ATOM   953  C  CD  . LYS A 1 115 ? -5.374  -8.906  31.609  1.00 78.43  ? 1585 LYS A CD  1 
ATOM   954  C  CE  . LYS A 1 115 ? -6.608  -8.047  31.300  1.00 88.75  ? 1585 LYS A CE  1 
ATOM   955  N  NZ  . LYS A 1 115 ? -6.385  -7.192  30.089  1.00 88.16  ? 1585 LYS A NZ  1 
ATOM   956  N  N   . ALA A 1 116 ? -5.375  -13.492 31.678  1.00 57.53  ? 1586 ALA A N   1 
ATOM   957  C  CA  . ALA A 1 116 ? -6.307  -14.154 30.772  1.00 54.68  ? 1586 ALA A CA  1 
ATOM   958  C  C   . ALA A 1 116 ? -6.992  -15.359 31.404  1.00 58.25  ? 1586 ALA A C   1 
ATOM   959  O  O   . ALA A 1 116 ? -8.073  -15.742 30.943  1.00 51.26  ? 1586 ALA A O   1 
ATOM   960  C  CB  . ALA A 1 116 ? -5.614  -14.582 29.480  1.00 43.27  ? 1586 ALA A CB  1 
ATOM   961  N  N   . VAL A 1 117 ? -6.394  -16.001 32.408  1.00 55.28  ? 1587 VAL A N   1 
ATOM   962  C  CA  . VAL A 1 117 ? -7.136  -17.046 33.116  1.00 53.18  ? 1587 VAL A CA  1 
ATOM   963  C  C   . VAL A 1 117 ? -7.794  -16.515 34.380  1.00 57.40  ? 1587 VAL A C   1 
ATOM   964  O  O   . VAL A 1 117 ? -8.249  -17.307 35.205  1.00 55.25  ? 1587 VAL A O   1 
ATOM   965  C  CB  . VAL A 1 117 ? -6.265  -18.257 33.465  1.00 51.77  ? 1587 VAL A CB  1 
ATOM   966  C  CG1 . VAL A 1 117 ? -5.730  -18.902 32.211  1.00 62.98  ? 1587 VAL A CG1 1 
ATOM   967  C  CG2 . VAL A 1 117 ? -5.158  -17.843 34.402  1.00 46.40  ? 1587 VAL A CG2 1 
ATOM   968  N  N   . GLY A 1 118 ? -7.839  -15.193 34.561  1.00 62.63  ? 1588 GLY A N   1 
ATOM   969  C  CA  . GLY A 1 118 ? -8.510  -14.606 35.709  1.00 56.22  ? 1588 GLY A CA  1 
ATOM   970  C  C   . GLY A 1 118 ? -7.726  -14.605 37.006  1.00 61.60  ? 1588 GLY A C   1 
ATOM   971  O  O   . GLY A 1 118 ? -8.320  -14.430 38.077  1.00 58.86  ? 1588 GLY A O   1 
ATOM   972  N  N   . TRP A 1 119 ? -6.403  -14.766 36.953  1.00 52.41  ? 1589 TRP A N   1 
ATOM   973  C  CA  . TRP A 1 119 ? -5.572  -14.693 38.157  1.00 56.14  ? 1589 TRP A CA  1 
ATOM   974  C  C   . TRP A 1 119 ? -5.080  -13.251 38.323  1.00 66.54  ? 1589 TRP A C   1 
ATOM   975  O  O   . TRP A 1 119 ? -3.934  -12.898 38.035  1.00 62.09  ? 1589 TRP A O   1 
ATOM   976  C  CB  . TRP A 1 119 ? -4.419  -15.689 38.066  1.00 56.57  ? 1589 TRP A CB  1 
ATOM   977  C  CG  . TRP A 1 119 ? -4.854  -17.137 37.969  1.00 55.32  ? 1589 TRP A CG  1 
ATOM   978  C  CD1 . TRP A 1 119 ? -6.081  -17.647 38.274  1.00 70.31  ? 1589 TRP A CD1 1 
ATOM   979  C  CD2 . TRP A 1 119 ? -4.053  -18.251 37.546  1.00 68.22  ? 1589 TRP A CD2 1 
ATOM   980  N  NE1 . TRP A 1 119 ? -6.099  -19.004 38.059  1.00 65.30  ? 1589 TRP A NE1 1 
ATOM   981  C  CE2 . TRP A 1 119 ? -4.866  -19.400 37.613  1.00 65.34  ? 1589 TRP A CE2 1 
ATOM   982  C  CE3 . TRP A 1 119 ? -2.730  -18.387 37.108  1.00 56.72  ? 1589 TRP A CE3 1 
ATOM   983  C  CZ2 . TRP A 1 119 ? -4.402  -20.667 37.260  1.00 56.76  ? 1589 TRP A CZ2 1 
ATOM   984  C  CZ3 . TRP A 1 119 ? -2.267  -19.653 36.762  1.00 56.96  ? 1589 TRP A CZ3 1 
ATOM   985  C  CH2 . TRP A 1 119 ? -3.099  -20.773 36.847  1.00 53.54  ? 1589 TRP A CH2 1 
ATOM   986  N  N   . ASP A 1 120 ? -5.959  -12.406 38.856  1.00 64.74  ? 1590 ASP A N   1 
ATOM   987  C  CA  . ASP A 1 120 ? -5.740  -10.969 38.731  1.00 45.94  ? 1590 ASP A CA  1 
ATOM   988  C  C   . ASP A 1 120 ? -4.727  -10.429 39.740  1.00 52.48  ? 1590 ASP A C   1 
ATOM   989  O  O   . ASP A 1 120 ? -4.017  -9.471  39.426  1.00 54.90  ? 1590 ASP A O   1 
ATOM   990  C  CB  . ASP A 1 120 ? -7.086  -10.242 38.834  1.00 65.98  ? 1590 ASP A CB  1 
ATOM   991  C  CG  . ASP A 1 120 ? -7.946  -10.465 37.603  1.00 63.87  ? 1590 ASP A CG  1 
ATOM   992  O  OD1 . ASP A 1 120 ? -7.458  -11.104 36.642  1.00 67.76  ? 1590 ASP A OD1 1 
ATOM   993  O  OD2 . ASP A 1 120 ? -9.091  -9.988  37.578  1.00 77.37  ? 1590 ASP A OD2 1 
ATOM   994  N  N   . ASN A 1 121 ? -4.635  -11.005 40.943  1.00 53.57  ? 1591 ASN A N   1 
ATOM   995  C  CA  . ASN A 1 121 ? -3.562  -10.616 41.862  1.00 52.13  ? 1591 ASN A CA  1 
ATOM   996  C  C   . ASN A 1 121 ? -2.193  -10.880 41.249  1.00 70.67  ? 1591 ASN A C   1 
ATOM   997  O  O   . ASN A 1 121 ? -1.319  -10.001 41.232  1.00 76.11  ? 1591 ASN A O   1 
ATOM   998  C  CB  . ASN A 1 121 ? -3.684  -11.373 43.182  1.00 50.75  ? 1591 ASN A CB  1 
ATOM   999  C  CG  . ASN A 1 121 ? -4.897  -10.968 43.969  1.00 79.32  ? 1591 ASN A CG  1 
ATOM   1000 O  OD1 . ASN A 1 121 ? -5.486  -9.916  43.721  1.00 75.12  ? 1591 ASN A OD1 1 
ATOM   1001 N  ND2 . ASN A 1 121 ? -5.280  -11.795 44.935  1.00 90.66  ? 1591 ASN A ND2 1 
ATOM   1002 N  N   . MET A 1 122 ? -1.971  -12.111 40.787  1.00 62.22  ? 1592 MET A N   1 
ATOM   1003 C  CA  . MET A 1 122 ? -0.718  -12.425 40.118  1.00 61.94  ? 1592 MET A CA  1 
ATOM   1004 C  C   . MET A 1 122 ? -0.516  -11.553 38.888  1.00 44.53  ? 1592 MET A C   1 
ATOM   1005 O  O   . MET A 1 122 ? 0.598   -11.082 38.637  1.00 47.99  ? 1592 MET A O   1 
ATOM   1006 C  CB  . MET A 1 122 ? -0.676  -13.908 39.754  1.00 54.10  ? 1592 MET A CB  1 
ATOM   1007 C  CG  . MET A 1 122 ? -0.419  -14.790 40.957  1.00 72.64  ? 1592 MET A CG  1 
ATOM   1008 S  SD  . MET A 1 122 ? 0.101   -16.444 40.490  1.00 76.99  ? 1592 MET A SD  1 
ATOM   1009 C  CE  . MET A 1 122 ? -1.486  -17.072 39.983  1.00 56.52  ? 1592 MET A CE  1 
ATOM   1010 N  N   . ALA A 1 123 ? -1.573  -11.341 38.098  1.00 44.21  ? 1593 ALA A N   1 
ATOM   1011 C  CA  . ALA A 1 123 ? -1.445  -10.485 36.926  1.00 46.80  ? 1593 ALA A CA  1 
ATOM   1012 C  C   . ALA A 1 123 ? -0.978  -9.092  37.327  1.00 56.24  ? 1593 ALA A C   1 
ATOM   1013 O  O   . ALA A 1 123 ? -0.055  -8.542  36.721  1.00 59.73  ? 1593 ALA A O   1 
ATOM   1014 C  CB  . ALA A 1 123 ? -2.761  -10.411 36.159  1.00 43.70  ? 1593 ALA A CB  1 
ATOM   1015 N  N   . PHE A 1 124 ? -1.566  -8.534  38.382  1.00 52.97  ? 1594 PHE A N   1 
ATOM   1016 C  CA  . PHE A 1 124 ? -1.194  -7.198  38.825  1.00 53.82  ? 1594 PHE A CA  1 
ATOM   1017 C  C   . PHE A 1 124 ? 0.251   -7.156  39.286  1.00 50.06  ? 1594 PHE A C   1 
ATOM   1018 O  O   . PHE A 1 124 ? 1.007   -6.256  38.911  1.00 59.12  ? 1594 PHE A O   1 
ATOM   1019 C  CB  . PHE A 1 124 ? -2.120  -6.739  39.949  1.00 57.86  ? 1594 PHE A CB  1 
ATOM   1020 C  CG  . PHE A 1 124 ? -1.842  -5.330  40.430  1.00 50.60  ? 1594 PHE A CG  1 
ATOM   1021 C  CD1 . PHE A 1 124 ? -2.315  -4.235  39.715  1.00 51.30  ? 1594 PHE A CD1 1 
ATOM   1022 C  CD2 . PHE A 1 124 ? -1.105  -5.104  41.585  1.00 51.61  ? 1594 PHE A CD2 1 
ATOM   1023 C  CE1 . PHE A 1 124 ? -2.082  -2.931  40.148  1.00 52.74  ? 1594 PHE A CE1 1 
ATOM   1024 C  CE2 . PHE A 1 124 ? -0.848  -3.793  42.026  1.00 57.48  ? 1594 PHE A CE2 1 
ATOM   1025 C  CZ  . PHE A 1 124 ? -1.341  -2.709  41.303  1.00 61.83  ? 1594 PHE A CZ  1 
ATOM   1026 N  N   . ILE A 1 125 ? 0.652   -8.121  40.107  1.00 55.67  ? 1595 ILE A N   1 
ATOM   1027 C  CA  . ILE A 1 125 ? 2.010   -8.121  40.650  1.00 52.62  ? 1595 ILE A CA  1 
ATOM   1028 C  C   . ILE A 1 125 ? 3.039   -8.305  39.531  1.00 54.74  ? 1595 ILE A C   1 
ATOM   1029 O  O   . ILE A 1 125 ? 4.023   -7.557  39.429  1.00 62.22  ? 1595 ILE A O   1 
ATOM   1030 C  CB  . ILE A 1 125 ? 2.129   -9.206  41.734  1.00 58.28  ? 1595 ILE A CB  1 
ATOM   1031 C  CG1 . ILE A 1 125 ? 1.401   -8.752  42.999  1.00 60.13  ? 1595 ILE A CG1 1 
ATOM   1032 C  CG2 . ILE A 1 125 ? 3.566   -9.544  42.025  1.00 55.79  ? 1595 ILE A CG2 1 
ATOM   1033 C  CD1 . ILE A 1 125 ? 1.003   -9.894  43.889  1.00 60.03  ? 1595 ILE A CD1 1 
ATOM   1034 N  N   . PHE A 1 126 ? 2.803   -9.277  38.649  1.00 54.10  ? 1596 PHE A N   1 
ATOM   1035 C  CA  . PHE A 1 126 ? 3.748   -9.547  37.577  1.00 50.44  ? 1596 PHE A CA  1 
ATOM   1036 C  C   . PHE A 1 126 ? 3.816   -8.388  36.592  1.00 49.62  ? 1596 PHE A C   1 
ATOM   1037 O  O   . PHE A 1 126 ? 4.906   -8.025  36.143  1.00 55.70  ? 1596 PHE A O   1 
ATOM   1038 C  CB  . PHE A 1 126 ? 3.378   -10.839 36.837  1.00 46.77  ? 1596 PHE A CB  1 
ATOM   1039 C  CG  . PHE A 1 126 ? 3.403   -12.084 37.697  1.00 50.05  ? 1596 PHE A CG  1 
ATOM   1040 C  CD1 . PHE A 1 126 ? 4.223   -12.169 38.808  1.00 48.41  ? 1596 PHE A CD1 1 
ATOM   1041 C  CD2 . PHE A 1 126 ? 2.601   -13.176 37.376  1.00 52.88  ? 1596 PHE A CD2 1 
ATOM   1042 C  CE1 . PHE A 1 126 ? 4.239   -13.318 39.590  1.00 55.75  ? 1596 PHE A CE1 1 
ATOM   1043 C  CE2 . PHE A 1 126 ? 2.611   -14.330 38.152  1.00 56.03  ? 1596 PHE A CE2 1 
ATOM   1044 C  CZ  . PHE A 1 126 ? 3.434   -14.399 39.262  1.00 52.36  ? 1596 PHE A CZ  1 
ATOM   1045 N  N   . LEU A 1 127 ? 2.674   -7.787  36.242  1.00 48.20  ? 1597 LEU A N   1 
ATOM   1046 C  CA  . LEU A 1 127 ? 2.699   -6.720  35.250  1.00 59.83  ? 1597 LEU A CA  1 
ATOM   1047 C  C   . LEU A 1 127 ? 3.243   -5.415  35.834  1.00 60.17  ? 1597 LEU A C   1 
ATOM   1048 O  O   . LEU A 1 127 ? 3.888   -4.642  35.116  1.00 56.06  ? 1597 LEU A O   1 
ATOM   1049 C  CB  . LEU A 1 127 ? 1.306   -6.543  34.639  1.00 47.40  ? 1597 LEU A CB  1 
ATOM   1050 C  CG  . LEU A 1 127 ? 0.822   -7.730  33.773  1.00 55.15  ? 1597 LEU A CG  1 
ATOM   1051 C  CD1 . LEU A 1 127 ? -0.655  -7.609  33.365  1.00 44.01  ? 1597 LEU A CD1 1 
ATOM   1052 C  CD2 . LEU A 1 127 ? 1.694   -7.937  32.537  1.00 46.34  ? 1597 LEU A CD2 1 
ATOM   1053 N  N   . ASN A 1 128 ? 3.043   -5.173  37.134  1.00 57.32  ? 1598 ASN A N   1 
ATOM   1054 C  CA  . ASN A 1 128 ? 3.688   -4.038  37.779  1.00 53.12  ? 1598 ASN A CA  1 
ATOM   1055 C  C   . ASN A 1 128 ? 5.195   -4.214  37.767  1.00 58.89  ? 1598 ASN A C   1 
ATOM   1056 O  O   . ASN A 1 128 ? 5.941   -3.294  37.410  1.00 64.10  ? 1598 ASN A O   1 
ATOM   1057 C  CB  . ASN A 1 128 ? 3.179   -3.899  39.214  1.00 59.99  ? 1598 ASN A CB  1 
ATOM   1058 C  CG  . ASN A 1 128 ? 3.078   -2.462  39.661  1.00 64.92  ? 1598 ASN A CG  1 
ATOM   1059 O  OD1 . ASN A 1 128 ? 2.633   -1.605  38.907  1.00 76.99  ? 1598 ASN A OD1 1 
ATOM   1060 N  ND2 . ASN A 1 128 ? 3.496   -2.186  40.894  1.00 71.85  ? 1598 ASN A ND2 1 
ATOM   1061 N  N   . ARG A 1 129 ? 5.662   -5.409  38.136  1.00 66.55  ? 1599 ARG A N   1 
ATOM   1062 C  CA  . ARG A 1 129 ? 7.089   -5.691  38.054  1.00 62.00  ? 1599 ARG A CA  1 
ATOM   1063 C  C   . ARG A 1 129 ? 7.610   -5.504  36.635  1.00 67.44  ? 1599 ARG A C   1 
ATOM   1064 O  O   . ARG A 1 129 ? 8.702   -4.961  36.432  1.00 54.24  ? 1599 ARG A O   1 
ATOM   1065 C  CB  . ARG A 1 129 ? 7.358   -7.109  38.541  1.00 61.04  ? 1599 ARG A CB  1 
ATOM   1066 C  CG  . ARG A 1 129 ? 8.768   -7.578  38.321  1.00 56.60  ? 1599 ARG A CG  1 
ATOM   1067 C  CD  . ARG A 1 129 ? 9.800   -6.619  38.930  1.00 62.55  ? 1599 ARG A CD  1 
ATOM   1068 N  NE  . ARG A 1 129 ? 10.913  -7.391  39.469  1.00 76.15  ? 1599 ARG A NE  1 
ATOM   1069 C  CZ  . ARG A 1 129 ? 11.225  -7.447  40.758  1.00 81.00  ? 1599 ARG A CZ  1 
ATOM   1070 N  NH1 . ARG A 1 129 ? 10.523  -6.747  41.642  1.00 78.29  ? 1599 ARG A NH1 1 
ATOM   1071 N  NH2 . ARG A 1 129 ? 12.242  -8.199  41.158  1.00 79.98  ? 1599 ARG A NH2 1 
ATOM   1072 N  N   . PHE A 1 130 ? 6.842   -5.953  35.642  1.00 54.57  ? 1600 PHE A N   1 
ATOM   1073 C  CA  . PHE A 1 130 ? 7.206   -5.752  34.241  1.00 52.47  ? 1600 PHE A CA  1 
ATOM   1074 C  C   . PHE A 1 130 ? 7.389   -4.267  33.914  1.00 60.86  ? 1600 PHE A C   1 
ATOM   1075 O  O   . PHE A 1 130 ? 8.364   -3.875  33.254  1.00 55.78  ? 1600 PHE A O   1 
ATOM   1076 C  CB  . PHE A 1 130 ? 6.138   -6.388  33.355  1.00 45.78  ? 1600 PHE A CB  1 
ATOM   1077 C  CG  . PHE A 1 130 ? 6.033   -5.788  31.987  1.00 60.90  ? 1600 PHE A CG  1 
ATOM   1078 C  CD1 . PHE A 1 130 ? 7.013   -6.035  31.025  1.00 45.52  ? 1600 PHE A CD1 1 
ATOM   1079 C  CD2 . PHE A 1 130 ? 4.938   -4.982  31.651  1.00 46.79  ? 1600 PHE A CD2 1 
ATOM   1080 C  CE1 . PHE A 1 130 ? 6.907   -5.482  29.747  1.00 49.47  ? 1600 PHE A CE1 1 
ATOM   1081 C  CE2 . PHE A 1 130 ? 4.820   -4.441  30.381  1.00 46.21  ? 1600 PHE A CE2 1 
ATOM   1082 C  CZ  . PHE A 1 130 ? 5.815   -4.684  29.422  1.00 46.60  ? 1600 PHE A CZ  1 
ATOM   1083 N  N   . LEU A 1 131 ? 6.431   -3.432  34.321  1.00 49.08  ? 1601 LEU A N   1 
ATOM   1084 C  CA  . LEU A 1 131 ? 6.558   -1.994  34.066  1.00 50.92  ? 1601 LEU A CA  1 
ATOM   1085 C  C   . LEU A 1 131 ? 7.835   -1.445  34.691  1.00 64.28  ? 1601 LEU A C   1 
ATOM   1086 O  O   . LEU A 1 131 ? 8.577   -0.661  34.069  1.00 55.86  ? 1601 LEU A O   1 
ATOM   1087 C  CB  . LEU A 1 131 ? 5.343   -1.249  34.617  1.00 51.28  ? 1601 LEU A CB  1 
ATOM   1088 C  CG  . LEU A 1 131 ? 4.001   -1.526  33.941  1.00 53.92  ? 1601 LEU A CG  1 
ATOM   1089 C  CD1 . LEU A 1 131 ? 2.886   -0.779  34.657  1.00 64.85  ? 1601 LEU A CD1 1 
ATOM   1090 C  CD2 . LEU A 1 131 ? 4.024   -1.194  32.455  1.00 50.20  ? 1601 LEU A CD2 1 
ATOM   1091 N  N   . ASP A 1 132 ? 8.097   -1.844  35.934  1.00 64.38  ? 1602 ASP A N   1 
ATOM   1092 C  CA  . ASP A 1 132 ? 9.309   -1.397  36.598  1.00 57.26  ? 1602 ASP A CA  1 
ATOM   1093 C  C   . ASP A 1 132 ? 10.535  -1.849  35.820  1.00 64.63  ? 1602 ASP A C   1 
ATOM   1094 O  O   . ASP A 1 132 ? 11.510  -1.101  35.685  1.00 56.53  ? 1602 ASP A O   1 
ATOM   1095 C  CB  . ASP A 1 132 ? 9.335   -1.918  38.033  1.00 56.54  ? 1602 ASP A CB  1 
ATOM   1096 C  CG  . ASP A 1 132 ? 8.262   -1.280  38.901  1.00 72.52  ? 1602 ASP A CG  1 
ATOM   1097 O  OD1 . ASP A 1 132 ? 7.495   -0.435  38.375  1.00 66.73  ? 1602 ASP A OD1 1 
ATOM   1098 O  OD2 . ASP A 1 132 ? 8.190   -1.623  40.104  1.00 74.58  ? 1602 ASP A OD2 1 
ATOM   1099 N  N   . LEU A 1 133 ? 10.484  -3.049  35.248  1.00 68.33  ? 1603 LEU A N   1 
ATOM   1100 C  CA  . LEU A 1 133 ? 11.650  -3.521  34.518  1.00 67.05  ? 1603 LEU A CA  1 
ATOM   1101 C  C   . LEU A 1 133 ? 11.829  -2.794  33.189  1.00 56.75  ? 1603 LEU A C   1 
ATOM   1102 O  O   . LEU A 1 133 ? 12.962  -2.599  32.751  1.00 59.27  ? 1603 LEU A O   1 
ATOM   1103 C  CB  . LEU A 1 133 ? 11.579  -5.038  34.314  1.00 57.15  ? 1603 LEU A CB  1 
ATOM   1104 C  CG  . LEU A 1 133 ? 11.595  -5.877  35.604  1.00 61.34  ? 1603 LEU A CG  1 
ATOM   1105 C  CD1 . LEU A 1 133 ? 10.825  -7.183  35.445  1.00 60.71  ? 1603 LEU A CD1 1 
ATOM   1106 C  CD2 . LEU A 1 133 ? 13.042  -6.116  36.063  1.00 61.30  ? 1603 LEU A CD2 1 
ATOM   1107 N  N   . THR A 1 134 ? 10.745  -2.392  32.528  1.00 56.52  ? 1604 THR A N   1 
ATOM   1108 C  CA  . THR A 1 134 ? 10.913  -1.585  31.320  1.00 58.35  ? 1604 THR A CA  1 
ATOM   1109 C  C   . THR A 1 134 ? 11.525  -0.226  31.656  1.00 63.39  ? 1604 THR A C   1 
ATOM   1110 O  O   . THR A 1 134 ? 12.414  0.266   30.943  1.00 62.28  ? 1604 THR A O   1 
ATOM   1111 C  CB  . THR A 1 134 ? 9.582   -1.413  30.596  1.00 51.14  ? 1604 THR A CB  1 
ATOM   1112 O  OG1 . THR A 1 134 ? 8.698   -0.650  31.417  1.00 51.84  ? 1604 THR A OG1 1 
ATOM   1113 C  CG2 . THR A 1 134 ? 8.977   -2.752  30.319  1.00 49.33  ? 1604 THR A CG2 1 
ATOM   1114 N  N   . ASP A 1 135 ? 11.082  0.390   32.751  1.00 65.01  ? 1605 ASP A N   1 
ATOM   1115 C  CA  . ASP A 1 135 ? 11.709  1.649   33.144  1.00 77.75  ? 1605 ASP A CA  1 
ATOM   1116 C  C   . ASP A 1 135 ? 13.175  1.441   33.478  1.00 76.00  ? 1605 ASP A C   1 
ATOM   1117 O  O   . ASP A 1 135 ? 14.016  2.278   33.144  1.00 75.17  ? 1605 ASP A O   1 
ATOM   1118 C  CB  . ASP A 1 135 ? 10.988  2.283   34.330  1.00 77.35  ? 1605 ASP A CB  1 
ATOM   1119 C  CG  . ASP A 1 135 ? 9.553   2.611   34.021  1.00 86.84  ? 1605 ASP A CG  1 
ATOM   1120 O  OD1 . ASP A 1 135 ? 9.181   2.593   32.823  1.00 93.38  ? 1605 ASP A OD1 1 
ATOM   1121 O  OD2 . ASP A 1 135 ? 8.802   2.887   34.978  1.00 89.39  ? 1605 ASP A OD2 1 
ATOM   1122 N  N   . ALA A 1 136 ? 13.500  0.344   34.161  1.00 66.52  ? 1606 ALA A N   1 
ATOM   1123 C  CA  . ALA A 1 136 ? 14.892  0.109   34.525  1.00 69.37  ? 1606 ALA A CA  1 
ATOM   1124 C  C   . ALA A 1 136 ? 15.754  -0.169  33.300  1.00 57.05  ? 1606 ALA A C   1 
ATOM   1125 O  O   . ALA A 1 136 ? 16.929  0.204   33.276  1.00 58.40  ? 1606 ALA A O   1 
ATOM   1126 C  CB  . ALA A 1 136 ? 14.983  -1.045  35.522  1.00 65.53  ? 1606 ALA A CB  1 
ATOM   1127 N  N   . ILE A 1 137 ? 15.197  -0.825  32.282  1.00 55.59  ? 1607 ILE A N   1 
ATOM   1128 C  CA  . ILE A 1 137 ? 15.908  -0.968  31.015  1.00 55.66  ? 1607 ILE A CA  1 
ATOM   1129 C  C   . ILE A 1 137 ? 16.209  0.406   30.435  1.00 69.28  ? 1607 ILE A C   1 
ATOM   1130 O  O   . ILE A 1 137 ? 17.339  0.687   30.011  1.00 80.09  ? 1607 ILE A O   1 
ATOM   1131 C  CB  . ILE A 1 137 ? 15.102  -1.847  30.036  1.00 57.66  ? 1607 ILE A CB  1 
ATOM   1132 C  CG1 . ILE A 1 137 ? 15.213  -3.315  30.427  1.00 55.11  ? 1607 ILE A CG1 1 
ATOM   1133 C  CG2 . ILE A 1 137 ? 15.599  -1.682  28.607  1.00 63.80  ? 1607 ILE A CG2 1 
ATOM   1134 C  CD1 . ILE A 1 137 ? 14.136  -4.179  29.818  1.00 50.70  ? 1607 ILE A CD1 1 
ATOM   1135 N  N   A GLU A 1 138 ? 15.204  1.288   30.427  0.57 67.93  ? 1608 GLU A N   1 
ATOM   1136 N  N   B GLU A 1 138 ? 15.206  1.289   30.426  0.43 67.94  ? 1608 GLU A N   1 
ATOM   1137 C  CA  A GLU A 1 138 ? 15.426  2.626   29.879  0.57 70.23  ? 1608 GLU A CA  1 
ATOM   1138 C  CA  B GLU A 1 138 ? 15.407  2.638   29.897  0.43 70.03  ? 1608 GLU A CA  1 
ATOM   1139 C  C   A GLU A 1 138 ? 16.462  3.405   30.689  0.57 69.31  ? 1608 GLU A C   1 
ATOM   1140 C  C   B GLU A 1 138 ? 16.463  3.399   30.691  0.43 69.21  ? 1608 GLU A C   1 
ATOM   1141 O  O   A GLU A 1 138 ? 17.271  4.149   30.122  0.57 70.21  ? 1608 GLU A O   1 
ATOM   1142 O  O   B GLU A 1 138 ? 17.281  4.127   30.116  0.43 70.16  ? 1608 GLU A O   1 
ATOM   1143 C  CB  A GLU A 1 138 ? 14.106  3.390   29.799  0.57 72.81  ? 1608 GLU A CB  1 
ATOM   1144 C  CB  B GLU A 1 138 ? 14.082  3.403   29.893  0.43 72.16  ? 1608 GLU A CB  1 
ATOM   1145 C  CG  A GLU A 1 138 ? 13.374  3.167   28.479  0.57 68.38  ? 1608 GLU A CG  1 
ATOM   1146 C  CG  B GLU A 1 138 ? 13.139  2.972   28.780  0.43 66.74  ? 1608 GLU A CG  1 
ATOM   1147 C  CD  A GLU A 1 138 ? 14.335  3.026   27.305  0.57 71.10  ? 1608 GLU A CD  1 
ATOM   1148 C  CD  B GLU A 1 138 ? 11.798  3.683   28.810  0.43 65.88  ? 1608 GLU A CD  1 
ATOM   1149 O  OE1 A GLU A 1 138 ? 15.071  4.010   27.011  0.57 64.09  ? 1608 GLU A OE1 1 
ATOM   1150 O  OE1 B GLU A 1 138 ? 11.643  4.651   29.595  0.43 64.13  ? 1608 GLU A OE1 1 
ATOM   1151 O  OE2 A GLU A 1 138 ? 14.362  1.926   26.698  0.57 57.54  ? 1608 GLU A OE2 1 
ATOM   1152 O  OE2 B GLU A 1 138 ? 10.899  3.271   28.038  0.43 57.22  ? 1608 GLU A OE2 1 
ATOM   1153 N  N   . GLU A 1 139 ? 16.467  3.231   32.013  1.00 64.85  ? 1609 GLU A N   1 
ATOM   1154 C  CA  . GLU A 1 139 ? 17.410  3.922   32.886  1.00 63.40  ? 1609 GLU A CA  1 
ATOM   1155 C  C   . GLU A 1 139 ? 18.793  3.276   32.927  1.00 69.56  ? 1609 GLU A C   1 
ATOM   1156 O  O   . GLU A 1 139 ? 19.758  3.939   33.311  1.00 84.41  ? 1609 GLU A O   1 
ATOM   1157 C  CB  . GLU A 1 139 ? 16.845  3.990   34.309  1.00 68.36  ? 1609 GLU A CB  1 
ATOM   1158 C  CG  . GLU A 1 139 ? 15.710  5.014   34.506  1.00 76.24  ? 1609 GLU A CG  1 
ATOM   1159 C  CD  . GLU A 1 139 ? 16.201  6.439   34.776  1.00 80.44  ? 1609 GLU A CD  1 
ATOM   1160 O  OE1 . GLU A 1 139 ? 16.080  7.288   33.858  1.00 86.64  ? 1609 GLU A OE1 1 
ATOM   1161 O  OE2 . GLU A 1 139 ? 16.699  6.710   35.906  1.00 67.73  ? 1609 GLU A OE2 1 
ATOM   1162 N  N   . GLY A 1 140 ? 18.918  2.000   32.575  1.00 87.97  ? 1610 GLY A N   1 
ATOM   1163 C  CA  . GLY A 1 140 ? 20.214  1.355   32.587  1.00 86.42  ? 1610 GLY A CA  1 
ATOM   1164 C  C   . GLY A 1 140 ? 20.660  0.798   33.924  1.00 89.97  ? 1610 GLY A C   1 
ATOM   1165 O  O   . GLY A 1 140 ? 21.796  0.307   34.023  1.00 85.37  ? 1610 GLY A O   1 
ATOM   1166 N  N   . THR A 1 141 ? 19.819  0.855   34.957  1.00 91.94  ? 1611 THR A N   1 
ATOM   1167 C  CA  . THR A 1 141 ? 20.146  0.238   36.234  1.00 86.82  ? 1611 THR A CA  1 
ATOM   1168 C  C   . THR A 1 141 ? 18.945  -0.499  36.799  1.00 86.90  ? 1611 THR A C   1 
ATOM   1169 O  O   . THR A 1 141 ? 17.788  -0.243  36.452  1.00 79.26  ? 1611 THR A O   1 
ATOM   1170 C  CB  . THR A 1 141 ? 20.623  1.232   37.291  1.00 92.24  ? 1611 THR A CB  1 
ATOM   1171 O  OG1 . THR A 1 141 ? 20.895  0.517   38.504  1.00 93.12  ? 1611 THR A OG1 1 
ATOM   1172 C  CG2 . THR A 1 141 ? 19.555  2.276   37.568  1.00 92.96  ? 1611 THR A CG2 1 
ATOM   1173 N  N   . LEU A 1 142 ? 19.255  -1.399  37.716  1.00 83.24  ? 1612 LEU A N   1 
ATOM   1174 C  CA  . LEU A 1 142 ? 18.270  -2.197  38.411  1.00 69.73  ? 1612 LEU A CA  1 
ATOM   1175 C  C   . LEU A 1 142 ? 18.080  -1.736  39.846  1.00 82.32  ? 1612 LEU A C   1 
ATOM   1176 O  O   . LEU A 1 142 ? 17.275  -2.333  40.571  1.00 78.06  ? 1612 LEU A O   1 
ATOM   1177 C  CB  . LEU A 1 142 ? 18.714  -3.664  38.391  1.00 85.34  ? 1612 LEU A CB  1 
ATOM   1178 C  CG  . LEU A 1 142 ? 17.730  -4.825  38.339  1.00 74.68  ? 1612 LEU A CG  1 
ATOM   1179 C  CD1 . LEU A 1 142 ? 16.943  -4.789  37.046  1.00 70.15  ? 1612 LEU A CD1 1 
ATOM   1180 C  CD2 . LEU A 1 142 ? 18.509  -6.121  38.453  1.00 82.53  ? 1612 LEU A CD2 1 
ATOM   1181 N  N   . ASP A 1 143 ? 18.763  -0.659  40.261  1.00 84.59  ? 1613 ASP A N   1 
ATOM   1182 C  CA  . ASP A 1 143 ? 18.736  -0.210  41.649  1.00 93.65  ? 1613 ASP A CA  1 
ATOM   1183 C  C   . ASP A 1 143 ? 17.453  0.525   41.994  1.00 99.13  ? 1613 ASP A C   1 
ATOM   1184 O  O   . ASP A 1 143 ? 17.269  0.917   43.151  1.00 113.43 ? 1613 ASP A O   1 
ATOM   1185 C  CB  . ASP A 1 143 ? 19.943  0.684   41.951  1.00 105.35 ? 1613 ASP A CB  1 
ATOM   1186 C  CG  . ASP A 1 143 ? 21.268  -0.022  41.721  1.00 119.27 ? 1613 ASP A CG  1 
ATOM   1187 O  OD1 . ASP A 1 143 ? 21.994  -0.270  42.710  1.00 125.57 ? 1613 ASP A OD1 1 
ATOM   1188 O  OD2 . ASP A 1 143 ? 21.583  -0.330  40.552  1.00 124.79 ? 1613 ASP A OD2 1 
ATOM   1189 N  N   . GLY A 1 144 ? 16.567  0.712   41.023  1.00 89.39  ? 1614 GLY A N   1 
ATOM   1190 C  CA  . GLY A 1 144 ? 15.265  1.278   41.282  1.00 93.00  ? 1614 GLY A CA  1 
ATOM   1191 C  C   . GLY A 1 144 ? 14.229  0.278   41.741  1.00 98.13  ? 1614 GLY A C   1 
ATOM   1192 O  O   . GLY A 1 144 ? 13.172  0.685   42.228  1.00 101.96 ? 1614 GLY A O   1 
ATOM   1193 N  N   . LEU A 1 145 ? 14.502  -1.018  41.603  1.00 96.58  ? 1615 LEU A N   1 
ATOM   1194 C  CA  . LEU A 1 145 ? 13.478  -2.038  41.795  1.00 95.97  ? 1615 LEU A CA  1 
ATOM   1195 C  C   . LEU A 1 145 ? 13.193  -2.315  43.263  1.00 88.90  ? 1615 LEU A C   1 
ATOM   1196 O  O   . LEU A 1 145 ? 14.096  -2.307  44.108  1.00 95.49  ? 1615 LEU A O   1 
ATOM   1197 C  CB  . LEU A 1 145 ? 13.904  -3.360  41.154  1.00 99.94  ? 1615 LEU A CB  1 
ATOM   1198 C  CG  . LEU A 1 145 ? 13.669  -3.706  39.687  1.00 99.28  ? 1615 LEU A CG  1 
ATOM   1199 C  CD1 . LEU A 1 145 ? 13.849  -5.209  39.494  1.00 98.55  ? 1615 LEU A CD1 1 
ATOM   1200 C  CD2 . LEU A 1 145 ? 12.284  -3.278  39.264  1.00 100.99 ? 1615 LEU A CD2 1 
ATOM   1201 N  N   . ASP A 1 146 ? 11.927  -2.582  43.556  1.00 76.81  ? 1616 ASP A N   1 
ATOM   1202 C  CA  . ASP A 1 146 ? 11.516  -3.066  44.864  1.00 85.82  ? 1616 ASP A CA  1 
ATOM   1203 C  C   . ASP A 1 146 ? 11.268  -4.559  44.747  1.00 88.24  ? 1616 ASP A C   1 
ATOM   1204 O  O   . ASP A 1 146 ? 10.463  -4.994  43.916  1.00 82.00  ? 1616 ASP A O   1 
ATOM   1205 C  CB  . ASP A 1 146 ? 10.251  -2.388  45.371  1.00 90.92  ? 1616 ASP A CB  1 
ATOM   1206 C  CG  . ASP A 1 146 ? 9.580   -3.202  46.449  1.00 96.04  ? 1616 ASP A CG  1 
ATOM   1207 O  OD1 . ASP A 1 146 ? 10.275  -3.546  47.434  1.00 91.99  ? 1616 ASP A OD1 1 
ATOM   1208 O  OD2 . ASP A 1 146 ? 8.384   -3.533  46.294  1.00 98.39  ? 1616 ASP A OD2 1 
ATOM   1209 N  N   . HIS A 1 147 ? 11.952  -5.335  45.576  1.00 91.88  ? 1617 HIS A N   1 
ATOM   1210 C  CA  . HIS A 1 147 ? 11.842  -6.780  45.548  1.00 95.50  ? 1617 HIS A CA  1 
ATOM   1211 C  C   . HIS A 1 147 ? 10.967  -7.310  46.677  1.00 94.32  ? 1617 HIS A C   1 
ATOM   1212 O  O   . HIS A 1 147 ? 10.975  -8.515  46.944  1.00 81.43  ? 1617 HIS A O   1 
ATOM   1213 C  CB  . HIS A 1 147 ? 13.239  -7.384  45.580  1.00 103.40 ? 1617 HIS A CB  1 
ATOM   1214 C  CG  . HIS A 1 147 ? 14.106  -6.920  44.450  1.00 120.15 ? 1617 HIS A CG  1 
ATOM   1215 N  ND1 . HIS A 1 147 ? 15.385  -7.390  44.244  1.00 127.43 ? 1617 HIS A ND1 1 
ATOM   1216 C  CD2 . HIS A 1 147 ? 13.867  -6.040  43.448  1.00 123.93 ? 1617 HIS A CD2 1 
ATOM   1217 C  CE1 . HIS A 1 147 ? 15.901  -6.814  43.173  1.00 127.26 ? 1617 HIS A CE1 1 
ATOM   1218 N  NE2 . HIS A 1 147 ? 15.000  -5.989  42.672  1.00 126.36 ? 1617 HIS A NE2 1 
ATOM   1219 N  N   . SER A 1 148 ? 10.242  -6.421  47.365  1.00 95.97  ? 1618 SER A N   1 
ATOM   1220 C  CA  . SER A 1 148 ? 9.396   -6.822  48.488  1.00 99.00  ? 1618 SER A CA  1 
ATOM   1221 C  C   . SER A 1 148 ? 8.337   -7.829  48.067  1.00 98.83  ? 1618 SER A C   1 
ATOM   1222 O  O   . SER A 1 148 ? 7.960   -8.708  48.854  1.00 99.85  ? 1618 SER A O   1 
ATOM   1223 C  CB  . SER A 1 148 ? 8.709   -5.597  49.094  1.00 93.29  ? 1618 SER A CB  1 
ATOM   1224 O  OG  . SER A 1 148 ? 7.782   -5.041  48.169  1.00 91.81  ? 1618 SER A OG  1 
ATOM   1225 N  N   . ASP A 1 149 ? 7.832   -7.703  46.840  1.00 88.07  ? 1619 ASP A N   1 
ATOM   1226 C  CA  . ASP A 1 149 ? 6.732   -8.553  46.413  1.00 89.50  ? 1619 ASP A CA  1 
ATOM   1227 C  C   . ASP A 1 149 ? 7.125   -10.023 46.372  1.00 82.43  ? 1619 ASP A C   1 
ATOM   1228 O  O   . ASP A 1 149 ? 6.259   -10.896 46.533  1.00 81.62  ? 1619 ASP A O   1 
ATOM   1229 C  CB  . ASP A 1 149 ? 6.254   -8.112  45.036  1.00 96.22  ? 1619 ASP A CB  1 
ATOM   1230 C  CG  . ASP A 1 149 ? 5.323   -6.933  45.094  1.00 90.71  ? 1619 ASP A CG  1 
ATOM   1231 O  OD1 . ASP A 1 149 ? 4.841   -6.623  46.199  1.00 92.02  ? 1619 ASP A OD1 1 
ATOM   1232 O  OD2 . ASP A 1 149 ? 5.086   -6.316  44.033  1.00 88.90  ? 1619 ASP A OD2 1 
ATOM   1233 N  N   . PHE A 1 150 ? 8.418   -10.320 46.184  1.00 58.85  ? 1620 PHE A N   1 
ATOM   1234 C  CA  . PHE A 1 150 ? 8.888   -11.685 45.970  1.00 68.45  ? 1620 PHE A CA  1 
ATOM   1235 C  C   . PHE A 1 150 ? 9.902   -12.133 47.018  1.00 75.70  ? 1620 PHE A C   1 
ATOM   1236 O  O   . PHE A 1 150 ? 10.759  -12.970 46.726  1.00 81.12  ? 1620 PHE A O   1 
ATOM   1237 C  CB  . PHE A 1 150 ? 9.500   -11.838 44.577  1.00 69.33  ? 1620 PHE A CB  1 
ATOM   1238 C  CG  . PHE A 1 150 ? 8.807   -11.047 43.511  1.00 74.80  ? 1620 PHE A CG  1 
ATOM   1239 C  CD1 . PHE A 1 150 ? 7.808   -11.631 42.742  1.00 68.86  ? 1620 PHE A CD1 1 
ATOM   1240 C  CD2 . PHE A 1 150 ? 9.153   -9.727  43.264  1.00 76.58  ? 1620 PHE A CD2 1 
ATOM   1241 C  CE1 . PHE A 1 150 ? 7.159   -10.902 41.755  1.00 57.56  ? 1620 PHE A CE1 1 
ATOM   1242 C  CE2 . PHE A 1 150 ? 8.510   -8.997  42.279  1.00 75.42  ? 1620 PHE A CE2 1 
ATOM   1243 C  CZ  . PHE A 1 150 ? 7.517   -9.588  41.520  1.00 65.18  ? 1620 PHE A CZ  1 
ATOM   1244 N  N   . GLN A 1 151 ? 9.775   -11.665 48.260  1.00 80.66  ? 1621 GLN A N   1 
ATOM   1245 C  CA  . GLN A 1 151 ? 10.906  -11.771 49.171  1.00 99.62  ? 1621 GLN A CA  1 
ATOM   1246 C  C   . GLN A 1 151 ? 11.143  -13.180 49.711  1.00 98.78  ? 1621 GLN A C   1 
ATOM   1247 O  O   . GLN A 1 151 ? 12.276  -13.491 50.091  1.00 103.86 ? 1621 GLN A O   1 
ATOM   1248 C  CB  . GLN A 1 151 ? 10.750  -10.783 50.332  1.00 108.42 ? 1621 GLN A CB  1 
ATOM   1249 C  CG  . GLN A 1 151 ? 11.733  -9.604  50.245  1.00 115.08 ? 1621 GLN A CG  1 
ATOM   1250 C  CD  . GLN A 1 151 ? 13.201  -10.027 50.379  1.00 116.86 ? 1621 GLN A CD  1 
ATOM   1251 O  OE1 . GLN A 1 151 ? 13.538  -10.894 51.188  1.00 117.44 ? 1621 GLN A OE1 1 
ATOM   1252 N  NE2 . GLN A 1 151 ? 14.075  -9.419  49.577  1.00 112.86 ? 1621 GLN A NE2 1 
ATOM   1253 N  N   . ASP A 1 152 ? 10.143  -14.053 49.729  1.00 90.69  ? 1622 ASP A N   1 
ATOM   1254 C  CA  . ASP A 1 152 ? 10.362  -15.417 50.205  1.00 98.05  ? 1622 ASP A CA  1 
ATOM   1255 C  C   . ASP A 1 152 ? 10.066  -16.436 49.114  1.00 92.91  ? 1622 ASP A C   1 
ATOM   1256 O  O   . ASP A 1 152 ? 9.523   -17.515 49.370  1.00 103.86 ? 1622 ASP A O   1 
ATOM   1257 C  CB  . ASP A 1 152 ? 9.527   -15.694 51.449  1.00 105.20 ? 1622 ASP A CB  1 
ATOM   1258 C  CG  . ASP A 1 152 ? 9.821   -14.714 52.566  1.00 115.29 ? 1622 ASP A CG  1 
ATOM   1259 O  OD1 . ASP A 1 152 ? 9.103   -13.691 52.658  1.00 120.16 ? 1622 ASP A OD1 1 
ATOM   1260 O  OD2 . ASP A 1 152 ? 10.777  -14.959 53.336  1.00 109.72 ? 1622 ASP A OD2 1 
ATOM   1261 N  N   . THR A 1 153 ? 10.437  -16.097 47.884  1.00 67.74  ? 1623 THR A N   1 
ATOM   1262 C  CA  . THR A 1 153 ? 10.197  -16.912 46.704  1.00 69.19  ? 1623 THR A CA  1 
ATOM   1263 C  C   . THR A 1 153 ? 11.518  -17.359 46.095  1.00 78.11  ? 1623 THR A C   1 
ATOM   1264 O  O   . THR A 1 153 ? 12.589  -16.848 46.429  1.00 81.37  ? 1623 THR A O   1 
ATOM   1265 C  CB  . THR A 1 153 ? 9.403   -16.131 45.658  1.00 62.69  ? 1623 THR A CB  1 
ATOM   1266 O  OG1 . THR A 1 153 ? 10.282  -15.183 45.042  1.00 61.44  ? 1623 THR A OG1 1 
ATOM   1267 C  CG2 . THR A 1 153 ? 8.245   -15.387 46.318  1.00 70.06  ? 1623 THR A CG2 1 
ATOM   1268 N  N   . ASP A 1 154 ? 11.438  -18.323 45.182  1.00 69.53  ? 1624 ASP A N   1 
ATOM   1269 C  CA  . ASP A 1 154 ? 12.593  -18.676 44.372  1.00 69.64  ? 1624 ASP A CA  1 
ATOM   1270 C  C   . ASP A 1 154 ? 12.723  -17.791 43.139  1.00 64.97  ? 1624 ASP A C   1 
ATOM   1271 O  O   . ASP A 1 154 ? 13.439  -18.148 42.200  1.00 76.67  ? 1624 ASP A O   1 
ATOM   1272 C  CB  . ASP A 1 154 ? 12.560  -20.167 43.982  1.00 65.38  ? 1624 ASP A CB  1 
ATOM   1273 C  CG  . ASP A 1 154 ? 11.297  -20.581 43.210  1.00 65.71  ? 1624 ASP A CG  1 
ATOM   1274 O  OD1 . ASP A 1 154 ? 10.364  -19.767 43.033  1.00 52.48  ? 1624 ASP A OD1 1 
ATOM   1275 O  OD2 . ASP A 1 154 ? 11.249  -21.758 42.778  1.00 62.35  ? 1624 ASP A OD2 1 
ATOM   1276 N  N   . ILE A 1 155 ? 12.047  -16.650 43.113  1.00 62.38  ? 1625 ILE A N   1 
ATOM   1277 C  CA  . ILE A 1 155 ? 12.218  -15.724 41.997  1.00 62.52  ? 1625 ILE A CA  1 
ATOM   1278 C  C   . ILE A 1 155 ? 13.488  -14.928 42.253  1.00 64.11  ? 1625 ILE A C   1 
ATOM   1279 O  O   . ILE A 1 155 ? 13.581  -14.213 43.261  1.00 69.57  ? 1625 ILE A O   1 
ATOM   1280 C  CB  . ILE A 1 155 ? 10.992  -14.816 41.821  1.00 59.07  ? 1625 ILE A CB  1 
ATOM   1281 C  CG1 . ILE A 1 155 ? 9.763   -15.672 41.478  1.00 60.83  ? 1625 ILE A CG1 1 
ATOM   1282 C  CG2 . ILE A 1 155 ? 11.267  -13.767 40.756  1.00 53.46  ? 1625 ILE A CG2 1 
ATOM   1283 C  CD1 . ILE A 1 155 ? 8.523   -14.887 41.128  1.00 63.72  ? 1625 ILE A CD1 1 
ATOM   1284 N  N   . PRO A 1 156 ? 14.476  -14.998 41.371  1.00 68.60  ? 1626 PRO A N   1 
ATOM   1285 C  CA  . PRO A 1 156 ? 15.746  -14.334 41.654  1.00 69.50  ? 1626 PRO A CA  1 
ATOM   1286 C  C   . PRO A 1 156 ? 15.624  -12.834 41.494  1.00 64.86  ? 1626 PRO A C   1 
ATOM   1287 O  O   . PRO A 1 156 ? 14.862  -12.324 40.672  1.00 67.64  ? 1626 PRO A O   1 
ATOM   1288 C  CB  . PRO A 1 156 ? 16.699  -14.924 40.607  1.00 58.32  ? 1626 PRO A CB  1 
ATOM   1289 C  CG  . PRO A 1 156 ? 15.809  -15.293 39.476  1.00 52.86  ? 1626 PRO A CG  1 
ATOM   1290 C  CD  . PRO A 1 156 ? 14.515  -15.743 40.100  1.00 62.96  ? 1626 PRO A CD  1 
ATOM   1291 N  N   . PHE A 1 157 ? 16.375  -12.131 42.326  1.00 72.75  ? 1627 PHE A N   1 
ATOM   1292 C  CA  . PHE A 1 157 ? 16.384  -10.679 42.332  1.00 87.98  ? 1627 PHE A CA  1 
ATOM   1293 C  C   . PHE A 1 157 ? 17.545  -10.096 41.557  1.00 88.20  ? 1627 PHE A C   1 
ATOM   1294 O  O   . PHE A 1 157 ? 17.360  -9.131  40.814  1.00 90.35  ? 1627 PHE A O   1 
ATOM   1295 C  CB  . PHE A 1 157 ? 16.368  -10.199 43.774  1.00 102.66 ? 1627 PHE A CB  1 
ATOM   1296 C  CG  . PHE A 1 157 ? 15.044  -10.443 44.433  1.00 115.87 ? 1627 PHE A CG  1 
ATOM   1297 C  CD1 . PHE A 1 157 ? 13.899  -10.522 43.648  1.00 101.46 ? 1627 PHE A CD1 1 
ATOM   1298 C  CD2 . PHE A 1 157 ? 14.933  -10.611 45.801  1.00 117.97 ? 1627 PHE A CD2 1 
ATOM   1299 C  CE1 . PHE A 1 157 ? 12.690  -10.744 44.206  1.00 94.67  ? 1627 PHE A CE1 1 
ATOM   1300 C  CE2 . PHE A 1 157 ? 13.704  -10.838 46.368  1.00 109.31 ? 1627 PHE A CE2 1 
ATOM   1301 C  CZ  . PHE A 1 157 ? 12.586  -10.900 45.567  1.00 105.10 ? 1627 PHE A CZ  1 
ATOM   1302 N  N   . GLU A 1 158 ? 18.727  -10.677 41.702  1.00 105.17 ? 1628 GLU A N   1 
ATOM   1303 C  CA  . GLU A 1 158 ? 19.874  -10.309 40.884  1.00 115.53 ? 1628 GLU A CA  1 
ATOM   1304 C  C   . GLU A 1 158 ? 19.737  -11.034 39.554  1.00 96.89  ? 1628 GLU A C   1 
ATOM   1305 O  O   . GLU A 1 158 ? 19.923  -12.251 39.469  1.00 101.58 ? 1628 GLU A O   1 
ATOM   1306 C  CB  . GLU A 1 158 ? 21.184  -10.670 41.577  1.00 130.27 ? 1628 GLU A CB  1 
ATOM   1307 C  CG  . GLU A 1 158 ? 21.185  -10.437 43.076  1.00 142.74 ? 1628 GLU A CG  1 
ATOM   1308 C  CD  . GLU A 1 158 ? 22.021  -11.466 43.822  1.00 152.35 ? 1628 GLU A CD  1 
ATOM   1309 O  OE1 . GLU A 1 158 ? 21.680  -11.772 44.987  1.00 151.21 ? 1628 GLU A OE1 1 
ATOM   1310 O  OE2 . GLU A 1 158 ? 23.020  -11.962 43.247  1.00 156.32 ? 1628 GLU A OE2 1 
ATOM   1311 N  N   . VAL A 1 159 ? 19.371  -10.286 38.513  1.00 70.76  ? 1629 VAL A N   1 
ATOM   1312 C  CA  . VAL A 1 159 ? 19.199  -10.845 37.178  1.00 66.76  ? 1629 VAL A CA  1 
ATOM   1313 C  C   . VAL A 1 159 ? 19.883  -9.923  36.179  1.00 63.62  ? 1629 VAL A C   1 
ATOM   1314 O  O   . VAL A 1 159 ? 20.085  -8.738  36.446  1.00 59.33  ? 1629 VAL A O   1 
ATOM   1315 C  CB  . VAL A 1 159 ? 17.706  -10.992 36.803  1.00 68.99  ? 1629 VAL A CB  1 
ATOM   1316 C  CG1 . VAL A 1 159 ? 17.078  -12.206 37.490  1.00 55.79  ? 1629 VAL A CG1 1 
ATOM   1317 C  CG2 . VAL A 1 159 ? 16.940  -9.694  37.153  1.00 61.20  ? 1629 VAL A CG2 1 
ATOM   1318 N  N   . PRO A 1 160 ? 20.268  -10.468 35.026  1.00 75.65  ? 1630 PRO A N   1 
ATOM   1319 C  CA  . PRO A 1 160 ? 20.819  -9.610  33.965  1.00 76.24  ? 1630 PRO A CA  1 
ATOM   1320 C  C   . PRO A 1 160 ? 19.789  -8.581  33.518  1.00 76.48  ? 1630 PRO A C   1 
ATOM   1321 O  O   . PRO A 1 160 ? 18.618  -8.899  33.302  1.00 73.08  ? 1630 PRO A O   1 
ATOM   1322 C  CB  . PRO A 1 160 ? 21.169  -10.601 32.842  1.00 70.29  ? 1630 PRO A CB  1 
ATOM   1323 C  CG  . PRO A 1 160 ? 20.477  -11.892 33.203  1.00 72.31  ? 1630 PRO A CG  1 
ATOM   1324 C  CD  . PRO A 1 160 ? 20.383  -11.898 34.701  1.00 74.06  ? 1630 PRO A CD  1 
ATOM   1325 N  N   . LEU A 1 161 ? 20.223  -7.334  33.427  1.00 84.14  ? 1631 LEU A N   1 
ATOM   1326 C  CA  . LEU A 1 161 ? 19.369  -6.276  32.908  1.00 67.43  ? 1631 LEU A CA  1 
ATOM   1327 C  C   . LEU A 1 161 ? 19.455  -6.248  31.387  1.00 62.50  ? 1631 LEU A C   1 
ATOM   1328 O  O   . LEU A 1 161 ? 20.546  -6.030  30.846  1.00 66.26  ? 1631 LEU A O   1 
ATOM   1329 C  CB  . LEU A 1 161 ? 19.806  -4.935  33.466  1.00 66.19  ? 1631 LEU A CB  1 
ATOM   1330 C  CG  . LEU A 1 161 ? 18.966  -3.694  33.163  1.00 61.17  ? 1631 LEU A CG  1 
ATOM   1331 C  CD1 . LEU A 1 161 ? 17.566  -3.871  33.657  1.00 59.26  ? 1631 LEU A CD1 1 
ATOM   1332 C  CD2 . LEU A 1 161 ? 19.637  -2.440  33.778  1.00 62.68  ? 1631 LEU A CD2 1 
ATOM   1333 N  N   . PRO A 1 162 ? 18.356  -6.457  30.669  1.00 65.58  ? 1632 PRO A N   1 
ATOM   1334 C  CA  . PRO A 1 162 ? 18.423  -6.440  29.202  1.00 69.58  ? 1632 PRO A CA  1 
ATOM   1335 C  C   . PRO A 1 162 ? 18.794  -5.063  28.672  1.00 76.61  ? 1632 PRO A C   1 
ATOM   1336 O  O   . PRO A 1 162 ? 18.492  -4.033  29.281  1.00 79.02  ? 1632 PRO A O   1 
ATOM   1337 C  CB  . PRO A 1 162 ? 17.006  -6.844  28.775  1.00 62.08  ? 1632 PRO A CB  1 
ATOM   1338 C  CG  . PRO A 1 162 ? 16.427  -7.538  29.973  1.00 58.06  ? 1632 PRO A CG  1 
ATOM   1339 C  CD  . PRO A 1 162 ? 17.034  -6.880  31.163  1.00 53.66  ? 1632 PRO A CD  1 
ATOM   1340 N  N   . ALA A 1 163 ? 19.488  -5.056  27.528  1.00 81.97  ? 1633 ALA A N   1 
ATOM   1341 C  CA  . ALA A 1 163 ? 19.859  -3.791  26.901  1.00 93.02  ? 1633 ALA A CA  1 
ATOM   1342 C  C   . ALA A 1 163 ? 18.700  -3.162  26.140  1.00 87.46  ? 1633 ALA A C   1 
ATOM   1343 O  O   . ALA A 1 163 ? 18.650  -1.934  26.004  1.00 82.14  ? 1633 ALA A O   1 
ATOM   1344 C  CB  . ALA A 1 163 ? 21.053  -3.985  25.965  1.00 91.19  ? 1633 ALA A CB  1 
ATOM   1345 N  N   . LYS A 1 164 ? 17.762  -3.972  25.658  1.00 79.30  ? 1634 LYS A N   1 
ATOM   1346 C  CA  . LYS A 1 164 ? 16.644  -3.499  24.855  1.00 84.79  ? 1634 LYS A CA  1 
ATOM   1347 C  C   . LYS A 1 164 ? 15.339  -3.998  25.466  1.00 86.96  ? 1634 LYS A C   1 
ATOM   1348 O  O   . LYS A 1 164 ? 15.308  -4.994  26.193  1.00 83.97  ? 1634 LYS A O   1 
ATOM   1349 C  CB  . LYS A 1 164 ? 16.763  -3.968  23.389  1.00 81.19  ? 1634 LYS A CB  1 
ATOM   1350 C  CG  . LYS A 1 164 ? 17.258  -5.421  23.227  1.00 88.03  ? 1634 LYS A CG  1 
ATOM   1351 C  CD  . LYS A 1 164 ? 16.893  -6.036  21.865  1.00 87.95  ? 1634 LYS A CD  1 
ATOM   1352 C  CE  . LYS A 1 164 ? 15.549  -6.772  21.923  1.00 96.95  ? 1634 LYS A CE  1 
ATOM   1353 N  NZ  . LYS A 1 164 ? 14.775  -6.721  20.641  1.00 102.96 ? 1634 LYS A NZ  1 
ATOM   1354 N  N   . GLN A 1 165 ? 14.254  -3.284  25.179  1.00 82.98  ? 1635 GLN A N   1 
ATOM   1355 C  CA  . GLN A 1 165 ? 12.941  -3.680  25.676  1.00 61.02  ? 1635 GLN A CA  1 
ATOM   1356 C  C   . GLN A 1 165 ? 12.372  -4.745  24.763  1.00 51.64  ? 1635 GLN A C   1 
ATOM   1357 O  O   . GLN A 1 165 ? 12.272  -4.539  23.550  1.00 73.02  ? 1635 GLN A O   1 
ATOM   1358 C  CB  . GLN A 1 165 ? 12.005  -2.478  25.750  1.00 67.81  ? 1635 GLN A CB  1 
ATOM   1359 C  CG  . GLN A 1 165 ? 12.037  -1.785  27.105  1.00 66.92  ? 1635 GLN A CG  1 
ATOM   1360 C  CD  . GLN A 1 165 ? 11.191  -0.541  27.131  1.00 81.25  ? 1635 GLN A CD  1 
ATOM   1361 O  OE1 . GLN A 1 165 ? 9.960   -0.607  27.026  1.00 78.29  ? 1635 GLN A OE1 1 
ATOM   1362 N  NE2 . GLN A 1 165 ? 11.842  0.612   27.256  1.00 85.43  ? 1635 GLN A NE2 1 
ATOM   1363 N  N   . HIS A 1 166 ? 12.006  -5.888  25.339  1.00 47.14  ? 1636 HIS A N   1 
ATOM   1364 C  CA  . HIS A 1 166 ? 11.470  -6.965  24.516  1.00 66.77  ? 1636 HIS A CA  1 
ATOM   1365 C  C   . HIS A 1 166 ? 10.062  -6.676  24.019  1.00 72.55  ? 1636 HIS A C   1 
ATOM   1366 O  O   . HIS A 1 166 ? 9.685   -7.148  22.939  1.00 62.87  ? 1636 HIS A O   1 
ATOM   1367 C  CB  . HIS A 1 166 ? 11.452  -8.282  25.271  1.00 63.73  ? 1636 HIS A CB  1 
ATOM   1368 C  CG  . HIS A 1 166 ? 10.834  -9.390  24.483  1.00 74.54  ? 1636 HIS A CG  1 
ATOM   1369 N  ND1 . HIS A 1 166 ? 9.470   -9.587  24.419  1.00 74.16  ? 1636 HIS A ND1 1 
ATOM   1370 C  CD2 . HIS A 1 166 ? 11.390  -10.335 23.687  1.00 72.87  ? 1636 HIS A CD2 1 
ATOM   1371 C  CE1 . HIS A 1 166 ? 9.213   -10.616 23.632  1.00 70.84  ? 1636 HIS A CE1 1 
ATOM   1372 N  NE2 . HIS A 1 166 ? 10.361  -11.090 23.178  1.00 77.54  ? 1636 HIS A NE2 1 
ATOM   1373 N  N   . VAL A 1 167 ? 9.251   -5.984  24.810  1.00 62.73  ? 1637 VAL A N   1 
ATOM   1374 C  CA  . VAL A 1 167 ? 7.828   -5.833  24.550  1.00 62.75  ? 1637 VAL A CA  1 
ATOM   1375 C  C   . VAL A 1 167 ? 7.583   -4.494  23.810  1.00 67.66  ? 1637 VAL A C   1 
ATOM   1376 O  O   . VAL A 1 167 ? 8.103   -3.472  24.271  1.00 66.76  ? 1637 VAL A O   1 
ATOM   1377 C  CB  . VAL A 1 167 ? 7.008   -5.896  25.843  1.00 58.14  ? 1637 VAL A CB  1 
ATOM   1378 C  CG1 . VAL A 1 167 ? 5.598   -5.336  25.629  1.00 63.95  ? 1637 VAL A CG1 1 
ATOM   1379 C  CG2 . VAL A 1 167 ? 6.958   -7.356  26.353  1.00 49.70  ? 1637 VAL A CG2 1 
ATOM   1380 N  N   . PRO A 1 168 ? 6.832   -4.498  22.717  1.00 58.97  ? 1638 PRO A N   1 
ATOM   1381 C  CA  . PRO A 1 168 ? 6.599   -3.243  21.975  1.00 66.28  ? 1638 PRO A CA  1 
ATOM   1382 C  C   . PRO A 1 168 ? 5.820   -2.226  22.803  1.00 64.10  ? 1638 PRO A C   1 
ATOM   1383 O  O   . PRO A 1 168 ? 5.094   -2.574  23.736  1.00 54.02  ? 1638 PRO A O   1 
ATOM   1384 C  CB  . PRO A 1 168 ? 5.795   -3.696  20.747  1.00 70.03  ? 1638 PRO A CB  1 
ATOM   1385 C  CG  . PRO A 1 168 ? 6.012   -5.162  20.645  1.00 59.65  ? 1638 PRO A CG  1 
ATOM   1386 C  CD  . PRO A 1 168 ? 6.232   -5.657  22.043  1.00 62.26  ? 1638 PRO A CD  1 
ATOM   1387 N  N   . GLU A 1 169 ? 5.972   -0.946  22.433  1.00 71.52  ? 1639 GLU A N   1 
ATOM   1388 C  CA  . GLU A 1 169 ? 5.465   0.150   23.263  1.00 76.05  ? 1639 GLU A CA  1 
ATOM   1389 C  C   . GLU A 1 169 ? 3.955   0.082   23.449  1.00 72.81  ? 1639 GLU A C   1 
ATOM   1390 O  O   . GLU A 1 169 ? 3.446   0.405   24.527  1.00 82.29  ? 1639 GLU A O   1 
ATOM   1391 C  CB  . GLU A 1 169 ? 5.849   1.505   22.663  1.00 71.91  ? 1639 GLU A CB  1 
ATOM   1392 C  CG  . GLU A 1 169 ? 5.454   2.689   23.556  1.00 80.01  ? 1639 GLU A CG  1 
ATOM   1393 C  CD  . GLU A 1 169 ? 4.874   3.877   22.771  1.00 106.08 ? 1639 GLU A CD  1 
ATOM   1394 O  OE1 . GLU A 1 169 ? 4.901   3.833   21.519  1.00 113.86 ? 1639 GLU A OE1 1 
ATOM   1395 O  OE2 . GLU A 1 169 ? 4.394   4.855   23.405  1.00 103.54 ? 1639 GLU A OE2 1 
ATOM   1396 N  N   . ALA A 1 170 ? 3.221   -0.327  22.412  1.00 68.19  ? 1640 ALA A N   1 
ATOM   1397 C  CA  . ALA A 1 170 ? 1.765   -0.374  22.505  1.00 71.96  ? 1640 ALA A CA  1 
ATOM   1398 C  C   . ALA A 1 170 ? 1.312   -1.361  23.577  1.00 67.79  ? 1640 ALA A C   1 
ATOM   1399 O  O   . ALA A 1 170 ? 0.436   -1.052  24.397  1.00 74.68  ? 1640 ALA A O   1 
ATOM   1400 C  CB  . ALA A 1 170 ? 1.173   -0.741  21.144  1.00 78.54  ? 1640 ALA A CB  1 
ATOM   1401 N  N   . GLU A 1 171 ? 1.897   -2.559  23.582  1.00 56.43  ? 1641 GLU A N   1 
ATOM   1402 C  CA  . GLU A 1 171 ? 1.547   -3.548  24.597  1.00 61.49  ? 1641 GLU A CA  1 
ATOM   1403 C  C   . GLU A 1 171 ? 1.965   -3.081  25.992  1.00 55.95  ? 1641 GLU A C   1 
ATOM   1404 O  O   . GLU A 1 171 ? 1.225   -3.272  26.972  1.00 59.84  ? 1641 GLU A O   1 
ATOM   1405 C  CB  . GLU A 1 171 ? 2.203   -4.889  24.247  1.00 63.65  ? 1641 GLU A CB  1 
ATOM   1406 C  CG  . GLU A 1 171 ? 1.394   -5.773  23.299  1.00 66.27  ? 1641 GLU A CG  1 
ATOM   1407 C  CD  . GLU A 1 171 ? 1.696   -5.530  21.822  1.00 77.80  ? 1641 GLU A CD  1 
ATOM   1408 O  OE1 . GLU A 1 171 ? 2.065   -4.394  21.458  1.00 74.30  ? 1641 GLU A OE1 1 
ATOM   1409 O  OE2 . GLU A 1 171 ? 1.553   -6.491  21.027  1.00 81.84  ? 1641 GLU A OE2 1 
ATOM   1410 N  N   . ARG A 1 172 ? 3.136   -2.447  26.095  1.00 47.13  ? 1642 ARG A N   1 
ATOM   1411 C  CA  . ARG A 1 172 ? 3.552   -1.861  27.364  1.00 61.25  ? 1642 ARG A CA  1 
ATOM   1412 C  C   . ARG A 1 172 ? 2.527   -0.853  27.868  1.00 51.80  ? 1642 ARG A C   1 
ATOM   1413 O  O   . ARG A 1 172 ? 2.203   -0.836  29.057  1.00 55.85  ? 1642 ARG A O   1 
ATOM   1414 C  CB  . ARG A 1 172 ? 4.918   -1.174  27.238  1.00 49.11  ? 1642 ARG A CB  1 
ATOM   1415 C  CG  . ARG A 1 172 ? 5.381   -0.557  28.563  1.00 55.98  ? 1642 ARG A CG  1 
ATOM   1416 C  CD  . ARG A 1 172 ? 6.668   0.244   28.474  1.00 64.64  ? 1642 ARG A CD  1 
ATOM   1417 N  NE  . ARG A 1 172 ? 6.826   0.943   27.201  1.00 85.67  ? 1642 ARG A NE  1 
ATOM   1418 C  CZ  . ARG A 1 172 ? 7.757   1.870   26.964  1.00 94.47  ? 1642 ARG A CZ  1 
ATOM   1419 N  NH1 . ARG A 1 172 ? 8.616   2.236   27.921  1.00 87.67  ? 1642 ARG A NH1 1 
ATOM   1420 N  NH2 . ARG A 1 172 ? 7.824   2.442   25.769  1.00 95.98  ? 1642 ARG A NH2 1 
ATOM   1421 N  N   . GLU A 1 173 ? 2.000   -0.014  26.979  1.00 61.01  ? 1643 GLU A N   1 
ATOM   1422 C  CA  . GLU A 1 173 ? 1.081   1.036   27.420  1.00 61.98  ? 1643 GLU A CA  1 
ATOM   1423 C  C   . GLU A 1 173 ? -0.299  0.484   27.751  1.00 69.67  ? 1643 GLU A C   1 
ATOM   1424 O  O   . GLU A 1 173 ? -0.972  1.024   28.636  1.00 60.35  ? 1643 GLU A O   1 
ATOM   1425 C  CB  . GLU A 1 173 ? 0.983   2.133   26.367  1.00 52.54  ? 1643 GLU A CB  1 
ATOM   1426 C  CG  . GLU A 1 173 ? 2.226   3.037   26.288  1.00 65.88  ? 1643 GLU A CG  1 
ATOM   1427 C  CD  . GLU A 1 173 ? 2.785   3.416   27.653  1.00 75.29  ? 1643 GLU A CD  1 
ATOM   1428 O  OE1 . GLU A 1 173 ? 2.024   4.013   28.452  1.00 83.85  ? 1643 GLU A OE1 1 
ATOM   1429 O  OE2 . GLU A 1 173 ? 3.978   3.126   27.927  1.00 69.08  ? 1643 GLU A OE2 1 
ATOM   1430 N  N   . GLU A 1 174 ? -0.734  -0.590  27.077  1.00 55.60  ? 1644 GLU A N   1 
ATOM   1431 C  CA  . GLU A 1 174 ? -1.977  -1.225  27.497  1.00 62.60  ? 1644 GLU A CA  1 
ATOM   1432 C  C   . GLU A 1 174 ? -1.830  -1.814  28.889  1.00 63.02  ? 1644 GLU A C   1 
ATOM   1433 O  O   . GLU A 1 174 ? -2.719  -1.658  29.745  1.00 63.63  ? 1644 GLU A O   1 
ATOM   1434 C  CB  . GLU A 1 174 ? -2.385  -2.325  26.529  1.00 57.15  ? 1644 GLU A CB  1 
ATOM   1435 C  CG  . GLU A 1 174 ? -2.850  -1.867  25.182  1.00 71.22  ? 1644 GLU A CG  1 
ATOM   1436 C  CD  . GLU A 1 174 ? -3.034  -3.052  24.247  1.00 94.28  ? 1644 GLU A CD  1 
ATOM   1437 O  OE1 . GLU A 1 174 ? -3.926  -2.985  23.374  1.00 104.85 ? 1644 GLU A OE1 1 
ATOM   1438 O  OE2 . GLU A 1 174 ? -2.291  -4.056  24.391  1.00 94.68  ? 1644 GLU A OE2 1 
ATOM   1439 N  N   . VAL A 1 175 ? -0.699  -2.475  29.142  1.00 57.52  ? 1645 VAL A N   1 
ATOM   1440 C  CA  . VAL A 1 175 ? -0.455  -2.991  30.480  1.00 58.89  ? 1645 VAL A CA  1 
ATOM   1441 C  C   . VAL A 1 175 ? -0.436  -1.841  31.475  1.00 62.23  ? 1645 VAL A C   1 
ATOM   1442 O  O   . VAL A 1 175 ? -1.003  -1.937  32.571  1.00 51.14  ? 1645 VAL A O   1 
ATOM   1443 C  CB  . VAL A 1 175 ? 0.857   -3.801  30.523  1.00 46.39  ? 1645 VAL A CB  1 
ATOM   1444 C  CG1 . VAL A 1 175 ? 1.201   -4.157  31.948  1.00 46.55  ? 1645 VAL A CG1 1 
ATOM   1445 C  CG2 . VAL A 1 175 ? 0.738   -5.078  29.704  1.00 50.65  ? 1645 VAL A CG2 1 
ATOM   1446 N  N   . ARG A 1 176 ? 0.198   -0.729  31.099  1.00 50.75  ? 1646 ARG A N   1 
ATOM   1447 C  CA  . ARG A 1 176 ? 0.276   0.408   32.002  1.00 51.65  ? 1646 ARG A CA  1 
ATOM   1448 C  C   . ARG A 1 176 ? -1.121  0.936   32.331  1.00 55.12  ? 1646 ARG A C   1 
ATOM   1449 O  O   . ARG A 1 176 ? -1.433  1.163   33.505  1.00 53.32  ? 1646 ARG A O   1 
ATOM   1450 C  CB  . ARG A 1 176 ? 1.165   1.501   31.397  1.00 62.57  ? 1646 ARG A CB  1 
ATOM   1451 C  CG  . ARG A 1 176 ? 1.499   2.639   32.376  1.00 64.03  ? 1646 ARG A CG  1 
ATOM   1452 C  CD  . ARG A 1 176 ? 2.550   3.635   31.863  1.00 61.57  ? 1646 ARG A CD  1 
ATOM   1453 N  NE  . ARG A 1 176 ? 3.668   3.055   31.102  1.00 64.16  ? 1646 ARG A NE  1 
ATOM   1454 C  CZ  . ARG A 1 176 ? 4.859   2.753   31.622  1.00 71.43  ? 1646 ARG A CZ  1 
ATOM   1455 N  NH1 . ARG A 1 176 ? 5.093   2.953   32.916  1.00 63.17  ? 1646 ARG A NH1 1 
ATOM   1456 N  NH2 . ARG A 1 176 ? 5.820   2.243   30.854  1.00 75.15  ? 1646 ARG A NH2 1 
ATOM   1457 N  N   . ASP A 1 177 ? -1.991  1.069   31.317  1.00 59.18  ? 1647 ASP A N   1 
ATOM   1458 C  CA  . ASP A 1 177 ? -3.371  1.504   31.557  1.00 53.28  ? 1647 ASP A CA  1 
ATOM   1459 C  C   . ASP A 1 177 ? -4.054  0.593   32.555  1.00 57.84  ? 1647 ASP A C   1 
ATOM   1460 O  O   . ASP A 1 177 ? -4.630  1.060   33.547  1.00 57.40  ? 1647 ASP A O   1 
ATOM   1461 C  CB  . ASP A 1 177 ? -4.200  1.484   30.271  1.00 52.99  ? 1647 ASP A CB  1 
ATOM   1462 C  CG  . ASP A 1 177 ? -3.736  2.469   29.234  1.00 71.36  ? 1647 ASP A CG  1 
ATOM   1463 O  OD1 . ASP A 1 177 ? -2.976  3.419   29.547  1.00 55.13  ? 1647 ASP A OD1 1 
ATOM   1464 O  OD2 . ASP A 1 177 ? -4.156  2.260   28.076  1.00 76.33  ? 1647 ASP A OD2 1 
ATOM   1465 N  N   . TRP A 1 178 ? -4.003  -0.722  32.293  1.00 57.59  ? 1648 TRP A N   1 
ATOM   1466 C  CA  . TRP A 1 178 ? -4.727  -1.676  33.122  1.00 53.05  ? 1648 TRP A CA  1 
ATOM   1467 C  C   . TRP A 1 178 ? -4.216  -1.644  34.553  1.00 51.02  ? 1648 TRP A C   1 
ATOM   1468 O  O   . TRP A 1 178 ? -4.999  -1.608  35.507  1.00 54.16  ? 1648 TRP A O   1 
ATOM   1469 C  CB  . TRP A 1 178 ? -4.605  -3.089  32.536  1.00 62.57  ? 1648 TRP A CB  1 
ATOM   1470 C  CG  . TRP A 1 178 ? -5.342  -4.120  33.350  1.00 66.89  ? 1648 TRP A CG  1 
ATOM   1471 C  CD1 . TRP A 1 178 ? -6.689  -4.352  33.352  1.00 64.99  ? 1648 TRP A CD1 1 
ATOM   1472 C  CD2 . TRP A 1 178 ? -4.776  -5.047  34.290  1.00 67.69  ? 1648 TRP A CD2 1 
ATOM   1473 N  NE1 . TRP A 1 178 ? -6.995  -5.356  34.236  1.00 62.31  ? 1648 TRP A NE1 1 
ATOM   1474 C  CE2 . TRP A 1 178 ? -5.843  -5.800  34.828  1.00 59.79  ? 1648 TRP A CE2 1 
ATOM   1475 C  CE3 . TRP A 1 178 ? -3.474  -5.313  34.730  1.00 56.17  ? 1648 TRP A CE3 1 
ATOM   1476 C  CZ2 . TRP A 1 178 ? -5.650  -6.806  35.781  1.00 60.52  ? 1648 TRP A CZ2 1 
ATOM   1477 C  CZ3 . TRP A 1 178 ? -3.281  -6.315  35.678  1.00 61.77  ? 1648 TRP A CZ3 1 
ATOM   1478 C  CH2 . TRP A 1 178 ? -4.371  -7.049  36.194  1.00 56.27  ? 1648 TRP A CH2 1 
ATOM   1479 N  N   . VAL A 1 179 ? -2.898  -1.644  34.722  1.00 50.80  ? 1649 VAL A N   1 
ATOM   1480 C  CA  . VAL A 1 179 ? -2.330  -1.639  36.064  1.00 51.44  ? 1649 VAL A CA  1 
ATOM   1481 C  C   . VAL A 1 179 ? -2.754  -0.386  36.807  1.00 53.39  ? 1649 VAL A C   1 
ATOM   1482 O  O   . VAL A 1 179 ? -3.067  -0.431  38.001  1.00 65.56  ? 1649 VAL A O   1 
ATOM   1483 C  CB  . VAL A 1 179 ? -0.795  -1.770  35.989  1.00 51.04  ? 1649 VAL A CB  1 
ATOM   1484 C  CG1 . VAL A 1 179 ? -0.135  -1.295  37.271  1.00 52.25  ? 1649 VAL A CG1 1 
ATOM   1485 C  CG2 . VAL A 1 179 ? -0.413  -3.214  35.705  1.00 49.30  ? 1649 VAL A CG2 1 
ATOM   1486 N  N   . LEU A 1 180 ? -2.755  0.756   36.118  1.00 63.12  ? 1650 LEU A N   1 
ATOM   1487 C  CA  . LEU A 1 180 ? -3.175  1.999   36.751  1.00 56.37  ? 1650 LEU A CA  1 
ATOM   1488 C  C   . LEU A 1 180 ? -4.630  1.914   37.209  1.00 58.56  ? 1650 LEU A C   1 
ATOM   1489 O  O   . LEU A 1 180 ? -4.955  2.238   38.356  1.00 69.78  ? 1650 LEU A O   1 
ATOM   1490 C  CB  . LEU A 1 180 ? -2.972  3.162   35.784  1.00 57.31  ? 1650 LEU A CB  1 
ATOM   1491 C  CG  . LEU A 1 180 ? -3.269  4.530   36.418  1.00 60.44  ? 1650 LEU A CG  1 
ATOM   1492 C  CD1 . LEU A 1 180 ? -2.384  4.759   37.624  1.00 60.49  ? 1650 LEU A CD1 1 
ATOM   1493 C  CD2 . LEU A 1 180 ? -3.123  5.623   35.401  1.00 60.60  ? 1650 LEU A CD2 1 
ATOM   1494 N  N   . THR A 1 181 ? -5.518  1.466   36.324  1.00 62.26  ? 1651 THR A N   1 
ATOM   1495 C  CA  . THR A 1 181 ? -6.925  1.322   36.690  1.00 64.02  ? 1651 THR A CA  1 
ATOM   1496 C  C   . THR A 1 181 ? -7.098  0.406   37.902  1.00 66.66  ? 1651 THR A C   1 
ATOM   1497 O  O   . THR A 1 181 ? -7.779  0.758   38.874  1.00 66.63  ? 1651 THR A O   1 
ATOM   1498 C  CB  . THR A 1 181 ? -7.715  0.808   35.492  1.00 63.95  ? 1651 THR A CB  1 
ATOM   1499 O  OG1 . THR A 1 181 ? -8.014  1.910   34.625  1.00 75.11  ? 1651 THR A OG1 1 
ATOM   1500 C  CG2 . THR A 1 181 ? -9.015  0.129   35.944  1.00 76.91  ? 1651 THR A CG2 1 
ATOM   1501 N  N   . VAL A 1 182 ? -6.468  -0.770  37.868  1.00 54.81  ? 1652 VAL A N   1 
ATOM   1502 C  CA  . VAL A 1 182 ? -6.633  -1.743  38.945  1.00 61.09  ? 1652 VAL A CA  1 
ATOM   1503 C  C   . VAL A 1 182 ? -6.049  -1.216  40.249  1.00 64.84  ? 1652 VAL A C   1 
ATOM   1504 O  O   . VAL A 1 182 ? -6.593  -1.475  41.333  1.00 61.91  ? 1652 VAL A O   1 
ATOM   1505 C  CB  . VAL A 1 182 ? -5.987  -3.087  38.546  1.00 64.34  ? 1652 VAL A CB  1 
ATOM   1506 C  CG1 . VAL A 1 182 ? -5.805  -3.986  39.765  1.00 53.72  ? 1652 VAL A CG1 1 
ATOM   1507 C  CG2 . VAL A 1 182 ? -6.805  -3.771  37.466  1.00 52.18  ? 1652 VAL A CG2 1 
ATOM   1508 N  N   . SER A 1 183 ? -4.939  -0.480  40.174  1.00 56.20  ? 1653 SER A N   1 
ATOM   1509 C  CA  . SER A 1 183 ? -4.311  0.156   41.326  1.00 57.63  ? 1653 SER A CA  1 
ATOM   1510 C  C   . SER A 1 183 ? -5.268  1.001   42.158  1.00 69.14  ? 1653 SER A C   1 
ATOM   1511 O  O   . SER A 1 183 ? -4.928  1.376   43.283  1.00 65.93  ? 1653 SER A O   1 
ATOM   1512 C  CB  . SER A 1 183 ? -3.113  1.018   40.878  1.00 68.73  ? 1653 SER A CB  1 
ATOM   1513 O  OG  . SER A 1 183 ? -3.503  1.961   39.902  1.00 83.48  ? 1653 SER A OG  1 
ATOM   1514 N  N   . MET A 1 184 ? -6.436  1.350   41.614  1.00 72.35  ? 1654 MET A N   1 
ATOM   1515 C  CA  . MET A 1 184 ? -7.327  2.259   42.332  1.00 86.96  ? 1654 MET A CA  1 
ATOM   1516 C  C   . MET A 1 184 ? -8.108  1.588   43.462  1.00 96.57  ? 1654 MET A C   1 
ATOM   1517 O  O   . MET A 1 184 ? -8.626  2.294   44.337  1.00 91.19  ? 1654 MET A O   1 
ATOM   1518 C  CB  . MET A 1 184 ? -8.304  2.910   41.349  1.00 69.27  ? 1654 MET A CB  1 
ATOM   1519 C  CG  . MET A 1 184 ? -7.696  3.997   40.452  1.00 67.49  ? 1654 MET A CG  1 
ATOM   1520 S  SD  . MET A 1 184 ? -6.638  5.218   41.264  1.00 77.77  ? 1654 MET A SD  1 
ATOM   1521 C  CE  . MET A 1 184 ? -5.008  4.486   41.143  1.00 73.62  ? 1654 MET A CE  1 
ATOM   1522 N  N   . ASP A 1 185 ? -8.220  0.260   43.464  1.00 105.42 ? 1655 ASP A N   1 
ATOM   1523 C  CA  . ASP A 1 185 ? -8.852  -0.446  44.584  1.00 107.89 ? 1655 ASP A CA  1 
ATOM   1524 C  C   . ASP A 1 185 ? -7.901  -0.560  45.778  1.00 96.72  ? 1655 ASP A C   1 
ATOM   1525 O  O   . ASP A 1 185 ? -8.075  0.117   46.792  1.00 96.54  ? 1655 ASP A O   1 
ATOM   1526 C  CB  . ASP A 1 185 ? -9.347  -1.820  44.145  1.00 110.39 ? 1655 ASP A CB  1 
ATOM   1527 C  CG  . ASP A 1 185 ? -10.333 -1.733  42.994  1.00 121.38 ? 1655 ASP A CG  1 
ATOM   1528 O  OD1 . ASP A 1 185 ? -10.124 -0.898  42.084  1.00 124.28 ? 1655 ASP A OD1 1 
ATOM   1529 O  OD2 . ASP A 1 185 ? -11.335 -2.478  43.015  1.00 126.72 ? 1655 ASP A OD2 1 
ATOM   1530 N  N   . LEU A 1 188 ? -8.457  -5.127  45.142  1.00 122.21 ? 1658 LEU A N   1 
ATOM   1531 C  CA  . LEU A 1 188 ? -7.722  -6.390  45.116  1.00 124.19 ? 1658 LEU A CA  1 
ATOM   1532 C  C   . LEU A 1 188 ? -6.693  -6.453  46.252  1.00 127.34 ? 1658 LEU A C   1 
ATOM   1533 O  O   . LEU A 1 188 ? -6.177  -5.426  46.702  1.00 124.01 ? 1658 LEU A O   1 
ATOM   1534 C  CB  . LEU A 1 188 ? -7.013  -6.595  43.760  1.00 119.42 ? 1658 LEU A CB  1 
ATOM   1535 C  CG  . LEU A 1 188 ? -7.690  -7.178  42.497  1.00 111.24 ? 1658 LEU A CG  1 
ATOM   1536 C  CD1 . LEU A 1 188 ? -6.746  -7.126  41.285  1.00 98.81  ? 1658 LEU A CD1 1 
ATOM   1537 C  CD2 . LEU A 1 188 ? -8.221  -8.602  42.687  1.00 104.11 ? 1658 LEU A CD2 1 
ATOM   1538 N  N   . GLU A 1 189 ? -6.431  -7.665  46.739  1.00 131.79 ? 1659 GLU A N   1 
ATOM   1539 C  CA  . GLU A 1 189 ? -5.287  -7.912  47.605  1.00 133.84 ? 1659 GLU A CA  1 
ATOM   1540 C  C   . GLU A 1 189 ? -4.073  -8.187  46.728  1.00 130.71 ? 1659 GLU A C   1 
ATOM   1541 O  O   . GLU A 1 189 ? -4.110  -9.083  45.881  1.00 136.19 ? 1659 GLU A O   1 
ATOM   1542 C  CB  . GLU A 1 189 ? -5.576  -9.116  48.503  1.00 137.07 ? 1659 GLU A CB  1 
ATOM   1543 C  CG  . GLU A 1 189 ? -7.066  -9.320  48.821  1.00 140.02 ? 1659 GLU A CG  1 
ATOM   1544 C  CD  . GLU A 1 189 ? -7.695  -10.479 48.046  1.00 138.83 ? 1659 GLU A CD  1 
ATOM   1545 O  OE1 . GLU A 1 189 ? -8.290  -11.371 48.686  1.00 139.21 ? 1659 GLU A OE1 1 
ATOM   1546 O  OE2 . GLU A 1 189 ? -7.610  -10.491 46.797  1.00 132.20 ? 1659 GLU A OE2 1 
ATOM   1547 N  N   . GLN A 1 190 ? -2.978  -7.472  46.950  1.00 113.91 ? 1660 GLN A N   1 
ATOM   1548 C  CA  . GLN A 1 190 ? -1.821  -7.631  46.078  1.00 101.43 ? 1660 GLN A CA  1 
ATOM   1549 C  C   . GLN A 1 190 ? -0.691  -8.348  46.807  1.00 94.71  ? 1660 GLN A C   1 
ATOM   1550 O  O   . GLN A 1 190 ? 0.333   -7.768  47.168  1.00 84.20  ? 1660 GLN A O   1 
ATOM   1551 C  CB  . GLN A 1 190 ? -1.391  -6.256  45.529  1.00 102.42 ? 1660 GLN A CB  1 
ATOM   1552 C  CG  . GLN A 1 190 ? -2.559  -5.309  45.179  1.00 95.18  ? 1660 GLN A CG  1 
ATOM   1553 C  CD  . GLN A 1 190 ? -3.508  -5.844  44.104  1.00 95.43  ? 1660 GLN A CD  1 
ATOM   1554 O  OE1 . GLN A 1 190 ? -3.549  -7.048  43.796  1.00 100.16 ? 1660 GLN A OE1 1 
ATOM   1555 N  NE2 . GLN A 1 190 ? -4.277  -4.931  43.516  1.00 75.14  ? 1660 GLN A NE2 1 
ATOM   1556 N  N   . VAL A 1 191 ? -0.882  -9.649  46.969  1.00 97.63  ? 1661 VAL A N   1 
ATOM   1557 C  CA  . VAL A 1 191 ? 0.125   -10.553 47.502  1.00 99.29  ? 1661 VAL A CA  1 
ATOM   1558 C  C   . VAL A 1 191 ? 0.072   -11.817 46.655  1.00 82.54  ? 1661 VAL A C   1 
ATOM   1559 O  O   . VAL A 1 191 ? -0.966  -12.164 46.085  1.00 81.99  ? 1661 VAL A O   1 
ATOM   1560 C  CB  . VAL A 1 191 ? -0.095  -10.852 49.007  1.00 109.57 ? 1661 VAL A CB  1 
ATOM   1561 C  CG1 . VAL A 1 191 ? -1.217  -11.861 49.209  1.00 112.27 ? 1661 VAL A CG1 1 
ATOM   1562 C  CG2 . VAL A 1 191 ? 1.203   -11.324 49.669  1.00 106.59 ? 1661 VAL A CG2 1 
ATOM   1563 N  N   . LEU A 1 192 ? 1.190   -12.478 46.542  1.00 76.71  ? 1662 LEU A N   1 
ATOM   1564 C  CA  . LEU A 1 192 ? 1.156   -13.684 45.742  1.00 74.12  ? 1662 LEU A CA  1 
ATOM   1565 C  C   . LEU A 1 192 ? 0.463   -14.788 46.536  1.00 81.18  ? 1662 LEU A C   1 
ATOM   1566 O  O   . LEU A 1 192 ? 0.572   -14.839 47.765  1.00 88.95  ? 1662 LEU A O   1 
ATOM   1567 C  CB  . LEU A 1 192 ? 2.574   -14.107 45.374  1.00 73.84  ? 1662 LEU A CB  1 
ATOM   1568 C  CG  . LEU A 1 192 ? 3.387   -13.087 44.577  1.00 56.14  ? 1662 LEU A CG  1 
ATOM   1569 C  CD1 . LEU A 1 192 ? 4.869   -13.344 44.722  1.00 69.80  ? 1662 LEU A CD1 1 
ATOM   1570 C  CD2 . LEU A 1 192 ? 2.994   -13.143 43.118  1.00 52.51  ? 1662 LEU A CD2 1 
ATOM   1571 N  N   . PRO A 1 193 ? -0.269  -15.672 45.864  1.00 72.32  ? 1663 PRO A N   1 
ATOM   1572 C  CA  . PRO A 1 193 ? -1.005  -16.713 46.597  1.00 74.46  ? 1663 PRO A CA  1 
ATOM   1573 C  C   . PRO A 1 193 ? -0.049  -17.710 47.234  1.00 75.77  ? 1663 PRO A C   1 
ATOM   1574 O  O   . PRO A 1 193 ? 0.984   -18.064 46.659  1.00 84.10  ? 1663 PRO A O   1 
ATOM   1575 C  CB  . PRO A 1 193 ? -1.878  -17.373 45.522  1.00 75.00  ? 1663 PRO A CB  1 
ATOM   1576 C  CG  . PRO A 1 193 ? -1.725  -16.526 44.280  1.00 75.48  ? 1663 PRO A CG  1 
ATOM   1577 C  CD  . PRO A 1 193 ? -0.454  -15.753 44.408  1.00 58.80  ? 1663 PRO A CD  1 
ATOM   1578 N  N   . ARG A 1 194 ? -0.398  -18.153 48.438  1.00 78.49  ? 1664 ARG A N   1 
ATOM   1579 C  CA  . ARG A 1 194 ? 0.373   -19.145 49.171  1.00 82.67  ? 1664 ARG A CA  1 
ATOM   1580 C  C   . ARG A 1 194 ? -0.332  -20.496 49.149  1.00 79.76  ? 1664 ARG A C   1 
ATOM   1581 O  O   . ARG A 1 194 ? -1.556  -20.577 49.015  1.00 77.54  ? 1664 ARG A O   1 
ATOM   1582 C  CB  . ARG A 1 194 ? 0.587   -18.707 50.620  1.00 90.44  ? 1664 ARG A CB  1 
ATOM   1583 C  CG  . ARG A 1 194 ? 1.082   -17.292 50.762  1.00 93.58  ? 1664 ARG A CG  1 
ATOM   1584 C  CD  . ARG A 1 194 ? 1.753   -17.074 52.102  1.00 99.85  ? 1664 ARG A CD  1 
ATOM   1585 N  NE  . ARG A 1 194 ? 3.196   -17.266 51.994  1.00 110.36 ? 1664 ARG A NE  1 
ATOM   1586 C  CZ  . ARG A 1 194 ? 4.028   -16.408 51.409  1.00 113.86 ? 1664 ARG A CZ  1 
ATOM   1587 N  NH1 . ARG A 1 194 ? 5.329   -16.679 51.353  1.00 109.00 ? 1664 ARG A NH1 1 
ATOM   1588 N  NH2 . ARG A 1 194 ? 3.562   -15.280 50.882  1.00 115.41 ? 1664 ARG A NH2 1 
ATOM   1589 N  N   . ASP A 1 195 ? 0.455   -21.558 49.260  1.00 81.62  ? 1665 ASP A N   1 
ATOM   1590 C  CA  . ASP A 1 195 ? -0.075  -22.908 49.260  1.00 84.91  ? 1665 ASP A CA  1 
ATOM   1591 C  C   . ASP A 1 195 ? -0.116  -23.440 50.689  1.00 83.86  ? 1665 ASP A C   1 
ATOM   1592 O  O   . ASP A 1 195 ? 0.140   -22.718 51.660  1.00 75.66  ? 1665 ASP A O   1 
ATOM   1593 C  CB  . ASP A 1 195 ? 0.748   -23.825 48.341  1.00 80.21  ? 1665 ASP A CB  1 
ATOM   1594 C  CG  . ASP A 1 195 ? 2.189   -24.031 48.821  1.00 82.47  ? 1665 ASP A CG  1 
ATOM   1595 O  OD1 . ASP A 1 195 ? 2.513   -23.698 49.980  1.00 83.77  ? 1665 ASP A OD1 1 
ATOM   1596 O  OD2 . ASP A 1 195 ? 3.011   -24.542 48.025  1.00 81.63  ? 1665 ASP A OD2 1 
ATOM   1597 N  N   . GLU A 1 196 ? -0.391  -24.737 50.814  1.00 77.14  ? 1666 GLU A N   1 
ATOM   1598 C  CA  . GLU A 1 196 ? -0.465  -25.365 52.123  1.00 88.36  ? 1666 GLU A CA  1 
ATOM   1599 C  C   . GLU A 1 196 ? 0.863   -25.328 52.866  1.00 88.03  ? 1666 GLU A C   1 
ATOM   1600 O  O   . GLU A 1 196 ? 0.876   -25.546 54.081  1.00 95.09  ? 1666 GLU A O   1 
ATOM   1601 C  CB  . GLU A 1 196 ? -0.952  -26.810 51.978  1.00 97.31  ? 1666 GLU A CB  1 
ATOM   1602 C  CG  . GLU A 1 196 ? -0.120  -27.645 51.014  1.00 99.14  ? 1666 GLU A CG  1 
ATOM   1603 C  CD  . GLU A 1 196 ? -0.502  -29.116 51.029  1.00 100.90 ? 1666 GLU A CD  1 
ATOM   1604 O  OE1 . GLU A 1 196 ? -0.725  -29.684 49.935  1.00 99.65  ? 1666 GLU A OE1 1 
ATOM   1605 O  OE2 . GLU A 1 196 ? -0.582  -29.703 52.131  1.00 103.69 ? 1666 GLU A OE2 1 
ATOM   1606 N  N   . ARG A 1 197 ? 1.979   -25.072 52.177  1.00 84.84  ? 1667 ARG A N   1 
ATOM   1607 C  CA  . ARG A 1 197 ? 3.263   -24.961 52.864  1.00 84.77  ? 1667 ARG A CA  1 
ATOM   1608 C  C   . ARG A 1 197 ? 3.472   -23.600 53.502  1.00 88.46  ? 1667 ARG A C   1 
ATOM   1609 O  O   . ARG A 1 197 ? 4.495   -23.398 54.172  1.00 85.78  ? 1667 ARG A O   1 
ATOM   1610 C  CB  . ARG A 1 197 ? 4.441   -25.237 51.920  1.00 80.75  ? 1667 ARG A CB  1 
ATOM   1611 C  CG  . ARG A 1 197 ? 4.496   -26.632 51.340  1.00 82.88  ? 1667 ARG A CG  1 
ATOM   1612 C  CD  . ARG A 1 197 ? 5.459   -26.683 50.158  1.00 80.27  ? 1667 ARG A CD  1 
ATOM   1613 N  NE  . ARG A 1 197 ? 5.258   -25.563 49.246  1.00 75.21  ? 1667 ARG A NE  1 
ATOM   1614 C  CZ  . ARG A 1 197 ? 6.149   -25.179 48.340  1.00 69.06  ? 1667 ARG A CZ  1 
ATOM   1615 N  NH1 . ARG A 1 197 ? 7.298   -25.833 48.225  1.00 51.37  ? 1667 ARG A NH1 1 
ATOM   1616 N  NH2 . ARG A 1 197 ? 5.885   -24.148 47.546  1.00 62.33  ? 1667 ARG A NH2 1 
ATOM   1617 N  N   . GLY A 1 198 ? 2.558   -22.658 53.279  1.00 89.84  ? 1668 GLY A N   1 
ATOM   1618 C  CA  . GLY A 1 198 ? 2.845   -21.298 53.671  1.00 105.30 ? 1668 GLY A CA  1 
ATOM   1619 C  C   . GLY A 1 198 ? 3.871   -20.639 52.785  1.00 107.48 ? 1668 GLY A C   1 
ATOM   1620 O  O   . GLY A 1 198 ? 4.482   -19.644 53.185  1.00 116.20 ? 1668 GLY A O   1 
ATOM   1621 N  N   . ALA A 1 199 ? 4.099   -21.194 51.600  1.00 86.88  ? 1669 ALA A N   1 
ATOM   1622 C  CA  . ALA A 1 199 ? 5.003   -20.632 50.616  1.00 73.87  ? 1669 ALA A CA  1 
ATOM   1623 C  C   . ALA A 1 199 ? 4.211   -20.193 49.391  1.00 72.01  ? 1669 ALA A C   1 
ATOM   1624 O  O   . ALA A 1 199 ? 3.107   -20.682 49.131  1.00 69.23  ? 1669 ALA A O   1 
ATOM   1625 C  CB  . ALA A 1 199 ? 6.082   -21.648 50.226  1.00 75.67  ? 1669 ALA A CB  1 
ATOM   1626 N  N   . TYR A 1 200 ? 4.791   -19.245 48.654  1.00 78.14  ? 1670 TYR A N   1 
ATOM   1627 C  CA  . TYR A 1 200 ? 4.277   -18.831 47.350  1.00 75.25  ? 1670 TYR A CA  1 
ATOM   1628 C  C   . TYR A 1 200 ? 4.043   -20.063 46.484  1.00 71.50  ? 1670 TYR A C   1 
ATOM   1629 O  O   . TYR A 1 200 ? 4.926   -20.915 46.355  1.00 70.23  ? 1670 TYR A O   1 
ATOM   1630 C  CB  . TYR A 1 200 ? 5.285   -17.863 46.705  1.00 66.48  ? 1670 TYR A CB  1 
ATOM   1631 C  CG  . TYR A 1 200 ? 5.180   -17.618 45.208  1.00 58.80  ? 1670 TYR A CG  1 
ATOM   1632 C  CD1 . TYR A 1 200 ? 3.969   -17.278 44.606  1.00 56.47  ? 1670 TYR A CD1 1 
ATOM   1633 C  CD2 . TYR A 1 200 ? 6.314   -17.692 44.403  1.00 55.77  ? 1670 TYR A CD2 1 
ATOM   1634 C  CE1 . TYR A 1 200 ? 3.890   -17.037 43.235  1.00 48.34  ? 1670 TYR A CE1 1 
ATOM   1635 C  CE2 . TYR A 1 200 ? 6.248   -17.455 43.041  1.00 45.75  ? 1670 TYR A CE2 1 
ATOM   1636 C  CZ  . TYR A 1 200 ? 5.039   -17.126 42.462  1.00 48.77  ? 1670 TYR A CZ  1 
ATOM   1637 O  OH  . TYR A 1 200 ? 4.990   -16.909 41.100  1.00 52.63  ? 1670 TYR A OH  1 
ATOM   1638 N  N   . GLU A 1 201 ? 2.832   -20.171 45.917  1.00 66.36  ? 1671 GLU A N   1 
ATOM   1639 C  CA  . GLU A 1 201 ? 2.374   -21.452 45.379  1.00 59.32  ? 1671 GLU A CA  1 
ATOM   1640 C  C   . GLU A 1 201 ? 3.264   -21.950 44.248  1.00 66.30  ? 1671 GLU A C   1 
ATOM   1641 O  O   . GLU A 1 201 ? 3.375   -23.165 44.039  1.00 54.35  ? 1671 GLU A O   1 
ATOM   1642 C  CB  . GLU A 1 201 ? 0.914   -21.357 44.904  1.00 65.53  ? 1671 GLU A CB  1 
ATOM   1643 C  CG  . GLU A 1 201 ? 0.622   -20.280 43.850  1.00 77.49  ? 1671 GLU A CG  1 
ATOM   1644 C  CD  . GLU A 1 201 ? -0.767  -20.413 43.190  1.00 83.67  ? 1671 GLU A CD  1 
ATOM   1645 O  OE1 . GLU A 1 201 ? -1.784  -20.620 43.912  1.00 67.47  ? 1671 GLU A OE1 1 
ATOM   1646 O  OE2 . GLU A 1 201 ? -0.828  -20.300 41.937  1.00 75.96  ? 1671 GLU A OE2 1 
ATOM   1647 N  N   . ALA A 1 202 ? 3.948   -21.041 43.552  1.00 61.22  ? 1672 ALA A N   1 
ATOM   1648 C  CA  . ALA A 1 202 ? 4.821   -21.396 42.446  1.00 53.06  ? 1672 ALA A CA  1 
ATOM   1649 C  C   . ALA A 1 202 ? 6.251   -21.662 42.879  1.00 56.49  ? 1672 ALA A C   1 
ATOM   1650 O  O   . ALA A 1 202 ? 7.090   -21.965 42.026  1.00 47.44  ? 1672 ALA A O   1 
ATOM   1651 C  CB  . ALA A 1 202 ? 4.801   -20.299 41.380  1.00 50.17  ? 1672 ALA A CB  1 
ATOM   1652 N  N   . SER A 1 203 ? 6.548   -21.585 44.171  1.00 59.69  ? 1673 SER A N   1 
ATOM   1653 C  CA  . SER A 1 203 ? 7.924   -21.623 44.628  1.00 69.98  ? 1673 SER A CA  1 
ATOM   1654 C  C   . SER A 1 203 ? 8.334   -23.048 44.976  1.00 66.04  ? 1673 SER A C   1 
ATOM   1655 O  O   . SER A 1 203 ? 7.619   -23.754 45.695  1.00 60.80  ? 1673 SER A O   1 
ATOM   1656 C  CB  . SER A 1 203 ? 8.098   -20.707 45.842  1.00 80.75  ? 1673 SER A CB  1 
ATOM   1657 O  OG  . SER A 1 203 ? 9.085   -21.203 46.732  1.00 96.27  ? 1673 SER A OG  1 
ATOM   1658 N  N   . LEU A 1 204 ? 9.493   -23.462 44.459  1.00 64.04  ? 1674 LEU A N   1 
ATOM   1659 C  CA  . LEU A 1 204 ? 10.009  -24.788 44.765  1.00 65.42  ? 1674 LEU A CA  1 
ATOM   1660 C  C   . LEU A 1 204 ? 10.591  -24.826 46.169  1.00 64.81  ? 1674 LEU A C   1 
ATOM   1661 O  O   . LEU A 1 204 ? 10.578  -25.878 46.814  1.00 62.56  ? 1674 LEU A O   1 
ATOM   1662 C  CB  . LEU A 1 204 ? 11.066  -25.217 43.735  1.00 59.70  ? 1674 LEU A CB  1 
ATOM   1663 C  CG  . LEU A 1 204 ? 10.708  -25.242 42.242  1.00 55.07  ? 1674 LEU A CG  1 
ATOM   1664 C  CD1 . LEU A 1 204 ? 11.833  -25.870 41.423  1.00 64.12  ? 1674 LEU A CD1 1 
ATOM   1665 C  CD2 . LEU A 1 204 ? 9.412   -25.971 41.987  1.00 55.56  ? 1674 LEU A CD2 1 
ATOM   1666 N  N   . VAL A 1 205 ? 11.088  -23.698 46.664  1.00 79.56  ? 1675 VAL A N   1 
ATOM   1667 C  CA  . VAL A 1 205 ? 11.635  -23.627 48.011  1.00 87.26  ? 1675 VAL A CA  1 
ATOM   1668 C  C   . VAL A 1 205 ? 10.532  -23.174 48.956  1.00 104.01 ? 1675 VAL A C   1 
ATOM   1669 O  O   . VAL A 1 205 ? 9.947   -22.097 48.784  1.00 101.04 ? 1675 VAL A O   1 
ATOM   1670 C  CB  . VAL A 1 205 ? 12.845  -22.685 48.080  1.00 85.34  ? 1675 VAL A CB  1 
ATOM   1671 C  CG1 . VAL A 1 205 ? 12.490  -21.281 47.571  1.00 86.61  ? 1675 VAL A CG1 1 
ATOM   1672 C  CG2 . VAL A 1 205 ? 13.360  -22.623 49.506  1.00 89.57  ? 1675 VAL A CG2 1 
ATOM   1673 N  N   . ALA A 1 206 ? 10.220  -24.004 49.943  1.00 120.08 ? 1676 ALA A N   1 
ATOM   1674 C  CA  . ALA A 1 206 ? 9.324   -23.560 50.998  1.00 131.65 ? 1676 ALA A CA  1 
ATOM   1675 C  C   . ALA A 1 206 ? 10.172  -22.724 51.940  1.00 137.82 ? 1676 ALA A C   1 
ATOM   1676 O  O   . ALA A 1 206 ? 11.027  -23.257 52.655  1.00 132.74 ? 1676 ALA A O   1 
ATOM   1677 C  CB  . ALA A 1 206 ? 8.671   -24.740 51.711  1.00 131.48 ? 1676 ALA A CB  1 
ATOM   1678 N  N   . ALA A 1 207 ? 9.965   -21.407 51.908  1.00 145.87 ? 1677 ALA A N   1 
ATOM   1679 C  CA  . ALA A 1 207 ? 10.754  -20.527 52.756  1.00 151.04 ? 1677 ALA A CA  1 
ATOM   1680 C  C   . ALA A 1 207 ? 10.646  -20.957 54.209  1.00 149.57 ? 1677 ALA A C   1 
ATOM   1681 O  O   . ALA A 1 207 ? 11.646  -20.982 54.937  1.00 152.09 ? 1677 ALA A O   1 
ATOM   1682 C  CB  . ALA A 1 207 ? 10.300  -19.080 52.575  1.00 153.41 ? 1677 ALA A CB  1 
ATOM   1683 N  N   . SER A 1 208 ? 9.440   -21.340 54.628  1.00 141.02 ? 1678 SER A N   1 
ATOM   1684 C  CA  . SER A 1 208 ? 9.176   -21.836 55.971  1.00 132.57 ? 1678 SER A CA  1 
ATOM   1685 C  C   . SER A 1 208 ? 10.006  -23.074 56.280  1.00 134.39 ? 1678 SER A C   1 
ATOM   1686 O  O   . SER A 1 208 ? 10.985  -23.007 57.032  1.00 123.11 ? 1678 SER A O   1 
ATOM   1687 C  CB  . SER A 1 208 ? 7.682   -22.147 56.122  1.00 119.58 ? 1678 SER A CB  1 
ATOM   1688 O  OG  . SER A 1 208 ? 7.469   -23.246 56.991  1.00 111.96 ? 1678 SER A OG  1 
ATOM   1689 N  N   . THR A 1 209 ? 9.632   -24.203 55.678  1.00 146.00 ? 1679 THR A N   1 
ATOM   1690 C  CA  . THR A 1 209 ? 10.307  -25.466 55.960  1.00 147.33 ? 1679 THR A CA  1 
ATOM   1691 C  C   . THR A 1 209 ? 11.763  -25.434 55.497  1.00 149.17 ? 1679 THR A C   1 
ATOM   1692 O  O   . THR A 1 209 ? 12.693  -25.503 56.312  1.00 157.30 ? 1679 THR A O   1 
ATOM   1693 C  CB  . THR A 1 209 ? 9.537   -26.618 55.304  1.00 139.05 ? 1679 THR A CB  1 
ATOM   1694 O  OG1 . THR A 1 209 ? 9.856   -26.687 53.908  1.00 138.13 ? 1679 THR A OG1 1 
ATOM   1695 C  CG2 . THR A 1 209 ? 8.037   -26.401 55.458  1.00 131.61 ? 1679 THR A CG2 1 
ATOM   1696 N  N   . GLY A 1 210 ? 11.981  -25.322 54.198  1.00 139.48 ? 1680 GLY A N   1 
ATOM   1697 C  CA  . GLY A 1 210 ? 13.305  -25.379 53.627  1.00 129.64 ? 1680 GLY A CA  1 
ATOM   1698 C  C   . GLY A 1 210 ? 13.597  -26.656 52.873  1.00 128.59 ? 1680 GLY A C   1 
ATOM   1699 O  O   . GLY A 1 210 ? 14.774  -27.020 52.736  1.00 126.32 ? 1680 GLY A O   1 
ATOM   1700 N  N   . VAL A 1 211 ? 12.569  -27.345 52.388  1.00 128.23 ? 1681 VAL A N   1 
ATOM   1701 C  CA  . VAL A 1 211 ? 12.709  -28.484 51.490  1.00 118.87 ? 1681 VAL A CA  1 
ATOM   1702 C  C   . VAL A 1 211 ? 12.397  -28.006 50.080  1.00 112.48 ? 1681 VAL A C   1 
ATOM   1703 O  O   . VAL A 1 211 ? 11.383  -27.335 49.850  1.00 116.94 ? 1681 VAL A O   1 
ATOM   1704 C  CB  . VAL A 1 211 ? 11.781  -29.644 51.890  1.00 110.93 ? 1681 VAL A CB  1 
ATOM   1705 C  CG1 . VAL A 1 211 ? 11.924  -30.806 50.912  1.00 96.62  ? 1681 VAL A CG1 1 
ATOM   1706 C  CG2 . VAL A 1 211 ? 12.072  -30.088 53.316  1.00 111.34 ? 1681 VAL A CG2 1 
ATOM   1707 N  N   . ARG A 1 212 ? 13.265  -28.352 49.141  1.00 100.13 ? 1682 ARG A N   1 
ATOM   1708 C  CA  . ARG A 1 212 ? 13.076  -28.005 47.740  1.00 78.99  ? 1682 ARG A CA  1 
ATOM   1709 C  C   . ARG A 1 212 ? 12.144  -29.028 47.117  1.00 70.42  ? 1682 ARG A C   1 
ATOM   1710 O  O   . ARG A 1 212 ? 12.452  -30.223 47.092  1.00 76.63  ? 1682 ARG A O   1 
ATOM   1711 C  CB  . ARG A 1 212 ? 14.417  -27.972 47.022  1.00 74.11  ? 1682 ARG A CB  1 
ATOM   1712 C  CG  . ARG A 1 212 ? 15.149  -26.682 47.220  1.00 78.68  ? 1682 ARG A CG  1 
ATOM   1713 C  CD  . ARG A 1 212 ? 14.624  -25.681 46.232  1.00 91.80  ? 1682 ARG A CD  1 
ATOM   1714 N  NE  . ARG A 1 212 ? 14.789  -26.189 44.878  1.00 91.61  ? 1682 ARG A NE  1 
ATOM   1715 C  CZ  . ARG A 1 212 ? 15.886  -26.003 44.153  1.00 98.24  ? 1682 ARG A CZ  1 
ATOM   1716 N  NH1 . ARG A 1 212 ? 16.906  -25.311 44.658  1.00 97.74  ? 1682 ARG A NH1 1 
ATOM   1717 N  NH2 . ARG A 1 212 ? 15.965  -26.503 42.926  1.00 98.13  ? 1682 ARG A NH2 1 
ATOM   1718 N  N   . ALA A 1 213 ? 10.974  -28.580 46.694  1.00 61.94  ? 1683 ALA A N   1 
ATOM   1719 C  CA  . ALA A 1 213 ? 10.050  -29.458 45.998  1.00 69.54  ? 1683 ALA A CA  1 
ATOM   1720 C  C   . ALA A 1 213 ? 10.483  -29.673 44.556  1.00 59.36  ? 1683 ALA A C   1 
ATOM   1721 O  O   . ALA A 1 213 ? 11.111  -28.813 43.935  1.00 63.46  ? 1683 ALA A O   1 
ATOM   1722 C  CB  . ALA A 1 213 ? 8.637   -28.878 46.034  1.00 72.14  ? 1683 ALA A CB  1 
ATOM   1723 N  N   . LEU A 1 214 ? 10.125  -30.829 44.019  1.00 64.75  ? 1684 LEU A N   1 
ATOM   1724 C  CA  . LEU A 1 214 ? 10.410  -31.098 42.625  1.00 52.56  ? 1684 LEU A CA  1 
ATOM   1725 C  C   . LEU A 1 214 ? 9.452   -30.293 41.752  1.00 62.24  ? 1684 LEU A C   1 
ATOM   1726 O  O   . LEU A 1 214 ? 8.279   -30.122 42.108  1.00 62.70  ? 1684 LEU A O   1 
ATOM   1727 C  CB  . LEU A 1 214 ? 10.254  -32.589 42.324  1.00 57.01  ? 1684 LEU A CB  1 
ATOM   1728 C  CG  . LEU A 1 214 ? 11.200  -33.534 43.045  1.00 64.90  ? 1684 LEU A CG  1 
ATOM   1729 C  CD1 . LEU A 1 214 ? 11.048  -34.957 42.520  1.00 66.95  ? 1684 LEU A CD1 1 
ATOM   1730 C  CD2 . LEU A 1 214 ? 12.629  -33.036 42.887  1.00 56.12  ? 1684 LEU A CD2 1 
ATOM   1731 N  N   . PRO A 1 215 ? 9.909   -29.789 40.616  1.00 57.00  ? 1685 PRO A N   1 
ATOM   1732 C  CA  . PRO A 1 215 ? 8.994   -29.080 39.717  1.00 52.16  ? 1685 PRO A CA  1 
ATOM   1733 C  C   . PRO A 1 215 ? 8.265   -30.042 38.790  1.00 60.09  ? 1685 PRO A C   1 
ATOM   1734 O  O   . PRO A 1 215 ? 8.895   -30.886 38.144  1.00 54.78  ? 1685 PRO A O   1 
ATOM   1735 C  CB  . PRO A 1 215 ? 9.922   -28.137 38.942  1.00 53.75  ? 1685 PRO A CB  1 
ATOM   1736 C  CG  . PRO A 1 215 ? 11.244  -28.858 38.936  1.00 54.97  ? 1685 PRO A CG  1 
ATOM   1737 C  CD  . PRO A 1 215 ? 11.318  -29.659 40.213  1.00 45.31  ? 1685 PRO A CD  1 
ATOM   1738 N  N   . CYS A 1 216 ? 6.945   -29.890 38.675  1.00 43.28  ? 1686 CYS A N   1 
ATOM   1739 C  CA  . CYS A 1 216 ? 6.166   -30.773 37.819  1.00 41.68  ? 1686 CYS A CA  1 
ATOM   1740 C  C   . CYS A 1 216 ? 6.578   -30.580 36.355  1.00 49.27  ? 1686 CYS A C   1 
ATOM   1741 O  O   . CYS A 1 216 ? 6.755   -29.451 35.881  1.00 43.94  ? 1686 CYS A O   1 
ATOM   1742 C  CB  . CYS A 1 216 ? 4.663   -30.489 38.015  1.00 41.76  ? 1686 CYS A CB  1 
ATOM   1743 S  SG  . CYS A 1 216 ? 3.540   -31.305 36.854  1.00 51.44  ? 1686 CYS A SG  1 
ATOM   1744 N  N   . LEU A 1 217 ? 6.746   -31.695 35.635  1.00 44.06  ? 1687 LEU A N   1 
ATOM   1745 C  CA  . LEU A 1 217 ? 7.167   -31.641 34.236  1.00 41.72  ? 1687 LEU A CA  1 
ATOM   1746 C  C   . LEU A 1 217 ? 6.098   -31.033 33.334  1.00 38.80  ? 1687 LEU A C   1 
ATOM   1747 O  O   . LEU A 1 217 ? 6.404   -30.641 32.207  1.00 42.89  ? 1687 LEU A O   1 
ATOM   1748 C  CB  . LEU A 1 217 ? 7.493   -33.053 33.723  1.00 43.79  ? 1687 LEU A CB  1 
ATOM   1749 C  CG  . LEU A 1 217 ? 8.908   -33.575 33.948  1.00 50.15  ? 1687 LEU A CG  1 
ATOM   1750 C  CD1 . LEU A 1 217 ? 9.034   -35.077 33.587  1.00 53.09  ? 1687 LEU A CD1 1 
ATOM   1751 C  CD2 . LEU A 1 217 ? 9.902   -32.755 33.144  1.00 58.57  ? 1687 LEU A CD2 1 
ATOM   1752 N  N   . ILE A 1 218 ? 4.857   -30.943 33.804  1.00 38.68  ? 1688 ILE A N   1 
ATOM   1753 C  CA  . ILE A 1 218 ? 3.751   -30.430 33.013  1.00 38.97  ? 1688 ILE A CA  1 
ATOM   1754 C  C   . ILE A 1 218 ? 3.509   -28.945 33.285  1.00 41.20  ? 1688 ILE A C   1 
ATOM   1755 O  O   . ILE A 1 218 ? 3.291   -28.173 32.354  1.00 43.49  ? 1688 ILE A O   1 
ATOM   1756 C  CB  . ILE A 1 218 ? 2.473   -31.271 33.260  1.00 43.91  ? 1688 ILE A CB  1 
ATOM   1757 C  CG1 . ILE A 1 218 ? 2.712   -32.759 32.925  1.00 45.86  ? 1688 ILE A CG1 1 
ATOM   1758 C  CG2 . ILE A 1 218 ? 1.279   -30.676 32.501  1.00 42.14  ? 1688 ILE A CG2 1 
ATOM   1759 C  CD1 . ILE A 1 218 ? 3.132   -33.053 31.465  1.00 41.16  ? 1688 ILE A CD1 1 
ATOM   1760 N  N   . THR A 1 219 ? 3.530   -28.517 34.546  1.00 38.23  ? 1689 THR A N   1 
ATOM   1761 C  CA  . THR A 1 219 ? 3.251   -27.129 34.860  1.00 40.05  ? 1689 THR A CA  1 
ATOM   1762 C  C   . THR A 1 219 ? 4.426   -26.363 35.454  1.00 52.55  ? 1689 THR A C   1 
ATOM   1763 O  O   . THR A 1 219 ? 4.345   -25.136 35.555  1.00 47.19  ? 1689 THR A O   1 
ATOM   1764 C  CB  . THR A 1 219 ? 2.074   -27.019 35.840  1.00 44.94  ? 1689 THR A CB  1 
ATOM   1765 O  OG1 . THR A 1 219 ? 2.484   -27.538 37.110  1.00 41.00  ? 1689 THR A OG1 1 
ATOM   1766 C  CG2 . THR A 1 219 ? 0.842   -27.761 35.328  1.00 50.30  ? 1689 THR A CG2 1 
ATOM   1767 N  N   . GLY A 1 220 ? 5.487   -27.033 35.891  1.00 49.74  ? 1690 GLY A N   1 
ATOM   1768 C  CA  . GLY A 1 220 ? 6.579   -26.355 36.562  1.00 41.37  ? 1690 GLY A CA  1 
ATOM   1769 C  C   . GLY A 1 220 ? 6.373   -26.115 38.047  1.00 47.77  ? 1690 GLY A C   1 
ATOM   1770 O  O   . GLY A 1 220 ? 7.350   -25.839 38.760  1.00 46.04  ? 1690 GLY A O   1 
ATOM   1771 N  N   . TYR A 1 221 ? 5.136   -26.207 38.535  1.00 43.99  ? 1691 TYR A N   1 
ATOM   1772 C  CA  . TYR A 1 221 ? 4.822   -25.921 39.927  1.00 50.89  ? 1691 TYR A CA  1 
ATOM   1773 C  C   . TYR A 1 221 ? 5.429   -26.974 40.844  1.00 50.30  ? 1691 TYR A C   1 
ATOM   1774 O  O   . TYR A 1 221 ? 5.703   -28.097 40.420  1.00 51.36  ? 1691 TYR A O   1 
ATOM   1775 C  CB  . TYR A 1 221 ? 3.302   -25.864 40.128  1.00 47.26  ? 1691 TYR A CB  1 
ATOM   1776 C  CG  . TYR A 1 221 ? 2.720   -24.478 40.000  1.00 53.97  ? 1691 TYR A CG  1 
ATOM   1777 C  CD1 . TYR A 1 221 ? 3.138   -23.629 38.984  1.00 53.59  ? 1691 TYR A CD1 1 
ATOM   1778 C  CD2 . TYR A 1 221 ? 1.761   -24.009 40.896  1.00 54.12  ? 1691 TYR A CD2 1 
ATOM   1779 C  CE1 . TYR A 1 221 ? 2.615   -22.365 38.845  1.00 49.69  ? 1691 TYR A CE1 1 
ATOM   1780 C  CE2 . TYR A 1 221 ? 1.235   -22.729 40.771  1.00 63.09  ? 1691 TYR A CE2 1 
ATOM   1781 C  CZ  . TYR A 1 221 ? 1.676   -21.907 39.737  1.00 51.94  ? 1691 TYR A CZ  1 
ATOM   1782 O  OH  . TYR A 1 221 ? 1.181   -20.626 39.582  1.00 46.41  ? 1691 TYR A OH  1 
ATOM   1783 N  N   . PRO A 1 222 ? 5.638   -26.640 42.114  1.00 49.74  ? 1692 PRO A N   1 
ATOM   1784 C  CA  . PRO A 1 222 ? 6.124   -27.651 43.062  1.00 45.33  ? 1692 PRO A CA  1 
ATOM   1785 C  C   . PRO A 1 222 ? 5.122   -28.788 43.221  1.00 59.63  ? 1692 PRO A C   1 
ATOM   1786 O  O   . PRO A 1 222 ? 3.922   -28.571 43.390  1.00 53.40  ? 1692 PRO A O   1 
ATOM   1787 C  CB  . PRO A 1 222 ? 6.298   -26.858 44.358  1.00 54.09  ? 1692 PRO A CB  1 
ATOM   1788 C  CG  . PRO A 1 222 ? 5.341   -25.694 44.211  1.00 58.66  ? 1692 PRO A CG  1 
ATOM   1789 C  CD  . PRO A 1 222 ? 5.389   -25.338 42.764  1.00 48.83  ? 1692 PRO A CD  1 
ATOM   1790 N  N   . ILE A 1 223 ? 5.624   -30.014 43.156  1.00 61.76  ? 1693 ILE A N   1 
ATOM   1791 C  CA  . ILE A 1 223 ? 4.791   -31.182 43.396  1.00 67.88  ? 1693 ILE A CA  1 
ATOM   1792 C  C   . ILE A 1 223 ? 4.605   -31.315 44.903  1.00 67.75  ? 1693 ILE A C   1 
ATOM   1793 O  O   . ILE A 1 223 ? 5.562   -31.579 45.634  1.00 68.19  ? 1693 ILE A O   1 
ATOM   1794 C  CB  . ILE A 1 223 ? 5.407   -32.446 42.791  1.00 72.32  ? 1693 ILE A CB  1 
ATOM   1795 C  CG1 . ILE A 1 223 ? 5.776   -32.191 41.331  1.00 60.02  ? 1693 ILE A CG1 1 
ATOM   1796 C  CG2 . ILE A 1 223 ? 4.416   -33.602 42.898  1.00 69.20  ? 1693 ILE A CG2 1 
ATOM   1797 C  CD1 . ILE A 1 223 ? 6.307   -33.401 40.620  1.00 52.70  ? 1693 ILE A CD1 1 
ATOM   1798 N  N   . LEU A 1 224 ? 3.379   -31.099 45.373  1.00 65.70  ? 1694 LEU A N   1 
ATOM   1799 C  CA  . LEU A 1 224 ? 3.082   -31.170 46.795  1.00 72.29  ? 1694 LEU A CA  1 
ATOM   1800 C  C   . LEU A 1 224 ? 2.367   -32.444 47.192  1.00 72.69  ? 1694 LEU A C   1 
ATOM   1801 O  O   . LEU A 1 224 ? 2.433   -32.840 48.361  1.00 77.46  ? 1694 LEU A O   1 
ATOM   1802 C  CB  . LEU A 1 224 ? 2.200   -29.989 47.213  1.00 69.54  ? 1694 LEU A CB  1 
ATOM   1803 C  CG  . LEU A 1 224 ? 2.780   -28.607 46.975  1.00 66.96  ? 1694 LEU A CG  1 
ATOM   1804 C  CD1 . LEU A 1 224 ? 1.963   -27.592 47.732  1.00 60.41  ? 1694 LEU A CD1 1 
ATOM   1805 C  CD2 . LEU A 1 224 ? 4.214   -28.607 47.438  1.00 73.91  ? 1694 LEU A CD2 1 
ATOM   1806 N  N   . ARG A 1 225 ? 1.685   -33.079 46.248  1.00 60.46  ? 1695 ARG A N   1 
ATOM   1807 C  CA  . ARG A 1 225 ? 0.938   -34.295 46.503  1.00 71.09  ? 1695 ARG A CA  1 
ATOM   1808 C  C   . ARG A 1 225 ? 0.820   -35.031 45.182  1.00 67.83  ? 1695 ARG A C   1 
ATOM   1809 O  O   . ARG A 1 225 ? 0.971   -34.435 44.115  1.00 63.02  ? 1695 ARG A O   1 
ATOM   1810 C  CB  . ARG A 1 225 ? -0.449  -33.975 47.062  1.00 66.99  ? 1695 ARG A CB  1 
ATOM   1811 C  CG  . ARG A 1 225 ? -1.311  -33.263 46.032  1.00 71.08  ? 1695 ARG A CG  1 
ATOM   1812 C  CD  . ARG A 1 225 ? -2.504  -32.510 46.597  1.00 78.11  ? 1695 ARG A CD  1 
ATOM   1813 N  NE  . ARG A 1 225 ? -2.258  -31.872 47.886  1.00 93.01  ? 1695 ARG A NE  1 
ATOM   1814 C  CZ  . ARG A 1 225 ? -3.120  -31.038 48.463  1.00 107.36 ? 1695 ARG A CZ  1 
ATOM   1815 N  NH1 . ARG A 1 225 ? -4.263  -30.737 47.855  1.00 105.79 ? 1695 ARG A NH1 1 
ATOM   1816 N  NH2 . ARG A 1 225 ? -2.841  -30.495 49.639  1.00 113.62 ? 1695 ARG A NH2 1 
ATOM   1817 N  N   . ASN A 1 226 ? 0.527   -36.329 45.257  1.00 72.61  ? 1696 ASN A N   1 
ATOM   1818 C  CA  . ASN A 1 226 ? 0.247   -37.127 44.060  1.00 61.43  ? 1696 ASN A CA  1 
ATOM   1819 C  C   . ASN A 1 226 ? 1.444   -37.176 43.119  1.00 60.77  ? 1696 ASN A C   1 
ATOM   1820 O  O   . ASN A 1 226 ? 1.298   -37.115 41.896  1.00 66.42  ? 1696 ASN A O   1 
ATOM   1821 C  CB  . ASN A 1 226 ? -0.969  -36.585 43.309  1.00 53.84  ? 1696 ASN A CB  1 
ATOM   1822 C  CG  . ASN A 1 226 ? -2.260  -37.144 43.811  1.00 74.71  ? 1696 ASN A CG  1 
ATOM   1823 O  OD1 . ASN A 1 226 ? -2.286  -38.065 44.632  1.00 80.03  ? 1696 ASN A OD1 1 
ATOM   1824 N  ND2 . ASN A 1 226 ? -3.356  -36.600 43.307  1.00 78.55  ? 1696 ASN A ND2 1 
ATOM   1825 N  N   . LYS A 1 227 ? 2.638   -37.268 43.682  1.00 56.94  ? 1697 LYS A N   1 
ATOM   1826 C  CA  . LYS A 1 227 ? 3.828   -37.308 42.847  1.00 67.24  ? 1697 LYS A CA  1 
ATOM   1827 C  C   . LYS A 1 227 ? 3.863   -38.626 42.086  1.00 74.82  ? 1697 LYS A C   1 
ATOM   1828 O  O   . LYS A 1 227 ? 3.597   -39.689 42.653  1.00 78.44  ? 1697 LYS A O   1 
ATOM   1829 C  CB  . LYS A 1 227 ? 5.081   -37.135 43.706  1.00 65.90  ? 1697 LYS A CB  1 
ATOM   1830 C  CG  . LYS A 1 227 ? 6.397   -37.249 42.959  1.00 76.46  ? 1697 LYS A CG  1 
ATOM   1831 C  CD  . LYS A 1 227 ? 7.550   -36.678 43.790  1.00 81.34  ? 1697 LYS A CD  1 
ATOM   1832 C  CE  . LYS A 1 227 ? 8.327   -37.769 44.524  1.00 77.16  ? 1697 LYS A CE  1 
ATOM   1833 N  NZ  . LYS A 1 227 ? 9.570   -37.237 45.184  1.00 73.02  ? 1697 LYS A NZ  1 
ATOM   1834 N  N   . ILE A 1 228 ? 4.150   -38.555 40.793  1.00 68.91  ? 1698 ILE A N   1 
ATOM   1835 C  CA  . ILE A 1 228 ? 4.466   -39.730 40.000  1.00 66.39  ? 1698 ILE A CA  1 
ATOM   1836 C  C   . ILE A 1 228 ? 5.870   -39.538 39.448  1.00 63.10  ? 1698 ILE A C   1 
ATOM   1837 O  O   . ILE A 1 228 ? 6.243   -38.430 39.037  1.00 59.46  ? 1698 ILE A O   1 
ATOM   1838 C  CB  . ILE A 1 228 ? 3.445   -39.978 38.873  1.00 66.68  ? 1698 ILE A CB  1 
ATOM   1839 C  CG1 . ILE A 1 228 ? 3.452   -38.823 37.876  1.00 51.29  ? 1698 ILE A CG1 1 
ATOM   1840 C  CG2 . ILE A 1 228 ? 2.060   -40.194 39.456  1.00 83.46  ? 1698 ILE A CG2 1 
ATOM   1841 C  CD1 . ILE A 1 228 ? 2.648   -39.110 36.646  1.00 59.83  ? 1698 ILE A CD1 1 
ATOM   1842 N  N   . GLU A 1 229 ? 6.656   -40.610 39.490  1.00 63.07  ? 1699 GLU A N   1 
ATOM   1843 C  CA  . GLU A 1 229 ? 8.093   -40.553 39.253  1.00 67.82  ? 1699 GLU A CA  1 
ATOM   1844 C  C   . GLU A 1 229 ? 8.454   -41.272 37.961  1.00 60.43  ? 1699 GLU A C   1 
ATOM   1845 O  O   . GLU A 1 229 ? 7.915   -42.340 37.656  1.00 73.67  ? 1699 GLU A O   1 
ATOM   1846 C  CB  . GLU A 1 229 ? 8.858   -41.177 40.424  1.00 73.88  ? 1699 GLU A CB  1 
ATOM   1847 C  CG  . GLU A 1 229 ? 9.492   -40.165 41.381  1.00 89.36  ? 1699 GLU A CG  1 
ATOM   1848 C  CD  . GLU A 1 229 ? 9.890   -40.782 42.723  1.00 104.57 ? 1699 GLU A CD  1 
ATOM   1849 O  OE1 . GLU A 1 229 ? 9.810   -42.028 42.875  1.00 103.72 ? 1699 GLU A OE1 1 
ATOM   1850 O  OE2 . GLU A 1 229 ? 10.304  -40.014 43.622  1.00 107.88 ? 1699 GLU A OE2 1 
ATOM   1851 N  N   . PHE A 1 230 ? 9.366   -40.677 37.209  1.00 55.49  ? 1700 PHE A N   1 
ATOM   1852 C  CA  . PHE A 1 230 ? 9.896   -41.277 35.997  1.00 63.84  ? 1700 PHE A CA  1 
ATOM   1853 C  C   . PHE A 1 230 ? 11.192  -42.034 36.292  1.00 65.77  ? 1700 PHE A C   1 
ATOM   1854 O  O   . PHE A 1 230 ? 11.803  -41.907 37.361  1.00 62.03  ? 1700 PHE A O   1 
ATOM   1855 C  CB  . PHE A 1 230 ? 10.141  -40.203 34.935  1.00 62.39  ? 1700 PHE A CB  1 
ATOM   1856 C  CG  . PHE A 1 230 ? 8.896   -39.553 34.443  1.00 59.09  ? 1700 PHE A CG  1 
ATOM   1857 C  CD1 . PHE A 1 230 ? 8.317   -38.514 35.149  1.00 50.98  ? 1700 PHE A CD1 1 
ATOM   1858 C  CD2 . PHE A 1 230 ? 8.290   -39.991 33.279  1.00 60.76  ? 1700 PHE A CD2 1 
ATOM   1859 C  CE1 . PHE A 1 230 ? 7.158   -37.923 34.705  1.00 60.19  ? 1700 PHE A CE1 1 
ATOM   1860 C  CE2 . PHE A 1 230 ? 7.119   -39.401 32.828  1.00 59.34  ? 1700 PHE A CE2 1 
ATOM   1861 C  CZ  . PHE A 1 230 ? 6.555   -38.365 33.543  1.00 61.05  ? 1700 PHE A CZ  1 
ATOM   1862 N  N   . LYS A 1 231 ? 11.616  -42.836 35.319  1.00 62.39  ? 1701 LYS A N   1 
ATOM   1863 C  CA  . LYS A 1 231 ? 12.797  -43.659 35.547  1.00 72.70  ? 1701 LYS A CA  1 
ATOM   1864 C  C   . LYS A 1 231 ? 14.058  -42.809 35.667  1.00 74.26  ? 1701 LYS A C   1 
ATOM   1865 O  O   . LYS A 1 231 ? 14.931  -43.114 36.489  1.00 69.97  ? 1701 LYS A O   1 
ATOM   1866 C  CB  . LYS A 1 231 ? 12.923  -44.720 34.450  1.00 72.84  ? 1701 LYS A CB  1 
ATOM   1867 C  CG  . LYS A 1 231 ? 12.132  -45.993 34.779  1.00 88.69  ? 1701 LYS A CG  1 
ATOM   1868 C  CD  . LYS A 1 231 ? 11.489  -46.632 33.550  1.00 95.57  ? 1701 LYS A CD  1 
ATOM   1869 C  CE  . LYS A 1 231 ? 11.837  -48.118 33.454  1.00 103.01 ? 1701 LYS A CE  1 
ATOM   1870 N  NZ  . LYS A 1 231 ? 11.478  -48.727 32.138  1.00 99.13  ? 1701 LYS A NZ  1 
ATOM   1871 N  N   . ARG A 1 232 ? 14.168  -41.718 34.901  1.00 68.94  ? 1702 ARG A N   1 
ATOM   1872 C  CA  . ARG A 1 232 ? 15.294  -40.828 35.147  1.00 64.19  ? 1702 ARG A CA  1 
ATOM   1873 C  C   . ARG A 1 232 ? 15.122  -40.208 36.529  1.00 75.27  ? 1702 ARG A C   1 
ATOM   1874 O  O   . ARG A 1 232 ? 14.016  -39.792 36.889  1.00 82.26  ? 1702 ARG A O   1 
ATOM   1875 C  CB  . ARG A 1 232 ? 15.415  -39.712 34.094  1.00 74.39  ? 1702 ARG A CB  1 
ATOM   1876 C  CG  . ARG A 1 232 ? 16.503  -38.644 34.456  1.00 62.69  ? 1702 ARG A CG  1 
ATOM   1877 C  CD  . ARG A 1 232 ? 16.646  -37.512 33.434  1.00 60.43  ? 1702 ARG A CD  1 
ATOM   1878 N  NE  . ARG A 1 232 ? 16.912  -38.011 32.089  1.00 66.69  ? 1702 ARG A NE  1 
ATOM   1879 C  CZ  . ARG A 1 232 ? 18.133  -38.173 31.583  1.00 76.86  ? 1702 ARG A CZ  1 
ATOM   1880 N  NH1 . ARG A 1 232 ? 19.206  -37.855 32.306  1.00 55.46  ? 1702 ARG A NH1 1 
ATOM   1881 N  NH2 . ARG A 1 232 ? 18.285  -38.647 30.349  1.00 72.01  ? 1702 ARG A NH2 1 
ATOM   1882 N  N   . PRO A 1 233 ? 16.177  -40.156 37.332  1.00 85.04  ? 1703 PRO A N   1 
ATOM   1883 C  CA  . PRO A 1 233 ? 16.046  -39.557 38.661  1.00 93.54  ? 1703 PRO A CA  1 
ATOM   1884 C  C   . PRO A 1 233 ? 15.877  -38.049 38.576  1.00 88.86  ? 1703 PRO A C   1 
ATOM   1885 O  O   . PRO A 1 233 ? 16.451  -37.377 37.712  1.00 81.22  ? 1703 PRO A O   1 
ATOM   1886 C  CB  . PRO A 1 233 ? 17.357  -39.943 39.361  1.00 90.85  ? 1703 PRO A CB  1 
ATOM   1887 C  CG  . PRO A 1 233 ? 18.293  -40.279 38.260  1.00 89.19  ? 1703 PRO A CG  1 
ATOM   1888 C  CD  . PRO A 1 233 ? 17.456  -40.862 37.165  1.00 82.54  ? 1703 PRO A CD  1 
ATOM   1889 N  N   . GLY A 1 234 ? 15.113  -37.521 39.535  1.00 80.70  ? 1704 GLY A N   1 
ATOM   1890 C  CA  . GLY A 1 234 ? 14.771  -36.115 39.592  1.00 74.46  ? 1704 GLY A CA  1 
ATOM   1891 C  C   . GLY A 1 234 ? 13.666  -35.673 38.654  1.00 69.10  ? 1704 GLY A C   1 
ATOM   1892 O  O   . GLY A 1 234 ? 13.483  -34.467 38.472  1.00 78.89  ? 1704 GLY A O   1 
ATOM   1893 N  N   . LYS A 1 235 ? 12.938  -36.597 38.035  1.00 51.25  ? 1705 LYS A N   1 
ATOM   1894 C  CA  . LYS A 1 235 ? 11.904  -36.267 37.062  1.00 48.36  ? 1705 LYS A CA  1 
ATOM   1895 C  C   . LYS A 1 235 ? 10.567  -36.766 37.586  1.00 57.55  ? 1705 LYS A C   1 
ATOM   1896 O  O   . LYS A 1 235 ? 10.369  -37.976 37.748  1.00 64.40  ? 1705 LYS A O   1 
ATOM   1897 C  CB  . LYS A 1 235 ? 12.201  -36.882 35.693  1.00 61.30  ? 1705 LYS A CB  1 
ATOM   1898 C  CG  . LYS A 1 235 ? 13.410  -36.296 34.981  1.00 72.13  ? 1705 LYS A CG  1 
ATOM   1899 C  CD  . LYS A 1 235 ? 13.294  -34.788 34.873  1.00 69.39  ? 1705 LYS A CD  1 
ATOM   1900 C  CE  . LYS A 1 235 ? 14.576  -34.190 34.346  1.00 69.73  ? 1705 LYS A CE  1 
ATOM   1901 N  NZ  . LYS A 1 235 ? 14.811  -32.850 34.931  1.00 53.18  ? 1705 LYS A NZ  1 
ATOM   1902 N  N   . ALA A 1 236 ? 9.648   -35.839 37.831  1.00 56.54  ? 1706 ALA A N   1 
ATOM   1903 C  CA  . ALA A 1 236 ? 8.357   -36.196 38.380  1.00 58.25  ? 1706 ALA A CA  1 
ATOM   1904 C  C   . ALA A 1 236 ? 7.292   -35.264 37.824  1.00 59.93  ? 1706 ALA A C   1 
ATOM   1905 O  O   . ALA A 1 236 ? 7.581   -34.202 37.256  1.00 52.16  ? 1706 ALA A O   1 
ATOM   1906 C  CB  . ALA A 1 236 ? 8.378   -36.157 39.914  1.00 52.81  ? 1706 ALA A CB  1 
ATOM   1907 N  N   . ALA A 1 237 ? 6.045   -35.696 37.971  1.00 46.33  ? 1707 ALA A N   1 
ATOM   1908 C  CA  . ALA A 1 237 ? 4.916   -34.852 37.633  1.00 46.15  ? 1707 ALA A CA  1 
ATOM   1909 C  C   . ALA A 1 237 ? 3.850   -35.049 38.689  1.00 54.57  ? 1707 ALA A C   1 
ATOM   1910 O  O   . ALA A 1 237 ? 3.793   -36.079 39.374  1.00 51.30  ? 1707 ALA A O   1 
ATOM   1911 C  CB  . ALA A 1 237 ? 4.356   -35.159 36.237  1.00 50.89  ? 1707 ALA A CB  1 
ATOM   1912 N  N   . ASN A 1 238 ? 2.986   -34.056 38.806  1.00 53.44  ? 1708 ASN A N   1 
ATOM   1913 C  CA  . ASN A 1 238 ? 1.802   -34.239 39.620  1.00 43.82  ? 1708 ASN A CA  1 
ATOM   1914 C  C   . ASN A 1 238 ? 0.794   -35.036 38.802  1.00 43.47  ? 1708 ASN A C   1 
ATOM   1915 O  O   . ASN A 1 238 ? 0.467   -34.665 37.670  1.00 56.48  ? 1708 ASN A O   1 
ATOM   1916 C  CB  . ASN A 1 238 ? 1.234   -32.891 40.057  1.00 46.86  ? 1708 ASN A CB  1 
ATOM   1917 C  CG  . ASN A 1 238 ? -0.199  -33.008 40.513  1.00 57.34  ? 1708 ASN A CG  1 
ATOM   1918 O  OD1 . ASN A 1 238 ? -1.120  -32.959 39.701  1.00 50.53  ? 1708 ASN A OD1 1 
ATOM   1919 N  ND2 . ASN A 1 238 ? -0.393  -33.206 41.811  1.00 48.71  ? 1708 ASN A ND2 1 
ATOM   1920 N  N   . LYS A 1 239 ? 0.310   -36.134 39.371  1.00 44.58  ? 1709 LYS A N   1 
ATOM   1921 C  CA  . LYS A 1 239 ? -0.542  -37.042 38.603  1.00 44.64  ? 1709 LYS A CA  1 
ATOM   1922 C  C   . LYS A 1 239 ? -1.743  -36.320 38.009  1.00 43.61  ? 1709 LYS A C   1 
ATOM   1923 O  O   . LYS A 1 239 ? -2.168  -36.654 36.902  1.00 53.35  ? 1709 LYS A O   1 
ATOM   1924 C  CB  . LYS A 1 239 ? -0.983  -38.226 39.482  1.00 50.93  ? 1709 LYS A CB  1 
ATOM   1925 C  CG  . LYS A 1 239 ? -1.958  -39.198 38.811  1.00 57.42  ? 1709 LYS A CG  1 
ATOM   1926 C  CD  . LYS A 1 239 ? -2.187  -40.471 39.648  1.00 68.25  ? 1709 LYS A CD  1 
ATOM   1927 C  CE  . LYS A 1 239 ? -3.602  -40.546 40.214  1.00 68.30  ? 1709 LYS A CE  1 
ATOM   1928 N  NZ  . LYS A 1 239 ? -3.734  -39.874 41.532  1.00 81.15  ? 1709 LYS A NZ  1 
ATOM   1929 N  N   . ASP A 1 240 ? -2.260  -35.285 38.683  1.00 49.94  ? 1710 ASP A N   1 
ATOM   1930 C  CA  . ASP A 1 240 ? -3.414  -34.567 38.142  1.00 50.89  ? 1710 ASP A CA  1 
ATOM   1931 C  C   . ASP A 1 240 ? -3.046  -33.740 36.915  1.00 53.47  ? 1710 ASP A C   1 
ATOM   1932 O  O   . ASP A 1 240 ? -3.783  -33.749 35.919  1.00 44.17  ? 1710 ASP A O   1 
ATOM   1933 C  CB  . ASP A 1 240 ? -4.056  -33.694 39.222  1.00 43.69  ? 1710 ASP A CB  1 
ATOM   1934 C  CG  . ASP A 1 240 ? -4.794  -34.525 40.268  1.00 60.15  ? 1710 ASP A CG  1 
ATOM   1935 O  OD1 . ASP A 1 240 ? -5.196  -35.669 39.946  1.00 70.54  ? 1710 ASP A OD1 1 
ATOM   1936 O  OD2 . ASP A 1 240 ? -4.988  -34.039 41.400  1.00 67.10  ? 1710 ASP A OD2 1 
ATOM   1937 N  N   . ASN A 1 241 ? -1.910  -33.031 36.954  1.00 42.79  ? 1711 ASN A N   1 
ATOM   1938 C  CA  . ASN A 1 241 ? -1.429  -32.354 35.748  1.00 45.68  ? 1711 ASN A CA  1 
ATOM   1939 C  C   . ASN A 1 241 ? -1.148  -33.361 34.635  1.00 39.47  ? 1711 ASN A C   1 
ATOM   1940 O  O   . ASN A 1 241 ? -1.434  -33.111 33.447  1.00 40.31  ? 1711 ASN A O   1 
ATOM   1941 C  CB  . ASN A 1 241 ? -0.145  -31.551 36.035  1.00 41.28  ? 1711 ASN A CB  1 
ATOM   1942 C  CG  . ASN A 1 241 ? -0.292  -30.540 37.166  1.00 51.08  ? 1711 ASN A CG  1 
ATOM   1943 O  OD1 . ASN A 1 241 ? 0.708   -30.146 37.788  1.00 47.67  ? 1711 ASN A OD1 1 
ATOM   1944 N  ND2 . ASN A 1 241 ? -1.517  -30.113 37.436  1.00 52.33  ? 1711 ASN A ND2 1 
ATOM   1945 N  N   . TRP A 1 242 ? -0.520  -34.479 34.996  1.00 40.21  ? 1712 TRP A N   1 
ATOM   1946 C  CA  . TRP A 1 242 ? -0.216  -35.497 34.006  1.00 41.74  ? 1712 TRP A CA  1 
ATOM   1947 C  C   . TRP A 1 242 ? -1.491  -35.926 33.305  1.00 46.42  ? 1712 TRP A C   1 
ATOM   1948 O  O   . TRP A 1 242 ? -1.595  -35.871 32.070  1.00 44.80  ? 1712 TRP A O   1 
ATOM   1949 C  CB  . TRP A 1 242 ? 0.465   -36.686 34.690  1.00 41.18  ? 1712 TRP A CB  1 
ATOM   1950 C  CG  . TRP A 1 242 ? 0.954   -37.741 33.736  1.00 60.38  ? 1712 TRP A CG  1 
ATOM   1951 C  CD1 . TRP A 1 242 ? 0.458   -39.011 33.592  1.00 64.89  ? 1712 TRP A CD1 1 
ATOM   1952 C  CD2 . TRP A 1 242 ? 2.042   -37.628 32.798  1.00 50.25  ? 1712 TRP A CD2 1 
ATOM   1953 N  NE1 . TRP A 1 242 ? 1.163   -39.681 32.619  1.00 62.93  ? 1712 TRP A NE1 1 
ATOM   1954 C  CE2 . TRP A 1 242 ? 2.138   -38.855 32.118  1.00 56.89  ? 1712 TRP A CE2 1 
ATOM   1955 C  CE3 . TRP A 1 242 ? 2.925   -36.602 32.455  1.00 50.02  ? 1712 TRP A CE3 1 
ATOM   1956 C  CZ2 . TRP A 1 242 ? 3.095   -39.087 31.126  1.00 50.42  ? 1712 TRP A CZ2 1 
ATOM   1957 C  CZ3 . TRP A 1 242 ? 3.873   -36.838 31.469  1.00 60.71  ? 1712 TRP A CZ3 1 
ATOM   1958 C  CH2 . TRP A 1 242 ? 3.951   -38.072 30.821  1.00 46.39  ? 1712 TRP A CH2 1 
ATOM   1959 N  N   . ASN A 1 243 ? -2.492  -36.310 34.100  1.00 50.13  ? 1713 ASN A N   1 
ATOM   1960 C  CA  . ASN A 1 243 ? -3.761  -36.762 33.558  1.00 47.68  ? 1713 ASN A CA  1 
ATOM   1961 C  C   . ASN A 1 243 ? -4.443  -35.676 32.749  1.00 46.36  ? 1713 ASN A C   1 
ATOM   1962 O  O   . ASN A 1 243 ? -5.059  -35.975 31.724  1.00 50.58  ? 1713 ASN A O   1 
ATOM   1963 C  CB  . ASN A 1 243 ? -4.669  -37.268 34.675  1.00 48.70  ? 1713 ASN A CB  1 
ATOM   1964 C  CG  . ASN A 1 243 ? -4.221  -38.627 35.218  1.00 50.67  ? 1713 ASN A CG  1 
ATOM   1965 O  OD1 . ASN A 1 243 ? -3.272  -39.240 34.706  1.00 51.73  ? 1713 ASN A OD1 1 
ATOM   1966 N  ND2 . ASN A 1 243 ? -4.898  -39.098 36.261  1.00 48.47  ? 1713 ASN A ND2 1 
ATOM   1967 N  N   . LYS A 1 244 ? -4.361  -34.410 33.187  1.00 41.00  ? 1714 LYS A N   1 
ATOM   1968 C  CA  . LYS A 1 244 ? -4.985  -33.340 32.404  1.00 39.61  ? 1714 LYS A CA  1 
ATOM   1969 C  C   . LYS A 1 244 ? -4.378  -33.266 31.009  1.00 42.04  ? 1714 LYS A C   1 
ATOM   1970 O  O   . LYS A 1 244 ? -5.093  -33.158 30.002  1.00 44.88  ? 1714 LYS A O   1 
ATOM   1971 C  CB  . LYS A 1 244 ? -4.837  -31.995 33.119  1.00 53.61  ? 1714 LYS A CB  1 
ATOM   1972 C  CG  . LYS A 1 244 ? -5.612  -30.847 32.468  1.00 59.67  ? 1714 LYS A CG  1 
ATOM   1973 C  CD  . LYS A 1 244 ? -6.056  -29.824 33.513  1.00 82.80  ? 1714 LYS A CD  1 
ATOM   1974 C  CE  . LYS A 1 244 ? -7.248  -28.984 33.025  1.00 89.06  ? 1714 LYS A CE  1 
ATOM   1975 N  NZ  . LYS A 1 244 ? -8.377  -28.942 34.022  1.00 72.32  ? 1714 LYS A NZ  1 
ATOM   1976 N  N   . PHE A 1 245 ? -3.055  -33.385 30.929  1.00 43.90  ? 1715 PHE A N   1 
ATOM   1977 C  CA  . PHE A 1 245 ? -2.389  -33.334 29.634  1.00 50.65  ? 1715 PHE A CA  1 
ATOM   1978 C  C   . PHE A 1 245 ? -2.746  -34.546 28.779  1.00 42.07  ? 1715 PHE A C   1 
ATOM   1979 O  O   . PHE A 1 245 ? -3.011  -34.423 27.566  1.00 49.89  ? 1715 PHE A O   1 
ATOM   1980 C  CB  . PHE A 1 245 ? -0.876  -33.244 29.864  1.00 46.72  ? 1715 PHE A CB  1 
ATOM   1981 C  CG  . PHE A 1 245 ? -0.118  -32.768 28.687  1.00 36.88  ? 1715 PHE A CG  1 
ATOM   1982 C  CD1 . PHE A 1 245 ? 0.082   -31.413 28.485  1.00 44.88  ? 1715 PHE A CD1 1 
ATOM   1983 C  CD2 . PHE A 1 245 ? 0.429   -33.670 27.791  1.00 51.14  ? 1715 PHE A CD2 1 
ATOM   1984 C  CE1 . PHE A 1 245 ? 0.794   -30.976 27.403  1.00 46.59  ? 1715 PHE A CE1 1 
ATOM   1985 C  CE2 . PHE A 1 245 ? 1.133   -33.240 26.703  1.00 61.10  ? 1715 PHE A CE2 1 
ATOM   1986 C  CZ  . PHE A 1 245 ? 1.320   -31.884 26.505  1.00 49.13  ? 1715 PHE A CZ  1 
ATOM   1987 N  N   . LEU A 1 246 ? -2.739  -35.729 29.390  1.00 37.59  ? 1716 LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 246 ? -3.097  -36.927 28.640  1.00 50.61  ? 1716 LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 246 ? -4.539  -36.851 28.146  1.00 58.99  ? 1716 LEU A C   1 
ATOM   1990 O  O   . LEU A 1 246 ? -4.841  -37.237 27.009  1.00 50.52  ? 1716 LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 246 ? -2.863  -38.165 29.501  1.00 48.21  ? 1716 LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 246 ? -1.413  -38.518 29.842  1.00 48.98  ? 1716 LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 246 ? -1.282  -39.950 30.329  1.00 51.67  ? 1716 LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 246 ? -0.517  -38.317 28.663  1.00 55.64  ? 1716 LEU A CD2 1 
ATOM   1995 N  N   . MET A 1 247 ? -5.436  -36.311 28.974  1.00 47.02  ? 1717 MET A N   1 
ATOM   1996 C  CA  . MET A 1 247 ? -6.826  -36.148 28.569  1.00 41.91  ? 1717 MET A CA  1 
ATOM   1997 C  C   . MET A 1 247 ? -6.944  -35.193 27.404  1.00 58.86  ? 1717 MET A C   1 
ATOM   1998 O  O   . MET A 1 247 ? -7.784  -35.398 26.525  1.00 47.15  ? 1717 MET A O   1 
ATOM   1999 C  CB  . MET A 1 247 ? -7.674  -35.661 29.735  1.00 41.52  ? 1717 MET A CB  1 
ATOM   2000 C  CG  . MET A 1 247 ? -8.169  -36.809 30.610  1.00 62.01  ? 1717 MET A CG  1 
ATOM   2001 S  SD  . MET A 1 247 ? -9.381  -37.783 29.704  1.00 79.95  ? 1717 MET A SD  1 
ATOM   2002 C  CE  . MET A 1 247 ? -10.589 -36.503 29.297  1.00 58.24  ? 1717 MET A CE  1 
ATOM   2003 N  N   . ALA A 1 248 ? -6.132  -34.120 27.394  1.00 41.45  ? 1718 ALA A N   1 
ATOM   2004 C  CA  . ALA A 1 248 ? -6.216  -33.204 26.273  1.00 37.33  ? 1718 ALA A CA  1 
ATOM   2005 C  C   . ALA A 1 248 ? -5.779  -33.888 24.990  1.00 45.29  ? 1718 ALA A C   1 
ATOM   2006 O  O   . ALA A 1 248 ? -6.309  -33.576 23.913  1.00 46.73  ? 1718 ALA A O   1 
ATOM   2007 C  CB  . ALA A 1 248 ? -5.407  -31.926 26.551  1.00 35.25  ? 1718 ALA A CB  1 
ATOM   2008 N  N   . ILE A 1 249 ? -4.804  -34.804 25.081  1.00 40.92  ? 1719 ILE A N   1 
ATOM   2009 C  CA  . ILE A 1 249 ? -4.429  -35.600 23.907  1.00 45.53  ? 1719 ILE A CA  1 
ATOM   2010 C  C   . ILE A 1 249 ? -5.582  -36.522 23.504  1.00 55.61  ? 1719 ILE A C   1 
ATOM   2011 O  O   . ILE A 1 249 ? -5.948  -36.614 22.326  1.00 52.46  ? 1719 ILE A O   1 
ATOM   2012 C  CB  . ILE A 1 249 ? -3.136  -36.400 24.164  1.00 44.21  ? 1719 ILE A CB  1 
ATOM   2013 C  CG1 . ILE A 1 249 ? -1.899  -35.485 24.197  1.00 58.15  ? 1719 ILE A CG1 1 
ATOM   2014 C  CG2 . ILE A 1 249 ? -2.951  -37.458 23.088  1.00 52.54  ? 1719 ILE A CG2 1 
ATOM   2015 C  CD1 . ILE A 1 249 ? -0.631  -36.173 24.671  1.00 44.22  ? 1719 ILE A CD1 1 
ATOM   2016 N  N   . LYS A 1 250 ? -6.162  -37.221 24.482  1.00 50.19  ? 1720 LYS A N   1 
ATOM   2017 C  CA  . LYS A 1 250 ? -7.268  -38.142 24.206  1.00 56.88  ? 1720 LYS A CA  1 
ATOM   2018 C  C   . LYS A 1 250 ? -8.433  -37.444 23.507  1.00 61.23  ? 1720 LYS A C   1 
ATOM   2019 O  O   . LYS A 1 250 ? -9.019  -37.983 22.562  1.00 72.92  ? 1720 LYS A O   1 
ATOM   2020 C  CB  . LYS A 1 250 ? -7.764  -38.787 25.498  1.00 59.67  ? 1720 LYS A CB  1 
ATOM   2021 C  CG  . LYS A 1 250 ? -9.025  -39.621 25.262  1.00 69.00  ? 1720 LYS A CG  1 
ATOM   2022 C  CD  . LYS A 1 250 ? -9.630  -40.147 26.545  1.00 69.20  ? 1720 LYS A CD  1 
ATOM   2023 C  CE  . LYS A 1 250 ? -10.749 -41.143 26.248  1.00 68.53  ? 1720 LYS A CE  1 
ATOM   2024 N  NZ  . LYS A 1 250 ? -11.671 -41.247 27.400  1.00 74.12  ? 1720 LYS A NZ  1 
ATOM   2025 N  N   . THR A 1 251 ? -8.798  -36.256 23.967  1.00 65.10  ? 1721 THR A N   1 
ATOM   2026 C  CA  . THR A 1 251 ? -9.935  -35.556 23.400  1.00 63.66  ? 1721 THR A CA  1 
ATOM   2027 C  C   . THR A 1 251 ? -9.593  -34.787 22.127  1.00 62.56  ? 1721 THR A C   1 
ATOM   2028 O  O   . THR A 1 251 ? -10.476 -34.592 21.283  1.00 67.87  ? 1721 THR A O   1 
ATOM   2029 C  CB  . THR A 1 251 ? -10.525 -34.582 24.430  1.00 78.96  ? 1721 THR A CB  1 
ATOM   2030 O  OG1 . THR A 1 251 ? -11.498 -33.750 23.790  1.00 88.20  ? 1721 THR A OG1 1 
ATOM   2031 C  CG2 . THR A 1 251 ? -9.470  -33.660 24.954  1.00 71.55  ? 1721 THR A CG2 1 
ATOM   2032 N  N   . SER A 1 252 ? -8.347  -34.350 21.945  1.00 48.51  ? 1722 SER A N   1 
ATOM   2033 C  CA  . SER A 1 252 ? -8.047  -33.508 20.797  1.00 47.12  ? 1722 SER A CA  1 
ATOM   2034 C  C   . SER A 1 252 ? -7.137  -34.142 19.759  1.00 56.19  ? 1722 SER A C   1 
ATOM   2035 O  O   . SER A 1 252 ? -7.117  -33.666 18.616  1.00 52.14  ? 1722 SER A O   1 
ATOM   2036 C  CB  . SER A 1 252 ? -7.394  -32.202 21.268  1.00 52.53  ? 1722 SER A CB  1 
ATOM   2037 O  OG  . SER A 1 252 ? -6.028  -32.430 21.606  1.00 40.77  ? 1722 SER A OG  1 
ATOM   2038 N  N   . HIS A 1 253 ? -6.374  -35.175 20.125  1.00 48.63  ? 1723 HIS A N   1 
ATOM   2039 C  CA  . HIS A 1 253 ? -5.356  -35.755 19.245  1.00 60.98  ? 1723 HIS A CA  1 
ATOM   2040 C  C   . HIS A 1 253 ? -4.346  -34.718 18.747  1.00 51.86  ? 1723 HIS A C   1 
ATOM   2041 O  O   . HIS A 1 253 ? -3.779  -34.865 17.658  1.00 52.46  ? 1723 HIS A O   1 
ATOM   2042 C  CB  . HIS A 1 253 ? -6.017  -36.495 18.081  1.00 43.33  ? 1723 HIS A CB  1 
ATOM   2043 C  CG  . HIS A 1 253 ? -6.868  -37.622 18.539  1.00 49.44  ? 1723 HIS A CG  1 
ATOM   2044 N  ND1 . HIS A 1 253 ? -8.205  -37.723 18.228  1.00 51.96  ? 1723 HIS A ND1 1 
ATOM   2045 C  CD2 . HIS A 1 253 ? -6.583  -38.666 19.349  1.00 47.39  ? 1723 HIS A CD2 1 
ATOM   2046 C  CE1 . HIS A 1 253 ? -8.702  -38.809 18.798  1.00 57.96  ? 1723 HIS A CE1 1 
ATOM   2047 N  NE2 . HIS A 1 253 ? -7.739  -39.393 19.489  1.00 59.55  ? 1723 HIS A NE2 1 
ATOM   2048 N  N   . SER A 1 254 ? -4.138  -33.657 19.541  1.00 43.70  ? 1724 SER A N   1 
ATOM   2049 C  CA  . SER A 1 254 ? -3.100  -32.655 19.332  1.00 40.28  ? 1724 SER A CA  1 
ATOM   2050 C  C   . SER A 1 254 ? -1.762  -33.271 18.949  1.00 47.69  ? 1724 SER A C   1 
ATOM   2051 O  O   . SER A 1 254 ? -1.144  -33.922 19.791  1.00 39.23  ? 1724 SER A O   1 
ATOM   2052 C  CB  . SER A 1 254 ? -2.858  -31.851 20.600  1.00 41.26  ? 1724 SER A CB  1 
ATOM   2053 O  OG  . SER A 1 254 ? -1.989  -30.752 20.317  1.00 46.34  ? 1724 SER A OG  1 
ATOM   2054 N  N   . PRO A 1 255 ? -1.279  -33.096 17.723  1.00 38.64  ? 1725 PRO A N   1 
ATOM   2055 C  CA  . PRO A 1 255 ? 0.081   -33.561 17.424  1.00 50.35  ? 1725 PRO A CA  1 
ATOM   2056 C  C   . PRO A 1 255 ? 1.151   -32.866 18.253  1.00 44.63  ? 1725 PRO A C   1 
ATOM   2057 O  O   . PRO A 1 255 ? 2.139   -33.510 18.609  1.00 47.34  ? 1725 PRO A O   1 
ATOM   2058 C  CB  . PRO A 1 255 ? 0.243   -33.257 15.925  1.00 47.62  ? 1725 PRO A CB  1 
ATOM   2059 C  CG  . PRO A 1 255 ? -1.129  -33.052 15.425  1.00 49.20  ? 1725 PRO A CG  1 
ATOM   2060 C  CD  . PRO A 1 255 ? -1.917  -32.488 16.558  1.00 48.23  ? 1725 PRO A CD  1 
ATOM   2061 N  N   . VAL A 1 256 ? 1.002   -31.584 18.592  1.00 43.63  ? 1726 VAL A N   1 
ATOM   2062 C  CA  . VAL A 1 256 ? 2.093   -30.977 19.351  1.00 37.96  ? 1726 VAL A CA  1 
ATOM   2063 C  C   . VAL A 1 256 ? 2.089   -31.517 20.777  1.00 40.01  ? 1726 VAL A C   1 
ATOM   2064 O  O   . VAL A 1 256 ? 3.158   -31.754 21.363  1.00 42.74  ? 1726 VAL A O   1 
ATOM   2065 C  CB  . VAL A 1 256 ? 2.036   -29.430 19.306  1.00 45.65  ? 1726 VAL A CB  1 
ATOM   2066 C  CG1 . VAL A 1 256 ? 2.266   -28.927 17.886  1.00 38.32  ? 1726 VAL A CG1 1 
ATOM   2067 C  CG2 . VAL A 1 256 ? 0.693   -28.876 19.835  1.00 43.89  ? 1726 VAL A CG2 1 
ATOM   2068 N  N   . CYS A 1 257 ? 0.906   -31.800 21.338  1.00 39.70  ? 1727 CYS A N   1 
ATOM   2069 C  CA  . CYS A 1 257 ? 0.885   -32.446 22.653  1.00 34.29  ? 1727 CYS A CA  1 
ATOM   2070 C  C   . CYS A 1 257 ? 1.419   -33.877 22.592  1.00 37.58  ? 1727 CYS A C   1 
ATOM   2071 O  O   . CYS A 1 257 ? 2.108   -34.321 23.519  1.00 41.94  ? 1727 CYS A O   1 
ATOM   2072 C  CB  . CYS A 1 257 ? -0.506  -32.402 23.284  1.00 34.18  ? 1727 CYS A CB  1 
ATOM   2073 S  SG  . CYS A 1 257 ? -1.214  -30.695 23.469  1.00 49.15  ? 1727 CYS A SG  1 
ATOM   2074 N  N   A GLN A 1 258 ? 1.121   -34.623 21.519  0.57 36.08  ? 1728 GLN A N   1 
ATOM   2075 N  N   B GLN A 1 258 ? 1.124   -34.604 21.511  0.43 36.74  ? 1728 GLN A N   1 
ATOM   2076 C  CA  A GLN A 1 258 ? 1.683   -35.968 21.400  0.57 42.67  ? 1728 GLN A CA  1 
ATOM   2077 C  CA  B GLN A 1 258 ? 1.657   -35.952 21.363  0.43 42.48  ? 1728 GLN A CA  1 
ATOM   2078 C  C   A GLN A 1 258 ? 3.195   -35.902 21.252  0.57 46.65  ? 1728 GLN A C   1 
ATOM   2079 C  C   B GLN A 1 258 ? 3.176   -35.915 21.220  0.43 46.62  ? 1728 GLN A C   1 
ATOM   2080 O  O   A GLN A 1 258 ? 3.910   -36.748 21.788  0.57 51.77  ? 1728 GLN A O   1 
ATOM   2081 O  O   B GLN A 1 258 ? 3.877   -36.779 21.752  0.43 51.59  ? 1728 GLN A O   1 
ATOM   2082 C  CB  A GLN A 1 258 ? 1.079   -36.741 20.222  0.57 39.77  ? 1728 GLN A CB  1 
ATOM   2083 C  CB  B GLN A 1 258 ? 1.003   -36.657 20.168  0.43 42.14  ? 1728 GLN A CB  1 
ATOM   2084 C  CG  A GLN A 1 258 ? -0.012  -37.770 20.619  0.57 55.16  ? 1728 GLN A CG  1 
ATOM   2085 C  CG  B GLN A 1 258 ? -0.523  -36.838 20.331  0.43 56.44  ? 1728 GLN A CG  1 
ATOM   2086 C  CD  A GLN A 1 258 ? 0.528   -39.052 21.238  0.57 50.84  ? 1728 GLN A CD  1 
ATOM   2087 C  CD  B GLN A 1 258 ? -1.146  -37.702 19.243  0.43 50.50  ? 1728 GLN A CD  1 
ATOM   2088 O  OE1 A GLN A 1 258 ? 1.736   -39.314 21.221  0.57 55.46  ? 1728 GLN A OE1 1 
ATOM   2089 O  OE1 B GLN A 1 258 ? -1.892  -37.214 18.392  0.43 43.29  ? 1728 GLN A OE1 1 
ATOM   2090 N  NE2 A GLN A 1 258 ? -0.371  -39.866 21.780  0.57 47.83  ? 1728 GLN A NE2 1 
ATOM   2091 N  NE2 B GLN A 1 258 ? -0.839  -38.995 19.271  0.43 56.23  ? 1728 GLN A NE2 1 
ATOM   2092 N  N   . ASP A 1 259 ? 3.701   -34.890 20.544  1.00 47.30  ? 1729 ASP A N   1 
ATOM   2093 C  CA  . ASP A 1 259 ? 5.144   -34.715 20.468  1.00 50.26  ? 1729 ASP A CA  1 
ATOM   2094 C  C   . ASP A 1 259 ? 5.743   -34.448 21.842  1.00 40.73  ? 1729 ASP A C   1 
ATOM   2095 O  O   . ASP A 1 259 ? 6.762   -35.043 22.205  1.00 44.55  ? 1729 ASP A O   1 
ATOM   2096 C  CB  . ASP A 1 259 ? 5.488   -33.589 19.505  1.00 36.39  ? 1729 ASP A CB  1 
ATOM   2097 C  CG  . ASP A 1 259 ? 6.976   -33.591 19.134  1.00 48.69  ? 1729 ASP A CG  1 
ATOM   2098 O  OD1 . ASP A 1 259 ? 7.409   -34.548 18.457  1.00 60.67  ? 1729 ASP A OD1 1 
ATOM   2099 O  OD2 . ASP A 1 259 ? 7.709   -32.658 19.529  1.00 42.68  ? 1729 ASP A OD2 1 
ATOM   2100 N  N   . VAL A 1 260 ? 5.114   -33.579 22.630  1.00 49.17  ? 1730 VAL A N   1 
ATOM   2101 C  CA  . VAL A 1 260 ? 5.587   -33.342 23.997  1.00 40.01  ? 1730 VAL A CA  1 
ATOM   2102 C  C   . VAL A 1 260 ? 5.666   -34.657 24.756  1.00 42.09  ? 1730 VAL A C   1 
ATOM   2103 O  O   . VAL A 1 260 ? 6.671   -34.957 25.419  1.00 44.16  ? 1730 VAL A O   1 
ATOM   2104 C  CB  . VAL A 1 260 ? 4.667   -32.341 24.732  1.00 38.67  ? 1730 VAL A CB  1 
ATOM   2105 C  CG1 . VAL A 1 260 ? 4.914   -32.385 26.231  1.00 35.91  ? 1730 VAL A CG1 1 
ATOM   2106 C  CG2 . VAL A 1 260 ? 4.858   -30.918 24.210  1.00 35.01  ? 1730 VAL A CG2 1 
ATOM   2107 N  N   . LEU A 1 261 ? 4.593   -35.455 24.668  1.00 37.12  ? 1731 LEU A N   1 
ATOM   2108 C  CA  . LEU A 1 261 ? 4.538   -36.732 25.359  1.00 39.19  ? 1731 LEU A CA  1 
ATOM   2109 C  C   . LEU A 1 261 ? 5.685   -37.653 24.917  1.00 49.03  ? 1731 LEU A C   1 
ATOM   2110 O  O   . LEU A 1 261 ? 6.369   -38.262 25.749  1.00 41.02  ? 1731 LEU A O   1 
ATOM   2111 C  CB  . LEU A 1 261 ? 3.182   -37.382 25.096  1.00 46.22  ? 1731 LEU A CB  1 
ATOM   2112 C  CG  . LEU A 1 261 ? 2.958   -38.560 26.028  1.00 58.02  ? 1731 LEU A CG  1 
ATOM   2113 C  CD1 . LEU A 1 261 ? 3.002   -38.061 27.458  1.00 68.87  ? 1731 LEU A CD1 1 
ATOM   2114 C  CD2 . LEU A 1 261 ? 1.634   -39.217 25.698  1.00 66.61  ? 1731 LEU A CD2 1 
ATOM   2115 N  N   . LYS A 1 262 ? 5.888   -37.766 23.602  1.00 38.15  ? 1732 LYS A N   1 
ATOM   2116 C  CA  . LYS A 1 262 ? 7.002   -38.524 23.051  1.00 42.66  ? 1732 LYS A CA  1 
ATOM   2117 C  C   . LYS A 1 262 ? 8.329   -38.076 23.656  1.00 49.71  ? 1732 LYS A C   1 
ATOM   2118 O  O   . LYS A 1 262 ? 9.142   -38.904 24.085  1.00 58.56  ? 1732 LYS A O   1 
ATOM   2119 C  CB  . LYS A 1 262 ? 7.022   -38.357 21.527  1.00 50.35  ? 1732 LYS A CB  1 
ATOM   2120 C  CG  . LYS A 1 262 ? 8.419   -38.540 20.899  1.00 81.87  ? 1732 LYS A CG  1 
ATOM   2121 C  CD  . LYS A 1 262 ? 8.538   -37.900 19.505  1.00 87.36  ? 1732 LYS A CD  1 
ATOM   2122 C  CE  . LYS A 1 262 ? 9.870   -37.147 19.316  1.00 80.20  ? 1732 LYS A CE  1 
ATOM   2123 N  NZ  . LYS A 1 262 ? 9.844   -35.685 19.717  1.00 67.74  ? 1732 LYS A NZ  1 
ATOM   2124 N  N   . PHE A 1 263 ? 8.559   -36.763 23.710  1.00 53.77  ? 1733 PHE A N   1 
ATOM   2125 C  CA  . PHE A 1 263 ? 9.823   -36.265 24.247  1.00 42.52  ? 1733 PHE A CA  1 
ATOM   2126 C  C   . PHE A 1 263 ? 9.984   -36.595 25.728  1.00 44.10  ? 1733 PHE A C   1 
ATOM   2127 O  O   . PHE A 1 263 ? 11.071  -36.977 26.165  1.00 50.53  ? 1733 PHE A O   1 
ATOM   2128 C  CB  . PHE A 1 263 ? 9.959   -34.767 24.042  1.00 42.19  ? 1733 PHE A CB  1 
ATOM   2129 C  CG  . PHE A 1 263 ? 11.093  -34.189 24.808  1.00 39.29  ? 1733 PHE A CG  1 
ATOM   2130 C  CD1 . PHE A 1 263 ? 12.386  -34.320 24.348  1.00 43.97  ? 1733 PHE A CD1 1 
ATOM   2131 C  CD2 . PHE A 1 263 ? 10.868  -33.556 26.016  1.00 46.20  ? 1733 PHE A CD2 1 
ATOM   2132 C  CE1 . PHE A 1 263 ? 13.457  -33.804 25.078  1.00 41.26  ? 1733 PHE A CE1 1 
ATOM   2133 C  CE2 . PHE A 1 263 ? 11.899  -33.028 26.745  1.00 39.74  ? 1733 PHE A CE2 1 
ATOM   2134 C  CZ  . PHE A 1 263 ? 13.218  -33.164 26.280  1.00 48.81  ? 1733 PHE A CZ  1 
ATOM   2135 N  N   . ILE A 1 264 ? 8.936   -36.402 26.529  1.00 39.47  ? 1734 ILE A N   1 
ATOM   2136 C  CA  . ILE A 1 264 ? 9.045   -36.721 27.953  1.00 44.95  ? 1734 ILE A CA  1 
ATOM   2137 C  C   . ILE A 1 264 ? 9.381   -38.195 28.137  1.00 46.38  ? 1734 ILE A C   1 
ATOM   2138 O  O   . ILE A 1 264 ? 10.213  -38.566 28.983  1.00 46.43  ? 1734 ILE A O   1 
ATOM   2139 C  CB  . ILE A 1 264 ? 7.743   -36.368 28.693  1.00 47.02  ? 1734 ILE A CB  1 
ATOM   2140 C  CG1 . ILE A 1 264 ? 7.477   -34.859 28.669  1.00 49.09  ? 1734 ILE A CG1 1 
ATOM   2141 C  CG2 . ILE A 1 264 ? 7.801   -36.926 30.119  1.00 49.00  ? 1734 ILE A CG2 1 
ATOM   2142 C  CD1 . ILE A 1 264 ? 6.106   -34.485 29.250  1.00 43.10  ? 1734 ILE A CD1 1 
ATOM   2143 N  N   . SER A 1 265 ? 8.772   -39.057 27.323  1.00 44.87  ? 1735 SER A N   1 
ATOM   2144 C  CA  . SER A 1 265 ? 9.068   -40.483 27.440  1.00 50.89  ? 1735 SER A CA  1 
ATOM   2145 C  C   . SER A 1 265 ? 10.531  -40.768 27.073  1.00 49.23  ? 1735 SER A C   1 
ATOM   2146 O  O   . SER A 1 265 ? 11.265  -41.390 27.847  1.00 45.91  ? 1735 SER A O   1 
ATOM   2147 C  CB  . SER A 1 265 ? 8.097   -41.300 26.586  1.00 59.63  ? 1735 SER A CB  1 
ATOM   2148 O  OG  . SER A 1 265 ? 8.675   -41.665 25.349  1.00 90.34  ? 1735 SER A OG  1 
ATOM   2149 N  N   . GLN A 1 266 ? 10.984  -40.261 25.926  1.00 42.96  ? 1736 GLN A N   1 
ATOM   2150 C  CA  . GLN A 1 266 ? 12.371  -40.468 25.498  1.00 60.02  ? 1736 GLN A CA  1 
ATOM   2151 C  C   . GLN A 1 266 ? 13.373  -39.928 26.518  1.00 53.84  ? 1736 GLN A C   1 
ATOM   2152 O  O   . GLN A 1 266 ? 14.367  -40.591 26.830  1.00 55.37  ? 1736 GLN A O   1 
ATOM   2153 C  CB  . GLN A 1 266 ? 12.593  -39.817 24.132  1.00 56.86  ? 1736 GLN A CB  1 
ATOM   2154 C  CG  . GLN A 1 266 ? 14.033  -39.843 23.653  1.00 76.04  ? 1736 GLN A CG  1 
ATOM   2155 C  CD  . GLN A 1 266 ? 14.312  -38.808 22.563  1.00 88.00  ? 1736 GLN A CD  1 
ATOM   2156 O  OE1 . GLN A 1 266 ? 13.572  -37.826 22.404  1.00 85.65  ? 1736 GLN A OE1 1 
ATOM   2157 N  NE2 . GLN A 1 266 ? 15.385  -39.028 21.806  1.00 86.80  ? 1736 GLN A NE2 1 
ATOM   2158 N  N   . TRP A 1 267 ? 13.101  -38.748 27.079  1.00 57.75  ? 1737 TRP A N   1 
ATOM   2159 C  CA  . TRP A 1 267 ? 14.027  -38.028 27.950  1.00 44.17  ? 1737 TRP A CA  1 
ATOM   2160 C  C   . TRP A 1 267 ? 14.095  -38.631 29.346  1.00 50.26  ? 1737 TRP A C   1 
ATOM   2161 O  O   . TRP A 1 267 ? 15.178  -38.733 29.929  1.00 58.65  ? 1737 TRP A O   1 
ATOM   2162 C  CB  . TRP A 1 267 ? 13.576  -36.572 28.032  1.00 44.95  ? 1737 TRP A CB  1 
ATOM   2163 C  CG  . TRP A 1 267 ? 14.338  -35.692 28.951  1.00 58.16  ? 1737 TRP A CG  1 
ATOM   2164 C  CD1 . TRP A 1 267 ? 15.666  -35.782 29.283  1.00 61.02  ? 1737 TRP A CD1 1 
ATOM   2165 C  CD2 . TRP A 1 267 ? 13.833  -34.542 29.631  1.00 50.74  ? 1737 TRP A CD2 1 
ATOM   2166 N  NE1 . TRP A 1 267 ? 16.011  -34.756 30.137  1.00 54.87  ? 1737 TRP A NE1 1 
ATOM   2167 C  CE2 . TRP A 1 267 ? 14.905  -33.980 30.361  1.00 58.07  ? 1737 TRP A CE2 1 
ATOM   2168 C  CE3 . TRP A 1 267 ? 12.577  -33.927 29.693  1.00 67.28  ? 1737 TRP A CE3 1 
ATOM   2169 C  CZ2 . TRP A 1 267 ? 14.754  -32.838 31.148  1.00 63.57  ? 1737 TRP A CZ2 1 
ATOM   2170 C  CZ3 . TRP A 1 267 ? 12.429  -32.784 30.467  1.00 61.56  ? 1737 TRP A CZ3 1 
ATOM   2171 C  CH2 . TRP A 1 267 ? 13.512  -32.255 31.187  1.00 61.08  ? 1737 TRP A CH2 1 
ATOM   2172 N  N   . CYS A 1 268 ? 12.966  -39.073 29.889  1.00 55.05  ? 1738 CYS A N   1 
ATOM   2173 C  CA  . CYS A 1 268 ? 12.927  -39.572 31.257  1.00 63.78  ? 1738 CYS A CA  1 
ATOM   2174 C  C   . CYS A 1 268 ? 12.802  -41.091 31.308  1.00 64.30  ? 1738 CYS A C   1 
ATOM   2175 O  O   . CYS A 1 268 ? 12.690  -41.662 32.398  1.00 68.90  ? 1738 CYS A O   1 
ATOM   2176 C  CB  . CYS A 1 268 ? 11.767  -38.929 32.027  1.00 64.53  ? 1738 CYS A CB  1 
ATOM   2177 S  SG  . CYS A 1 268 ? 11.652  -37.150 31.868  1.00 67.18  ? 1738 CYS A SG  1 
ATOM   2178 N  N   . GLY A 1 269 ? 12.857  -41.758 30.158  1.00 58.73  ? 1739 GLY A N   1 
ATOM   2179 C  CA  . GLY A 1 269 ? 13.053  -43.194 30.136  1.00 63.72  ? 1739 GLY A CA  1 
ATOM   2180 C  C   . GLY A 1 269 ? 11.757  -43.972 30.242  1.00 73.72  ? 1739 GLY A C   1 
ATOM   2181 O  O   . GLY A 1 269 ? 11.691  -44.974 30.959  1.00 82.12  ? 1739 GLY A O   1 
ATOM   2182 N  N   . GLY A 1 270 ? 10.727  -43.534 29.538  1.00 80.39  ? 1740 GLY A N   1 
ATOM   2183 C  CA  . GLY A 1 270 ? 9.485   -44.281 29.513  1.00 85.76  ? 1740 GLY A CA  1 
ATOM   2184 C  C   . GLY A 1 270 ? 8.402   -43.659 30.381  1.00 96.42  ? 1740 GLY A C   1 
ATOM   2185 O  O   . GLY A 1 270 ? 8.673   -42.917 31.335  1.00 85.30  ? 1740 GLY A O   1 
ATOM   2186 N  N   . LEU A 1 271 ? 7.148   -43.935 30.017  1.00 110.70 ? 1741 LEU A N   1 
ATOM   2187 C  CA  . LEU A 1 271 ? 6.006   -43.400 30.744  1.00 112.07 ? 1741 LEU A CA  1 
ATOM   2188 C  C   . LEU A 1 271 ? 6.018   -43.913 32.187  1.00 106.19 ? 1741 LEU A C   1 
ATOM   2189 O  O   . LEU A 1 271 ? 6.451   -45.041 32.452  1.00 121.66 ? 1741 LEU A O   1 
ATOM   2190 C  CB  . LEU A 1 271 ? 4.700   -43.793 30.046  1.00 113.14 ? 1741 LEU A CB  1 
ATOM   2191 C  CG  . LEU A 1 271 ? 4.459   -43.244 28.631  1.00 112.99 ? 1741 LEU A CG  1 
ATOM   2192 C  CD1 . LEU A 1 271 ? 4.844   -44.264 27.559  1.00 117.66 ? 1741 LEU A CD1 1 
ATOM   2193 C  CD2 . LEU A 1 271 ? 3.017   -42.776 28.443  1.00 104.40 ? 1741 LEU A CD2 1 
ATOM   2194 N  N   . PRO A 1 272 ? 5.551   -43.098 33.151  1.00 75.42  ? 1742 PRO A N   1 
ATOM   2195 C  CA  . PRO A 1 272 ? 5.725   -43.400 34.577  1.00 76.95  ? 1742 PRO A CA  1 
ATOM   2196 C  C   . PRO A 1 272 ? 4.790   -44.491 35.085  1.00 78.84  ? 1742 PRO A C   1 
ATOM   2197 O  O   . PRO A 1 272 ? 3.903   -44.886 34.328  1.00 89.38  ? 1742 PRO A O   1 
ATOM   2198 C  CB  . PRO A 1 272 ? 5.407   -42.066 35.244  1.00 73.29  ? 1742 PRO A CB  1 
ATOM   2199 C  CG  . PRO A 1 272 ? 4.350   -41.480 34.355  1.00 71.18  ? 1742 PRO A CG  1 
ATOM   2200 C  CD  . PRO A 1 272 ? 4.717   -41.898 32.947  1.00 71.00  ? 1742 PRO A CD  1 
ATOM   2201 N  N   . ASN B 1 7   ? -32.312 -28.946 10.712  1.00 120.67 ? 1477 ASN B N   1 
ATOM   2202 C  CA  . ASN B 1 7   ? -33.745 -28.699 10.682  1.00 116.43 ? 1477 ASN B CA  1 
ATOM   2203 C  C   . ASN B 1 7   ? -34.035 -27.190 10.641  1.00 120.13 ? 1477 ASN B C   1 
ATOM   2204 O  O   . ASN B 1 7   ? -35.136 -26.764 11.019  1.00 115.18 ? 1477 ASN B O   1 
ATOM   2205 C  CB  . ASN B 1 7   ? -34.416 -29.360 11.890  1.00 113.71 ? 1477 ASN B CB  1 
ATOM   2206 C  CG  . ASN B 1 7   ? -34.486 -30.870 11.763  1.00 113.28 ? 1477 ASN B CG  1 
ATOM   2207 O  OD1 . ASN B 1 7   ? -34.433 -31.411 10.656  1.00 111.35 ? 1477 ASN B OD1 1 
ATOM   2208 N  ND2 . ASN B 1 7   ? -34.597 -31.559 12.897  1.00 113.66 ? 1477 ASN B ND2 1 
ATOM   2209 N  N   . PHE B 1 8   ? -33.013 -26.435 10.188  1.00 117.60 ? 1478 PHE B N   1 
ATOM   2210 C  CA  . PHE B 1 8   ? -32.980 -25.002 9.859   1.00 109.80 ? 1478 PHE B CA  1 
ATOM   2211 C  C   . PHE B 1 8   ? -32.069 -24.155 10.752  1.00 89.65  ? 1478 PHE B C   1 
ATOM   2212 O  O   . PHE B 1 8   ? -30.899 -24.498 10.970  1.00 81.56  ? 1478 PHE B O   1 
ATOM   2213 C  CB  . PHE B 1 8   ? -34.381 -24.372 9.852   1.00 115.84 ? 1478 PHE B CB  1 
ATOM   2214 N  N   A ASN B 1 9   ? -32.619 -23.091 11.342  0.50 78.27  ? 1479 ASN B N   1 
ATOM   2215 N  N   B ASN B 1 9   ? -32.619 -23.007 11.173  0.50 78.55  ? 1479 ASN B N   1 
ATOM   2216 C  CA  A ASN B 1 9   ? -31.789 -21.968 11.775  0.50 68.81  ? 1479 ASN B CA  1 
ATOM   2217 C  CA  B ASN B 1 9   ? -32.033 -21.934 11.974  0.50 69.88  ? 1479 ASN B CA  1 
ATOM   2218 C  C   A ASN B 1 9   ? -30.751 -22.357 12.827  0.50 61.82  ? 1479 ASN B C   1 
ATOM   2219 C  C   B ASN B 1 9   ? -30.835 -22.359 12.810  0.50 61.69  ? 1479 ASN B C   1 
ATOM   2220 O  O   A ASN B 1 9   ? -29.634 -21.832 12.806  0.50 55.50  ? 1479 ASN B O   1 
ATOM   2221 O  O   B ASN B 1 9   ? -29.713 -21.894 12.597  0.50 58.06  ? 1479 ASN B O   1 
ATOM   2222 C  CB  A ASN B 1 9   ? -32.657 -20.831 12.297  0.50 75.23  ? 1479 ASN B CB  1 
ATOM   2223 C  CB  B ASN B 1 9   ? -33.116 -21.364 12.904  0.50 75.84  ? 1479 ASN B CB  1 
ATOM   2224 C  CG  A ASN B 1 9   ? -31.850 -19.585 12.581  0.50 81.45  ? 1479 ASN B CG  1 
ATOM   2225 C  CG  B ASN B 1 9   ? -33.345 -19.880 12.710  0.50 82.07  ? 1479 ASN B CG  1 
ATOM   2226 O  OD1 A ASN B 1 9   ? -31.497 -18.841 11.665  0.50 86.68  ? 1479 ASN B OD1 1 
ATOM   2227 O  OD1 B ASN B 1 9   ? -32.513 -19.184 12.126  0.50 85.47  ? 1479 ASN B OD1 1 
ATOM   2228 N  ND2 A ASN B 1 9   ? -31.534 -19.360 13.852  0.50 83.05  ? 1479 ASN B ND2 1 
ATOM   2229 N  ND2 B ASN B 1 9   ? -34.481 -19.383 13.204  0.50 73.62  ? 1479 ASN B ND2 1 
ATOM   2230 N  N   . ILE B 1 10  ? -31.088 -23.238 13.777  1.00 53.67  ? 1480 ILE B N   1 
ATOM   2231 C  CA  . ILE B 1 10  ? -30.082 -23.609 14.775  1.00 58.11  ? 1480 ILE B CA  1 
ATOM   2232 C  C   . ILE B 1 10  ? -28.862 -24.237 14.096  1.00 52.70  ? 1480 ILE B C   1 
ATOM   2233 O  O   . ILE B 1 10  ? -27.714 -23.831 14.330  1.00 50.88  ? 1480 ILE B O   1 
ATOM   2234 C  CB  . ILE B 1 10  ? -30.690 -24.542 15.838  1.00 52.85  ? 1480 ILE B CB  1 
ATOM   2235 C  CG1 . ILE B 1 10  ? -31.786 -23.823 16.638  1.00 84.87  ? 1480 ILE B CG1 1 
ATOM   2236 C  CG2 . ILE B 1 10  ? -29.612 -25.040 16.781  1.00 53.49  ? 1480 ILE B CG2 1 
ATOM   2237 C  CD1 . ILE B 1 10  ? -31.291 -22.689 17.523  1.00 84.16  ? 1480 ILE B CD1 1 
ATOM   2238 N  N   . TYR B 1 11  ? -29.098 -25.211 13.216  1.00 57.76  ? 1481 TYR B N   1 
ATOM   2239 C  CA  . TYR B 1 11  ? -27.986 -25.916 12.582  1.00 49.14  ? 1481 TYR B CA  1 
ATOM   2240 C  C   . TYR B 1 11  ? -27.236 -25.008 11.608  1.00 60.24  ? 1481 TYR B C   1 
ATOM   2241 O  O   . TYR B 1 11  ? -25.988 -25.021 11.557  1.00 54.44  ? 1481 TYR B O   1 
ATOM   2242 C  CB  . TYR B 1 11  ? -28.516 -27.157 11.879  1.00 49.77  ? 1481 TYR B CB  1 
ATOM   2243 C  CG  . TYR B 1 11  ? -29.126 -28.153 12.851  1.00 52.82  ? 1481 TYR B CG  1 
ATOM   2244 C  CD1 . TYR B 1 11  ? -28.328 -29.023 13.579  1.00 53.66  ? 1481 TYR B CD1 1 
ATOM   2245 C  CD2 . TYR B 1 11  ? -30.499 -28.197 13.066  1.00 63.72  ? 1481 TYR B CD2 1 
ATOM   2246 C  CE1 . TYR B 1 11  ? -28.877 -29.922 14.479  1.00 50.12  ? 1481 TYR B CE1 1 
ATOM   2247 C  CE2 . TYR B 1 11  ? -31.059 -29.095 13.962  1.00 61.91  ? 1481 TYR B CE2 1 
ATOM   2248 C  CZ  . TYR B 1 11  ? -30.240 -29.957 14.668  1.00 62.62  ? 1481 TYR B CZ  1 
ATOM   2249 O  OH  . TYR B 1 11  ? -30.793 -30.845 15.565  1.00 57.35  ? 1481 TYR B OH  1 
ATOM   2250 N  N   . LYS B 1 12  ? -27.974 -24.192 10.846  1.00 50.67  ? 1482 LYS B N   1 
ATOM   2251 C  CA  . LYS B 1 12  ? -27.311 -23.242 9.959   1.00 66.10  ? 1482 LYS B CA  1 
ATOM   2252 C  C   . LYS B 1 12  ? -26.456 -22.265 10.751  1.00 53.12  ? 1482 LYS B C   1 
ATOM   2253 O  O   . LYS B 1 12  ? -25.338 -21.934 10.345  1.00 48.73  ? 1482 LYS B O   1 
ATOM   2254 C  CB  . LYS B 1 12  ? -28.329 -22.495 9.101   1.00 73.02  ? 1482 LYS B CB  1 
ATOM   2255 C  CG  . LYS B 1 12  ? -27.665 -21.553 8.099   1.00 81.23  ? 1482 LYS B CG  1 
ATOM   2256 C  CD  . LYS B 1 12  ? -28.454 -21.441 6.796   1.00 84.61  ? 1482 LYS B CD  1 
ATOM   2257 C  CE  . LYS B 1 12  ? -27.860 -20.368 5.878   1.00 80.76  ? 1482 LYS B CE  1 
ATOM   2258 N  NZ  . LYS B 1 12  ? -28.327 -18.987 6.245   1.00 87.00  ? 1482 LYS B NZ  1 
ATOM   2259 N  N   . ARG B 1 13  ? -26.955 -21.812 11.896  1.00 48.87  ? 1483 ARG B N   1 
ATOM   2260 C  CA  . ARG B 1 13  ? -26.197 -20.880 12.709  1.00 50.21  ? 1483 ARG B CA  1 
ATOM   2261 C  C   . ARG B 1 13  ? -24.951 -21.533 13.283  1.00 53.90  ? 1483 ARG B C   1 
ATOM   2262 O  O   . ARG B 1 13  ? -23.912 -20.879 13.418  1.00 59.13  ? 1483 ARG B O   1 
ATOM   2263 C  CB  . ARG B 1 13  ? -27.086 -20.311 13.810  1.00 57.11  ? 1483 ARG B CB  1 
ATOM   2264 C  CG  . ARG B 1 13  ? -27.676 -18.978 13.421  1.00 73.31  ? 1483 ARG B CG  1 
ATOM   2265 C  CD  . ARG B 1 13  ? -26.546 -17.997 13.221  1.00 86.59  ? 1483 ARG B CD  1 
ATOM   2266 N  NE  . ARG B 1 13  ? -25.665 -17.998 14.386  1.00 92.53  ? 1483 ARG B NE  1 
ATOM   2267 C  CZ  . ARG B 1 13  ? -25.901 -17.284 15.485  1.00 86.98  ? 1483 ARG B CZ  1 
ATOM   2268 N  NH1 . ARG B 1 13  ? -26.982 -16.511 15.544  1.00 66.92  ? 1483 ARG B NH1 1 
ATOM   2269 N  NH2 . ARG B 1 13  ? -25.062 -17.336 16.516  1.00 86.07  ? 1483 ARG B NH2 1 
ATOM   2270 N  N   . ILE B 1 14  ? -25.017 -22.824 13.609  1.00 59.95  ? 1484 ILE B N   1 
ATOM   2271 C  CA  . ILE B 1 14  ? -23.807 -23.500 14.075  1.00 45.90  ? 1484 ILE B CA  1 
ATOM   2272 C  C   . ILE B 1 14  ? -22.761 -23.517 12.972  1.00 43.69  ? 1484 ILE B C   1 
ATOM   2273 O  O   . ILE B 1 14  ? -21.566 -23.288 13.210  1.00 44.46  ? 1484 ILE B O   1 
ATOM   2274 C  CB  . ILE B 1 14  ? -24.123 -24.928 14.543  1.00 50.24  ? 1484 ILE B CB  1 
ATOM   2275 C  CG1 . ILE B 1 14  ? -24.842 -24.920 15.889  1.00 70.18  ? 1484 ILE B CG1 1 
ATOM   2276 C  CG2 . ILE B 1 14  ? -22.832 -25.751 14.611  1.00 46.65  ? 1484 ILE B CG2 1 
ATOM   2277 C  CD1 . ILE B 1 14  ? -25.484 -26.275 16.218  1.00 60.39  ? 1484 ILE B CD1 1 
ATOM   2278 N  N   . PHE B 1 15  ? -23.199 -23.812 11.751  1.00 44.25  ? 1485 PHE B N   1 
ATOM   2279 C  CA  . PHE B 1 15  ? -22.292 -23.833 10.619  1.00 46.55  ? 1485 PHE B CA  1 
ATOM   2280 C  C   . PHE B 1 15  ? -21.654 -22.460 10.399  1.00 52.69  ? 1485 PHE B C   1 
ATOM   2281 O  O   . PHE B 1 15  ? -20.421 -22.342 10.314  1.00 50.58  ? 1485 PHE B O   1 
ATOM   2282 C  CB  . PHE B 1 15  ? -23.052 -24.299 9.382   1.00 44.56  ? 1485 PHE B CB  1 
ATOM   2283 C  CG  . PHE B 1 15  ? -22.267 -24.209 8.106   1.00 44.24  ? 1485 PHE B CG  1 
ATOM   2284 C  CD1 . PHE B 1 15  ? -21.549 -25.295 7.636   1.00 43.55  ? 1485 PHE B CD1 1 
ATOM   2285 C  CD2 . PHE B 1 15  ? -22.259 -23.037 7.355   1.00 63.95  ? 1485 PHE B CD2 1 
ATOM   2286 C  CE1 . PHE B 1 15  ? -20.829 -25.210 6.452   1.00 46.04  ? 1485 PHE B CE1 1 
ATOM   2287 C  CE2 . PHE B 1 15  ? -21.524 -22.946 6.170   1.00 48.07  ? 1485 PHE B CE2 1 
ATOM   2288 C  CZ  . PHE B 1 15  ? -20.811 -24.034 5.720   1.00 44.63  ? 1485 PHE B CZ  1 
ATOM   2289 N  N   . THR B 1 16  ? -22.485 -21.418 10.248  1.00 45.78  ? 1486 THR B N   1 
ATOM   2290 C  CA  . THR B 1 16  ? -21.964 -20.072 9.977   1.00 44.65  ? 1486 THR B CA  1 
ATOM   2291 C  C   . THR B 1 16  ? -21.009 -19.636 11.078  1.00 46.06  ? 1486 THR B C   1 
ATOM   2292 O  O   . THR B 1 16  ? -19.924 -19.095 10.807  1.00 59.67  ? 1486 THR B O   1 
ATOM   2293 C  CB  . THR B 1 16  ? -23.100 -19.045 9.835   1.00 62.73  ? 1486 THR B CB  1 
ATOM   2294 O  OG1 . THR B 1 16  ? -23.810 -18.957 11.067  1.00 76.64  ? 1486 THR B OG1 1 
ATOM   2295 C  CG2 . THR B 1 16  ? -24.081 -19.413 8.727   1.00 48.44  ? 1486 THR B CG2 1 
ATOM   2296 N  N   . ASP B 1 17  ? -21.399 -19.858 12.340  1.00 45.08  ? 1487 ASP B N   1 
ATOM   2297 C  CA  . ASP B 1 17  ? -20.513 -19.523 13.446  1.00 47.23  ? 1487 ASP B CA  1 
ATOM   2298 C  C   . ASP B 1 17  ? -19.176 -20.240 13.315  1.00 62.07  ? 1487 ASP B C   1 
ATOM   2299 O  O   . ASP B 1 17  ? -18.109 -19.623 13.455  1.00 50.20  ? 1487 ASP B O   1 
ATOM   2300 C  CB  . ASP B 1 17  ? -21.179 -19.878 14.777  1.00 45.57  ? 1487 ASP B CB  1 
ATOM   2301 C  CG  . ASP B 1 17  ? -22.266 -18.883 15.172  1.00 84.65  ? 1487 ASP B CG  1 
ATOM   2302 O  OD1 . ASP B 1 17  ? -22.922 -19.089 16.219  1.00 89.92  ? 1487 ASP B OD1 1 
ATOM   2303 O  OD2 . ASP B 1 17  ? -22.474 -17.897 14.427  1.00 92.70  ? 1487 ASP B OD2 1 
ATOM   2304 N  N   . MET B 1 18  ? -19.213 -21.543 13.012  1.00 42.57  ? 1488 MET B N   1 
ATOM   2305 C  CA  . MET B 1 18  ? -17.985 -22.323 12.992  1.00 39.84  ? 1488 MET B CA  1 
ATOM   2306 C  C   . MET B 1 18  ? -17.050 -21.872 11.888  1.00 40.89  ? 1488 MET B C   1 
ATOM   2307 O  O   . MET B 1 18  ? -15.847 -21.725 12.120  1.00 38.78  ? 1488 MET B O   1 
ATOM   2308 C  CB  . MET B 1 18  ? -18.322 -23.805 12.818  1.00 49.97  ? 1488 MET B CB  1 
ATOM   2309 C  CG  . MET B 1 18  ? -17.120 -24.686 12.869  1.00 74.50  ? 1488 MET B CG  1 
ATOM   2310 S  SD  . MET B 1 18  ? -16.923 -25.307 14.530  1.00 85.40  ? 1488 MET B SD  1 
ATOM   2311 C  CE  . MET B 1 18  ? -15.917 -24.043 15.277  1.00 72.37  ? 1488 MET B CE  1 
ATOM   2312 N  N   . VAL B 1 19  ? -17.595 -21.634 10.687  1.00 41.64  ? 1489 VAL B N   1 
ATOM   2313 C  CA  . VAL B 1 19  ? -16.765 -21.300 9.533   1.00 40.20  ? 1489 VAL B CA  1 
ATOM   2314 C  C   . VAL B 1 19  ? -16.314 -19.846 9.549   1.00 51.83  ? 1489 VAL B C   1 
ATOM   2315 O  O   . VAL B 1 19  ? -15.431 -19.467 8.773   1.00 48.36  ? 1489 VAL B O   1 
ATOM   2316 C  CB  . VAL B 1 19  ? -17.487 -21.545 8.195   1.00 41.10  ? 1489 VAL B CB  1 
ATOM   2317 C  CG1 . VAL B 1 19  ? -17.887 -23.017 8.029   1.00 52.59  ? 1489 VAL B CG1 1 
ATOM   2318 C  CG2 . VAL B 1 19  ? -18.718 -20.605 8.044   1.00 42.38  ? 1489 VAL B CG2 1 
ATOM   2319 N  N   . SER B 1 20  ? -16.904 -19.022 10.396  1.00 40.90  ? 1490 SER B N   1 
ATOM   2320 C  CA  . SER B 1 20  ? -16.385 -17.688 10.650  1.00 55.04  ? 1490 SER B CA  1 
ATOM   2321 C  C   . SER B 1 20  ? -15.592 -17.629 11.944  1.00 56.53  ? 1490 SER B C   1 
ATOM   2322 O  O   . SER B 1 20  ? -15.123 -16.558 12.323  1.00 52.20  ? 1490 SER B O   1 
ATOM   2323 C  CB  . SER B 1 20  ? -17.539 -16.667 10.681  1.00 51.15  ? 1490 SER B CB  1 
ATOM   2324 O  OG  . SER B 1 20  ? -18.120 -16.605 11.976  1.00 59.04  ? 1490 SER B OG  1 
ATOM   2325 N  N   . SER B 1 21  ? -15.443 -18.714 12.607  1.00 49.42  ? 1491 SER B N   1 
ATOM   2326 C  CA  . SER B 1 21  ? -14.791 -18.621 13.901  1.00 43.76  ? 1491 SER B CA  1 
ATOM   2327 C  C   . SER B 1 21  ? -13.262 -18.684 13.782  1.00 61.80  ? 1491 SER B C   1 
ATOM   2328 O  O   . SER B 1 21  ? -12.721 -19.348 12.881  1.00 44.94  ? 1491 SER B O   1 
ATOM   2329 C  CB  . SER B 1 21  ? -15.292 -19.748 14.802  1.00 47.70  ? 1491 SER B CB  1 
ATOM   2330 O  OG  . SER B 1 21  ? -14.333 -20.124 15.764  1.00 63.35  ? 1491 SER B OG  1 
ATOM   2331 N  N   . PRO B 1 22  ? -12.547 -18.048 14.715  1.00 50.68  ? 1492 PRO B N   1 
ATOM   2332 C  CA  . PRO B 1 22  ? -11.081 -18.091 14.691  1.00 47.51  ? 1492 PRO B CA  1 
ATOM   2333 C  C   . PRO B 1 22  ? -10.546 -19.410 15.224  1.00 57.55  ? 1492 PRO B C   1 
ATOM   2334 O  O   . PRO B 1 22  ? -11.242 -20.179 15.889  1.00 44.74  ? 1492 PRO B O   1 
ATOM   2335 C  CB  . PRO B 1 22  ? -10.674 -16.946 15.622  1.00 54.30  ? 1492 PRO B CB  1 
ATOM   2336 C  CG  . PRO B 1 22  ? -11.810 -16.871 16.605  1.00 59.86  ? 1492 PRO B CG  1 
ATOM   2337 C  CD  . PRO B 1 22  ? -13.058 -17.203 15.814  1.00 56.68  ? 1492 PRO B CD  1 
ATOM   2338 N  N   . GLY B 1 23  ? -9.277  -19.658 14.917  1.00 54.83  ? 1493 GLY B N   1 
ATOM   2339 C  CA  . GLY B 1 23  ? -8.580  -20.799 15.480  1.00 45.63  ? 1493 GLY B CA  1 
ATOM   2340 C  C   . GLY B 1 23  ? -9.005  -22.150 14.944  1.00 56.01  ? 1493 GLY B C   1 
ATOM   2341 O  O   . GLY B 1 23  ? -8.852  -23.160 15.638  1.00 48.86  ? 1493 GLY B O   1 
ATOM   2342 N  N   . THR B 1 24  ? -9.514  -22.205 13.718  1.00 48.52  ? 1494 THR B N   1 
ATOM   2343 C  CA  . THR B 1 24  ? -9.997  -23.452 13.153  1.00 43.08  ? 1494 THR B CA  1 
ATOM   2344 C  C   . THR B 1 24  ? -9.100  -23.990 12.061  1.00 54.62  ? 1494 THR B C   1 
ATOM   2345 O  O   . THR B 1 24  ? -9.364  -25.080 11.535  1.00 44.10  ? 1494 THR B O   1 
ATOM   2346 C  CB  . THR B 1 24  ? -11.374 -23.259 12.560  1.00 41.33  ? 1494 THR B CB  1 
ATOM   2347 O  OG1 . THR B 1 24  ? -11.291 -22.195 11.599  1.00 42.01  ? 1494 THR B OG1 1 
ATOM   2348 C  CG2 . THR B 1 24  ? -12.398 -22.960 13.660  1.00 49.58  ? 1494 THR B CG2 1 
ATOM   2349 N  N   . ASN B 1 25  ? -8.069  -23.253 11.683  1.00 39.51  ? 1495 ASN B N   1 
ATOM   2350 C  CA  . ASN B 1 25  ? -7.202  -23.682 10.598  1.00 42.10  ? 1495 ASN B CA  1 
ATOM   2351 C  C   . ASN B 1 25  ? -5.980  -24.392 11.167  1.00 52.23  ? 1495 ASN B C   1 
ATOM   2352 O  O   . ASN B 1 25  ? -4.857  -23.965 10.967  1.00 44.27  ? 1495 ASN B O   1 
ATOM   2353 C  CB  . ASN B 1 25  ? -6.807  -22.489 9.732   1.00 42.73  ? 1495 ASN B CB  1 
ATOM   2354 C  CG  . ASN B 1 25  ? -6.041  -22.906 8.496   1.00 47.89  ? 1495 ASN B CG  1 
ATOM   2355 O  OD1 . ASN B 1 25  ? -6.138  -24.052 8.049   1.00 49.86  ? 1495 ASN B OD1 1 
ATOM   2356 N  ND2 . ASN B 1 25  ? -5.289  -21.983 7.926   1.00 41.76  ? 1495 ASN B ND2 1 
ATOM   2357 N  N   . CYS B 1 26  ? -6.224  -25.464 11.930  1.00 48.59  ? 1496 CYS B N   1 
ATOM   2358 C  CA  . CYS B 1 26  ? -5.128  -26.237 12.502  1.00 48.26  ? 1496 CYS B CA  1 
ATOM   2359 C  C   . CYS B 1 26  ? -5.593  -27.664 12.765  1.00 40.06  ? 1496 CYS B C   1 
ATOM   2360 O  O   . CYS B 1 26  ? -6.795  -27.946 12.837  1.00 44.69  ? 1496 CYS B O   1 
ATOM   2361 C  CB  . CYS B 1 26  ? -4.584  -25.595 13.787  1.00 43.07  ? 1496 CYS B CB  1 
ATOM   2362 S  SG  . CYS B 1 26  ? -5.781  -25.557 15.119  1.00 53.39  ? 1496 CYS B SG  1 
ATOM   2363 N  N   . ALA B 1 27  ? -4.610  -28.561 12.911  1.00 38.47  ? 1497 ALA B N   1 
ATOM   2364 C  CA  . ALA B 1 27  ? -4.898  -29.967 13.201  1.00 39.98  ? 1497 ALA B CA  1 
ATOM   2365 C  C   . ALA B 1 27  ? -5.752  -30.121 14.454  1.00 53.48  ? 1497 ALA B C   1 
ATOM   2366 O  O   . ALA B 1 27  ? -6.658  -30.965 14.498  1.00 38.45  ? 1497 ALA B O   1 
ATOM   2367 C  CB  . ALA B 1 27  ? -3.594  -30.760 13.343  1.00 33.90  ? 1497 ALA B CB  1 
ATOM   2368 N  N   . GLU B 1 28  ? -5.478  -29.312 15.481  1.00 46.63  ? 1498 GLU B N   1 
ATOM   2369 C  CA  . GLU B 1 28  ? -6.188  -29.396 16.750  1.00 48.61  ? 1498 GLU B CA  1 
ATOM   2370 C  C   . GLU B 1 28  ? -7.657  -29.035 16.619  1.00 50.96  ? 1498 GLU B C   1 
ATOM   2371 O  O   . GLU B 1 28  ? -8.424  -29.333 17.540  1.00 57.83  ? 1498 GLU B O   1 
ATOM   2372 C  CB  . GLU B 1 28  ? -5.553  -28.494 17.808  1.00 47.10  ? 1498 GLU B CB  1 
ATOM   2373 C  CG  . GLU B 1 28  ? -4.293  -29.070 18.465  1.00 54.31  ? 1498 GLU B CG  1 
ATOM   2374 C  CD  . GLU B 1 28  ? -3.057  -28.962 17.576  1.00 49.08  ? 1498 GLU B CD  1 
ATOM   2375 O  OE1 . GLU B 1 28  ? -3.116  -28.223 16.563  1.00 42.03  ? 1498 GLU B OE1 1 
ATOM   2376 O  OE2 . GLU B 1 28  ? -2.043  -29.624 17.890  1.00 44.64  ? 1498 GLU B OE2 1 
ATOM   2377 N  N   . ALA B 1 29  ? -8.061  -28.420 15.507  1.00 42.71  ? 1499 ALA B N   1 
ATOM   2378 C  CA  . ALA B 1 29  ? -9.468  -28.125 15.273  1.00 48.16  ? 1499 ALA B CA  1 
ATOM   2379 C  C   . ALA B 1 29  ? -10.217 -29.316 14.696  1.00 43.97  ? 1499 ALA B C   1 
ATOM   2380 O  O   . ALA B 1 29  ? -11.414 -29.200 14.413  1.00 40.38  ? 1499 ALA B O   1 
ATOM   2381 C  CB  . ALA B 1 29  ? -9.612  -26.928 14.336  1.00 39.47  ? 1499 ALA B CB  1 
ATOM   2382 N  N   . TYR B 1 30  ? -9.543  -30.451 14.497  1.00 40.58  ? 1500 TYR B N   1 
ATOM   2383 C  CA  . TYR B 1 30  ? -10.186 -31.558 13.803  1.00 37.30  ? 1500 TYR B CA  1 
ATOM   2384 C  C   . TYR B 1 30  ? -11.529 -31.897 14.435  1.00 35.61  ? 1500 TYR B C   1 
ATOM   2385 O  O   . TYR B 1 30  ? -12.549 -31.999 13.745  1.00 43.26  ? 1500 TYR B O   1 
ATOM   2386 C  CB  . TYR B 1 30  ? -9.303  -32.808 13.789  1.00 44.05  ? 1500 TYR B CB  1 
ATOM   2387 C  CG  . TYR B 1 30  ? -10.106 -33.958 13.264  1.00 35.78  ? 1500 TYR B CG  1 
ATOM   2388 C  CD1 . TYR B 1 30  ? -10.359 -34.072 11.896  1.00 36.16  ? 1500 TYR B CD1 1 
ATOM   2389 C  CD2 . TYR B 1 30  ? -10.661 -34.905 14.127  1.00 36.17  ? 1500 TYR B CD2 1 
ATOM   2390 C  CE1 . TYR B 1 30  ? -11.114 -35.126 11.392  1.00 45.16  ? 1500 TYR B CE1 1 
ATOM   2391 C  CE2 . TYR B 1 30  ? -11.424 -35.981 13.629  1.00 37.84  ? 1500 TYR B CE2 1 
ATOM   2392 C  CZ  . TYR B 1 30  ? -11.648 -36.074 12.263  1.00 40.30  ? 1500 TYR B CZ  1 
ATOM   2393 O  OH  . TYR B 1 30  ? -12.413 -37.080 11.749  1.00 38.11  ? 1500 TYR B OH  1 
ATOM   2394 N  N   . HIS B 1 31  ? -11.537 -32.072 15.756  1.00 41.19  ? 1501 HIS B N   1 
ATOM   2395 C  CA  . HIS B 1 31  ? -12.742 -32.529 16.431  1.00 44.64  ? 1501 HIS B CA  1 
ATOM   2396 C  C   . HIS B 1 31  ? -13.817 -31.446 16.450  1.00 54.46  ? 1501 HIS B C   1 
ATOM   2397 O  O   . HIS B 1 31  ? -15.007 -31.790 16.529  1.00 42.81  ? 1501 HIS B O   1 
ATOM   2398 C  CB  . HIS B 1 31  ? -12.411 -33.051 17.836  1.00 37.66  ? 1501 HIS B CB  1 
ATOM   2399 C  CG  . HIS B 1 31  ? -11.946 -34.482 17.848  1.00 53.91  ? 1501 HIS B CG  1 
ATOM   2400 N  ND1 . HIS B 1 31  ? -12.793 -35.549 17.612  1.00 69.77  ? 1501 HIS B ND1 1 
ATOM   2401 C  CD2 . HIS B 1 31  ? -10.716 -35.022 18.044  1.00 70.65  ? 1501 HIS B CD2 1 
ATOM   2402 C  CE1 . HIS B 1 31  ? -12.107 -36.679 17.671  1.00 62.78  ? 1501 HIS B CE1 1 
ATOM   2403 N  NE2 . HIS B 1 31  ? -10.847 -36.390 17.937  1.00 61.22  ? 1501 HIS B NE2 1 
ATOM   2404 N  N   . SER B 1 32  ? -13.444 -30.157 16.292  1.00 42.92  ? 1502 SER B N   1 
ATOM   2405 C  CA  . SER B 1 32  ? -14.496 -29.156 16.164  1.00 42.87  ? 1502 SER B CA  1 
ATOM   2406 C  C   . SER B 1 32  ? -15.191 -29.305 14.828  1.00 37.20  ? 1502 SER B C   1 
ATOM   2407 O  O   . SER B 1 32  ? -16.431 -29.331 14.768  1.00 38.46  ? 1502 SER B O   1 
ATOM   2408 C  CB  . SER B 1 32  ? -13.952 -27.710 16.269  1.00 47.72  ? 1502 SER B CB  1 
ATOM   2409 O  OG  . SER B 1 32  ? -13.245 -27.433 17.474  1.00 47.07  ? 1502 SER B OG  1 
ATOM   2410 N  N   . TRP B 1 33  ? -14.420 -29.547 13.771  1.00 36.74  ? 1503 TRP B N   1 
ATOM   2411 C  CA  . TRP B 1 33  ? -15.035 -29.753 12.464  1.00 39.63  ? 1503 TRP B CA  1 
ATOM   2412 C  C   . TRP B 1 33  ? -15.768 -31.101 12.395  1.00 41.86  ? 1503 TRP B C   1 
ATOM   2413 O  O   . TRP B 1 33  ? -16.897 -31.180 11.884  1.00 47.08  ? 1503 TRP B O   1 
ATOM   2414 C  CB  . TRP B 1 33  ? -13.969 -29.654 11.368  1.00 36.95  ? 1503 TRP B CB  1 
ATOM   2415 C  CG  . TRP B 1 33  ? -13.355 -28.296 11.171  1.00 41.40  ? 1503 TRP B CG  1 
ATOM   2416 C  CD1 . TRP B 1 33  ? -12.048 -27.940 11.363  1.00 48.32  ? 1503 TRP B CD1 1 
ATOM   2417 C  CD2 . TRP B 1 33  ? -14.031 -27.115 10.726  1.00 42.02  ? 1503 TRP B CD2 1 
ATOM   2418 N  NE1 . TRP B 1 33  ? -11.869 -26.598 11.061  1.00 36.03  ? 1503 TRP B NE1 1 
ATOM   2419 C  CE2 . TRP B 1 33  ? -13.074 -26.080 10.661  1.00 45.20  ? 1503 TRP B CE2 1 
ATOM   2420 C  CE3 . TRP B 1 33  ? -15.351 -26.842 10.349  1.00 50.59  ? 1503 TRP B CE3 1 
ATOM   2421 C  CZ2 . TRP B 1 33  ? -13.403 -24.801 10.251  1.00 40.45  ? 1503 TRP B CZ2 1 
ATOM   2422 C  CZ3 . TRP B 1 33  ? -15.678 -25.571 9.950   1.00 46.75  ? 1503 TRP B CZ3 1 
ATOM   2423 C  CH2 . TRP B 1 33  ? -14.709 -24.568 9.899   1.00 43.33  ? 1503 TRP B CH2 1 
ATOM   2424 N  N   . ALA B 1 34  ? -15.146 -32.170 12.904  1.00 45.53  ? 1504 ALA B N   1 
ATOM   2425 C  CA  . ALA B 1 34  ? -15.782 -33.481 12.849  1.00 38.38  ? 1504 ALA B CA  1 
ATOM   2426 C  C   . ALA B 1 34  ? -17.159 -33.440 13.505  1.00 41.58  ? 1504 ALA B C   1 
ATOM   2427 O  O   . ALA B 1 34  ? -18.141 -33.911 12.920  1.00 44.56  ? 1504 ALA B O   1 
ATOM   2428 C  CB  . ALA B 1 34  ? -14.902 -34.536 13.522  1.00 38.38  ? 1504 ALA B CB  1 
ATOM   2429 N  N   . ASP B 1 35  ? -17.245 -32.842 14.705  1.00 43.81  ? 1505 ASP B N   1 
ATOM   2430 C  CA  . ASP B 1 35  ? -18.530 -32.667 15.380  1.00 43.67  ? 1505 ASP B CA  1 
ATOM   2431 C  C   . ASP B 1 35  ? -19.526 -31.978 14.464  1.00 54.70  ? 1505 ASP B C   1 
ATOM   2432 O  O   . ASP B 1 35  ? -20.625 -32.495 14.226  1.00 45.88  ? 1505 ASP B O   1 
ATOM   2433 C  CB  . ASP B 1 35  ? -18.354 -31.880 16.683  1.00 43.45  ? 1505 ASP B CB  1 
ATOM   2434 C  CG  . ASP B 1 35  ? -19.715 -31.545 17.365  1.00 61.27  ? 1505 ASP B CG  1 
ATOM   2435 O  OD1 . ASP B 1 35  ? -19.984 -30.360 17.677  1.00 49.09  ? 1505 ASP B OD1 1 
ATOM   2436 O  OD2 . ASP B 1 35  ? -20.520 -32.468 17.588  1.00 59.57  ? 1505 ASP B OD2 1 
ATOM   2437 N  N   . LEU B 1 36  ? -19.144 -30.822 13.905  1.00 53.98  ? 1506 LEU B N   1 
ATOM   2438 C  CA  . LEU B 1 36  ? -20.052 -30.155 12.981  1.00 45.99  ? 1506 LEU B CA  1 
ATOM   2439 C  C   . LEU B 1 36  ? -20.434 -31.110 11.865  1.00 41.42  ? 1506 LEU B C   1 
ATOM   2440 O  O   . LEU B 1 36  ? -21.621 -31.317 11.586  1.00 42.53  ? 1506 LEU B O   1 
ATOM   2441 C  CB  . LEU B 1 36  ? -19.417 -28.879 12.424  1.00 40.29  ? 1506 LEU B CB  1 
ATOM   2442 C  CG  . LEU B 1 36  ? -20.104 -28.206 11.229  1.00 41.05  ? 1506 LEU B CG  1 
ATOM   2443 C  CD1 . LEU B 1 36  ? -21.422 -27.526 11.663  1.00 49.67  ? 1506 LEU B CD1 1 
ATOM   2444 C  CD2 . LEU B 1 36  ? -19.165 -27.191 10.575  1.00 45.99  ? 1506 LEU B CD2 1 
ATOM   2445 N  N   . ARG B 1 37  ? -19.426 -31.757 11.268  1.00 40.81  ? 1507 ARG B N   1 
ATOM   2446 C  CA  . ARG B 1 37  ? -19.666 -32.754 10.229  1.00 48.93  ? 1507 ARG B CA  1 
ATOM   2447 C  C   . ARG B 1 37  ? -20.686 -33.789 10.690  1.00 48.65  ? 1507 ARG B C   1 
ATOM   2448 O  O   . ARG B 1 37  ? -21.690 -34.033 10.013  1.00 50.19  ? 1507 ARG B O   1 
ATOM   2449 C  CB  . ARG B 1 37  ? -18.351 -33.456 9.844   1.00 40.67  ? 1507 ARG B CB  1 
ATOM   2450 C  CG  . ARG B 1 37  ? -18.470 -34.471 8.674   1.00 41.34  ? 1507 ARG B CG  1 
ATOM   2451 C  CD  . ARG B 1 37  ? -17.241 -35.380 8.606   1.00 40.81  ? 1507 ARG B CD  1 
ATOM   2452 N  NE  . ARG B 1 37  ? -17.103 -36.124 9.857   1.00 49.20  ? 1507 ARG B NE  1 
ATOM   2453 C  CZ  . ARG B 1 37  ? -15.957 -36.519 10.404  1.00 57.44  ? 1507 ARG B CZ  1 
ATOM   2454 N  NH1 . ARG B 1 37  ? -14.786 -36.239 9.819   1.00 39.33  ? 1507 ARG B NH1 1 
ATOM   2455 N  NH2 . ARG B 1 37  ? -15.993 -37.195 11.549  1.00 40.04  ? 1507 ARG B NH2 1 
ATOM   2456 N  N   . ASP B 1 38  ? -20.465 -34.369 11.872  1.00 42.17  ? 1508 ASP B N   1 
ATOM   2457 C  CA  . ASP B 1 38  ? -21.337 -35.441 12.305  1.00 43.22  ? 1508 ASP B CA  1 
ATOM   2458 C  C   . ASP B 1 38  ? -22.754 -34.897 12.524  1.00 55.97  ? 1508 ASP B C   1 
ATOM   2459 O  O   . ASP B 1 38  ? -23.732 -35.494 12.044  1.00 53.13  ? 1508 ASP B O   1 
ATOM   2460 C  CB  . ASP B 1 38  ? -20.749 -36.116 13.546  1.00 42.86  ? 1508 ASP B CB  1 
ATOM   2461 C  CG  . ASP B 1 38  ? -19.398 -36.820 13.253  1.00 62.38  ? 1508 ASP B CG  1 
ATOM   2462 O  OD1 . ASP B 1 38  ? -19.054 -37.046 12.063  1.00 42.00  ? 1508 ASP B OD1 1 
ATOM   2463 O  OD2 . ASP B 1 38  ? -18.666 -37.124 14.219  1.00 41.57  ? 1508 ASP B OD2 1 
ATOM   2464 N  N   . VAL B 1 39  ? -22.872 -33.691 13.120  1.00 47.98  ? 1509 VAL B N   1 
ATOM   2465 C  CA  . VAL B 1 39  ? -24.208 -33.150 13.359  1.00 45.22  ? 1509 VAL B CA  1 
ATOM   2466 C  C   . VAL B 1 39  ? -24.910 -32.955 12.027  1.00 50.72  ? 1509 VAL B C   1 
ATOM   2467 O  O   . VAL B 1 39  ? -26.024 -33.471 11.812  1.00 48.84  ? 1509 VAL B O   1 
ATOM   2468 C  CB  . VAL B 1 39  ? -24.141 -31.837 14.161  1.00 44.84  ? 1509 VAL B CB  1 
ATOM   2469 C  CG1 . VAL B 1 39  ? -25.486 -31.155 14.139  1.00 51.13  ? 1509 VAL B CG1 1 
ATOM   2470 C  CG2 . VAL B 1 39  ? -23.681 -32.080 15.595  1.00 44.41  ? 1509 VAL B CG2 1 
ATOM   2471 N  N   . LEU B 1 40  ? -24.185 -32.396 11.046  1.00 50.28  ? 1510 LEU B N   1 
ATOM   2472 C  CA  . LEU B 1 40  ? -24.832 -32.150 9.764   1.00 50.15  ? 1510 LEU B CA  1 
ATOM   2473 C  C   . LEU B 1 40  ? -25.178 -33.465 9.093   1.00 48.59  ? 1510 LEU B C   1 
ATOM   2474 O  O   . LEU B 1 40  ? -26.287 -33.616 8.558   1.00 48.27  ? 1510 LEU B O   1 
ATOM   2475 C  CB  . LEU B 1 40  ? -23.954 -31.279 8.863   1.00 45.32  ? 1510 LEU B CB  1 
ATOM   2476 C  CG  . LEU B 1 40  ? -23.951 -29.775 9.199   1.00 48.21  ? 1510 LEU B CG  1 
ATOM   2477 C  CD1 . LEU B 1 40  ? -22.976 -29.006 8.302   1.00 44.36  ? 1510 LEU B CD1 1 
ATOM   2478 C  CD2 . LEU B 1 40  ? -25.350 -29.171 9.104   1.00 46.54  ? 1510 LEU B CD2 1 
ATOM   2479 N  N   . PHE B 1 41  ? -24.286 -34.463 9.219   1.00 46.22  ? 1511 PHE B N   1 
ATOM   2480 C  CA  . PHE B 1 41  ? -24.558 -35.761 8.605   1.00 47.04  ? 1511 PHE B CA  1 
ATOM   2481 C  C   . PHE B 1 41  ? -25.839 -36.350 9.169   1.00 48.48  ? 1511 PHE B C   1 
ATOM   2482 O  O   . PHE B 1 41  ? -26.744 -36.728 8.412   1.00 49.78  ? 1511 PHE B O   1 
ATOM   2483 C  CB  . PHE B 1 41  ? -23.398 -36.733 8.821   1.00 46.20  ? 1511 PHE B CB  1 
ATOM   2484 C  CG  . PHE B 1 41  ? -23.690 -38.129 8.353   1.00 47.19  ? 1511 PHE B CG  1 
ATOM   2485 C  CD1 . PHE B 1 41  ? -23.901 -38.393 7.004   1.00 52.53  ? 1511 PHE B CD1 1 
ATOM   2486 C  CD2 . PHE B 1 41  ? -23.775 -39.172 9.256   1.00 54.54  ? 1511 PHE B CD2 1 
ATOM   2487 C  CE1 . PHE B 1 41  ? -24.188 -39.671 6.559   1.00 48.92  ? 1511 PHE B CE1 1 
ATOM   2488 C  CE2 . PHE B 1 41  ? -24.068 -40.468 8.827   1.00 58.77  ? 1511 PHE B CE2 1 
ATOM   2489 C  CZ  . PHE B 1 41  ? -24.273 -40.715 7.475   1.00 63.11  ? 1511 PHE B CZ  1 
ATOM   2490 N  N   . ASN B 1 42  ? -25.961 -36.366 10.505  1.00 48.38  ? 1512 ASN B N   1 
ATOM   2491 C  CA  . ASN B 1 42  ? -27.156 -36.956 11.088  1.00 49.93  ? 1512 ASN B CA  1 
ATOM   2492 C  C   . ASN B 1 42  ? -28.372 -36.175 10.636  1.00 51.10  ? 1512 ASN B C   1 
ATOM   2493 O  O   . ASN B 1 42  ? -29.375 -36.762 10.206  1.00 52.63  ? 1512 ASN B O   1 
ATOM   2494 C  CB  . ASN B 1 42  ? -27.066 -36.998 12.613  1.00 49.70  ? 1512 ASN B CB  1 
ATOM   2495 C  CG  . ASN B 1 42  ? -28.250 -37.727 13.246  1.00 85.47  ? 1512 ASN B CG  1 
ATOM   2496 O  OD1 . ASN B 1 42  ? -28.705 -38.762 12.744  1.00 88.79  ? 1512 ASN B OD1 1 
ATOM   2497 N  ND2 . ASN B 1 42  ? -28.763 -37.180 14.345  1.00 88.46  ? 1512 ASN B ND2 1 
ATOM   2498 N  N   . LEU B 1 43  ? -28.236 -34.846 10.570  1.00 50.50  ? 1513 LEU B N   1 
ATOM   2499 C  CA  . LEU B 1 43  ? -29.372 -34.046 10.140  1.00 68.26  ? 1513 LEU B CA  1 
ATOM   2500 C  C   . LEU B 1 43  ? -29.773 -34.436 8.727   1.00 52.61  ? 1513 LEU B C   1 
ATOM   2501 O  O   . LEU B 1 43  ? -30.946 -34.720 8.460   1.00 54.28  ? 1513 LEU B O   1 
ATOM   2502 C  CB  . LEU B 1 43  ? -29.029 -32.558 10.235  1.00 55.16  ? 1513 LEU B CB  1 
ATOM   2503 C  CG  . LEU B 1 43  ? -30.062 -31.488 9.898   1.00 69.56  ? 1513 LEU B CG  1 
ATOM   2504 C  CD1 . LEU B 1 43  ? -29.458 -30.194 10.340  1.00 80.19  ? 1513 LEU B CD1 1 
ATOM   2505 C  CD2 . LEU B 1 43  ? -30.384 -31.393 8.420   1.00 67.77  ? 1513 LEU B CD2 1 
ATOM   2506 N  N   . CYS B 1 44  ? -28.797 -34.557 7.831   1.00 51.62  ? 1514 CYS B N   1 
ATOM   2507 C  CA  . CYS B 1 44  ? -29.167 -34.807 6.446   1.00 56.02  ? 1514 CYS B CA  1 
ATOM   2508 C  C   . CYS B 1 44  ? -29.686 -36.213 6.266   1.00 53.66  ? 1514 CYS B C   1 
ATOM   2509 O  O   . CYS B 1 44  ? -30.384 -36.476 5.283   1.00 62.82  ? 1514 CYS B O   1 
ATOM   2510 C  CB  . CYS B 1 44  ? -27.972 -34.602 5.509   1.00 64.79  ? 1514 CYS B CB  1 
ATOM   2511 S  SG  . CYS B 1 44  ? -27.291 -32.926 5.515   1.00 63.45  ? 1514 CYS B SG  1 
ATOM   2512 N  N   . GLU B 1 45  ? -29.343 -37.119 7.187   1.00 53.31  ? 1515 GLU B N   1 
ATOM   2513 C  CA  . GLU B 1 45  ? -29.888 -38.470 7.132   1.00 63.42  ? 1515 GLU B CA  1 
ATOM   2514 C  C   . GLU B 1 45  ? -31.358 -38.486 7.510   1.00 76.63  ? 1515 GLU B C   1 
ATOM   2515 O  O   . GLU B 1 45  ? -32.100 -39.372 7.068   1.00 79.75  ? 1515 GLU B O   1 
ATOM   2516 C  CB  . GLU B 1 45  ? -29.093 -39.400 8.051   1.00 82.36  ? 1515 GLU B CB  1 
ATOM   2517 C  CG  . GLU B 1 45  ? -27.682 -39.688 7.575   1.00 83.38  ? 1515 GLU B CG  1 
ATOM   2518 C  CD  . GLU B 1 45  ? -27.638 -40.682 6.426   1.00 91.40  ? 1515 GLU B CD  1 
ATOM   2519 O  OE1 . GLU B 1 45  ? -27.435 -41.889 6.696   1.00 102.80 ? 1515 GLU B OE1 1 
ATOM   2520 O  OE2 . GLU B 1 45  ? -27.807 -40.257 5.256   1.00 84.27  ? 1515 GLU B OE2 1 
ATOM   2521 N  N   . ASN B 1 46  ? -31.793 -37.520 8.323   1.00 56.43  ? 1516 ASN B N   1 
ATOM   2522 C  CA  . ASN B 1 46  ? -33.166 -37.485 8.810   1.00 58.27  ? 1516 ASN B CA  1 
ATOM   2523 C  C   . ASN B 1 46  ? -34.101 -36.704 7.898   1.00 70.67  ? 1516 ASN B C   1 
ATOM   2524 O  O   . ASN B 1 46  ? -35.322 -36.875 7.997   1.00 86.65  ? 1516 ASN B O   1 
ATOM   2525 C  CB  . ASN B 1 46  ? -33.198 -36.930 10.237  1.00 65.90  ? 1516 ASN B CB  1 
ATOM   2526 C  CG  . ASN B 1 46  ? -32.498 -37.850 11.232  1.00 87.86  ? 1516 ASN B CG  1 
ATOM   2527 O  OD1 . ASN B 1 46  ? -32.371 -39.057 11.002  1.00 94.60  ? 1516 ASN B OD1 1 
ATOM   2528 N  ND2 . ASN B 1 46  ? -32.034 -37.279 12.340  1.00 98.82  ? 1516 ASN B ND2 1 
ATOM   2529 N  N   . LEU B 1 47  ? -33.573 -35.817 7.053   1.00 78.03  ? 1517 LEU B N   1 
ATOM   2530 C  CA  . LEU B 1 47  ? -34.431 -35.105 6.112   1.00 84.98  ? 1517 LEU B CA  1 
ATOM   2531 C  C   . LEU B 1 47  ? -35.110 -36.083 5.157   1.00 100.33 ? 1517 LEU B C   1 
ATOM   2532 O  O   . LEU B 1 47  ? -36.321 -35.993 4.912   1.00 112.04 ? 1517 LEU B O   1 
ATOM   2533 C  CB  . LEU B 1 47  ? -33.608 -34.070 5.340   1.00 79.50  ? 1517 LEU B CB  1 
ATOM   2534 C  CG  . LEU B 1 47  ? -32.842 -33.036 6.173   1.00 80.32  ? 1517 LEU B CG  1 
ATOM   2535 C  CD1 . LEU B 1 47  ? -31.910 -32.221 5.282   1.00 81.74  ? 1517 LEU B CD1 1 
ATOM   2536 C  CD2 . LEU B 1 47  ? -33.788 -32.130 6.941   1.00 73.44  ? 1517 LEU B CD2 1 
ATOM   2537 N  N   . VAL B 1 48  ? -34.338 -37.021 4.605   1.00 118.74 ? 1518 VAL B N   1 
ATOM   2538 C  CA  . VAL B 1 48  ? -34.834 -38.041 3.675   1.00 130.18 ? 1518 VAL B CA  1 
ATOM   2539 C  C   . VAL B 1 48  ? -35.805 -39.040 4.328   1.00 130.43 ? 1518 VAL B C   1 
ATOM   2540 O  O   . VAL B 1 48  ? -35.570 -39.569 5.423   1.00 121.62 ? 1518 VAL B O   1 
ATOM   2541 C  CB  . VAL B 1 48  ? -33.644 -38.782 2.989   1.00 130.90 ? 1518 VAL B CB  1 
ATOM   2542 C  CG1 . VAL B 1 48  ? -32.565 -37.786 2.581   1.00 122.97 ? 1518 VAL B CG1 1 
ATOM   2543 C  CG2 . VAL B 1 48  ? -33.056 -39.881 3.882   1.00 130.59 ? 1518 VAL B CG2 1 
ATOM   2544 N  N   . SER B 1 55  ? -35.800 -29.876 -3.376  1.00 113.92 ? 1525 SER B N   1 
ATOM   2545 C  CA  . SER B 1 55  ? -35.627 -29.508 -1.992  1.00 113.75 ? 1525 SER B CA  1 
ATOM   2546 C  C   . SER B 1 55  ? -34.452 -28.622 -1.827  1.00 114.13 ? 1525 SER B C   1 
ATOM   2547 O  O   . SER B 1 55  ? -33.355 -29.128 -1.613  1.00 109.54 ? 1525 SER B O   1 
ATOM   2548 C  CB  . SER B 1 55  ? -35.437 -30.729 -1.118  1.00 111.70 ? 1525 SER B CB  1 
ATOM   2549 O  OG  . SER B 1 55  ? -35.570 -30.329 0.250   1.00 111.29 ? 1525 SER B OG  1 
ATOM   2550 N  N   . PRO B 1 56  ? -34.650 -27.305 -1.932  1.00 114.03 ? 1526 PRO B N   1 
ATOM   2551 C  CA  . PRO B 1 56  ? -33.498 -26.381 -1.846  1.00 112.59 ? 1526 PRO B CA  1 
ATOM   2552 C  C   . PRO B 1 56  ? -32.829 -26.317 -0.478  1.00 110.54 ? 1526 PRO B C   1 
ATOM   2553 O  O   . PRO B 1 56  ? -31.612 -26.103 -0.404  1.00 106.91 ? 1526 PRO B O   1 
ATOM   2554 C  CB  . PRO B 1 56  ? -34.131 -25.037 -2.203  1.00 109.37 ? 1526 PRO B CB  1 
ATOM   2555 C  CG  . PRO B 1 56  ? -35.541 -25.163 -1.622  1.00 100.36 ? 1526 PRO B CG  1 
ATOM   2556 C  CD  . PRO B 1 56  ? -35.946 -26.603 -1.829  1.00 107.80 ? 1526 PRO B CD  1 
ATOM   2557 N  N   . ALA B 1 57  ? -33.583 -26.476 0.616   1.00 111.44 ? 1527 ALA B N   1 
ATOM   2558 C  CA  . ALA B 1 57  ? -32.968 -26.421 1.938   1.00 107.30 ? 1527 ALA B CA  1 
ATOM   2559 C  C   . ALA B 1 57  ? -32.191 -27.696 2.224   1.00 96.00  ? 1527 ALA B C   1 
ATOM   2560 O  O   . ALA B 1 57  ? -31.123 -27.647 2.843   1.00 96.19  ? 1527 ALA B O   1 
ATOM   2561 C  CB  . ALA B 1 57  ? -34.029 -26.157 3.009   1.00 108.62 ? 1527 ALA B CB  1 
ATOM   2562 N  N   . HIS B 1 58  ? -32.728 -28.841 1.794   1.00 80.28  ? 1528 HIS B N   1 
ATOM   2563 C  CA  . HIS B 1 58  ? -31.967 -30.082 1.824   1.00 89.30  ? 1528 HIS B CA  1 
ATOM   2564 C  C   . HIS B 1 58  ? -30.647 -29.922 1.079   1.00 84.35  ? 1528 HIS B C   1 
ATOM   2565 O  O   . HIS B 1 58  ? -29.600 -30.352 1.568   1.00 70.90  ? 1528 HIS B O   1 
ATOM   2566 C  CB  . HIS B 1 58  ? -32.798 -31.226 1.243   1.00 77.42  ? 1528 HIS B CB  1 
ATOM   2567 N  N   . GLU B 1 59  ? -30.675 -29.291 -0.108  1.00 85.13  ? 1529 GLU B N   1 
ATOM   2568 C  CA  . GLU B 1 59  ? -29.446 -29.161 -0.891  1.00 83.67  ? 1529 GLU B CA  1 
ATOM   2569 C  C   . GLU B 1 59  ? -28.448 -28.230 -0.209  1.00 76.92  ? 1529 GLU B C   1 
ATOM   2570 O  O   . GLU B 1 59  ? -27.239 -28.492 -0.234  1.00 71.13  ? 1529 GLU B O   1 
ATOM   2571 C  CB  . GLU B 1 59  ? -29.749 -28.656 -2.306  1.00 81.08  ? 1529 GLU B CB  1 
ATOM   2572 C  CG  . GLU B 1 59  ? -30.406 -29.668 -3.235  1.00 89.06  ? 1529 GLU B CG  1 
ATOM   2573 C  CD  . GLU B 1 59  ? -29.574 -30.927 -3.425  1.00 101.73 ? 1529 GLU B CD  1 
ATOM   2574 O  OE1 . GLU B 1 59  ? -28.327 -30.825 -3.456  1.00 106.74 ? 1529 GLU B OE1 1 
ATOM   2575 O  OE2 . GLU B 1 59  ? -30.164 -32.023 -3.557  1.00 104.09 ? 1529 GLU B OE2 1 
ATOM   2576 N  N   . GLU B 1 60  ? -28.928 -27.159 0.440   1.00 68.24  ? 1530 GLU B N   1 
ATOM   2577 C  CA  . GLU B 1 60  ? -27.991 -26.286 1.146   1.00 63.35  ? 1530 GLU B CA  1 
ATOM   2578 C  C   . GLU B 1 60  ? -27.421 -26.965 2.386   1.00 60.25  ? 1530 GLU B C   1 
ATOM   2579 O  O   . GLU B 1 60  ? -26.237 -26.779 2.698   1.00 60.87  ? 1530 GLU B O   1 
ATOM   2580 C  CB  . GLU B 1 60  ? -28.644 -24.949 1.523   1.00 69.22  ? 1530 GLU B CB  1 
ATOM   2581 C  CG  . GLU B 1 60  ? -27.660 -23.979 2.212   1.00 81.15  ? 1530 GLU B CG  1 
ATOM   2582 C  CD  . GLU B 1 60  ? -28.278 -22.637 2.631   1.00 87.18  ? 1530 GLU B CD  1 
ATOM   2583 O  OE1 . GLU B 1 60  ? -28.034 -21.620 1.936   1.00 72.22  ? 1530 GLU B OE1 1 
ATOM   2584 O  OE2 . GLU B 1 60  ? -28.988 -22.598 3.662   1.00 84.19  ? 1530 GLU B OE2 1 
ATOM   2585 N  N   . PHE B 1 61  ? -28.215 -27.800 3.072   1.00 52.05  ? 1531 PHE B N   1 
ATOM   2586 C  CA  . PHE B 1 61  ? -27.660 -28.548 4.200   1.00 63.53  ? 1531 PHE B CA  1 
ATOM   2587 C  C   . PHE B 1 61  ? -26.684 -29.624 3.726   1.00 61.87  ? 1531 PHE B C   1 
ATOM   2588 O  O   . PHE B 1 61  ? -25.673 -29.878 4.389   1.00 58.57  ? 1531 PHE B O   1 
ATOM   2589 C  CB  . PHE B 1 61  ? -28.777 -29.185 5.039   1.00 56.66  ? 1531 PHE B CB  1 
ATOM   2590 C  CG  . PHE B 1 61  ? -29.344 -28.273 6.113   1.00 63.73  ? 1531 PHE B CG  1 
ATOM   2591 C  CD1 . PHE B 1 61  ? -28.547 -27.794 7.137   1.00 76.74  ? 1531 PHE B CD1 1 
ATOM   2592 C  CD2 . PHE B 1 61  ? -30.679 -27.912 6.102   1.00 71.59  ? 1531 PHE B CD2 1 
ATOM   2593 C  CE1 . PHE B 1 61  ? -29.070 -26.952 8.127   1.00 72.39  ? 1531 PHE B CE1 1 
ATOM   2594 C  CE2 . PHE B 1 61  ? -31.202 -27.074 7.084   1.00 76.71  ? 1531 PHE B CE2 1 
ATOM   2595 C  CZ  . PHE B 1 61  ? -30.392 -26.596 8.094   1.00 63.40  ? 1531 PHE B CZ  1 
ATOM   2596 N  N   . LYS B 1 62  ? -26.950 -30.234 2.569   1.00 56.48  ? 1532 LYS B N   1 
ATOM   2597 C  CA  . LYS B 1 62  ? -26.006 -31.179 1.981   1.00 60.54  ? 1532 LYS B CA  1 
ATOM   2598 C  C   . LYS B 1 62  ? -24.692 -30.485 1.647   1.00 59.22  ? 1532 LYS B C   1 
ATOM   2599 O  O   . LYS B 1 62  ? -23.603 -31.004 1.937   1.00 51.13  ? 1532 LYS B O   1 
ATOM   2600 C  CB  . LYS B 1 62  ? -26.609 -31.818 0.723   1.00 57.63  ? 1532 LYS B CB  1 
ATOM   2601 C  CG  . LYS B 1 62  ? -27.698 -32.880 0.971   1.00 68.16  ? 1532 LYS B CG  1 
ATOM   2602 C  CD  . LYS B 1 62  ? -28.037 -33.598 -0.333  1.00 78.58  ? 1532 LYS B CD  1 
ATOM   2603 C  CE  . LYS B 1 62  ? -29.473 -33.323 -0.751  1.00 94.56  ? 1532 LYS B CE  1 
ATOM   2604 N  NZ  . LYS B 1 62  ? -29.899 -34.154 -1.915  1.00 99.39  ? 1532 LYS B NZ  1 
ATOM   2605 N  N   . THR B 1 63  ? -24.778 -29.294 1.043   1.00 49.39  ? 1533 THR B N   1 
ATOM   2606 C  CA  . THR B 1 63  ? -23.565 -28.552 0.722   1.00 56.04  ? 1533 THR B CA  1 
ATOM   2607 C  C   . THR B 1 63  ? -22.805 -28.199 1.989   1.00 48.40  ? 1533 THR B C   1 
ATOM   2608 O  O   . THR B 1 63  ? -21.578 -28.358 2.052   1.00 55.27  ? 1533 THR B O   1 
ATOM   2609 C  CB  . THR B 1 63  ? -23.907 -27.306 -0.096  1.00 57.64  ? 1533 THR B CB  1 
ATOM   2610 O  OG1 . THR B 1 63  ? -24.451 -27.708 -1.360  1.00 60.61  ? 1533 THR B OG1 1 
ATOM   2611 C  CG2 . THR B 1 63  ? -22.670 -26.472 -0.346  1.00 48.58  ? 1533 THR B CG2 1 
ATOM   2612 N  N   . MET B 1 64  ? -23.520 -27.765 3.029   1.00 49.39  ? 1534 MET B N   1 
ATOM   2613 C  CA  . MET B 1 64  ? -22.845 -27.471 4.286   1.00 48.96  ? 1534 MET B CA  1 
ATOM   2614 C  C   . MET B 1 64  ? -22.131 -28.704 4.822   1.00 59.32  ? 1534 MET B C   1 
ATOM   2615 O  O   . MET B 1 64  ? -20.991 -28.614 5.306   1.00 46.34  ? 1534 MET B O   1 
ATOM   2616 C  CB  . MET B 1 64  ? -23.846 -26.933 5.304   1.00 51.31  ? 1534 MET B CB  1 
ATOM   2617 C  CG  . MET B 1 64  ? -24.193 -25.454 5.084   1.00 59.55  ? 1534 MET B CG  1 
ATOM   2618 S  SD  . MET B 1 64  ? -25.728 -24.916 5.871   1.00 64.41  ? 1534 MET B SD  1 
ATOM   2619 C  CE  . MET B 1 64  ? -25.624 -25.557 7.527   1.00 65.58  ? 1534 MET B CE  1 
ATOM   2620 N  N   . LEU B 1 65  ? -22.770 -29.871 4.708   1.00 54.95  ? 1535 LEU B N   1 
ATOM   2621 C  CA  . LEU B 1 65  ? -22.133 -31.107 5.143   1.00 49.77  ? 1535 LEU B CA  1 
ATOM   2622 C  C   . LEU B 1 65  ? -20.830 -31.341 4.392   1.00 44.15  ? 1535 LEU B C   1 
ATOM   2623 O  O   . LEU B 1 65  ? -19.814 -31.697 4.991   1.00 43.99  ? 1535 LEU B O   1 
ATOM   2624 C  CB  . LEU B 1 65  ? -23.085 -32.292 4.946   1.00 50.02  ? 1535 LEU B CB  1 
ATOM   2625 C  CG  . LEU B 1 65  ? -22.489 -33.678 5.204   1.00 45.59  ? 1535 LEU B CG  1 
ATOM   2626 C  CD1 . LEU B 1 65  ? -21.985 -33.790 6.652   1.00 44.61  ? 1535 LEU B CD1 1 
ATOM   2627 C  CD2 . LEU B 1 65  ? -23.541 -34.774 4.861   1.00 46.97  ? 1535 LEU B CD2 1 
ATOM   2628 N  N   . LEU B 1 66  ? -20.857 -31.169 3.070   1.00 44.83  ? 1536 LEU B N   1 
ATOM   2629 C  CA  . LEU B 1 66  ? -19.658 -31.387 2.270   1.00 46.62  ? 1536 LEU B CA  1 
ATOM   2630 C  C   . LEU B 1 66  ? -18.530 -30.445 2.695   1.00 51.05  ? 1536 LEU B C   1 
ATOM   2631 O  O   . LEU B 1 66  ? -17.367 -30.858 2.811   1.00 47.64  ? 1536 LEU B O   1 
ATOM   2632 C  CB  . LEU B 1 66  ? -19.993 -31.209 0.790   1.00 45.51  ? 1536 LEU B CB  1 
ATOM   2633 C  CG  . LEU B 1 66  ? -18.811 -31.362 -0.167  1.00 54.96  ? 1536 LEU B CG  1 
ATOM   2634 C  CD1 . LEU B 1 66  ? -18.222 -32.783 -0.127  1.00 45.10  ? 1536 LEU B CD1 1 
ATOM   2635 C  CD2 . LEU B 1 66  ? -19.284 -31.002 -1.574  1.00 46.64  ? 1536 LEU B CD2 1 
ATOM   2636 N  N   . ILE B 1 67  ? -18.876 -29.175 2.942   1.00 43.32  ? 1537 ILE B N   1 
ATOM   2637 C  CA  . ILE B 1 67  ? -17.906 -28.179 3.380   1.00 42.44  ? 1537 ILE B CA  1 
ATOM   2638 C  C   . ILE B 1 67  ? -17.325 -28.587 4.722   1.00 49.39  ? 1537 ILE B C   1 
ATOM   2639 O  O   . ILE B 1 67  ? -16.126 -28.409 4.994   1.00 46.15  ? 1537 ILE B O   1 
ATOM   2640 C  CB  . ILE B 1 67  ? -18.571 -26.786 3.463   1.00 42.94  ? 1537 ILE B CB  1 
ATOM   2641 C  CG1 . ILE B 1 67  ? -18.749 -26.149 2.085   1.00 47.04  ? 1537 ILE B CG1 1 
ATOM   2642 C  CG2 . ILE B 1 67  ? -17.782 -25.838 4.396   1.00 42.02  ? 1537 ILE B CG2 1 
ATOM   2643 C  CD1 . ILE B 1 67  ? -19.801 -25.057 2.071   1.00 52.99  ? 1537 ILE B CD1 1 
ATOM   2644 N  N   . ALA B 1 68  ? -18.180 -29.081 5.609   1.00 42.78  ? 1538 ALA B N   1 
ATOM   2645 C  CA  . ALA B 1 68  ? -17.690 -29.509 6.911   1.00 47.97  ? 1538 ALA B CA  1 
ATOM   2646 C  C   . ALA B 1 68  ? -16.759 -30.712 6.773   1.00 48.56  ? 1538 ALA B C   1 
ATOM   2647 O  O   . ALA B 1 68  ? -15.778 -30.830 7.513   1.00 41.15  ? 1538 ALA B O   1 
ATOM   2648 C  CB  . ALA B 1 68  ? -18.858 -29.826 7.836   1.00 42.56  ? 1538 ALA B CB  1 
ATOM   2649 N  N   . HIS B 1 69  ? -17.058 -31.607 5.835   1.00 40.82  ? 1539 HIS B N   1 
ATOM   2650 C  CA  . HIS B 1 69  ? -16.183 -32.753 5.600   1.00 44.99  ? 1539 HIS B CA  1 
ATOM   2651 C  C   . HIS B 1 69  ? -14.824 -32.296 5.086   1.00 44.92  ? 1539 HIS B C   1 
ATOM   2652 O  O   . HIS B 1 69  ? -13.787 -32.800 5.524   1.00 40.70  ? 1539 HIS B O   1 
ATOM   2653 C  CB  . HIS B 1 69  ? -16.820 -33.720 4.609   1.00 41.64  ? 1539 HIS B CB  1 
ATOM   2654 C  CG  . HIS B 1 69  ? -15.832 -34.605 3.924   1.00 57.10  ? 1539 HIS B CG  1 
ATOM   2655 N  ND1 . HIS B 1 69  ? -15.162 -35.624 4.575   1.00 41.28  ? 1539 HIS B ND1 1 
ATOM   2656 C  CD2 . HIS B 1 69  ? -15.387 -34.615 2.645   1.00 42.12  ? 1539 HIS B CD2 1 
ATOM   2657 C  CE1 . HIS B 1 69  ? -14.362 -36.228 3.721   1.00 49.15  ? 1539 HIS B CE1 1 
ATOM   2658 N  NE2 . HIS B 1 69  ? -14.485 -35.640 2.544   1.00 51.62  ? 1539 HIS B NE2 1 
ATOM   2659 N  N   . TYR B 1 70  ? -14.818 -31.328 4.164   1.00 40.35  ? 1540 TYR B N   1 
ATOM   2660 C  CA  . TYR B 1 70  ? -13.553 -30.779 3.677   1.00 42.10  ? 1540 TYR B CA  1 
ATOM   2661 C  C   . TYR B 1 70  ? -12.729 -30.201 4.818   1.00 43.28  ? 1540 TYR B C   1 
ATOM   2662 O  O   . TYR B 1 70  ? -11.530 -30.464 4.926   1.00 45.56  ? 1540 TYR B O   1 
ATOM   2663 C  CB  . TYR B 1 70  ? -13.802 -29.699 2.641   1.00 40.62  ? 1540 TYR B CB  1 
ATOM   2664 C  CG  . TYR B 1 70  ? -14.219 -30.177 1.282   1.00 41.70  ? 1540 TYR B CG  1 
ATOM   2665 C  CD1 . TYR B 1 70  ? -13.804 -31.417 0.770   1.00 41.96  ? 1540 TYR B CD1 1 
ATOM   2666 C  CD2 . TYR B 1 70  ? -15.035 -29.381 0.494   1.00 42.60  ? 1540 TYR B CD2 1 
ATOM   2667 C  CE1 . TYR B 1 70  ? -14.196 -31.822 -0.504  1.00 43.09  ? 1540 TYR B CE1 1 
ATOM   2668 C  CE2 . TYR B 1 70  ? -15.428 -29.772 -0.758  1.00 47.52  ? 1540 TYR B CE2 1 
ATOM   2669 C  CZ  . TYR B 1 70  ? -15.021 -30.992 -1.254  1.00 48.40  ? 1540 TYR B CZ  1 
ATOM   2670 O  OH  . TYR B 1 70  ? -15.467 -31.327 -2.515  1.00 46.77  ? 1540 TYR B OH  1 
ATOM   2671 N  N   . TYR B 1 71  ? -13.353 -29.386 5.672   1.00 43.20  ? 1541 TYR B N   1 
ATOM   2672 C  CA  . TYR B 1 71  ? -12.612 -28.778 6.778   1.00 37.87  ? 1541 TYR B CA  1 
ATOM   2673 C  C   . TYR B 1 71  ? -12.082 -29.833 7.747   1.00 41.84  ? 1541 TYR B C   1 
ATOM   2674 O  O   . TYR B 1 71  ? -10.916 -29.777 8.175   1.00 43.81  ? 1541 TYR B O   1 
ATOM   2675 C  CB  . TYR B 1 71  ? -13.511 -27.785 7.517   1.00 41.12  ? 1541 TYR B CB  1 
ATOM   2676 C  CG  . TYR B 1 71  ? -13.537 -26.359 6.957   1.00 38.30  ? 1541 TYR B CG  1 
ATOM   2677 C  CD1 . TYR B 1 71  ? -12.390 -25.542 6.980   1.00 38.54  ? 1541 TYR B CD1 1 
ATOM   2678 C  CD2 . TYR B 1 71  ? -14.707 -25.822 6.452   1.00 39.17  ? 1541 TYR B CD2 1 
ATOM   2679 C  CE1 . TYR B 1 71  ? -12.436 -24.224 6.490   1.00 38.90  ? 1541 TYR B CE1 1 
ATOM   2680 C  CE2 . TYR B 1 71  ? -14.766 -24.516 5.982   1.00 39.65  ? 1541 TYR B CE2 1 
ATOM   2681 C  CZ  . TYR B 1 71  ? -13.634 -23.722 5.990   1.00 47.38  ? 1541 TYR B CZ  1 
ATOM   2682 O  OH  . TYR B 1 71  ? -13.715 -22.428 5.506   1.00 43.76  ? 1541 TYR B OH  1 
ATOM   2683 N  N   . ALA B 1 72  ? -12.917 -30.826 8.094   1.00 37.59  ? 1542 ALA B N   1 
ATOM   2684 C  CA  . ALA B 1 72  ? -12.443 -31.862 9.002   1.00 44.95  ? 1542 ALA B CA  1 
ATOM   2685 C  C   . ALA B 1 72  ? -11.288 -32.649 8.373   1.00 37.15  ? 1542 ALA B C   1 
ATOM   2686 O  O   . ALA B 1 72  ? -10.291 -32.956 9.039   1.00 36.93  ? 1542 ALA B O   1 
ATOM   2687 C  CB  . ALA B 1 72  ? -13.597 -32.790 9.391   1.00 37.79  ? 1542 ALA B CB  1 
ATOM   2688 N  N   . THR B 1 73  ? -11.407 -32.968 7.088   1.00 37.78  ? 1543 THR B N   1 
ATOM   2689 C  CA  . THR B 1 73  ? -10.345 -33.681 6.406   1.00 37.91  ? 1543 THR B CA  1 
ATOM   2690 C  C   . THR B 1 73  ? -9.070  -32.840 6.323   1.00 37.42  ? 1543 THR B C   1 
ATOM   2691 O  O   . THR B 1 73  ? -7.973  -33.388 6.397   1.00 37.30  ? 1543 THR B O   1 
ATOM   2692 C  CB  . THR B 1 73  ? -10.823 -34.115 5.010   1.00 40.69  ? 1543 THR B CB  1 
ATOM   2693 O  OG1 . THR B 1 73  ? -12.043 -34.876 5.119   1.00 40.05  ? 1543 THR B OG1 1 
ATOM   2694 C  CG2 . THR B 1 73  ? -9.744  -35.009 4.323   1.00 41.47  ? 1543 THR B CG2 1 
ATOM   2695 N  N   . ARG B 1 74  ? -9.206  -31.519 6.175   1.00 37.28  ? 1544 ARG B N   1 
ATOM   2696 C  CA  . ARG B 1 74  ? -8.050  -30.636 6.177   1.00 36.93  ? 1544 ARG B CA  1 
ATOM   2697 C  C   . ARG B 1 74  ? -7.336  -30.689 7.514   1.00 41.09  ? 1544 ARG B C   1 
ATOM   2698 O  O   . ARG B 1 74  ? -6.115  -30.825 7.557   1.00 40.69  ? 1544 ARG B O   1 
ATOM   2699 C  CB  . ARG B 1 74  ? -8.456  -29.192 5.850   1.00 42.34  ? 1544 ARG B CB  1 
ATOM   2700 C  CG  . ARG B 1 74  ? -7.256  -28.210 5.787   1.00 45.22  ? 1544 ARG B CG  1 
ATOM   2701 C  CD  . ARG B 1 74  ? -7.714  -26.740 5.570   1.00 37.13  ? 1544 ARG B CD  1 
ATOM   2702 N  NE  . ARG B 1 74  ? -8.353  -26.188 6.775   1.00 44.38  ? 1544 ARG B NE  1 
ATOM   2703 C  CZ  . ARG B 1 74  ? -8.890  -24.967 6.846   1.00 36.90  ? 1544 ARG B CZ  1 
ATOM   2704 N  NH1 . ARG B 1 74  ? -8.860  -24.153 5.787   1.00 37.61  ? 1544 ARG B NH1 1 
ATOM   2705 N  NH2 . ARG B 1 74  ? -9.419  -24.548 7.975   1.00 36.57  ? 1544 ARG B NH2 1 
ATOM   2706 N  N   . SER B 1 75  ? -8.065  -30.584 8.620   1.00 35.82  ? 1545 SER B N   1 
ATOM   2707 C  CA  . SER B 1 75  ? -7.370  -30.704 9.900   1.00 44.72  ? 1545 SER B CA  1 
ATOM   2708 C  C   . SER B 1 75  ? -6.704  -32.086 10.044  1.00 36.53  ? 1545 SER B C   1 
ATOM   2709 O  O   . SER B 1 75  ? -5.567  -32.191 10.538  1.00 50.91  ? 1545 SER B O   1 
ATOM   2710 C  CB  . SER B 1 75  ? -8.322  -30.411 11.056  1.00 35.01  ? 1545 SER B CB  1 
ATOM   2711 O  OG  . SER B 1 75  ? -8.672  -29.035 11.106  1.00 47.60  ? 1545 SER B OG  1 
ATOM   2712 N  N   . ALA B 1 76  ? -7.382  -33.151 9.576   1.00 42.44  ? 1546 ALA B N   1 
ATOM   2713 C  CA  . ALA B 1 76  ? -6.776  -34.485 9.557   1.00 49.51  ? 1546 ALA B CA  1 
ATOM   2714 C  C   . ALA B 1 76  ? -5.458  -34.484 8.793   1.00 50.17  ? 1546 ALA B C   1 
ATOM   2715 O  O   . ALA B 1 76  ? -4.447  -35.033 9.253   1.00 39.85  ? 1546 ALA B O   1 
ATOM   2716 C  CB  . ALA B 1 76  ? -7.741  -35.517 8.938   1.00 37.56  ? 1546 ALA B CB  1 
ATOM   2717 N  N   . ALA B 1 77  ? -5.484  -33.922 7.591   1.00 37.70  ? 1547 ALA B N   1 
ATOM   2718 C  CA  . ALA B 1 77  ? -4.296  -33.825 6.761   1.00 39.03  ? 1547 ALA B CA  1 
ATOM   2719 C  C   . ALA B 1 77  ? -3.207  -32.995 7.435   1.00 51.50  ? 1547 ALA B C   1 
ATOM   2720 O  O   . ALA B 1 77  ? -2.024  -33.336 7.357   1.00 48.81  ? 1547 ALA B O   1 
ATOM   2721 C  CB  . ALA B 1 77  ? -4.677  -33.232 5.407   1.00 38.79  ? 1547 ALA B CB  1 
ATOM   2722 N  N   . GLN B 1 78  ? -3.588  -31.907 8.108   1.00 47.96  ? 1548 GLN B N   1 
ATOM   2723 C  CA  . GLN B 1 78  ? -2.633  -31.057 8.814   1.00 48.77  ? 1548 GLN B CA  1 
ATOM   2724 C  C   . GLN B 1 78  ? -1.948  -31.783 9.955   1.00 39.91  ? 1548 GLN B C   1 
ATOM   2725 O  O   . GLN B 1 78  ? -0.952  -31.284 10.482  1.00 44.82  ? 1548 GLN B O   1 
ATOM   2726 C  CB  . GLN B 1 78  ? -3.336  -29.801 9.381   1.00 44.64  ? 1548 GLN B CB  1 
ATOM   2727 C  CG  . GLN B 1 78  ? -3.736  -28.801 8.334   1.00 36.76  ? 1548 GLN B CG  1 
ATOM   2728 C  CD  . GLN B 1 78  ? -4.739  -27.760 8.822   1.00 42.58  ? 1548 GLN B CD  1 
ATOM   2729 O  OE1 . GLN B 1 78  ? -5.462  -27.960 9.816   1.00 38.88  ? 1548 GLN B OE1 1 
ATOM   2730 N  NE2 . GLN B 1 78  ? -4.766  -26.625 8.133   1.00 44.30  ? 1548 GLN B NE2 1 
ATOM   2731 N  N   . SER B 1 79  ? -2.495  -32.910 10.398  1.00 35.26  ? 1549 SER B N   1 
ATOM   2732 C  CA  . SER B 1 79  ? -1.848  -33.608 11.500  1.00 44.59  ? 1549 SER B CA  1 
ATOM   2733 C  C   . SER B 1 79  ? -0.700  -34.531 11.073  1.00 50.14  ? 1549 SER B C   1 
ATOM   2734 O  O   . SER B 1 79  ? 0.011   -35.024 11.952  1.00 52.58  ? 1549 SER B O   1 
ATOM   2735 C  CB  . SER B 1 79  ? -2.871  -34.418 12.293  1.00 48.83  ? 1549 SER B CB  1 
ATOM   2736 O  OG  . SER B 1 79  ? -3.498  -35.344 11.436  1.00 61.01  ? 1549 SER B OG  1 
ATOM   2737 N  N   A VAL B 1 80  ? -0.497  -34.790 9.787   0.27 46.93  ? 1550 VAL B N   1 
ATOM   2738 N  N   B VAL B 1 80  ? -0.511  -34.772 9.766   0.73 45.43  ? 1550 VAL B N   1 
ATOM   2739 C  CA  A VAL B 1 80  ? 0.605   -35.656 9.372   0.27 48.04  ? 1550 VAL B CA  1 
ATOM   2740 C  CA  B VAL B 1 80  ? 0.503   -35.698 9.226   0.73 49.16  ? 1550 VAL B CA  1 
ATOM   2741 C  C   A VAL B 1 80  ? 1.313   -35.025 8.182   0.27 49.85  ? 1550 VAL B C   1 
ATOM   2742 C  C   B VAL B 1 80  ? 1.305   -34.976 8.140   0.73 51.03  ? 1550 VAL B C   1 
ATOM   2743 O  O   A VAL B 1 80  ? 0.677   -34.634 7.197   0.27 48.41  ? 1550 VAL B O   1 
ATOM   2744 O  O   B VAL B 1 80  ? 0.722   -34.482 7.164   0.73 43.03  ? 1550 VAL B O   1 
ATOM   2745 C  CB  A VAL B 1 80  ? 0.128   -37.086 9.058   0.27 48.44  ? 1550 VAL B CB  1 
ATOM   2746 C  CB  B VAL B 1 80  ? -0.136  -36.972 8.640   0.73 49.08  ? 1550 VAL B CB  1 
ATOM   2747 C  CG1 A VAL B 1 80  ? 0.075   -37.901 10.346  0.27 45.48  ? 1550 VAL B CG1 1 
ATOM   2748 C  CG1 B VAL B 1 80  ? 0.939   -37.970 8.218   0.73 43.24  ? 1550 VAL B CG1 1 
ATOM   2749 C  CG2 A VAL B 1 80  ? -1.231  -37.055 8.424   0.27 49.38  ? 1550 VAL B CG2 1 
ATOM   2750 C  CG2 B VAL B 1 80  ? -1.126  -37.619 9.628   0.73 48.39  ? 1550 VAL B CG2 1 
ATOM   2751 N  N   . LYS B 1 81  ? 2.640   -34.938 8.282   1.00 58.30  ? 1551 LYS B N   1 
ATOM   2752 C  CA  . LYS B 1 81  ? 3.429   -34.095 7.376   1.00 48.82  ? 1551 LYS B CA  1 
ATOM   2753 C  C   . LYS B 1 81  ? 3.279   -34.524 5.918   1.00 43.42  ? 1551 LYS B C   1 
ATOM   2754 O  O   . LYS B 1 81  ? 3.206   -33.678 5.012   1.00 39.47  ? 1551 LYS B O   1 
ATOM   2755 C  CB  . LYS B 1 81  ? 4.901   -34.097 7.797   1.00 69.50  ? 1551 LYS B CB  1 
ATOM   2756 N  N   . GLN B 1 82  ? 3.144   -35.822 5.667   1.00 39.75  ? 1552 GLN B N   1 
ATOM   2757 C  CA  . GLN B 1 82  ? 3.082   -36.185 4.261   1.00 44.29  ? 1552 GLN B CA  1 
ATOM   2758 C  C   . GLN B 1 82  ? 1.714   -35.905 3.644   1.00 41.85  ? 1552 GLN B C   1 
ATOM   2759 O  O   . GLN B 1 82  ? 1.556   -36.101 2.439   1.00 47.26  ? 1552 GLN B O   1 
ATOM   2760 C  CB  . GLN B 1 82  ? 3.503   -37.661 4.050   1.00 54.23  ? 1552 GLN B CB  1 
ATOM   2761 C  CG  . GLN B 1 82  ? 2.643   -38.711 4.705   1.00 76.08  ? 1552 GLN B CG  1 
ATOM   2762 C  CD  . GLN B 1 82  ? 3.131   -39.088 6.087   1.00 82.33  ? 1552 GLN B CD  1 
ATOM   2763 O  OE1 . GLN B 1 82  ? 3.751   -38.268 6.789   1.00 64.67  ? 1552 GLN B OE1 1 
ATOM   2764 N  NE2 . GLN B 1 82  ? 2.821   -40.329 6.509   1.00 69.63  ? 1552 GLN B NE2 1 
ATOM   2765 N  N   . LEU B 1 83  ? 0.743   -35.396 4.412   1.00 41.34  ? 1553 LEU B N   1 
ATOM   2766 C  CA  . LEU B 1 83  ? -0.537  -34.948 3.864   1.00 42.76  ? 1553 LEU B CA  1 
ATOM   2767 C  C   . LEU B 1 83  ? -0.625  -33.411 3.735   1.00 47.66  ? 1553 LEU B C   1 
ATOM   2768 O  O   . LEU B 1 83  ? -1.715  -32.868 3.476   1.00 43.29  ? 1553 LEU B O   1 
ATOM   2769 C  CB  . LEU B 1 83  ? -1.693  -35.510 4.719   1.00 40.14  ? 1553 LEU B CB  1 
ATOM   2770 C  CG  . LEU B 1 83  ? -1.860  -37.047 4.727   1.00 41.71  ? 1553 LEU B CG  1 
ATOM   2771 C  CD1 . LEU B 1 83  ? -3.027  -37.437 5.595   1.00 38.93  ? 1553 LEU B CD1 1 
ATOM   2772 C  CD2 . LEU B 1 83  ? -2.054  -37.616 3.328   1.00 40.46  ? 1553 LEU B CD2 1 
ATOM   2773 N  N   . GLU B 1 84  ? 0.503   -32.706 3.899   1.00 39.03  ? 1554 GLU B N   1 
ATOM   2774 C  CA  . GLU B 1 84  ? 0.495   -31.248 3.795   1.00 38.83  ? 1554 GLU B CA  1 
ATOM   2775 C  C   . GLU B 1 84  ? -0.159  -30.770 2.494   1.00 46.39  ? 1554 GLU B C   1 
ATOM   2776 O  O   . GLU B 1 84  ? -1.008  -29.857 2.504   1.00 41.52  ? 1554 GLU B O   1 
ATOM   2777 C  CB  . GLU B 1 84  ? 1.924   -30.698 3.900   1.00 49.00  ? 1554 GLU B CB  1 
ATOM   2778 C  CG  . GLU B 1 84  ? 1.962   -29.177 3.870   1.00 61.66  ? 1554 GLU B CG  1 
ATOM   2779 C  CD  . GLU B 1 84  ? 3.325   -28.583 4.226   1.00 69.97  ? 1554 GLU B CD  1 
ATOM   2780 O  OE1 . GLU B 1 84  ? 4.369   -29.232 3.956   1.00 64.53  ? 1554 GLU B OE1 1 
ATOM   2781 O  OE2 . GLU B 1 84  ? 3.335   -27.450 4.765   1.00 75.21  ? 1554 GLU B OE2 1 
ATOM   2782 N  N   . THR B 1 85  ? 0.220   -31.363 1.356   1.00 40.54  ? 1555 THR B N   1 
ATOM   2783 C  CA  . THR B 1 85  ? -0.357  -30.844 0.120   1.00 46.11  ? 1555 THR B CA  1 
ATOM   2784 C  C   . THR B 1 85  ? -1.836  -31.188 0.026   1.00 50.46  ? 1555 THR B C   1 
ATOM   2785 O  O   . THR B 1 85  ? -2.600  -30.405 -0.540  1.00 46.31  ? 1555 THR B O   1 
ATOM   2786 C  CB  . THR B 1 85  ? 0.391   -31.330 -1.127  1.00 51.01  ? 1555 THR B CB  1 
ATOM   2787 O  OG1 . THR B 1 85  ? -0.044  -32.641 -1.493  1.00 59.37  ? 1555 THR B OG1 1 
ATOM   2788 C  CG2 . THR B 1 85  ? 1.903   -31.339 -0.913  1.00 53.64  ? 1555 THR B CG2 1 
ATOM   2789 N  N   . VAL B 1 86  ? -2.271  -32.322 0.602   1.00 55.70  ? 1556 VAL B N   1 
ATOM   2790 C  CA  . VAL B 1 86  ? -3.708  -32.577 0.661   1.00 41.66  ? 1556 VAL B CA  1 
ATOM   2791 C  C   . VAL B 1 86  ? -4.403  -31.429 1.372   1.00 46.34  ? 1556 VAL B C   1 
ATOM   2792 O  O   . VAL B 1 86  ? -5.377  -30.855 0.861   1.00 40.94  ? 1556 VAL B O   1 
ATOM   2793 C  CB  . VAL B 1 86  ? -4.023  -33.916 1.344   1.00 43.16  ? 1556 VAL B CB  1 
ATOM   2794 C  CG1 . VAL B 1 86  ? -5.565  -33.985 1.661   1.00 40.36  ? 1556 VAL B CG1 1 
ATOM   2795 C  CG2 . VAL B 1 86  ? -3.619  -35.081 0.446   1.00 47.87  ? 1556 VAL B CG2 1 
ATOM   2796 N  N   . ALA B 1 87  ? -3.873  -31.044 2.543   1.00 38.92  ? 1557 ALA B N   1 
ATOM   2797 C  CA  . ALA B 1 87  ? -4.477  -29.952 3.291   1.00 38.28  ? 1557 ALA B CA  1 
ATOM   2798 C  C   . ALA B 1 87  ? -4.533  -28.701 2.435   1.00 51.02  ? 1557 ALA B C   1 
ATOM   2799 O  O   . ALA B 1 87  ? -5.575  -28.030 2.364   1.00 42.66  ? 1557 ALA B O   1 
ATOM   2800 C  CB  . ALA B 1 87  ? -3.701  -29.677 4.581   1.00 37.47  ? 1557 ALA B CB  1 
ATOM   2801 N  N   . ALA B 1 88  ? -3.455  -28.444 1.688   1.00 42.41  ? 1558 ALA B N   1 
ATOM   2802 C  CA  . ALA B 1 88  ? -3.405  -27.235 0.890   1.00 47.43  ? 1558 ALA B CA  1 
ATOM   2803 C  C   . ALA B 1 88  ? -4.488  -27.271 -0.164  1.00 42.14  ? 1558 ALA B C   1 
ATOM   2804 O  O   . ALA B 1 88  ? -5.223  -26.290 -0.342  1.00 43.10  ? 1558 ALA B O   1 
ATOM   2805 C  CB  . ALA B 1 88  ? -2.029  -27.085 0.256   1.00 42.63  ? 1558 ALA B CB  1 
ATOM   2806 N  N   . ARG B 1 89  ? -4.665  -28.429 -0.805  1.00 41.34  ? 1559 ARG B N   1 
ATOM   2807 C  CA  . ARG B 1 89  ? -5.675  -28.521 -1.852  1.00 49.19  ? 1559 ARG B CA  1 
ATOM   2808 C  C   . ARG B 1 89  ? -7.069  -28.301 -1.280  1.00 43.72  ? 1559 ARG B C   1 
ATOM   2809 O  O   . ARG B 1 89  ? -7.917  -27.667 -1.921  1.00 46.10  ? 1559 ARG B O   1 
ATOM   2810 C  CB  . ARG B 1 89  ? -5.582  -29.871 -2.569  1.00 42.86  ? 1559 ARG B CB  1 
ATOM   2811 C  CG  . ARG B 1 89  ? -4.472  -29.935 -3.628  1.00 49.95  ? 1559 ARG B CG  1 
ATOM   2812 C  CD  . ARG B 1 89  ? -4.271  -31.377 -4.125  1.00 47.38  ? 1559 ARG B CD  1 
ATOM   2813 N  NE  . ARG B 1 89  ? -2.888  -31.723 -4.445  1.00 78.06  ? 1559 ARG B NE  1 
ATOM   2814 C  CZ  . ARG B 1 89  ? -2.237  -31.321 -5.538  1.00 82.72  ? 1559 ARG B CZ  1 
ATOM   2815 N  NH1 . ARG B 1 89  ? -2.838  -30.530 -6.422  1.00 79.48  ? 1559 ARG B NH1 1 
ATOM   2816 N  NH2 . ARG B 1 89  ? -0.979  -31.708 -5.750  1.00 79.77  ? 1559 ARG B NH2 1 
ATOM   2817 N  N   . LEU B 1 90  ? -7.316  -28.766 -0.050  1.00 49.31  ? 1560 LEU B N   1 
ATOM   2818 C  CA  . LEU B 1 90  ? -8.658  -28.579 0.480   1.00 43.01  ? 1560 LEU B CA  1 
ATOM   2819 C  C   . LEU B 1 90  ? -8.924  -27.093 0.661   1.00 44.08  ? 1560 LEU B C   1 
ATOM   2820 O  O   . LEU B 1 90  ? -10.009 -26.601 0.308   1.00 41.12  ? 1560 LEU B O   1 
ATOM   2821 C  CB  . LEU B 1 90  ? -8.848  -29.375 1.771   1.00 39.64  ? 1560 LEU B CB  1 
ATOM   2822 C  CG  . LEU B 1 90  ? -8.944  -30.926 1.568   1.00 39.89  ? 1560 LEU B CG  1 
ATOM   2823 C  CD1 . LEU B 1 90  ? -8.638  -31.674 2.835   1.00 39.08  ? 1560 LEU B CD1 1 
ATOM   2824 C  CD2 . LEU B 1 90  ? -10.299 -31.331 1.045   1.00 44.83  ? 1560 LEU B CD2 1 
ATOM   2825 N  N   . SER B 1 91  ? -7.895  -26.331 1.065   1.00 42.16  ? 1561 SER B N   1 
ATOM   2826 C  CA  . SER B 1 91  ? -8.169  -24.915 1.287   1.00 52.98  ? 1561 SER B CA  1 
ATOM   2827 C  C   . SER B 1 91  ? -8.401  -24.228 -0.039  1.00 52.71  ? 1561 SER B C   1 
ATOM   2828 O  O   . SER B 1 91  ? -9.383  -23.476 -0.182  1.00 48.70  ? 1561 SER B O   1 
ATOM   2829 C  CB  . SER B 1 91  ? -7.007  -24.233 2.014   1.00 45.16  ? 1561 SER B CB  1 
ATOM   2830 O  OG  . SER B 1 91  ? -7.010  -24.525 3.397   1.00 45.70  ? 1561 SER B OG  1 
ATOM   2831 N  N   . VAL B 1 92  ? -7.702  -24.694 -1.071  1.00 42.13  ? 1562 VAL B N   1 
ATOM   2832 C  CA  . VAL B 1 92  ? -7.948  -24.160 -2.400  1.00 48.34  ? 1562 VAL B CA  1 
ATOM   2833 C  C   . VAL B 1 92  ? -9.351  -24.526 -2.850  1.00 51.69  ? 1562 VAL B C   1 
ATOM   2834 O  O   . VAL B 1 92  ? -10.132 -23.662 -3.272  1.00 49.54  ? 1562 VAL B O   1 
ATOM   2835 C  CB  . VAL B 1 92  ? -6.870  -24.653 -3.378  1.00 49.58  ? 1562 VAL B CB  1 
ATOM   2836 C  CG1 . VAL B 1 92  ? -7.234  -24.294 -4.796  1.00 45.68  ? 1562 VAL B CG1 1 
ATOM   2837 C  CG2 . VAL B 1 92  ? -5.525  -24.040 -2.987  1.00 44.89  ? 1562 VAL B CG2 1 
ATOM   2838 N  N   . SER B 1 93  ? -9.742  -25.781 -2.650  1.00 44.87  ? 1563 SER B N   1 
ATOM   2839 C  CA  . SER B 1 93  ? -11.034 -26.125 -3.200  1.00 44.36  ? 1563 SER B CA  1 
ATOM   2840 C  C   . SER B 1 93  ? -12.148 -25.469 -2.402  1.00 46.22  ? 1563 SER B C   1 
ATOM   2841 O  O   . SER B 1 93  ? -13.201 -25.172 -2.976  1.00 45.02  ? 1563 SER B O   1 
ATOM   2842 C  CB  . SER B 1 93  ? -11.232 -27.652 -3.232  1.00 52.10  ? 1563 SER B CB  1 
ATOM   2843 O  OG  . SER B 1 93  ? -10.071 -28.349 -3.705  1.00 50.57  ? 1563 SER B OG  1 
ATOM   2844 N  N   . LEU B 1 94  ? -11.898 -25.099 -1.139  1.00 43.01  ? 1564 LEU B N   1 
ATOM   2845 C  CA  . LEU B 1 94  ? -12.998 -24.489 -0.409  1.00 47.66  ? 1564 LEU B CA  1 
ATOM   2846 C  C   . LEU B 1 94  ? -13.380 -23.147 -1.008  1.00 58.36  ? 1564 LEU B C   1 
ATOM   2847 O  O   . LEU B 1 94  ? -14.495 -22.668 -0.749  1.00 48.86  ? 1564 LEU B O   1 
ATOM   2848 C  CB  . LEU B 1 94  ? -12.652 -24.344 1.074   1.00 44.53  ? 1564 LEU B CB  1 
ATOM   2849 C  CG  . LEU B 1 94  ? -13.023 -25.583 1.887   1.00 42.18  ? 1564 LEU B CG  1 
ATOM   2850 C  CD1 . LEU B 1 94  ? -12.253 -25.614 3.189   1.00 39.90  ? 1564 LEU B CD1 1 
ATOM   2851 C  CD2 . LEU B 1 94  ? -14.559 -25.660 2.140   1.00 41.55  ? 1564 LEU B CD2 1 
ATOM   2852 N  N   . LEU B 1 95  ? -12.500 -22.571 -1.848  1.00 44.49  ? 1565 LEU B N   1 
ATOM   2853 C  CA  . LEU B 1 95  ? -12.802 -21.296 -2.488  1.00 57.80  ? 1565 LEU B CA  1 
ATOM   2854 C  C   . LEU B 1 95  ? -14.048 -21.395 -3.354  1.00 65.30  ? 1565 LEU B C   1 
ATOM   2855 O  O   . LEU B 1 95  ? -14.772 -20.403 -3.505  1.00 68.08  ? 1565 LEU B O   1 
ATOM   2856 C  CB  . LEU B 1 95  ? -11.607 -20.819 -3.318  1.00 47.08  ? 1565 LEU B CB  1 
ATOM   2857 C  CG  . LEU B 1 95  ? -10.320 -20.472 -2.557  1.00 49.89  ? 1565 LEU B CG  1 
ATOM   2858 C  CD1 . LEU B 1 95  ? -9.166  -20.222 -3.547  1.00 46.10  ? 1565 LEU B CD1 1 
ATOM   2859 C  CD2 . LEU B 1 95  ? -10.517 -19.269 -1.598  1.00 45.02  ? 1565 LEU B CD2 1 
ATOM   2860 N  N   . ARG B 1 96  ? -14.349 -22.585 -3.888  1.00 54.28  ? 1566 ARG B N   1 
ATOM   2861 C  CA  . ARG B 1 96  ? -15.546 -22.678 -4.714  1.00 48.35  ? 1566 ARG B CA  1 
ATOM   2862 C  C   . ARG B 1 96  ? -16.817 -22.606 -3.887  1.00 55.11  ? 1566 ARG B C   1 
ATOM   2863 O  O   . ARG B 1 96  ? -17.903 -22.489 -4.461  1.00 59.34  ? 1566 ARG B O   1 
ATOM   2864 C  CB  . ARG B 1 96  ? -15.540 -23.954 -5.551  1.00 51.16  ? 1566 ARG B CB  1 
ATOM   2865 C  CG  . ARG B 1 96  ? -15.965 -25.217 -4.786  1.00 47.89  ? 1566 ARG B CG  1 
ATOM   2866 C  CD  . ARG B 1 96  ? -15.992 -26.415 -5.735  1.00 63.55  ? 1566 ARG B CD  1 
ATOM   2867 N  NE  . ARG B 1 96  ? -14.662 -26.710 -6.259  1.00 63.77  ? 1566 ARG B NE  1 
ATOM   2868 C  CZ  . ARG B 1 96  ? -13.878 -27.692 -5.819  1.00 63.52  ? 1566 ARG B CZ  1 
ATOM   2869 N  NH1 . ARG B 1 96  ? -14.293 -28.501 -4.838  1.00 48.96  ? 1566 ARG B NH1 1 
ATOM   2870 N  NH2 . ARG B 1 96  ? -12.672 -27.856 -6.361  1.00 49.11  ? 1566 ARG B NH2 1 
ATOM   2871 N  N   . HIS B 1 97  ? -16.708 -22.697 -2.563  1.00 55.11  ? 1567 HIS B N   1 
ATOM   2872 C  CA  . HIS B 1 97  ? -17.848 -22.634 -1.659  1.00 59.55  ? 1567 HIS B CA  1 
ATOM   2873 C  C   . HIS B 1 97  ? -17.934 -21.303 -0.924  1.00 59.54  ? 1567 HIS B C   1 
ATOM   2874 O  O   . HIS B 1 97  ? -18.492 -21.253 0.177   1.00 47.80  ? 1567 HIS B O   1 
ATOM   2875 C  CB  . HIS B 1 97  ? -17.793 -23.787 -0.658  1.00 46.07  ? 1567 HIS B CB  1 
ATOM   2876 C  CG  . HIS B 1 97  ? -17.987 -25.119 -1.291  1.00 46.02  ? 1567 HIS B CG  1 
ATOM   2877 N  ND1 . HIS B 1 97  ? -19.213 -25.545 -1.755  1.00 48.04  ? 1567 HIS B ND1 1 
ATOM   2878 C  CD2 . HIS B 1 97  ? -17.103 -26.110 -1.584  1.00 51.62  ? 1567 HIS B CD2 1 
ATOM   2879 C  CE1 . HIS B 1 97  ? -19.082 -26.752 -2.286  1.00 53.43  ? 1567 HIS B CE1 1 
ATOM   2880 N  NE2 . HIS B 1 97  ? -17.810 -27.115 -2.200  1.00 46.30  ? 1567 HIS B NE2 1 
ATOM   2881 N  N   . THR B 1 98  ? -17.350 -20.233 -1.480  1.00 47.43  ? 1568 THR B N   1 
ATOM   2882 C  CA  . THR B 1 98  ? -17.339 -18.952 -0.783  1.00 51.54  ? 1568 THR B CA  1 
ATOM   2883 C  C   . THR B 1 98  ? -18.715 -18.285 -0.727  1.00 62.64  ? 1568 THR B C   1 
ATOM   2884 O  O   . THR B 1 98  ? -18.856 -17.264 -0.045  1.00 65.25  ? 1568 THR B O   1 
ATOM   2885 C  CB  . THR B 1 98  ? -16.317 -17.993 -1.416  1.00 50.68  ? 1568 THR B CB  1 
ATOM   2886 O  OG1 . THR B 1 98  ? -16.353 -18.080 -2.847  1.00 57.86  ? 1568 THR B OG1 1 
ATOM   2887 C  CG2 . THR B 1 98  ? -14.941 -18.323 -0.938  1.00 46.93  ? 1568 THR B CG2 1 
ATOM   2888 N  N   . GLN B 1 99  ? -19.734 -18.845 -1.382  1.00 59.63  ? 1569 GLN B N   1 
ATOM   2889 C  CA  . GLN B 1 99  ? -21.092 -18.397 -1.114  1.00 67.39  ? 1569 GLN B CA  1 
ATOM   2890 C  C   . GLN B 1 99  ? -21.554 -18.745 0.293   1.00 71.86  ? 1569 GLN B C   1 
ATOM   2891 O  O   . GLN B 1 99  ? -22.553 -18.176 0.745   1.00 67.45  ? 1569 GLN B O   1 
ATOM   2892 C  CB  . GLN B 1 99  ? -22.068 -19.007 -2.125  1.00 66.40  ? 1569 GLN B CB  1 
ATOM   2893 C  CG  . GLN B 1 99  ? -22.432 -18.090 -3.281  1.00 90.56  ? 1569 GLN B CG  1 
ATOM   2894 C  CD  . GLN B 1 99  ? -22.680 -18.848 -4.579  1.00 97.11  ? 1569 GLN B CD  1 
ATOM   2895 O  OE1 . GLN B 1 99  ? -22.442 -20.063 -4.670  1.00 96.60  ? 1569 GLN B OE1 1 
ATOM   2896 N  NE2 . GLN B 1 99  ? -23.179 -18.134 -5.590  1.00 93.43  ? 1569 GLN B NE2 1 
ATOM   2897 N  N   . LEU B 1 100 ? -20.846 -19.630 1.004   1.00 52.04  ? 1570 LEU B N   1 
ATOM   2898 C  CA  . LEU B 1 100 ? -21.247 -20.028 2.347   1.00 50.56  ? 1570 LEU B CA  1 
ATOM   2899 C  C   . LEU B 1 100 ? -20.161 -19.793 3.384   1.00 61.68  ? 1570 LEU B C   1 
ATOM   2900 O  O   . LEU B 1 100 ? -20.347 -20.167 4.550   1.00 55.61  ? 1570 LEU B O   1 
ATOM   2901 C  CB  . LEU B 1 100 ? -21.669 -21.506 2.365   1.00 51.57  ? 1570 LEU B CB  1 
ATOM   2902 C  CG  . LEU B 1 100 ? -23.011 -21.864 1.696   1.00 61.42  ? 1570 LEU B CG  1 
ATOM   2903 C  CD1 . LEU B 1 100 ? -23.180 -23.356 1.578   1.00 48.47  ? 1570 LEU B CD1 1 
ATOM   2904 C  CD2 . LEU B 1 100 ? -24.219 -21.273 2.434   1.00 55.62  ? 1570 LEU B CD2 1 
ATOM   2905 N  N   . LEU B 1 101 ? -19.042 -19.181 2.997   1.00 58.38  ? 1571 LEU B N   1 
ATOM   2906 C  CA  . LEU B 1 101 ? -17.896 -18.957 3.863   1.00 49.47  ? 1571 LEU B CA  1 
ATOM   2907 C  C   . LEU B 1 101 ? -17.527 -17.486 3.850   1.00 54.10  ? 1571 LEU B C   1 
ATOM   2908 O  O   . LEU B 1 101 ? -17.731 -16.803 2.842   1.00 59.95  ? 1571 LEU B O   1 
ATOM   2909 C  CB  . LEU B 1 101 ? -16.676 -19.764 3.405   1.00 62.78  ? 1571 LEU B CB  1 
ATOM   2910 C  CG  . LEU B 1 101 ? -16.824 -21.218 2.997   1.00 50.68  ? 1571 LEU B CG  1 
ATOM   2911 C  CD1 . LEU B 1 101 ? -15.481 -21.690 2.433   1.00 52.26  ? 1571 LEU B CD1 1 
ATOM   2912 C  CD2 . LEU B 1 101 ? -17.240 -22.052 4.192   1.00 48.73  ? 1571 LEU B CD2 1 
ATOM   2913 N  N   . PRO B 1 102 ? -16.995 -16.965 4.960   1.00 45.09  ? 1572 PRO B N   1 
ATOM   2914 C  CA  . PRO B 1 102 ? -16.455 -15.601 4.927   1.00 58.32  ? 1572 PRO B CA  1 
ATOM   2915 C  C   . PRO B 1 102 ? -15.322 -15.563 3.919   1.00 52.73  ? 1572 PRO B C   1 
ATOM   2916 O  O   . PRO B 1 102 ? -14.308 -16.239 4.102   1.00 45.33  ? 1572 PRO B O   1 
ATOM   2917 C  CB  . PRO B 1 102 ? -15.974 -15.353 6.364   1.00 56.69  ? 1572 PRO B CB  1 
ATOM   2918 C  CG  . PRO B 1 102 ? -16.224 -16.643 7.132   1.00 51.65  ? 1572 PRO B CG  1 
ATOM   2919 C  CD  . PRO B 1 102 ? -16.569 -17.714 6.157   1.00 51.80  ? 1572 PRO B CD  1 
ATOM   2920 N  N   . VAL B 1 103 ? -15.489 -14.814 2.833   1.00 48.85  ? 1573 VAL B N   1 
ATOM   2921 C  CA  . VAL B 1 103 ? -14.611 -15.032 1.694   1.00 59.52  ? 1573 VAL B CA  1 
ATOM   2922 C  C   . VAL B 1 103 ? -13.203 -14.469 1.934   1.00 51.58  ? 1573 VAL B C   1 
ATOM   2923 O  O   . VAL B 1 103 ? -12.230 -14.962 1.352   1.00 56.59  ? 1573 VAL B O   1 
ATOM   2924 C  CB  . VAL B 1 103 ? -15.305 -14.440 0.454   1.00 48.11  ? 1573 VAL B CB  1 
ATOM   2925 C  CG1 . VAL B 1 103 ? -15.453 -12.926 0.624   1.00 54.48  ? 1573 VAL B CG1 1 
ATOM   2926 C  CG2 . VAL B 1 103 ? -14.546 -14.783 -0.805  1.00 58.25  ? 1573 VAL B CG2 1 
ATOM   2927 N  N   . ASP B 1 104 ? -13.054 -13.492 2.835   1.00 61.71  ? 1574 ASP B N   1 
ATOM   2928 C  CA  . ASP B 1 104 ? -11.718 -13.026 3.191   1.00 58.85  ? 1574 ASP B CA  1 
ATOM   2929 C  C   . ASP B 1 104 ? -10.927 -14.115 3.916   1.00 57.22  ? 1574 ASP B C   1 
ATOM   2930 O  O   . ASP B 1 104 ? -9.771  -14.388 3.570   1.00 55.59  ? 1574 ASP B O   1 
ATOM   2931 C  CB  . ASP B 1 104 ? -11.810 -11.750 4.038   1.00 62.23  ? 1574 ASP B CB  1 
ATOM   2932 C  CG  . ASP B 1 104 ? -12.586 -11.953 5.328   1.00 69.17  ? 1574 ASP B CG  1 
ATOM   2933 O  OD1 . ASP B 1 104 ? -13.619 -12.663 5.305   1.00 60.60  ? 1574 ASP B OD1 1 
ATOM   2934 O  OD2 . ASP B 1 104 ? -12.161 -11.393 6.364   1.00 60.58  ? 1574 ASP B OD2 1 
ATOM   2935 N  N   . LYS B 1 105 ? -11.531 -14.753 4.926   1.00 55.43  ? 1575 LYS B N   1 
ATOM   2936 C  CA  . LYS B 1 105 ? -10.870 -15.879 5.591   1.00 44.47  ? 1575 LYS B CA  1 
ATOM   2937 C  C   . LYS B 1 105 ? -10.478 -16.946 4.590   1.00 42.32  ? 1575 LYS B C   1 
ATOM   2938 O  O   . LYS B 1 105 ? -9.363  -17.483 4.641   1.00 45.20  ? 1575 LYS B O   1 
ATOM   2939 C  CB  . LYS B 1 105 ? -11.768 -16.500 6.662   1.00 42.69  ? 1575 LYS B CB  1 
ATOM   2940 C  CG  . LYS B 1 105 ? -11.082 -17.595 7.476   1.00 46.30  ? 1575 LYS B CG  1 
ATOM   2941 C  CD  . LYS B 1 105 ? -12.068 -18.616 8.091   1.00 50.36  ? 1575 LYS B CD  1 
ATOM   2942 C  CE  . LYS B 1 105 ? -12.398 -19.769 7.123   1.00 56.26  ? 1575 LYS B CE  1 
ATOM   2943 N  NZ  . LYS B 1 105 ? -13.176 -20.897 7.750   1.00 39.03  ? 1575 LYS B NZ  1 
ATOM   2944 N  N   . ALA B 1 106 ? -11.398 -17.291 3.683   1.00 46.42  ? 1576 ALA B N   1 
ATOM   2945 C  CA  . ALA B 1 106 ? -11.133 -18.395 2.758   1.00 52.18  ? 1576 ALA B CA  1 
ATOM   2946 C  C   . ALA B 1 106 ? -9.938  -18.091 1.868   1.00 46.49  ? 1576 ALA B C   1 
ATOM   2947 O  O   . ALA B 1 106 ? -9.082  -18.954 1.636   1.00 45.33  ? 1576 ALA B O   1 
ATOM   2948 C  CB  . ALA B 1 106 ? -12.369 -18.679 1.907   1.00 46.81  ? 1576 ALA B CB  1 
ATOM   2949 N  N   . PHE B 1 107 ? -9.854  -16.862 1.360   1.00 49.27  ? 1577 PHE B N   1 
ATOM   2950 C  CA  . PHE B 1 107 ? -8.720  -16.558 0.500   1.00 54.57  ? 1577 PHE B CA  1 
ATOM   2951 C  C   . PHE B 1 107 ? -7.441  -16.450 1.306   1.00 52.31  ? 1577 PHE B C   1 
ATOM   2952 O  O   . PHE B 1 107 ? -6.379  -16.869 0.839   1.00 43.52  ? 1577 PHE B O   1 
ATOM   2953 C  CB  . PHE B 1 107 ? -8.979  -15.291 -0.302  1.00 55.88  ? 1577 PHE B CB  1 
ATOM   2954 C  CG  . PHE B 1 107 ? -9.705  -15.551 -1.577  1.00 49.94  ? 1577 PHE B CG  1 
ATOM   2955 C  CD1 . PHE B 1 107 ? -9.037  -16.094 -2.663  1.00 52.24  ? 1577 PHE B CD1 1 
ATOM   2956 C  CD2 . PHE B 1 107 ? -11.061 -15.294 -1.681  1.00 47.58  ? 1577 PHE B CD2 1 
ATOM   2957 C  CE1 . PHE B 1 107 ? -9.705  -16.359 -3.839  1.00 52.80  ? 1577 PHE B CE1 1 
ATOM   2958 C  CE2 . PHE B 1 107 ? -11.737 -15.541 -2.860  1.00 48.72  ? 1577 PHE B CE2 1 
ATOM   2959 C  CZ  . PHE B 1 107 ? -11.061 -16.078 -3.940  1.00 51.27  ? 1577 PHE B CZ  1 
ATOM   2960 N  N   . TYR B 1 108 ? -7.516  -15.902 2.521   1.00 48.77  ? 1578 TYR B N   1 
ATOM   2961 C  CA  . TYR B 1 108 ? -6.338  -15.900 3.377   1.00 48.41  ? 1578 TYR B CA  1 
ATOM   2962 C  C   . TYR B 1 108 ? -5.809  -17.317 3.550   1.00 54.46  ? 1578 TYR B C   1 
ATOM   2963 O  O   . TYR B 1 108 ? -4.612  -17.575 3.374   1.00 47.57  ? 1578 TYR B O   1 
ATOM   2964 C  CB  . TYR B 1 108 ? -6.663  -15.272 4.735   1.00 42.35  ? 1578 TYR B CB  1 
ATOM   2965 C  CG  . TYR B 1 108 ? -5.507  -15.292 5.716   1.00 47.25  ? 1578 TYR B CG  1 
ATOM   2966 C  CD1 . TYR B 1 108 ? -4.393  -14.447 5.551   1.00 51.58  ? 1578 TYR B CD1 1 
ATOM   2967 C  CD2 . TYR B 1 108 ? -5.517  -16.164 6.806   1.00 52.49  ? 1578 TYR B CD2 1 
ATOM   2968 C  CE1 . TYR B 1 108 ? -3.314  -14.484 6.455   1.00 49.10  ? 1578 TYR B CE1 1 
ATOM   2969 C  CE2 . TYR B 1 108 ? -4.447  -16.214 7.712   1.00 54.40  ? 1578 TYR B CE2 1 
ATOM   2970 C  CZ  . TYR B 1 108 ? -3.357  -15.370 7.535   1.00 59.65  ? 1578 TYR B CZ  1 
ATOM   2971 O  OH  . TYR B 1 108 ? -2.328  -15.435 8.449   1.00 54.24  ? 1578 TYR B OH  1 
ATOM   2972 N  N   . GLU B 1 109 ? -6.702  -18.253 3.879   1.00 47.70  ? 1579 GLU B N   1 
ATOM   2973 C  CA  . GLU B 1 109 ? -6.267  -19.605 4.208   1.00 50.32  ? 1579 GLU B CA  1 
ATOM   2974 C  C   . GLU B 1 109 ? -5.693  -20.304 2.989   1.00 40.12  ? 1579 GLU B C   1 
ATOM   2975 O  O   . GLU B 1 109 ? -4.626  -20.923 3.057   1.00 43.54  ? 1579 GLU B O   1 
ATOM   2976 C  CB  . GLU B 1 109 ? -7.438  -20.411 4.790   1.00 43.22  ? 1579 GLU B CB  1 
ATOM   2977 C  CG  . GLU B 1 109 ? -7.826  -19.961 6.172   1.00 47.93  ? 1579 GLU B CG  1 
ATOM   2978 C  CD  . GLU B 1 109 ? -8.934  -20.795 6.808   1.00 47.84  ? 1579 GLU B CD  1 
ATOM   2979 O  OE1 . GLU B 1 109 ? -9.564  -21.636 6.122   1.00 49.15  ? 1579 GLU B OE1 1 
ATOM   2980 O  OE2 . GLU B 1 109 ? -9.173  -20.588 8.014   1.00 46.54  ? 1579 GLU B OE2 1 
ATOM   2981 N  N   . ALA B 1 110 ? -6.389  -20.215 1.863   1.00 41.04  ? 1580 ALA B N   1 
ATOM   2982 C  CA  . ALA B 1 110 ? -5.856  -20.787 0.638   1.00 41.74  ? 1580 ALA B CA  1 
ATOM   2983 C  C   . ALA B 1 110 ? -4.497  -20.174 0.285   1.00 50.92  ? 1580 ALA B C   1 
ATOM   2984 O  O   . ALA B 1 110 ? -3.551  -20.894 -0.060  1.00 48.21  ? 1580 ALA B O   1 
ATOM   2985 C  CB  . ALA B 1 110 ? -6.871  -20.585 -0.491  1.00 44.79  ? 1580 ALA B CB  1 
ATOM   2986 N  N   . GLY B 1 111 ? -4.369  -18.847 0.395   1.00 59.87  ? 1581 GLY B N   1 
ATOM   2987 C  CA  . GLY B 1 111 ? -3.124  -18.198 0.009   1.00 56.84  ? 1581 GLY B CA  1 
ATOM   2988 C  C   . GLY B 1 111 ? -1.952  -18.598 0.885   1.00 50.81  ? 1581 GLY B C   1 
ATOM   2989 O  O   . GLY B 1 111 ? -0.856  -18.875 0.387   1.00 44.62  ? 1581 GLY B O   1 
ATOM   2990 N  N   . ILE B 1 112 ? -2.169  -18.648 2.200   1.00 58.02  ? 1582 ILE B N   1 
ATOM   2991 C  CA  . ILE B 1 112 ? -1.101  -19.050 3.107   1.00 45.13  ? 1582 ILE B CA  1 
ATOM   2992 C  C   . ILE B 1 112 ? -0.705  -20.502 2.864   1.00 62.45  ? 1582 ILE B C   1 
ATOM   2993 O  O   . ILE B 1 112 ? 0.487   -20.830 2.831   1.00 51.40  ? 1582 ILE B O   1 
ATOM   2994 C  CB  . ILE B 1 112 ? -1.524  -18.805 4.564   1.00 50.09  ? 1582 ILE B CB  1 
ATOM   2995 C  CG1 . ILE B 1 112 ? -1.679  -17.302 4.805   1.00 71.49  ? 1582 ILE B CG1 1 
ATOM   2996 C  CG2 . ILE B 1 112 ? -0.479  -19.341 5.506   1.00 58.55  ? 1582 ILE B CG2 1 
ATOM   2997 C  CD1 . ILE B 1 112 ? -0.363  -16.574 5.020   1.00 57.09  ? 1582 ILE B CD1 1 
ATOM   2998 N  N   . ALA B 1 113 ? -1.692  -21.402 2.706   1.00 44.66  ? 1583 ALA B N   1 
ATOM   2999 C  CA  . ALA B 1 113 ? -1.349  -22.804 2.484   1.00 53.02  ? 1583 ALA B CA  1 
ATOM   3000 C  C   . ALA B 1 113 ? -0.570  -22.973 1.187   1.00 46.70  ? 1583 ALA B C   1 
ATOM   3001 O  O   . ALA B 1 113 ? 0.406   -23.740 1.127   1.00 47.34  ? 1583 ALA B O   1 
ATOM   3002 C  CB  . ALA B 1 113 ? -2.617  -23.679 2.485   1.00 39.51  ? 1583 ALA B CB  1 
ATOM   3003 N  N   . ALA B 1 114 ? -1.012  -22.288 0.128   1.00 47.90  ? 1584 ALA B N   1 
ATOM   3004 C  CA  . ALA B 1 114 ? -0.290  -22.334 -1.136  1.00 54.46  ? 1584 ALA B CA  1 
ATOM   3005 C  C   . ALA B 1 114 ? 1.146   -21.871 -0.951  1.00 57.95  ? 1584 ALA B C   1 
ATOM   3006 O  O   . ALA B 1 114 ? 2.086   -22.561 -1.353  1.00 48.85  ? 1584 ALA B O   1 
ATOM   3007 C  CB  . ALA B 1 114 ? -0.999  -21.471 -2.181  1.00 56.00  ? 1584 ALA B CB  1 
ATOM   3008 N  N   . LYS B 1 115 ? 1.330   -20.719 -0.297  1.00 56.86  ? 1585 LYS B N   1 
ATOM   3009 C  CA  . LYS B 1 115 ? 2.676   -20.203 -0.087  1.00 69.77  ? 1585 LYS B CA  1 
ATOM   3010 C  C   . LYS B 1 115 ? 3.524   -21.220 0.659   1.00 71.03  ? 1585 LYS B C   1 
ATOM   3011 O  O   . LYS B 1 115 ? 4.690   -21.437 0.315   1.00 64.99  ? 1585 LYS B O   1 
ATOM   3012 C  CB  . LYS B 1 115 ? 2.619   -18.873 0.674   1.00 72.34  ? 1585 LYS B CB  1 
ATOM   3013 C  CG  . LYS B 1 115 ? 3.931   -18.081 0.711   1.00 78.24  ? 1585 LYS B CG  1 
ATOM   3014 C  CD  . LYS B 1 115 ? 3.958   -17.142 1.912   1.00 87.43  ? 1585 LYS B CD  1 
ATOM   3015 C  CE  . LYS B 1 115 ? 5.332   -16.498 2.117   1.00 90.74  ? 1585 LYS B CE  1 
ATOM   3016 N  NZ  . LYS B 1 115 ? 5.354   -15.621 3.335   1.00 87.52  ? 1585 LYS B NZ  1 
ATOM   3017 N  N   . ALA B 1 116 ? 2.935   -21.890 1.652   1.00 59.58  ? 1586 ALA B N   1 
ATOM   3018 C  CA  . ALA B 1 116 ? 3.703   -22.843 2.441   1.00 55.80  ? 1586 ALA B CA  1 
ATOM   3019 C  C   . ALA B 1 116 ? 4.115   -24.066 1.628   1.00 62.33  ? 1586 ALA B C   1 
ATOM   3020 O  O   . ALA B 1 116 ? 5.182   -24.645 1.882   1.00 59.55  ? 1586 ALA B O   1 
ATOM   3021 C  CB  . ALA B 1 116 ? 2.898   -23.286 3.665   1.00 58.01  ? 1586 ALA B CB  1 
ATOM   3022 N  N   . VAL B 1 117 ? 3.346   -24.462 0.616   1.00 47.42  ? 1587 VAL B N   1 
ATOM   3023 C  CA  . VAL B 1 117 ? 3.817   -25.599 -0.181  1.00 58.99  ? 1587 VAL B CA  1 
ATOM   3024 C  C   . VAL B 1 117 ? 4.554   -25.161 -1.440  1.00 53.09  ? 1587 VAL B C   1 
ATOM   3025 O  O   . VAL B 1 117 ? 4.823   -25.993 -2.313  1.00 49.78  ? 1587 VAL B O   1 
ATOM   3026 C  CB  . VAL B 1 117 ? 2.683   -26.587 -0.515  1.00 45.58  ? 1587 VAL B CB  1 
ATOM   3027 C  CG1 . VAL B 1 117 ? 2.167   -27.197 0.757   1.00 48.46  ? 1587 VAL B CG1 1 
ATOM   3028 C  CG2 . VAL B 1 117 ? 1.568   -25.899 -1.257  1.00 52.19  ? 1587 VAL B CG2 1 
ATOM   3029 N  N   . GLY B 1 118 ? 4.918   -23.885 -1.544  1.00 54.83  ? 1588 GLY B N   1 
ATOM   3030 C  CA  . GLY B 1 118 ? 5.678   -23.442 -2.699  1.00 53.04  ? 1588 GLY B CA  1 
ATOM   3031 C  C   . GLY B 1 118 ? 4.842   -23.203 -3.928  1.00 59.82  ? 1588 GLY B C   1 
ATOM   3032 O  O   . GLY B 1 118 ? 5.372   -23.221 -5.043  1.00 49.48  ? 1588 GLY B O   1 
ATOM   3033 N  N   . TRP B 1 119 ? 3.531   -23.024 -3.759  1.00 56.10  ? 1589 TRP B N   1 
ATOM   3034 C  CA  . TRP B 1 119 ? 2.631   -22.689 -4.864  1.00 68.78  ? 1589 TRP B CA  1 
ATOM   3035 C  C   . TRP B 1 119 ? 2.490   -21.170 -4.912  1.00 50.93  ? 1589 TRP B C   1 
ATOM   3036 O  O   . TRP B 1 119 ? 1.510   -20.586 -4.442  1.00 60.61  ? 1589 TRP B O   1 
ATOM   3037 C  CB  . TRP B 1 119 ? 1.284   -23.382 -4.687  1.00 65.07  ? 1589 TRP B CB  1 
ATOM   3038 C  CG  . TRP B 1 119 ? 1.375   -24.874 -4.753  1.00 70.63  ? 1589 TRP B CG  1 
ATOM   3039 C  CD1 . TRP B 1 119 ? 2.409   -25.618 -5.266  1.00 67.20  ? 1589 TRP B CD1 1 
ATOM   3040 C  CD2 . TRP B 1 119 ? 0.394   -25.808 -4.299  1.00 63.62  ? 1589 TRP B CD2 1 
ATOM   3041 N  NE1 . TRP B 1 119 ? 2.125   -26.956 -5.155  1.00 81.17  ? 1589 TRP B NE1 1 
ATOM   3042 C  CE2 . TRP B 1 119 ? 0.895   -27.102 -4.565  1.00 80.20  ? 1589 TRP B CE2 1 
ATOM   3043 C  CE3 . TRP B 1 119 ? -0.861  -25.679 -3.688  1.00 53.89  ? 1589 TRP B CE3 1 
ATOM   3044 C  CZ2 . TRP B 1 119 ? 0.183   -28.260 -4.242  1.00 73.86  ? 1589 TRP B CZ2 1 
ATOM   3045 C  CZ3 . TRP B 1 119 ? -1.564  -26.826 -3.370  1.00 61.17  ? 1589 TRP B CZ3 1 
ATOM   3046 C  CH2 . TRP B 1 119 ? -1.040  -28.100 -3.643  1.00 63.54  ? 1589 TRP B CH2 1 
ATOM   3047 N  N   . ASP B 1 120 ? 3.485   -20.522 -5.523  1.00 52.51  ? 1590 ASP B N   1 
ATOM   3048 C  CA  . ASP B 1 120 ? 3.643   -19.087 -5.316  1.00 67.46  ? 1590 ASP B CA  1 
ATOM   3049 C  C   . ASP B 1 120 ? 2.703   -18.236 -6.171  1.00 57.35  ? 1590 ASP B C   1 
ATOM   3050 O  O   . ASP B 1 120 ? 2.258   -17.182 -5.707  1.00 58.50  ? 1590 ASP B O   1 
ATOM   3051 C  CB  . ASP B 1 120 ? 5.104   -18.703 -5.558  1.00 79.01  ? 1590 ASP B CB  1 
ATOM   3052 C  CG  . ASP B 1 120 ? 6.024   -19.235 -4.470  1.00 84.54  ? 1590 ASP B CG  1 
ATOM   3053 O  OD1 . ASP B 1 120 ? 7.257   -19.232 -4.678  1.00 84.39  ? 1590 ASP B OD1 1 
ATOM   3054 O  OD2 . ASP B 1 120 ? 5.507   -19.663 -3.408  1.00 79.81  ? 1590 ASP B OD2 1 
ATOM   3055 N  N   . ASN B 1 121 ? 2.389   -18.658 -7.403  1.00 56.59  ? 1591 ASN B N   1 
ATOM   3056 C  CA  . ASN B 1 121 ? 1.406   -17.935 -8.211  1.00 56.94  ? 1591 ASN B CA  1 
ATOM   3057 C  C   . ASN B 1 121 ? 0.056   -17.909 -7.512  1.00 75.00  ? 1591 ASN B C   1 
ATOM   3058 O  O   . ASN B 1 121 ? -0.565  -16.847 -7.340  1.00 82.42  ? 1591 ASN B O   1 
ATOM   3059 C  CB  . ASN B 1 121 ? 1.265   -18.585 -9.592  1.00 60.22  ? 1591 ASN B CB  1 
ATOM   3060 C  CG  . ASN B 1 121 ? 2.490   -18.369 -10.480 1.00 92.54  ? 1591 ASN B CG  1 
ATOM   3061 O  OD1 . ASN B 1 121 ? 3.343   -17.519 -10.202 1.00 94.14  ? 1591 ASN B OD1 1 
ATOM   3062 N  ND2 . ASN B 1 121 ? 2.576   -19.141 -11.560 1.00 99.81  ? 1591 ASN B ND2 1 
ATOM   3063 N  N   . MET B 1 122 ? -0.419  -19.091 -7.128  1.00 57.21  ? 1592 MET B N   1 
ATOM   3064 C  CA  . MET B 1 122 ? -1.650  -19.188 -6.377  1.00 59.27  ? 1592 MET B CA  1 
ATOM   3065 C  C   . MET B 1 122 ? -1.560  -18.372 -5.096  1.00 48.79  ? 1592 MET B C   1 
ATOM   3066 O  O   . MET B 1 122 ? -2.514  -17.681 -4.719  1.00 59.26  ? 1592 MET B O   1 
ATOM   3067 C  CB  . MET B 1 122 ? -1.919  -20.662 -6.073  1.00 58.83  ? 1592 MET B CB  1 
ATOM   3068 C  CG  . MET B 1 122 ? -2.005  -21.545 -7.309  1.00 66.84  ? 1592 MET B CG  1 
ATOM   3069 S  SD  . MET B 1 122 ? -2.427  -23.258 -6.891  1.00 72.08  ? 1592 MET B SD  1 
ATOM   3070 C  CE  . MET B 1 122 ? -4.192  -23.072 -6.674  1.00 48.13  ? 1592 MET B CE  1 
ATOM   3071 N  N   . ALA B 1 123 ? -0.417  -18.438 -4.418  1.00 48.28  ? 1593 ALA B N   1 
ATOM   3072 C  CA  . ALA B 1 123 ? -0.259  -17.700 -3.179  1.00 47.40  ? 1593 ALA B CA  1 
ATOM   3073 C  C   . ALA B 1 123 ? -0.466  -16.213 -3.418  1.00 53.20  ? 1593 ALA B C   1 
ATOM   3074 O  O   . ALA B 1 123 ? -1.232  -15.560 -2.702  1.00 53.24  ? 1593 ALA B O   1 
ATOM   3075 C  CB  . ALA B 1 123 ? 1.122   -17.963 -2.583  1.00 47.31  ? 1593 ALA B CB  1 
ATOM   3076 N  N   . PHE B 1 124 ? 0.170   -15.674 -4.462  1.00 51.84  ? 1594 PHE B N   1 
ATOM   3077 C  CA  . PHE B 1 124 ? 0.046   -14.248 -4.736  1.00 58.10  ? 1594 PHE B CA  1 
ATOM   3078 C  C   . PHE B 1 124 ? -1.383  -13.883 -5.101  1.00 57.83  ? 1594 PHE B C   1 
ATOM   3079 O  O   . PHE B 1 124 ? -1.939  -12.919 -4.573  1.00 63.57  ? 1594 PHE B O   1 
ATOM   3080 C  CB  . PHE B 1 124 ? 1.004   -13.823 -5.853  1.00 67.26  ? 1594 PHE B CB  1 
ATOM   3081 C  CG  . PHE B 1 124 ? 0.979   -12.338 -6.139  1.00 65.44  ? 1594 PHE B CG  1 
ATOM   3082 C  CD1 . PHE B 1 124 ? 1.645   -11.445 -5.311  1.00 68.90  ? 1594 PHE B CD1 1 
ATOM   3083 C  CD2 . PHE B 1 124 ? 0.273   -11.835 -7.227  1.00 70.96  ? 1594 PHE B CD2 1 
ATOM   3084 C  CE1 . PHE B 1 124 ? 1.618   -10.069 -5.573  1.00 65.47  ? 1594 PHE B CE1 1 
ATOM   3085 C  CE2 . PHE B 1 124 ? 0.243   -10.464 -7.494  1.00 63.65  ? 1594 PHE B CE2 1 
ATOM   3086 C  CZ  . PHE B 1 124 ? 0.913   -9.586  -6.661  1.00 62.96  ? 1594 PHE B CZ  1 
ATOM   3087 N  N   . ILE B 1 125 ? -2.003  -14.646 -5.999  1.00 62.27  ? 1595 ILE B N   1 
ATOM   3088 C  CA  . ILE B 1 125 ? -3.346  -14.280 -6.446  1.00 63.37  ? 1595 ILE B CA  1 
ATOM   3089 C  C   . ILE B 1 125 ? -4.331  -14.334 -5.284  1.00 60.24  ? 1595 ILE B C   1 
ATOM   3090 O  O   . ILE B 1 125 ? -5.124  -13.405 -5.076  1.00 64.64  ? 1595 ILE B O   1 
ATOM   3091 C  CB  . ILE B 1 125 ? -3.799  -15.181 -7.603  1.00 55.29  ? 1595 ILE B CB  1 
ATOM   3092 C  CG1 . ILE B 1 125 ? -2.971  -14.871 -8.839  1.00 59.82  ? 1595 ILE B CG1 1 
ATOM   3093 C  CG2 . ILE B 1 125 ? -5.287  -14.985 -7.859  1.00 53.66  ? 1595 ILE B CG2 1 
ATOM   3094 C  CD1 . ILE B 1 125 ? -3.030  -15.928 -9.881  1.00 55.83  ? 1595 ILE B CD1 1 
ATOM   3095 N  N   . PHE B 1 126 ? -4.294  -15.415 -4.504  1.00 51.06  ? 1596 PHE B N   1 
ATOM   3096 C  CA  . PHE B 1 126 ? -5.233  -15.536 -3.390  1.00 56.32  ? 1596 PHE B CA  1 
ATOM   3097 C  C   . PHE B 1 126 ? -4.964  -14.478 -2.317  1.00 59.64  ? 1596 PHE B C   1 
ATOM   3098 O  O   . PHE B 1 126 ? -5.911  -13.922 -1.754  1.00 58.31  ? 1596 PHE B O   1 
ATOM   3099 C  CB  . PHE B 1 126 ? -5.192  -16.945 -2.782  1.00 46.74  ? 1596 PHE B CB  1 
ATOM   3100 C  CG  . PHE B 1 126 ? -5.531  -18.067 -3.765  1.00 47.09  ? 1596 PHE B CG  1 
ATOM   3101 C  CD1 . PHE B 1 126 ? -6.391  -17.860 -4.822  1.00 48.32  ? 1596 PHE B CD1 1 
ATOM   3102 C  CD2 . PHE B 1 126 ? -4.987  -19.333 -3.603  1.00 48.76  ? 1596 PHE B CD2 1 
ATOM   3103 C  CE1 . PHE B 1 126 ? -6.691  -18.887 -5.708  1.00 57.98  ? 1596 PHE B CE1 1 
ATOM   3104 C  CE2 . PHE B 1 126 ? -5.276  -20.361 -4.493  1.00 50.64  ? 1596 PHE B CE2 1 
ATOM   3105 C  CZ  . PHE B 1 126 ? -6.127  -20.146 -5.542  1.00 47.92  ? 1596 PHE B CZ  1 
ATOM   3106 N  N   . LEU B 1 127 ? -3.688  -14.173 -2.017  1.00 51.88  ? 1597 LEU B N   1 
ATOM   3107 C  CA  . LEU B 1 127 ? -3.395  -13.200 -0.966  1.00 49.41  ? 1597 LEU B CA  1 
ATOM   3108 C  C   . LEU B 1 127 ? -3.670  -11.776 -1.430  1.00 49.73  ? 1597 LEU B C   1 
ATOM   3109 O  O   . LEU B 1 127 ? -4.105  -10.939 -0.633  1.00 56.41  ? 1597 LEU B O   1 
ATOM   3110 C  CB  . LEU B 1 127 ? -1.944  -13.340 -0.499  1.00 51.63  ? 1597 LEU B CB  1 
ATOM   3111 C  CG  . LEU B 1 127 ? -1.700  -14.655 0.250   1.00 66.51  ? 1597 LEU B CG  1 
ATOM   3112 C  CD1 . LEU B 1 127 ? -0.249  -14.817 0.689   1.00 63.79  ? 1597 LEU B CD1 1 
ATOM   3113 C  CD2 . LEU B 1 127 ? -2.664  -14.790 1.437   1.00 58.21  ? 1597 LEU B CD2 1 
ATOM   3114 N  N   . ASN B 1 128 ? -3.477  -11.496 -2.716  1.00 56.36  ? 1598 ASN B N   1 
ATOM   3115 C  CA  . ASN B 1 128 ? -3.867  -10.205 -3.266  1.00 63.60  ? 1598 ASN B CA  1 
ATOM   3116 C  C   . ASN B 1 128 ? -5.374  -10.039 -3.214  1.00 70.02  ? 1598 ASN B C   1 
ATOM   3117 O  O   . ASN B 1 128 ? -5.883  -8.977  -2.825  1.00 70.85  ? 1598 ASN B O   1 
ATOM   3118 C  CB  . ASN B 1 128 ? -3.372  -10.073 -4.700  1.00 56.66  ? 1598 ASN B CB  1 
ATOM   3119 C  CG  . ASN B 1 128 ? -3.482  -8.667  -5.212  1.00 56.11  ? 1598 ASN B CG  1 
ATOM   3120 O  OD1 . ASN B 1 128 ? -3.284  -7.703  -4.469  1.00 71.36  ? 1598 ASN B OD1 1 
ATOM   3121 N  ND2 . ASN B 1 128 ? -3.805  -8.531  -6.491  1.00 65.36  ? 1598 ASN B ND2 1 
ATOM   3122 N  N   . ARG B 1 129 ? -6.102  -11.081 -3.627  1.00 58.99  ? 1599 ARG B N   1 
ATOM   3123 C  CA  . ARG B 1 129 ? -7.553  -11.068 -3.509  1.00 59.84  ? 1599 ARG B CA  1 
ATOM   3124 C  C   . ARG B 1 129 ? -7.971  -10.868 -2.058  1.00 65.41  ? 1599 ARG B C   1 
ATOM   3125 O  O   . ARG B 1 129 ? -8.905  -10.109 -1.772  1.00 52.01  ? 1599 ARG B O   1 
ATOM   3126 C  CB  . ARG B 1 129 ? -8.128  -12.364 -4.073  1.00 56.87  ? 1599 ARG B CB  1 
ATOM   3127 C  CG  . ARG B 1 129 ? -9.602  -12.503 -3.865  1.00 71.20  ? 1599 ARG B CG  1 
ATOM   3128 C  CD  . ARG B 1 129 ? -10.341 -11.264 -4.380  1.00 78.40  ? 1599 ARG B CD  1 
ATOM   3129 N  NE  . ARG B 1 129 ? -11.669 -11.628 -4.853  1.00 85.52  ? 1599 ARG B NE  1 
ATOM   3130 C  CZ  . ARG B 1 129 ? -12.078 -11.486 -6.107  1.00 92.12  ? 1599 ARG B CZ  1 
ATOM   3131 N  NH1 . ARG B 1 129 ? -11.262 -10.959 -7.014  1.00 93.50  ? 1599 ARG B NH1 1 
ATOM   3132 N  NH2 . ARG B 1 129 ? -13.306 -11.860 -6.447  1.00 92.18  ? 1599 ARG B NH2 1 
ATOM   3133 N  N   . PHE B 1 130 ? -7.269  -11.520 -1.128  1.00 49.19  ? 1600 PHE B N   1 
ATOM   3134 C  CA  . PHE B 1 130 ? -7.527  -11.312 0.293   1.00 53.04  ? 1600 PHE B CA  1 
ATOM   3135 C  C   . PHE B 1 130 ? -7.386  -9.844  0.681   1.00 58.77  ? 1600 PHE B C   1 
ATOM   3136 O  O   . PHE B 1 130 ? -8.256  -9.279  1.353   1.00 62.04  ? 1600 PHE B O   1 
ATOM   3137 C  CB  . PHE B 1 130 ? -6.560  -12.149 1.115   1.00 49.23  ? 1600 PHE B CB  1 
ATOM   3138 C  CG  . PHE B 1 130 ? -6.399  -11.668 2.511   1.00 55.89  ? 1600 PHE B CG  1 
ATOM   3139 C  CD1 . PHE B 1 130 ? -7.452  -11.760 3.411   1.00 47.10  ? 1600 PHE B CD1 1 
ATOM   3140 C  CD2 . PHE B 1 130 ? -5.196  -11.128 2.935   1.00 53.38  ? 1600 PHE B CD2 1 
ATOM   3141 C  CE1 . PHE B 1 130 ? -7.314  -11.322 4.716   1.00 47.17  ? 1600 PHE B CE1 1 
ATOM   3142 C  CE2 . PHE B 1 130 ? -5.043  -10.686 4.239   1.00 47.00  ? 1600 PHE B CE2 1 
ATOM   3143 C  CZ  . PHE B 1 130 ? -6.109  -10.784 5.136   1.00 51.12  ? 1600 PHE B CZ  1 
ATOM   3144 N  N   . LEU B 1 131 ? -6.267  -9.224  0.309   1.00 58.45  ? 1601 LEU B N   1 
ATOM   3145 C  CA  . LEU B 1 131 ? -6.068  -7.826  0.668   1.00 64.67  ? 1601 LEU B CA  1 
ATOM   3146 C  C   . LEU B 1 131 ? -7.192  -6.967  0.112   1.00 61.29  ? 1601 LEU B C   1 
ATOM   3147 O  O   . LEU B 1 131 ? -7.765  -6.125  0.823   1.00 62.71  ? 1601 LEU B O   1 
ATOM   3148 C  CB  . LEU B 1 131 ? -4.709  -7.345  0.157   1.00 63.12  ? 1601 LEU B CB  1 
ATOM   3149 C  CG  . LEU B 1 131 ? -3.439  -7.928  0.787   1.00 53.25  ? 1601 LEU B CG  1 
ATOM   3150 C  CD1 . LEU B 1 131 ? -2.204  -7.330  0.103   1.00 58.28  ? 1601 LEU B CD1 1 
ATOM   3151 C  CD2 . LEU B 1 131 ? -3.388  -7.693  2.303   1.00 49.57  ? 1601 LEU B CD2 1 
ATOM   3152 N  N   . ASP B 1 132 ? -7.543  -7.192  -1.154  1.00 53.40  ? 1602 ASP B N   1 
ATOM   3153 C  CA  . ASP B 1 132 ? -8.614  -6.417  -1.762  1.00 55.01  ? 1602 ASP B CA  1 
ATOM   3154 C  C   . ASP B 1 132 ? -9.939  -6.638  -1.038  1.00 64.12  ? 1602 ASP B C   1 
ATOM   3155 O  O   . ASP B 1 132 ? -10.714 -5.691  -0.832  1.00 73.13  ? 1602 ASP B O   1 
ATOM   3156 C  CB  . ASP B 1 132 ? -8.721  -6.768  -3.248  1.00 69.24  ? 1602 ASP B CB  1 
ATOM   3157 C  CG  . ASP B 1 132 ? -7.488  -6.332  -4.049  1.00 75.58  ? 1602 ASP B CG  1 
ATOM   3158 O  OD1 . ASP B 1 132 ? -6.515  -5.816  -3.449  1.00 73.77  ? 1602 ASP B OD1 1 
ATOM   3159 O  OD2 . ASP B 1 132 ? -7.495  -6.503  -5.286  1.00 73.94  ? 1602 ASP B OD2 1 
ATOM   3160 N  N   . LEU B 1 133 ? -10.205 -7.872  -0.605  1.00 54.57  ? 1603 LEU B N   1 
ATOM   3161 C  CA  . LEU B 1 133 ? -11.468 -8.123  0.067   1.00 60.43  ? 1603 LEU B CA  1 
ATOM   3162 C  C   . LEU B 1 133 ? -11.480 -7.484  1.442   1.00 64.48  ? 1603 LEU B C   1 
ATOM   3163 O  O   . LEU B 1 133 ? -12.517 -6.964  1.869   1.00 60.40  ? 1603 LEU B O   1 
ATOM   3164 C  CB  . LEU B 1 133 ? -11.722 -9.631  0.201   1.00 50.75  ? 1603 LEU B CB  1 
ATOM   3165 C  CG  . LEU B 1 133 ? -11.964 -10.412 -1.093  1.00 64.58  ? 1603 LEU B CG  1 
ATOM   3166 C  CD1 . LEU B 1 133 ? -11.703 -11.928 -0.912  1.00 55.05  ? 1603 LEU B CD1 1 
ATOM   3167 C  CD2 . LEU B 1 133 ? -13.356 -10.143 -1.642  1.00 52.53  ? 1603 LEU B CD2 1 
ATOM   3168 N  N   . THR B 1 134 ? -10.323 -7.455  2.107   1.00 56.97  ? 1604 THR B N   1 
ATOM   3169 C  CA  . THR B 1 134 ? -10.215 -6.805  3.406   1.00 51.22  ? 1604 THR B CA  1 
ATOM   3170 C  C   . THR B 1 134 ? -10.519 -5.320  3.295   1.00 65.11  ? 1604 THR B C   1 
ATOM   3171 O  O   . THR B 1 134 ? -11.219 -4.750  4.142   1.00 61.36  ? 1604 THR B O   1 
ATOM   3172 C  CB  . THR B 1 134 ? -8.807  -6.999  3.968   1.00 65.98  ? 1604 THR B CB  1 
ATOM   3173 O  OG1 . THR B 1 134 ? -8.682  -8.292  4.571   1.00 67.88  ? 1604 THR B OG1 1 
ATOM   3174 C  CG2 . THR B 1 134 ? -8.505  -5.931  4.988   1.00 79.67  ? 1604 THR B CG2 1 
ATOM   3175 N  N   . ASP B 1 135 ? -9.992  -4.676  2.256   1.00 68.68  ? 1605 ASP B N   1 
ATOM   3176 C  CA  . ASP B 1 135 ? -10.310 -3.268  2.046   1.00 78.72  ? 1605 ASP B CA  1 
ATOM   3177 C  C   . ASP B 1 135 ? -11.792 -3.078  1.729   1.00 82.15  ? 1605 ASP B C   1 
ATOM   3178 O  O   . ASP B 1 135 ? -12.449 -2.184  2.286   1.00 80.39  ? 1605 ASP B O   1 
ATOM   3179 C  CB  . ASP B 1 135 ? -9.419  -2.701  0.939   1.00 86.79  ? 1605 ASP B CB  1 
ATOM   3180 C  CG  . ASP B 1 135 ? -7.930  -3.014  1.169   1.00 89.47  ? 1605 ASP B CG  1 
ATOM   3181 O  OD1 . ASP B 1 135 ? -7.552  -3.380  2.322   1.00 70.03  ? 1605 ASP B OD1 1 
ATOM   3182 O  OD2 . ASP B 1 135 ? -7.148  -2.909  0.188   1.00 80.55  ? 1605 ASP B OD2 1 
ATOM   3183 N  N   . ALA B 1 136 ? -12.352 -3.948  0.886   1.00 85.54  ? 1606 ALA B N   1 
ATOM   3184 C  CA  . ALA B 1 136 ? -13.755 -3.802  0.506   1.00 82.60  ? 1606 ALA B CA  1 
ATOM   3185 C  C   . ALA B 1 136 ? -14.702 -4.035  1.681   1.00 88.03  ? 1606 ALA B C   1 
ATOM   3186 O  O   . ALA B 1 136 ? -15.806 -3.475  1.698   1.00 92.43  ? 1606 ALA B O   1 
ATOM   3187 C  CB  . ALA B 1 136 ? -14.089 -4.753  -0.639  1.00 75.77  ? 1606 ALA B CB  1 
ATOM   3188 N  N   . ILE B 1 137 ? -14.305 -4.867  2.651   1.00 88.79  ? 1607 ILE B N   1 
ATOM   3189 C  CA  . ILE B 1 137 ? -15.112 -5.062  3.859   1.00 83.92  ? 1607 ILE B CA  1 
ATOM   3190 C  C   . ILE B 1 137 ? -15.385 -3.725  4.527   1.00 87.93  ? 1607 ILE B C   1 
ATOM   3191 O  O   . ILE B 1 137 ? -16.534 -3.380  4.830   1.00 80.83  ? 1607 ILE B O   1 
ATOM   3192 C  CB  . ILE B 1 137 ? -14.407 -6.014  4.844   1.00 73.76  ? 1607 ILE B CB  1 
ATOM   3193 C  CG1 . ILE B 1 137 ? -14.431 -7.466  4.362   1.00 64.12  ? 1607 ILE B CG1 1 
ATOM   3194 C  CG2 . ILE B 1 137 ? -15.043 -5.912  6.232   1.00 66.45  ? 1607 ILE B CG2 1 
ATOM   3195 C  CD1 . ILE B 1 137 ? -13.498 -8.354  5.162   1.00 63.50  ? 1607 ILE B CD1 1 
ATOM   3196 N  N   . GLU B 1 138 ? -14.318 -2.967  4.788   1.00 83.54  ? 1608 GLU B N   1 
ATOM   3197 C  CA  . GLU B 1 138 ? -14.470 -1.634  5.353   1.00 96.55  ? 1608 GLU B CA  1 
ATOM   3198 C  C   . GLU B 1 138 ? -15.291 -0.748  4.428   1.00 94.49  ? 1608 GLU B C   1 
ATOM   3199 O  O   . GLU B 1 138 ? -16.241 -0.088  4.865   1.00 80.27  ? 1608 GLU B O   1 
ATOM   3200 C  CB  . GLU B 1 138 ? -13.093 -1.036  5.612   1.00 91.69  ? 1608 GLU B CB  1 
ATOM   3201 C  CG  . GLU B 1 138 ? -12.034 -2.103  5.836   1.00 74.19  ? 1608 GLU B CG  1 
ATOM   3202 C  CD  . GLU B 1 138 ? -10.740 -1.524  6.383   1.00 93.44  ? 1608 GLU B CD  1 
ATOM   3203 O  OE1 . GLU B 1 138 ? -10.214 -0.556  5.782   1.00 97.58  ? 1608 GLU B OE1 1 
ATOM   3204 O  OE2 . GLU B 1 138 ? -10.254 -2.022  7.424   1.00 94.16  ? 1608 GLU B OE2 1 
ATOM   3205 N  N   . GLU B 1 139 ? -14.961 -0.752  3.130   1.00 97.52  ? 1609 GLU B N   1 
ATOM   3206 C  CA  . GLU B 1 139 ? -15.730 0.061   2.190   1.00 89.02  ? 1609 GLU B CA  1 
ATOM   3207 C  C   . GLU B 1 139 ? -17.190 -0.384  2.079   1.00 90.93  ? 1609 GLU B C   1 
ATOM   3208 O  O   . GLU B 1 139 ? -18.043 0.423   1.690   1.00 100.06 ? 1609 GLU B O   1 
ATOM   3209 C  CB  . GLU B 1 139 ? -15.063 0.048   0.808   1.00 82.83  ? 1609 GLU B CB  1 
ATOM   3210 N  N   . GLY B 1 140 ? -17.501 -1.643  2.393   1.00 88.00  ? 1610 GLY B N   1 
ATOM   3211 C  CA  . GLY B 1 140 ? -18.875 -2.109  2.376   1.00 75.95  ? 1610 GLY B CA  1 
ATOM   3212 C  C   . GLY B 1 140 ? -19.434 -2.501  1.024   1.00 82.31  ? 1610 GLY B C   1 
ATOM   3213 O  O   . GLY B 1 140 ? -20.607 -2.885  0.954   1.00 89.46  ? 1610 GLY B O   1 
ATOM   3214 N  N   . THR B 1 141 ? -18.640 -2.443  -0.047  1.00 94.16  ? 1611 THR B N   1 
ATOM   3215 C  CA  . THR B 1 141 ? -19.090 -2.863  -1.371  1.00 95.85  ? 1611 THR B CA  1 
ATOM   3216 C  C   . THR B 1 141 ? -17.999 -3.669  -2.062  1.00 94.56  ? 1611 THR B C   1 
ATOM   3217 O  O   . THR B 1 141 ? -16.812 -3.566  -1.736  1.00 93.46  ? 1611 THR B O   1 
ATOM   3218 C  CB  . THR B 1 141 ? -19.458 -1.664  -2.265  1.00 94.71  ? 1611 THR B CB  1 
ATOM   3219 O  OG1 . THR B 1 141 ? -19.963 -2.127  -3.526  1.00 85.91  ? 1611 THR B OG1 1 
ATOM   3220 C  CG2 . THR B 1 141 ? -18.229 -0.812  -2.524  1.00 90.75  ? 1611 THR B CG2 1 
ATOM   3221 N  N   . LEU B 1 142 ? -18.424 -4.465  -3.043  1.00 81.28  ? 1612 LEU B N   1 
ATOM   3222 C  CA  . LEU B 1 142 ? -17.527 -5.269  -3.859  1.00 80.73  ? 1612 LEU B CA  1 
ATOM   3223 C  C   . LEU B 1 142 ? -17.416 -4.743  -5.285  1.00 88.63  ? 1612 LEU B C   1 
ATOM   3224 O  O   . LEU B 1 142 ? -16.797 -5.403  -6.129  1.00 80.74  ? 1612 LEU B O   1 
ATOM   3225 C  CB  . LEU B 1 142 ? -17.980 -6.730  -3.868  1.00 84.61  ? 1612 LEU B CB  1 
ATOM   3226 N  N   . ASP B 1 143 ? -18.020 -3.583  -5.582  1.00 98.12  ? 1613 ASP B N   1 
ATOM   3227 C  CA  . ASP B 1 143 ? -18.053 -3.084  -6.952  1.00 109.24 ? 1613 ASP B CA  1 
ATOM   3228 C  C   . ASP B 1 143 ? -16.753 -2.428  -7.389  1.00 105.17 ? 1613 ASP B C   1 
ATOM   3229 O  O   . ASP B 1 143 ? -16.606 -2.129  -8.580  1.00 103.22 ? 1613 ASP B O   1 
ATOM   3230 C  CB  . ASP B 1 143 ? -19.183 -2.057  -7.132  1.00 125.48 ? 1613 ASP B CB  1 
ATOM   3231 C  CG  . ASP B 1 143 ? -20.566 -2.692  -7.202  1.00 130.43 ? 1613 ASP B CG  1 
ATOM   3232 O  OD1 . ASP B 1 143 ? -20.689 -3.913  -6.951  1.00 132.66 ? 1613 ASP B OD1 1 
ATOM   3233 O  OD2 . ASP B 1 143 ? -21.532 -1.959  -7.523  1.00 126.24 ? 1613 ASP B OD2 1 
ATOM   3234 N  N   . GLY B 1 144 ? -15.802 -2.223  -6.483  1.00 97.26  ? 1614 GLY B N   1 
ATOM   3235 C  CA  . GLY B 1 144 ? -14.530 -1.679  -6.906  1.00 104.06 ? 1614 GLY B CA  1 
ATOM   3236 C  C   . GLY B 1 144 ? -13.534 -2.733  -7.345  1.00 108.18 ? 1614 GLY B C   1 
ATOM   3237 O  O   . GLY B 1 144 ? -12.578 -2.434  -8.068  1.00 110.41 ? 1614 GLY B O   1 
ATOM   3238 N  N   . LEU B 1 145 ? -13.764 -3.976  -6.937  1.00 113.03 ? 1615 LEU B N   1 
ATOM   3239 C  CA  . LEU B 1 145 ? -12.761 -5.021  -7.084  1.00 108.76 ? 1615 LEU B CA  1 
ATOM   3240 C  C   . LEU B 1 145 ? -12.772 -5.626  -8.484  1.00 108.99 ? 1615 LEU B C   1 
ATOM   3241 O  O   . LEU B 1 145 ? -13.819 -5.732  -9.133  1.00 104.22 ? 1615 LEU B O   1 
ATOM   3242 C  CB  . LEU B 1 145 ? -12.967 -6.099  -6.026  1.00 101.87 ? 1615 LEU B CB  1 
ATOM   3243 C  CG  . LEU B 1 145 ? -12.625 -5.567  -4.629  1.00 98.57  ? 1615 LEU B CG  1 
ATOM   3244 C  CD1 . LEU B 1 145 ? -12.313 -6.724  -3.671  1.00 85.41  ? 1615 LEU B CD1 1 
ATOM   3245 C  CD2 . LEU B 1 145 ? -11.491 -4.501  -4.659  1.00 87.74  ? 1615 LEU B CD2 1 
ATOM   3246 N  N   . ASP B 1 146 ? -11.581 -6.032  -8.939  1.00 104.32 ? 1616 ASP B N   1 
ATOM   3247 C  CA  . ASP B 1 146 ? -11.387 -6.659  -10.243 1.00 104.13 ? 1616 ASP B CA  1 
ATOM   3248 C  C   . ASP B 1 146 ? -11.284 -8.175  -10.097 1.00 99.22  ? 1616 ASP B C   1 
ATOM   3249 O  O   . ASP B 1 146 ? -10.402 -8.682  -9.392  1.00 91.79  ? 1616 ASP B O   1 
ATOM   3250 C  CB  . ASP B 1 146 ? -10.133 -6.101  -10.918 1.00 107.89 ? 1616 ASP B CB  1 
ATOM   3251 C  CG  . ASP B 1 146 ? -9.579  -7.029  -11.979 1.00 115.59 ? 1616 ASP B CG  1 
ATOM   3252 O  OD1 . ASP B 1 146 ? -8.370  -7.346  -11.918 1.00 115.24 ? 1616 ASP B OD1 1 
ATOM   3253 O  OD2 . ASP B 1 146 ? -10.351 -7.438  -12.872 1.00 118.85 ? 1616 ASP B OD2 1 
ATOM   3254 N  N   . HIS B 1 147 ? -12.162 -8.889  -10.800 1.00 96.43  ? 1617 HIS B N   1 
ATOM   3255 C  CA  . HIS B 1 147 ? -12.267 -10.340 -10.728 1.00 95.60  ? 1617 HIS B CA  1 
ATOM   3256 C  C   . HIS B 1 147 ? -11.602 -11.036 -11.910 1.00 92.03  ? 1617 HIS B C   1 
ATOM   3257 O  O   . HIS B 1 147 ? -11.845 -12.228 -12.129 1.00 92.85  ? 1617 HIS B O   1 
ATOM   3258 C  CB  . HIS B 1 147 ? -13.741 -10.766 -10.660 1.00 99.97  ? 1617 HIS B CB  1 
ATOM   3259 C  CG  . HIS B 1 147 ? -14.587 -9.928  -9.745  1.00 107.49 ? 1617 HIS B CG  1 
ATOM   3260 N  ND1 . HIS B 1 147 ? -15.905 -9.633  -10.024 1.00 110.32 ? 1617 HIS B ND1 1 
ATOM   3261 C  CD2 . HIS B 1 147 ? -14.313 -9.328  -8.561  1.00 107.89 ? 1617 HIS B CD2 1 
ATOM   3262 C  CE1 . HIS B 1 147 ? -16.402 -8.879  -9.059  1.00 110.00 ? 1617 HIS B CE1 1 
ATOM   3263 N  NE2 . HIS B 1 147 ? -15.456 -8.679  -8.159  1.00 108.42 ? 1617 HIS B NE2 1 
ATOM   3264 N  N   . SER B 1 148 ? -10.797 -10.315 -12.695 1.00 84.35  ? 1618 SER B N   1 
ATOM   3265 C  CA  . SER B 1 148 ? -10.238 -10.894 -13.913 1.00 86.24  ? 1618 SER B CA  1 
ATOM   3266 C  C   . SER B 1 148 ? -9.453  -12.174 -13.633 1.00 74.78  ? 1618 SER B C   1 
ATOM   3267 O  O   . SER B 1 148 ? -9.439  -13.083 -14.470 1.00 83.09  ? 1618 SER B O   1 
ATOM   3268 C  CB  . SER B 1 148 ? -9.358  -9.863  -14.634 1.00 86.90  ? 1618 SER B CB  1 
ATOM   3269 O  OG  . SER B 1 148 ? -8.243  -9.476  -13.843 1.00 85.20  ? 1618 SER B OG  1 
ATOM   3270 N  N   . ASP B 1 149 ? -8.814  -12.274 -12.467 1.00 62.02  ? 1619 ASP B N   1 
ATOM   3271 C  CA  . ASP B 1 149 ? -7.956  -13.419 -12.175 1.00 69.80  ? 1619 ASP B CA  1 
ATOM   3272 C  C   . ASP B 1 149 ? -8.714  -14.743 -12.162 1.00 76.43  ? 1619 ASP B C   1 
ATOM   3273 O  O   . ASP B 1 149 ? -8.086  -15.798 -12.287 1.00 69.19  ? 1619 ASP B O   1 
ATOM   3274 C  CB  . ASP B 1 149 ? -7.237  -13.222 -10.835 1.00 66.46  ? 1619 ASP B CB  1 
ATOM   3275 C  CG  . ASP B 1 149 ? -5.967  -12.386 -10.969 1.00 75.73  ? 1619 ASP B CG  1 
ATOM   3276 O  OD1 . ASP B 1 149 ? -5.568  -12.101 -12.121 1.00 71.72  ? 1619 ASP B OD1 1 
ATOM   3277 O  OD2 . ASP B 1 149 ? -5.357  -12.032 -9.928  1.00 70.71  ? 1619 ASP B OD2 1 
ATOM   3278 N  N   . PHE B 1 150 ? -10.036 -14.724 -11.984 1.00 77.06  ? 1620 PHE B N   1 
ATOM   3279 C  CA  . PHE B 1 150 ? -10.823 -15.942 -11.811 1.00 81.88  ? 1620 PHE B CA  1 
ATOM   3280 C  C   . PHE B 1 150 ? -11.892 -16.095 -12.887 1.00 96.33  ? 1620 PHE B C   1 
ATOM   3281 O  O   . PHE B 1 150 ? -12.969 -16.638 -12.633 1.00 96.98  ? 1620 PHE B O   1 
ATOM   3282 C  CB  . PHE B 1 150 ? -11.471 -15.978 -10.425 1.00 73.02  ? 1620 PHE B CB  1 
ATOM   3283 C  CG  . PHE B 1 150 ? -10.600 -15.431 -9.326  1.00 68.94  ? 1620 PHE B CG  1 
ATOM   3284 C  CD1 . PHE B 1 150 ? -9.637  -16.226 -8.724  1.00 62.90  ? 1620 PHE B CD1 1 
ATOM   3285 C  CD2 . PHE B 1 150 ? -10.741 -14.122 -8.894  1.00 66.71  ? 1620 PHE B CD2 1 
ATOM   3286 C  CE1 . PHE B 1 150 ? -8.825  -15.729 -7.716  1.00 62.65  ? 1620 PHE B CE1 1 
ATOM   3287 C  CE2 . PHE B 1 150 ? -9.931  -13.622 -7.885  1.00 70.61  ? 1620 PHE B CE2 1 
ATOM   3288 C  CZ  . PHE B 1 150 ? -8.972  -14.426 -7.296  1.00 66.13  ? 1620 PHE B CZ  1 
ATOM   3289 N  N   . GLN B 1 151 ? -11.605 -15.664 -14.117 1.00 105.99 ? 1621 GLN B N   1 
ATOM   3290 C  CA  . GLN B 1 151 ? -12.692 -15.462 -15.069 1.00 113.53 ? 1621 GLN B CA  1 
ATOM   3291 C  C   . GLN B 1 151 ? -13.262 -16.756 -15.646 1.00 113.50 ? 1621 GLN B C   1 
ATOM   3292 O  O   . GLN B 1 151 ? -14.446 -16.782 -16.000 1.00 123.42 ? 1621 GLN B O   1 
ATOM   3293 C  CB  . GLN B 1 151 ? -12.226 -14.556 -16.215 1.00 110.07 ? 1621 GLN B CB  1 
ATOM   3294 N  N   . ASP B 1 152 ? -12.492 -17.839 -15.707 1.00 95.43  ? 1622 ASP B N   1 
ATOM   3295 C  CA  . ASP B 1 152 ? -13.009 -19.106 -16.217 1.00 103.94 ? 1622 ASP B CA  1 
ATOM   3296 C  C   . ASP B 1 152 ? -12.925 -20.201 -15.165 1.00 98.70  ? 1622 ASP B C   1 
ATOM   3297 O  O   . ASP B 1 152 ? -12.650 -21.366 -15.464 1.00 101.32 ? 1622 ASP B O   1 
ATOM   3298 C  CB  . ASP B 1 152 ? -12.285 -19.526 -17.492 1.00 111.81 ? 1622 ASP B CB  1 
ATOM   3299 C  CG  . ASP B 1 152 ? -12.616 -18.625 -18.664 1.00 120.94 ? 1622 ASP B CG  1 
ATOM   3300 O  OD1 . ASP B 1 152 ? -11.676 -18.127 -19.321 1.00 123.69 ? 1622 ASP B OD1 1 
ATOM   3301 O  OD2 . ASP B 1 152 ? -13.820 -18.408 -18.923 1.00 122.25 ? 1622 ASP B OD2 1 
ATOM   3302 N  N   . THR B 1 153 ? -13.191 -19.831 -13.920 1.00 86.84  ? 1623 THR B N   1 
ATOM   3303 C  CA  . THR B 1 153 ? -13.134 -20.735 -12.788 1.00 84.76  ? 1623 THR B CA  1 
ATOM   3304 C  C   . THR B 1 153 ? -14.532 -20.908 -12.214 1.00 80.03  ? 1623 THR B C   1 
ATOM   3305 O  O   . THR B 1 153 ? -15.442 -20.128 -12.496 1.00 91.20  ? 1623 THR B O   1 
ATOM   3306 C  CB  . THR B 1 153 ? -12.188 -20.194 -11.711 1.00 82.31  ? 1623 THR B CB  1 
ATOM   3307 O  OG1 . THR B 1 153 ? -12.843 -19.149 -10.979 1.00 64.05  ? 1623 THR B OG1 1 
ATOM   3308 C  CG2 . THR B 1 153 ? -10.924 -19.637 -12.344 1.00 81.01  ? 1623 THR B CG2 1 
ATOM   3309 N  N   . ASP B 1 154 ? -14.697 -21.936 -11.391 1.00 69.09  ? 1624 ASP B N   1 
ATOM   3310 C  CA  . ASP B 1 154 ? -15.920 -22.098 -10.625 1.00 67.49  ? 1624 ASP B CA  1 
ATOM   3311 C  C   . ASP B 1 154 ? -15.886 -21.308 -9.319  1.00 66.85  ? 1624 ASP B C   1 
ATOM   3312 O  O   . ASP B 1 154 ? -16.688 -21.576 -8.417  1.00 64.28  ? 1624 ASP B O   1 
ATOM   3313 C  CB  . ASP B 1 154 ? -16.183 -23.584 -10.354 1.00 74.14  ? 1624 ASP B CB  1 
ATOM   3314 C  CG  . ASP B 1 154 ? -15.065 -24.244 -9.568  1.00 76.00  ? 1624 ASP B CG  1 
ATOM   3315 O  OD1 . ASP B 1 154 ? -14.017 -23.586 -9.369  1.00 77.60  ? 1624 ASP B OD1 1 
ATOM   3316 O  OD2 . ASP B 1 154 ? -15.244 -25.415 -9.136  1.00 66.16  ? 1624 ASP B OD2 1 
ATOM   3317 N  N   . ILE B 1 155 ? -14.965 -20.354 -9.197  1.00 56.49  ? 1625 ILE B N   1 
ATOM   3318 C  CA  . ILE B 1 155 ? -14.908 -19.451 -8.054  1.00 59.56  ? 1625 ILE B CA  1 
ATOM   3319 C  C   . ILE B 1 155 ? -15.918 -18.328 -8.270  1.00 72.58  ? 1625 ILE B C   1 
ATOM   3320 O  O   . ILE B 1 155 ? -15.885 -17.661 -9.316  1.00 63.05  ? 1625 ILE B O   1 
ATOM   3321 C  CB  . ILE B 1 155 ? -13.492 -18.896 -7.860  1.00 64.74  ? 1625 ILE B CB  1 
ATOM   3322 C  CG1 . ILE B 1 155 ? -12.512 -20.054 -7.641  1.00 61.63  ? 1625 ILE B CG1 1 
ATOM   3323 C  CG2 . ILE B 1 155 ? -13.469 -17.884 -6.708  1.00 52.50  ? 1625 ILE B CG2 1 
ATOM   3324 C  CD1 . ILE B 1 155 ? -11.100 -19.627 -7.258  1.00 50.69  ? 1625 ILE B CD1 1 
ATOM   3325 N  N   . PRO B 1 156 ? -16.871 -18.133 -7.361  1.00 73.79  ? 1626 PRO B N   1 
ATOM   3326 C  CA  . PRO B 1 156 ? -17.892 -17.093 -7.558  1.00 75.22  ? 1626 PRO B CA  1 
ATOM   3327 C  C   . PRO B 1 156 ? -17.377 -15.704 -7.214  1.00 65.45  ? 1626 PRO B C   1 
ATOM   3328 O  O   . PRO B 1 156 ? -16.541 -15.521 -6.328  1.00 66.86  ? 1626 PRO B O   1 
ATOM   3329 C  CB  . PRO B 1 156 ? -19.017 -17.516 -6.602  1.00 70.64  ? 1626 PRO B CB  1 
ATOM   3330 C  CG  . PRO B 1 156 ? -18.293 -18.256 -5.498  1.00 76.31  ? 1626 PRO B CG  1 
ATOM   3331 C  CD  . PRO B 1 156 ? -17.103 -18.931 -6.143  1.00 71.84  ? 1626 PRO B CD  1 
ATOM   3332 N  N   . PHE B 1 157 ? -17.892 -14.709 -7.930  1.00 93.85  ? 1627 PHE B N   1 
ATOM   3333 C  CA  . PHE B 1 157 ? -17.491 -13.331 -7.667  1.00 100.37 ? 1627 PHE B CA  1 
ATOM   3334 C  C   . PHE B 1 157 ? -18.473 -12.611 -6.761  1.00 97.66  ? 1627 PHE B C   1 
ATOM   3335 O  O   . PHE B 1 157 ? -18.067 -11.992 -5.772  1.00 90.36  ? 1627 PHE B O   1 
ATOM   3336 C  CB  . PHE B 1 157 ? -17.363 -12.561 -8.979  1.00 103.66 ? 1627 PHE B CB  1 
ATOM   3337 C  CG  . PHE B 1 157 ? -16.443 -13.206 -9.946  1.00 102.70 ? 1627 PHE B CG  1 
ATOM   3338 C  CD1 . PHE B 1 157 ? -15.318 -13.874 -9.494  1.00 85.05  ? 1627 PHE B CD1 1 
ATOM   3339 C  CD2 . PHE B 1 157 ? -16.725 -13.193 -11.300 1.00 110.57 ? 1627 PHE B CD2 1 
ATOM   3340 C  CE1 . PHE B 1 157 ? -14.477 -14.485 -10.374 1.00 96.73  ? 1627 PHE B CE1 1 
ATOM   3341 C  CE2 . PHE B 1 157 ? -15.885 -13.811 -12.192 1.00 113.70 ? 1627 PHE B CE2 1 
ATOM   3342 C  CZ  . PHE B 1 157 ? -14.758 -14.457 -11.729 1.00 112.13 ? 1627 PHE B CZ  1 
ATOM   3343 N  N   . GLU B 1 158 ? -19.762 -12.728 -7.051  1.00 108.83 ? 1628 GLU B N   1 
ATOM   3344 C  CA  . GLU B 1 158 ? -20.787 -12.146 -6.196  1.00 119.17 ? 1628 GLU B CA  1 
ATOM   3345 C  C   . GLU B 1 158 ? -21.032 -13.100 -5.037  1.00 112.18 ? 1628 GLU B C   1 
ATOM   3346 O  O   . GLU B 1 158 ? -21.703 -14.124 -5.186  1.00 127.20 ? 1628 GLU B O   1 
ATOM   3347 C  CB  . GLU B 1 158 ? -22.061 -11.882 -6.992  1.00 130.92 ? 1628 GLU B CB  1 
ATOM   3348 N  N   . VAL B 1 159 ? -20.467 -12.775 -3.880  1.00 83.37  ? 1629 VAL B N   1 
ATOM   3349 C  CA  . VAL B 1 159 ? -20.671 -13.560 -2.664  1.00 83.99  ? 1629 VAL B CA  1 
ATOM   3350 C  C   . VAL B 1 159 ? -20.922 -12.599 -1.519  1.00 88.57  ? 1629 VAL B C   1 
ATOM   3351 O  O   . VAL B 1 159 ? -20.630 -11.396 -1.625  1.00 80.74  ? 1629 VAL B O   1 
ATOM   3352 C  CB  . VAL B 1 159 ? -19.475 -14.484 -2.341  1.00 71.63  ? 1629 VAL B CB  1 
ATOM   3353 C  CG1 . VAL B 1 159 ? -19.206 -15.433 -3.488  1.00 78.86  ? 1629 VAL B CG1 1 
ATOM   3354 C  CG2 . VAL B 1 159 ? -18.252 -13.674 -1.991  1.00 76.34  ? 1629 VAL B CG2 1 
ATOM   3355 N  N   . PRO B 1 160 ? -21.490 -13.087 -0.416  1.00 100.51 ? 1630 PRO B N   1 
ATOM   3356 C  CA  . PRO B 1 160 ? -21.726 -12.199 0.726   1.00 103.32 ? 1630 PRO B CA  1 
ATOM   3357 C  C   . PRO B 1 160 ? -20.431 -11.554 1.187   1.00 85.61  ? 1630 PRO B C   1 
ATOM   3358 O  O   . PRO B 1 160 ? -19.438 -12.232 1.447   1.00 87.32  ? 1630 PRO B O   1 
ATOM   3359 C  CB  . PRO B 1 160 ? -22.302 -13.138 1.796   1.00 103.75 ? 1630 PRO B CB  1 
ATOM   3360 C  CG  . PRO B 1 160 ? -21.997 -14.533 1.316   1.00 99.88  ? 1630 PRO B CG  1 
ATOM   3361 C  CD  . PRO B 1 160 ? -22.014 -14.444 -0.168  1.00 101.52 ? 1630 PRO B CD  1 
ATOM   3362 N  N   . LEU B 1 161 ? -20.454 -10.233 1.297   1.00 81.21  ? 1631 LEU B N   1 
ATOM   3363 C  CA  . LEU B 1 161 ? -19.303 -9.500  1.788   1.00 76.43  ? 1631 LEU B CA  1 
ATOM   3364 C  C   . LEU B 1 161 ? -19.354 -9.478  3.309   1.00 76.58  ? 1631 LEU B C   1 
ATOM   3365 O  O   . LEU B 1 161 ? -20.344 -8.992  3.873   1.00 80.82  ? 1631 LEU B O   1 
ATOM   3366 C  CB  . LEU B 1 161 ? -19.286 -8.093  1.231   1.00 77.84  ? 1631 LEU B CB  1 
ATOM   3367 C  CG  . LEU B 1 161 ? -17.885 -7.565  0.925   1.00 78.92  ? 1631 LEU B CG  1 
ATOM   3368 C  CD1 . LEU B 1 161 ? -17.961 -6.308  0.077   1.00 94.13  ? 1631 LEU B CD1 1 
ATOM   3369 C  CD2 . LEU B 1 161 ? -17.149 -7.291  2.204   1.00 69.99  ? 1631 LEU B CD2 1 
ATOM   3370 N  N   . PRO B 1 162 ? -18.331 -9.983  4.005   1.00 70.06  ? 1632 PRO B N   1 
ATOM   3371 C  CA  . PRO B 1 162 ? -18.396 -10.058 5.470   1.00 73.73  ? 1632 PRO B CA  1 
ATOM   3372 C  C   . PRO B 1 162 ? -18.533 -8.689  6.120   1.00 83.41  ? 1632 PRO B C   1 
ATOM   3373 O  O   . PRO B 1 162 ? -18.034 -7.675  5.620   1.00 76.90  ? 1632 PRO B O   1 
ATOM   3374 C  CB  . PRO B 1 162 ? -17.065 -10.715 5.854   1.00 75.00  ? 1632 PRO B CB  1 
ATOM   3375 C  CG  . PRO B 1 162 ? -16.618 -11.444 4.619   1.00 74.34  ? 1632 PRO B CG  1 
ATOM   3376 C  CD  . PRO B 1 162 ? -17.110 -10.609 3.470   1.00 70.68  ? 1632 PRO B CD  1 
ATOM   3377 N  N   . ALA B 1 163 ? -19.224 -8.674  7.260   1.00 75.47  ? 1633 ALA B N   1 
ATOM   3378 C  CA  . ALA B 1 163 ? -19.380 -7.432  8.002   1.00 89.65  ? 1633 ALA B CA  1 
ATOM   3379 C  C   . ALA B 1 163 ? -18.119 -7.074  8.774   1.00 77.67  ? 1633 ALA B C   1 
ATOM   3380 O  O   . ALA B 1 163 ? -17.864 -5.891  9.022   1.00 71.08  ? 1633 ALA B O   1 
ATOM   3381 C  CB  . ALA B 1 163 ? -20.574 -7.534  8.952   1.00 91.34  ? 1633 ALA B CB  1 
ATOM   3382 N  N   . LYS B 1 164 ? -17.325 -8.066  9.156   1.00 60.64  ? 1634 LYS B N   1 
ATOM   3383 C  CA  . LYS B 1 164 ? -16.125 -7.835  9.941   1.00 67.71  ? 1634 LYS B CA  1 
ATOM   3384 C  C   . LYS B 1 164 ? -14.953 -8.526  9.265   1.00 70.27  ? 1634 LYS B C   1 
ATOM   3385 O  O   . LYS B 1 164 ? -15.121 -9.464  8.483   1.00 74.59  ? 1634 LYS B O   1 
ATOM   3386 C  CB  . LYS B 1 164 ? -16.274 -8.344  11.384  1.00 73.77  ? 1634 LYS B CB  1 
ATOM   3387 N  N   . GLN B 1 165 ? -13.760 -8.036  9.570   1.00 72.28  ? 1635 GLN B N   1 
ATOM   3388 C  CA  . GLN B 1 165 ? -12.535 -8.603  9.029   1.00 71.13  ? 1635 GLN B CA  1 
ATOM   3389 C  C   . GLN B 1 165 ? -12.129 -9.812  9.852   1.00 71.79  ? 1635 GLN B C   1 
ATOM   3390 O  O   . GLN B 1 165 ? -11.962 -9.714  11.073  1.00 63.13  ? 1635 GLN B O   1 
ATOM   3391 C  CB  . GLN B 1 165 ? -11.421 -7.564  9.032   1.00 66.44  ? 1635 GLN B CB  1 
ATOM   3392 C  CG  . GLN B 1 165 ? -11.191 -6.906  7.699   1.00 76.38  ? 1635 GLN B CG  1 
ATOM   3393 C  CD  . GLN B 1 165 ? -10.203 -5.777  7.811   1.00 85.20  ? 1635 GLN B CD  1 
ATOM   3394 O  OE1 . GLN B 1 165 ? -9.038  -5.981  8.185   1.00 90.50  ? 1635 GLN B OE1 1 
ATOM   3395 N  NE2 . GLN B 1 165 ? -10.654 -4.576  7.496   1.00 80.78  ? 1635 GLN B NE2 1 
ATOM   3396 N  N   . HIS B 1 166 ? -11.954 -10.949 9.187   1.00 69.22  ? 1636 HIS B N   1 
ATOM   3397 C  CA  . HIS B 1 166 ? -11.581 -12.139 9.929   1.00 63.81  ? 1636 HIS B CA  1 
ATOM   3398 C  C   . HIS B 1 166 ? -10.133 -12.065 10.390  1.00 59.28  ? 1636 HIS B C   1 
ATOM   3399 O  O   . HIS B 1 166 ? -9.823  -12.434 11.532  1.00 51.88  ? 1636 HIS B O   1 
ATOM   3400 C  CB  . HIS B 1 166 ? -11.813 -13.388 9.076   1.00 58.17  ? 1636 HIS B CB  1 
ATOM   3401 C  CG  . HIS B 1 166 ? -11.313 -14.649 9.710   1.00 67.59  ? 1636 HIS B CG  1 
ATOM   3402 N  ND1 . HIS B 1 166 ? -12.097 -15.429 10.535  1.00 73.47  ? 1636 HIS B ND1 1 
ATOM   3403 C  CD2 . HIS B 1 166 ? -10.113 -15.269 9.638   1.00 74.20  ? 1636 HIS B CD2 1 
ATOM   3404 C  CE1 . HIS B 1 166 ? -11.401 -16.475 10.940  1.00 73.01  ? 1636 HIS B CE1 1 
ATOM   3405 N  NE2 . HIS B 1 166 ? -10.195 -16.404 10.409  1.00 73.76  ? 1636 HIS B NE2 1 
ATOM   3406 N  N   . VAL B 1 167 ? -9.243  -11.521 9.562   1.00 53.55  ? 1637 VAL B N   1 
ATOM   3407 C  CA  . VAL B 1 167 ? -7.820  -11.667 9.865   1.00 46.90  ? 1637 VAL B CA  1 
ATOM   3408 C  C   . VAL B 1 167 ? -7.336  -10.478 10.688  1.00 62.26  ? 1637 VAL B C   1 
ATOM   3409 O  O   . VAL B 1 167 ? -7.659  -9.314  10.374  1.00 67.94  ? 1637 VAL B O   1 
ATOM   3410 C  CB  . VAL B 1 167 ? -6.995  -11.861 8.582   1.00 60.16  ? 1637 VAL B CB  1 
ATOM   3411 C  CG1 . VAL B 1 167 ? -5.506  -11.772 8.887   1.00 67.57  ? 1637 VAL B CG1 1 
ATOM   3412 C  CG2 . VAL B 1 167 ? -7.296  -13.228 7.953   1.00 52.02  ? 1637 VAL B CG2 1 
ATOM   3413 N  N   . PRO B 1 168 ? -6.602  -10.728 11.776  1.00 67.55  ? 1638 PRO B N   1 
ATOM   3414 C  CA  . PRO B 1 168 ? -6.137  -9.620  12.613  1.00 80.65  ? 1638 PRO B CA  1 
ATOM   3415 C  C   . PRO B 1 168 ? -5.228  -8.689  11.825  1.00 86.41  ? 1638 PRO B C   1 
ATOM   3416 O  O   . PRO B 1 168 ? -4.556  -9.097  10.872  1.00 81.07  ? 1638 PRO B O   1 
ATOM   3417 C  CB  . PRO B 1 168 ? -5.375  -10.322 13.744  1.00 73.55  ? 1638 PRO B CB  1 
ATOM   3418 C  CG  . PRO B 1 168 ? -5.933  -11.682 13.793  1.00 74.49  ? 1638 PRO B CG  1 
ATOM   3419 C  CD  . PRO B 1 168 ? -6.339  -12.039 12.392  1.00 77.50  ? 1638 PRO B CD  1 
ATOM   3420 N  N   . GLU B 1 169 ? -5.192  -7.428  12.264  1.00 83.83  ? 1639 GLU B N   1 
ATOM   3421 C  CA  . GLU B 1 169 ? -4.536  -6.392  11.477  1.00 75.81  ? 1639 GLU B CA  1 
ATOM   3422 C  C   . GLU B 1 169 ? -3.062  -6.706  11.276  1.00 65.65  ? 1639 GLU B C   1 
ATOM   3423 O  O   . GLU B 1 169 ? -2.522  -6.496  10.184  1.00 75.25  ? 1639 GLU B O   1 
ATOM   3424 C  CB  . GLU B 1 169 ? -4.718  -5.025  12.149  1.00 79.55  ? 1639 GLU B CB  1 
ATOM   3425 N  N   . ALA B 1 170 ? -2.406  -7.262  12.296  1.00 62.45  ? 1640 ALA B N   1 
ATOM   3426 C  CA  . ALA B 1 170 ? -0.976  -7.542  12.173  1.00 68.07  ? 1640 ALA B CA  1 
ATOM   3427 C  C   . ALA B 1 170 ? -0.699  -8.571  11.083  1.00 75.39  ? 1640 ALA B C   1 
ATOM   3428 O  O   . ALA B 1 170 ? 0.156   -8.355  10.212  1.00 88.47  ? 1640 ALA B O   1 
ATOM   3429 C  CB  . ALA B 1 170 ? -0.414  -8.026  13.510  1.00 67.06  ? 1640 ALA B CB  1 
ATOM   3430 N  N   . GLU B 1 171 ? -1.431  -9.689  11.099  1.00 64.93  ? 1641 GLU B N   1 
ATOM   3431 C  CA  . GLU B 1 171 ? -1.213  -10.730 10.094  1.00 76.29  ? 1641 GLU B CA  1 
ATOM   3432 C  C   . GLU B 1 171 ? -1.593  -10.234 8.701   1.00 69.23  ? 1641 GLU B C   1 
ATOM   3433 O  O   . GLU B 1 171 ? -0.936  -10.578 7.700   1.00 75.06  ? 1641 GLU B O   1 
ATOM   3434 C  CB  . GLU B 1 171 ? -2.014  -11.990 10.452  1.00 82.67  ? 1641 GLU B CB  1 
ATOM   3435 C  CG  . GLU B 1 171 ? -1.443  -12.825 11.607  1.00 85.15  ? 1641 GLU B CG  1 
ATOM   3436 C  CD  . GLU B 1 171 ? -2.108  -12.535 12.957  1.00 97.12  ? 1641 GLU B CD  1 
ATOM   3437 O  OE1 . GLU B 1 171 ? -2.598  -11.399 13.169  1.00 95.17  ? 1641 GLU B OE1 1 
ATOM   3438 O  OE2 . GLU B 1 171 ? -2.152  -13.459 13.804  1.00 100.50 ? 1641 GLU B OE2 1 
ATOM   3439 N  N   . ARG B 1 172 ? -2.662  -9.436  8.619   1.00 60.98  ? 1642 ARG B N   1 
ATOM   3440 C  CA  . ARG B 1 172 ? -3.016  -8.823  7.349   1.00 62.34  ? 1642 ARG B CA  1 
ATOM   3441 C  C   . ARG B 1 172 ? -1.872  -7.989  6.812   1.00 65.72  ? 1642 ARG B C   1 
ATOM   3442 O  O   . ARG B 1 172 ? -1.590  -8.020  5.610   1.00 59.13  ? 1642 ARG B O   1 
ATOM   3443 C  CB  . ARG B 1 172 ? -4.247  -7.949  7.479   1.00 56.15  ? 1642 ARG B CB  1 
ATOM   3444 C  CG  . ARG B 1 172 ? -4.515  -7.286  6.162   1.00 64.96  ? 1642 ARG B CG  1 
ATOM   3445 C  CD  . ARG B 1 172 ? -5.452  -6.166  6.323   1.00 74.61  ? 1642 ARG B CD  1 
ATOM   3446 N  NE  . ARG B 1 172 ? -5.269  -5.530  7.614   1.00 90.87  ? 1642 ARG B NE  1 
ATOM   3447 C  CZ  . ARG B 1 172 ? -5.859  -4.394  7.960   1.00 97.61  ? 1642 ARG B CZ  1 
ATOM   3448 N  NH1 . ARG B 1 172 ? -6.659  -3.776  7.096   1.00 98.13  ? 1642 ARG B NH1 1 
ATOM   3449 N  NH2 . ARG B 1 172 ? -5.642  -3.876  9.161   1.00 98.73  ? 1642 ARG B NH2 1 
ATOM   3450 N  N   . GLU B 1 173 ? -1.201  -7.237  7.695   1.00 71.91  ? 1643 GLU B N   1 
ATOM   3451 C  CA  . GLU B 1 173 ? -0.103  -6.371  7.265   1.00 76.38  ? 1643 GLU B CA  1 
ATOM   3452 C  C   . GLU B 1 173 ? 1.127   -7.185  6.885   1.00 72.89  ? 1643 GLU B C   1 
ATOM   3453 O  O   . GLU B 1 173 ? 1.913   -6.745  6.039   1.00 69.99  ? 1643 GLU B O   1 
ATOM   3454 C  CB  . GLU B 1 173 ? 0.250   -5.357  8.355   1.00 57.18  ? 1643 GLU B CB  1 
ATOM   3455 C  CG  . GLU B 1 173 ? -0.825  -4.306  8.627   1.00 67.76  ? 1643 GLU B CG  1 
ATOM   3456 C  CD  . GLU B 1 173 ? -1.440  -3.738  7.361   1.00 80.86  ? 1643 GLU B CD  1 
ATOM   3457 O  OE1 . GLU B 1 173 ? -0.723  -3.059  6.599   1.00 85.82  ? 1643 GLU B OE1 1 
ATOM   3458 O  OE2 . GLU B 1 173 ? -2.639  -3.982  7.119   1.00 84.35  ? 1643 GLU B OE2 1 
ATOM   3459 N  N   . GLU B 1 174 ? 1.316   -8.366  7.485   1.00 54.26  ? 1644 GLU B N   1 
ATOM   3460 C  CA  . GLU B 1 174 ? 2.388   -9.236  6.999   1.00 73.68  ? 1644 GLU B CA  1 
ATOM   3461 C  C   . GLU B 1 174 ? 2.100   -9.707  5.574   1.00 72.34  ? 1644 GLU B C   1 
ATOM   3462 O  O   . GLU B 1 174 ? 2.995   -9.738  4.709   1.00 67.00  ? 1644 GLU B O   1 
ATOM   3463 C  CB  . GLU B 1 174 ? 2.591   -10.425 7.942   1.00 90.38  ? 1644 GLU B CB  1 
ATOM   3464 C  CG  . GLU B 1 174 ? 3.629   -10.149 9.035   1.00 104.34 ? 1644 GLU B CG  1 
ATOM   3465 C  CD  . GLU B 1 174 ? 3.085   -9.310  10.183  1.00 113.46 ? 1644 GLU B CD  1 
ATOM   3466 O  OE1 . GLU B 1 174 ? 2.177   -9.804  10.888  1.00 111.54 ? 1644 GLU B OE1 1 
ATOM   3467 O  OE2 . GLU B 1 174 ? 3.542   -8.154  10.367  1.00 114.47 ? 1644 GLU B OE2 1 
ATOM   3468 N  N   . VAL B 1 175 ? 0.843   -10.056 5.309   1.00 71.79  ? 1645 VAL B N   1 
ATOM   3469 C  CA  . VAL B 1 175 ? 0.456   -10.413 3.946   1.00 66.44  ? 1645 VAL B CA  1 
ATOM   3470 C  C   . VAL B 1 175 ? 0.647   -9.219  3.010   1.00 73.08  ? 1645 VAL B C   1 
ATOM   3471 O  O   . VAL B 1 175 ? 1.124   -9.357  1.874   1.00 58.92  ? 1645 VAL B O   1 
ATOM   3472 C  CB  . VAL B 1 175 ? -0.998  -10.919 3.932   1.00 51.39  ? 1645 VAL B CB  1 
ATOM   3473 C  CG1 . VAL B 1 175 ? -1.523  -10.995 2.523   1.00 46.49  ? 1645 VAL B CG1 1 
ATOM   3474 C  CG2 . VAL B 1 175 ? -1.077  -12.287 4.600   1.00 61.28  ? 1645 VAL B CG2 1 
ATOM   3475 N  N   . ARG B 1 176 ? 0.272   -8.032  3.479   1.00 54.19  ? 1646 ARG B N   1 
ATOM   3476 C  CA  . ARG B 1 176 ? 0.369   -6.824  2.676   1.00 62.71  ? 1646 ARG B CA  1 
ATOM   3477 C  C   . ARG B 1 176 ? 1.818   -6.515  2.306   1.00 72.79  ? 1646 ARG B C   1 
ATOM   3478 O  O   . ARG B 1 176 ? 2.116   -6.209  1.142   1.00 60.35  ? 1646 ARG B O   1 
ATOM   3479 C  CB  . ARG B 1 176 ? -0.258  -5.665  3.440   1.00 58.91  ? 1646 ARG B CB  1 
ATOM   3480 C  CG  . ARG B 1 176 ? -0.279  -4.381  2.667   1.00 62.94  ? 1646 ARG B CG  1 
ATOM   3481 C  CD  . ARG B 1 176 ? -1.204  -3.394  3.330   1.00 64.78  ? 1646 ARG B CD  1 
ATOM   3482 N  NE  . ARG B 1 176 ? -2.452  -3.283  2.590   1.00 70.96  ? 1646 ARG B NE  1 
ATOM   3483 C  CZ  . ARG B 1 176 ? -3.650  -3.376  3.149   1.00 75.92  ? 1646 ARG B CZ  1 
ATOM   3484 N  NH1 . ARG B 1 176 ? -3.753  -3.571  4.460   1.00 73.78  ? 1646 ARG B NH1 1 
ATOM   3485 N  NH2 . ARG B 1 176 ? -4.740  -3.273  2.398   1.00 72.34  ? 1646 ARG B NH2 1 
ATOM   3486 N  N   . ASP B 1 177 ? 2.731   -6.621  3.281   1.00 74.72  ? 1647 ASP B N   1 
ATOM   3487 C  CA  . ASP B 1 177 ? 4.155   -6.442  3.009   1.00 72.60  ? 1647 ASP B CA  1 
ATOM   3488 C  C   . ASP B 1 177 ? 4.613   -7.403  1.924   1.00 68.10  ? 1647 ASP B C   1 
ATOM   3489 O  O   . ASP B 1 177 ? 5.227   -6.995  0.920   1.00 74.09  ? 1647 ASP B O   1 
ATOM   3490 C  CB  . ASP B 1 177 ? 4.983   -6.669  4.287   1.00 78.15  ? 1647 ASP B CB  1 
ATOM   3491 C  CG  . ASP B 1 177 ? 4.768   -5.585  5.348   1.00 72.12  ? 1647 ASP B CG  1 
ATOM   3492 O  OD1 . ASP B 1 177 ? 4.180   -4.540  5.034   1.00 59.88  ? 1647 ASP B OD1 1 
ATOM   3493 O  OD2 . ASP B 1 177 ? 5.186   -5.784  6.510   1.00 75.21  ? 1647 ASP B OD2 1 
ATOM   3494 N  N   . TRP B 1 178 ? 4.310   -8.693  2.107   1.00 62.37  ? 1648 TRP B N   1 
ATOM   3495 C  CA  . TRP B 1 178 ? 4.797   -9.705  1.174   1.00 62.98  ? 1648 TRP B CA  1 
ATOM   3496 C  C   . TRP B 1 178 ? 4.235   -9.495  -0.233  1.00 60.45  ? 1648 TRP B C   1 
ATOM   3497 O  O   . TRP B 1 178 ? 4.967   -9.576  -1.233  1.00 69.59  ? 1648 TRP B O   1 
ATOM   3498 C  CB  . TRP B 1 178 ? 4.452   -11.098 1.703   1.00 65.43  ? 1648 TRP B CB  1 
ATOM   3499 C  CG  . TRP B 1 178 ? 4.918   -12.167 0.789   1.00 72.64  ? 1648 TRP B CG  1 
ATOM   3500 C  CD1 . TRP B 1 178 ? 6.180   -12.671 0.690   1.00 72.97  ? 1648 TRP B CD1 1 
ATOM   3501 C  CD2 . TRP B 1 178 ? 4.134   -12.844 -0.191  1.00 73.31  ? 1648 TRP B CD2 1 
ATOM   3502 N  NE1 . TRP B 1 178 ? 6.229   -13.633 -0.291  1.00 77.68  ? 1648 TRP B NE1 1 
ATOM   3503 C  CE2 . TRP B 1 178 ? 4.982   -13.758 -0.845  1.00 72.86  ? 1648 TRP B CE2 1 
ATOM   3504 C  CE3 . TRP B 1 178 ? 2.795   -12.767 -0.581  1.00 73.84  ? 1648 TRP B CE3 1 
ATOM   3505 C  CZ2 . TRP B 1 178 ? 4.533   -14.595 -1.861  1.00 73.82  ? 1648 TRP B CZ2 1 
ATOM   3506 C  CZ3 . TRP B 1 178 ? 2.352   -13.594 -1.590  1.00 69.27  ? 1648 TRP B CZ3 1 
ATOM   3507 C  CH2 . TRP B 1 178 ? 3.218   -14.499 -2.218  1.00 67.66  ? 1648 TRP B CH2 1 
ATOM   3508 N  N   . VAL B 1 179 ? 2.931   -9.229  -0.329  1.00 55.45  ? 1649 VAL B N   1 
ATOM   3509 C  CA  . VAL B 1 179 ? 2.290   -9.026  -1.625  1.00 55.62  ? 1649 VAL B CA  1 
ATOM   3510 C  C   . VAL B 1 179 ? 2.887   -7.820  -2.345  1.00 66.39  ? 1649 VAL B C   1 
ATOM   3511 O  O   . VAL B 1 179 ? 3.114   -7.858  -3.561  1.00 58.07  ? 1649 VAL B O   1 
ATOM   3512 C  CB  . VAL B 1 179 ? 0.765   -8.878  -1.452  1.00 52.75  ? 1649 VAL B CB  1 
ATOM   3513 C  CG1 . VAL B 1 179 ? 0.133   -8.313  -2.724  1.00 54.33  ? 1649 VAL B CG1 1 
ATOM   3514 C  CG2 . VAL B 1 179 ? 0.121   -10.220 -1.069  1.00 50.79  ? 1649 VAL B CG2 1 
ATOM   3515 N  N   . LEU B 1 180 ? 3.140   -6.726  -1.617  1.00 76.25  ? 1650 LEU B N   1 
ATOM   3516 C  CA  . LEU B 1 180 ? 3.732   -5.548  -2.253  1.00 75.41  ? 1650 LEU B CA  1 
ATOM   3517 C  C   . LEU B 1 180 ? 5.104   -5.881  -2.837  1.00 64.25  ? 1650 LEU B C   1 
ATOM   3518 O  O   . LEU B 1 180 ? 5.381   -5.607  -4.024  1.00 66.04  ? 1650 LEU B O   1 
ATOM   3519 C  CB  . LEU B 1 180 ? 3.808   -4.405  -1.239  1.00 63.42  ? 1650 LEU B CB  1 
ATOM   3520 C  CG  . LEU B 1 180 ? 2.425   -3.820  -0.963  1.00 63.80  ? 1650 LEU B CG  1 
ATOM   3521 C  CD1 . LEU B 1 180 ? 2.448   -2.887  0.238   1.00 58.06  ? 1650 LEU B CD1 1 
ATOM   3522 C  CD2 . LEU B 1 180 ? 1.885   -3.110  -2.207  1.00 60.17  ? 1650 LEU B CD2 1 
ATOM   3523 N  N   . THR B 1 181 ? 5.948   -6.538  -2.029  1.00 78.82  ? 1651 THR B N   1 
ATOM   3524 C  CA  . THR B 1 181 ? 7.275   -6.935  -2.497  1.00 94.69  ? 1651 THR B CA  1 
ATOM   3525 C  C   . THR B 1 181 ? 7.185   -7.742  -3.792  1.00 89.98  ? 1651 THR B C   1 
ATOM   3526 O  O   . THR B 1 181 ? 7.862   -7.433  -4.787  1.00 93.50  ? 1651 THR B O   1 
ATOM   3527 C  CB  . THR B 1 181 ? 7.989   -7.762  -1.413  1.00 105.98 ? 1651 THR B CB  1 
ATOM   3528 O  OG1 . THR B 1 181 ? 8.356   -6.923  -0.306  1.00 118.02 ? 1651 THR B OG1 1 
ATOM   3529 C  CG2 . THR B 1 181 ? 9.235   -8.435  -1.974  1.00 92.49  ? 1651 THR B CG2 1 
ATOM   3530 N  N   . VAL B 1 182 ? 6.334   -8.772  -3.804  1.00 66.30  ? 1652 VAL B N   1 
ATOM   3531 C  CA  . VAL B 1 182 ? 6.283   -9.647  -4.971  1.00 58.62  ? 1652 VAL B CA  1 
ATOM   3532 C  C   . VAL B 1 182 ? 5.735   -8.893  -6.183  1.00 69.16  ? 1652 VAL B C   1 
ATOM   3533 O  O   . VAL B 1 182 ? 6.192   -9.096  -7.321  1.00 71.69  ? 1652 VAL B O   1 
ATOM   3534 C  CB  . VAL B 1 182 ? 5.458   -10.904 -4.649  1.00 73.10  ? 1652 VAL B CB  1 
ATOM   3535 C  CG1 . VAL B 1 182 ? 5.256   -11.746 -5.908  1.00 60.63  ? 1652 VAL B CG1 1 
ATOM   3536 C  CG2 . VAL B 1 182 ? 6.151   -11.730 -3.555  1.00 73.38  ? 1652 VAL B CG2 1 
ATOM   3537 N  N   . SER B 1 183 ? 4.769   -7.985  -5.955  1.00 72.83  ? 1653 SER B N   1 
ATOM   3538 C  CA  . SER B 1 183 ? 4.247   -7.120  -7.023  1.00 86.09  ? 1653 SER B CA  1 
ATOM   3539 C  C   . SER B 1 183 ? 5.377   -6.477  -7.799  1.00 92.21  ? 1653 SER B C   1 
ATOM   3540 O  O   . SER B 1 183 ? 5.483   -6.658  -9.016  1.00 104.49 ? 1653 SER B O   1 
ATOM   3541 C  CB  . SER B 1 183 ? 3.335   -6.011  -6.460  1.00 87.90  ? 1653 SER B CB  1 
ATOM   3542 O  OG  . SER B 1 183 ? 2.457   -6.456  -5.417  1.00 93.70  ? 1653 SER B OG  1 
ATOM   3543 N  N   . MET B 1 184 ? 6.278   -5.796  -7.095  1.00 89.98  ? 1654 MET B N   1 
ATOM   3544 C  CA  . MET B 1 184 ? 7.365   -5.127  -7.822  1.00 92.92  ? 1654 MET B CA  1 
ATOM   3545 C  C   . MET B 1 184 ? 8.500   -6.070  -8.210  1.00 111.36 ? 1654 MET B C   1 
ATOM   3546 O  O   . MET B 1 184 ? 9.405   -5.650  -8.955  1.00 109.08 ? 1654 MET B O   1 
ATOM   3547 C  CB  . MET B 1 184 ? 7.990   -3.963  -7.058  1.00 74.16  ? 1654 MET B CB  1 
ATOM   3548 C  CG  . MET B 1 184 ? 7.180   -2.678  -7.046  1.00 74.16  ? 1654 MET B CG  1 
ATOM   3549 S  SD  . MET B 1 184 ? 6.059   -2.816  -5.668  1.00 107.85 ? 1654 MET B SD  1 
ATOM   3550 C  CE  . MET B 1 184 ? 7.284   -3.056  -4.373  1.00 102.64 ? 1654 MET B CE  1 
ATOM   3551 N  N   . ASP B 1 185 ? 8.497   -7.318  -7.723  1.00 118.09 ? 1655 ASP B N   1 
ATOM   3552 C  CA  . ASP B 1 185 ? 9.585   -8.213  -8.100  1.00 122.23 ? 1655 ASP B CA  1 
ATOM   3553 C  C   . ASP B 1 185 ? 9.645   -8.469  -9.601  1.00 123.42 ? 1655 ASP B C   1 
ATOM   3554 O  O   . ASP B 1 185 ? 10.638  -9.043  -10.065 1.00 130.65 ? 1655 ASP B O   1 
ATOM   3555 C  CB  . ASP B 1 185 ? 9.444   -9.544  -7.359  1.00 119.29 ? 1655 ASP B CB  1 
ATOM   3556 N  N   . GLN B 1 186 ? 8.630   -8.037  -10.361 1.00 112.01 ? 1656 GLN B N   1 
ATOM   3557 C  CA  . GLN B 1 186 ? 8.634   -8.017  -11.825 1.00 117.11 ? 1656 GLN B CA  1 
ATOM   3558 C  C   . GLN B 1 186 ? 9.237   -9.287  -12.410 1.00 128.59 ? 1656 GLN B C   1 
ATOM   3559 O  O   . GLN B 1 186 ? 9.841   -9.267  -13.489 1.00 121.06 ? 1656 GLN B O   1 
ATOM   3560 C  CB  . GLN B 1 186 ? 9.388   -6.788  -12.346 1.00 110.56 ? 1656 GLN B CB  1 
ATOM   3561 N  N   . ARG B 1 187 ? 9.085   -10.392 -11.685 1.00 133.36 ? 1657 ARG B N   1 
ATOM   3562 C  CA  . ARG B 1 187 ? 9.652   -11.674 -12.063 1.00 137.88 ? 1657 ARG B CA  1 
ATOM   3563 C  C   . ARG B 1 187 ? 8.593   -12.626 -12.592 1.00 145.59 ? 1657 ARG B C   1 
ATOM   3564 O  O   . ARG B 1 187 ? 8.743   -13.179 -13.686 1.00 149.56 ? 1657 ARG B O   1 
ATOM   3565 C  CB  . ARG B 1 187 ? 10.369  -12.303 -10.860 1.00 133.30 ? 1657 ARG B CB  1 
ATOM   3566 N  N   . LEU B 1 188 ? 7.514   -12.808 -11.839 1.00 147.69 ? 1658 LEU B N   1 
ATOM   3567 C  CA  . LEU B 1 188 ? 6.501   -13.801 -12.152 1.00 148.88 ? 1658 LEU B CA  1 
ATOM   3568 C  C   . LEU B 1 188 ? 5.260   -13.158 -12.758 1.00 148.92 ? 1658 LEU B C   1 
ATOM   3569 O  O   . LEU B 1 188 ? 4.919   -12.008 -12.470 1.00 145.84 ? 1658 LEU B O   1 
ATOM   3570 C  CB  . LEU B 1 188 ? 6.108   -14.589 -10.898 1.00 143.42 ? 1658 LEU B CB  1 
ATOM   3571 N  N   . GLU B 1 189 ? 4.600   -13.924 -13.618 1.00 149.95 ? 1659 GLU B N   1 
ATOM   3572 C  CA  . GLU B 1 189 ? 3.254   -13.608 -14.064 1.00 148.85 ? 1659 GLU B CA  1 
ATOM   3573 C  C   . GLU B 1 189 ? 2.262   -14.135 -13.035 1.00 139.46 ? 1659 GLU B C   1 
ATOM   3574 O  O   . GLU B 1 189 ? 2.470   -15.193 -12.435 1.00 142.05 ? 1659 GLU B O   1 
ATOM   3575 C  CB  . GLU B 1 189 ? 2.980   -14.212 -15.441 1.00 151.07 ? 1659 GLU B CB  1 
ATOM   3576 N  N   . GLN B 1 190 ? 1.196   -13.375 -12.810 1.00 126.44 ? 1660 GLN B N   1 
ATOM   3577 C  CA  . GLN B 1 190 ? 0.202   -13.716 -11.798 1.00 109.64 ? 1660 GLN B CA  1 
ATOM   3578 C  C   . GLN B 1 190 ? -0.992  -14.339 -12.518 1.00 97.61  ? 1660 GLN B C   1 
ATOM   3579 O  O   . GLN B 1 190 ? -1.979  -13.677 -12.855 1.00 86.04  ? 1660 GLN B O   1 
ATOM   3580 C  CB  . GLN B 1 190 ? -0.189  -12.476 -10.993 1.00 114.32 ? 1660 GLN B CB  1 
ATOM   3581 N  N   . VAL B 1 191 ? -0.863  -15.643 -12.800 1.00 92.78  ? 1661 VAL B N   1 
ATOM   3582 C  CA  . VAL B 1 191 ? -1.925  -16.446 -13.399 1.00 92.50  ? 1661 VAL B CA  1 
ATOM   3583 C  C   . VAL B 1 191 ? -2.029  -17.776 -12.657 1.00 86.07  ? 1661 VAL B C   1 
ATOM   3584 O  O   . VAL B 1 191 ? -1.042  -18.291 -12.117 1.00 72.19  ? 1661 VAL B O   1 
ATOM   3585 C  CB  . VAL B 1 191 ? -1.692  -16.693 -14.917 1.00 93.56  ? 1661 VAL B CB  1 
ATOM   3586 C  CG1 . VAL B 1 191 ? -2.979  -17.164 -15.598 1.00 92.72  ? 1661 VAL B CG1 1 
ATOM   3587 C  CG2 . VAL B 1 191 ? -1.127  -15.438 -15.618 1.00 83.45  ? 1661 VAL B CG2 1 
ATOM   3588 N  N   . LEU B 1 192 ? -3.263  -18.325 -12.613 1.00 84.52  ? 1662 LEU B N   1 
ATOM   3589 C  CA  . LEU B 1 192 ? -3.552  -19.602 -11.977 1.00 85.99  ? 1662 LEU B CA  1 
ATOM   3590 C  C   . LEU B 1 192 ? -3.146  -20.778 -12.867 1.00 81.13  ? 1662 LEU B C   1 
ATOM   3591 O  O   . LEU B 1 192 ? -3.212  -20.688 -14.098 1.00 75.55  ? 1662 LEU B O   1 
ATOM   3592 C  CB  . LEU B 1 192 ? -5.036  -19.717 -11.632 1.00 85.64  ? 1662 LEU B CB  1 
ATOM   3593 C  CG  . LEU B 1 192 ? -5.703  -18.607 -10.823 1.00 75.43  ? 1662 LEU B CG  1 
ATOM   3594 C  CD1 . LEU B 1 192 ? -7.228  -18.720 -10.916 1.00 68.98  ? 1662 LEU B CD1 1 
ATOM   3595 C  CD2 . LEU B 1 192 ? -5.226  -18.685 -9.378  1.00 70.25  ? 1662 LEU B CD2 1 
ATOM   3596 N  N   . PRO B 1 193 ? -2.727  -21.893 -12.265 1.00 81.75  ? 1663 PRO B N   1 
ATOM   3597 C  CA  . PRO B 1 193 ? -2.308  -23.044 -13.073 1.00 78.52  ? 1663 PRO B CA  1 
ATOM   3598 C  C   . PRO B 1 193 ? -3.493  -23.662 -13.788 1.00 74.53  ? 1663 PRO B C   1 
ATOM   3599 O  O   . PRO B 1 193 ? -4.599  -23.736 -13.248 1.00 83.95  ? 1663 PRO B O   1 
ATOM   3600 C  CB  . PRO B 1 193 ? -1.714  -24.023 -12.049 1.00 68.45  ? 1663 PRO B CB  1 
ATOM   3601 C  CG  . PRO B 1 193 ? -1.643  -23.290 -10.760 1.00 74.81  ? 1663 PRO B CG  1 
ATOM   3602 C  CD  . PRO B 1 193 ? -2.624  -22.164 -10.823 1.00 73.82  ? 1663 PRO B CD  1 
ATOM   3603 N  N   . ARG B 1 194 ? -3.259  -24.074 -15.025 1.00 79.15  ? 1664 ARG B N   1 
ATOM   3604 C  CA  . ARG B 1 194 ? -4.239  -24.820 -15.792 1.00 87.69  ? 1664 ARG B CA  1 
ATOM   3605 C  C   . ARG B 1 194 ? -3.779  -26.270 -15.911 1.00 86.09  ? 1664 ARG B C   1 
ATOM   3606 O  O   . ARG B 1 194 ? -2.578  -26.568 -15.891 1.00 81.20  ? 1664 ARG B O   1 
ATOM   3607 C  CB  . ARG B 1 194 ? -4.459  -24.189 -17.170 1.00 92.90  ? 1664 ARG B CB  1 
ATOM   3608 C  CG  . ARG B 1 194 ? -4.870  -22.720 -17.090 1.00 102.92 ? 1664 ARG B CG  1 
ATOM   3609 C  CD  . ARG B 1 194 ? -5.512  -22.209 -18.380 1.00 112.04 ? 1664 ARG B CD  1 
ATOM   3610 N  NE  . ARG B 1 194 ? -6.975  -22.226 -18.330 1.00 118.62 ? 1664 ARG B NE  1 
ATOM   3611 C  CZ  . ARG B 1 194 ? -7.721  -21.368 -17.634 1.00 117.53 ? 1664 ARG B CZ  1 
ATOM   3612 N  NH1 . ARG B 1 194 ? -7.144  -20.412 -16.914 1.00 114.08 ? 1664 ARG B NH1 1 
ATOM   3613 N  NH2 . ARG B 1 194 ? -9.048  -21.466 -17.653 1.00 112.37 ? 1664 ARG B NH2 1 
ATOM   3614 N  N   . ASP B 1 195 ? -4.746  -27.167 -16.030 1.00 83.11  ? 1665 ASP B N   1 
ATOM   3615 C  CA  . ASP B 1 195 ? -4.473  -28.587 -16.121 1.00 81.56  ? 1665 ASP B CA  1 
ATOM   3616 C  C   . ASP B 1 195 ? -4.571  -29.034 -17.576 1.00 87.19  ? 1665 ASP B C   1 
ATOM   3617 O  O   . ASP B 1 195 ? -4.635  -28.217 -18.501 1.00 93.77  ? 1665 ASP B O   1 
ATOM   3618 C  CB  . ASP B 1 195 ? -5.419  -29.368 -15.196 1.00 79.31  ? 1665 ASP B CB  1 
ATOM   3619 C  CG  . ASP B 1 195 ? -6.898  -29.082 -15.464 1.00 78.65  ? 1665 ASP B CG  1 
ATOM   3620 O  OD1 . ASP B 1 195 ? -7.234  -28.587 -16.560 1.00 79.71  ? 1665 ASP B OD1 1 
ATOM   3621 O  OD2 . ASP B 1 195 ? -7.731  -29.348 -14.567 1.00 75.77  ? 1665 ASP B OD2 1 
ATOM   3622 N  N   . GLU B 1 196 ? -4.575  -30.352 -17.782 1.00 78.38  ? 1666 GLU B N   1 
ATOM   3623 C  CA  . GLU B 1 196 ? -4.664  -30.914 -19.124 1.00 77.58  ? 1666 GLU B CA  1 
ATOM   3624 C  C   . GLU B 1 196 ? -5.962  -30.546 -19.833 1.00 81.13  ? 1666 GLU B C   1 
ATOM   3625 O  O   . GLU B 1 196 ? -6.046  -30.710 -21.054 1.00 80.77  ? 1666 GLU B O   1 
ATOM   3626 C  CB  . GLU B 1 196 ? -4.540  -32.430 -19.043 1.00 87.21  ? 1666 GLU B CB  1 
ATOM   3627 C  CG  . GLU B 1 196 ? -5.568  -33.021 -18.100 1.00 92.12  ? 1666 GLU B CG  1 
ATOM   3628 C  CD  . GLU B 1 196 ? -5.605  -34.522 -18.134 1.00 95.98  ? 1666 GLU B CD  1 
ATOM   3629 O  OE1 . GLU B 1 196 ? -5.547  -35.132 -17.045 1.00 94.20  ? 1666 GLU B OE1 1 
ATOM   3630 O  OE2 . GLU B 1 196 ? -5.691  -35.091 -19.245 1.00 104.08 ? 1666 GLU B OE2 1 
ATOM   3631 N  N   . ARG B 1 197 ? -6.985  -30.085 -19.100 1.00 90.43  ? 1667 ARG B N   1 
ATOM   3632 C  CA  . ARG B 1 197 ? -8.234  -29.644 -19.716 1.00 86.06  ? 1667 ARG B CA  1 
ATOM   3633 C  C   . ARG B 1 197 ? -8.169  -28.219 -20.242 1.00 91.19  ? 1667 ARG B C   1 
ATOM   3634 O  O   . ARG B 1 197 ? -9.089  -27.801 -20.957 1.00 90.84  ? 1667 ARG B O   1 
ATOM   3635 C  CB  . ARG B 1 197 ? -9.392  -29.705 -18.717 1.00 85.72  ? 1667 ARG B CB  1 
ATOM   3636 C  CG  . ARG B 1 197 ? -9.596  -31.017 -18.021 1.00 87.01  ? 1667 ARG B CG  1 
ATOM   3637 C  CD  . ARG B 1 197 ? -9.783  -30.768 -16.530 1.00 88.58  ? 1667 ARG B CD  1 
ATOM   3638 N  NE  . ARG B 1 197 ? -11.155 -30.503 -16.116 1.00 83.90  ? 1667 ARG B NE  1 
ATOM   3639 C  CZ  . ARG B 1 197 ? -11.484 -29.643 -15.157 1.00 73.12  ? 1667 ARG B CZ  1 
ATOM   3640 N  NH1 . ARG B 1 197 ? -10.537 -28.962 -14.525 1.00 66.89  ? 1667 ARG B NH1 1 
ATOM   3641 N  NH2 . ARG B 1 197 ? -12.759 -29.462 -14.834 1.00 62.64  ? 1667 ARG B NH2 1 
ATOM   3642 N  N   . GLY B 1 198 ? -7.107  -27.475 -19.932 1.00 90.10  ? 1668 GLY B N   1 
ATOM   3643 C  CA  . GLY B 1 198 ? -7.122  -26.052 -20.198 1.00 94.03  ? 1668 GLY B CA  1 
ATOM   3644 C  C   . GLY B 1 198 ? -7.995  -25.255 -19.254 1.00 92.54  ? 1668 GLY B C   1 
ATOM   3645 O  O   . GLY B 1 198 ? -8.401  -24.141 -19.591 1.00 99.63  ? 1668 GLY B O   1 
ATOM   3646 N  N   . ALA B 1 199 ? -8.324  -25.813 -18.091 1.00 78.53  ? 1669 ALA B N   1 
ATOM   3647 C  CA  . ALA B 1 199 ? -9.111  -25.147 -17.066 1.00 67.94  ? 1669 ALA B CA  1 
ATOM   3648 C  C   . ALA B 1 199 ? -8.263  -24.925 -15.818 1.00 71.33  ? 1669 ALA B C   1 
ATOM   3649 O  O   . ALA B 1 199 ? -7.267  -25.614 -15.587 1.00 58.86  ? 1669 ALA B O   1 
ATOM   3650 C  CB  . ALA B 1 199 ? -10.360 -25.969 -16.719 1.00 69.24  ? 1669 ALA B CB  1 
ATOM   3651 N  N   . TYR B 1 200 ? -8.653  -23.934 -15.023 1.00 77.18  ? 1670 TYR B N   1 
ATOM   3652 C  CA  . TYR B 1 200 ? -8.044  -23.748 -13.712 1.00 75.14  ? 1670 TYR B CA  1 
ATOM   3653 C  C   . TYR B 1 200 ? -8.090  -25.061 -12.938 1.00 76.02  ? 1670 TYR B C   1 
ATOM   3654 O  O   . TYR B 1 200 ? -9.155  -25.671 -12.798 1.00 74.26  ? 1670 TYR B O   1 
ATOM   3655 C  CB  . TYR B 1 200 ? -8.789  -22.637 -12.970 1.00 65.06  ? 1670 TYR B CB  1 
ATOM   3656 C  CG  . TYR B 1 200 ? -8.592  -22.586 -11.481 1.00 57.07  ? 1670 TYR B CG  1 
ATOM   3657 C  CD1 . TYR B 1 200 ? -7.325  -22.495 -10.924 1.00 53.37  ? 1670 TYR B CD1 1 
ATOM   3658 C  CD2 . TYR B 1 200 ? -9.689  -22.602 -10.630 1.00 61.11  ? 1670 TYR B CD2 1 
ATOM   3659 C  CE1 . TYR B 1 200 ? -7.156  -22.440 -9.552  1.00 52.13  ? 1670 TYR B CE1 1 
ATOM   3660 C  CE2 . TYR B 1 200 ? -9.538  -22.539 -9.272  1.00 52.16  ? 1670 TYR B CE2 1 
ATOM   3661 C  CZ  . TYR B 1 200 ? -8.275  -22.461 -8.730  1.00 60.88  ? 1670 TYR B CZ  1 
ATOM   3662 O  OH  . TYR B 1 200 ? -8.149  -22.414 -7.356  1.00 58.02  ? 1670 TYR B OH  1 
ATOM   3663 N  N   . GLU B 1 201 ? -6.927  -25.508 -12.450 1.00 67.29  ? 1671 GLU B N   1 
ATOM   3664 C  CA  . GLU B 1 201 ? -6.818  -26.901 -12.016 1.00 71.62  ? 1671 GLU B CA  1 
ATOM   3665 C  C   . GLU B 1 201 ? -7.741  -27.235 -10.848 1.00 75.33  ? 1671 GLU B C   1 
ATOM   3666 O  O   . GLU B 1 201 ? -8.094  -28.408 -10.680 1.00 61.10  ? 1671 GLU B O   1 
ATOM   3667 C  CB  . GLU B 1 201 ? -5.367  -27.266 -11.684 1.00 62.76  ? 1671 GLU B CB  1 
ATOM   3668 C  CG  . GLU B 1 201 ? -4.689  -26.412 -10.651 1.00 71.24  ? 1671 GLU B CG  1 
ATOM   3669 C  CD  . GLU B 1 201 ? -3.300  -26.937 -10.293 1.00 73.31  ? 1671 GLU B CD  1 
ATOM   3670 O  OE1 . GLU B 1 201 ? -2.530  -27.305 -11.221 1.00 60.26  ? 1671 GLU B OE1 1 
ATOM   3671 O  OE2 . GLU B 1 201 ? -2.984  -26.970 -9.078  1.00 76.80  ? 1671 GLU B OE2 1 
ATOM   3672 N  N   . ALA B 1 202 ? -8.161  -26.247 -10.052 1.00 73.11  ? 1672 ALA B N   1 
ATOM   3673 C  CA  . ALA B 1 202 ? -9.076  -26.529 -8.951  1.00 61.53  ? 1672 ALA B CA  1 
ATOM   3674 C  C   . ALA B 1 202 ? -10.539 -26.429 -9.354  1.00 66.11  ? 1672 ALA B C   1 
ATOM   3675 O  O   . ALA B 1 202 ? -11.417 -26.702 -8.529  1.00 62.30  ? 1672 ALA B O   1 
ATOM   3676 C  CB  . ALA B 1 202 ? -8.815  -25.588 -7.776  1.00 57.07  ? 1672 ALA B CB  1 
ATOM   3677 N  N   . SER B 1 203 ? -10.834 -26.096 -10.601 1.00 68.50  ? 1673 SER B N   1 
ATOM   3678 C  CA  . SER B 1 203 ? -12.207 -25.822 -10.979 1.00 66.86  ? 1673 SER B CA  1 
ATOM   3679 C  C   . SER B 1 203 ? -12.838 -27.099 -11.512 1.00 59.02  ? 1673 SER B C   1 
ATOM   3680 O  O   . SER B 1 203 ? -12.240 -27.804 -12.330 1.00 66.94  ? 1673 SER B O   1 
ATOM   3681 C  CB  . SER B 1 203 ? -12.274 -24.695 -12.012 1.00 59.88  ? 1673 SER B CB  1 
ATOM   3682 O  OG  . SER B 1 203 ? -13.373 -24.858 -12.896 1.00 71.20  ? 1673 SER B OG  1 
ATOM   3683 N  N   . LEU B 1 204 ? -14.047 -27.388 -11.037 1.00 62.19  ? 1674 LEU B N   1 
ATOM   3684 C  CA  . LEU B 1 204 ? -14.760 -28.587 -11.449 1.00 64.68  ? 1674 LEU B CA  1 
ATOM   3685 C  C   . LEU B 1 204 ? -15.332 -28.458 -12.851 1.00 62.89  ? 1674 LEU B C   1 
ATOM   3686 O  O   . LEU B 1 204 ? -15.458 -29.458 -13.560 1.00 72.31  ? 1674 LEU B O   1 
ATOM   3687 C  CB  . LEU B 1 204 ? -15.874 -28.881 -10.449 1.00 63.54  ? 1674 LEU B CB  1 
ATOM   3688 C  CG  . LEU B 1 204 ? -15.429 -28.968 -8.985  1.00 57.70  ? 1674 LEU B CG  1 
ATOM   3689 C  CD1 . LEU B 1 204 ? -16.596 -29.356 -8.101  1.00 65.10  ? 1674 LEU B CD1 1 
ATOM   3690 C  CD2 . LEU B 1 204 ? -14.277 -29.960 -8.817  1.00 59.34  ? 1674 LEU B CD2 1 
ATOM   3691 N  N   . VAL B 1 205 ? -15.672 -27.253 -13.277 1.00 67.59  ? 1675 VAL B N   1 
ATOM   3692 C  CA  . VAL B 1 205 ? -16.202 -27.038 -14.616 1.00 79.70  ? 1675 VAL B CA  1 
ATOM   3693 C  C   . VAL B 1 205 ? -15.033 -26.677 -15.518 1.00 79.12  ? 1675 VAL B C   1 
ATOM   3694 O  O   . VAL B 1 205 ? -14.315 -25.704 -15.264 1.00 71.50  ? 1675 VAL B O   1 
ATOM   3695 C  CB  . VAL B 1 205 ? -17.279 -25.940 -14.630 1.00 83.78  ? 1675 VAL B CB  1 
ATOM   3696 C  CG1 . VAL B 1 205 ? -17.869 -25.794 -16.025 1.00 87.39  ? 1675 VAL B CG1 1 
ATOM   3697 C  CG2 . VAL B 1 205 ? -18.381 -26.247 -13.614 1.00 84.74  ? 1675 VAL B CG2 1 
ATOM   3698 N  N   . ALA B 1 206 ? -14.816 -27.480 -16.548 1.00 89.85  ? 1676 ALA B N   1 
ATOM   3699 C  CA  . ALA B 1 206 ? -13.825 -27.159 -17.567 1.00 107.62 ? 1676 ALA B CA  1 
ATOM   3700 C  C   . ALA B 1 206 ? -14.444 -26.161 -18.535 1.00 123.15 ? 1676 ALA B C   1 
ATOM   3701 O  O   . ALA B 1 206 ? -15.426 -26.474 -19.218 1.00 126.36 ? 1676 ALA B O   1 
ATOM   3702 C  CB  . ALA B 1 206 ? -13.342 -28.415 -18.278 1.00 111.13 ? 1676 ALA B CB  1 
ATOM   3703 N  N   . ALA B 1 207 ? -13.900 -24.942 -18.548 1.00 133.54 ? 1677 ALA B N   1 
ATOM   3704 C  CA  . ALA B 1 207 ? -14.436 -23.879 -19.393 1.00 139.42 ? 1677 ALA B CA  1 
ATOM   3705 C  C   . ALA B 1 207 ? -14.518 -24.295 -20.860 1.00 139.94 ? 1677 ALA B C   1 
ATOM   3706 O  O   . ALA B 1 207 ? -15.498 -23.977 -21.544 1.00 140.42 ? 1677 ALA B O   1 
ATOM   3707 C  CB  . ALA B 1 207 ? -13.580 -22.621 -19.242 1.00 141.22 ? 1677 ALA B CB  1 
ATOM   3708 N  N   . SER B 1 208 ? -13.500 -24.997 -21.364 1.00 137.68 ? 1678 SER B N   1 
ATOM   3709 C  CA  . SER B 1 208 ? -13.510 -25.462 -22.749 1.00 132.38 ? 1678 SER B CA  1 
ATOM   3710 C  C   . SER B 1 208 ? -14.703 -26.377 -23.010 1.00 136.30 ? 1678 SER B C   1 
ATOM   3711 O  O   . SER B 1 208 ? -15.657 -25.974 -23.685 1.00 139.29 ? 1678 SER B O   1 
ATOM   3712 C  CB  . SER B 1 208 ? -12.194 -26.169 -23.091 1.00 124.30 ? 1678 SER B CB  1 
ATOM   3713 O  OG  . SER B 1 208 ? -12.011 -27.338 -22.313 1.00 119.96 ? 1678 SER B OG  1 
ATOM   3714 N  N   . THR B 1 209 ? -14.670 -27.604 -22.490 1.00 136.41 ? 1679 THR B N   1 
ATOM   3715 C  CA  . THR B 1 209 ? -15.769 -28.535 -22.725 1.00 137.87 ? 1679 THR B CA  1 
ATOM   3716 C  C   . THR B 1 209 ? -17.060 -28.048 -22.071 1.00 139.35 ? 1679 THR B C   1 
ATOM   3717 O  O   . THR B 1 209 ? -18.016 -27.694 -22.768 1.00 142.72 ? 1679 THR B O   1 
ATOM   3718 C  CB  . THR B 1 209 ? -15.399 -29.954 -22.253 1.00 135.17 ? 1679 THR B CB  1 
ATOM   3719 O  OG1 . THR B 1 209 ? -16.576 -30.773 -22.185 1.00 135.55 ? 1679 THR B OG1 1 
ATOM   3720 C  CG2 . THR B 1 209 ? -14.691 -29.946 -20.919 1.00 129.64 ? 1679 THR B CG2 1 
ATOM   3721 N  N   . GLY B 1 210 ? -17.095 -27.990 -20.746 1.00 137.24 ? 1680 GLY B N   1 
ATOM   3722 C  CA  . GLY B 1 210 ? -18.312 -27.623 -20.057 1.00 129.15 ? 1680 GLY B CA  1 
ATOM   3723 C  C   . GLY B 1 210 ? -18.935 -28.807 -19.355 1.00 118.16 ? 1680 GLY B C   1 
ATOM   3724 O  O   . GLY B 1 210 ? -20.148 -28.840 -19.141 1.00 114.72 ? 1680 GLY B O   1 
ATOM   3725 N  N   . VAL B 1 211 ? -18.106 -29.789 -18.999 1.00 113.49 ? 1681 VAL B N   1 
ATOM   3726 C  CA  . VAL B 1 211 ? -18.517 -30.922 -18.176 1.00 105.24 ? 1681 VAL B CA  1 
ATOM   3727 C  C   . VAL B 1 211 ? -18.054 -30.657 -16.752 1.00 105.32 ? 1681 VAL B C   1 
ATOM   3728 O  O   . VAL B 1 211 ? -16.911 -30.238 -16.529 1.00 107.65 ? 1681 VAL B O   1 
ATOM   3729 C  CB  . VAL B 1 211 ? -17.935 -32.247 -18.704 1.00 99.34  ? 1681 VAL B CB  1 
ATOM   3730 C  CG1 . VAL B 1 211 ? -18.743 -32.752 -19.885 1.00 96.27  ? 1681 VAL B CG1 1 
ATOM   3731 C  CG2 . VAL B 1 211 ? -16.460 -32.097 -19.060 1.00 94.59  ? 1681 VAL B CG2 1 
ATOM   3732 N  N   . ARG B 1 212 ? -18.951 -30.854 -15.790 1.00 103.98 ? 1682 ARG B N   1 
ATOM   3733 C  CA  . ARG B 1 212 ? -18.598 -30.699 -14.385 1.00 100.37 ? 1682 ARG B CA  1 
ATOM   3734 C  C   . ARG B 1 212 ? -17.980 -32.007 -13.912 1.00 96.80  ? 1682 ARG B C   1 
ATOM   3735 O  O   . ARG B 1 212 ? -18.669 -33.028 -13.814 1.00 100.83 ? 1682 ARG B O   1 
ATOM   3736 C  CB  . ARG B 1 212 ? -19.823 -30.326 -13.552 1.00 98.81  ? 1682 ARG B CB  1 
ATOM   3737 N  N   . ALA B 1 213 ? -16.681 -31.983 -13.633 1.00 83.18  ? 1683 ALA B N   1 
ATOM   3738 C  CA  . ALA B 1 213 ? -16.029 -33.151 -13.071 1.00 75.35  ? 1683 ALA B CA  1 
ATOM   3739 C  C   . ALA B 1 213 ? -16.407 -33.283 -11.598 1.00 69.14  ? 1683 ALA B C   1 
ATOM   3740 O  O   . ALA B 1 213 ? -16.764 -32.305 -10.932 1.00 61.54  ? 1683 ALA B O   1 
ATOM   3741 C  CB  . ALA B 1 213 ? -14.510 -33.053 -13.238 1.00 64.72  ? 1683 ALA B CB  1 
ATOM   3742 N  N   . LEU B 1 214 ? -16.369 -34.515 -11.102 1.00 57.04  ? 1684 LEU B N   1 
ATOM   3743 C  CA  . LEU B 1 214 ? -16.652 -34.755 -9.700  1.00 61.57  ? 1684 LEU B CA  1 
ATOM   3744 C  C   . LEU B 1 214 ? -15.478 -34.302 -8.831  1.00 72.42  ? 1684 LEU B C   1 
ATOM   3745 O  O   . LEU B 1 214 ? -14.317 -34.396 -9.237  1.00 67.46  ? 1684 LEU B O   1 
ATOM   3746 C  CB  . LEU B 1 214 ? -16.936 -36.232 -9.450  1.00 62.78  ? 1684 LEU B CB  1 
ATOM   3747 C  CG  . LEU B 1 214 ? -18.272 -36.740 -9.994  1.00 71.56  ? 1684 LEU B CG  1 
ATOM   3748 C  CD1 . LEU B 1 214 ? -18.415 -38.246 -9.766  1.00 74.70  ? 1684 LEU B CD1 1 
ATOM   3749 C  CD2 . LEU B 1 214 ? -19.417 -35.977 -9.342  1.00 74.49  ? 1684 LEU B CD2 1 
ATOM   3750 N  N   . PRO B 1 215 ? -15.756 -33.786 -7.640  1.00 72.83  ? 1685 PRO B N   1 
ATOM   3751 C  CA  . PRO B 1 215 ? -14.666 -33.398 -6.738  1.00 48.91  ? 1685 PRO B CA  1 
ATOM   3752 C  C   . PRO B 1 215 ? -14.171 -34.564 -5.904  1.00 55.70  ? 1685 PRO B C   1 
ATOM   3753 O  O   . PRO B 1 215 ? -14.984 -35.313 -5.352  1.00 59.83  ? 1685 PRO B O   1 
ATOM   3754 C  CB  . PRO B 1 215 ? -15.314 -32.333 -5.856  1.00 67.37  ? 1685 PRO B CB  1 
ATOM   3755 C  CG  . PRO B 1 215 ? -16.766 -32.766 -5.778  1.00 69.33  ? 1685 PRO B CG  1 
ATOM   3756 C  CD  . PRO B 1 215 ? -17.084 -33.426 -7.097  1.00 66.18  ? 1685 PRO B CD  1 
ATOM   3757 N  N   . CYS B 1 216 ? -12.848 -34.731 -5.801  1.00 47.60  ? 1686 CYS B N   1 
ATOM   3758 C  CA  . CYS B 1 216 ? -12.311 -35.814 -4.998  1.00 46.96  ? 1686 CYS B CA  1 
ATOM   3759 C  C   . CYS B 1 216 ? -12.699 -35.615 -3.543  1.00 51.85  ? 1686 CYS B C   1 
ATOM   3760 O  O   . CYS B 1 216 ? -12.599 -34.510 -3.008  1.00 45.65  ? 1686 CYS B O   1 
ATOM   3761 C  CB  . CYS B 1 216 ? -10.795 -35.851 -5.119  1.00 46.70  ? 1686 CYS B CB  1 
ATOM   3762 S  SG  . CYS B 1 216 ? -10.015 -37.019 -4.024  1.00 52.19  ? 1686 CYS B SG  1 
ATOM   3763 N  N   . LEU B 1 217 ? -13.150 -36.690 -2.902  1.00 48.24  ? 1687 LEU B N   1 
ATOM   3764 C  CA  . LEU B 1 217 ? -13.539 -36.596 -1.504  1.00 44.68  ? 1687 LEU B CA  1 
ATOM   3765 C  C   . LEU B 1 217 ? -12.349 -36.326 -0.598  1.00 43.49  ? 1687 LEU B C   1 
ATOM   3766 O  O   . LEU B 1 217 ? -12.549 -36.000 0.573   1.00 42.62  ? 1687 LEU B O   1 
ATOM   3767 C  CB  . LEU B 1 217 ? -14.221 -37.894 -1.068  1.00 45.12  ? 1687 LEU B CB  1 
ATOM   3768 C  CG  . LEU B 1 217 ? -15.743 -37.934 -1.252  1.00 53.10  ? 1687 LEU B CG  1 
ATOM   3769 C  CD1 . LEU B 1 217 ? -16.241 -39.360 -1.229  1.00 61.50  ? 1687 LEU B CD1 1 
ATOM   3770 C  CD2 . LEU B 1 217 ? -16.409 -37.130 -0.180  1.00 59.21  ? 1687 LEU B CD2 1 
ATOM   3771 N  N   . ILE B 1 218 ? -11.126 -36.493 -1.101  1.00 43.56  ? 1688 ILE B N   1 
ATOM   3772 C  CA  . ILE B 1 218 ? -9.927  -36.343 -0.280  1.00 44.56  ? 1688 ILE B CA  1 
ATOM   3773 C  C   . ILE B 1 218 ? -9.353  -34.941 -0.379  1.00 42.55  ? 1688 ILE B C   1 
ATOM   3774 O  O   . ILE B 1 218 ? -9.059  -34.331 0.650   1.00 41.32  ? 1688 ILE B O   1 
ATOM   3775 C  CB  . ILE B 1 218 ? -8.871  -37.401 -0.670  1.00 43.11  ? 1688 ILE B CB  1 
ATOM   3776 C  CG1 . ILE B 1 218 ? -9.433  -38.820 -0.511  1.00 46.21  ? 1688 ILE B CG1 1 
ATOM   3777 C  CG2 . ILE B 1 218 ? -7.609  -37.239 0.164   1.00 42.27  ? 1688 ILE B CG2 1 
ATOM   3778 C  CD1 . ILE B 1 218 ? -9.839  -39.165 0.889   1.00 42.95  ? 1688 ILE B CD1 1 
ATOM   3779 N  N   . THR B 1 219 ? -9.214  -34.406 -1.603  1.00 42.92  ? 1689 THR B N   1 
ATOM   3780 C  CA  . THR B 1 219 ? -8.575  -33.106 -1.818  1.00 49.60  ? 1689 THR B CA  1 
ATOM   3781 C  C   . THR B 1 219 ? -9.514  -32.013 -2.326  1.00 53.75  ? 1689 THR B C   1 
ATOM   3782 O  O   . THR B 1 219 ? -9.124  -30.843 -2.313  1.00 45.87  ? 1689 THR B O   1 
ATOM   3783 C  CB  . THR B 1 219 ? -7.423  -33.210 -2.828  1.00 43.49  ? 1689 THR B CB  1 
ATOM   3784 O  OG1 . THR B 1 219 ? -7.977  -33.366 -4.140  1.00 48.32  ? 1689 THR B OG1 1 
ATOM   3785 C  CG2 . THR B 1 219 ? -6.468  -34.366 -2.512  1.00 43.42  ? 1689 THR B CG2 1 
ATOM   3786 N  N   . GLY B 1 220 ? -10.717 -32.359 -2.799  1.00 49.07  ? 1690 GLY B N   1 
ATOM   3787 C  CA  . GLY B 1 220 ? -11.633 -31.406 -3.399  1.00 54.56  ? 1690 GLY B CA  1 
ATOM   3788 C  C   . GLY B 1 220 ? -11.427 -31.136 -4.878  1.00 62.54  ? 1690 GLY B C   1 
ATOM   3789 O  O   . GLY B 1 220 ? -12.343 -30.613 -5.531  1.00 53.31  ? 1690 GLY B O   1 
ATOM   3790 N  N   . TYR B 1 221 ? -10.266 -31.491 -5.428  1.00 50.12  ? 1691 TYR B N   1 
ATOM   3791 C  CA  . TYR B 1 221 ? -9.963  -31.221 -6.824  1.00 47.41  ? 1691 TYR B CA  1 
ATOM   3792 C  C   . TYR B 1 221 ? -10.846 -32.039 -7.761  1.00 48.64  ? 1691 TYR B C   1 
ATOM   3793 O  O   . TYR B 1 221 ? -11.345 -33.104 -7.390  1.00 55.03  ? 1691 TYR B O   1 
ATOM   3794 C  CB  . TYR B 1 221 ? -8.500  -31.555 -7.100  1.00 47.54  ? 1691 TYR B CB  1 
ATOM   3795 C  CG  . TYR B 1 221 ? -7.623  -30.371 -6.916  1.00 50.99  ? 1691 TYR B CG  1 
ATOM   3796 C  CD1 . TYR B 1 221 ? -7.832  -29.494 -5.851  1.00 47.69  ? 1691 TYR B CD1 1 
ATOM   3797 C  CD2 . TYR B 1 221 ? -6.594  -30.104 -7.803  1.00 55.06  ? 1691 TYR B CD2 1 
ATOM   3798 C  CE1 . TYR B 1 221 ? -7.031  -28.364 -5.681  1.00 47.12  ? 1691 TYR B CE1 1 
ATOM   3799 C  CE2 . TYR B 1 221 ? -5.791  -28.991 -7.646  1.00 53.43  ? 1691 TYR B CE2 1 
ATOM   3800 C  CZ  . TYR B 1 221 ? -6.016  -28.123 -6.584  1.00 49.13  ? 1691 TYR B CZ  1 
ATOM   3801 O  OH  . TYR B 1 221 ? -5.197  -27.039 -6.429  1.00 57.04  ? 1691 TYR B OH  1 
ATOM   3802 N  N   . PRO B 1 222 ? -11.017 -31.590 -9.003  1.00 50.01  ? 1692 PRO B N   1 
ATOM   3803 C  CA  . PRO B 1 222 ? -11.721 -32.425 -9.983  1.00 51.36  ? 1692 PRO B CA  1 
ATOM   3804 C  C   . PRO B 1 222 ? -10.988 -33.749 -10.197 1.00 64.01  ? 1692 PRO B C   1 
ATOM   3805 O  O   . PRO B 1 222 ? -9.760  -33.798 -10.326 1.00 58.46  ? 1692 PRO B O   1 
ATOM   3806 C  CB  . PRO B 1 222 ? -11.713 -31.568 -11.252 1.00 52.81  ? 1692 PRO B CB  1 
ATOM   3807 C  CG  . PRO B 1 222 ? -10.501 -30.667 -11.086 1.00 52.35  ? 1692 PRO B CG  1 
ATOM   3808 C  CD  . PRO B 1 222 ? -10.494 -30.353 -9.610  1.00 53.30  ? 1692 PRO B CD  1 
ATOM   3809 N  N   . ILE B 1 223 ? -11.754 -34.832 -10.201 1.00 59.66  ? 1693 ILE B N   1 
ATOM   3810 C  CA  . ILE B 1 223 ? -11.231 -36.154 -10.523 1.00 59.08  ? 1693 ILE B CA  1 
ATOM   3811 C  C   . ILE B 1 223 ? -11.080 -36.219 -12.038 1.00 63.77  ? 1693 ILE B C   1 
ATOM   3812 O  O   . ILE B 1 223 ? -12.076 -36.270 -12.765 1.00 70.30  ? 1693 ILE B O   1 
ATOM   3813 C  CB  . ILE B 1 223 ? -12.170 -37.245 -10.015 1.00 58.49  ? 1693 ILE B CB  1 
ATOM   3814 C  CG1 . ILE B 1 223 ? -12.327 -37.106 -8.504  1.00 51.77  ? 1693 ILE B CG1 1 
ATOM   3815 C  CG2 . ILE B 1 223 ? -11.648 -38.615 -10.430 1.00 79.62  ? 1693 ILE B CG2 1 
ATOM   3816 C  CD1 . ILE B 1 223 ? -13.107 -38.213 -7.880  1.00 60.06  ? 1693 ILE B CD1 1 
ATOM   3817 N  N   . LEU B 1 224 ? -9.837  -36.235 -12.521 1.00 68.40  ? 1694 LEU B N   1 
ATOM   3818 C  CA  . LEU B 1 224 ? -9.591  -36.292 -13.959 1.00 72.22  ? 1694 LEU B CA  1 
ATOM   3819 C  C   . LEU B 1 224 ? -9.180  -37.680 -14.446 1.00 76.08  ? 1694 LEU B C   1 
ATOM   3820 O  O   . LEU B 1 224 ? -9.349  -37.986 -15.635 1.00 62.17  ? 1694 LEU B O   1 
ATOM   3821 C  CB  . LEU B 1 224 ? -8.510  -35.277 -14.349 1.00 63.64  ? 1694 LEU B CB  1 
ATOM   3822 C  CG  . LEU B 1 224 ? -8.853  -33.823 -14.003 1.00 69.05  ? 1694 LEU B CG  1 
ATOM   3823 C  CD1 . LEU B 1 224 ? -7.875  -32.914 -14.719 1.00 77.15  ? 1694 LEU B CD1 1 
ATOM   3824 C  CD2 . LEU B 1 224 ? -10.305 -33.477 -14.353 1.00 56.74  ? 1694 LEU B CD2 1 
ATOM   3825 N  N   . ARG B 1 225 ? -8.650  -38.515 -13.560 1.00 79.88  ? 1695 ARG B N   1 
ATOM   3826 C  CA  . ARG B 1 225 ? -8.243  -39.862 -13.917 1.00 88.29  ? 1695 ARG B CA  1 
ATOM   3827 C  C   . ARG B 1 225 ? -8.263  -40.703 -12.651 1.00 84.18  ? 1695 ARG B C   1 
ATOM   3828 O  O   . ARG B 1 225 ? -8.243  -40.170 -11.536 1.00 62.90  ? 1695 ARG B O   1 
ATOM   3829 C  CB  . ARG B 1 225 ? -6.860  -39.858 -14.579 1.00 93.42  ? 1695 ARG B CB  1 
ATOM   3830 C  CG  . ARG B 1 225 ? -5.740  -39.329 -13.691 1.00 94.29  ? 1695 ARG B CG  1 
ATOM   3831 C  CD  . ARG B 1 225 ? -4.559  -40.294 -13.706 1.00 108.32 ? 1695 ARG B CD  1 
ATOM   3832 N  NE  . ARG B 1 225 ? -4.287  -40.798 -15.055 1.00 119.90 ? 1695 ARG B NE  1 
ATOM   3833 C  CZ  . ARG B 1 225 ? -3.460  -41.805 -15.338 1.00 121.33 ? 1695 ARG B CZ  1 
ATOM   3834 N  NH1 . ARG B 1 225 ? -3.279  -42.183 -16.601 1.00 120.41 ? 1695 ARG B NH1 1 
ATOM   3835 N  NH2 . ARG B 1 225 ? -2.820  -42.443 -14.362 1.00 115.83 ? 1695 ARG B NH2 1 
ATOM   3836 N  N   . ASN B 1 226 ? -8.309  -42.027 -12.835 1.00 77.22  ? 1696 ASN B N   1 
ATOM   3837 C  CA  . ASN B 1 226 ? -8.211  -42.966 -11.716 1.00 62.76  ? 1696 ASN B CA  1 
ATOM   3838 C  C   . ASN B 1 226 ? -9.359  -42.783 -10.730 1.00 60.01  ? 1696 ASN B C   1 
ATOM   3839 O  O   . ASN B 1 226 ? -9.175  -42.872 -9.516  1.00 61.23  ? 1696 ASN B O   1 
ATOM   3840 C  CB  . ASN B 1 226 ? -6.864  -42.837 -10.998 1.00 64.75  ? 1696 ASN B CB  1 
ATOM   3841 C  CG  . ASN B 1 226 ? -5.808  -43.759 -11.578 1.00 91.32  ? 1696 ASN B CG  1 
ATOM   3842 O  OD1 . ASN B 1 226 ? -5.361  -43.576 -12.713 1.00 98.73  ? 1696 ASN B OD1 1 
ATOM   3843 N  ND2 . ASN B 1 226 ? -5.420  -44.776 -10.807 1.00 90.69  ? 1696 ASN B ND2 1 
ATOM   3844 N  N   . LYS B 1 227 ? -10.553 -42.530 -11.251 1.00 77.97  ? 1697 LYS B N   1 
ATOM   3845 C  CA  . LYS B 1 227 ? -11.708 -42.319 -10.388 1.00 82.61  ? 1697 LYS B CA  1 
ATOM   3846 C  C   . LYS B 1 227 ? -12.063 -43.616 -9.676  1.00 76.59  ? 1697 LYS B C   1 
ATOM   3847 O  O   . LYS B 1 227 ? -12.050 -44.689 -10.286 1.00 82.50  ? 1697 LYS B O   1 
ATOM   3848 C  CB  . LYS B 1 227 ? -12.892 -41.813 -11.217 1.00 89.16  ? 1697 LYS B CB  1 
ATOM   3849 C  CG  . LYS B 1 227 ? -14.205 -41.632 -10.462 1.00 89.39  ? 1697 LYS B CG  1 
ATOM   3850 C  CD  . LYS B 1 227 ? -15.059 -40.558 -11.139 1.00 91.19  ? 1697 LYS B CD  1 
ATOM   3851 C  CE  . LYS B 1 227 ? -16.037 -41.153 -12.138 1.00 94.08  ? 1697 LYS B CE  1 
ATOM   3852 N  NZ  . LYS B 1 227 ? -16.940 -40.118 -12.732 1.00 93.17  ? 1697 LYS B NZ  1 
ATOM   3853 N  N   . ILE B 1 228 ? -12.329 -43.537 -8.375  1.00 62.05  ? 1698 ILE B N   1 
ATOM   3854 C  CA  . ILE B 1 228 ? -12.937 -44.652 -7.661  1.00 63.11  ? 1698 ILE B CA  1 
ATOM   3855 C  C   . ILE B 1 228 ? -14.243 -44.170 -7.049  1.00 67.88  ? 1698 ILE B C   1 
ATOM   3856 O  O   . ILE B 1 228 ? -14.318 -43.070 -6.482  1.00 56.96  ? 1698 ILE B O   1 
ATOM   3857 C  CB  . ILE B 1 228 ? -11.996 -45.274 -6.607  1.00 69.58  ? 1698 ILE B CB  1 
ATOM   3858 C  CG1 . ILE B 1 228 ? -11.755 -44.353 -5.417  1.00 63.47  ? 1698 ILE B CG1 1 
ATOM   3859 C  CG2 . ILE B 1 228 ? -10.658 -45.654 -7.253  1.00 69.36  ? 1698 ILE B CG2 1 
ATOM   3860 C  CD1 . ILE B 1 228 ? -10.977 -45.047 -4.303  1.00 55.75  ? 1698 ILE B CD1 1 
ATOM   3861 N  N   . GLU B 1 229 ? -15.280 -44.997 -7.189  1.00 66.88  ? 1699 GLU B N   1 
ATOM   3862 C  CA  . GLU B 1 229 ? -16.656 -44.610 -6.901  1.00 73.24  ? 1699 GLU B CA  1 
ATOM   3863 C  C   . GLU B 1 229 ? -17.191 -45.363 -5.691  1.00 63.97  ? 1699 GLU B C   1 
ATOM   3864 O  O   . GLU B 1 229 ? -16.929 -46.559 -5.516  1.00 68.10  ? 1699 GLU B O   1 
ATOM   3865 C  CB  . GLU B 1 229 ? -17.554 -44.854 -8.114  1.00 72.52  ? 1699 GLU B CB  1 
ATOM   3866 C  CG  . GLU B 1 229 ? -17.922 -43.574 -8.839  1.00 88.21  ? 1699 GLU B CG  1 
ATOM   3867 C  CD  . GLU B 1 229 ? -18.221 -43.794 -10.306 1.00 100.45 ? 1699 GLU B CD  1 
ATOM   3868 O  OE1 . GLU B 1 229 ? -18.264 -44.967 -10.745 1.00 89.97  ? 1699 GLU B OE1 1 
ATOM   3869 O  OE2 . GLU B 1 229 ? -18.420 -42.783 -11.017 1.00 106.64 ? 1699 GLU B OE2 1 
ATOM   3870 N  N   . PHE B 1 230 ? -17.931 -44.652 -4.851  1.00 60.70  ? 1700 PHE B N   1 
ATOM   3871 C  CA  . PHE B 1 230 ? -18.563 -45.266 -3.696  1.00 77.53  ? 1700 PHE B CA  1 
ATOM   3872 C  C   . PHE B 1 230 ? -19.999 -45.678 -4.044  1.00 73.21  ? 1700 PHE B C   1 
ATOM   3873 O  O   . PHE B 1 230 ? -20.560 -45.267 -5.062  1.00 72.09  ? 1700 PHE B O   1 
ATOM   3874 C  CB  . PHE B 1 230 ? -18.486 -44.307 -2.505  1.00 72.58  ? 1700 PHE B CB  1 
ATOM   3875 C  CG  . PHE B 1 230 ? -17.067 -44.022 -2.064  1.00 75.63  ? 1700 PHE B CG  1 
ATOM   3876 C  CD1 . PHE B 1 230 ? -16.289 -43.085 -2.730  1.00 67.58  ? 1700 PHE B CD1 1 
ATOM   3877 C  CD2 . PHE B 1 230 ? -16.503 -44.718 -1.005  1.00 72.96  ? 1700 PHE B CD2 1 
ATOM   3878 C  CE1 . PHE B 1 230 ? -14.984 -42.842 -2.339  1.00 70.96  ? 1700 PHE B CE1 1 
ATOM   3879 C  CE2 . PHE B 1 230 ? -15.201 -44.472 -0.604  1.00 63.79  ? 1700 PHE B CE2 1 
ATOM   3880 C  CZ  . PHE B 1 230 ? -14.437 -43.537 -1.274  1.00 61.09  ? 1700 PHE B CZ  1 
ATOM   3881 N  N   . LYS B 1 231 ? -20.601 -46.513 -3.188  1.00 83.23  ? 1701 LYS B N   1 
ATOM   3882 C  CA  . LYS B 1 231 ? -21.917 -47.051 -3.530  1.00 88.86  ? 1701 LYS B CA  1 
ATOM   3883 C  C   . LYS B 1 231 ? -22.960 -45.946 -3.603  1.00 95.25  ? 1701 LYS B C   1 
ATOM   3884 O  O   . LYS B 1 231 ? -23.877 -46.014 -4.427  1.00 103.26 ? 1701 LYS B O   1 
ATOM   3885 C  CB  . LYS B 1 231 ? -22.342 -48.130 -2.528  1.00 73.74  ? 1701 LYS B CB  1 
ATOM   3886 N  N   . ARG B 1 232 ? -22.824 -44.919 -2.773  1.00 100.33 ? 1702 ARG B N   1 
ATOM   3887 C  CA  . ARG B 1 232 ? -23.673 -43.744 -2.888  1.00 102.62 ? 1702 ARG B CA  1 
ATOM   3888 C  C   . ARG B 1 232 ? -23.379 -42.998 -4.191  1.00 104.80 ? 1702 ARG B C   1 
ATOM   3889 O  O   . ARG B 1 232 ? -22.217 -42.884 -4.596  1.00 105.71 ? 1702 ARG B O   1 
ATOM   3890 C  CB  . ARG B 1 232 ? -23.465 -42.818 -1.693  1.00 109.64 ? 1702 ARG B CB  1 
ATOM   3891 N  N   . PRO B 1 233 ? -24.407 -42.500 -4.874  1.00 109.24 ? 1703 PRO B N   1 
ATOM   3892 C  CA  . PRO B 1 233 ? -24.191 -41.781 -6.138  1.00 107.33 ? 1703 PRO B CA  1 
ATOM   3893 C  C   . PRO B 1 233 ? -23.553 -40.416 -5.940  1.00 96.59  ? 1703 PRO B C   1 
ATOM   3894 O  O   . PRO B 1 233 ? -23.739 -39.758 -4.914  1.00 89.27  ? 1703 PRO B O   1 
ATOM   3895 C  CB  . PRO B 1 233 ? -25.607 -41.634 -6.703  1.00 112.74 ? 1703 PRO B CB  1 
ATOM   3896 C  CG  . PRO B 1 233 ? -26.485 -41.646 -5.490  1.00 114.64 ? 1703 PRO B CG  1 
ATOM   3897 C  CD  . PRO B 1 233 ? -25.834 -42.594 -4.523  1.00 115.46 ? 1703 PRO B CD  1 
ATOM   3898 N  N   . GLY B 1 234 ? -22.779 -39.998 -6.944  1.00 92.65  ? 1704 GLY B N   1 
ATOM   3899 C  CA  . GLY B 1 234 ? -22.113 -38.707 -6.905  1.00 84.85  ? 1704 GLY B CA  1 
ATOM   3900 C  C   . GLY B 1 234 ? -20.930 -38.619 -5.965  1.00 86.54  ? 1704 GLY B C   1 
ATOM   3901 O  O   . GLY B 1 234 ? -20.417 -37.518 -5.739  1.00 88.36  ? 1704 GLY B O   1 
ATOM   3902 N  N   . LYS B 1 235 ? -20.472 -39.743 -5.416  1.00 75.72  ? 1705 LYS B N   1 
ATOM   3903 C  CA  . LYS B 1 235 ? -19.420 -39.756 -4.409  1.00 70.70  ? 1705 LYS B CA  1 
ATOM   3904 C  C   . LYS B 1 235 ? -18.225 -40.501 -4.976  1.00 65.28  ? 1705 LYS B C   1 
ATOM   3905 O  O   . LYS B 1 235 ? -18.319 -41.703 -5.260  1.00 73.77  ? 1705 LYS B O   1 
ATOM   3906 C  CB  . LYS B 1 235 ? -19.906 -40.412 -3.110  1.00 69.46  ? 1705 LYS B CB  1 
ATOM   3907 C  CG  . LYS B 1 235 ? -20.986 -39.617 -2.369  1.00 71.87  ? 1705 LYS B CG  1 
ATOM   3908 C  CD  . LYS B 1 235 ? -20.524 -38.198 -2.076  1.00 75.34  ? 1705 LYS B CD  1 
ATOM   3909 C  CE  . LYS B 1 235 ? -21.662 -37.302 -1.558  1.00 87.80  ? 1705 LYS B CE  1 
ATOM   3910 N  NZ  . LYS B 1 235 ? -21.374 -35.833 -1.749  1.00 77.28  ? 1705 LYS B NZ  1 
ATOM   3911 N  N   . ALA B 1 236 ? -17.107 -39.791 -5.143  1.00 62.59  ? 1706 ALA B N   1 
ATOM   3912 C  CA  . ALA B 1 236 ? -15.913 -40.384 -5.733  1.00 56.30  ? 1706 ALA B CA  1 
ATOM   3913 C  C   . ALA B 1 236 ? -14.654 -39.766 -5.142  1.00 56.70  ? 1706 ALA B C   1 
ATOM   3914 O  O   . ALA B 1 236 ? -14.678 -38.705 -4.514  1.00 55.67  ? 1706 ALA B O   1 
ATOM   3915 C  CB  . ALA B 1 236 ? -15.903 -40.228 -7.256  1.00 57.57  ? 1706 ALA B CB  1 
ATOM   3916 N  N   . ALA B 1 237 ? -13.543 -40.458 -5.367  1.00 60.67  ? 1707 ALA B N   1 
ATOM   3917 C  CA  . ALA B 1 237 ? -12.227 -39.977 -4.994  1.00 52.55  ? 1707 ALA B CA  1 
ATOM   3918 C  C   . ALA B 1 237 ? -11.259 -40.309 -6.111  1.00 61.55  ? 1707 ALA B C   1 
ATOM   3919 O  O   . ALA B 1 237 ? -11.540 -41.134 -6.981  1.00 69.92  ? 1707 ALA B O   1 
ATOM   3920 C  CB  . ALA B 1 237 ? -11.735 -40.593 -3.684  1.00 49.79  ? 1707 ALA B CB  1 
ATOM   3921 N  N   . ASN B 1 238 ? -10.145 -39.597 -6.126  1.00 61.70  ? 1708 ASN B N   1 
ATOM   3922 C  CA  . ASN B 1 238 ? -9.028  -40.000 -6.959  1.00 49.84  ? 1708 ASN B CA  1 
ATOM   3923 C  C   . ASN B 1 238 ? -8.261  -41.079 -6.212  1.00 49.58  ? 1708 ASN B C   1 
ATOM   3924 O  O   . ASN B 1 238 ? -7.949  -40.914 -5.026  1.00 50.50  ? 1708 ASN B O   1 
ATOM   3925 C  CB  . ASN B 1 238 ? -8.125  -38.813 -7.283  1.00 62.69  ? 1708 ASN B CB  1 
ATOM   3926 C  CG  . ASN B 1 238 ? -6.778  -39.252 -7.833  1.00 59.86  ? 1708 ASN B CG  1 
ATOM   3927 O  OD1 . ASN B 1 238 ? -5.831  -39.478 -7.079  1.00 55.05  ? 1708 ASN B OD1 1 
ATOM   3928 N  ND2 . ASN B 1 238 ? -6.696  -39.392 -9.149  1.00 53.75  ? 1708 ASN B ND2 1 
ATOM   3929 N  N   . LYS B 1 239 ? -8.011  -42.209 -6.880  1.00 63.93  ? 1709 LYS B N   1 
ATOM   3930 C  CA  . LYS B 1 239 ? -7.412  -43.353 -6.193  1.00 64.60  ? 1709 LYS B CA  1 
ATOM   3931 C  C   . LYS B 1 239 ? -6.054  -43.030 -5.587  1.00 58.45  ? 1709 LYS B C   1 
ATOM   3932 O  O   . LYS B 1 239 ? -5.707  -43.570 -4.531  1.00 49.50  ? 1709 LYS B O   1 
ATOM   3933 C  CB  . LYS B 1 239 ? -7.274  -44.536 -7.139  1.00 56.70  ? 1709 LYS B CB  1 
ATOM   3934 C  CG  . LYS B 1 239 ? -6.927  -45.816 -6.424  1.00 61.24  ? 1709 LYS B CG  1 
ATOM   3935 C  CD  . LYS B 1 239 ? -6.867  -46.954 -7.421  1.00 73.74  ? 1709 LYS B CD  1 
ATOM   3936 C  CE  . LYS B 1 239 ? -6.483  -48.248 -6.755  1.00 69.37  ? 1709 LYS B CE  1 
ATOM   3937 N  NZ  . LYS B 1 239 ? -5.989  -49.224 -7.773  1.00 70.08  ? 1709 LYS B NZ  1 
ATOM   3938 N  N   . ASP B 1 240 ? -5.277  -42.150 -6.221  1.00 61.40  ? 1710 ASP B N   1 
ATOM   3939 C  CA  . ASP B 1 240 ? -3.965  -41.823 -5.671  1.00 49.64  ? 1710 ASP B CA  1 
ATOM   3940 C  C   . ASP B 1 240 ? -4.091  -41.026 -4.381  1.00 50.90  ? 1710 ASP B C   1 
ATOM   3941 O  O   . ASP B 1 240 ? -3.372  -41.297 -3.412  1.00 47.85  ? 1710 ASP B O   1 
ATOM   3942 C  CB  . ASP B 1 240 ? -3.134  -41.078 -6.711  1.00 59.66  ? 1710 ASP B CB  1 
ATOM   3943 C  CG  . ASP B 1 240 ? -2.519  -42.015 -7.733  1.00 72.56  ? 1710 ASP B CG  1 
ATOM   3944 O  OD1 . ASP B 1 240 ? -2.133  -43.146 -7.359  1.00 83.30  ? 1710 ASP B OD1 1 
ATOM   3945 O  OD2 . ASP B 1 240 ? -2.444  -41.632 -8.917  1.00 76.41  ? 1710 ASP B OD2 1 
ATOM   3946 N  N   . ASN B 1 241 ? -5.015  -40.055 -4.333  1.00 53.07  ? 1711 ASN B N   1 
ATOM   3947 C  CA  . ASN B 1 241 ? -5.288  -39.356 -3.076  1.00 50.71  ? 1711 ASN B CA  1 
ATOM   3948 C  C   . ASN B 1 241 ? -5.777  -40.321 -2.005  1.00 45.33  ? 1711 ASN B C   1 
ATOM   3949 O  O   . ASN B 1 241 ? -5.376  -40.230 -0.834  1.00 48.62  ? 1711 ASN B O   1 
ATOM   3950 C  CB  . ASN B 1 241 ? -6.341  -38.260 -3.283  1.00 57.99  ? 1711 ASN B CB  1 
ATOM   3951 C  CG  . ASN B 1 241 ? -5.932  -37.235 -4.307  1.00 59.44  ? 1711 ASN B CG  1 
ATOM   3952 O  OD1 . ASN B 1 241 ? -4.729  -37.031 -4.555  1.00 53.89  ? 1711 ASN B OD1 1 
ATOM   3953 N  ND2 . ASN B 1 241 ? -6.928  -36.561 -4.903  1.00 50.25  ? 1711 ASN B ND2 1 
ATOM   3954 N  N   . TRP B 1 242 ? -6.692  -41.216 -2.383  1.00 54.98  ? 1712 TRP B N   1 
ATOM   3955 C  CA  . TRP B 1 242 ? -7.198  -42.224 -1.456  1.00 52.37  ? 1712 TRP B CA  1 
ATOM   3956 C  C   . TRP B 1 242 ? -6.055  -43.046 -0.876  1.00 49.56  ? 1712 TRP B C   1 
ATOM   3957 O  O   . TRP B 1 242 ? -5.902  -43.147 0.351   1.00 45.26  ? 1712 TRP B O   1 
ATOM   3958 C  CB  . TRP B 1 242 ? -8.212  -43.114 -2.189  1.00 67.41  ? 1712 TRP B CB  1 
ATOM   3959 C  CG  . TRP B 1 242 ? -8.948  -44.119 -1.340  1.00 69.15  ? 1712 TRP B CG  1 
ATOM   3960 C  CD1 . TRP B 1 242 ? -8.780  -45.466 -1.350  1.00 66.63  ? 1712 TRP B CD1 1 
ATOM   3961 C  CD2 . TRP B 1 242 ? -9.985  -43.852 -0.381  1.00 69.70  ? 1712 TRP B CD2 1 
ATOM   3962 N  NE1 . TRP B 1 242 ? -9.636  -46.060 -0.453  1.00 66.93  ? 1712 TRP B NE1 1 
ATOM   3963 C  CE2 . TRP B 1 242 ? -10.386 -45.090 0.154   1.00 66.80  ? 1712 TRP B CE2 1 
ATOM   3964 C  CE3 . TRP B 1 242 ? -10.605 -42.688 0.077   1.00 53.77  ? 1712 TRP B CE3 1 
ATOM   3965 C  CZ2 . TRP B 1 242 ? -11.377 -45.197 1.124   1.00 63.11  ? 1712 TRP B CZ2 1 
ATOM   3966 C  CZ3 . TRP B 1 242 ? -11.587 -42.796 1.040   1.00 61.57  ? 1712 TRP B CZ3 1 
ATOM   3967 C  CH2 . TRP B 1 242 ? -11.964 -44.043 1.552   1.00 56.89  ? 1712 TRP B CH2 1 
ATOM   3968 N  N   . ASN B 1 243 ? -5.220  -43.616 -1.750  1.00 47.18  ? 1713 ASN B N   1 
ATOM   3969 C  CA  . ASN B 1 243 ? -4.089  -44.399 -1.279  1.00 48.88  ? 1713 ASN B CA  1 
ATOM   3970 C  C   . ASN B 1 243 ? -3.171  -43.575 -0.394  1.00 46.31  ? 1713 ASN B C   1 
ATOM   3971 O  O   . ASN B 1 243 ? -2.677  -44.080 0.612   1.00 46.44  ? 1713 ASN B O   1 
ATOM   3972 C  CB  . ASN B 1 243 ? -3.319  -44.959 -2.464  1.00 65.95  ? 1713 ASN B CB  1 
ATOM   3973 C  CG  . ASN B 1 243 ? -3.983  -46.170 -3.043  1.00 57.67  ? 1713 ASN B CG  1 
ATOM   3974 O  OD1 . ASN B 1 243 ? -4.798  -46.809 -2.379  1.00 56.44  ? 1713 ASN B OD1 1 
ATOM   3975 N  ND2 . ASN B 1 243 ? -3.680  -46.474 -4.295  1.00 59.86  ? 1713 ASN B ND2 1 
ATOM   3976 N  N   . LYS B 1 244 ? -2.957  -42.296 -0.734  1.00 47.95  ? 1714 LYS B N   1 
ATOM   3977 C  CA  . LYS B 1 244 ? -2.106  -41.428 0.081   1.00 56.49  ? 1714 LYS B CA  1 
ATOM   3978 C  C   . LYS B 1 244 ? -2.660  -41.306 1.498   1.00 54.37  ? 1714 LYS B C   1 
ATOM   3979 O  O   . LYS B 1 244 ? -1.916  -41.357 2.492   1.00 59.44  ? 1714 LYS B O   1 
ATOM   3980 C  CB  . LYS B 1 244 ? -1.997  -40.058 -0.599  1.00 61.16  ? 1714 LYS B CB  1 
ATOM   3981 C  CG  . LYS B 1 244 ? -0.880  -39.140 -0.136  1.00 77.18  ? 1714 LYS B CG  1 
ATOM   3982 C  CD  . LYS B 1 244 ? -0.532  -38.117 -1.234  1.00 76.28  ? 1714 LYS B CD  1 
ATOM   3983 C  CE  . LYS B 1 244 ? 0.836   -37.452 -1.025  1.00 73.54  ? 1714 LYS B CE  1 
ATOM   3984 N  NZ  . LYS B 1 244 ? 1.812   -38.217 -0.173  1.00 62.55  ? 1714 LYS B NZ  1 
ATOM   3985 N  N   . PHE B 1 245 ? -3.978  -41.177 1.606   1.00 55.77  ? 1715 PHE B N   1 
ATOM   3986 C  CA  . PHE B 1 245 ? -4.616  -41.086 2.911   1.00 42.28  ? 1715 PHE B CA  1 
ATOM   3987 C  C   . PHE B 1 245 ? -4.514  -42.411 3.671   1.00 49.86  ? 1715 PHE B C   1 
ATOM   3988 O  O   . PHE B 1 245 ? -4.175  -42.437 4.866   1.00 50.54  ? 1715 PHE B O   1 
ATOM   3989 C  CB  . PHE B 1 245 ? -6.070  -40.664 2.702   1.00 53.19  ? 1715 PHE B CB  1 
ATOM   3990 C  CG  . PHE B 1 245 ? -6.628  -39.864 3.816   1.00 54.66  ? 1715 PHE B CG  1 
ATOM   3991 C  CD1 . PHE B 1 245 ? -7.379  -40.476 4.809   1.00 54.57  ? 1715 PHE B CD1 1 
ATOM   3992 C  CD2 . PHE B 1 245 ? -6.411  -38.496 3.876   1.00 55.16  ? 1715 PHE B CD2 1 
ATOM   3993 C  CE1 . PHE B 1 245 ? -7.899  -39.738 5.845   1.00 46.08  ? 1715 PHE B CE1 1 
ATOM   3994 C  CE2 . PHE B 1 245 ? -6.941  -37.754 4.909   1.00 57.36  ? 1715 PHE B CE2 1 
ATOM   3995 C  CZ  . PHE B 1 245 ? -7.689  -38.384 5.896   1.00 53.47  ? 1715 PHE B CZ  1 
ATOM   3996 N  N   . LEU B 1 246 ? -4.789  -43.529 2.986   1.00 43.85  ? 1716 LEU B N   1 
ATOM   3997 C  CA  . LEU B 1 246 ? -4.641  -44.851 3.607   1.00 45.89  ? 1716 LEU B CA  1 
ATOM   3998 C  C   . LEU B 1 246 ? -3.206  -45.102 4.065   1.00 50.38  ? 1716 LEU B C   1 
ATOM   3999 O  O   . LEU B 1 246 ? -2.977  -45.705 5.119   1.00 45.80  ? 1716 LEU B O   1 
ATOM   4000 C  CB  . LEU B 1 246 ? -5.027  -45.940 2.615   1.00 50.10  ? 1716 LEU B CB  1 
ATOM   4001 C  CG  . LEU B 1 246 ? -6.486  -46.357 2.461   1.00 54.41  ? 1716 LEU B CG  1 
ATOM   4002 C  CD1 . LEU B 1 246 ? -7.439  -45.170 2.429   1.00 56.69  ? 1716 LEU B CD1 1 
ATOM   4003 C  CD2 . LEU B 1 246 ? -6.673  -47.247 1.243   1.00 56.29  ? 1716 LEU B CD2 1 
ATOM   4004 N  N   . MET B 1 247 ? -2.229  -44.644 3.278   1.00 56.02  ? 1717 MET B N   1 
ATOM   4005 C  CA  . MET B 1 247 ? -0.821  -44.800 3.634   1.00 61.07  ? 1717 MET B CA  1 
ATOM   4006 C  C   . MET B 1 247 ? -0.492  -44.011 4.881   1.00 58.07  ? 1717 MET B C   1 
ATOM   4007 O  O   . MET B 1 247 ? 0.257   -44.482 5.748   1.00 49.18  ? 1717 MET B O   1 
ATOM   4008 C  CB  . MET B 1 247 ? 0.080   -44.323 2.496   1.00 59.70  ? 1717 MET B CB  1 
ATOM   4009 C  CG  . MET B 1 247 ? 0.337   -45.342 1.398   1.00 85.33  ? 1717 MET B CG  1 
ATOM   4010 S  SD  . MET B 1 247 ? 1.298   -46.762 1.973   1.00 108.79 ? 1717 MET B SD  1 
ATOM   4011 C  CE  . MET B 1 247 ? 2.505   -45.954 3.024   1.00 72.21  ? 1717 MET B CE  1 
ATOM   4012 N  N   . ALA B 1 248 ? -1.031  -42.790 4.984   1.00 50.67  ? 1718 ALA B N   1 
ATOM   4013 C  CA  . ALA B 1 248 ? -0.758  -42.015 6.184   1.00 45.56  ? 1718 ALA B CA  1 
ATOM   4014 C  C   . ALA B 1 248 ? -1.364  -42.693 7.405   1.00 44.35  ? 1718 ALA B C   1 
ATOM   4015 O  O   . ALA B 1 248 ? -0.768  -42.677 8.492   1.00 54.59  ? 1718 ALA B O   1 
ATOM   4016 C  CB  . ALA B 1 248 ? -1.276  -40.578 6.026   1.00 43.16  ? 1718 ALA B CB  1 
ATOM   4017 N  N   . ILE B 1 249 ? -2.522  -43.333 7.233   1.00 45.03  ? 1719 ILE B N   1 
ATOM   4018 C  CA  . ILE B 1 249 ? -3.123  -44.060 8.348   1.00 55.41  ? 1719 ILE B CA  1 
ATOM   4019 C  C   . ILE B 1 249 ? -2.244  -45.237 8.731   1.00 62.73  ? 1719 ILE B C   1 
ATOM   4020 O  O   . ILE B 1 249 ? -1.916  -45.430 9.909   1.00 58.11  ? 1719 ILE B O   1 
ATOM   4021 C  CB  . ILE B 1 249 ? -4.553  -44.521 8.000   1.00 54.33  ? 1719 ILE B CB  1 
ATOM   4022 C  CG1 . ILE B 1 249 ? -5.526  -43.330 7.935   1.00 48.74  ? 1719 ILE B CG1 1 
ATOM   4023 C  CG2 . ILE B 1 249 ? -5.037  -45.512 9.039   1.00 63.27  ? 1719 ILE B CG2 1 
ATOM   4024 C  CD1 . ILE B 1 249 ? -6.838  -43.648 7.260   1.00 48.09  ? 1719 ILE B CD1 1 
ATOM   4025 N  N   . LYS B 1 250 ? -1.841  -46.031 7.731   1.00 59.79  ? 1720 LYS B N   1 
ATOM   4026 C  CA  . LYS B 1 250 ? -1.017  -47.216 7.977   1.00 57.50  ? 1720 LYS B CA  1 
ATOM   4027 C  C   . LYS B 1 250 ? 0.284   -46.868 8.686   1.00 54.21  ? 1720 LYS B C   1 
ATOM   4028 O  O   . LYS B 1 250 ? 0.677   -47.554 9.637   1.00 65.44  ? 1720 LYS B O   1 
ATOM   4029 C  CB  . LYS B 1 250 ? -0.725  -47.938 6.660   1.00 66.54  ? 1720 LYS B CB  1 
ATOM   4030 C  CG  . LYS B 1 250 ? 0.205   -49.136 6.801   1.00 61.70  ? 1720 LYS B CG  1 
ATOM   4031 C  CD  . LYS B 1 250 ? 0.457   -49.788 5.459   1.00 69.09  ? 1720 LYS B CD  1 
ATOM   4032 C  CE  . LYS B 1 250 ? 1.117   -51.151 5.638   1.00 69.08  ? 1720 LYS B CE  1 
ATOM   4033 N  NZ  . LYS B 1 250 ? 2.375   -51.082 6.455   1.00 74.62  ? 1720 LYS B NZ  1 
ATOM   4034 N  N   . THR B 1 251 ? 0.970   -45.804 8.245   1.00 48.84  ? 1721 THR B N   1 
ATOM   4035 C  CA  . THR B 1 251 ? 2.284   -45.481 8.797   1.00 62.77  ? 1721 THR B CA  1 
ATOM   4036 C  C   . THR B 1 251 ? 2.235   -44.659 10.079  1.00 63.01  ? 1721 THR B C   1 
ATOM   4037 O  O   . THR B 1 251 ? 3.197   -44.688 10.849  1.00 70.84  ? 1721 THR B O   1 
ATOM   4038 C  CB  . THR B 1 251 ? 3.158   -44.770 7.753   1.00 62.94  ? 1721 THR B CB  1 
ATOM   4039 O  OG1 . THR B 1 251 ? 2.629   -43.467 7.459   1.00 70.45  ? 1721 THR B OG1 1 
ATOM   4040 C  CG2 . THR B 1 251 ? 3.228   -45.616 6.478   1.00 66.88  ? 1721 THR B CG2 1 
ATOM   4041 N  N   . SER B 1 252 ? 1.162   -43.914 10.330  1.00 63.31  ? 1722 SER B N   1 
ATOM   4042 C  CA  . SER B 1 252 ? 1.116   -43.072 11.514  1.00 62.85  ? 1722 SER B CA  1 
ATOM   4043 C  C   . SER B 1 252 ? 0.109   -43.532 12.558  1.00 56.37  ? 1722 SER B C   1 
ATOM   4044 O  O   . SER B 1 252 ? 0.188   -43.084 13.706  1.00 58.72  ? 1722 SER B O   1 
ATOM   4045 C  CB  . SER B 1 252 ? 0.797   -41.625 11.122  1.00 63.41  ? 1722 SER B CB  1 
ATOM   4046 O  OG  . SER B 1 252 ? -0.595  -41.466 10.873  1.00 71.03  ? 1722 SER B OG  1 
ATOM   4047 N  N   . HIS B 1 253 ? -0.835  -44.394 12.186  1.00 53.77  ? 1723 HIS B N   1 
ATOM   4048 C  CA  . HIS B 1 253 ? -1.959  -44.773 13.046  1.00 75.08  ? 1723 HIS B CA  1 
ATOM   4049 C  C   . HIS B 1 253 ? -2.759  -43.553 13.509  1.00 77.57  ? 1723 HIS B C   1 
ATOM   4050 O  O   . HIS B 1 253 ? -3.402  -43.589 14.562  1.00 82.75  ? 1723 HIS B O   1 
ATOM   4051 C  CB  . HIS B 1 253 ? -1.488  -45.587 14.257  1.00 74.10  ? 1723 HIS B CB  1 
ATOM   4052 C  CG  . HIS B 1 253 ? -0.796  -46.858 13.888  1.00 89.73  ? 1723 HIS B CG  1 
ATOM   4053 N  ND1 . HIS B 1 253 ? -1.460  -48.063 13.777  1.00 95.99  ? 1723 HIS B ND1 1 
ATOM   4054 C  CD2 . HIS B 1 253 ? 0.501   -47.112 13.589  1.00 91.90  ? 1723 HIS B CD2 1 
ATOM   4055 C  CE1 . HIS B 1 253 ? -0.600  -49.005 13.429  1.00 94.54  ? 1723 HIS B CE1 1 
ATOM   4056 N  NE2 . HIS B 1 253 ? 0.596   -48.453 13.306  1.00 91.72  ? 1723 HIS B NE2 1 
ATOM   4057 N  N   . SER B 1 254 ? -2.723  -42.465 12.721  1.00 43.28  ? 1724 SER B N   1 
ATOM   4058 C  CA  . SER B 1 254 ? -3.519  -41.260 12.969  1.00 52.67  ? 1724 SER B CA  1 
ATOM   4059 C  C   . SER B 1 254 ? -4.973  -41.584 13.292  1.00 49.43  ? 1724 SER B C   1 
ATOM   4060 O  O   . SER B 1 254 ? -5.727  -41.955 12.384  1.00 39.06  ? 1724 SER B O   1 
ATOM   4061 C  CB  . SER B 1 254 ? -3.476  -40.330 11.760  1.00 55.81  ? 1724 SER B CB  1 
ATOM   4062 O  OG  . SER B 1 254 ? -3.947  -39.038 12.101  1.00 63.17  ? 1724 SER B OG  1 
ATOM   4063 N  N   . PRO B 1 255 ? -5.414  -41.432 14.549  1.00 53.61  ? 1725 PRO B N   1 
ATOM   4064 C  CA  . PRO B 1 255 ? -6.848  -41.635 14.836  1.00 45.19  ? 1725 PRO B CA  1 
ATOM   4065 C  C   . PRO B 1 255 ? -7.722  -40.655 14.094  1.00 54.12  ? 1725 PRO B C   1 
ATOM   4066 O  O   . PRO B 1 255 ? -8.873  -40.971 13.773  1.00 48.42  ? 1725 PRO B O   1 
ATOM   4067 C  CB  . PRO B 1 255 ? -6.950  -41.431 16.359  1.00 46.58  ? 1725 PRO B CB  1 
ATOM   4068 C  CG  . PRO B 1 255 ? -5.529  -41.415 16.870  1.00 60.37  ? 1725 PRO B CG  1 
ATOM   4069 C  CD  . PRO B 1 255 ? -4.681  -40.935 15.728  1.00 54.81  ? 1725 PRO B CD  1 
ATOM   4070 N  N   A VAL B 1 256 ? -7.205  -39.466 13.789  0.66 41.78  ? 1726 VAL B N   1 
ATOM   4071 N  N   B VAL B 1 256 ? -7.208  -39.459 13.794  0.34 44.23  ? 1726 VAL B N   1 
ATOM   4072 C  CA  A VAL B 1 256 ? -8.037  -38.465 13.140  0.66 46.53  ? 1726 VAL B CA  1 
ATOM   4073 C  CA  B VAL B 1 256 ? -8.041  -38.463 13.131  0.34 46.83  ? 1726 VAL B CA  1 
ATOM   4074 C  C   A VAL B 1 256 ? -8.297  -38.839 11.676  0.66 48.34  ? 1726 VAL B C   1 
ATOM   4075 C  C   B VAL B 1 256 ? -8.303  -38.859 11.677  0.34 48.00  ? 1726 VAL B C   1 
ATOM   4076 O  O   A VAL B 1 256 ? -9.432  -38.744 11.185  0.66 50.52  ? 1726 VAL B O   1 
ATOM   4077 O  O   B VAL B 1 256 ? -9.440  -38.779 11.190  0.34 49.92  ? 1726 VAL B O   1 
ATOM   4078 C  CB  A VAL B 1 256 ? -7.379  -37.084 13.315  0.66 54.15  ? 1726 VAL B CB  1 
ATOM   4079 C  CB  B VAL B 1 256 ? -7.410  -37.061 13.258  0.34 51.54  ? 1726 VAL B CB  1 
ATOM   4080 C  CG1 A VAL B 1 256 ? -7.832  -36.163 12.284  0.66 60.14  ? 1726 VAL B CG1 1 
ATOM   4081 C  CG1 B VAL B 1 256 ? -5.927  -37.076 13.007  0.34 42.92  ? 1726 VAL B CG1 1 
ATOM   4082 C  CG2 A VAL B 1 256 ? -7.693  -36.532 14.697  0.66 37.67  ? 1726 VAL B CG2 1 
ATOM   4083 C  CG2 B VAL B 1 256 ? -8.000  -36.180 12.283  0.34 57.67  ? 1726 VAL B CG2 1 
ATOM   4084 N  N   . CYS B 1 257 ? -7.271  -39.325 10.969  1.00 49.30  ? 1727 CYS B N   1 
ATOM   4085 C  CA  . CYS B 1 257 ? -7.496  -39.833 9.616   1.00 43.07  ? 1727 CYS B CA  1 
ATOM   4086 C  C   . CYS B 1 257 ? -8.319  -41.121 9.622   1.00 39.54  ? 1727 CYS B C   1 
ATOM   4087 O  O   . CYS B 1 257 ? -9.091  -41.371 8.685   1.00 47.45  ? 1727 CYS B O   1 
ATOM   4088 C  CB  . CYS B 1 257 ? -6.165  -40.050 8.906   1.00 59.06  ? 1727 CYS B CB  1 
ATOM   4089 S  SG  . CYS B 1 257 ? -5.059  -38.637 8.884   1.00 86.33  ? 1727 CYS B SG  1 
ATOM   4090 N  N   . GLN B 1 258 ? -8.185  -41.944 10.665  1.00 39.78  ? 1728 GLN B N   1 
ATOM   4091 C  CA  . GLN B 1 258 ? -9.034  -43.131 10.765  1.00 54.56  ? 1728 GLN B CA  1 
ATOM   4092 C  C   . GLN B 1 258 ? -10.495 -42.717 10.905  1.00 46.29  ? 1728 GLN B C   1 
ATOM   4093 O  O   . GLN B 1 258 ? -11.387 -43.336 10.314  1.00 46.94  ? 1728 GLN B O   1 
ATOM   4094 C  CB  . GLN B 1 258 ? -8.609  -43.999 11.955  1.00 42.66  ? 1728 GLN B CB  1 
ATOM   4095 C  CG  . GLN B 1 258 ? -7.227  -44.668 11.843  1.00 79.68  ? 1728 GLN B CG  1 
ATOM   4096 C  CD  . GLN B 1 258 ? -6.724  -45.241 13.181  1.00 85.09  ? 1728 GLN B CD  1 
ATOM   4097 O  OE1 . GLN B 1 258 ? -5.530  -45.172 13.503  1.00 80.30  ? 1728 GLN B OE1 1 
ATOM   4098 N  NE2 . GLN B 1 258 ? -7.643  -45.803 13.963  1.00 90.99  ? 1728 GLN B NE2 1 
ATOM   4099 N  N   . ASP B 1 259 ? -10.749 -41.663 11.689  1.00 48.62  ? 1729 ASP B N   1 
ATOM   4100 C  CA  . ASP B 1 259 ? -12.101 -41.132 11.823  1.00 47.11  ? 1729 ASP B CA  1 
ATOM   4101 C  C   . ASP B 1 259 ? -12.610 -40.591 10.493  1.00 40.31  ? 1729 ASP B C   1 
ATOM   4102 O  O   . ASP B 1 259 ? -13.771 -40.803 10.137  1.00 43.64  ? 1729 ASP B O   1 
ATOM   4103 C  CB  . ASP B 1 259 ? -12.135 -40.062 12.912  1.00 39.36  ? 1729 ASP B CB  1 
ATOM   4104 C  CG  . ASP B 1 259 ? -13.583 -39.656 13.328  1.00 50.34  ? 1729 ASP B CG  1 
ATOM   4105 O  OD1 . ASP B 1 259 ? -14.334 -40.504 13.862  1.00 50.32  ? 1729 ASP B OD1 1 
ATOM   4106 O  OD2 . ASP B 1 259 ? -13.953 -38.472 13.155  1.00 47.60  ? 1729 ASP B OD2 1 
ATOM   4107 N  N   . VAL B 1 260 ? -11.765 -39.880 9.749   1.00 45.64  ? 1730 VAL B N   1 
ATOM   4108 C  CA  . VAL B 1 260 ? -12.214 -39.412 8.435   1.00 42.73  ? 1730 VAL B CA  1 
ATOM   4109 C  C   . VAL B 1 260 ? -12.654 -40.593 7.597   1.00 41.16  ? 1730 VAL B C   1 
ATOM   4110 O  O   . VAL B 1 260 ? -13.683 -40.549 6.905   1.00 47.91  ? 1730 VAL B O   1 
ATOM   4111 C  CB  . VAL B 1 260 ? -11.128 -38.581 7.712   1.00 40.54  ? 1730 VAL B CB  1 
ATOM   4112 C  CG1 . VAL B 1 260 ? -11.572 -38.287 6.274   1.00 40.04  ? 1730 VAL B CG1 1 
ATOM   4113 C  CG2 . VAL B 1 260 ? -10.884 -37.278 8.429   1.00 38.51  ? 1730 VAL B CG2 1 
ATOM   4114 N  N   . LEU B 1 261 ? -11.847 -41.654 7.618   1.00 43.38  ? 1731 LEU B N   1 
ATOM   4115 C  CA  . LEU B 1 261 ? -12.147 -42.861 6.864   1.00 46.86  ? 1731 LEU B CA  1 
ATOM   4116 C  C   . LEU B 1 261 ? -13.486 -43.468 7.281   1.00 53.50  ? 1731 LEU B C   1 
ATOM   4117 O  O   . LEU B 1 261 ? -14.316 -43.817 6.428   1.00 44.45  ? 1731 LEU B O   1 
ATOM   4118 C  CB  . LEU B 1 261 ? -11.014 -43.868 7.073   1.00 47.97  ? 1731 LEU B CB  1 
ATOM   4119 C  CG  . LEU B 1 261 ? -10.801 -44.764 5.875   1.00 64.76  ? 1731 LEU B CG  1 
ATOM   4120 C  CD1 . LEU B 1 261 ? -10.470 -43.878 4.690   1.00 71.59  ? 1731 LEU B CD1 1 
ATOM   4121 C  CD2 . LEU B 1 261 ? -9.687  -45.760 6.168   1.00 77.38  ? 1731 LEU B CD2 1 
ATOM   4122 N  N   . LYS B 1 262 ? -13.685 -43.643 8.596   1.00 47.75  ? 1732 LYS B N   1 
ATOM   4123 C  CA  . LYS B 1 262 ? -14.962 -44.152 9.106   1.00 57.56  ? 1732 LYS B CA  1 
ATOM   4124 C  C   . LYS B 1 262 ? -16.115 -43.302 8.618   1.00 56.44  ? 1732 LYS B C   1 
ATOM   4125 O  O   . LYS B 1 262 ? -17.152 -43.829 8.181   1.00 45.45  ? 1732 LYS B O   1 
ATOM   4126 C  CB  . LYS B 1 262 ? -14.975 -44.196 10.637  1.00 62.58  ? 1732 LYS B CB  1 
ATOM   4127 N  N   . PHE B 1 263 ? -15.949 -41.974 8.687   1.00 47.01  ? 1733 PHE B N   1 
ATOM   4128 C  CA  . PHE B 1 263 ? -17.028 -41.102 8.263   1.00 49.02  ? 1733 PHE B CA  1 
ATOM   4129 C  C   . PHE B 1 263 ? -17.342 -41.311 6.790   1.00 48.16  ? 1733 PHE B C   1 
ATOM   4130 O  O   . PHE B 1 263 ? -18.513 -41.381 6.400   1.00 48.47  ? 1733 PHE B O   1 
ATOM   4131 C  CB  . PHE B 1 263 ? -16.706 -39.617 8.501   1.00 42.37  ? 1733 PHE B CB  1 
ATOM   4132 C  CG  . PHE B 1 263 ? -17.700 -38.729 7.832   1.00 50.10  ? 1733 PHE B CG  1 
ATOM   4133 C  CD1 . PHE B 1 263 ? -18.975 -38.587 8.378   1.00 48.71  ? 1733 PHE B CD1 1 
ATOM   4134 C  CD2 . PHE B 1 263 ? -17.432 -38.157 6.599   1.00 46.63  ? 1733 PHE B CD2 1 
ATOM   4135 C  CE1 . PHE B 1 263 ? -19.932 -37.825 7.746   1.00 52.28  ? 1733 PHE B CE1 1 
ATOM   4136 C  CE2 . PHE B 1 263 ? -18.392 -37.383 5.963   1.00 43.25  ? 1733 PHE B CE2 1 
ATOM   4137 C  CZ  . PHE B 1 263 ? -19.638 -37.219 6.532   1.00 52.80  ? 1733 PHE B CZ  1 
ATOM   4138 N  N   . ILE B 1 264 ? -16.307 -41.350 5.947   1.00 45.87  ? 1734 ILE B N   1 
ATOM   4139 C  CA  . ILE B 1 264 ? -16.548 -41.523 4.520   1.00 48.45  ? 1734 ILE B CA  1 
ATOM   4140 C  C   . ILE B 1 264 ? -17.268 -42.836 4.275   1.00 53.55  ? 1734 ILE B C   1 
ATOM   4141 O  O   . ILE B 1 264 ? -18.091 -42.943 3.362   1.00 52.97  ? 1734 ILE B O   1 
ATOM   4142 C  CB  . ILE B 1 264 ? -15.233 -41.438 3.729   1.00 49.60  ? 1734 ILE B CB  1 
ATOM   4143 C  CG1 . ILE B 1 264 ? -14.655 -40.027 3.801   1.00 47.74  ? 1734 ILE B CG1 1 
ATOM   4144 C  CG2 . ILE B 1 264 ? -15.451 -41.837 2.285   1.00 54.48  ? 1734 ILE B CG2 1 
ATOM   4145 C  CD1 . ILE B 1 264 ? -13.358 -39.886 3.050   1.00 54.10  ? 1734 ILE B CD1 1 
ATOM   4146 N  N   . SER B 1 265 ? -16.953 -43.855 5.075   1.00 50.31  ? 1735 SER B N   1 
ATOM   4147 C  CA  . SER B 1 265 ? -17.610 -45.153 4.932   1.00 67.43  ? 1735 SER B CA  1 
ATOM   4148 C  C   . SER B 1 265 ? -19.104 -45.049 5.229   1.00 62.56  ? 1735 SER B C   1 
ATOM   4149 O  O   . SER B 1 265 ? -19.939 -45.525 4.447   1.00 52.87  ? 1735 SER B O   1 
ATOM   4150 C  CB  . SER B 1 265 ? -16.930 -46.178 5.849   1.00 65.52  ? 1735 SER B CB  1 
ATOM   4151 O  OG  . SER B 1 265 ? -17.448 -47.471 5.647   1.00 82.37  ? 1735 SER B OG  1 
ATOM   4152 N  N   . GLN B 1 266 ? -19.462 -44.447 6.370   1.00 55.46  ? 1736 GLN B N   1 
ATOM   4153 C  CA  . GLN B 1 266 ? -20.886 -44.282 6.685   1.00 63.96  ? 1736 GLN B CA  1 
ATOM   4154 C  C   . GLN B 1 266 ? -21.591 -43.433 5.636   1.00 62.63  ? 1736 GLN B C   1 
ATOM   4155 O  O   . GLN B 1 266 ? -22.684 -43.776 5.167   1.00 57.63  ? 1736 GLN B O   1 
ATOM   4156 C  CB  . GLN B 1 266 ? -21.083 -43.637 8.056   1.00 55.40  ? 1736 GLN B CB  1 
ATOM   4157 C  CG  . GLN B 1 266 ? -20.449 -44.369 9.215   1.00 72.08  ? 1736 GLN B CG  1 
ATOM   4158 C  CD  . GLN B 1 266 ? -21.289 -44.281 10.471  1.00 96.43  ? 1736 GLN B CD  1 
ATOM   4159 O  OE1 . GLN B 1 266 ? -21.566 -43.185 10.971  1.00 99.98  ? 1736 GLN B OE1 1 
ATOM   4160 N  NE2 . GLN B 1 266 ? -21.719 -45.440 10.983  1.00 101.02 ? 1736 GLN B NE2 1 
ATOM   4161 N  N   . TRP B 1 267 ? -20.954 -42.349 5.222   1.00 48.45  ? 1737 TRP B N   1 
ATOM   4162 C  CA  . TRP B 1 267 ? -21.601 -41.344 4.395   1.00 54.34  ? 1737 TRP B CA  1 
ATOM   4163 C  C   . TRP B 1 267 ? -21.752 -41.818 2.961   1.00 59.33  ? 1737 TRP B C   1 
ATOM   4164 O  O   . TRP B 1 267 ? -22.778 -41.557 2.320   1.00 57.27  ? 1737 TRP B O   1 
ATOM   4165 C  CB  . TRP B 1 267 ? -20.776 -40.048 4.451   1.00 46.89  ? 1737 TRP B CB  1 
ATOM   4166 C  CG  . TRP B 1 267 ? -21.314 -38.890 3.647   1.00 71.25  ? 1737 TRP B CG  1 
ATOM   4167 C  CD1 . TRP B 1 267 ? -22.624 -38.596 3.398   1.00 74.59  ? 1737 TRP B CD1 1 
ATOM   4168 C  CD2 . TRP B 1 267 ? -20.543 -37.854 3.012   1.00 82.39  ? 1737 TRP B CD2 1 
ATOM   4169 N  NE1 . TRP B 1 267 ? -22.713 -37.451 2.636   1.00 81.19  ? 1737 TRP B NE1 1 
ATOM   4170 C  CE2 . TRP B 1 267 ? -21.450 -36.978 2.390   1.00 74.07  ? 1737 TRP B CE2 1 
ATOM   4171 C  CE3 . TRP B 1 267 ? -19.172 -37.595 2.899   1.00 80.46  ? 1737 TRP B CE3 1 
ATOM   4172 C  CZ2 . TRP B 1 267 ? -21.034 -35.862 1.669   1.00 70.55  ? 1737 TRP B CZ2 1 
ATOM   4173 C  CZ3 . TRP B 1 267 ? -18.763 -36.478 2.193   1.00 71.29  ? 1737 TRP B CZ3 1 
ATOM   4174 C  CH2 . TRP B 1 267 ? -19.689 -35.634 1.579   1.00 68.66  ? 1737 TRP B CH2 1 
ATOM   4175 N  N   . CYS B 1 268 ? -20.754 -42.535 2.450   1.00 50.38  ? 1738 CYS B N   1 
ATOM   4176 C  CA  . CYS B 1 268 ? -20.705 -42.856 1.036   1.00 63.88  ? 1738 CYS B CA  1 
ATOM   4177 C  C   . CYS B 1 268 ? -20.921 -44.331 0.738   1.00 68.63  ? 1738 CYS B C   1 
ATOM   4178 O  O   . CYS B 1 268 ? -20.966 -44.711 -0.437  1.00 77.86  ? 1738 CYS B O   1 
ATOM   4179 C  CB  . CYS B 1 268 ? -19.350 -42.401 0.489   1.00 68.66  ? 1738 CYS B CB  1 
ATOM   4180 S  SG  . CYS B 1 268 ? -19.193 -40.596 0.615   1.00 64.94  ? 1738 CYS B SG  1 
ATOM   4181 N  N   . GLY B 1 269 ? -21.106 -45.159 1.759   1.00 69.12  ? 1739 GLY B N   1 
ATOM   4182 C  CA  . GLY B 1 269 ? -21.646 -46.493 1.558   1.00 93.82  ? 1739 GLY B CA  1 
ATOM   4183 C  C   . GLY B 1 269 ? -20.667 -47.574 1.144   1.00 99.87  ? 1739 GLY B C   1 
ATOM   4184 O  O   . GLY B 1 269 ? -21.016 -48.435 0.325   1.00 105.49 ? 1739 GLY B O   1 
ATOM   4185 N  N   . GLY B 1 270 ? -19.459 -47.565 1.683   1.00 89.91  ? 1740 GLY B N   1 
ATOM   4186 C  CA  . GLY B 1 270 ? -18.520 -48.643 1.442   1.00 93.34  ? 1740 GLY B CA  1 
ATOM   4187 C  C   . GLY B 1 270 ? -17.502 -48.294 0.373   1.00 111.79 ? 1740 GLY B C   1 
ATOM   4188 O  O   . GLY B 1 270 ? -17.794 -47.580 -0.594  1.00 118.14 ? 1740 GLY B O   1 
ATOM   4189 N  N   . LEU B 1 271 ? -16.299 -48.865 0.514   1.00 114.08 ? 1741 LEU B N   1 
ATOM   4190 C  CA  . LEU B 1 271 ? -15.155 -48.583 -0.372  1.00 108.21 ? 1741 LEU B CA  1 
ATOM   4191 C  C   . LEU B 1 271 ? -15.354 -48.997 -1.832  1.00 98.63  ? 1741 LEU B C   1 
ATOM   4192 O  O   . LEU B 1 271 ? -15.934 -50.040 -2.125  1.00 103.33 ? 1741 LEU B O   1 
ATOM   4193 C  CB  . LEU B 1 271 ? -13.895 -49.258 0.176   1.00 107.22 ? 1741 LEU B CB  1 
HETATM 4194 N  N1  . EPE C 2 .   ? -4.797  -18.844 42.626  0.98 94.48  ? 1801 EPE A N1  1 
HETATM 4195 C  C2  . EPE C 2 .   ? -5.740  -19.771 43.289  0.98 95.89  ? 1801 EPE A C2  1 
HETATM 4196 C  C3  . EPE C 2 .   ? -5.213  -21.205 43.278  0.98 96.53  ? 1801 EPE A C3  1 
HETATM 4197 N  N4  . EPE C 2 .   ? -4.677  -21.590 41.983  0.98 101.64 ? 1801 EPE A N4  1 
HETATM 4198 C  C5  . EPE C 2 .   ? -3.833  -20.631 41.295  0.98 94.51  ? 1801 EPE A C5  1 
HETATM 4199 C  C6  . EPE C 2 .   ? -4.513  -19.278 41.247  0.98 97.29  ? 1801 EPE A C6  1 
HETATM 4200 C  C7  . EPE C 2 .   ? -4.504  -23.004 41.691  0.98 104.48 ? 1801 EPE A C7  1 
HETATM 4201 C  C8  . EPE C 2 .   ? -3.872  -23.265 40.321  0.98 101.80 ? 1801 EPE A C8  1 
HETATM 4202 O  O8  . EPE C 2 .   ? -2.461  -23.207 40.386  0.98 90.43  ? 1801 EPE A O8  1 
HETATM 4203 C  C9  . EPE C 2 .   ? -5.423  -17.524 42.535  0.98 99.36  ? 1801 EPE A C9  1 
HETATM 4204 C  C10 . EPE C 2 .   ? -4.469  -16.623 41.762  0.98 112.67 ? 1801 EPE A C10 1 
HETATM 4205 S  S   . EPE C 2 .   ? -4.624  -14.854 42.111  0.98 114.07 ? 1801 EPE A S   1 
HETATM 4206 O  O1S . EPE C 2 .   ? -5.987  -14.536 42.574  0.98 117.00 ? 1801 EPE A O1S 1 
HETATM 4207 O  O2S . EPE C 2 .   ? -3.633  -14.498 43.124  0.98 109.85 ? 1801 EPE A O2S 1 
HETATM 4208 O  O3S . EPE C 2 .   ? -4.326  -14.102 40.900  0.98 68.98  ? 1801 EPE A O3S 1 
HETATM 4209 CL CL  . CL  D 3 .   ? 33.243  -26.741 23.443  1.00 85.63  ? 1802 CL  A CL  1 
HETATM 4210 N  N1  . EPE E 2 .   ? 1.341   -26.272 -9.501  1.00 95.43  ? 1801 EPE B N1  1 
HETATM 4211 C  C2  . EPE E 2 .   ? 2.347   -27.243 -9.970  1.00 94.54  ? 1801 EPE B C2  1 
HETATM 4212 C  C3  . EPE E 2 .   ? 1.734   -28.608 -10.272 1.00 96.18  ? 1801 EPE B C3  1 
HETATM 4213 N  N4  . EPE E 2 .   ? 0.820   -29.033 -9.226  1.00 106.91 ? 1801 EPE B N4  1 
HETATM 4214 C  C5  . EPE E 2 .   ? -0.110  -28.051 -8.707  1.00 101.91 ? 1801 EPE B C5  1 
HETATM 4215 C  C6  . EPE E 2 .   ? 0.626   -26.783 -8.322  1.00 93.40  ? 1801 EPE B C6  1 
HETATM 4216 C  C7  . EPE E 2 .   ? 0.467   -30.439 -9.119  1.00 108.72 ? 1801 EPE B C7  1 
HETATM 4217 C  C8  . EPE E 2 .   ? -0.694  -30.834 -10.025 1.00 104.61 ? 1801 EPE B C8  1 
HETATM 4218 O  O8  . EPE E 2 .   ? -1.907  -30.410 -9.439  1.00 103.37 ? 1801 EPE B O8  1 
HETATM 4219 C  C9  . EPE E 2 .   ? 2.049   -25.052 -9.084  1.00 104.46 ? 1801 EPE B C9  1 
HETATM 4220 C  C10 . EPE E 2 .   ? 1.041   -24.064 -8.501  1.00 110.01 ? 1801 EPE B C10 1 
HETATM 4221 S  S   . EPE E 2 .   ? 1.526   -22.317 -8.574  1.00 100.62 ? 1801 EPE B S   1 
HETATM 4222 O  O1S . EPE E 2 .   ? 1.041   -21.638 -7.381  1.00 70.94  ? 1801 EPE B O1S 1 
HETATM 4223 O  O2S . EPE E 2 .   ? 2.989   -22.186 -8.657  1.00 110.42 ? 1801 EPE B O2S 1 
HETATM 4224 O  O3S . EPE E 2 .   ? 0.900   -21.726 -9.750  1.00 103.25 ? 1801 EPE B O3S 1 
HETATM 4225 O  O   . HOH F 4 .   ? -8.492  -11.061 34.573  1.00 61.33  ? 1901 HOH A O   1 
HETATM 4226 O  O   . HOH F 4 .   ? -4.141  -40.680 43.735  1.00 90.74  ? 1902 HOH A O   1 
HETATM 4227 O  O   . HOH F 4 .   ? 8.798   -19.881 41.240  1.00 45.95  ? 1903 HOH A O   1 
HETATM 4228 O  O   . HOH F 4 .   ? -10.824 -11.541 38.327  1.00 77.97  ? 1904 HOH A O   1 
HETATM 4229 O  O   . HOH F 4 .   ? 32.636  -23.701 24.172  1.00 66.54  ? 1905 HOH A O   1 
HETATM 4230 O  O   . HOH F 4 .   ? -2.893  -33.973 42.669  1.00 72.13  ? 1906 HOH A O   1 
HETATM 4231 O  O   . HOH F 4 .   ? -7.626  -31.675 29.593  1.00 54.63  ? 1907 HOH A O   1 
HETATM 4232 O  O   . HOH F 4 .   ? 11.426  -15.768 22.836  1.00 45.83  ? 1908 HOH A O   1 
HETATM 4233 O  O   . HOH F 4 .   ? 2.465   -17.308 28.128  1.00 45.15  ? 1909 HOH A O   1 
HETATM 4234 O  O   . HOH F 4 .   ? 10.073  -5.023  27.496  1.00 62.87  ? 1910 HOH A O   1 
HETATM 4235 O  O   . HOH F 4 .   ? 9.559   -43.594 33.616  1.00 56.81  ? 1911 HOH A O   1 
HETATM 4236 O  O   . HOH F 4 .   ? 6.974   -18.084 50.017  1.00 89.51  ? 1912 HOH A O   1 
HETATM 4237 O  O   . HOH F 4 .   ? 14.254  -14.602 45.689  1.00 75.90  ? 1913 HOH A O   1 
HETATM 4238 O  O   . HOH F 4 .   ? 8.237   -2.504  27.073  1.00 52.19  ? 1914 HOH A O   1 
HETATM 4239 O  O   . HOH F 4 .   ? -6.010  -33.102 16.374  1.00 61.81  ? 1915 HOH A O   1 
HETATM 4240 O  O   . HOH F 4 .   ? 16.722  -13.242 19.395  1.00 66.62  ? 1916 HOH A O   1 
HETATM 4241 O  O   . HOH F 4 .   ? 13.182  -24.382 14.273  1.00 53.90  ? 1917 HOH A O   1 
HETATM 4242 O  O   . HOH F 4 .   ? 8.817   -16.385 29.394  1.00 38.92  ? 1918 HOH A O   1 
HETATM 4243 O  O   . HOH F 4 .   ? 3.180   -8.338  47.194  1.00 75.28  ? 1919 HOH A O   1 
HETATM 4244 O  O   . HOH F 4 .   ? 3.446   -11.354 47.291  1.00 79.49  ? 1920 HOH A O   1 
HETATM 4245 O  O   . HOH F 4 .   ? 32.035  -24.661 18.384  1.00 66.69  ? 1921 HOH A O   1 
HETATM 4246 O  O   . HOH F 4 .   ? 4.512   -20.457 24.225  1.00 49.64  ? 1922 HOH A O   1 
HETATM 4247 O  O   . HOH F 4 .   ? -2.283  -41.680 34.429  1.00 55.33  ? 1923 HOH A O   1 
HETATM 4248 O  O   . HOH F 4 .   ? 1.658   -27.249 43.828  1.00 59.01  ? 1924 HOH A O   1 
HETATM 4249 O  O   . HOH F 4 .   ? 13.709  -12.166 38.168  1.00 47.53  ? 1925 HOH A O   1 
HETATM 4250 O  O   . HOH F 4 .   ? 12.016  -25.438 36.918  1.00 48.30  ? 1926 HOH A O   1 
HETATM 4251 O  O   . HOH F 4 .   ? 8.462   -16.395 25.088  1.00 45.62  ? 1927 HOH A O   1 
HETATM 4252 O  O   . HOH F 4 .   ? 10.569  -32.984 37.998  1.00 45.90  ? 1928 HOH A O   1 
HETATM 4253 O  O   . HOH F 4 .   ? -10.924 -13.882 38.518  1.00 64.01  ? 1929 HOH A O   1 
HETATM 4254 O  O   . HOH F 4 .   ? 7.134   -18.247 39.639  1.00 49.21  ? 1930 HOH A O   1 
HETATM 4255 O  O   . HOH F 4 .   ? -7.459  -25.184 31.495  1.00 69.67  ? 1931 HOH A O   1 
HETATM 4256 O  O   . HOH F 4 .   ? 6.328   -12.255 24.221  1.00 54.29  ? 1932 HOH A O   1 
HETATM 4257 O  O   . HOH F 4 .   ? 10.029  -30.044 35.789  1.00 45.62  ? 1933 HOH A O   1 
HETATM 4258 O  O   . HOH F 4 .   ? 1.823   -24.925 45.473  1.00 61.65  ? 1934 HOH A O   1 
HETATM 4259 O  O   . HOH F 4 .   ? 5.513   -0.618  41.917  1.00 77.81  ? 1935 HOH A O   1 
HETATM 4260 O  O   . HOH F 4 .   ? 1.343   -14.605 28.181  1.00 48.77  ? 1936 HOH A O   1 
HETATM 4261 O  O   . HOH F 4 .   ? 13.527  -31.174 16.010  1.00 61.73  ? 1937 HOH A O   1 
HETATM 4262 O  O   . HOH F 4 .   ? 19.782  -37.031 34.895  1.00 81.68  ? 1938 HOH A O   1 
HETATM 4263 O  O   . HOH F 4 .   ? 35.416  -25.165 17.300  1.00 69.43  ? 1939 HOH A O   1 
HETATM 4264 O  O   . HOH F 4 .   ? 13.673  -28.695 42.772  1.00 62.65  ? 1940 HOH A O   1 
HETATM 4265 O  O   . HOH F 4 .   ? -4.327  -35.136 14.909  1.00 54.55  ? 1941 HOH A O   1 
HETATM 4266 O  O   . HOH F 4 .   ? 8.320   -30.522 25.745  1.00 36.64  ? 1942 HOH A O   1 
HETATM 4267 O  O   . HOH F 4 .   ? 7.340   -16.251 31.697  1.00 42.49  ? 1943 HOH A O   1 
HETATM 4268 O  O   . HOH F 4 .   ? 22.530  -31.344 19.492  1.00 49.19  ? 1944 HOH A O   1 
HETATM 4269 O  O   . HOH F 4 .   ? 17.180  -31.006 32.726  1.00 53.02  ? 1945 HOH A O   1 
HETATM 4270 O  O   . HOH F 4 .   ? 25.230  -34.944 17.618  1.00 54.51  ? 1946 HOH A O   1 
HETATM 4271 O  O   . HOH F 4 .   ? 26.014  -32.379 20.910  1.00 61.93  ? 1947 HOH A O   1 
HETATM 4272 O  O   . HOH F 4 .   ? -4.804  -22.990 25.834  1.00 38.37  ? 1948 HOH A O   1 
HETATM 4273 O  O   . HOH F 4 .   ? -12.316 -27.886 26.403  1.00 75.18  ? 1949 HOH A O   1 
HETATM 4274 O  O   . HOH F 4 .   ? 9.488   2.211   37.772  1.00 62.91  ? 1950 HOH A O   1 
HETATM 4275 O  O   . HOH F 4 .   ? 19.709  -1.331  29.537  1.00 69.73  ? 1951 HOH A O   1 
HETATM 4276 O  O   . HOH F 4 .   ? 19.199  -11.734 20.724  1.00 70.56  ? 1952 HOH A O   1 
HETATM 4277 O  O   . HOH F 4 .   ? -1.539  -19.047 20.205  1.00 58.41  ? 1953 HOH A O   1 
HETATM 4278 O  O   . HOH F 4 .   ? 1.044   -31.007 43.515  1.00 48.39  ? 1954 HOH A O   1 
HETATM 4279 O  O   . HOH F 4 .   ? -9.956  -5.284  33.722  1.00 79.79  ? 1955 HOH A O   1 
HETATM 4280 O  O   . HOH F 4 .   ? -6.730  -34.304 36.147  1.00 50.58  ? 1956 HOH A O   1 
HETATM 4281 O  O   . HOH F 4 .   ? -3.808  -19.856 23.108  1.00 66.87  ? 1957 HOH A O   1 
HETATM 4282 O  O   . HOH F 4 .   ? 10.503  -27.270 12.668  1.00 74.81  ? 1958 HOH A O   1 
HETATM 4283 O  O   . HOH F 4 .   ? -0.445  -18.567 27.697  1.00 55.10  ? 1959 HOH A O   1 
HETATM 4284 O  O   . HOH F 4 .   ? 7.460   -22.923 15.108  1.00 67.39  ? 1960 HOH A O   1 
HETATM 4285 O  O   . HOH F 4 .   ? 14.236  -43.658 26.461  1.00 61.77  ? 1961 HOH A O   1 
HETATM 4286 O  O   . HOH F 4 .   ? 14.533  -8.101  26.580  1.00 66.01  ? 1962 HOH A O   1 
HETATM 4287 O  O   . HOH F 4 .   ? -1.040  -16.437 23.019  1.00 65.86  ? 1963 HOH A O   1 
HETATM 4288 O  O   . HOH F 4 .   ? 13.496  -9.127  38.467  1.00 73.80  ? 1964 HOH A O   1 
HETATM 4289 O  O   . HOH F 4 .   ? 22.810  -6.615  35.005  1.00 71.54  ? 1965 HOH A O   1 
HETATM 4290 O  O   . HOH F 4 .   ? 3.135   -12.230 24.173  1.00 54.55  ? 1966 HOH A O   1 
HETATM 4291 O  O   . HOH F 4 .   ? 17.773  -20.628 36.210  1.00 52.12  ? 1967 HOH A O   1 
HETATM 4292 O  O   . HOH F 4 .   ? 0.531   -25.767 17.815  1.00 62.13  ? 1968 HOH A O   1 
HETATM 4293 O  O   . HOH F 4 .   ? -2.460  -29.864 40.479  1.00 67.33  ? 1969 HOH A O   1 
HETATM 4294 O  O   . HOH F 4 .   ? 7.289   -10.486 21.120  1.00 57.71  ? 1970 HOH A O   1 
HETATM 4295 O  O   . HOH F 4 .   ? 16.368  -34.853 19.847  1.00 54.03  ? 1971 HOH A O   1 
HETATM 4296 O  O   . HOH F 4 .   ? 12.282  -31.297 36.557  1.00 54.18  ? 1972 HOH A O   1 
HETATM 4297 O  O   . HOH F 4 .   ? 19.432  -35.055 29.856  1.00 70.51  ? 1973 HOH A O   1 
HETATM 4298 O  O   . HOH F 4 .   ? 4.561   -2.928  44.544  1.00 72.67  ? 1974 HOH A O   1 
HETATM 4299 O  O   . HOH F 4 .   ? 18.497  -33.924 32.445  1.00 77.51  ? 1975 HOH A O   1 
HETATM 4300 O  O   . HOH F 4 .   ? 28.947  -35.155 18.752  1.00 62.91  ? 1976 HOH A O   1 
HETATM 4301 O  O   . HOH F 4 .   ? -9.656  -5.922  31.143  1.00 68.02  ? 1977 HOH A O   1 
HETATM 4302 O  O   . HOH F 4 .   ? 5.167   -46.547 37.442  1.00 73.55  ? 1978 HOH A O   1 
HETATM 4303 O  O   . HOH F 4 .   ? 8.482   -28.828 11.355  1.00 78.13  ? 1979 HOH A O   1 
HETATM 4304 O  O   . HOH F 4 .   ? -8.010  -10.614 29.813  1.00 67.13  ? 1980 HOH A O   1 
HETATM 4305 O  O   . HOH F 4 .   ? 14.647  -9.321  24.742  1.00 61.45  ? 1981 HOH A O   1 
HETATM 4306 O  O   . HOH F 4 .   ? -8.426  -34.934 33.556  1.00 60.64  ? 1982 HOH A O   1 
HETATM 4307 O  O   . HOH F 4 .   ? 23.420  -36.229 15.614  1.00 55.86  ? 1983 HOH A O   1 
HETATM 4308 O  O   . HOH F 4 .   ? 14.106  -30.341 38.051  1.00 64.94  ? 1984 HOH A O   1 
HETATM 4309 O  O   . HOH F 4 .   ? -7.595  -31.915 36.736  1.00 59.36  ? 1985 HOH A O   1 
HETATM 4310 O  O   . HOH F 4 .   ? -8.991  -33.259 41.859  1.00 69.31  ? 1986 HOH A O   1 
HETATM 4311 O  O   . HOH F 4 .   ? -3.657  -20.301 26.336  1.00 55.70  ? 1987 HOH A O   1 
HETATM 4312 O  O   . HOH F 4 .   ? 29.486  -19.380 25.392  1.00 85.76  ? 1988 HOH A O   1 
HETATM 4313 O  O   . HOH F 4 .   ? 16.342  -17.798 16.701  1.00 78.20  ? 1989 HOH A O   1 
HETATM 4314 O  O   . HOH F 4 .   ? 18.398  -10.360 27.147  1.00 62.67  ? 1990 HOH A O   1 
HETATM 4315 O  O   . HOH F 4 .   ? -3.307  -1.630  48.450  1.00 74.86  ? 1991 HOH A O   1 
HETATM 4316 O  O   . HOH F 4 .   ? 22.192  -11.866 29.160  1.00 65.64  ? 1992 HOH A O   1 
HETATM 4317 O  O   . HOH G 4 .   ? -2.681  -37.510 13.145  1.00 64.11  ? 1901 HOH B O   1 
HETATM 4318 O  O   . HOH G 4 .   ? -5.367  -24.380 5.219   1.00 55.91  ? 1902 HOH B O   1 
HETATM 4319 O  O   . HOH G 4 .   ? -20.449 -43.092 -6.382  1.00 64.17  ? 1903 HOH B O   1 
HETATM 4320 O  O   . HOH G 4 .   ? -7.502  -32.829 -10.896 1.00 52.26  ? 1904 HOH B O   1 
HETATM 4321 O  O   . HOH G 4 .   ? -14.360 -35.860 6.959   1.00 39.91  ? 1905 HOH B O   1 
HETATM 4322 O  O   . HOH G 4 .   ? -7.275  -30.427 -12.319 1.00 74.45  ? 1906 HOH B O   1 
HETATM 4323 O  O   . HOH G 4 .   ? -15.535 -15.718 -4.004  1.00 59.62  ? 1907 HOH B O   1 
HETATM 4324 O  O   . HOH G 4 .   ? -10.801 -22.281 8.990   1.00 45.60  ? 1908 HOH B O   1 
HETATM 4325 O  O   . HOH G 4 .   ? -14.263 -22.221 17.207  1.00 65.02  ? 1909 HOH B O   1 
HETATM 4326 O  O   . HOH G 4 .   ? -13.450 -20.962 11.042  1.00 41.74  ? 1910 HOH B O   1 
HETATM 4327 O  O   . HOH G 4 .   ? -0.066  -20.597 -12.696 1.00 70.63  ? 1911 HOH B O   1 
HETATM 4328 O  O   . HOH G 4 .   ? -15.423 -36.531 -12.435 1.00 61.50  ? 1912 HOH B O   1 
HETATM 4329 O  O   . HOH G 4 .   ? -18.197 -14.161 2.664   1.00 69.76  ? 1913 HOH B O   1 
HETATM 4330 O  O   . HOH G 4 .   ? -13.474 -42.873 14.565  1.00 73.85  ? 1914 HOH B O   1 
HETATM 4331 O  O   . HOH G 4 .   ? -9.174  -31.852 17.563  1.00 49.50  ? 1915 HOH B O   1 
HETATM 4332 O  O   . HOH G 4 .   ? -11.452 -21.696 4.294   1.00 39.89  ? 1916 HOH B O   1 
HETATM 4333 O  O   . HOH G 4 .   ? -8.237  -27.243 9.227   1.00 49.74  ? 1917 HOH B O   1 
HETATM 4334 O  O   . HOH G 4 .   ? -9.713  -10.571 6.976   1.00 53.02  ? 1918 HOH B O   1 
HETATM 4335 O  O   . HOH G 4 .   ? -2.445  -34.194 -3.567  1.00 60.80  ? 1919 HOH B O   1 
HETATM 4336 O  O   . HOH G 4 .   ? -10.476 -22.939 -5.818  1.00 47.59  ? 1920 HOH B O   1 
HETATM 4337 O  O   . HOH G 4 .   ? -5.755  -33.086 13.064  1.00 63.18  ? 1921 HOH B O   1 
HETATM 4338 O  O   . HOH G 4 .   ? -19.773 -36.697 16.647  1.00 74.57  ? 1922 HOH B O   1 
HETATM 4339 O  O   . HOH G 4 .   ? -9.733  -8.797  -6.453  1.00 59.46  ? 1923 HOH B O   1 
HETATM 4340 O  O   . HOH G 4 .   ? -11.839 -22.327 17.432  1.00 46.74  ? 1924 HOH B O   1 
HETATM 4341 O  O   . HOH G 4 .   ? -16.734 -29.391 -4.062  1.00 57.51  ? 1925 HOH B O   1 
HETATM 4342 O  O   . HOH G 4 .   ? 0.355   -34.584 0.356   1.00 60.31  ? 1926 HOH B O   1 
HETATM 4343 O  O   . HOH G 4 .   ? -4.431  -40.464 -10.348 1.00 75.14  ? 1927 HOH B O   1 
HETATM 4344 O  O   . HOH G 4 .   ? -24.754 -36.302 1.207   1.00 69.71  ? 1928 HOH B O   1 
HETATM 4345 O  O   . HOH G 4 .   ? -20.314 -21.116 -3.249  1.00 54.15  ? 1929 HOH B O   1 
HETATM 4346 O  O   . HOH G 4 .   ? -3.620  -21.687 5.524   1.00 49.96  ? 1930 HOH B O   1 
HETATM 4347 O  O   . HOH G 4 .   ? -22.515 -33.317 -1.332  1.00 58.74  ? 1931 HOH B O   1 
HETATM 4348 O  O   . HOH G 4 .   ? 2.932   -49.206 9.529   1.00 85.98  ? 1932 HOH B O   1 
HETATM 4349 O  O   . HOH G 4 .   ? -21.215 -23.590 -1.950  1.00 59.70  ? 1933 HOH B O   1 
HETATM 4350 O  O   . HOH G 4 .   ? -12.128 -24.118 -7.360  1.00 54.39  ? 1934 HOH B O   1 
HETATM 4351 O  O   . HOH G 4 .   ? -16.119 -34.063 -2.506  1.00 45.90  ? 1935 HOH B O   1 
HETATM 4352 O  O   . HOH G 4 .   ? -1.093  -27.603 4.204   1.00 50.52  ? 1936 HOH B O   1 
HETATM 4353 O  O   . HOH G 4 .   ? -10.126 -21.581 1.998   1.00 41.28  ? 1937 HOH B O   1 
HETATM 4354 O  O   . HOH G 4 .   ? -23.040 -33.593 0.886   1.00 66.35  ? 1938 HOH B O   1 
HETATM 4355 O  O   . HOH G 4 .   ? -17.442 -36.951 -5.087  1.00 58.31  ? 1939 HOH B O   1 
HETATM 4356 O  O   . HOH G 4 .   ? -16.861 -36.323 16.289  1.00 74.88  ? 1940 HOH B O   1 
HETATM 4357 O  O   . HOH G 4 .   ? -0.769  -42.159 -4.259  1.00 60.01  ? 1941 HOH B O   1 
HETATM 4358 O  O   . HOH G 4 .   ? 0.922   -41.032 2.946   1.00 61.60  ? 1942 HOH B O   1 
HETATM 4359 O  O   . HOH G 4 .   ? -28.098 -34.073 13.806  1.00 55.12  ? 1943 HOH B O   1 
HETATM 4360 O  O   . HOH G 4 .   ? -1.708  -27.809 12.981  1.00 40.61  ? 1944 HOH B O   1 
HETATM 4361 O  O   . HOH G 4 .   ? -14.860 -12.418 8.032   1.00 57.11  ? 1945 HOH B O   1 
HETATM 4362 O  O   . HOH G 4 .   ? -19.262 -14.055 13.109  1.00 81.90  ? 1946 HOH B O   1 
HETATM 4363 O  O   . HOH G 4 .   ? -8.181  -35.237 -8.195  1.00 49.86  ? 1947 HOH B O   1 
HETATM 4364 O  O   . HOH G 4 .   ? -7.920  -18.859 10.156  1.00 57.36  ? 1948 HOH B O   1 
HETATM 4365 O  O   . HOH G 4 .   ? 0.557   -25.418 3.657   1.00 66.64  ? 1949 HOH B O   1 
HETATM 4366 O  O   . HOH G 4 .   ? 3.289   -13.756 4.591   1.00 77.30  ? 1950 HOH B O   1 
HETATM 4367 O  O   . HOH G 4 .   ? -5.124  -19.476 9.664   1.00 50.12  ? 1951 HOH B O   1 
HETATM 4368 O  O   . HOH G 4 .   ? -15.750 -34.781 17.732  1.00 50.84  ? 1952 HOH B O   1 
HETATM 4369 O  O   . HOH G 4 .   ? 0.467   -31.436 7.056   1.00 46.55  ? 1953 HOH B O   1 
HETATM 4370 O  O   . HOH G 4 .   ? -2.966  -26.041 5.655   1.00 50.74  ? 1954 HOH B O   1 
HETATM 4371 O  O   . HOH G 4 .   ? -2.021  -24.111 9.675   1.00 65.33  ? 1955 HOH B O   1 
HETATM 4372 O  O   . HOH G 4 .   ? -14.129 -13.205 -3.748  1.00 54.57  ? 1956 HOH B O   1 
HETATM 4373 O  O   . HOH G 4 .   ? -3.863  -36.803 -7.561  1.00 76.71  ? 1957 HOH B O   1 
HETATM 4374 O  O   . HOH G 4 .   ? -7.063  -20.203 12.756  1.00 74.19  ? 1958 HOH B O   1 
HETATM 4375 O  O   . HOH G 4 .   ? -0.931  -43.684 -10.800 1.00 82.61  ? 1959 HOH B O   1 
HETATM 4376 O  O   . HOH G 4 .   ? -17.428 -17.111 15.269  1.00 72.66  ? 1960 HOH B O   1 
HETATM 4377 O  O   . HOH G 4 .   ? 4.623   -29.017 -3.577  1.00 63.24  ? 1961 HOH B O   1 
HETATM 4378 O  O   . HOH G 4 .   ? 2.289   -32.052 10.482  1.00 67.61  ? 1962 HOH B O   1 
HETATM 4379 O  O   . HOH G 4 .   ? -1.038  -40.833 15.868  1.00 69.02  ? 1963 HOH B O   1 
HETATM 4380 O  O   . HOH G 4 .   ? -37.505 -32.487 -4.898  1.00 72.00  ? 1964 HOH B O   1 
HETATM 4381 O  O   . HOH G 4 .   ? -22.506 0.975   -9.100  1.00 95.39  ? 1965 HOH B O   1 
HETATM 4382 O  O   . HOH G 4 .   ? -4.135  -37.952 15.397  1.00 61.93  ? 1966 HOH B O   1 
HETATM 4383 O  O   . HOH G 4 .   ? -5.789  -33.653 -6.937  1.00 47.58  ? 1967 HOH B O   1 
HETATM 4384 O  O   . HOH G 4 .   ? -18.382 -34.932 -3.493  1.00 60.83  ? 1968 HOH B O   1 
HETATM 4385 O  O   . HOH G 4 .   ? -20.434 -17.493 6.935   1.00 51.89  ? 1969 HOH B O   1 
HETATM 4386 O  O   . HOH G 4 .   ? -21.831 -28.472 -3.691  1.00 73.19  ? 1970 HOH B O   1 
HETATM 4387 O  O   . HOH G 4 .   ? -25.925 -17.955 2.064   1.00 68.36  ? 1971 HOH B O   1 
HETATM 4388 O  O   . HOH G 4 .   ? -8.808  -2.961  -3.044  1.00 83.80  ? 1972 HOH B O   1 
HETATM 4389 O  O   . HOH G 4 .   ? -1.786  -21.917 10.840  1.00 60.62  ? 1973 HOH B O   1 
HETATM 4390 O  O   . HOH G 4 .   ? -18.942 -29.798 -4.973  1.00 66.02  ? 1974 HOH B O   1 
HETATM 4391 O  O   . HOH G 4 .   ? -1.281  -25.537 12.153  1.00 62.30  ? 1975 HOH B O   1 
HETATM 4392 O  O   . HOH G 4 .   ? -36.784 -30.660 16.371  1.00 76.65  ? 1976 HOH B O   1 
HETATM 4393 O  O   . HOH G 4 .   ? -9.416  -49.015 -3.455  1.00 74.68  ? 1977 HOH B O   1 
HETATM 4394 O  O   . HOH G 4 .   ? -0.422  -28.420 6.782   1.00 52.44  ? 1978 HOH B O   1 
HETATM 4395 O  O   . HOH G 4 .   ? -17.178 -13.427 8.827   1.00 70.35  ? 1979 HOH B O   1 
HETATM 4396 O  O   . HOH G 4 .   ? -5.703  -15.469 11.398  1.00 61.76  ? 1980 HOH B O   1 
HETATM 4397 O  O   . HOH G 4 .   ? 5.183   -15.473 8.055   1.00 72.83  ? 1981 HOH B O   1 
HETATM 4398 O  O   . HOH G 4 .   ? 2.316   -44.911 -6.794  1.00 93.23  ? 1982 HOH B O   1 
HETATM 4399 O  O   . HOH G 4 .   ? -38.465 -34.351 15.240  1.00 84.53  ? 1983 HOH B O   1 
HETATM 4400 O  O   . HOH G 4 .   ? 5.412   -31.244 -1.732  1.00 82.05  ? 1984 HOH B O   1 
HETATM 4401 O  O   . HOH G 4 .   ? -40.798 -28.546 11.098  1.00 91.68  ? 1985 HOH B 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   . ALA A 1   ? 0.6246 1.3920 1.6152 -0.1983 0.2206  -0.0923 1471 ALA A N   
2    C  CA  . ALA A 1   ? 0.8290 1.5649 1.7926 -0.1809 0.2271  -0.0913 1471 ALA A CA  
3    C  C   . ALA A 1   ? 0.7780 1.5308 1.7596 -0.1513 0.2199  -0.1002 1471 ALA A C   
4    O  O   . ALA A 1   ? 0.9610 1.7494 1.9616 -0.1414 0.2272  -0.1055 1471 ALA A O   
5    C  CB  . ALA A 1   ? 0.9892 1.7225 1.9332 -0.1890 0.2482  -0.0861 1471 ALA A CB  
6    N  N   . PRO A 2   ? 0.4331 1.1601 1.4090 -0.1370 0.2050  -0.1016 1472 PRO A N   
7    C  CA  . PRO A 2   ? 0.4217 1.1588 1.4119 -0.1086 0.1963  -0.1088 1472 PRO A CA  
8    C  C   . PRO A 2   ? 0.4253 1.1266 1.3876 -0.0926 0.2019  -0.1070 1472 PRO A C   
9    O  O   . PRO A 2   ? 0.4578 1.1204 1.3894 -0.1019 0.2076  -0.1000 1472 PRO A O   
10   C  CB  . PRO A 2   ? 0.4124 1.1463 1.4165 -0.1054 0.1746  -0.1107 1472 PRO A CB  
11   C  CG  . PRO A 2   ? 0.5376 1.2321 1.5149 -0.1245 0.1745  -0.1030 1472 PRO A CG  
12   C  CD  . PRO A 2   ? 0.6004 1.2956 1.5640 -0.1473 0.1927  -0.0976 1472 PRO A CD  
13   N  N   . ALA A 3   ? 0.4085 1.1210 1.3809 -0.0683 0.1996  -0.1133 1473 ALA A N   
14   C  CA  . ALA A 3   ? 0.4011 1.0806 1.3487 -0.0525 0.2037  -0.1122 1473 ALA A CA  
15   C  C   . ALA A 3   ? 0.3862 1.0319 1.3246 -0.0426 0.1879  -0.1095 1473 ALA A C   
16   O  O   . ALA A 3   ? 0.3818 1.0375 1.3395 -0.0389 0.1713  -0.1114 1473 ALA A O   
17   C  CB  . ALA A 3   ? 0.4062 1.1080 1.3666 -0.0303 0.2072  -0.1202 1473 ALA A CB  
18   N  N   . ASN A 4   ? 0.3798 0.9859 1.2883 -0.0384 0.1930  -0.1047 1474 ASN A N   
19   C  CA  . ASN A 4   ? 0.3970 0.9682 1.2933 -0.0285 0.1806  -0.1010 1474 ASN A CA  
20   C  C   . ASN A 4   ? 0.3646 0.9221 1.2525 -0.0055 0.1811  -0.1036 1474 ASN A C   
21   O  O   . ASN A 4   ? 0.4849 1.0100 1.3455 -0.0047 0.1889  -0.0993 1474 ASN A O   
22   C  CB  . ASN A 4   ? 0.3625 0.8962 1.2302 -0.0452 0.1856  -0.0924 1474 ASN A CB  
23   C  CG  . ASN A 4   ? 0.3968 0.9405 1.2705 -0.0686 0.1850  -0.0901 1474 ASN A CG  
24   O  OD1 . ASN A 4   ? 0.4888 1.0466 1.3609 -0.0841 0.1973  -0.0894 1474 ASN A OD1 
25   N  ND2 . ASN A 4   ? 0.3662 0.9041 1.2479 -0.0714 0.1700  -0.0892 1474 ASN A ND2 
26   N  N   . PRO A 5   ? 0.3699 0.9510 1.2806 0.0135  0.1723  -0.1106 1475 PRO A N   
27   C  CA  . PRO A 5   ? 0.3737 0.9430 1.2760 0.0347  0.1739  -0.1141 1475 PRO A CA  
28   C  C   . PRO A 5   ? 0.3617 0.8860 1.2403 0.0430  0.1678  -0.1080 1475 PRO A C   
29   O  O   . PRO A 5   ? 0.3645 0.8701 1.2257 0.0530  0.1745  -0.1088 1475 PRO A O   
30   C  CB  . PRO A 5   ? 0.3782 0.9789 1.3113 0.0532  0.1612  -0.1220 1475 PRO A CB  
31   C  CG  . PRO A 5   ? 0.4127 1.0386 1.3694 0.0423  0.1509  -0.1219 1475 PRO A CG  
32   C  CD  . PRO A 5   ? 0.3736 0.9959 1.3186 0.0156  0.1622  -0.1166 1475 PRO A CD  
33   N  N   . GLN A 6   ? 0.3520 0.8590 1.2291 0.0387  0.1559  -0.1020 1476 GLN A N   
34   C  CA  . GLN A 6   ? 0.4629 0.9287 1.3182 0.0456  0.1508  -0.0954 1476 GLN A CA  
35   C  C   . GLN A 6   ? 0.4377 0.8744 1.2656 0.0284  0.1617  -0.0878 1476 GLN A C   
36   O  O   . GLN A 6   ? 0.3314 0.7343 1.1397 0.0331  0.1598  -0.0821 1476 GLN A O   
37   C  CB  . GLN A 6   ? 0.5120 0.9744 1.3807 0.0536  0.1306  -0.0928 1476 GLN A CB  
38   C  CG  . GLN A 6   ? 0.6076 1.0805 1.4929 0.0773  0.1175  -0.0979 1476 GLN A CG  
39   C  CD  . GLN A 6   ? 0.6148 1.1056 1.5246 0.0822  0.0976  -0.0984 1476 GLN A CD  
40   O  OE1 . GLN A 6   ? 0.3879 0.9067 1.3156 0.0697  0.0959  -0.1010 1476 GLN A OE1 
41   N  NE2 . GLN A 6   ? 0.6307 1.1045 1.5408 0.1000  0.0814  -0.0955 1476 GLN A NE2 
42   N  N   . ASN A 7   ? 0.3404 0.7887 1.1660 0.0089  0.1729  -0.0873 1477 ASN A N   
43   C  CA  . ASN A 7   ? 0.3388 0.7604 1.1374 -0.0074 0.1841  -0.0806 1477 ASN A CA  
44   C  C   . ASN A 7   ? 0.3301 0.7287 1.1212 -0.0158 0.1756  -0.0739 1477 ASN A C   
45   O  O   . ASN A 7   ? 0.3275 0.6955 1.0936 -0.0226 0.1817  -0.0678 1477 ASN A O   
46   C  CB  . ASN A 7   ? 0.3494 0.7446 1.1227 0.0005  0.1936  -0.0788 1477 ASN A CB  
47   C  CG  . ASN A 7   ? 0.4065 0.8207 1.1797 0.0018  0.2067  -0.0845 1477 ASN A CG  
48   O  OD1 . ASN A 7   ? 0.3585 0.8019 1.1447 -0.0088 0.2128  -0.0875 1477 ASN A OD1 
49   N  ND2 . ASN A 7   ? 0.3530 0.7511 1.1113 0.0142  0.2114  -0.0861 1477 ASN A ND2 
50   N  N   . PHE A 8   ? 0.4221 0.8357 1.2346 -0.0148 0.1613  -0.0753 1478 PHE A N   
51   C  CA  . PHE A 8   ? 0.3899 0.7852 1.1972 -0.0234 0.1528  -0.0700 1478 PHE A CA  
52   C  C   . PHE A 8   ? 0.3239 0.7036 1.1123 -0.0451 0.1630  -0.0658 1478 PHE A C   
53   O  O   . PHE A 8   ? 0.3208 0.6695 1.0887 -0.0493 0.1637  -0.0601 1478 PHE A O   
54   C  CB  . PHE A 8   ? 0.3761 0.7976 1.2121 -0.0225 0.1365  -0.0738 1478 PHE A CB  
55   C  CG  . PHE A 8   ? 0.4327 0.8629 1.2848 -0.0001 0.1229  -0.0762 1478 PHE A CG  
56   C  CD1 . PHE A 8   ? 0.3726 0.8333 1.2534 0.0048  0.1083  -0.0812 1478 PHE A CD1 
57   C  CD2 . PHE A 8   ? 0.6003 1.0063 1.4379 0.0160  0.1235  -0.0730 1478 PHE A CD2 
58   C  CE1 . PHE A 8   ? 0.5360 1.0018 1.4299 0.0264  0.0942  -0.0827 1478 PHE A CE1 
59   C  CE2 . PHE A 8   ? 0.5025 0.9125 1.3527 0.0365  0.1099  -0.0744 1478 PHE A CE2 
60   C  CZ  . PHE A 8   ? 0.5316 0.9706 1.4095 0.0421  0.0951  -0.0790 1478 PHE A CZ  
61   N  N   . ASN A 9   ? 0.3341 0.7346 1.1287 -0.0590 0.1708  -0.0685 1479 ASN A N   
62   C  CA  . ASN A 9   ? 0.3421 0.7267 1.1189 -0.0801 0.1788  -0.0641 1479 ASN A CA  
63   C  C   . ASN A 9   ? 0.3431 0.6947 1.0885 -0.0801 0.1908  -0.0585 1479 ASN A C   
64   O  O   . ASN A 9   ? 0.4534 0.7754 1.1785 -0.0894 0.1917  -0.0531 1479 ASN A O   
65   C  CB  . ASN A 9   ? 0.3757 0.7904 1.1657 -0.0949 0.1851  -0.0673 1479 ASN A CB  
66   C  CG  . ASN A 9   ? 0.3951 0.8338 1.1920 -0.0863 0.1955  -0.0714 1479 ASN A CG  
67   O  OD1 . ASN A 9   ? 0.3997 0.8394 1.1990 -0.0670 0.1943  -0.0742 1479 ASN A OD1 
68   N  ND2 . ASN A 9   ? 0.3741 0.8317 1.1735 -0.1013 0.2057  -0.0717 1479 ASN A ND2 
69   N  N   . ILE A 10  ? 0.3437 0.6995 1.0847 -0.0688 0.1992  -0.0602 1480 ILE A N   
70   C  CA  . ILE A 10  ? 0.3461 0.6732 1.0582 -0.0685 0.2103  -0.0556 1480 ILE A CA  
71   C  C   . ILE A 10  ? 0.3657 0.6594 1.0621 -0.0610 0.2042  -0.0508 1480 ILE A C   
72   O  O   . ILE A 10  ? 0.3814 0.6464 1.0545 -0.0690 0.2087  -0.0451 1480 ILE A O   
73   C  CB  . ILE A 10  ? 0.3491 0.6891 1.0621 -0.0560 0.2185  -0.0600 1480 ILE A CB  
74   C  CG1 . ILE A 10  ? 0.5042 0.8808 1.2338 -0.0636 0.2256  -0.0650 1480 ILE A CG1 
75   C  CG2 . ILE A 10  ? 0.3521 0.6627 1.0354 -0.0554 0.2289  -0.0556 1480 ILE A CG2 
76   C  CD1 . ILE A 10  ? 0.3753 0.7474 1.0882 -0.0832 0.2386  -0.0605 1480 ILE A CD1 
77   N  N   . TYR A 11  ? 0.4956 0.7926 1.2044 -0.0452 0.1938  -0.0527 1481 TYR A N   
78   C  CA  . TYR A 11  ? 0.4590 0.7266 1.1532 -0.0374 0.1891  -0.0479 1481 TYR A CA  
79   C  C   . TYR A 11  ? 0.3539 0.6046 1.0378 -0.0486 0.1816  -0.0437 1481 TYR A C   
80   O  O   . TYR A 11  ? 0.3190 0.5376 0.9747 -0.0499 0.1819  -0.0385 1481 TYR A O   
81   C  CB  . TYR A 11  ? 0.3094 0.5838 1.0178 -0.0181 0.1791  -0.0502 1481 TYR A CB  
82   C  CG  . TYR A 11  ? 0.3246 0.6005 1.0289 -0.0051 0.1850  -0.0535 1481 TYR A CG  
83   C  CD1 . TYR A 11  ? 0.3139 0.5640 0.9935 -0.0030 0.1933  -0.0504 1481 TYR A CD1 
84   C  CD2 . TYR A 11  ? 0.3170 0.6198 1.0422 0.0057  0.1814  -0.0604 1481 TYR A CD2 
85   C  CE1 . TYR A 11  ? 0.3231 0.5735 0.9983 0.0084  0.1981  -0.0542 1481 TYR A CE1 
86   C  CE2 . TYR A 11  ? 0.3225 0.6255 1.0432 0.0180  0.1866  -0.0645 1481 TYR A CE2 
87   C  CZ  . TYR A 11  ? 0.3300 0.6065 1.0255 0.0190  0.1949  -0.0615 1481 TYR A CZ  
88   O  OH  . TYR A 11  ? 0.3303 0.6060 1.0205 0.0307  0.1994  -0.0663 1481 TYR A OH  
89   N  N   . LYS A 12  ? 0.4258 0.6961 1.1277 -0.0562 0.1734  -0.0466 1482 LYS A N   
90   C  CA  . LYS A 12  ? 0.3976 0.6495 1.0840 -0.0674 0.1652  -0.0438 1482 LYS A CA  
91   C  C   . LYS A 12  ? 0.3728 0.6044 1.0402 -0.0829 0.1763  -0.0405 1482 LYS A C   
92   O  O   . LYS A 12  ? 0.3388 0.5393 0.9801 -0.0857 0.1730  -0.0366 1482 LYS A O   
93   C  CB  . LYS A 12  ? 0.3295 0.6087 1.0406 -0.0745 0.1550  -0.0486 1482 LYS A CB  
94   C  CG  . LYS A 12  ? 0.6341 0.8949 1.3295 -0.0846 0.1441  -0.0473 1482 LYS A CG  
95   C  CD  . LYS A 12  ? 0.7633 1.0477 1.4792 -0.0839 0.1282  -0.0519 1482 LYS A CD  
96   C  CE  . LYS A 12  ? 0.7748 1.0420 1.4749 -0.0958 0.1179  -0.0522 1482 LYS A CE  
97   N  NZ  . LYS A 12  ? 0.5476 0.8429 1.2720 -0.1024 0.1049  -0.0581 1482 LYS A NZ  
98   N  N   A ARG A 13  ? 0.3541 0.6025 1.0331 -0.0924 0.1895  -0.0418 1483 ARG A N   
99   N  N   B ARG A 13  ? 0.3492 0.5972 1.0281 -0.0926 0.1894  -0.0418 1483 ARG A N   
100  C  CA  A ARG A 13  ? 0.4030 0.6297 1.0588 -0.1069 0.1985  -0.0375 1483 ARG A CA  
101  C  CA  B ARG A 13  ? 0.4060 0.6319 1.0620 -0.1078 0.1977  -0.0374 1483 ARG A CA  
102  C  C   A ARG A 13  ? 0.4027 0.5974 1.0322 -0.1000 0.2043  -0.0324 1483 ARG A C   
103  C  C   B ARG A 13  ? 0.4128 0.6069 1.0422 -0.1011 0.2040  -0.0323 1483 ARG A C   
104  O  O   A ARG A 13  ? 0.3576 0.5229 0.9644 -0.1075 0.2041  -0.0282 1483 ARG A O   
105  O  O   B ARG A 13  ? 0.3671 0.5320 0.9737 -0.1090 0.2042  -0.0281 1483 ARG A O   
106  C  CB  A ARG A 13  ? 0.3706 0.6184 1.0306 -0.1151 0.2083  -0.0388 1483 ARG A CB  
107  C  CB  B ARG A 13  ? 0.3682 0.6144 1.0284 -0.1178 0.2068  -0.0386 1483 ARG A CB  
108  C  CG  A ARG A 13  ? 0.4847 0.7144 1.1244 -0.1336 0.2158  -0.0339 1483 ARG A CG  
109  C  CG  B ARG A 13  ? 0.4501 0.7200 1.1303 -0.1317 0.2013  -0.0421 1483 ARG A CG  
110  C  CD  A ARG A 13  ? 0.6953 0.9545 1.3475 -0.1459 0.2221  -0.0358 1483 ARG A CD  
111  C  CD  B ARG A 13  ? 0.6809 0.9563 1.3537 -0.1484 0.2118  -0.0398 1483 ARG A CD  
112  N  NE  A ARG A 13  ? 0.6716 0.9624 1.3536 -0.1477 0.2128  -0.0418 1483 ARG A NE  
113  N  NE  B ARG A 13  ? 0.7113 0.9830 1.3697 -0.1420 0.2244  -0.0375 1483 ARG A NE  
114  C  CZ  A ARG A 13  ? 0.6237 0.9519 1.3273 -0.1505 0.2157  -0.0461 1483 ARG A CZ  
115  C  CZ  B ARG A 13  ? 0.6260 0.9273 1.2978 -0.1356 0.2310  -0.0416 1483 ARG A CZ  
116  N  NH1 A ARG A 13  ? 0.7208 1.0605 1.4192 -0.1523 0.2287  -0.0453 1483 ARG A NH1 
117  N  NH1 B ARG A 13  ? 0.4023 0.6970 1.0584 -0.1302 0.2421  -0.0399 1483 ARG A NH1 
118  N  NH2 A ARG A 13  ? 0.4029 0.7584 1.1339 -0.1514 0.2054  -0.0516 1483 ARG A NH2 
119  N  NH2 B ARG A 13  ? 0.7136 1.0515 1.4143 -0.1344 0.2262  -0.0478 1483 ARG A NH2 
120  N  N   A ILE A 14  ? 0.3410 0.5392 0.9700 -0.0849 0.2080  -0.0331 1484 ILE A N   
121  N  N   B ILE A 14  ? 0.3414 0.5390 0.9703 -0.0860 0.2076  -0.0330 1484 ILE A N   
122  C  CA  A ILE A 14  ? 0.3709 0.5401 0.9750 -0.0789 0.2131  -0.0287 1484 ILE A CA  
123  C  CA  B ILE A 14  ? 0.3703 0.5390 0.9741 -0.0802 0.2130  -0.0285 1484 ILE A CA  
124  C  C   A ILE A 14  ? 0.4334 0.5760 1.0189 -0.0723 0.2013  -0.0259 1484 ILE A C   
125  C  C   B ILE A 14  ? 0.4397 0.5821 1.0250 -0.0727 0.2012  -0.0259 1484 ILE A C   
126  O  O   A ILE A 14  ? 0.4012 0.5154 0.9623 -0.0744 0.2026  -0.0218 1484 ILE A O   
127  O  O   B ILE A 14  ? 0.4017 0.5156 0.9627 -0.0745 0.2024  -0.0218 1484 ILE A O   
128  C  CB  A ILE A 14  ? 0.4018 0.5791 1.0071 -0.0646 0.2186  -0.0309 1484 ILE A CB  
129  C  CB  B ILE A 14  ? 0.4059 0.5831 1.0105 -0.0668 0.2192  -0.0307 1484 ILE A CB  
130  C  CG1 A ILE A 14  ? 0.3226 0.5075 0.9417 -0.0482 0.2089  -0.0335 1484 ILE A CG1 
131  C  CG1 B ILE A 14  ? 0.4922 0.6794 1.0914 -0.0753 0.2308  -0.0313 1484 ILE A CG1 
132  C  CG2 A ILE A 14  ? 0.4471 0.6499 1.0613 -0.0690 0.2265  -0.0347 1484 ILE A CG2 
133  C  CG2 B ILE A 14  ? 0.3328 0.4821 0.9161 -0.0575 0.2203  -0.0270 1484 ILE A CG2 
134  C  CD1 A ILE A 14  ? 0.4768 0.6444 1.0813 -0.0343 0.2104  -0.0324 1484 ILE A CD1 
135  C  CD1 B ILE A 14  ? 0.5076 0.7295 1.1282 -0.0704 0.2326  -0.0378 1484 ILE A CD1 
136  N  N   . PHE A 15  ? 0.3824 0.5346 0.9788 -0.0647 0.1894  -0.0281 1485 PHE A N   
137  C  CA  . PHE A 15  ? 0.4028 0.5324 0.9813 -0.0609 0.1787  -0.0258 1485 PHE A CA  
138  C  C   . PHE A 15  ? 0.3417 0.4535 0.9059 -0.0747 0.1775  -0.0247 1485 PHE A C   
139  O  O   . PHE A 15  ? 0.4468 0.5312 0.9877 -0.0739 0.1776  -0.0218 1485 PHE A O   
140  C  CB  . PHE A 15  ? 0.3261 0.4708 0.9184 -0.0533 0.1658  -0.0280 1485 PHE A CB  
141  C  CG  . PHE A 15  ? 0.3289 0.4533 0.9023 -0.0510 0.1552  -0.0259 1485 PHE A CG  
142  C  CD1 . PHE A 15  ? 0.3922 0.5001 0.9503 -0.0396 0.1527  -0.0225 1485 PHE A CD1 
143  C  CD2 . PHE A 15  ? 0.3720 0.4949 0.9431 -0.0608 0.1479  -0.0279 1485 PHE A CD2 
144  C  CE1 . PHE A 15  ? 0.4701 0.5620 1.0108 -0.0382 0.1443  -0.0208 1485 PHE A CE1 
145  C  CE2 . PHE A 15  ? 0.3418 0.4478 0.8949 -0.0586 0.1391  -0.0270 1485 PHE A CE2 
146  C  CZ  . PHE A 15  ? 0.3721 0.4633 0.9097 -0.0474 0.1378  -0.0233 1485 PHE A CZ  
147  N  N   . THR A 16  ? 0.3750 0.5022 0.9538 -0.0873 0.1761  -0.0275 1486 THR A N   
148  C  CA  . THR A 16  ? 0.4302 0.5396 0.9967 -0.1011 0.1736  -0.0272 1486 THR A CA  
149  C  C   . THR A 16  ? 0.5212 0.6051 1.0670 -0.1069 0.1833  -0.0229 1486 THR A C   
150  O  O   . THR A 16  ? 0.5787 0.6343 1.1026 -0.1074 0.1799  -0.0214 1486 THR A O   
151  C  CB  . THR A 16  ? 0.5423 0.6750 1.1307 -0.1155 0.1724  -0.0308 1486 THR A CB  
152  O  OG1 . THR A 16  ? 0.5718 0.7298 1.1807 -0.1090 0.1622  -0.0350 1486 THR A OG1 
153  C  CG2 . THR A 16  ? 0.5511 0.6629 1.1264 -0.1304 0.1683  -0.0312 1486 THR A CG2 
154  N  N   . ASP A 17  ? 0.3727 0.4664 0.9243 -0.1105 0.1951  -0.0211 1487 ASP A N   
155  C  CA  . ASP A 17  ? 0.4068 0.4761 0.9372 -0.1157 0.2037  -0.0162 1487 ASP A CA  
156  C  C   . ASP A 17  ? 0.5053 0.5498 1.0139 -0.1022 0.2016  -0.0137 1487 ASP A C   
157  O  O   . ASP A 17  ? 0.4394 0.4556 0.9267 -0.1049 0.2011  -0.0108 1487 ASP A O   
158  C  CB  . ASP A 17  ? 0.4384 0.5258 0.9783 -0.1200 0.2171  -0.0149 1487 ASP A CB  
159  C  CG  . ASP A 17  ? 0.5879 0.6945 1.1408 -0.1367 0.2197  -0.0162 1487 ASP A CG  
160  O  OD1 . ASP A 17  ? 0.6598 0.7581 1.2129 -0.1483 0.2132  -0.0166 1487 ASP A OD1 
161  O  OD2 . ASP A 17  ? 0.6876 0.8175 1.2486 -0.1375 0.2270  -0.0173 1487 ASP A OD2 
162  N  N   . MET A 18  ? 0.5511 0.6057 1.0655 -0.0875 0.1999  -0.0150 1488 MET A N   
163  C  CA  . MET A 18  ? 0.3585 0.3925 0.8545 -0.0759 0.1989  -0.0127 1488 MET A CA  
164  C  C   . MET A 18  ? 0.4556 0.4693 0.9373 -0.0743 0.1896  -0.0130 1488 MET A C   
165  O  O   . MET A 18  ? 0.3662 0.3566 0.8288 -0.0714 0.1900  -0.0109 1488 MET A O   
166  C  CB  . MET A 18  ? 0.4622 0.5107 0.9684 -0.0619 0.1983  -0.0141 1488 MET A CB  
167  C  CG  . MET A 18  ? 0.4638 0.4923 0.9525 -0.0511 0.1968  -0.0118 1488 MET A CG  
168  S  SD  . MET A 18  ? 0.5775 0.5857 1.0462 -0.0527 0.2061  -0.0083 1488 MET A SD  
169  C  CE  . MET A 18  ? 0.5347 0.5234 0.9878 -0.0405 0.2002  -0.0070 1488 MET A CE  
170  N  N   . VAL A 19  ? 0.4362 0.4594 0.9268 -0.0755 0.1809  -0.0162 1489 VAL A N   
171  C  CA  . VAL A 19  ? 0.4029 0.4083 0.8786 -0.0729 0.1728  -0.0174 1489 VAL A CA  
172  C  C   . VAL A 19  ? 0.5640 0.5495 1.0277 -0.0839 0.1717  -0.0184 1489 VAL A C   
173  O  O   . VAL A 19  ? 0.4120 0.3789 0.8604 -0.0810 0.1665  -0.0201 1489 VAL A O   
174  C  CB  . VAL A 19  ? 0.4178 0.4382 0.9034 -0.0700 0.1630  -0.0206 1489 VAL A CB  
175  C  CG1 . VAL A 19  ? 0.3665 0.4015 0.8614 -0.0580 0.1623  -0.0190 1489 VAL A CG1 
176  C  CG2 . VAL A 19  ? 0.4196 0.4576 0.9226 -0.0818 0.1604  -0.0237 1489 VAL A CG2 
177  N  N   . SER A 20  ? 0.3918 0.3803 0.8617 -0.0966 0.1767  -0.0174 1490 SER A N   
178  C  CA  . SER A 20  ? 0.5352 0.5001 0.9915 -0.1076 0.1762  -0.0171 1490 SER A CA  
179  C  C   . SER A 20  ? 0.5389 0.4844 0.9801 -0.1084 0.1842  -0.0117 1490 SER A C   
180  O  O   . SER A 20  ? 0.6205 0.5436 1.0492 -0.1176 0.1840  -0.0100 1490 SER A O   
181  C  CB  . SER A 20  ? 0.4807 0.4580 0.9515 -0.1238 0.1754  -0.0189 1490 SER A CB  
182  O  OG  . SER A 20  ? 0.5815 0.5755 1.0642 -0.1304 0.1855  -0.0155 1490 SER A OG  
183  N  N   . SER A 21  ? 0.5817 0.5336 1.0228 -0.0990 0.1903  -0.0088 1491 SER A N   
184  C  CA  . SER A 21  ? 0.5282 0.4628 0.9540 -0.0998 0.1973  -0.0037 1491 SER A CA  
185  C  C   . SER A 21  ? 0.5791 0.4861 0.9844 -0.0907 0.1924  -0.0033 1491 SER A C   
186  O  O   . SER A 21  ? 0.5227 0.4300 0.9280 -0.0812 0.1861  -0.0070 1491 SER A O   
187  C  CB  . SER A 21  ? 0.4060 0.3584 0.8390 -0.0936 0.2056  -0.0019 1491 SER A CB  
188  O  OG  . SER A 21  ? 0.5765 0.5386 1.0150 -0.0793 0.2021  -0.0044 1491 SER A OG  
189  N  N   . PRO A 22  ? 0.6086 0.4916 0.9965 -0.0939 0.1946  0.0009  1492 PRO A N   
190  C  CA  . PRO A 22  ? 0.5344 0.3924 0.9047 -0.0844 0.1893  0.0006  1492 PRO A CA  
191  C  C   . PRO A 22  ? 0.6714 0.5332 1.0386 -0.0713 0.1916  0.0019  1492 PRO A C   
192  O  O   . PRO A 22  ? 0.5993 0.4768 0.9730 -0.0704 0.1982  0.0040  1492 PRO A O   
193  C  CB  . PRO A 22  ? 0.7587 0.5891 1.1119 -0.0937 0.1898  0.0054  1492 PRO A CB  
194  C  CG  . PRO A 22  ? 0.7747 0.6180 1.1331 -0.1049 0.1993  0.0105  1492 PRO A CG  
195  C  CD  . PRO A 22  ? 0.6752 0.5517 1.0579 -0.1077 0.2013  0.0063  1492 PRO A CD  
196  N  N   . GLY A 23  ? 0.6871 0.5344 1.0444 -0.0611 0.1861  -0.0002 1493 GLY A N   
197  C  CA  . GLY A 23  ? 0.6642 0.5114 1.0169 -0.0497 0.1871  0.0009  1493 GLY A CA  
198  C  C   . GLY A 23  ? 0.6795 0.5503 1.0461 -0.0427 0.1885  -0.0011 1493 GLY A C   
199  O  O   . GLY A 23  ? 0.8293 0.7049 1.1955 -0.0370 0.1917  0.0006  1493 GLY A O   
200  N  N   . THR A 24  ? 0.5208 0.4050 0.8985 -0.0433 0.1855  -0.0046 1494 THR A N   
201  C  CA  . THR A 24  ? 0.4708 0.3759 0.8613 -0.0376 0.1860  -0.0056 1494 THR A CA  
202  C  C   . THR A 24  ? 0.4871 0.3924 0.8759 -0.0291 0.1810  -0.0082 1494 THR A C   
203  O  O   . THR A 24  ? 0.4097 0.3290 0.8068 -0.0243 0.1806  -0.0081 1494 THR A O   
204  C  CB  . THR A 24  ? 0.4856 0.4093 0.8914 -0.0444 0.1860  -0.0068 1494 THR A CB  
205  O  OG1 . THR A 24  ? 0.5123 0.4311 0.9168 -0.0499 0.1805  -0.0099 1494 THR A OG1 
206  C  CG2 . THR A 24  ? 0.4237 0.3537 0.8345 -0.0526 0.1931  -0.0043 1494 THR A CG2 
207  N  N   . ASN A 25  ? 0.4084 0.2984 0.7864 -0.0270 0.1774  -0.0107 1495 ASN A N   
208  C  CA  . ASN A 25  ? 0.5710 0.4628 0.9468 -0.0194 0.1740  -0.0138 1495 ASN A CA  
209  C  C   . ASN A 25  ? 0.5945 0.4803 0.9649 -0.0114 0.1751  -0.0129 1495 ASN A C   
210  O  O   . ASN A 25  ? 0.6289 0.5046 0.9920 -0.0068 0.1726  -0.0161 1495 ASN A O   
211  C  CB  . ASN A 25  ? 0.3917 0.2733 0.7605 -0.0209 0.1695  -0.0190 1495 ASN A CB  
212  C  CG  . ASN A 25  ? 0.4737 0.3603 0.8400 -0.0139 0.1672  -0.0231 1495 ASN A CG  
213  O  OD1 . ASN A 25  ? 0.5006 0.4020 0.8725 -0.0117 0.1677  -0.0216 1495 ASN A OD1 
214  N  ND2 . ASN A 25  ? 0.5719 0.4456 0.9292 -0.0103 0.1648  -0.0283 1495 ASN A ND2 
215  N  N   . CYS A 26  ? 0.6468 0.5391 1.0213 -0.0093 0.1783  -0.0094 1496 CYS A N   
216  C  CA  . CYS A 26  ? 0.5810 0.4695 0.9517 -0.0022 0.1785  -0.0089 1496 CYS A CA  
217  C  C   . CYS A 26  ? 0.5361 0.4368 0.9146 -0.0003 0.1808  -0.0065 1496 CYS A C   
218  O  O   . CYS A 26  ? 0.5002 0.4097 0.8860 -0.0038 0.1829  -0.0051 1496 CYS A O   
219  C  CB  . CYS A 26  ? 0.4846 0.3568 0.8450 -0.0019 0.1788  -0.0073 1496 CYS A CB  
220  S  SG  . CYS A 26  ? 0.6480 0.5188 1.0072 -0.0102 0.1839  -0.0030 1496 CYS A SG  
221  N  N   . ALA A 27  ? 0.3355 0.2367 0.7134 0.0055  0.1800  -0.0065 1497 ALA A N   
222  C  CA  . ALA A 27  ? 0.3783 0.2873 0.7622 0.0075  0.1814  -0.0047 1497 ALA A CA  
223  C  C   . ALA A 27  ? 0.4168 0.3240 0.7999 0.0058  0.1849  -0.0032 1497 ALA A C   
224  O  O   . ALA A 27  ? 0.4412 0.3571 0.8318 0.0060  0.1866  -0.0027 1497 ALA A O   
225  C  CB  . ALA A 27  ? 0.4772 0.3851 0.8598 0.0126  0.1796  -0.0054 1497 ALA A CB  
226  N  N   . GLU A 28  ? 0.4900 0.3858 0.8634 0.0043  0.1860  -0.0027 1498 GLU A N   
227  C  CA  . GLU A 28  ? 0.5467 0.4405 0.9161 0.0022  0.1903  -0.0012 1498 GLU A CA  
228  C  C   . GLU A 28  ? 0.6415 0.5458 1.0192 -0.0035 0.1946  -0.0009 1498 GLU A C   
229  O  O   . GLU A 28  ? 0.4806 0.3891 0.8586 -0.0047 0.1995  -0.0006 1498 GLU A O   
230  C  CB  . GLU A 28  ? 0.7550 0.6321 1.1095 0.0005  0.1900  0.0005  1498 GLU A CB  
231  C  CG  . GLU A 28  ? 1.0023 0.8698 1.3491 0.0073  0.1851  -0.0001 1498 GLU A CG  
232  C  CD  . GLU A 28  ? 0.9760 0.8425 1.3259 0.0110  0.1801  -0.0027 1498 GLU A CD  
233  O  OE1 . GLU A 28  ? 1.0225 0.8906 1.3758 0.0078  0.1800  -0.0037 1498 GLU A OE1 
234  O  OE2 . GLU A 28  ? 1.0977 0.9630 1.4469 0.0170  0.1763  -0.0043 1498 GLU A OE2 
235  N  N   . ALA A 29  ? 0.5307 0.4409 0.9156 -0.0067 0.1928  -0.0015 1499 ALA A N   
236  C  CA  . ALA A 29  ? 0.5892 0.5121 0.9846 -0.0120 0.1958  -0.0018 1499 ALA A CA  
237  C  C   . ALA A 29  ? 0.4733 0.4115 0.8821 -0.0075 0.1951  -0.0029 1499 ALA A C   
238  O  O   . ALA A 29  ? 0.5324 0.4839 0.9526 -0.0103 0.1969  -0.0038 1499 ALA A O   
239  C  CB  . ALA A 29  ? 0.4725 0.3945 0.8693 -0.0180 0.1928  -0.0025 1499 ALA A CB  
240  N  N   . TYR A 30  ? 0.4609 0.3973 0.8690 -0.0007 0.1923  -0.0029 1500 TYR A N   
241  C  CA  . TYR A 30  ? 0.4540 0.4008 0.8732 0.0036  0.1897  -0.0032 1500 TYR A CA  
242  C  C   . TYR A 30  ? 0.3590 0.3177 0.7889 0.0043  0.1935  -0.0049 1500 TYR A C   
243  O  O   . TYR A 30  ? 0.4786 0.4493 0.9205 0.0044  0.1913  -0.0055 1500 TYR A O   
244  C  CB  . TYR A 30  ? 0.3957 0.3364 0.8115 0.0093  0.1872  -0.0026 1500 TYR A CB  
245  C  CG  . TYR A 30  ? 0.4347 0.3825 0.8604 0.0134  0.1841  -0.0022 1500 TYR A CG  
246  C  CD1 . TYR A 30  ? 0.3604 0.3124 0.7898 0.0129  0.1791  -0.0001 1500 TYR A CD1 
247  C  CD2 . TYR A 30  ? 0.3133 0.2629 0.7439 0.0180  0.1857  -0.0041 1500 TYR A CD2 
248  C  CE1 . TYR A 30  ? 0.3953 0.3516 0.8326 0.0168  0.1751  0.0012  1500 TYR A CE1 
249  C  CE2 . TYR A 30  ? 0.3297 0.2835 0.7694 0.0226  0.1817  -0.0039 1500 TYR A CE2 
250  C  CZ  . TYR A 30  ? 0.3474 0.3039 0.7903 0.0219  0.1761  -0.0007 1500 TYR A CZ  
251  O  OH  . TYR A 30  ? 0.3414 0.2995 0.7917 0.0267  0.1710  0.0006  1500 TYR A OH  
252  N  N   . HIS A 31  ? 0.3697 0.3259 0.7951 0.0050  0.1990  -0.0063 1501 HIS A N   
253  C  CA  . HIS A 31  ? 0.5425 0.5113 0.9782 0.0075  0.2034  -0.0093 1501 HIS A CA  
254  C  C   . HIS A 31  ? 0.5525 0.5360 0.9987 0.0013  0.2070  -0.0102 1501 HIS A C   
255  O  O   . HIS A 31  ? 0.3910 0.3904 0.8520 0.0044  0.2084  -0.0133 1501 HIS A O   
256  C  CB  . HIS A 31  ? 0.5483 0.5110 0.9739 0.0092  0.2090  -0.0111 1501 HIS A CB  
257  C  CG  . HIS A 31  ? 0.7456 0.6975 1.1650 0.0160  0.2050  -0.0117 1501 HIS A CG  
258  N  ND1 . HIS A 31  ? 0.6428 0.5982 1.0704 0.0232  0.2029  -0.0147 1501 HIS A ND1 
259  C  CD2 . HIS A 31  ? 0.6702 0.6080 1.0772 0.0163  0.2019  -0.0099 1501 HIS A CD2 
260  C  CE1 . HIS A 31  ? 0.8036 0.7467 1.2234 0.0264  0.1990  -0.0145 1501 HIS A CE1 
261  N  NE2 . HIS A 31  ? 0.6469 0.5808 1.0550 0.0224  0.1984  -0.0118 1501 HIS A NE2 
262  N  N   . SER A 32  ? 0.3983 0.3772 0.8386 -0.0072 0.2077  -0.0080 1502 SER A N   
263  C  CA  . SER A 32  ? 0.4789 0.4722 0.9305 -0.0147 0.2103  -0.0088 1502 SER A CA  
264  C  C   . SER A 32  ? 0.4356 0.4396 0.9008 -0.0130 0.2029  -0.0096 1502 SER A C   
265  O  O   . SER A 32  ? 0.3542 0.3773 0.8363 -0.0135 0.2034  -0.0121 1502 SER A O   
266  C  CB  . SER A 32  ? 0.5769 0.5585 1.0166 -0.0251 0.2124  -0.0061 1502 SER A CB  
267  O  OG  . SER A 32  ? 0.6331 0.6046 1.0589 -0.0272 0.2190  -0.0045 1502 SER A OG  
268  N  N   . TRP A 33  ? 0.3178 0.3111 0.7761 -0.0103 0.1958  -0.0077 1503 TRP A N   
269  C  CA  . TRP A 33  ? 0.4156 0.4174 0.8832 -0.0084 0.1881  -0.0078 1503 TRP A CA  
270  C  C   . TRP A 33  ? 0.3087 0.3200 0.7878 0.0008  0.1854  -0.0087 1503 TRP A C   
271  O  O   . TRP A 33  ? 0.3989 0.4259 0.8932 0.0023  0.1819  -0.0103 1503 TRP A O   
272  C  CB  . TRP A 33  ? 0.3350 0.3229 0.7897 -0.0080 0.1825  -0.0057 1503 TRP A CB  
273  C  CG  . TRP A 33  ? 0.5625 0.5414 1.0079 -0.0157 0.1822  -0.0060 1503 TRP A CG  
274  C  CD1 . TRP A 33  ? 0.4636 0.4258 0.8941 -0.0160 0.1828  -0.0054 1503 TRP A CD1 
275  C  CD2 . TRP A 33  ? 0.5414 0.5269 0.9923 -0.0236 0.1802  -0.0077 1503 TRP A CD2 
276  N  NE1 . TRP A 33  ? 0.3824 0.3386 0.8079 -0.0229 0.1813  -0.0068 1503 TRP A NE1 
277  C  CE2 . TRP A 33  ? 0.5601 0.5298 0.9975 -0.0283 0.1797  -0.0081 1503 TRP A CE2 
278  C  CE3 . TRP A 33  ? 0.4765 0.4801 0.9433 -0.0269 0.1782  -0.0094 1503 TRP A CE3 
279  C  CZ2 . TRP A 33  ? 0.4218 0.3909 0.8598 -0.0368 0.1772  -0.0102 1503 TRP A CZ2 
280  C  CZ3 . TRP A 33  ? 0.4802 0.4855 0.9486 -0.0360 0.1758  -0.0113 1503 TRP A CZ3 
281  C  CH2 . TRP A 33  ? 0.3695 0.3565 0.8229 -0.0412 0.1753  -0.0116 1503 TRP A CH2 
282  N  N   . ALA A 34  ? 0.4025 0.4039 0.8750 0.0073  0.1865  -0.0082 1504 ALA A N   
283  C  CA  . ALA A 34  ? 0.4384 0.4444 0.9200 0.0164  0.1834  -0.0093 1504 ALA A CA  
284  C  C   . ALA A 34  ? 0.4326 0.4573 0.9311 0.0186  0.1874  -0.0140 1504 ALA A C   
285  O  O   . ALA A 34  ? 0.4549 0.4913 0.9680 0.0241  0.1820  -0.0153 1504 ALA A O   
286  C  CB  . ALA A 34  ? 0.3087 0.2999 0.7797 0.0212  0.1847  -0.0089 1504 ALA A CB  
287  N  N   . ASP A 35  ? 0.4406 0.4692 0.9373 0.0141  0.1969  -0.0165 1505 ASP A N   
288  C  CA  . ASP A 35  ? 0.4461 0.4959 0.9591 0.0141  0.2030  -0.0214 1505 ASP A CA  
289  C  C   . ASP A 35  ? 0.5403 0.6087 1.0707 0.0107  0.1986  -0.0221 1505 ASP A C   
290  O  O   . ASP A 35  ? 0.4434 0.5295 0.9926 0.0174  0.1961  -0.0260 1505 ASP A O   
291  C  CB  . ASP A 35  ? 0.3415 0.3913 0.8459 0.0058  0.2142  -0.0220 1505 ASP A CB  
292  C  CG  . ASP A 35  ? 0.4376 0.4763 0.9293 0.0111  0.2195  -0.0237 1505 ASP A CG  
293  O  OD1 . ASP A 35  ? 0.3829 0.4137 0.8737 0.0206  0.2143  -0.0248 1505 ASP A OD1 
294  O  OD2 . ASP A 35  ? 0.4760 0.5126 0.9573 0.0053  0.2282  -0.0238 1505 ASP A OD2 
295  N  N   . LEU A 36  ? 0.4685 0.5332 0.9932 0.0007  0.1967  -0.0190 1506 LEU A N   
296  C  CA  . LEU A 36  ? 0.3511 0.4329 0.8916 -0.0031 0.1911  -0.0202 1506 LEU A CA  
297  C  C   . LEU A 36  ? 0.3612 0.4456 0.9093 0.0071  0.1799  -0.0197 1506 LEU A C   
298  O  O   . LEU A 36  ? 0.3374 0.4418 0.9056 0.0119  0.1763  -0.0230 1506 LEU A O   
299  C  CB  . LEU A 36  ? 0.3118 0.3840 0.8416 -0.0144 0.1889  -0.0174 1506 LEU A CB  
300  C  CG  . LEU A 36  ? 0.5496 0.6342 1.0906 -0.0196 0.1809  -0.0183 1506 LEU A CG  
301  C  CD1 . LEU A 36  ? 0.3628 0.4738 0.9259 -0.0260 0.1851  -0.0225 1506 LEU A CD1 
302  C  CD2 . LEU A 36  ? 0.3176 0.3848 0.8418 -0.0287 0.1782  -0.0161 1506 LEU A CD2 
303  N  N   . ARG A 37  ? 0.3625 0.4266 0.8946 0.0110  0.1745  -0.0154 1507 ARG A N   
304  C  CA  . ARG A 37  ? 0.3114 0.3735 0.8463 0.0198  0.1639  -0.0133 1507 ARG A CA  
305  C  C   . ARG A 37  ? 0.3525 0.4261 0.9041 0.0307  0.1633  -0.0171 1507 ARG A C   
306  O  O   . ARG A 37  ? 0.3494 0.4361 0.9161 0.0363  0.1551  -0.0182 1507 ARG A O   
307  C  CB  . ARG A 37  ? 0.3082 0.3471 0.8233 0.0217  0.1616  -0.0083 1507 ARG A CB  
308  C  CG  . ARG A 37  ? 0.4087 0.4416 0.9223 0.0287  0.1507  -0.0042 1507 ARG A CG  
309  C  CD  . ARG A 37  ? 0.4315 0.4436 0.9284 0.0302  0.1511  -0.0001 1507 ARG A CD  
310  N  NE  . ARG A 37  ? 0.4522 0.4602 0.9510 0.0349  0.1574  -0.0032 1507 ARG A NE  
311  C  CZ  . ARG A 37  ? 0.3443 0.3375 0.8305 0.0342  0.1612  -0.0021 1507 ARG A CZ  
312  N  NH1 . ARG A 37  ? 0.3162 0.2984 0.7884 0.0292  0.1601  0.0021  1507 ARG A NH1 
313  N  NH2 . ARG A 37  ? 0.3306 0.3215 0.8189 0.0387  0.1662  -0.0060 1507 ARG A NH2 
314  N  N   . ASP A 38  ? 0.3091 0.3788 0.8584 0.0340  0.1716  -0.0200 1508 ASP A N   
315  C  CA  . ASP A 38  ? 0.3129 0.3896 0.8753 0.0459  0.1709  -0.0246 1508 ASP A CA  
316  C  C   . ASP A 38  ? 0.4477 0.5538 1.0351 0.0476  0.1726  -0.0309 1508 ASP A C   
317  O  O   . ASP A 38  ? 0.3408 0.4569 0.9441 0.0579  0.1645  -0.0332 1508 ASP A O   
318  C  CB  . ASP A 38  ? 0.3152 0.3803 0.8669 0.0483  0.1798  -0.0272 1508 ASP A CB  
319  C  CG  . ASP A 38  ? 0.4507 0.4886 0.9821 0.0491  0.1756  -0.0217 1508 ASP A CG  
320  O  OD1 . ASP A 38  ? 0.3244 0.3534 0.8512 0.0492  0.1663  -0.0162 1508 ASP A OD1 
321  O  OD2 . ASP A 38  ? 0.4248 0.4512 0.9446 0.0491  0.1816  -0.0231 1508 ASP A OD2 
322  N  N   . VAL A 39  ? 0.3525 0.4732 0.9444 0.0371  0.1820  -0.0331 1509 VAL A N   
323  C  CA  . VAL A 39  ? 0.3097 0.4615 0.9275 0.0377  0.1845  -0.0395 1509 VAL A CA  
324  C  C   . VAL A 39  ? 0.3619 0.5247 0.9931 0.0388  0.1715  -0.0381 1509 VAL A C   
325  O  O   . VAL A 39  ? 0.3913 0.5750 1.0455 0.0479  0.1663  -0.0430 1509 VAL A O   
326  C  CB  . VAL A 39  ? 0.4292 0.5935 1.0472 0.0242  0.1975  -0.0414 1509 VAL A CB  
327  C  CG1 . VAL A 39  ? 0.3485 0.4994 0.9470 0.0244  0.2077  -0.0425 1509 VAL A CG1 
328  C  CG2 . VAL A 39  ? 0.3142 0.4699 0.9216 0.0095  0.1962  -0.0358 1509 VAL A CG2 
329  N  N   . LEU A 40  ? 0.3321 0.4799 0.9481 0.0312  0.1649  -0.0317 1510 LEU A N   
330  C  CA  . LEU A 40  ? 0.3239 0.4813 0.9498 0.0319  0.1518  -0.0304 1510 LEU A CA  
331  C  C   . LEU A 40  ? 0.4355 0.5870 1.0647 0.0471  0.1400  -0.0290 1510 LEU A C   
332  O  O   . LEU A 40  ? 0.3187 0.4881 0.9673 0.0539  0.1304  -0.0314 1510 LEU A O   
333  C  CB  . LEU A 40  ? 0.3097 0.4515 0.9164 0.0209  0.1479  -0.0250 1510 LEU A CB  
334  C  CG  . LEU A 40  ? 0.3924 0.5406 0.9986 0.0055  0.1569  -0.0267 1510 LEU A CG  
335  C  CD1 . LEU A 40  ? 0.3667 0.4962 0.9522 -0.0040 0.1529  -0.0225 1510 LEU A CD1 
336  C  CD2 . LEU A 40  ? 0.3083 0.4881 0.9414 0.0006  0.1570  -0.0322 1510 LEU A CD2 
337  N  N   . PHE A 41  ? 0.3176 0.4443 0.9292 0.0528  0.1404  -0.0253 1511 PHE A N   
338  C  CA  . PHE A 41  ? 0.3263 0.4434 0.9392 0.0663  0.1293  -0.0233 1511 PHE A CA  
339  C  C   . PHE A 41  ? 0.3496 0.4873 0.9881 0.0785  0.1294  -0.0314 1511 PHE A C   
340  O  O   . PHE A 41  ? 0.4085 0.5548 1.0614 0.0885  0.1172  -0.0320 1511 PHE A O   
341  C  CB  . PHE A 41  ? 0.3294 0.4170 0.9201 0.0684  0.1311  -0.0186 1511 PHE A CB  
342  C  CG  . PHE A 41  ? 0.4356 0.5094 1.0260 0.0811  0.1200  -0.0159 1511 PHE A CG  
343  C  CD1 . PHE A 41  ? 0.3902 0.4556 0.9741 0.0825  0.1063  -0.0087 1511 PHE A CD1 
344  C  CD2 . PHE A 41  ? 0.6197 0.6881 1.2153 0.0916  0.1226  -0.0207 1511 PHE A CD2 
345  C  CE1 . PHE A 41  ? 0.4626 0.5126 1.0446 0.0937  0.0952  -0.0050 1511 PHE A CE1 
346  C  CE2 . PHE A 41  ? 0.6151 0.6678 1.2100 0.1033  0.1114  -0.0182 1511 PHE A CE2 
347  C  CZ  . PHE A 41  ? 0.4771 0.5200 1.0652 0.1041  0.0975  -0.0098 1511 PHE A CZ  
348  N  N   . ASN A 42  ? 0.4113 0.5587 1.0561 0.0780  0.1430  -0.0382 1512 ASN A N   
349  C  CA  . ASN A 42  ? 0.3293 0.4980 0.9986 0.0903  0.1448  -0.0474 1512 ASN A CA  
350  C  C   . ASN A 42  ? 0.5336 0.7351 1.2300 0.0900  0.1397  -0.0514 1512 ASN A C   
351  O  O   . ASN A 42  ? 0.3762 0.5900 1.0896 0.1032  0.1299  -0.0557 1512 ASN A O   
352  C  CB  . ASN A 42  ? 0.4007 0.5716 1.0594 0.0860  0.1593  -0.0531 1512 ASN A CB  
353  C  CG  . ASN A 42  ? 0.6231 0.8127 1.2932 0.0966  0.1597  -0.0629 1512 ASN A CG  
354  O  OD1 . ASN A 42  ? 0.5574 0.7746 1.2391 0.0917  0.1667  -0.0688 1512 ASN A OD1 
355  N  ND2 . ASN A 42  ? 0.4318 0.6066 1.0985 0.1112  0.1520  -0.0649 1512 ASN A ND2 
356  N  N   . LEU A 43  ? 0.4012 0.6138 1.0972 0.0745  0.1436  -0.0496 1513 LEU A N   
357  C  CA  . LEU A 43  ? 0.3755 0.6201 1.0976 0.0722  0.1383  -0.0536 1513 LEU A CA  
358  C  C   . LEU A 43  ? 0.3263 0.5669 1.0518 0.0814  0.1187  -0.0497 1513 LEU A C   
359  O  O   . LEU A 43  ? 0.3524 0.6177 1.1045 0.0911  0.1104  -0.0551 1513 LEU A O   
360  C  CB  . LEU A 43  ? 0.3623 0.6138 1.0798 0.0527  0.1449  -0.0516 1513 LEU A CB  
361  C  CG  . LEU A 43  ? 0.3125 0.5925 1.0529 0.0471  0.1369  -0.0544 1513 LEU A CG  
362  C  CD1 . LEU A 43  ? 0.3150 0.6328 1.0851 0.0509  0.1414  -0.0642 1513 LEU A CD1 
363  C  CD2 . LEU A 43  ? 0.3097 0.5836 1.0364 0.0273  0.1415  -0.0507 1513 LEU A CD2 
364  N  N   . CYS A 44  ? 0.3299 0.5399 1.0284 0.0790  0.1108  -0.0403 1514 CYS A N   
365  C  CA  . CYS A 44  ? 0.4306 0.6357 1.1286 0.0861  0.0922  -0.0355 1514 CYS A CA  
366  C  C   . CYS A 44  ? 0.3513 0.5513 1.0585 0.1053  0.0838  -0.0371 1514 CYS A C   
367  O  O   . CYS A 44  ? 0.4128 0.6258 1.1370 0.1157  0.0695  -0.0383 1514 CYS A O   
368  C  CB  . CYS A 44  ? 0.4601 0.6341 1.1253 0.0784  0.0876  -0.0252 1514 CYS A CB  
369  S  SG  . CYS A 44  ? 0.4433 0.6204 1.0969 0.0584  0.0918  -0.0235 1514 CYS A SG  
370  N  N   . GLU A 45  ? 0.4049 0.5916 1.1060 0.1107  0.0936  -0.0395 1515 GLU A N   
371  C  CA  . GLU A 45  ? 0.5856 0.7652 1.2952 0.1292  0.0870  -0.0426 1515 GLU A CA  
372  C  C   . GLU A 45  ? 0.5618 0.7776 1.3077 0.1405  0.0857  -0.0538 1515 GLU A C   
373  O  O   . GLU A 45  ? 0.5314 0.7462 1.2880 0.1572  0.0731  -0.0560 1515 GLU A O   
374  C  CB  . GLU A 45  ? 0.6520 0.8107 1.3466 0.1304  0.0991  -0.0441 1515 GLU A CB  
375  C  CG  . GLU A 45  ? 0.9053 1.0387 1.5939 0.1458  0.0900  -0.0430 1515 GLU A CG  
376  C  CD  . GLU A 45  ? 0.9344 1.0356 1.5957 0.1406  0.0969  -0.0384 1515 GLU A CD  
377  O  OE1 . GLU A 45  ? 0.8344 0.9396 1.4909 0.1338  0.1122  -0.0433 1515 GLU A OE1 
378  O  OE2 . GLU A 45  ? 0.9114 0.9832 1.5546 0.1425  0.0866  -0.0295 1515 GLU A OE2 
379  N  N   . ASN A 46  ? 0.4347 0.6807 1.1942 0.1301  0.0972  -0.0603 1516 ASN A N   
380  C  CA  . ASN A 46  ? 0.4941 0.7731 1.2753 0.1369  0.0954  -0.0703 1516 ASN A CA  
381  C  C   . ASN A 46  ? 0.4581 0.7614 1.2641 0.1375  0.0816  -0.0699 1516 ASN A C   
382  O  O   . ASN A 46  ? 0.5573 0.8786 1.3816 0.1509  0.0707  -0.0754 1516 ASN A O   
383  C  CB  . ASN A 46  ? 0.4208 0.7198 1.2005 0.1247  0.1142  -0.0772 1516 ASN A CB  
384  C  CG  . ASN A 46  ? 0.5846 0.8633 1.3417 0.1268  0.1260  -0.0793 1516 ASN A CG  
385  O  OD1 . ASN A 46  ? 0.7178 0.9744 1.4657 0.1403  0.1195  -0.0792 1516 ASN A OD1 
386  N  ND2 . ASN A 46  ? 0.5511 0.8360 1.2985 0.1131  0.1425  -0.0811 1516 ASN A ND2 
387  N  N   . LEU A 47  ? 0.4620 0.7611 1.2629 0.1241  0.0790  -0.0626 1517 LEU A N   
388  C  CA  . LEU A 47  ? 0.5019 0.8217 1.3184 0.1224  0.0642  -0.0622 1517 LEU A CA  
389  C  C   . LEU A 47  ? 0.6170 0.9261 1.4355 0.1405  0.0426  -0.0587 1517 LEU A C   
390  O  O   . LEU A 47  ? 0.8725 1.2098 1.7209 0.1515  0.0315  -0.0649 1517 LEU A O   
391  C  CB  . LEU A 47  ? 0.5247 0.8323 1.3183 0.1028  0.0641  -0.0545 1517 LEU A CB  
392  C  CG  . LEU A 47  ? 0.4477 0.7693 1.2439 0.0848  0.0832  -0.0585 1517 LEU A CG  
393  C  CD1 . LEU A 47  ? 0.4311 0.7412 1.2070 0.0666  0.0818  -0.0525 1517 LEU A CD1 
394  C  CD2 . LEU A 47  ? 0.6217 0.9893 1.4580 0.0857  0.0881  -0.0697 1517 LEU A CD2 
395  N  N   . VAL A 48  ? 0.6750 0.9434 1.4628 0.1448  0.0368  -0.0490 1518 VAL A N   
396  C  CA  . VAL A 48  ? 0.8460 1.0982 1.6307 0.1610  0.0160  -0.0437 1518 VAL A CA  
397  C  C   . VAL A 48  ? 0.8986 1.1670 1.7133 0.1822  0.0123  -0.0536 1518 VAL A C   
398  O  O   . VAL A 48  ? 0.9102 1.1875 1.7410 0.1966  -0.0061 -0.0544 1518 VAL A O   
399  C  CB  . VAL A 48  ? 0.7959 1.0009 1.5416 0.1596  0.0131  -0.0314 1518 VAL A CB  
400  C  CG1 . VAL A 48  ? 0.4529 0.6438 1.1697 0.1395  0.0176  -0.0228 1518 VAL A CG1 
401  C  CG2 . VAL A 48  ? 0.9083 1.0960 1.6479 0.1646  0.0265  -0.0345 1518 VAL A CG2 
402  N  N   . LYS A 49  ? 0.8464 1.1189 1.6650 0.1842  0.0293  -0.0619 1519 LYS A N   
403  C  CA  . LYS A 49  ? 0.8990 1.1821 1.7261 0.2002  0.0263  -0.0715 1519 LYS A CA  
404  C  C   . LYS A 49  ? 1.0130 1.3423 1.8695 0.2007  0.0244  -0.0808 1519 LYS A C   
405  O  O   . LYS A 49  ? 1.0832 1.4244 1.9546 0.2169  0.0104  -0.0851 1519 LYS A O   
406  C  CB  . LYS A 49  ? 0.7597 1.0331 1.5706 0.1989  0.0443  -0.0775 1519 LYS A CB  
407  C  CG  . LYS A 49  ? 0.7984 1.0268 1.5811 0.2013  0.0445  -0.0703 1519 LYS A CG  
408  C  CD  . LYS A 49  ? 0.8712 1.0952 1.6403 0.2002  0.0613  -0.0781 1519 LYS A CD  
409  C  CE  . LYS A 49  ? 1.0122 1.1947 1.7525 0.1961  0.0650  -0.0707 1519 LYS A CE  
410  N  NZ  . LYS A 49  ? 0.9823 1.1580 1.7091 0.1984  0.0772  -0.0788 1519 LYS A NZ  
411  N  N   . SER A 50  ? 1.0090 1.3638 1.8737 0.1827  0.0378  -0.0836 1520 SER A N   
412  C  CA  . SER A 50  ? 1.0969 1.4968 1.9885 0.1807  0.0391  -0.0929 1520 SER A CA  
413  C  C   . SER A 50  ? 1.2084 1.6255 2.1210 0.1843  0.0185  -0.0909 1520 SER A C   
414  O  O   . SER A 50  ? 1.2652 1.7207 2.2025 0.1843  0.0163  -0.0986 1520 SER A O   
415  C  CB  . SER A 50  ? 1.0683 1.4868 1.9594 0.1585  0.0594  -0.0955 1520 SER A CB  
416  O  OG  . SER A 50  ? 1.0790 1.4943 1.9570 0.1578  0.0775  -0.1007 1520 SER A OG  
417  N  N   . SER A 51  ? 1.2258 1.6159 2.1289 0.1872  0.0032  -0.0804 1521 SER A N   
418  C  CA  . SER A 51  ? 1.3664 1.7662 2.2845 0.1922  -0.0198 -0.0765 1521 SER A CA  
419  C  C   . SER A 51  ? 1.2988 1.7266 2.2318 0.1730  -0.0181 -0.0776 1521 SER A C   
420  O  O   . SER A 51  ? 1.4598 1.8980 2.3992 0.1739  -0.0370 -0.0754 1521 SER A O   
421  C  CB  . SER A 51  ? 1.5024 1.9218 2.4394 0.2119  -0.0350 -0.0833 1521 SER A CB  
422  O  OG  . SER A 51  ? 1.5270 1.9334 2.4646 0.2237  -0.0613 -0.0756 1521 SER A OG  
423  N  N   . GLU A 52  ? 1.1362 1.5711 2.0643 0.1538  0.0033  -0.0800 1522 GLU A N   
424  C  CA  . GLU A 52  ? 1.1600 1.6035 2.0825 0.1321  0.0040  -0.0774 1522 GLU A CA  
425  C  C   . GLU A 52  ? 1.1909 1.5894 2.0669 0.1217  0.0011  -0.0643 1522 GLU A C   
426  O  O   . GLU A 52  ? 1.1280 1.5248 1.9910 0.1024  0.0059  -0.0621 1522 GLU A O   
427  C  CB  . GLU A 52  ? 1.0311 1.5006 1.9679 0.1149  0.0267  -0.0849 1522 GLU A CB  
428  C  CG  . GLU A 52  ? 0.9983 1.4960 1.9506 0.0960  0.0243  -0.0876 1522 GLU A CG  
429  C  CD  . GLU A 52  ? 0.9523 1.4782 1.9317 0.1047  0.0014  -0.0913 1522 GLU A CD  
430  O  OE1 . GLU A 52  ? 0.7895 1.3196 1.7646 0.0910  -0.0083 -0.0892 1522 GLU A OE1 
431  O  OE2 . GLU A 52  ? 0.8368 1.3740 1.8287 0.1240  -0.0074 -0.0954 1522 GLU A OE2 
432  N  N   . ALA A 53  ? 1.1404 1.5029 1.9918 0.1342  -0.0067 -0.0562 1523 ALA A N   
433  C  CA  . ALA A 53  ? 1.0960 1.4179 1.9045 0.1257  -0.0100 -0.0439 1523 ALA A CA  
434  C  C   . ALA A 53  ? 1.0650 1.3902 1.8656 0.1184  -0.0270 -0.0396 1523 ALA A C   
435  O  O   . ALA A 53  ? 1.1431 1.4922 1.9668 0.1268  -0.0436 -0.0432 1523 ALA A O   
436  C  CB  . ALA A 53  ? 1.1049 1.3915 1.8931 0.1412  -0.0176 -0.0361 1523 ALA A CB  
437  N  N   . ASN A 54  ? 0.9688 1.2705 1.7365 0.1030  -0.0229 -0.0328 1524 ASN A N   
438  C  CA  . ASN A 54  ? 0.9954 1.2893 1.7430 0.0947  -0.0371 -0.0273 1524 ASN A CA  
439  C  C   . ASN A 54  ? 0.8646 1.1924 1.6346 0.0825  -0.0395 -0.0356 1524 ASN A C   
440  O  O   . ASN A 54  ? 0.8025 1.1267 1.5575 0.0750  -0.0518 -0.0329 1524 ASN A O   
441  C  CB  . ASN A 54  ? 1.0352 1.3162 1.7733 0.1097  -0.0601 -0.0198 1524 ASN A CB  
442  C  CG  . ASN A 54  ? 1.0262 1.2669 1.7337 0.1170  -0.0586 -0.0093 1524 ASN A CG  
443  O  OD1 . ASN A 54  ? 1.0245 1.2594 1.7406 0.1262  -0.0496 -0.0110 1524 ASN A OD1 
444  N  ND2 . ASN A 54  ? 1.0102 1.2232 1.6813 0.1118  -0.0665 0.0013  1524 ASN A ND2 
445  N  N   . SER A 55  ? 0.9122 1.2726 1.7166 0.0795  -0.0281 -0.0457 1525 SER A N   
446  C  CA  . SER A 55  ? 0.8631 1.2490 1.6826 0.0618  -0.0239 -0.0526 1525 SER A CA  
447  C  C   . SER A 55  ? 0.9296 1.2883 1.7162 0.0439  -0.0109 -0.0485 1525 SER A C   
448  O  O   . SER A 55  ? 0.8734 1.2029 1.6357 0.0452  0.0005  -0.0429 1525 SER A O   
449  C  CB  . SER A 55  ? 0.8705 1.2947 1.7308 0.0609  -0.0109 -0.0632 1525 SER A CB  
450  O  OG  . SER A 55  ? 0.9308 1.3418 1.7826 0.0581  0.0109  -0.0628 1525 SER A OG  
451  N  N   . PRO A 56  ? 0.9268 1.2935 1.7118 0.0275  -0.0137 -0.0516 1526 PRO A N   
452  C  CA  . PRO A 56  ? 0.9259 1.2655 1.6796 0.0116  -0.0027 -0.0486 1526 PRO A CA  
453  C  C   . PRO A 56  ? 0.9061 1.2381 1.6586 0.0062  0.0203  -0.0491 1526 PRO A C   
454  O  O   . PRO A 56  ? 0.9746 1.2775 1.6974 -0.0013 0.0293  -0.0448 1526 PRO A O   
455  C  CB  . PRO A 56  ? 0.9214 1.2792 1.6849 -0.0045 -0.0093 -0.0548 1526 PRO A CB  
456  C  CG  . PRO A 56  ? 0.9068 1.2893 1.6912 0.0053  -0.0307 -0.0573 1526 PRO A CG  
457  C  CD  . PRO A 56  ? 0.8886 1.2861 1.6973 0.0239  -0.0298 -0.0576 1526 PRO A CD  
458  N  N   . ALA A 57  ? 0.8669 1.2251 1.6505 0.0098  0.0299  -0.0547 1527 ALA A N   
459  C  CA  . ALA A 57  ? 0.7923 1.1418 1.5715 0.0056  0.0511  -0.0547 1527 ALA A CA  
460  C  C   . ALA A 57  ? 0.8845 1.2057 1.6427 0.0198  0.0545  -0.0484 1527 ALA A C   
461  O  O   . ALA A 57  ? 0.9076 1.2035 1.6422 0.0145  0.0671  -0.0445 1527 ALA A O   
462  C  CB  . ALA A 57  ? 0.8234 1.2109 1.6407 0.0047  0.0613  -0.0630 1527 ALA A CB  
463  N  N   . HIS A 58  ? 0.7780 1.1017 1.5439 0.0377  0.0425  -0.0471 1528 HIS A N   
464  C  CA  . HIS A 58  ? 0.7524 1.0450 1.4953 0.0498  0.0431  -0.0401 1528 HIS A CA  
465  C  C   . HIS A 58  ? 0.6967 0.9544 1.4004 0.0423  0.0410  -0.0316 1528 HIS A C   
466  O  O   . HIS A 58  ? 0.6595 0.8921 1.3415 0.0409  0.0520  -0.0274 1528 HIS A O   
467  C  CB  . HIS A 58  ? 0.7458 1.0427 1.5005 0.0694  0.0271  -0.0391 1528 HIS A CB  
468  C  CG  . HIS A 58  ? 0.8184 1.0849 1.5539 0.0815  0.0287  -0.0329 1528 HIS A CG  
469  N  ND1 . HIS A 58  ? 0.8864 1.1364 1.6121 0.0951  0.0121  -0.0264 1528 HIS A ND1 
470  C  CD2 . HIS A 58  ? 0.8427 1.0914 1.5661 0.0814  0.0441  -0.0320 1528 HIS A CD2 
471  C  CE1 . HIS A 58  ? 0.8414 1.0647 1.5509 0.1021  0.0176  -0.0219 1528 HIS A CE1 
472  N  NE2 . HIS A 58  ? 0.8224 1.0452 1.5307 0.0942  0.0368  -0.0256 1528 HIS A NE2 
473  N  N   . GLU A 59  ? 0.5210 0.7784 1.2158 0.0374  0.0270  -0.0298 1529 GLU A N   
474  C  CA  . GLU A 59  ? 0.6586 0.8850 1.3162 0.0318  0.0247  -0.0225 1529 GLU A CA  
475  C  C   . GLU A 59  ? 0.6651 0.8803 1.3083 0.0166  0.0401  -0.0240 1529 GLU A C   
476  O  O   . GLU A 59  ? 0.4969 0.6848 1.1126 0.0149  0.0464  -0.0187 1529 GLU A O   
477  C  CB  . GLU A 59  ? 0.7033 0.9329 1.3536 0.0307  0.0058  -0.0209 1529 GLU A CB  
478  C  CG  . GLU A 59  ? 0.8363 1.0674 1.4916 0.0471  -0.0113 -0.0165 1529 GLU A CG  
479  C  CD  . GLU A 59  ? 0.9809 1.1778 1.6010 0.0524  -0.0158 -0.0055 1529 GLU A CD  
480  O  OE1 . GLU A 59  ? 1.0947 1.2865 1.7157 0.0661  -0.0284 -0.0003 1529 GLU A OE1 
481  O  OE2 . GLU A 59  ? 0.9628 1.1381 1.5550 0.0429  -0.0068 -0.0022 1529 GLU A OE2 
482  N  N   . GLU A 60  ? 0.4110 0.6466 1.0732 0.0054  0.0465  -0.0311 1530 GLU A N   
483  C  CA  . GLU A 60  ? 0.5998 0.8215 1.2475 -0.0083 0.0605  -0.0319 1530 GLU A CA  
484  C  C   . GLU A 60  ? 0.4727 0.6832 1.1169 -0.0046 0.0765  -0.0301 1530 GLU A C   
485  O  O   . GLU A 60  ? 0.4047 0.5921 1.0263 -0.0104 0.0855  -0.0274 1530 GLU A O   
486  C  CB  . GLU A 60  ? 0.8592 1.1028 1.5264 -0.0229 0.0630  -0.0390 1530 GLU A CB  
487  C  CG  . GLU A 60  ? 0.9371 1.1616 1.5860 -0.0375 0.0750  -0.0393 1530 GLU A CG  
488  C  CD  . GLU A 60  ? 0.9149 1.1587 1.5831 -0.0534 0.0789  -0.0455 1530 GLU A CD  
489  O  OE1 . GLU A 60  ? 0.9003 1.1723 1.5980 -0.0535 0.0836  -0.0491 1530 GLU A OE1 
490  O  OE2 . GLU A 60  ? 0.7991 1.0292 1.4526 -0.0660 0.0779  -0.0469 1530 GLU A OE2 
491  N  N   . PHE A 61  ? 0.3379 0.5639 1.0035 0.0057  0.0796  -0.0320 1531 PHE A N   
492  C  CA  . PHE A 61  ? 0.4069 0.6198 1.0657 0.0098  0.0937  -0.0305 1531 PHE A CA  
493  C  C   . PHE A 61  ? 0.3582 0.5415 0.9911 0.0186  0.0904  -0.0232 1531 PHE A C   
494  O  O   . PHE A 61  ? 0.3934 0.5581 1.0109 0.0176  0.1013  -0.0209 1531 PHE A O   
495  C  CB  . PHE A 61  ? 0.3252 0.5624 1.0126 0.0187  0.0988  -0.0360 1531 PHE A CB  
496  C  CG  . PHE A 61  ? 0.3871 0.6485 1.0943 0.0069  0.1107  -0.0423 1531 PHE A CG  
497  C  CD1 . PHE A 61  ? 0.4001 0.6478 1.0921 -0.0054 0.1250  -0.0411 1531 PHE A CD1 
498  C  CD2 . PHE A 61  ? 0.3196 0.6174 1.0603 0.0076  0.1074  -0.0491 1531 PHE A CD2 
499  C  CE1 . PHE A 61  ? 0.3205 0.5878 1.0278 -0.0179 0.1362  -0.0455 1531 PHE A CE1 
500  C  CE2 . PHE A 61  ? 0.3995 0.7204 1.1582 -0.0054 0.1194  -0.0544 1531 PHE A CE2 
501  C  CZ  . PHE A 61  ? 0.3632 0.6679 1.1041 -0.0186 0.1340  -0.0521 1531 PHE A CZ  
502  N  N   . LYS A 62  ? 0.3962 0.5752 1.0242 0.0268  0.0755  -0.0193 1532 LYS A N   
503  C  CA  . LYS A 62  ? 0.4983 0.6486 1.0994 0.0320  0.0724  -0.0113 1532 LYS A CA  
504  C  C   . LYS A 62  ? 0.4554 0.5869 1.0300 0.0203  0.0775  -0.0088 1532 LYS A C   
505  O  O   . LYS A 62  ? 0.4710 0.5814 1.0268 0.0203  0.0849  -0.0048 1532 LYS A O   
506  C  CB  . LYS A 62  ? 0.4886 0.6374 1.0875 0.0415  0.0545  -0.0066 1532 LYS A CB  
507  C  CG  . LYS A 62  ? 0.5732 0.7308 1.1926 0.0573  0.0485  -0.0075 1532 LYS A CG  
508  C  CD  . LYS A 62  ? 0.7390 0.8956 1.3568 0.0663  0.0285  -0.0026 1532 LYS A CD  
509  C  CE  . LYS A 62  ? 0.9436 1.0879 1.5639 0.0823  0.0225  0.0012  1532 LYS A CE  
510  N  NZ  . LYS A 62  ? 0.9244 1.0648 1.5412 0.0916  0.0018  0.0071  1532 LYS A NZ  
511  N  N   . THR A 63  ? 0.4392 0.5789 1.0133 0.0103  0.0735  -0.0119 1533 THR A N   
512  C  CA  . THR A 63  ? 0.5067 0.6289 1.0569 0.0001  0.0785  -0.0113 1533 THR A CA  
513  C  C   . THR A 63  ? 0.3442 0.4590 0.8928 -0.0055 0.0944  -0.0133 1533 THR A C   
514  O  O   . THR A 63  ? 0.4160 0.5104 0.9436 -0.0074 0.1006  -0.0106 1533 THR A O   
515  C  CB  . THR A 63  ? 0.6050 0.7370 1.1562 -0.0094 0.0705  -0.0157 1533 THR A CB  
516  O  OG1 . THR A 63  ? 0.6010 0.7368 1.1486 -0.0037 0.0546  -0.0130 1533 THR A OG1 
517  C  CG2 . THR A 63  ? 0.4216 0.5350 0.9491 -0.0190 0.0758  -0.0167 1533 THR A CG2 
518  N  N   . MET A 64  ? 0.4142 0.5463 0.9846 -0.0084 0.1012  -0.0180 1534 MET A N   
519  C  CA  . MET A 64  ? 0.4044 0.5289 0.9717 -0.0136 0.1160  -0.0190 1534 MET A CA  
520  C  C   . MET A 64  ? 0.3932 0.5022 0.9504 -0.0043 0.1218  -0.0150 1534 MET A C   
521  O  O   . MET A 64  ? 0.3289 0.4211 0.8709 -0.0076 0.1307  -0.0136 1534 MET A O   
522  C  CB  . MET A 64  ? 0.3253 0.4735 0.9179 -0.0185 0.1225  -0.0243 1534 MET A CB  
523  C  CG  . MET A 64  ? 0.3793 0.5376 0.9785 -0.0327 0.1208  -0.0283 1534 MET A CG  
524  S  SD  . MET A 64  ? 0.4517 0.6432 1.0840 -0.0397 0.1286  -0.0341 1534 MET A SD  
525  C  CE  . MET A 64  ? 0.6277 0.8489 1.2857 -0.0353 0.1127  -0.0380 1534 MET A CE  
526  N  N   . LEU A 65  ? 0.4489 0.5633 1.0154 0.0074  0.1163  -0.0134 1535 LEU A N   
527  C  CA  . LEU A 65  ? 0.3721 0.4700 0.9285 0.0159  0.1200  -0.0097 1535 LEU A CA  
528  C  C   . LEU A 65  ? 0.3776 0.4522 0.9076 0.0140  0.1180  -0.0040 1535 LEU A C   
529  O  O   . LEU A 65  ? 0.3243 0.3834 0.8416 0.0138  0.1257  -0.0022 1535 LEU A O   
530  C  CB  . LEU A 65  ? 0.4092 0.5142 0.9791 0.0289  0.1118  -0.0090 1535 LEU A CB  
531  C  CG  . LEU A 65  ? 0.4019 0.4874 0.9609 0.0378  0.1126  -0.0048 1535 LEU A CG  
532  C  CD1 . LEU A 65  ? 0.3224 0.4028 0.8800 0.0366  0.1264  -0.0077 1535 LEU A CD1 
533  C  CD2 . LEU A 65  ? 0.3384 0.4310 0.9130 0.0513  0.1024  -0.0049 1535 LEU A CD2 
534  N  N   . LEU A 66  ? 0.3365 0.4099 0.8582 0.0127  0.1076  -0.0015 1536 LEU A N   
535  C  CA  . LEU A 66  ? 0.4041 0.4583 0.9008 0.0105  0.1065  0.0034  1536 LEU A CA  
536  C  C   . LEU A 66  ? 0.4616 0.5070 0.9468 0.0020  0.1162  0.0007  1536 LEU A C   
537  O  O   . LEU A 66  ? 0.3515 0.3816 0.8216 0.0023  0.1216  0.0034  1536 LEU A O   
538  C  CB  . LEU A 66  ? 0.3992 0.4556 0.8877 0.0095  0.0941  0.0057  1536 LEU A CB  
539  C  CG  . LEU A 66  ? 0.3630 0.4027 0.8248 0.0061  0.0939  0.0098  1536 LEU A CG  
540  C  CD1 . LEU A 66  ? 0.3741 0.3996 0.8268 0.0117  0.0961  0.0165  1536 LEU A CD1 
541  C  CD2 . LEU A 66  ? 0.4924 0.5358 0.9455 0.0051  0.0813  0.0115  1536 LEU A CD2 
542  N  N   . ILE A 67  ? 0.3766 0.4314 0.8697 -0.0055 0.1183  -0.0046 1537 ILE A N   
543  C  CA  . ILE A 67  ? 0.4573 0.5016 0.9395 -0.0134 0.1262  -0.0073 1537 ILE A CA  
544  C  C   . ILE A 67  ? 0.3726 0.4090 0.8545 -0.0116 0.1371  -0.0067 1537 ILE A C   
545  O  O   . ILE A 67  ? 0.4420 0.4632 0.9089 -0.0127 0.1421  -0.0059 1537 ILE A O   
546  C  CB  . ILE A 67  ? 0.4480 0.5027 0.9399 -0.0228 0.1253  -0.0127 1537 ILE A CB  
547  C  CG1 . ILE A 67  ? 0.5299 0.5857 1.0138 -0.0266 0.1149  -0.0145 1537 ILE A CG1 
548  C  CG2 . ILE A 67  ? 0.3372 0.3802 0.8221 -0.0299 0.1350  -0.0149 1537 ILE A CG2 
549  C  CD1 . ILE A 67  ? 0.3710 0.4442 0.8716 -0.0340 0.1094  -0.0195 1537 ILE A CD1 
550  N  N   . ALA A 68  ? 0.3301 0.3778 0.8289 -0.0084 0.1408  -0.0077 1538 ALA A N   
551  C  CA  . ALA A 68  ? 0.4079 0.4482 0.9048 -0.0064 0.1506  -0.0074 1538 ALA A CA  
552  C  C   . ALA A 68  ? 0.3671 0.3928 0.8515 0.0006  0.1502  -0.0033 1538 ALA A C   
553  O  O   . ALA A 68  ? 0.3123 0.3258 0.7868 0.0004  0.1567  -0.0027 1538 ALA A O   
554  C  CB  . ALA A 68  ? 0.3119 0.3686 0.8284 -0.0032 0.1547  -0.0101 1538 ALA A CB  
555  N  N   . HIS A 69  ? 0.3181 0.3444 0.8027 0.0064  0.1419  -0.0001 1539 HIS A N   
556  C  CA  . HIS A 69  ? 0.3198 0.3317 0.7921 0.0110  0.1412  0.0046  1539 HIS A CA  
557  C  C   . HIS A 69  ? 0.4218 0.4220 0.8758 0.0059  0.1432  0.0058  1539 HIS A C   
558  O  O   . HIS A 69  ? 0.3826 0.3721 0.8282 0.0066  0.1482  0.0070  1539 HIS A O   
559  C  CB  . HIS A 69  ? 0.3272 0.3407 0.8021 0.0172  0.1312  0.0088  1539 HIS A CB  
560  C  CG  . HIS A 69  ? 0.3837 0.3824 0.8417 0.0177  0.1287  0.0148  1539 HIS A CG  
561  N  ND1 . HIS A 69  ? 0.3326 0.3195 0.7860 0.0204  0.1326  0.0171  1539 HIS A ND1 
562  C  CD2 . HIS A 69  ? 0.3694 0.3640 0.8135 0.0148  0.1231  0.0189  1539 HIS A CD2 
563  C  CE1 . HIS A 69  ? 0.4355 0.4125 0.8744 0.0186  0.1298  0.0228  1539 HIS A CE1 
564  N  NE2 . HIS A 69  ? 0.4022 0.3838 0.8346 0.0153  0.1245  0.0241  1539 HIS A NE2 
565  N  N   . TYR A 70  ? 0.4304 0.4334 0.8787 0.0009  0.1392  0.0046  1540 TYR A N   
566  C  CA  . TYR A 70  ? 0.3887 0.3820 0.8205 -0.0032 0.1417  0.0038  1540 TYR A CA  
567  C  C   . TYR A 70  ? 0.3408 0.3270 0.7708 -0.0053 0.1503  0.0006  1540 TYR A C   
568  O  O   . TYR A 70  ? 0.3876 0.3644 0.8078 -0.0042 0.1540  0.0012  1540 TYR A O   
569  C  CB  . TYR A 70  ? 0.3378 0.3353 0.7646 -0.0082 0.1364  0.0008  1540 TYR A CB  
570  C  CG  . TYR A 70  ? 0.3473 0.3486 0.7683 -0.0067 0.1273  0.0043  1540 TYR A CG  
571  C  CD1 . TYR A 70  ? 0.4097 0.4059 0.8239 -0.0025 0.1254  0.0108  1540 TYR A CD1 
572  C  CD2 . TYR A 70  ? 0.3555 0.3642 0.7763 -0.0103 0.1199  0.0014  1540 TYR A CD2 
573  C  CE1 . TYR A 70  ? 0.3632 0.3606 0.7689 -0.0017 0.1166  0.0153  1540 TYR A CE1 
574  C  CE2 . TYR A 70  ? 0.4298 0.4412 0.8429 -0.0089 0.1106  0.0050  1540 TYR A CE2 
575  C  CZ  . TYR A 70  ? 0.3745 0.3797 0.7792 -0.0045 0.1091  0.0124  1540 TYR A CZ  
576  O  OH  . TYR A 70  ? 0.4193 0.4252 0.8136 -0.0037 0.0994  0.0171  1540 TYR A OH  
577  N  N   . TYR A 71  ? 0.3486 0.3394 0.7880 -0.0086 0.1531  -0.0026 1541 TYR A N   
578  C  CA  . TYR A 71  ? 0.3509 0.3326 0.7861 -0.0109 0.1604  -0.0045 1541 TYR A CA  
579  C  C   . TYR A 71  ? 0.3155 0.2916 0.7499 -0.0056 0.1652  -0.0023 1541 TYR A C   
580  O  O   . TYR A 71  ? 0.4668 0.4322 0.8919 -0.0053 0.1688  -0.0026 1541 TYR A O   
581  C  CB  . TYR A 71  ? 0.3225 0.3104 0.7673 -0.0169 0.1631  -0.0071 1541 TYR A CB  
582  C  CG  . TYR A 71  ? 0.5130 0.4987 0.9540 -0.0246 0.1603  -0.0105 1541 TYR A CG  
583  C  CD1 . TYR A 71  ? 0.4660 0.4359 0.8928 -0.0268 0.1616  -0.0124 1541 TYR A CD1 
584  C  CD2 . TYR A 71  ? 0.3338 0.3330 0.7861 -0.0292 0.1555  -0.0124 1541 TYR A CD2 
585  C  CE1 . TYR A 71  ? 0.3486 0.3142 0.7714 -0.0337 0.1582  -0.0163 1541 TYR A CE1 
586  C  CE2 . TYR A 71  ? 0.5360 0.5323 0.9849 -0.0370 0.1521  -0.0160 1541 TYR A CE2 
587  C  CZ  . TYR A 71  ? 0.4120 0.3902 0.8453 -0.0392 0.1535  -0.0181 1541 TYR A CZ  
588  O  OH  . TYR A 71  ? 0.4769 0.4504 0.9066 -0.0468 0.1495  -0.0225 1541 TYR A OH  
589  N  N   . ALA A 72  ? 0.4343 0.4175 0.8789 -0.0011 0.1647  -0.0008 1542 ALA A N   
590  C  CA  . ALA A 72  ? 0.3843 0.3612 0.8276 0.0038  0.1685  0.0004  1542 ALA A CA  
591  C  C   . ALA A 72  ? 0.3521 0.3198 0.7852 0.0060  0.1666  0.0032  1542 ALA A C   
592  O  O   . ALA A 72  ? 0.3078 0.2673 0.7350 0.0072  0.1701  0.0031  1542 ALA A O   
593  C  CB  . ALA A 72  ? 0.4088 0.3940 0.8649 0.0092  0.1675  0.0003  1542 ALA A CB  
594  N  N   . THR A 73  ? 0.3123 0.2822 0.7433 0.0063  0.1609  0.0060  1543 THR A N   
595  C  CA  . THR A 73  ? 0.3521 0.3154 0.7734 0.0068  0.1598  0.0092  1543 THR A CA  
596  C  C   . THR A 73  ? 0.5582 0.5173 0.9699 0.0038  0.1634  0.0064  1543 THR A C   
597  O  O   . THR A 73  ? 0.3730 0.3275 0.7794 0.0045  0.1656  0.0072  1543 THR A O   
598  C  CB  . THR A 73  ? 0.3572 0.3236 0.7755 0.0065  0.1531  0.0133  1543 THR A CB  
599  O  OG1 . THR A 73  ? 0.3636 0.3343 0.7926 0.0106  0.1483  0.0150  1543 THR A OG1 
600  C  CG2 . THR A 73  ? 0.4460 0.4060 0.8546 0.0059  0.1529  0.0179  1543 THR A CG2 
601  N  N   . ARG A 74  ? 0.4972 0.4579 0.9076 0.0005  0.1637  0.0027  1544 ARG A N   
602  C  CA  . ARG A 74  ? 0.4202 0.3748 0.8218 -0.0009 0.1663  -0.0009 1544 ARG A CA  
603  C  C   . ARG A 74  ? 0.3458 0.2930 0.7471 0.0010  0.1708  -0.0019 1544 ARG A C   
604  O  O   . ARG A 74  ? 0.4141 0.3570 0.8098 0.0029  0.1724  -0.0031 1544 ARG A O   
605  C  CB  . ARG A 74  ? 0.3251 0.2800 0.7252 -0.0051 0.1647  -0.0048 1544 ARG A CB  
606  C  CG  . ARG A 74  ? 0.3314 0.2777 0.7214 -0.0054 0.1662  -0.0096 1544 ARG A CG  
607  C  CD  . ARG A 74  ? 0.3399 0.2834 0.7280 -0.0102 0.1638  -0.0138 1544 ARG A CD  
608  N  NE  . ARG A 74  ? 0.3608 0.2996 0.7541 -0.0134 0.1660  -0.0136 1544 ARG A NE  
609  C  CZ  . ARG A 74  ? 0.3489 0.2831 0.7418 -0.0193 0.1646  -0.0165 1544 ARG A CZ  
610  N  NH1 . ARG A 74  ? 0.3957 0.3285 0.7832 -0.0219 0.1603  -0.0209 1544 ARG A NH1 
611  N  NH2 . ARG A 74  ? 0.3504 0.2812 0.7475 -0.0233 0.1677  -0.0151 1544 ARG A NH2 
612  N  N   . SER A 75  ? 0.3483 0.2950 0.7555 0.0008  0.1729  -0.0018 1545 SER A N   
613  C  CA  . SER A 75  ? 0.3140 0.2527 0.7181 0.0026  0.1765  -0.0024 1545 SER A CA  
614  C  C   . SER A 75  ? 0.4100 0.3477 0.8140 0.0067  0.1765  -0.0006 1545 SER A C   
615  O  O   . SER A 75  ? 0.5142 0.4460 0.9132 0.0085  0.1775  -0.0018 1545 SER A O   
616  C  CB  . SER A 75  ? 0.3148 0.2544 0.7235 0.0011  0.1797  -0.0024 1545 SER A CB  
617  O  OG  . SER A 75  ? 0.3967 0.3361 0.8052 -0.0045 0.1801  -0.0039 1545 SER A OG  
618  N  N   . ALA A 76  ? 0.3520 0.2947 0.7617 0.0081  0.1745  0.0021  1546 ALA A N   
619  C  CA  . ALA A 76  ? 0.3312 0.2715 0.7406 0.0103  0.1737  0.0041  1546 ALA A CA  
620  C  C   . ALA A 76  ? 0.4395 0.3802 0.8432 0.0091  0.1736  0.0041  1546 ALA A C   
621  O  O   . ALA A 76  ? 0.4033 0.3413 0.8055 0.0103  0.1747  0.0031  1546 ALA A O   
622  C  CB  . ALA A 76  ? 0.3389 0.2817 0.7539 0.0116  0.1703  0.0076  1546 ALA A CB  
623  N  N   . ALA A 77  ? 0.4083 0.3536 0.8089 0.0069  0.1723  0.0045  1547 ALA A N   
624  C  CA  . ALA A 77  ? 0.3126 0.2609 0.7077 0.0058  0.1733  0.0035  1547 ALA A CA  
625  C  C   . ALA A 77  ? 0.4285 0.3736 0.8212 0.0080  0.1756  -0.0017 1547 ALA A C   
626  O  O   . ALA A 77  ? 0.4593 0.4074 0.8514 0.0091  0.1770  -0.0032 1547 ALA A O   
627  C  CB  . ALA A 77  ? 0.3426 0.2960 0.7325 0.0032  0.1715  0.0038  1547 ALA A CB  
628  N  N   . GLN A 78  ? 0.5075 0.4467 0.8989 0.0086  0.1757  -0.0044 1548 GLN A N   
629  C  CA  . GLN A 78  ? 0.4183 0.3506 0.8060 0.0113  0.1765  -0.0084 1548 GLN A CA  
630  C  C   . GLN A 78  ? 0.5751 0.5041 0.9648 0.0142  0.1768  -0.0078 1548 GLN A C   
631  O  O   . GLN A 78  ? 0.4587 0.3829 0.8456 0.0176  0.1763  -0.0108 1548 GLN A O   
632  C  CB  . GLN A 78  ? 0.3233 0.2470 0.7078 0.0095  0.1761  -0.0099 1548 GLN A CB  
633  C  CG  . GLN A 78  ? 0.3423 0.2677 0.7241 0.0065  0.1746  -0.0123 1548 GLN A CG  
634  C  CD  . GLN A 78  ? 0.4769 0.3954 0.8579 0.0023  0.1741  -0.0128 1548 GLN A CD  
635  O  OE1 . GLN A 78  ? 0.3588 0.2747 0.7425 0.0009  0.1758  -0.0102 1548 GLN A OE1 
636  N  NE2 . GLN A 78  ? 0.3885 0.3043 0.7654 -0.0002 0.1720  -0.0165 1548 GLN A NE2 
637  N  N   . SER A 79  ? 0.3838 0.3143 0.7777 0.0135  0.1769  -0.0044 1549 SER A N   
638  C  CA  . SER A 79  ? 0.4397 0.3665 0.8343 0.0161  0.1765  -0.0046 1549 SER A CA  
639  C  C   . SER A 79  ? 0.4349 0.3678 0.8326 0.0170  0.1758  -0.0056 1549 SER A C   
640  O  O   . SER A 79  ? 0.4574 0.3876 0.8553 0.0197  0.1744  -0.0073 1549 SER A O   
641  C  CB  . SER A 79  ? 0.4717 0.3970 0.8696 0.0157  0.1766  -0.0021 1549 SER A CB  
642  O  OG  . SER A 79  ? 0.4905 0.4207 0.8931 0.0141  0.1753  0.0007  1549 SER A OG  
643  N  N   . VAL A 80  ? 0.4698 0.4117 0.8698 0.0145  0.1766  -0.0045 1550 VAL A N   
644  C  CA  . VAL A 80  ? 0.4125 0.3630 0.8167 0.0139  0.1771  -0.0054 1550 VAL A CA  
645  C  C   . VAL A 80  ? 0.4602 0.4202 0.8629 0.0137  0.1795  -0.0083 1550 VAL A C   
646  O  O   . VAL A 80  ? 0.4528 0.4146 0.8512 0.0113  0.1805  -0.0069 1550 VAL A O   
647  C  CB  . VAL A 80  ? 0.4389 0.3921 0.8471 0.0092  0.1766  -0.0005 1550 VAL A CB  
648  C  CG1 . VAL A 80  ? 0.6330 0.5776 1.0432 0.0104  0.1740  0.0001  1550 VAL A CG1 
649  C  CG2 . VAL A 80  ? 0.5701 0.5229 0.9752 0.0058  0.1766  0.0042  1550 VAL A CG2 
650  N  N   . LYS A 81  ? 0.5279 0.4955 0.9348 0.0166  0.1802  -0.0128 1551 LYS A N   
651  C  CA  . LYS A 81  ? 0.4594 0.4368 0.8654 0.0184  0.1829  -0.0179 1551 LYS A CA  
652  C  C   . LYS A 81  ? 0.4891 0.4761 0.8922 0.0123  0.1864  -0.0147 1551 LYS A C   
653  O  O   . LYS A 81  ? 0.4118 0.4008 0.8083 0.0127  0.1881  -0.0174 1551 LYS A O   
654  C  CB  . LYS A 81  ? 0.5048 0.4928 0.9194 0.0226  0.1831  -0.0232 1551 LYS A CB  
655  C  CG  . LYS A 81  ? 0.5439 0.5450 0.9594 0.0255  0.1868  -0.0299 1551 LYS A CG  
656  C  CD  . LYS A 81  ? 0.5075 0.4973 0.9157 0.0322  0.1847  -0.0354 1551 LYS A CD  
657  C  CE  . LYS A 81  ? 0.7740 0.7766 1.1841 0.0376  0.1878  -0.0445 1551 LYS A CE  
658  N  NZ  . LYS A 81  ? 0.9060 0.8937 1.3091 0.0451  0.1842  -0.0506 1551 LYS A NZ  
659  N  N   A GLN A 82  ? 0.3334 0.3242 0.7395 0.0061  0.1871  -0.0086 1552 GLN A N   
660  N  N   B GLN A 82  ? 0.3361 0.3269 0.7422 0.0061  0.1871  -0.0085 1552 GLN A N   
661  C  CA  A GLN A 82  ? 0.4427 0.4421 0.8444 -0.0006 0.1903  -0.0043 1552 GLN A CA  
662  C  CA  B GLN A 82  ? 0.4416 0.4410 0.8431 -0.0006 0.1903  -0.0044 1552 GLN A CA  
663  C  C   A GLN A 82  ? 0.4376 0.4289 0.8295 -0.0025 0.1883  -0.0001 1552 GLN A C   
664  C  C   B GLN A 82  ? 0.4405 0.4320 0.8322 -0.0024 0.1883  -0.0003 1552 GLN A C   
665  O  O   A GLN A 82  ? 0.4852 0.4821 0.8704 -0.0078 0.1901  0.0038  1552 GLN A O   
666  O  O   B GLN A 82  ? 0.4854 0.4827 0.8701 -0.0074 0.1903  0.0031  1552 GLN A O   
667  C  CB  A GLN A 82  ? 0.4729 0.4752 0.8800 -0.0074 0.1905  0.0018  1552 GLN A CB  
668  C  CB  B GLN A 82  ? 0.4730 0.4753 0.8795 -0.0076 0.1906  0.0021  1552 GLN A CB  
669  C  CG  A GLN A 82  ? 0.5721 0.5596 0.9819 -0.0068 0.1853  0.0057  1552 GLN A CG  
670  C  CG  B GLN A 82  ? 0.5117 0.4986 0.9174 -0.0091 0.1856  0.0085  1552 GLN A CG  
671  C  CD  A GLN A 82  ? 0.6171 0.6044 1.0358 -0.0034 0.1834  0.0015  1552 GLN A CD  
672  C  CD  B GLN A 82  ? 0.4800 0.4664 0.8919 -0.0148 0.1845  0.0128  1552 GLN A CD  
673  O  OE1 A GLN A 82  ? 0.3100 0.3007 0.7312 0.0028  0.1835  -0.0051 1552 GLN A OE1 
674  O  OE1 B GLN A 82  ? 0.5103 0.4929 0.9184 -0.0215 0.1837  0.0202  1552 GLN A OE1 
675  N  NE2 A GLN A 82  ? 0.5009 0.4828 0.9236 -0.0073 0.1807  0.0052  1552 GLN A NE2 
676  N  NE2 B GLN A 82  ? 0.4248 0.4137 0.8455 -0.0125 0.1836  0.0083  1552 GLN A NE2 
677  N  N   . LEU A 83  ? 0.4074 0.3868 0.7983 0.0011  0.1845  -0.0005 1553 LEU A N   
678  C  CA  . LEU A 83  ? 0.4396 0.4142 0.8237 -0.0002 0.1820  0.0020  1553 LEU A CA  
679  C  C   . LEU A 83  ? 0.4177 0.3906 0.7970 0.0031  0.1818  -0.0047 1553 LEU A C   
680  O  O   . LEU A 83  ? 0.3845 0.3533 0.7600 0.0020  0.1788  -0.0036 1553 LEU A O   
681  C  CB  . LEU A 83  ? 0.3913 0.3558 0.7794 0.0003  0.1779  0.0064  1553 LEU A CB  
682  C  CG  . LEU A 83  ? 0.4453 0.4077 0.8367 -0.0028 0.1766  0.0128  1553 LEU A CG  
683  C  CD1 . LEU A 83  ? 0.3192 0.2719 0.7151 -0.0004 0.1728  0.0152  1553 LEU A CD1 
684  C  CD2 . LEU A 83  ? 0.3728 0.3394 0.7574 -0.0085 0.1765  0.0188  1553 LEU A CD2 
685  N  N   A GLU A 84  ? 0.4004 0.3758 0.7807 0.0073  0.1841  -0.0118 1554 GLU A N   
686  N  N   B GLU A 84  ? 0.3943 0.3703 0.7741 0.0070  0.1842  -0.0118 1554 GLU A N   
687  C  CA  A GLU A 84  ? 0.4353 0.4060 0.8103 0.0106  0.1832  -0.0187 1554 GLU A CA  
688  C  CA  B GLU A 84  ? 0.4434 0.4145 0.8180 0.0103  0.1833  -0.0186 1554 GLU A CA  
689  C  C   A GLU A 84  ? 0.3963 0.3695 0.7622 0.0071  0.1824  -0.0188 1554 GLU A C   
690  C  C   B GLU A 84  ? 0.3926 0.3665 0.7578 0.0068  0.1825  -0.0188 1554 GLU A C   
691  O  O   A GLU A 84  ? 0.4640 0.4296 0.8269 0.0064  0.1789  -0.0199 1554 GLU A O   
692  O  O   B GLU A 84  ? 0.4118 0.3782 0.7737 0.0063  0.1790  -0.0201 1554 GLU A O   
693  C  CB  A GLU A 84  ? 0.4125 0.3887 0.7891 0.0161  0.1859  -0.0267 1554 GLU A CB  
694  C  CB  B GLU A 84  ? 0.4286 0.4040 0.8047 0.0161  0.1857  -0.0268 1554 GLU A CB  
695  C  CG  A GLU A 84  ? 0.4635 0.4269 0.8393 0.0221  0.1831  -0.0328 1554 GLU A CG  
696  C  CG  B GLU A 84  ? 0.4007 0.3933 0.7783 0.0149  0.1908  -0.0282 1554 GLU A CG  
697  C  CD  A GLU A 84  ? 0.4743 0.4425 0.8548 0.0295  0.1842  -0.0399 1554 GLU A CD  
698  C  CD  B GLU A 84  ? 0.5419 0.5416 0.9233 0.0222  0.1932  -0.0379 1554 GLU A CD  
699  O  OE1 A GLU A 84  ? 0.4698 0.4530 0.8514 0.0306  0.1882  -0.0442 1554 GLU A OE1 
700  O  OE1 B GLU A 84  ? 0.4699 0.4585 0.8527 0.0288  0.1897  -0.0427 1554 GLU A OE1 
701  O  OE2 A GLU A 84  ? 0.4620 0.4196 0.8449 0.0344  0.1809  -0.0413 1554 GLU A OE2 
702  O  OE2 B GLU A 84  ? 0.5558 0.5725 0.9386 0.0213  0.1985  -0.0407 1554 GLU A OE2 
703  N  N   A THR A 85  ? 0.4002 0.3846 0.7611 0.0040  0.1854  -0.0172 1555 THR A N   
704  N  N   B THR A 85  ? 0.3884 0.3735 0.7484 0.0038  0.1855  -0.0173 1555 THR A N   
705  C  CA  A THR A 85  ? 0.3572 0.3444 0.7066 0.0008  0.1842  -0.0175 1555 THR A CA  
706  C  CA  B THR A 85  ? 0.3580 0.3457 0.7065 0.0005  0.1842  -0.0174 1555 THR A CA  
707  C  C   A THR A 85  ? 0.4669 0.4477 0.8154 -0.0026 0.1783  -0.0106 1555 THR A C   
708  C  C   B THR A 85  ? 0.4760 0.4570 0.8242 -0.0028 0.1783  -0.0104 1555 THR A C   
709  O  O   A THR A 85  ? 0.4837 0.4617 0.8263 -0.0035 0.1745  -0.0130 1555 THR A O   
710  O  O   B THR A 85  ? 0.4583 0.4366 0.8005 -0.0037 0.1743  -0.0127 1555 THR A O   
711  C  CB  A THR A 85  ? 0.3832 0.3837 0.7259 -0.0029 0.1892  -0.0156 1555 THR A CB  
712  C  CB  B THR A 85  ? 0.3707 0.3714 0.7120 -0.0034 0.1891  -0.0152 1555 THR A CB  
713  O  OG1 A THR A 85  ? 0.5778 0.5876 0.9233 0.0013  0.1950  -0.0240 1555 THR A OG1 
714  O  OG1 B THR A 85  ? 0.3612 0.3637 0.7082 -0.0074 0.1898  -0.0061 1555 THR A OG1 
715  C  CG2 A THR A 85  ? 0.4027 0.4055 0.7306 -0.0064 0.1876  -0.0153 1555 THR A CG2 
716  C  CG2 B THR A 85  ? 0.5303 0.5417 0.8723 0.0008  0.1955  -0.0248 1555 THR A CG2 
717  N  N   . VAL A 86  ? 0.4585 0.4372 0.8138 -0.0041 0.1770  -0.0027 1556 VAL A N   
718  C  CA  . VAL A 86  ? 0.3482 0.3217 0.7058 -0.0055 0.1712  0.0028  1556 VAL A CA  
719  C  C   . VAL A 86  ? 0.3532 0.3210 0.7158 -0.0033 0.1687  -0.0021 1556 VAL A C   
720  O  O   . VAL A 86  ? 0.4063 0.3741 0.7663 -0.0050 0.1643  -0.0028 1556 VAL A O   
721  C  CB  . VAL A 86  ? 0.3423 0.3125 0.7078 -0.0057 0.1704  0.0100  1556 VAL A CB  
722  C  CG1 . VAL A 86  ? 0.3401 0.3056 0.7114 -0.0046 0.1645  0.0133  1556 VAL A CG1 
723  C  CG2 . VAL A 86  ? 0.6309 0.6048 0.9900 -0.0101 0.1715  0.0166  1556 VAL A CG2 
724  N  N   . ALA A 87  ? 0.3969 0.3597 0.7655 -0.0003 0.1714  -0.0058 1557 ALA A N   
725  C  CA  . ALA A 87  ? 0.4691 0.4250 0.8407 0.0001  0.1696  -0.0094 1557 ALA A CA  
726  C  C   . ALA A 87  ? 0.4979 0.4530 0.8614 -0.0013 0.1677  -0.0155 1557 ALA A C   
727  O  O   . ALA A 87  ? 0.4656 0.4189 0.8302 -0.0042 0.1639  -0.0164 1557 ALA A O   
728  C  CB  . ALA A 87  ? 0.4306 0.3794 0.8062 0.0034  0.1724  -0.0119 1557 ALA A CB  
729  N  N   . ALA A 88  ? 0.3536 0.3116 0.7093 0.0004  0.1702  -0.0202 1558 ALA A N   
730  C  CA  . ALA A 88  ? 0.3999 0.3555 0.7467 -0.0001 0.1683  -0.0276 1558 ALA A CA  
731  C  C   . ALA A 88  ? 0.4076 0.3685 0.7491 -0.0046 0.1636  -0.0251 1558 ALA A C   
732  O  O   . ALA A 88  ? 0.4189 0.3758 0.7586 -0.0071 0.1590  -0.0288 1558 ALA A O   
733  C  CB  . ALA A 88  ? 0.4250 0.3847 0.7647 0.0038  0.1725  -0.0346 1558 ALA A CB  
734  N  N   A ARG A 89  ? 0.3924 0.3612 0.7314 -0.0061 0.1637  -0.0183 1559 ARG A N   
735  N  N   B ARG A 89  ? 0.3881 0.3570 0.7269 -0.0060 0.1638  -0.0183 1559 ARG A N   
736  C  CA  A ARG A 89  ? 0.3804 0.3532 0.7124 -0.0096 0.1578  -0.0156 1559 ARG A CA  
737  C  CA  B ARG A 89  ? 0.3800 0.3531 0.7122 -0.0096 0.1580  -0.0149 1559 ARG A CA  
738  C  C   A ARG A 89  ? 0.4122 0.3831 0.7550 -0.0111 0.1519  -0.0127 1559 ARG A C   
739  C  C   B ARG A 89  ? 0.4075 0.3784 0.7502 -0.0111 0.1520  -0.0127 1559 ARG A C   
740  O  O   A ARG A 89  ? 0.4054 0.3779 0.7453 -0.0138 0.1457  -0.0150 1559 ARG A O   
741  O  O   B ARG A 89  ? 0.4165 0.3888 0.7561 -0.0138 0.1459  -0.0152 1559 ARG A O   
742  C  CB  A ARG A 89  ? 0.4669 0.4461 0.7919 -0.0112 0.1587  -0.0077 1559 ARG A CB  
743  C  CB  B ARG A 89  ? 0.4410 0.4199 0.7683 -0.0111 0.1587  -0.0061 1559 ARG A CB  
744  C  CG  A ARG A 89  ? 0.4040 0.3893 0.7168 -0.0113 0.1652  -0.0115 1559 ARG A CG  
745  C  CG  B ARG A 89  ? 0.5460 0.5316 0.8565 -0.0130 0.1622  -0.0075 1559 ARG A CG  
746  C  CD  A ARG A 89  ? 0.4308 0.4219 0.7368 -0.0148 0.1674  -0.0024 1559 ARG A CD  
747  C  CD  B ARG A 89  ? 0.5145 0.5035 0.8196 -0.0165 0.1627  0.0035  1559 ARG A CD  
748  N  NE  A ARG A 89  ? 0.5816 0.5733 0.8983 -0.0140 0.1728  0.0010  1559 ARG A NE  
749  N  NE  B ARG A 89  ? 0.6188 0.6122 0.9048 -0.0205 0.1607  0.0064  1559 ARG A NE  
750  C  CZ  A ARG A 89  ? 0.5672 0.5620 0.8819 -0.0178 0.1753  0.0091  1559 ARG A CZ  
751  C  CZ  B ARG A 89  ? 0.5378 0.5296 0.8161 -0.0241 0.1563  0.0174  1559 ARG A CZ  
752  N  NH1 A ARG A 89  ? 0.4681 0.4647 0.7688 -0.0229 0.1733  0.0163  1559 ARG A NH1 
753  N  NH1 B ARG A 89  ? 0.4234 0.4091 0.7128 -0.0235 0.1530  0.0257  1559 ARG A NH1 
754  N  NH2 A ARG A 89  ? 0.3808 0.3760 0.7069 -0.0171 0.1794  0.0104  1559 ARG A NH2 
755  N  NH2 B ARG A 89  ? 0.4517 0.4467 0.7099 -0.0281 0.1545  0.0200  1559 ARG A NH2 
756  N  N   . LEU A 90  ? 0.4144 0.3828 0.7701 -0.0095 0.1538  -0.0092 1560 LEU A N   
757  C  CA  . LEU A 90  ? 0.4980 0.4675 0.8653 -0.0108 0.1495  -0.0077 1560 LEU A CA  
758  C  C   . LEU A 90  ? 0.3686 0.3345 0.7366 -0.0139 0.1479  -0.0148 1560 LEU A C   
759  O  O   . LEU A 90  ? 0.4611 0.4316 0.8321 -0.0172 0.1419  -0.0158 1560 LEU A O   
760  C  CB  . LEU A 90  ? 0.4011 0.3690 0.7805 -0.0082 0.1527  -0.0036 1560 LEU A CB  
761  C  CG  . LEU A 90  ? 0.3819 0.3523 0.7627 -0.0060 0.1512  0.0040  1560 LEU A CG  
762  C  CD1 . LEU A 90  ? 0.3339 0.3002 0.7222 -0.0030 0.1558  0.0062  1560 LEU A CD1 
763  C  CD2 . LEU A 90  ? 0.3466 0.3228 0.7334 -0.0058 0.1438  0.0076  1560 LEU A CD2 
764  N  N   . SER A 91  ? 0.4338 0.3909 0.7973 -0.0132 0.1520  -0.0204 1561 SER A N   
765  C  CA  . SER A 91  ? 0.4445 0.3957 0.8082 -0.0174 0.1491  -0.0264 1561 SER A CA  
766  C  C   . SER A 91  ? 0.4484 0.4016 0.8013 -0.0199 0.1437  -0.0316 1561 SER A C   
767  O  O   . SER A 91  ? 0.4670 0.4210 0.8229 -0.0250 0.1382  -0.0343 1561 SER A O   
768  C  CB  . SER A 91  ? 0.3753 0.3131 0.7366 -0.0160 0.1531  -0.0308 1561 SER A CB  
769  O  OG  . SER A 91  ? 0.4453 0.3810 0.8137 -0.0133 0.1578  -0.0261 1561 SER A OG  
770  N  N   . VAL A 92  ? 0.5415 0.4982 0.8825 -0.0170 0.1447  -0.0322 1562 VAL A N   
771  C  CA  . VAL A 92  ? 0.5173 0.4769 0.8461 -0.0195 0.1392  -0.0369 1562 VAL A CA  
772  C  C   . VAL A 92  ? 0.4915 0.4601 0.8256 -0.0230 0.1315  -0.0318 1562 VAL A C   
773  O  O   . VAL A 92  ? 0.4916 0.4609 0.8251 -0.0274 0.1246  -0.0364 1562 VAL A O   
774  C  CB  . VAL A 92  ? 0.5392 0.5025 0.8526 -0.0163 0.1431  -0.0383 1562 VAL A CB  
775  C  CG1 . VAL A 92  ? 0.4344 0.4008 0.7326 -0.0191 0.1371  -0.0432 1562 VAL A CG1 
776  C  CG2 . VAL A 92  ? 0.4614 0.4176 0.7725 -0.0118 0.1498  -0.0453 1562 VAL A CG2 
777  N  N   . SER A 93  ? 0.4937 0.4689 0.8350 -0.0209 0.1317  -0.0227 1563 SER A N   
778  C  CA  . SER A 93  ? 0.4052 0.3890 0.7509 -0.0226 0.1229  -0.0184 1563 SER A CA  
779  C  C   . SER A 93  ? 0.4441 0.4312 0.8071 -0.0258 0.1194  -0.0205 1563 SER A C   
780  O  O   . SER A 93  ? 0.4596 0.4544 0.8259 -0.0286 0.1107  -0.0214 1563 SER A O   
781  C  CB  . SER A 93  ? 0.4107 0.3985 0.7602 -0.0190 0.1224  -0.0083 1563 SER A CB  
782  O  OG  . SER A 93  ? 0.4660 0.4507 0.8035 -0.0171 0.1280  -0.0048 1563 SER A OG  
783  N  N   . LEU A 94  ? 0.5027 0.4844 0.8755 -0.0263 0.1259  -0.0221 1564 LEU A N   
784  C  CA  . LEU A 94  ? 0.3818 0.3682 0.7708 -0.0309 0.1239  -0.0236 1564 LEU A CA  
785  C  C   . LEU A 94  ? 0.5749 0.5597 0.9602 -0.0378 0.1180  -0.0311 1564 LEU A C   
786  O  O   . LEU A 94  ? 0.5010 0.4938 0.9001 -0.0433 0.1140  -0.0325 1564 LEU A O   
787  C  CB  . LEU A 94  ? 0.4178 0.3973 0.8145 -0.0307 0.1325  -0.0229 1564 LEU A CB  
788  C  CG  . LEU A 94  ? 0.3896 0.3759 0.7985 -0.0260 0.1359  -0.0163 1564 LEU A CG  
789  C  CD1 . LEU A 94  ? 0.3633 0.3399 0.7723 -0.0242 0.1446  -0.0155 1564 LEU A CD1 
790  C  CD2 . LEU A 94  ? 0.3546 0.3556 0.7824 -0.0285 0.1322  -0.0156 1564 LEU A CD2 
791  N  N   . LEU A 95  ? 0.5087 0.4845 0.8759 -0.0377 0.1171  -0.0366 1565 LEU A N   
792  C  CA  . LEU A 95  ? 0.4290 0.4013 0.7909 -0.0441 0.1106  -0.0449 1565 LEU A CA  
793  C  C   . LEU A 95  ? 0.5147 0.5014 0.8818 -0.0473 0.0999  -0.0443 1565 LEU A C   
794  O  O   . LEU A 95  ? 0.5378 0.5257 0.9090 -0.0545 0.0935  -0.0502 1565 LEU A O   
795  C  CB  . LEU A 95  ? 0.4395 0.4004 0.7799 -0.0416 0.1116  -0.0520 1565 LEU A CB  
796  C  CG  . LEU A 95  ? 0.5394 0.4856 0.8761 -0.0381 0.1204  -0.0546 1565 LEU A CG  
797  C  CD1 . LEU A 95  ? 0.5356 0.4744 0.8527 -0.0336 0.1220  -0.0623 1565 LEU A CD1 
798  C  CD2 . LEU A 95  ? 0.4690 0.4038 0.8142 -0.0443 0.1203  -0.0579 1565 LEU A CD2 
799  N  N   . ARG A 96  ? 0.5992 0.5962 0.9661 -0.0422 0.0969  -0.0373 1566 ARG A N   
800  C  CA  . ARG A 96  ? 0.5926 0.6031 0.9648 -0.0442 0.0851  -0.0365 1566 ARG A CA  
801  C  C   . ARG A 96  ? 0.5446 0.5684 0.9436 -0.0472 0.0829  -0.0351 1566 ARG A C   
802  O  O   . ARG A 96  ? 0.5130 0.5498 0.9210 -0.0502 0.0725  -0.0368 1566 ARG A O   
803  C  CB  . ARG A 96  ? 0.6052 0.6204 0.9673 -0.0377 0.0811  -0.0287 1566 ARG A CB  
804  C  CG  . ARG A 96  ? 0.6157 0.6360 0.9914 -0.0315 0.0841  -0.0192 1566 ARG A CG  
805  C  CD  . ARG A 96  ? 0.6251 0.6464 0.9883 -0.0262 0.0781  -0.0109 1566 ARG A CD  
806  N  NE  . ARG A 96  ? 0.4376 0.4485 0.7773 -0.0254 0.0842  -0.0092 1566 ARG A NE  
807  C  CZ  . ARG A 96  ? 0.4595 0.4646 0.7969 -0.0218 0.0926  -0.0033 1566 ARG A CZ  
808  N  NH1 . ARG A 96  ? 0.5342 0.5405 0.8896 -0.0182 0.0955  0.0014  1566 ARG A NH1 
809  N  NH2 . ARG A 96  ? 0.5266 0.5255 0.8443 -0.0222 0.0986  -0.0027 1566 ARG A NH2 
810  N  N   . HIS A 97  ? 0.4893 0.5114 0.9014 -0.0467 0.0924  -0.0328 1567 HIS A N   
811  C  CA  . HIS A 97  ? 0.3981 0.4347 0.8353 -0.0495 0.0924  -0.0319 1567 HIS A CA  
812  C  C   . HIS A 97  ? 0.5655 0.5985 1.0103 -0.0596 0.0962  -0.0374 1567 HIS A C   
813  O  O   . HIS A 97  ? 0.5144 0.5578 0.9789 -0.0629 0.1003  -0.0363 1567 HIS A O   
814  C  CB  . HIS A 97  ? 0.4416 0.4805 0.8880 -0.0420 0.1001  -0.0251 1567 HIS A CB  
815  C  CG  . HIS A 97  ? 0.5720 0.6139 1.0134 -0.0330 0.0952  -0.0189 1567 HIS A CG  
816  N  ND1 . HIS A 97  ? 0.4595 0.5158 0.9098 -0.0304 0.0840  -0.0172 1567 HIS A ND1 
817  C  CD2 . HIS A 97  ? 0.3960 0.4274 0.8237 -0.0267 0.0992  -0.0136 1567 HIS A CD2 
818  C  CE1 . HIS A 97  ? 0.3980 0.4501 0.8388 -0.0226 0.0812  -0.0105 1567 HIS A CE1 
819  N  NE2 . HIS A 97  ? 0.4677 0.5052 0.8951 -0.0210 0.0907  -0.0081 1567 HIS A NE2 
820  N  N   . THR A 98  ? 0.4202 0.4382 0.8493 -0.0651 0.0947  -0.0436 1568 THR A N   
821  C  CA  . THR A 98  ? 0.5565 0.5659 0.9899 -0.0755 0.0975  -0.0485 1568 THR A CA  
822  C  C   . THR A 98  ? 0.4384 0.4641 0.8905 -0.0859 0.0903  -0.0519 1568 THR A C   
823  O  O   . THR A 98  ? 0.6088 0.6280 1.0659 -0.0966 0.0927  -0.0551 1568 THR A O   
824  C  CB  . THR A 98  ? 0.4390 0.4260 0.8504 -0.0774 0.0966  -0.0552 1568 THR A CB  
825  O  OG1 . THR A 98  ? 0.4744 0.4642 0.8726 -0.0750 0.0873  -0.0591 1568 THR A OG1 
826  C  CG2 . THR A 98  ? 0.5179 0.4892 0.9165 -0.0696 0.1059  -0.0526 1568 THR A CG2 
827  N  N   . GLN A 99  ? 0.5292 0.5754 0.9919 -0.0838 0.0809  -0.0515 1569 GLN A N   
828  C  CA  . GLN A 99  ? 0.6932 0.7600 1.1805 -0.0930 0.0761  -0.0540 1569 GLN A CA  
829  C  C   . GLN A 99  ? 0.4781 0.5579 0.9875 -0.0936 0.0864  -0.0495 1569 GLN A C   
830  O  O   . GLN A 99  ? 0.4188 0.5161 0.9501 -0.1031 0.0858  -0.0518 1569 GLN A O   
831  C  CB  . GLN A 99  ? 0.7488 0.8360 1.2438 -0.0896 0.0623  -0.0549 1569 GLN A CB  
832  C  CG  . GLN A 99  ? 0.9164 1.0046 1.4089 -0.1003 0.0506  -0.0632 1569 GLN A CG  
833  C  CD  . GLN A 99  ? 1.0237 1.1217 1.5091 -0.0948 0.0356  -0.0643 1569 GLN A CD  
834  O  OE1 . GLN A 99  ? 0.9175 1.0206 1.3994 -0.0831 0.0337  -0.0580 1569 GLN A OE1 
835  N  NE2 . GLN A 99  ? 1.0806 1.1797 1.5626 -0.1038 0.0242  -0.0722 1569 GLN A NE2 
836  N  N   . LEU A 100 ? 0.4532 0.5254 0.9572 -0.0844 0.0960  -0.0437 1570 LEU A N   
837  C  CA  . LEU A 100 ? 0.4845 0.5674 1.0059 -0.0837 0.1063  -0.0400 1570 LEU A CA  
838  C  C   . LEU A 100 ? 0.5874 0.6492 1.0963 -0.0848 0.1187  -0.0373 1570 LEU A C   
839  O  O   . LEU A 100 ? 0.3745 0.4435 0.8942 -0.0836 0.1279  -0.0341 1570 LEU A O   
840  C  CB  . LEU A 100 ? 0.3728 0.4694 0.9027 -0.0701 0.1052  -0.0355 1570 LEU A CB  
841  C  CG  . LEU A 100 ? 0.4001 0.5213 0.9479 -0.0674 0.0932  -0.0372 1570 LEU A CG  
842  C  CD1 . LEU A 100 ? 0.3957 0.5180 0.9395 -0.0525 0.0887  -0.0321 1570 LEU A CD1 
843  C  CD2 . LEU A 100 ? 0.5352 0.6828 1.1135 -0.0733 0.0967  -0.0397 1570 LEU A CD2 
844  N  N   . LEU A 101 ? 0.5224 0.5589 1.0087 -0.0862 0.1188  -0.0390 1571 LEU A N   
845  C  CA  . LEU A 101 ? 0.4848 0.4987 0.9567 -0.0856 0.1282  -0.0367 1571 LEU A CA  
846  C  C   . LEU A 101 ? 0.5330 0.5271 0.9943 -0.0966 0.1269  -0.0411 1571 LEU A C   
847  O  O   . LEU A 101 ? 0.5676 0.5593 1.0242 -0.1007 0.1179  -0.0467 1571 LEU A O   
848  C  CB  . LEU A 101 ? 0.5208 0.5214 0.9745 -0.0733 0.1291  -0.0347 1571 LEU A CB  
849  C  CG  . LEU A 101 ? 0.5281 0.5429 0.9879 -0.0624 0.1283  -0.0304 1571 LEU A CG  
850  C  CD1 . LEU A 101 ? 0.5941 0.5955 1.0348 -0.0535 0.1285  -0.0290 1571 LEU A CD1 
851  C  CD2 . LEU A 101 ? 0.5810 0.6040 1.0542 -0.0604 0.1371  -0.0262 1571 LEU A CD2 
852  N  N   . PRO A 102 ? 0.5974 0.5752 1.0532 -0.1012 0.1349  -0.0386 1572 PRO A N   
853  C  CA  . PRO A 102 ? 0.4878 0.4405 0.9300 -0.1102 0.1327  -0.0424 1572 PRO A CA  
854  C  C   . PRO A 102 ? 0.5069 0.4424 0.9292 -0.1013 0.1273  -0.0472 1572 PRO A C   
855  O  O   . PRO A 102 ? 0.4961 0.4231 0.9075 -0.0901 0.1313  -0.0450 1572 PRO A O   
856  C  CB  . PRO A 102 ? 0.4440 0.3810 0.8807 -0.1125 0.1424  -0.0368 1572 PRO A CB  
857  C  CG  . PRO A 102 ? 0.4535 0.4118 0.9039 -0.1071 0.1503  -0.0311 1572 PRO A CG  
858  C  CD  . PRO A 102 ? 0.5712 0.5475 1.0275 -0.0960 0.1452  -0.0325 1572 PRO A CD  
859  N  N   . VAL A 103 ? 0.5503 0.4827 0.9683 -0.1065 0.1181  -0.0544 1573 VAL A N   
860  C  CA  . VAL A 103 ? 0.5879 0.5130 0.9893 -0.0971 0.1128  -0.0598 1573 VAL A CA  
861  C  C   . VAL A 103 ? 0.5032 0.3995 0.8850 -0.0922 0.1155  -0.0628 1573 VAL A C   
862  O  O   . VAL A 103 ? 0.5551 0.4474 0.9243 -0.0809 0.1162  -0.0649 1573 VAL A O   
863  C  CB  . VAL A 103 ? 0.5470 0.4782 0.9488 -0.1042 0.1015  -0.0673 1573 VAL A CB  
864  C  CG1 . VAL A 103 ? 0.5048 0.4170 0.9040 -0.1177 0.0980  -0.0728 1573 VAL A CG1 
865  C  CG2 . VAL A 103 ? 0.6662 0.5947 1.0503 -0.0947 0.0963  -0.0727 1573 VAL A CG2 
866  N  N   . ASP A 104 ? 0.5606 0.4373 0.9403 -0.1000 0.1176  -0.0623 1574 ASP A N   
867  C  CA  . ASP A 104 ? 0.6031 0.4517 0.9655 -0.0937 0.1195  -0.0646 1574 ASP A CA  
868  C  C   . ASP A 104 ? 0.4879 0.3393 0.8489 -0.0819 0.1275  -0.0582 1574 ASP A C   
869  O  O   . ASP A 104 ? 0.5579 0.4008 0.9072 -0.0705 0.1281  -0.0615 1574 ASP A O   
870  C  CB  . ASP A 104 ? 0.5772 0.4017 0.9365 -0.1055 0.1189  -0.0642 1574 ASP A CB  
871  C  CG  . ASP A 104 ? 0.7992 0.6346 1.1731 -0.1156 0.1253  -0.0549 1574 ASP A CG  
872  O  OD1 . ASP A 104 ? 0.6985 0.5629 1.0894 -0.1180 0.1267  -0.0523 1574 ASP A OD1 
873  O  OD2 . ASP A 104 ? 0.8058 0.6208 1.1738 -0.1208 0.1289  -0.0504 1574 ASP A OD2 
874  N  N   . LYS A 105 ? 0.5049 0.3693 0.8784 -0.0845 0.1339  -0.0497 1575 LYS A N   
875  C  CA  . LYS A 105 ? 0.6757 0.5450 1.0491 -0.0738 0.1407  -0.0440 1575 LYS A CA  
876  C  C   . LYS A 105 ? 0.5123 0.3957 0.8840 -0.0629 0.1395  -0.0458 1575 LYS A C   
877  O  O   . LYS A 105 ? 0.5016 0.3791 0.8649 -0.0528 0.1422  -0.0460 1575 LYS A O   
878  C  CB  . LYS A 105 ? 0.6981 0.5835 1.0862 -0.0783 0.1471  -0.0362 1575 LYS A CB  
879  C  CG  . LYS A 105 ? 0.6776 0.5644 1.0640 -0.0681 0.1538  -0.0307 1575 LYS A CG  
880  C  CD  . LYS A 105 ? 0.5293 0.4376 0.9312 -0.0693 0.1593  -0.0251 1575 LYS A CD  
881  C  CE  . LYS A 105 ? 0.4329 0.3628 0.8437 -0.0624 0.1565  -0.0257 1575 LYS A CE  
882  N  NZ  . LYS A 105 ? 0.4568 0.4053 0.8813 -0.0591 0.1614  -0.0210 1575 LYS A NZ  
883  N  N   . ALA A 106 ? 0.5955 0.4978 0.9750 -0.0653 0.1351  -0.0471 1576 ALA A N   
884  C  CA  . ALA A 106 ? 0.6289 0.5449 1.0061 -0.0563 0.1340  -0.0467 1576 ALA A CA  
885  C  C   . ALA A 106 ? 0.4542 0.3585 0.8143 -0.0497 0.1324  -0.0532 1576 ALA A C   
886  O  O   . ALA A 106 ? 0.4470 0.3550 0.8020 -0.0408 0.1359  -0.0516 1576 ALA A O   
887  C  CB  . ALA A 106 ? 0.4226 0.3581 0.8091 -0.0604 0.1275  -0.0470 1576 ALA A CB  
888  N  N   . PHE A 107 ? 0.5017 0.3924 0.8531 -0.0542 0.1271  -0.0613 1577 PHE A N   
889  C  CA  . PHE A 107 ? 0.5342 0.4143 0.8691 -0.0470 0.1258  -0.0695 1577 PHE A CA  
890  C  C   . PHE A 107 ? 0.5003 0.3638 0.8294 -0.0397 0.1310  -0.0700 1577 PHE A C   
891  O  O   . PHE A 107 ? 0.4999 0.3644 0.8211 -0.0300 0.1338  -0.0733 1577 PHE A O   
892  C  CB  . PHE A 107 ? 0.4919 0.3612 0.8184 -0.0532 0.1179  -0.0794 1577 PHE A CB  
893  C  CG  . PHE A 107 ? 0.5591 0.4454 0.8845 -0.0560 0.1116  -0.0817 1577 PHE A CG  
894  C  CD1 . PHE A 107 ? 0.5390 0.4311 0.8506 -0.0488 0.1110  -0.0863 1577 PHE A CD1 
895  C  CD2 . PHE A 107 ? 0.5098 0.4079 0.8482 -0.0659 0.1062  -0.0790 1577 PHE A CD2 
896  C  CE1 . PHE A 107 ? 0.5024 0.4088 0.8102 -0.0514 0.1043  -0.0875 1577 PHE A CE1 
897  C  CE2 . PHE A 107 ? 0.5903 0.5040 0.9276 -0.0677 0.0988  -0.0808 1577 PHE A CE2 
898  C  CZ  . PHE A 107 ? 0.5006 0.4172 0.8212 -0.0605 0.0974  -0.0847 1577 PHE A CZ  
899  N  N   . TYR A 108 ? 0.5264 0.3754 0.8593 -0.0441 0.1324  -0.0666 1578 TYR A N   
900  C  CA  . TYR A 108 ? 0.5969 0.4302 0.9243 -0.0364 0.1362  -0.0660 1578 TYR A CA  
901  C  C   . TYR A 108 ? 0.5046 0.3533 0.8361 -0.0273 0.1422  -0.0608 1578 TYR A C   
902  O  O   . TYR A 108 ? 0.4943 0.3402 0.8198 -0.0175 0.1441  -0.0645 1578 TYR A O   
903  C  CB  . TYR A 108 ? 0.4838 0.3017 0.8142 -0.0437 0.1371  -0.0603 1578 TYR A CB  
904  C  CG  . TYR A 108 ? 0.5061 0.3080 0.8306 -0.0358 0.1399  -0.0579 1578 TYR A CG  
905  C  CD1 . TYR A 108 ? 0.5757 0.3557 0.8884 -0.0287 0.1362  -0.0655 1578 TYR A CD1 
906  C  CD2 . TYR A 108 ? 0.5404 0.3488 0.8710 -0.0347 0.1456  -0.0489 1578 TYR A CD2 
907  C  CE1 . TYR A 108 ? 0.5114 0.2774 0.8196 -0.0205 0.1373  -0.0635 1578 TYR A CE1 
908  C  CE2 . TYR A 108 ? 0.5960 0.3897 0.9204 -0.0274 0.1468  -0.0468 1578 TYR A CE2 
909  C  CZ  . TYR A 108 ? 0.6169 0.3895 0.9305 -0.0202 0.1422  -0.0540 1578 TYR A CZ  
910  O  OH  . TYR A 108 ? 0.6719 0.4300 0.9798 -0.0119 0.1419  -0.0523 1578 TYR A OH  
911  N  N   . GLU A 109 ? 0.5595 0.4251 0.9023 -0.0307 0.1451  -0.0527 1579 GLU A N   
912  C  CA  . GLU A 109 ? 0.4409 0.3189 0.7883 -0.0236 0.1503  -0.0470 1579 GLU A CA  
913  C  C   . GLU A 109 ? 0.4152 0.3057 0.7580 -0.0176 0.1504  -0.0500 1579 GLU A C   
914  O  O   . GLU A 109 ? 0.4729 0.3662 0.8139 -0.0100 0.1543  -0.0497 1579 GLU A O   
915  C  CB  . GLU A 109 ? 0.4435 0.3350 0.8037 -0.0285 0.1525  -0.0389 1579 GLU A CB  
916  C  CG  . GLU A 109 ? 0.4396 0.3211 0.8030 -0.0324 0.1556  -0.0346 1579 GLU A CG  
917  C  CD  . GLU A 109 ? 0.4947 0.3912 0.8711 -0.0367 0.1587  -0.0282 1579 GLU A CD  
918  O  OE1 . GLU A 109 ? 0.5420 0.4559 0.9265 -0.0370 0.1569  -0.0274 1579 GLU A OE1 
919  O  OE2 . GLU A 109 ? 0.5280 0.4185 0.9058 -0.0392 0.1627  -0.0242 1579 GLU A OE2 
920  N  N   . ALA A 110 ? 0.4754 0.3744 0.8158 -0.0214 0.1462  -0.0528 1580 ALA A N   
921  C  CA  . ALA A 110 ? 0.4397 0.3493 0.7722 -0.0167 0.1465  -0.0555 1580 ALA A CA  
922  C  C   . ALA A 110 ? 0.4544 0.3546 0.7761 -0.0097 0.1484  -0.0643 1580 ALA A C   
923  O  O   . ALA A 110 ? 0.4867 0.3954 0.8057 -0.0034 0.1530  -0.0645 1580 ALA A O   
924  C  CB  . ALA A 110 ? 0.4288 0.3462 0.7577 -0.0223 0.1402  -0.0577 1580 ALA A CB  
925  N  N   . GLY A 111 ? 0.4790 0.3615 0.7952 -0.0107 0.1448  -0.0719 1581 GLY A N   
926  C  CA  . GLY A 111 ? 0.5718 0.4448 0.8782 -0.0026 0.1456  -0.0820 1581 GLY A CA  
927  C  C   . GLY A 111 ? 0.4577 0.3275 0.7684 0.0059  0.1503  -0.0803 1581 GLY A C   
928  O  O   . GLY A 111 ? 0.5823 0.4593 0.8900 0.0142  0.1539  -0.0854 1581 GLY A O   
929  N  N   . ILE A 112 ? 0.5647 0.4254 0.8826 0.0037  0.1504  -0.0732 1582 ILE A N   
930  C  CA  . ILE A 112 ? 0.4837 0.3409 0.8053 0.0114  0.1536  -0.0709 1582 ILE A CA  
931  C  C   . ILE A 112 ? 0.5721 0.4514 0.9001 0.0149  0.1592  -0.0663 1582 ILE A C   
932  O  O   . ILE A 112 ? 0.5200 0.4040 0.8490 0.0233  0.1620  -0.0696 1582 ILE A O   
933  C  CB  . ILE A 112 ? 0.6192 0.4625 0.9446 0.0066  0.1525  -0.0633 1582 ILE A CB  
934  C  CG1 . ILE A 112 ? 0.6777 0.4955 0.9952 0.0035  0.1470  -0.0679 1582 ILE A CG1 
935  C  CG2 . ILE A 112 ? 0.8501 0.6934 1.1795 0.0136  0.1553  -0.0591 1582 ILE A CG2 
936  C  CD1 . ILE A 112 ? 0.6409 0.4407 0.9524 0.0135  0.1447  -0.0734 1582 ILE A CD1 
937  N  N   . ALA A 113 ? 0.5286 0.4213 0.8615 0.0086  0.1605  -0.0586 1583 ALA A N   
938  C  CA  . ALA A 113 ? 0.4825 0.3929 0.8203 0.0108  0.1650  -0.0536 1583 ALA A CA  
939  C  C   . ALA A 113 ? 0.4116 0.3337 0.7428 0.0146  0.1676  -0.0599 1583 ALA A C   
940  O  O   . ALA A 113 ? 0.4390 0.3709 0.7732 0.0197  0.1721  -0.0604 1583 ALA A O   
941  C  CB  . ALA A 113 ? 0.3858 0.3056 0.7291 0.0039  0.1645  -0.0448 1583 ALA A CB  
942  N  N   . ALA A 114 ? 0.4789 0.4009 0.8009 0.0117  0.1649  -0.0652 1584 ALA A N   
943  C  CA  . ALA A 114 ? 0.5535 0.4862 0.8662 0.0150  0.1678  -0.0724 1584 ALA A CA  
944  C  C   . ALA A 114 ? 0.6150 0.5449 0.9278 0.0246  0.1708  -0.0817 1584 ALA A C   
945  O  O   . ALA A 114 ? 0.4585 0.4039 0.7721 0.0288  0.1767  -0.0838 1584 ALA A O   
946  C  CB  . ALA A 114 ? 0.4418 0.3707 0.7427 0.0109  0.1630  -0.0784 1584 ALA A CB  
947  N  N   . LYS A 115 ? 0.6966 0.6070 1.0091 0.0282  0.1665  -0.0873 1585 LYS A N   
948  C  CA  . LYS A 115 ? 0.6950 0.6007 1.0079 0.0391  0.1677  -0.0970 1585 LYS A CA  
949  C  C   . LYS A 115 ? 0.6118 0.5286 0.9365 0.0441  0.1719  -0.0922 1585 LYS A C   
950  O  O   . LYS A 115 ? 0.6133 0.5426 0.9409 0.0519  0.1762  -0.0990 1585 LYS A O   
951  C  CB  . LYS A 115 ? 0.6333 0.5117 0.9429 0.0414  0.1608  -0.1016 1585 LYS A CB  
952  C  CG  . LYS A 115 ? 0.5553 0.4256 0.8649 0.0543  0.1599  -0.1125 1585 LYS A CG  
953  C  CD  . LYS A 115 ? 0.9427 0.7852 1.2523 0.0561  0.1532  -0.1105 1585 LYS A CD  
954  C  CE  . LYS A 115 ? 1.0758 0.9095 1.3868 0.0708  0.1509  -0.1201 1585 LYS A CE  
955  N  NZ  . LYS A 115 ? 1.0790 0.8829 1.3876 0.0721  0.1434  -0.1163 1585 LYS A NZ  
956  N  N   . ALA A 116 ? 0.6468 0.5603 0.9787 0.0395  0.1710  -0.0812 1586 ALA A N   
957  C  CA  . ALA A 116 ? 0.6044 0.5262 0.9469 0.0436  0.1737  -0.0769 1586 ALA A CA  
958  C  C   . ALA A 116 ? 0.6398 0.5866 0.9870 0.0419  0.1803  -0.0743 1586 ALA A C   
959  O  O   . ALA A 116 ? 0.5446 0.5020 0.9009 0.0465  0.1831  -0.0746 1586 ALA A O   
960  C  CB  . ALA A 116 ? 0.4617 0.3736 0.8089 0.0389  0.1712  -0.0665 1586 ALA A CB  
961  N  N   . VAL A 117 ? 0.6011 0.5572 0.9421 0.0346  0.1823  -0.0711 1587 VAL A N   
962  C  CA  . VAL A 117 ? 0.5667 0.5446 0.9092 0.0324  0.1888  -0.0688 1587 VAL A CA  
963  C  C   . VAL A 117 ? 0.6190 0.6083 0.9535 0.0359  0.1931  -0.0794 1587 VAL A C   
964  O  O   . VAL A 117 ? 0.5867 0.5941 0.9185 0.0320  0.1991  -0.0773 1587 VAL A O   
965  C  CB  . VAL A 117 ? 0.5484 0.5307 0.8881 0.0227  0.1887  -0.0577 1587 VAL A CB  
966  C  CG1 . VAL A 117 ? 0.6900 0.6641 1.0388 0.0202  0.1857  -0.0484 1587 VAL A CG1 
967  C  CG2 . VAL A 117 ? 0.4864 0.4627 0.8140 0.0186  0.1849  -0.0593 1587 VAL A CG2 
968  N  N   . GLY A 118 ? 0.6907 0.6689 1.0202 0.0429  0.1903  -0.0907 1588 GLY A N   
969  C  CA  . GLY A 118 ? 0.6085 0.5973 0.9302 0.0480  0.1946  -0.1030 1588 GLY A CA  
970  C  C   . GLY A 118 ? 0.6818 0.6718 0.9869 0.0417  0.1945  -0.1046 1588 GLY A C   
971  O  O   . GLY A 118 ? 0.6454 0.6491 0.9421 0.0441  0.2000  -0.1132 1588 GLY A O   
972  N  N   . TRP A 119 ? 0.5713 0.5485 0.8713 0.0340  0.1882  -0.0972 1589 TRP A N   
973  C  CA  . TRP A 119 ? 0.6239 0.6011 0.9080 0.0283  0.1858  -0.0991 1589 TRP A CA  
974  C  C   . TRP A 119 ? 0.7644 0.7224 1.0412 0.0320  0.1794  -0.1108 1589 TRP A C   
975  O  O   . TRP A 119 ? 0.7137 0.6559 0.9896 0.0270  0.1718  -0.1080 1589 TRP A O   
976  C  CB  . TRP A 119 ? 0.6297 0.6057 0.9140 0.0184  0.1816  -0.0854 1589 TRP A CB  
977  C  CG  . TRP A 119 ? 0.6070 0.5983 0.8967 0.0144  0.1868  -0.0738 1589 TRP A CG  
978  C  CD1 . TRP A 119 ? 0.7908 0.7992 1.0815 0.0160  0.1953  -0.0745 1589 TRP A CD1 
979  C  CD2 . TRP A 119 ? 0.7689 0.7591 1.0638 0.0077  0.1836  -0.0603 1589 TRP A CD2 
980  N  NE1 . TRP A 119 ? 0.7232 0.7392 1.0186 0.0097  0.1971  -0.0616 1589 TRP A NE1 
981  C  CE2 . TRP A 119 ? 0.7270 0.7311 1.0247 0.0054  0.1897  -0.0531 1589 TRP A CE2 
982  C  CE3 . TRP A 119 ? 0.6257 0.6052 0.9242 0.0036  0.1761  -0.0542 1589 TRP A CE3 
983  C  CZ2 . TRP A 119 ? 0.6166 0.6208 0.9190 -0.0002 0.1878  -0.0401 1589 TRP A CZ2 
984  C  CZ3 . TRP A 119 ? 0.6258 0.6083 0.9302 -0.0008 0.1748  -0.0419 1589 TRP A CZ3 
985  C  CH2 . TRP A 119 ? 0.5786 0.5717 0.8841 -0.0024 0.1802  -0.0351 1589 TRP A CH2 
986  N  N   . ASP A 120 ? 0.7429 0.7029 1.0142 0.0407  0.1825  -0.1248 1590 ASP A N   
987  C  CA  . ASP A 120 ? 0.5135 0.4514 0.7808 0.0465  0.1760  -0.1366 1590 ASP A CA  
988  C  C   . ASP A 120 ? 0.6049 0.5334 0.8559 0.0409  0.1701  -0.1425 1590 ASP A C   
989  O  O   . ASP A 120 ? 0.6437 0.5494 0.8928 0.0400  0.1620  -0.1465 1590 ASP A O   
990  C  CB  . ASP A 120 ? 0.7650 0.7074 1.0346 0.0599  0.1806  -0.1506 1590 ASP A CB  
991  C  CG  . ASP A 120 ? 0.7315 0.6765 1.0189 0.0663  0.1826  -0.1460 1590 ASP A CG  
992  O  OD1 . ASP A 120 ? 0.7794 0.7198 1.0754 0.0601  0.1803  -0.1325 1590 ASP A OD1 
993  O  OD2 . ASP A 120 ? 0.8983 0.8500 1.1912 0.0779  0.1860  -0.1564 1590 ASP A OD2 
994  N  N   . ASN A 121 ? 0.6175 0.5623 0.8556 0.0365  0.1733  -0.1429 1591 ASN A N   
995  C  CA  . ASN A 121 ? 0.6072 0.5438 0.8297 0.0301  0.1660  -0.1470 1591 ASN A CA  
996  C  C   . ASN A 121 ? 0.8433 0.7689 1.0728 0.0202  0.1576  -0.1354 1591 ASN A C   
997  O  O   . ASN A 121 ? 0.9192 0.8268 1.1458 0.0169  0.1491  -0.1403 1591 ASN A O   
998  C  CB  . ASN A 121 ? 0.5884 0.5452 0.7947 0.0263  0.1707  -0.1464 1591 ASN A CB  
999  C  CG  . ASN A 121 ? 0.9495 0.9185 1.1460 0.0350  0.1793  -0.1604 1591 ASN A CG  
1000 O  OD1 . ASN A 121 ? 0.8984 0.8577 1.0980 0.0449  0.1795  -0.1737 1591 ASN A OD1 
1001 N  ND2 . ASN A 121 ? 1.0901 1.0804 1.2744 0.0316  0.1866  -0.1577 1591 ASN A ND2 
1002 N  N   . MET A 122 ? 0.7293 0.6663 0.9683 0.0151  0.1598  -0.1203 1592 MET A N   
1003 C  CA  . MET A 122 ? 0.7250 0.6547 0.9736 0.0070  0.1529  -0.1098 1592 MET A CA  
1004 C  C   . MET A 122 ? 0.5072 0.4174 0.7673 0.0085  0.1497  -0.1110 1592 MET A C   
1005 O  O   . MET A 122 ? 0.5543 0.4524 0.8168 0.0019  0.1425  -0.1100 1592 MET A O   
1006 C  CB  . MET A 122 ? 0.6179 0.5623 0.8753 0.0035  0.1564  -0.0948 1592 MET A CB  
1007 C  CG  . MET A 122 ? 0.8523 0.8110 1.0967 -0.0011 0.1560  -0.0904 1592 MET A CG  
1008 S  SD  . MET A 122 ? 0.9007 0.8691 1.1557 -0.0065 0.1555  -0.0721 1592 MET A SD  
1009 C  CE  . MET A 122 ? 0.6360 0.6144 0.8972 -0.0013 0.1671  -0.0693 1592 MET A CE  
1010 N  N   . ALA A 123 ? 0.5017 0.4089 0.7690 0.0166  0.1549  -0.1127 1593 ALA A N   
1011 C  CA  . ALA A 123 ? 0.5389 0.4253 0.8141 0.0183  0.1514  -0.1132 1593 ALA A CA  
1012 C  C   . ALA A 123 ? 0.6686 0.5340 0.9341 0.0177  0.1442  -0.1248 1593 ALA A C   
1013 O  O   . ALA A 123 ? 0.7175 0.5659 0.9862 0.0110  0.1382  -0.1220 1593 ALA A O   
1014 C  CB  . ALA A 123 ? 0.4971 0.3839 0.7795 0.0286  0.1566  -0.1147 1593 ALA A CB  
1015 N  N   . PHE A 124 ? 0.6312 0.4976 0.8841 0.0238  0.1448  -0.1381 1594 PHE A N   
1016 C  CA  . PHE A 124 ? 0.6527 0.4973 0.8950 0.0240  0.1375  -0.1508 1594 PHE A CA  
1017 C  C   . PHE A 124 ? 0.6077 0.4485 0.8458 0.0112  0.1298  -0.1483 1594 PHE A C   
1018 O  O   . PHE A 124 ? 0.7295 0.5488 0.9681 0.0055  0.1224  -0.1505 1594 PHE A O   
1019 C  CB  . PHE A 124 ? 0.7065 0.5564 0.9354 0.0337  0.1405  -0.1666 1594 PHE A CB  
1020 C  CG  . PHE A 124 ? 0.6268 0.4520 0.8436 0.0355  0.1326  -0.1818 1594 PHE A CG  
1021 C  CD1 . PHE A 124 ? 0.6433 0.4435 0.8625 0.0436  0.1291  -0.1888 1594 PHE A CD1 
1022 C  CD2 . PHE A 124 ? 0.6444 0.4697 0.8466 0.0292  0.1275  -0.1891 1594 PHE A CD2 
1023 C  CE1 . PHE A 124 ? 0.6740 0.4483 0.8815 0.0455  0.1210  -0.2032 1594 PHE A CE1 
1024 C  CE2 . PHE A 124 ? 0.7309 0.5316 0.9215 0.0305  0.1194  -0.2041 1594 PHE A CE2 
1025 C  CZ  . PHE A 124 ? 0.7939 0.5683 0.9873 0.0386  0.1163  -0.2112 1594 PHE A CZ  
1026 N  N   . ILE A 125 ? 0.6731 0.5348 0.9074 0.0061  0.1309  -0.1436 1595 ILE A N   
1027 C  CA  . ILE A 125 ? 0.6357 0.4970 0.8667 -0.0052 0.1225  -0.1420 1595 ILE A CA  
1028 C  C   . ILE A 125 ? 0.6587 0.5148 0.9063 -0.0141 0.1192  -0.1302 1595 ILE A C   
1029 O  O   . ILE A 125 ? 0.7574 0.6000 1.0066 -0.0225 0.1114  -0.1327 1595 ILE A O   
1030 C  CB  . ILE A 125 ? 0.7025 0.5872 0.9248 -0.0073 0.1240  -0.1382 1595 ILE A CB  
1031 C  CG1 . ILE A 125 ? 0.7319 0.6191 0.9337 -0.0012 0.1257  -0.1524 1595 ILE A CG1 
1032 C  CG2 . ILE A 125 ? 0.6687 0.5576 0.8936 -0.0184 0.1152  -0.1322 1595 ILE A CG2 
1033 C  CD1 . ILE A 125 ? 0.7260 0.6367 0.9179 -0.0007 0.1314  -0.1474 1595 ILE A CD1 
1034 N  N   . PHE A 126 ? 0.6426 0.5097 0.9032 -0.0128 0.1253  -0.1179 1596 PHE A N   
1035 C  CA  . PHE A 126 ? 0.5917 0.4570 0.8678 -0.0207 0.1236  -0.1071 1596 PHE A CA  
1036 C  C   . PHE A 126 ? 0.5884 0.4291 0.8677 -0.0222 0.1216  -0.1096 1596 PHE A C   
1037 O  O   . PHE A 126 ? 0.6656 0.4992 0.9517 -0.0323 0.1170  -0.1063 1596 PHE A O   
1038 C  CB  . PHE A 126 ? 0.5363 0.4171 0.8236 -0.0177 0.1307  -0.0947 1596 PHE A CB  
1039 C  CG  . PHE A 126 ? 0.5715 0.4740 0.8560 -0.0176 0.1320  -0.0896 1596 PHE A CG  
1040 C  CD1 . PHE A 126 ? 0.5510 0.4603 0.8279 -0.0230 0.1254  -0.0920 1596 PHE A CD1 
1041 C  CD2 . PHE A 126 ? 0.6019 0.5166 0.8908 -0.0127 0.1392  -0.0820 1596 PHE A CD2 
1042 C  CE1 . PHE A 126 ? 0.6398 0.5665 0.9119 -0.0229 0.1257  -0.0861 1596 PHE A CE1 
1043 C  CE2 . PHE A 126 ? 0.6375 0.5691 0.9223 -0.0134 0.1400  -0.0761 1596 PHE A CE2 
1044 C  CZ  . PHE A 126 ? 0.5924 0.5292 0.8680 -0.0183 0.1332  -0.0778 1596 PHE A CZ  
1045 N  N   . LEU A 127 ? 0.5764 0.4040 0.8509 -0.0124 0.1247  -0.1152 1597 LEU A N   
1046 C  CA  . LEU A 127 ? 0.7320 0.5334 1.0078 -0.0134 0.1219  -0.1160 1597 LEU A CA  
1047 C  C   . LEU A 127 ? 0.7470 0.5265 1.0127 -0.0185 0.1134  -0.1270 1597 LEU A C   
1048 O  O   . LEU A 127 ? 0.7010 0.4601 0.9690 -0.0266 0.1091  -0.1247 1597 LEU A O   
1049 C  CB  . LEU A 127 ? 0.5772 0.3716 0.8523 -0.0003 0.1265  -0.1179 1597 LEU A CB  
1050 C  CG  . LEU A 127 ? 0.6658 0.4774 0.9523 0.0030  0.1338  -0.1062 1597 LEU A CG  
1051 C  CD1 . LEU A 127 ? 0.5255 0.3349 0.8119 0.0166  0.1376  -0.1099 1597 LEU A CD1 
1052 C  CD2 . LEU A 127 ? 0.5529 0.3591 0.8488 -0.0061 0.1337  -0.0943 1597 LEU A CD2 
1053 N  N   . ASN A 128 ? 0.7137 0.4968 0.9674 -0.0152 0.1108  -0.1388 1598 ASN A N   
1054 C  CA  . ASN A 128 ? 0.6702 0.4339 0.9141 -0.0214 0.1016  -0.1498 1598 ASN A CA  
1055 C  C   . ASN A 128 ? 0.7389 0.5081 0.9908 -0.0375 0.0962  -0.1432 1598 ASN A C   
1056 O  O   . ASN A 128 ? 0.8113 0.5600 1.0642 -0.0473 0.0898  -0.1446 1598 ASN A O   
1057 C  CB  . ASN A 128 ? 0.7603 0.5305 0.9885 -0.0143 0.1006  -0.1638 1598 ASN A CB  
1058 C  CG  . ASN A 128 ? 0.8367 0.5783 1.0517 -0.0122 0.0931  -0.1797 1598 ASN A CG  
1059 O  OD1 . ASN A 128 ? 0.9979 0.7144 1.2130 -0.0076 0.0917  -0.1821 1598 ASN A OD1 
1060 N  ND2 . ASN A 128 ? 0.9281 0.6717 1.1303 -0.0154 0.0874  -0.1907 1598 ASN A ND2 
1061 N  N   . ARG A 129 ? 0.8243 0.6215 1.0828 -0.0405 0.0983  -0.1357 1599 ARG A N   
1062 C  CA  . ARG A 129 ? 0.7596 0.5665 1.0294 -0.0543 0.0933  -0.1291 1599 ARG A CA  
1063 C  C   . ARG A 129 ? 0.8267 0.6248 1.1110 -0.0619 0.0955  -0.1192 1599 ARG A C   
1064 O  O   . ARG A 129 ? 0.6594 0.4513 0.9502 -0.0750 0.0900  -0.1186 1599 ARG A O   
1065 C  CB  . ARG A 129 ? 0.7356 0.5729 1.0109 -0.0535 0.0955  -0.1214 1599 ARG A CB  
1066 C  CG  . ARG A 129 ? 0.6692 0.5209 0.9604 -0.0652 0.0911  -0.1137 1599 ARG A CG  
1067 C  CD  . ARG A 129 ? 0.7481 0.5912 1.0371 -0.0767 0.0803  -0.1222 1599 ARG A CD  
1068 N  NE  . ARG A 129 ? 0.9092 0.7763 1.2079 -0.0834 0.0743  -0.1182 1599 ARG A NE  
1069 C  CZ  . ARG A 129 ? 0.9716 0.8465 1.2595 -0.0842 0.0660  -0.1251 1599 ARG A CZ  
1070 N  NH1 . ARG A 129 ? 0.9491 0.8100 1.2156 -0.0793 0.0636  -0.1373 1599 ARG A NH1 
1071 N  NH2 . ARG A 129 ? 0.9478 0.8449 1.2461 -0.0893 0.0597  -0.1204 1599 ARG A NH2 
1072 N  N   . PHE A 130 ? 0.6621 0.4603 0.9511 -0.0546 0.1036  -0.1114 1600 PHE A N   
1073 C  CA  . PHE A 130 ? 0.6354 0.4236 0.9345 -0.0608 0.1064  -0.1021 1600 PHE A CA  
1074 C  C   . PHE A 130 ? 0.7550 0.5107 1.0467 -0.0673 0.1008  -0.1075 1600 PHE A C   
1075 O  O   . PHE A 130 ? 0.6904 0.4395 0.9897 -0.0808 0.0992  -0.1021 1600 PHE A O   
1076 C  CB  . PHE A 130 ? 0.5491 0.3401 0.8502 -0.0498 0.1148  -0.0953 1600 PHE A CB  
1077 C  CG  . PHE A 130 ? 0.7471 0.5174 1.0495 -0.0521 0.1167  -0.0893 1600 PHE A CG  
1078 C  CD1 . PHE A 130 ? 0.5469 0.3219 0.8607 -0.0633 0.1192  -0.0792 1600 PHE A CD1 
1079 C  CD2 . PHE A 130 ? 0.5799 0.3262 0.8716 -0.0426 0.1161  -0.0940 1600 PHE A CD2 
1080 C  CE1 . PHE A 130 ? 0.6042 0.3592 0.9161 -0.0662 0.1214  -0.0729 1600 PHE A CE1 
1081 C  CE2 . PHE A 130 ? 0.5801 0.3054 0.8705 -0.0445 0.1168  -0.0875 1600 PHE A CE2 
1082 C  CZ  . PHE A 130 ? 0.5807 0.3097 0.8800 -0.0570 0.1197  -0.0765 1600 PHE A CZ  
1083 N  N   . LEU A 131 ? 0.6177 0.3522 0.8949 -0.0578 0.0981  -0.1179 1601 LEU A N   
1084 C  CA  . LEU A 131 ? 0.6557 0.3550 0.9241 -0.0631 0.0914  -0.1237 1601 LEU A CA  
1085 C  C   . LEU A 131 ? 0.8255 0.5218 1.0951 -0.0790 0.0832  -0.1282 1601 LEU A C   
1086 O  O   . LEU A 131 ? 0.7244 0.4016 0.9963 -0.0924 0.0796  -0.1249 1601 LEU A O   
1087 C  CB  . LEU A 131 ? 0.6718 0.3516 0.9248 -0.0483 0.0888  -0.1368 1601 LEU A CB  
1088 C  CG  . LEU A 131 ? 0.7059 0.3844 0.9583 -0.0324 0.0951  -0.1342 1601 LEU A CG  
1089 C  CD1 . LEU A 131 ? 0.8538 0.5173 1.0931 -0.0174 0.0921  -0.1495 1601 LEU A CD1 
1090 C  CD2 . LEU A 131 ? 0.6643 0.3232 0.9198 -0.0360 0.0961  -0.1230 1601 LEU A CD2 
1091 N  N   . ASP A 132 ? 0.8212 0.5364 1.0887 -0.0783 0.0799  -0.1355 1602 ASP A N   
1092 C  CA  . ASP A 132 ? 0.7302 0.4459 0.9997 -0.0931 0.0710  -0.1405 1602 ASP A CA  
1093 C  C   . ASP A 132 ? 0.8117 0.5434 1.1008 -0.1082 0.0728  -0.1281 1602 ASP A C   
1094 O  O   . ASP A 132 ? 0.7110 0.4322 1.0048 -0.1239 0.0669  -0.1290 1602 ASP A O   
1095 C  CB  . ASP A 132 ? 0.7164 0.4527 0.9792 -0.0885 0.0674  -0.1491 1602 ASP A CB  
1096 C  CG  . ASP A 132 ? 0.9311 0.6509 1.1734 -0.0757 0.0652  -0.1640 1602 ASP A CG  
1097 O  OD1 . ASP A 132 ? 0.8694 0.5615 1.1044 -0.0692 0.0659  -0.1680 1602 ASP A OD1 
1098 O  OD2 . ASP A 132 ? 0.9554 0.6900 1.1883 -0.0717 0.0627  -0.1719 1602 ASP A OD2 
1099 N  N   . LEU A 133 ? 0.8460 0.6029 1.1473 -0.1039 0.0812  -0.1169 1603 LEU A N   
1100 C  CA  . LEU A 133 ? 0.8173 0.5921 1.1381 -0.1169 0.0836  -0.1065 1603 LEU A CA  
1101 C  C   . LEU A 133 ? 0.6931 0.4465 1.0166 -0.1259 0.0872  -0.0993 1603 LEU A C   
1102 O  O   . LEU A 133 ? 0.7188 0.4780 1.0551 -0.1418 0.0866  -0.0948 1603 LEU A O   
1103 C  CB  . LEU A 133 ? 0.6774 0.4841 1.0099 -0.1091 0.0910  -0.0975 1603 LEU A CB  
1104 C  CG  . LEU A 133 ? 0.7236 0.5531 1.0540 -0.1026 0.0870  -0.1019 1603 LEU A CG  
1105 C  CD1 . LEU A 133 ? 0.7091 0.5564 1.0411 -0.0894 0.0948  -0.0949 1603 LEU A CD1 
1106 C  CD2 . LEU A 133 ? 0.7110 0.5617 1.0564 -0.1149 0.0800  -0.1017 1603 LEU A CD2 
1107 N  N   . THR A 134 ? 0.7022 0.4317 1.0137 -0.1166 0.0909  -0.0980 1604 THR A N   
1108 C  CA  . THR A 134 ? 0.7343 0.4387 1.0440 -0.1259 0.0927  -0.0910 1604 THR A CA  
1109 C  C   . THR A 134 ? 0.8095 0.4865 1.1125 -0.1399 0.0833  -0.0979 1604 THR A C   
1110 O  O   . THR A 134 ? 0.7959 0.4654 1.1052 -0.1570 0.0836  -0.0914 1604 THR A O   
1111 C  CB  . THR A 134 ? 0.6542 0.3375 0.9514 -0.1116 0.0965  -0.0887 1604 THR A CB  
1112 O  OG1 . THR A 134 ? 0.6758 0.3368 0.9572 -0.1009 0.0898  -0.1012 1604 THR A OG1 
1113 C  CG2 . THR A 134 ? 0.6199 0.3302 0.9241 -0.0989 0.1049  -0.0827 1604 THR A CG2 
1114 N  N   . ASP A 135 ? 0.8394 0.5014 1.1294 -0.1337 0.0750  -0.1114 1605 ASP A N   
1115 C  CA  . ASP A 135 ? 1.0117 0.6470 1.2952 -0.1476 0.0649  -0.1191 1605 ASP A CA  
1116 C  C   . ASP A 135 ? 0.9759 0.6352 1.2764 -0.1662 0.0619  -0.1179 1605 ASP A C   
1117 O  O   . ASP A 135 ? 0.9695 0.6133 1.2732 -0.1846 0.0578  -0.1165 1605 ASP A O   
1118 C  CB  . ASP A 135 ? 1.0186 0.6356 1.2847 -0.1365 0.0565  -0.1357 1605 ASP A CB  
1119 C  CG  . ASP A 135 ? 1.1516 0.7449 1.4029 -0.1179 0.0587  -0.1386 1605 ASP A CG  
1120 O  OD1 . ASP A 135 ? 1.2376 0.8206 1.4898 -0.1161 0.0644  -0.1276 1605 ASP A OD1 
1121 O  OD2 . ASP A 135 ? 1.1905 0.7767 1.4293 -0.1049 0.0546  -0.1523 1605 ASP A OD2 
1122 N  N   . ALA A 136 ? 0.8396 0.5366 1.1512 -0.1619 0.0631  -0.1187 1606 ALA A N   
1123 C  CA  . ALA A 136 ? 0.8612 0.5837 1.1908 -0.1779 0.0588  -0.1183 1606 ALA A CA  
1124 C  C   . ALA A 136 ? 0.6940 0.4306 1.0430 -0.1916 0.0667  -0.1050 1606 ALA A C   
1125 O  O   . ALA A 136 ? 0.7040 0.4483 1.0665 -0.2103 0.0630  -0.1047 1606 ALA A O   
1126 C  CB  . ALA A 136 ? 0.7988 0.5566 1.1343 -0.1684 0.0574  -0.1213 1606 ALA A CB  
1127 N  N   . ILE A 137 ? 0.6734 0.4149 1.0240 -0.1829 0.0777  -0.0945 1607 ILE A N   
1128 C  CA  . ILE A 137 ? 0.6665 0.4170 1.0314 -0.1955 0.0863  -0.0824 1607 ILE A CA  
1129 C  C   . ILE A 137 ? 0.8533 0.5688 1.2101 -0.2124 0.0836  -0.0809 1607 ILE A C   
1130 O  O   . ILE A 137 ? 0.9825 0.7070 1.3535 -0.2322 0.0848  -0.0765 1607 ILE A O   
1131 C  CB  . ILE A 137 ? 0.6901 0.4471 1.0536 -0.1817 0.0977  -0.0726 1607 ILE A CB  
1132 C  CG1 . ILE A 137 ? 0.6399 0.4364 1.0176 -0.1710 0.1012  -0.0714 1607 ILE A CG1 
1133 C  CG2 . ILE A 137 ? 0.7668 0.5210 1.1364 -0.1943 0.1066  -0.0608 1607 ILE A CG2 
1134 C  CD1 . ILE A 137 ? 0.5850 0.3841 0.9571 -0.1539 0.1096  -0.0655 1607 ILE A CD1 
1135 N  N   A GLU A 138 ? 0.8573 0.5323 1.1913 -0.2050 0.0796  -0.0848 1608 GLU A N   
1136 N  N   B GLU A 138 ? 0.8575 0.5326 1.1915 -0.2050 0.0796  -0.0848 1608 GLU A N   
1137 C  CA  A GLU A 138 ? 0.9029 0.5390 1.2264 -0.2205 0.0757  -0.0828 1608 GLU A CA  
1138 C  CA  B GLU A 138 ? 0.9008 0.5363 1.2238 -0.2202 0.0755  -0.0831 1608 GLU A CA  
1139 C  C   A GLU A 138 ? 0.8906 0.5231 1.2198 -0.2391 0.0653  -0.0913 1608 GLU A C   
1140 C  C   B GLU A 138 ? 0.8893 0.5220 1.2186 -0.2391 0.0653  -0.0913 1608 GLU A C   
1141 O  O   A GLU A 138 ? 0.9049 0.5246 1.2381 -0.2605 0.0649  -0.0861 1608 GLU A O   
1142 O  O   B GLU A 138 ? 0.9039 0.5245 1.2374 -0.2604 0.0651  -0.0860 1608 GLU A O   
1143 C  CB  A GLU A 138 ? 0.9584 0.5513 1.2567 -0.2061 0.0716  -0.0867 1608 GLU A CB  
1144 C  CB  B GLU A 138 ? 0.9504 0.5432 1.2483 -0.2054 0.0710  -0.0878 1608 GLU A CB  
1145 C  CG  A GLU A 138 ? 0.9083 0.4904 1.1994 -0.1984 0.0807  -0.0743 1608 GLU A CG  
1146 C  CG  B GLU A 138 ? 0.8861 0.4730 1.1769 -0.1923 0.0800  -0.0774 1608 GLU A CG  
1147 C  CD  A GLU A 138 ? 0.9354 0.5296 1.2364 -0.2167 0.0891  -0.0599 1608 GLU A CD  
1148 C  CD  B GLU A 138 ? 0.8955 0.4436 1.1640 -0.1756 0.0747  -0.0829 1608 GLU A CD  
1149 O  OE1 A GLU A 138 ? 0.8549 0.4325 1.1476 -0.2343 0.0836  -0.0558 1608 GLU A OE1 
1150 O  OE1 B GLU A 138 ? 0.8864 0.4069 1.1435 -0.1756 0.0642  -0.0945 1608 GLU A OE1 
1151 O  OE2 A GLU A 138 ? 0.7496 0.3737 1.0630 -0.2119 0.0999  -0.0522 1608 GLU A OE2 
1152 O  OE2 B GLU A 138 ? 0.7885 0.3342 1.0515 -0.1620 0.0807  -0.0762 1608 GLU A OE2 
1153 N  N   . GLU A 139 ? 0.8300 0.4744 1.1595 -0.2323 0.0568  -0.1041 1609 GLU A N   
1154 C  CA  . GLU A 139 ? 0.8107 0.4532 1.1451 -0.2487 0.0454  -0.1138 1609 GLU A CA  
1155 C  C   . GLU A 139 ? 0.8648 0.5509 1.2274 -0.2642 0.0470  -0.1101 1609 GLU A C   
1156 O  O   . GLU A 139 ? 1.0504 0.7355 1.4212 -0.2834 0.0388  -0.1151 1609 GLU A O   
1157 C  CB  . GLU A 139 ? 0.8795 0.5175 1.2004 -0.2346 0.0353  -0.1298 1609 GLU A CB  
1158 C  CG  . GLU A 139 ? 1.0043 0.5945 1.2981 -0.2236 0.0297  -0.1385 1609 GLU A CG  
1159 C  CD  . GLU A 139 ? 1.0732 0.6254 1.3579 -0.2407 0.0177  -0.1468 1609 GLU A CD  
1160 O  OE1 . GLU A 139 ? 1.1663 0.6829 1.4429 -0.2489 0.0184  -0.1401 1609 GLU A OE1 
1161 O  OE2 . GLU A 139 ? 0.9108 0.4673 1.1952 -0.2460 0.0070  -0.1597 1609 GLU A OE2 
1162 N  N   . GLY A 140 ? 1.0797 0.8046 1.4583 -0.2561 0.0565  -0.1023 1610 GLY A N   
1163 C  CA  . GLY A 140 ? 1.0361 0.8040 1.4434 -0.2686 0.0579  -0.0994 1610 GLY A CA  
1164 C  C   . GLY A 140 ? 1.0686 0.8649 1.4849 -0.2639 0.0478  -0.1095 1610 GLY A C   
1165 O  O   . GLY A 140 ? 0.9898 0.8226 1.4314 -0.2740 0.0467  -0.1084 1610 GLY A O   
1166 N  N   . THR A 141 ? 1.1050 0.8869 1.5012 -0.2488 0.0402  -0.1195 1611 THR A N   
1167 C  CA  . THR A 141 ? 1.0301 0.8382 1.4305 -0.2427 0.0308  -0.1281 1611 THR A CA  
1168 C  C   . THR A 141 ? 1.0371 0.8449 1.4197 -0.2186 0.0330  -0.1303 1611 THR A C   
1169 O  O   . THR A 141 ? 0.9554 0.7367 1.3193 -0.2070 0.0385  -0.1297 1611 THR A O   
1170 C  CB  . THR A 141 ? 1.1061 0.8993 1.4994 -0.2542 0.0154  -0.1418 1611 THR A CB  
1171 O  OG1 . THR A 141 ? 1.1073 0.9278 1.5029 -0.2467 0.0065  -0.1490 1611 THR A OG1 
1172 C  CG2 . THR A 141 ? 1.1410 0.8870 1.5042 -0.2476 0.0117  -0.1505 1611 THR A CG2 
1173 N  N   . LEU A 142 ? 0.9787 0.8167 1.3673 -0.2118 0.0278  -0.1333 1612 LEU A N   
1174 C  CA  . LEU A 142 ? 0.8112 0.6540 1.1840 -0.1913 0.0290  -0.1352 1612 LEU A CA  
1175 C  C   . LEU A 142 ? 0.9806 0.8135 1.3338 -0.1883 0.0165  -0.1495 1612 LEU A C   
1176 O  O   . LEU A 142 ? 0.9305 0.7674 1.2680 -0.1726 0.0171  -0.1522 1612 LEU A O   
1177 C  CB  . LEU A 142 ? 0.9895 0.8724 1.3807 -0.1847 0.0324  -0.1267 1612 LEU A CB  
1178 C  CG  . LEU A 142 ? 0.8539 0.7460 1.2376 -0.1654 0.0408  -0.1203 1612 LEU A CG  
1179 C  CD1 . LEU A 142 ? 0.8023 0.6788 1.1844 -0.1608 0.0541  -0.1120 1612 LEU A CD1 
1180 C  CD2 . LEU A 142 ? 0.9338 0.8641 1.3380 -0.1628 0.0398  -0.1136 1612 LEU A CD2 
1181 N  N   . ASP A 143 ? 1.0145 0.8330 1.3667 -0.2036 0.0056  -0.1590 1613 ASP A N   
1182 C  CA  . ASP A 143 ? 1.1379 0.9486 1.4719 -0.2023 -0.0076 -0.1738 1613 ASP A CA  
1183 C  C   . ASP A 143 ? 1.2292 1.0039 1.5334 -0.1905 -0.0065 -0.1835 1613 ASP A C   
1184 O  O   . ASP A 143 ? 1.4195 1.1855 1.7048 -0.1872 -0.0161 -0.1972 1613 ASP A O   
1185 C  CB  . ASP A 143 ? 1.2835 1.0915 1.6279 -0.2236 -0.0205 -0.1813 1613 ASP A CB  
1186 C  CG  . ASP A 143 ? 1.4358 1.2838 1.8122 -0.2351 -0.0228 -0.1737 1613 ASP A CG  
1187 O  OD1 . ASP A 143 ? 1.5071 1.3761 1.8879 -0.2385 -0.0354 -0.1803 1613 ASP A OD1 
1188 O  OD2 . ASP A 143 ? 1.4952 1.3543 1.8921 -0.2403 -0.0122 -0.1617 1613 ASP A OD2 
1189 N  N   . GLY A 144 ? 1.1140 0.8687 1.4138 -0.1833 0.0046  -0.1774 1614 GLY A N   
1190 C  CA  . GLY A 144 ? 1.1780 0.9029 1.4526 -0.1690 0.0066  -0.1861 1614 GLY A CA  
1191 C  C   . GLY A 144 ? 1.2412 0.9823 1.5049 -0.1488 0.0140  -0.1851 1614 GLY A C   
1192 O  O   . GLY A 144 ? 1.3030 1.0256 1.5456 -0.1361 0.0148  -0.1951 1614 GLY A O   
1193 N  N   . LEU A 145 ? 1.2055 0.9808 1.4834 -0.1457 0.0193  -0.1738 1615 LEU A N   
1194 C  CA  . LEU A 145 ? 1.1956 0.9852 1.4655 -0.1281 0.0282  -0.1696 1615 LEU A CA  
1195 C  C   . LEU A 145 ? 1.1095 0.9082 1.3599 -0.1204 0.0222  -0.1798 1615 LEU A C   
1196 O  O   . LEU A 145 ? 1.1893 0.9992 1.4398 -0.1287 0.0111  -0.1849 1615 LEU A O   
1197 C  CB  . LEU A 145 ? 1.2285 1.0492 1.5194 -0.1277 0.0350  -0.1540 1615 LEU A CB  
1198 C  CG  . LEU A 145 ? 1.2153 1.0359 1.5210 -0.1265 0.0467  -0.1409 1615 LEU A CG  
1199 C  CD1 . LEU A 145 ? 1.1907 1.0436 1.5102 -0.1209 0.0523  -0.1292 1615 LEU A CD1 
1200 C  CD2 . LEU A 145 ? 1.2502 1.0463 1.5408 -0.1145 0.0543  -0.1430 1615 LEU A CD2 
1201 N  N   . ASP A 146 ? 0.9630 0.7584 1.1969 -0.1048 0.0298  -0.1826 1616 ASP A N   
1202 C  CA  . ASP A 146 ? 1.0794 0.8876 1.2938 -0.0964 0.0276  -0.1895 1616 ASP A CA  
1203 C  C   . ASP A 146 ? 1.0983 0.9347 1.3197 -0.0892 0.0356  -0.1756 1616 ASP A C   
1204 O  O   . ASP A 146 ? 1.0172 0.8539 1.2444 -0.0813 0.0470  -0.1675 1616 ASP A O   
1205 C  CB  . ASP A 146 ? 1.1585 0.9469 1.3493 -0.0841 0.0313  -0.2030 1616 ASP A CB  
1206 C  CG  . ASP A 146 ? 1.2230 1.0303 1.3956 -0.0735 0.0349  -0.2055 1616 ASP A CG  
1207 O  OD1 . ASP A 146 ? 1.1697 0.9911 1.3345 -0.0786 0.0261  -0.2077 1616 ASP A OD1 
1208 O  OD2 . ASP A 146 ? 1.2541 1.0634 1.4208 -0.0610 0.0462  -0.2043 1616 ASP A OD2 
1209 N  N   . HIS A 147 ? 1.1374 0.9960 1.3576 -0.0920 0.0286  -0.1729 1617 HIS A N   
1210 C  CA  . HIS A 147 ? 1.1731 1.0564 1.3990 -0.0862 0.0340  -0.1594 1617 HIS A CA  
1211 C  C   . HIS A 147 ? 1.1644 1.0546 1.3648 -0.0762 0.0364  -0.1629 1617 HIS A C   
1212 O  O   . HIS A 147 ? 0.9945 0.9043 1.1950 -0.0728 0.0380  -0.1524 1617 HIS A O   
1213 C  CB  . HIS A 147 ? 1.2602 1.1641 1.5046 -0.0955 0.0244  -0.1519 1617 HIS A CB  
1214 C  CG  . HIS A 147 ? 1.4644 1.3655 1.7350 -0.1062 0.0237  -0.1481 1617 HIS A CG  
1215 N  ND1 . HIS A 147 ? 1.5423 1.4639 1.8356 -0.1149 0.0169  -0.1417 1617 HIS A ND1 
1216 C  CD2 . HIS A 147 ? 1.5169 1.3977 1.7943 -0.1098 0.0295  -0.1494 1617 HIS A CD2 
1217 C  CE1 . HIS A 147 ? 1.5356 1.4511 1.8486 -0.1243 0.0196  -0.1394 1617 HIS A CE1 
1218 N  NE2 . HIS A 147 ? 1.5364 1.4258 1.8389 -0.1217 0.0270  -0.1435 1617 HIS A NE2 
1219 N  N   . SER A 148 ? 1.1981 1.0722 1.3761 -0.0718 0.0366  -0.1777 1618 SER A N   
1220 C  CA  . SER A 148 ? 1.2428 1.1242 1.3946 -0.0632 0.0400  -0.1826 1618 SER A CA  
1221 C  C   . SER A 148 ? 1.2362 1.1291 1.3900 -0.0537 0.0543  -0.1715 1618 SER A C   
1222 O  O   . SER A 148 ? 1.2490 1.1569 1.3878 -0.0498 0.0569  -0.1673 1618 SER A O   
1223 C  CB  . SER A 148 ? 1.1844 1.0455 1.3148 -0.0588 0.0398  -0.2018 1618 SER A CB  
1224 O  OG  . SER A 148 ? 1.1684 1.0139 1.3060 -0.0517 0.0499  -0.2041 1618 SER A OG  
1225 N  N   . ASP A 149 ? 1.0968 0.9820 1.2676 -0.0504 0.0632  -0.1667 1619 ASP A N   
1226 C  CA  . ASP A 149 ? 1.1110 1.0057 1.2839 -0.0414 0.0765  -0.1580 1619 ASP A CA  
1227 C  C   . ASP A 149 ? 1.0117 0.9276 1.1927 -0.0432 0.0770  -0.1415 1619 ASP A C   
1228 O  O   . ASP A 149 ? 0.9999 0.9267 1.1745 -0.0372 0.0858  -0.1352 1619 ASP A O   
1229 C  CB  . ASP A 149 ? 1.1946 1.0762 1.3851 -0.0383 0.0836  -0.1557 1619 ASP A CB  
1230 C  CG  . ASP A 149 ? 1.1350 0.9972 1.3145 -0.0310 0.0868  -0.1706 1619 ASP A CG  
1231 O  OD1 . ASP A 149 ? 1.1584 1.0212 1.3169 -0.0265 0.0866  -0.1826 1619 ASP A OD1 
1232 O  OD2 . ASP A 149 ? 1.1134 0.9595 1.3048 -0.0295 0.0891  -0.1704 1619 ASP A OD2 
1233 N  N   . PHE A 150 ? 0.7062 0.6282 0.9014 -0.0515 0.0674  -0.1348 1620 PHE A N   
1234 C  CA  . PHE A 150 ? 0.8181 0.7579 1.0249 -0.0522 0.0668  -0.1193 1620 PHE A CA  
1235 C  C   . PHE A 150 ? 0.9086 0.8601 1.1077 -0.0571 0.0537  -0.1179 1620 PHE A C   
1236 O  O   . PHE A 150 ? 0.9678 0.9316 1.1829 -0.0597 0.0484  -0.1072 1620 PHE A O   
1237 C  CB  . PHE A 150 ? 0.8194 0.7597 1.0553 -0.0556 0.0684  -0.1107 1620 PHE A CB  
1238 C  CG  . PHE A 150 ? 0.8914 0.8157 1.1348 -0.0533 0.0772  -0.1141 1620 PHE A CG  
1239 C  CD1 . PHE A 150 ? 0.8142 0.7397 1.0624 -0.0460 0.0888  -0.1070 1620 PHE A CD1 
1240 C  CD2 . PHE A 150 ? 0.9191 0.8261 1.1644 -0.0586 0.0730  -0.1240 1620 PHE A CD2 
1241 C  CE1 . PHE A 150 ? 0.6741 0.5845 0.9284 -0.0431 0.0956  -0.1099 1620 PHE A CE1 
1242 C  CE2 . PHE A 150 ? 0.9084 0.7983 1.1588 -0.0560 0.0800  -0.1263 1620 PHE A CE2 
1243 C  CZ  . PHE A 150 ? 0.7766 0.6687 1.0315 -0.0478 0.0910  -0.1191 1620 PHE A CZ  
1244 N  N   . GLN A 151 ? 0.9809 0.9296 1.1545 -0.0574 0.0482  -0.1284 1621 GLN A N   
1245 C  CA  . GLN A 151 ? 1.2204 1.1769 1.3880 -0.0635 0.0327  -0.1297 1621 GLN A CA  
1246 C  C   . GLN A 151 ? 1.2062 1.1790 1.3681 -0.0614 0.0288  -0.1161 1621 GLN A C   
1247 O  O   . GLN A 151 ? 1.2656 1.2477 1.4330 -0.0659 0.0150  -0.1131 1621 GLN A O   
1248 C  CB  . GLN A 151 ? 1.3440 1.2911 1.4843 -0.0648 0.0267  -0.1462 1621 GLN A CB  
1249 C  CG  . GLN A 151 ? 1.4285 1.3655 1.5785 -0.0736 0.0152  -0.1576 1621 GLN A CG  
1250 C  CD  . GLN A 151 ? 1.4410 1.3923 1.6067 -0.0816 0.0001  -0.1518 1621 GLN A CD  
1251 O  OE1 . GLN A 151 ? 1.4473 1.4124 1.6024 -0.0805 -0.0074 -0.1456 1621 GLN A OE1 
1252 N  NE2 . GLN A 151 ? 1.3827 1.3313 1.5741 -0.0899 -0.0045 -0.1534 1621 GLN A NE2 
1253 N  N   . ASP A 152 ? 1.1057 1.0821 1.2580 -0.0552 0.0397  -0.1076 1622 ASP A N   
1254 C  CA  . ASP A 152 ? 1.1971 1.1853 1.3430 -0.0538 0.0355  -0.0934 1622 ASP A CA  
1255 C  C   . ASP A 152 ? 1.1236 1.1160 1.2905 -0.0501 0.0443  -0.0792 1622 ASP A C   
1256 O  O   . ASP A 152 ? 1.2643 1.2609 1.4210 -0.0470 0.0485  -0.0683 1622 ASP A O   
1257 C  CB  . ASP A 152 ? 1.2993 1.2884 1.4095 -0.0516 0.0385  -0.0947 1622 ASP A CB  
1258 C  CG  . ASP A 152 ? 1.4363 1.4210 1.5231 -0.0548 0.0293  -0.1097 1622 ASP A CG  
1259 O  OD1 . ASP A 152 ? 1.5042 1.4799 1.5814 -0.0532 0.0367  -0.1238 1622 ASP A OD1 
1260 O  OD2 . ASP A 152 ? 1.3668 1.3569 1.4453 -0.0584 0.0140  -0.1081 1622 ASP A OD2 
1261 N  N   . THR A 153 ? 0.7961 0.7864 0.9914 -0.0511 0.0470  -0.0794 1623 THR A N   
1262 C  CA  . THR A 153 ? 0.8065 0.7994 1.0231 -0.0476 0.0554  -0.0681 1623 THR A CA  
1263 C  C   . THR A 153 ? 0.9076 0.9097 1.1506 -0.0499 0.0463  -0.0619 1623 THR A C   
1264 O  O   . THR A 153 ? 0.9454 0.9520 1.1944 -0.0550 0.0346  -0.0674 1623 THR A O   
1265 C  CB  . THR A 153 ? 0.7242 0.7070 0.9508 -0.0461 0.0679  -0.0737 1623 THR A CB  
1266 O  OG1 . THR A 153 ? 0.7038 0.6824 0.9482 -0.0514 0.0630  -0.0803 1623 THR A OG1 
1267 C  CG2 . THR A 153 ? 0.8281 0.8027 1.0311 -0.0435 0.0750  -0.0843 1623 THR A CG2 
1268 N  N   . ASP A 154 ? 0.7920 0.7980 1.0519 -0.0461 0.0519  -0.0510 1624 ASP A N   
1269 C  CA  . ASP A 154 ? 0.7806 0.7962 1.0692 -0.0471 0.0464  -0.0466 1624 ASP A CA  
1270 C  C   . ASP A 154 ? 0.7159 0.7275 1.0252 -0.0505 0.0537  -0.0519 1624 ASP A C   
1271 O  O   . ASP A 154 ? 0.8533 0.8728 1.1872 -0.0508 0.0540  -0.0476 1624 ASP A O   
1272 C  CB  . ASP A 154 ? 0.7221 0.7432 1.0189 -0.0409 0.0476  -0.0331 1624 ASP A CB  
1273 C  CG  . ASP A 154 ? 0.7296 0.7425 1.0246 -0.0368 0.0624  -0.0282 1624 ASP A CG  
1274 O  OD1 . ASP A 154 ? 0.5678 0.5719 0.8543 -0.0377 0.0720  -0.0348 1624 ASP A OD1 
1275 O  OD2 . ASP A 154 ? 0.6837 0.6990 0.9865 -0.0323 0.0637  -0.0180 1624 ASP A OD2 
1276 N  N   . ILE A 155 ? 0.6908 0.6895 0.9898 -0.0529 0.0596  -0.0613 1625 ILE A N   
1277 C  CA  . ILE A 155 ? 0.6893 0.6810 1.0049 -0.0572 0.0650  -0.0659 1625 ILE A CA  
1278 C  C   . ILE A 155 ? 0.7047 0.7009 1.0302 -0.0662 0.0539  -0.0728 1625 ILE A C   
1279 O  O   . ILE A 155 ? 0.7807 0.7722 1.0903 -0.0696 0.0463  -0.0817 1625 ILE A O   
1280 C  CB  . ILE A 155 ? 0.6563 0.6304 0.9578 -0.0552 0.0744  -0.0730 1625 ILE A CB  
1281 C  CG1 . ILE A 155 ? 0.6806 0.6539 0.9765 -0.0470 0.0854  -0.0658 1625 ILE A CG1 
1282 C  CG2 . ILE A 155 ? 0.5840 0.5477 0.8997 -0.0606 0.0776  -0.0774 1625 ILE A CG2 
1283 C  CD1 . ILE A 155 ? 0.7250 0.6841 1.0119 -0.0435 0.0951  -0.0721 1625 ILE A CD1 
1284 N  N   . PRO A 156 ? 0.7495 0.7557 1.1013 -0.0707 0.0528  -0.0697 1626 PRO A N   
1285 C  CA  . PRO A 156 ? 0.7541 0.7686 1.1180 -0.0803 0.0418  -0.0759 1626 PRO A CA  
1286 C  C   . PRO A 156 ? 0.7029 0.6998 1.0617 -0.0888 0.0432  -0.0861 1626 PRO A C   
1287 O  O   . PRO A 156 ? 0.7441 0.7253 1.1007 -0.0880 0.0536  -0.0864 1626 PRO A O   
1288 C  CB  . PRO A 156 ? 0.5964 0.6283 0.9913 -0.0819 0.0435  -0.0691 1626 PRO A CB  
1289 C  CG  . PRO A 156 ? 0.5294 0.5529 0.9263 -0.0762 0.0579  -0.0628 1626 PRO A CG  
1290 C  CD  . PRO A 156 ? 0.6693 0.6817 1.0410 -0.0673 0.0615  -0.0609 1626 PRO A CD  
1291 N  N   . PHE A 157 ? 0.8033 0.8017 1.1592 -0.0967 0.0312  -0.0946 1627 PHE A N   
1292 C  CA  . PHE A 157 ? 1.0042 0.9843 1.3542 -0.1058 0.0296  -0.1054 1627 PHE A CA  
1293 C  C   . PHE A 157 ? 0.9962 0.9827 1.3722 -0.1189 0.0272  -0.1060 1627 PHE A C   
1294 O  O   . PHE A 157 ? 1.0289 0.9976 1.4065 -0.1254 0.0329  -0.1088 1627 PHE A O   
1295 C  CB  . PHE A 157 ? 1.1996 1.1744 1.5267 -0.1069 0.0181  -0.1159 1627 PHE A CB  
1296 C  CG  . PHE A 157 ? 1.3799 1.3439 1.6786 -0.0959 0.0237  -0.1174 1627 PHE A CG  
1297 C  CD1 . PHE A 157 ? 1.2024 1.1548 1.4977 -0.0885 0.0378  -0.1136 1627 PHE A CD1 
1298 C  CD2 . PHE A 157 ? 1.4132 1.3801 1.6889 -0.0930 0.0151  -0.1224 1627 PHE A CD2 
1299 C  CE1 . PHE A 157 ? 1.1263 1.0721 1.3987 -0.0791 0.0438  -0.1152 1627 PHE A CE1 
1300 C  CE2 . PHE A 157 ? 1.3146 1.2738 1.5648 -0.0838 0.0221  -0.1237 1627 PHE A CE2 
1301 C  CZ  . PHE A 157 ? 1.2646 1.2143 1.5146 -0.0770 0.0366  -0.1203 1627 PHE A CZ  
1302 N  N   . GLU A 158 ? 1.1958 1.2077 1.5924 -0.1227 0.0189  -0.1032 1628 GLU A N   
1303 C  CA  . GLU A 158 ? 1.3130 1.3378 1.7387 -0.1350 0.0185  -0.1026 1628 GLU A CA  
1304 C  C   . GLU A 158 ? 1.0688 1.1012 1.5115 -0.1303 0.0321  -0.0921 1628 GLU A C   
1305 O  O   . GLU A 158 ? 1.1182 1.1698 1.5714 -0.1214 0.0326  -0.0849 1628 GLU A O   
1306 C  CB  . GLU A 158 ? 1.4847 1.5371 1.9281 -0.1398 0.0039  -0.1046 1628 GLU A CB  
1307 C  CG  . GLU A 158 ? 1.6510 1.6997 2.0727 -0.1392 -0.0108 -0.1129 1628 GLU A CG  
1308 C  CD  . GLU A 158 ? 1.7602 1.8365 2.1920 -0.1343 -0.0238 -0.1099 1628 GLU A CD  
1309 O  OE1 . GLU A 158 ? 1.7548 1.8277 2.1626 -0.1277 -0.0327 -0.1119 1628 GLU A OE1 
1310 O  OE2 . GLU A 158 ? 1.7916 1.8931 2.2546 -0.1367 -0.0253 -0.1056 1628 GLU A OE2 
1311 N  N   . VAL A 159 ? 0.7432 0.7584 1.1868 -0.1359 0.0427  -0.0913 1629 VAL A N   
1312 C  CA  . VAL A 159 ? 0.6867 0.7065 1.1435 -0.1325 0.0560  -0.0822 1629 VAL A CA  
1313 C  C   . VAL A 159 ? 0.6425 0.6598 1.1150 -0.1477 0.0609  -0.0825 1629 VAL A C   
1314 O  O   . VAL A 159 ? 0.5952 0.5971 1.0618 -0.1595 0.0559  -0.0893 1629 VAL A O   
1315 C  CB  . VAL A 159 ? 0.7295 0.7268 1.1650 -0.1211 0.0663  -0.0788 1629 VAL A CB  
1316 C  CG1 . VAL A 159 ? 0.5631 0.5683 0.9885 -0.1066 0.0649  -0.0750 1629 VAL A CG1 
1317 C  CG2 . VAL A 159 ? 0.6487 0.6153 1.0614 -0.1245 0.0651  -0.0868 1629 VAL A CG2 
1318 N  N   . PRO A 160 ? 0.7834 0.8157 1.2754 -0.1483 0.0707  -0.0752 1630 PRO A N   
1319 C  CA  . PRO A 160 ? 0.7880 0.8166 1.2921 -0.1634 0.0777  -0.0740 1630 PRO A CA  
1320 C  C   . PRO A 160 ? 0.8115 0.8023 1.2920 -0.1656 0.0833  -0.0743 1630 PRO A C   
1321 O  O   . PRO A 160 ? 0.7794 0.7543 1.2428 -0.1530 0.0891  -0.0713 1630 PRO A O   
1322 C  CB  . PRO A 160 ? 0.6985 0.7496 1.2227 -0.1591 0.0886  -0.0660 1630 PRO A CB  
1323 C  CG  . PRO A 160 ? 0.7245 0.7812 1.2417 -0.1402 0.0884  -0.0626 1630 PRO A CG  
1324 C  CD  . PRO A 160 ? 0.7511 0.8064 1.2564 -0.1363 0.0746  -0.0684 1630 PRO A CD  
1325 N  N   . LEU A 161 ? 0.9136 0.8897 1.3935 -0.1817 0.0804  -0.0783 1631 LEU A N   
1326 C  CA  . LEU A 161 ? 0.7215 0.6599 1.1806 -0.1848 0.0847  -0.0782 1631 LEU A CA  
1327 C  C   . LEU A 161 ? 0.6572 0.5938 1.1237 -0.1905 0.0978  -0.0688 1631 LEU A C   
1328 O  O   . LEU A 161 ? 0.6930 0.6456 1.1791 -0.2056 0.1004  -0.0665 1631 LEU A O   
1329 C  CB  . LEU A 161 ? 0.7139 0.6334 1.1675 -0.2002 0.0751  -0.0864 1631 LEU A CB  
1330 C  CG  . LEU A 161 ? 0.6727 0.5485 1.1028 -0.2032 0.0757  -0.0885 1631 LEU A CG  
1331 C  CD1 . LEU A 161 ? 0.6627 0.5198 1.0691 -0.1842 0.0755  -0.0918 1631 LEU A CD1 
1332 C  CD2 . LEU A 161 ? 0.6978 0.5578 1.1260 -0.2204 0.0645  -0.0973 1631 LEU A CD2 
1333 N  N   . PRO A 162 ? 0.7071 0.6261 1.1587 -0.1793 0.1062  -0.0635 1632 PRO A N   
1334 C  CA  . PRO A 162 ? 0.7572 0.6737 1.2130 -0.1846 0.1184  -0.0544 1632 PRO A CA  
1335 C  C   . PRO A 162 ? 0.8560 0.7484 1.3066 -0.2033 0.1185  -0.0536 1632 PRO A C   
1336 O  O   . PRO A 162 ? 0.9007 0.7653 1.3363 -0.2075 0.1101  -0.0596 1632 PRO A O   
1337 C  CB  . PRO A 162 ? 0.6745 0.5729 1.1115 -0.1675 0.1239  -0.0508 1632 PRO A CB  
1338 C  CG  . PRO A 162 ? 0.6228 0.5287 1.0543 -0.1526 0.1172  -0.0563 1632 PRO A CG  
1339 C  CD  . PRO A 162 ? 0.5670 0.4728 0.9992 -0.1609 0.1054  -0.0652 1632 PRO A CD  
1340 N  N   . ALA A 163 ? 0.9162 0.8192 1.3790 -0.2151 0.1283  -0.0461 1633 ALA A N   
1341 C  CA  . ALA A 163 ? 1.0660 0.9453 1.5229 -0.2348 0.1297  -0.0431 1633 ALA A CA  
1342 C  C   . ALA A 163 ? 1.0185 0.8566 1.4481 -0.2298 0.1332  -0.0378 1633 ALA A C   
1343 O  O   . ALA A 163 ? 0.9667 0.7717 1.3825 -0.2418 0.1293  -0.0376 1633 ALA A O   
1344 C  CB  . ALA A 163 ? 1.0260 0.9334 1.5053 -0.2507 0.1398  -0.0368 1633 ALA A CB  
1345 N  N   . LYS A 164 ? 0.9178 0.7561 1.3392 -0.2121 0.1393  -0.0338 1634 LYS A N   
1346 C  CA  . LYS A 164 ? 1.0071 0.8102 1.4045 -0.2057 0.1423  -0.0285 1634 LYS A CA  
1347 C  C   . LYS A 164 ? 1.0413 0.8365 1.4263 -0.1831 0.1382  -0.0332 1634 LYS A C   
1348 O  O   . LYS A 164 ? 0.9913 0.8125 1.3867 -0.1723 0.1369  -0.0373 1634 LYS A O   
1349 C  CB  . LYS A 164 ? 0.9582 0.7695 1.3571 -0.2082 0.1554  -0.0176 1634 LYS A CB  
1350 C  CG  . LYS A 164 ? 1.0230 0.8780 1.4437 -0.2010 0.1629  -0.0167 1634 LYS A CG  
1351 C  CD  . LYS A 164 ? 1.0229 0.8805 1.4382 -0.1957 0.1747  -0.0080 1634 LYS A CD  
1352 C  CE  . LYS A 164 ? 1.1437 0.9932 1.5466 -0.1735 0.1735  -0.0087 1634 LYS A CE  
1353 N  NZ  . LYS A 164 ? 1.2323 1.0622 1.6173 -0.1695 0.1803  -0.0008 1634 LYS A NZ  
1354 N  N   . GLN A 165 ? 1.0104 0.7695 1.3732 -0.1764 0.1359  -0.0326 1635 GLN A N   
1355 C  CA  . GLN A 165 ? 0.7383 0.4904 1.0899 -0.1556 0.1329  -0.0373 1635 GLN A CA  
1356 C  C   . GLN A 165 ? 0.6145 0.3800 0.9675 -0.1442 0.1421  -0.0300 1635 GLN A C   
1357 O  O   . GLN A 165 ? 0.8917 0.6449 1.2377 -0.1481 0.1479  -0.0216 1635 GLN A O   
1358 C  CB  . GLN A 165 ? 0.8458 0.5554 1.1753 -0.1515 0.1260  -0.0409 1635 GLN A CB  
1359 C  CG  . GLN A 165 ? 0.8394 0.5386 1.1648 -0.1520 0.1153  -0.0532 1635 GLN A CG  
1360 C  CD  . GLN A 165 ? 1.0424 0.6981 1.3467 -0.1480 0.1081  -0.0577 1635 GLN A CD  
1361 O  OE1 . GLN A 165 ? 1.0127 0.6561 1.3058 -0.1310 0.1080  -0.0593 1635 GLN A OE1 
1362 N  NE2 . GLN A 165 ? 1.1049 0.7366 1.4043 -0.1636 0.1016  -0.0599 1635 GLN A NE2 
1363 N  N   . HIS A 166 ? 0.5469 0.3366 0.9077 -0.1307 0.1429  -0.0329 1636 HIS A N   
1364 C  CA  . HIS A 166 ? 0.7906 0.5931 1.1533 -0.1201 0.1508  -0.0268 1636 HIS A CA  
1365 C  C   . HIS A 166 ? 0.8783 0.6553 1.2229 -0.1079 0.1504  -0.0256 1636 HIS A C   
1366 O  O   . HIS A 166 ? 0.7566 0.5338 1.0983 -0.1039 0.1566  -0.0188 1636 HIS A O   
1367 C  CB  . HIS A 166 ? 0.7378 0.5706 1.1131 -0.1099 0.1510  -0.0296 1636 HIS A CB  
1368 C  CG  . HIS A 166 ? 0.8708 0.7141 1.2474 -0.0989 0.1581  -0.0243 1636 HIS A CG  
1369 N  ND1 . HIS A 166 ? 0.8739 0.7052 1.2386 -0.0851 0.1577  -0.0249 1636 HIS A ND1 
1370 C  CD2 . HIS A 166 ? 0.8386 0.7029 1.2272 -0.0998 0.1655  -0.0189 1636 HIS A CD2 
1371 C  CE1 . HIS A 166 ? 0.8263 0.6699 1.1952 -0.0788 0.1639  -0.0198 1636 HIS A CE1 
1372 N  NE2 . HIS A 166 ? 0.9003 0.7630 1.2828 -0.0871 0.1688  -0.0164 1636 HIS A NE2 
1373 N  N   . VAL A 167 ? 0.7644 0.5216 1.0974 -0.1008 0.1430  -0.0329 1637 VAL A N   
1374 C  CA  . VAL A 167 ? 0.7754 0.5141 1.0948 -0.0861 0.1417  -0.0340 1637 VAL A CA  
1375 C  C   . VAL A 167 ? 0.8557 0.5564 1.1587 -0.0910 0.1380  -0.0313 1637 VAL A C   
1376 O  O   . VAL A 167 ? 0.8516 0.5347 1.1503 -0.1007 0.1322  -0.0352 1637 VAL A O   
1377 C  CB  . VAL A 167 ? 0.7171 0.4583 1.0337 -0.0738 0.1364  -0.0444 1637 VAL A CB  
1378 C  CG1 . VAL A 167 ? 0.8032 0.5208 1.1058 -0.0603 0.1334  -0.0475 1637 VAL A CG1 
1379 C  CG2 . VAL A 167 ? 0.5947 0.3699 0.9236 -0.0668 0.1406  -0.0442 1637 VAL A CG2 
1380 N  N   . PRO A 168 ? 0.7533 0.4405 1.0468 -0.0846 0.1403  -0.0249 1638 PRO A N   
1381 C  CA  . PRO A 168 ? 0.8645 0.5131 1.1405 -0.0889 0.1358  -0.0211 1638 PRO A CA  
1382 C  C   . PRO A 168 ? 0.8495 0.4713 1.1148 -0.0803 0.1257  -0.0310 1638 PRO A C   
1383 O  O   . PRO A 168 ? 0.7167 0.3499 0.9858 -0.0670 0.1236  -0.0403 1638 PRO A O   
1384 C  CB  . PRO A 168 ? 0.9159 0.5607 1.1844 -0.0801 0.1395  -0.0132 1638 PRO A CB  
1385 C  CG  . PRO A 168 ? 0.7667 0.4491 1.0506 -0.0772 0.1479  -0.0112 1638 PRO A CG  
1386 C  CD  . PRO A 168 ? 0.7876 0.4930 1.0851 -0.0744 0.1466  -0.0203 1638 PRO A CD  
1387 N  N   . GLU A 169 ? 0.9606 0.5455 1.2116 -0.0882 0.1197  -0.0290 1639 GLU A N   
1388 C  CA  . GLU A 169 ? 1.0307 0.5872 1.2717 -0.0822 0.1094  -0.0396 1639 GLU A CA  
1389 C  C   . GLU A 169 ? 0.9932 0.5443 1.2291 -0.0595 0.1057  -0.0464 1639 GLU A C   
1390 O  O   . GLU A 169 ? 1.1142 0.6629 1.3497 -0.0498 0.1005  -0.0591 1639 GLU A O   
1391 C  CB  . GLU A 169 ? 0.9972 0.5169 1.2180 -0.0935 0.1011  -0.0339 1639 GLU A CB  
1392 C  CG  . GLU A 169 ? 1.1138 0.6036 1.3227 -0.0881 0.0889  -0.0455 1639 GLU A CG  
1393 C  CD  . GLU A 169 ? 1.4665 0.9144 1.6495 -0.0842 0.0780  -0.0407 1639 GLU A CD  
1394 O  OE1 . GLU A 169 ? 1.5705 1.0116 1.7440 -0.0885 0.0799  -0.0272 1639 GLU A OE1 
1395 O  OE2 . GLU A 169 ? 1.4474 0.8680 1.6186 -0.0766 0.0671  -0.0505 1639 GLU A OE2 
1396 N  N   . ALA A 170 ? 0.9359 0.4871 1.1677 -0.0508 0.1080  -0.0388 1640 ALA A N   
1397 C  CA  . ALA A 170 ? 0.9857 0.5343 1.2142 -0.0294 0.1039  -0.0451 1640 ALA A CA  
1398 C  C   . ALA A 170 ? 0.9160 0.4995 1.1600 -0.0192 0.1087  -0.0547 1640 ALA A C   
1399 O  O   . ALA A 170 ? 1.0044 0.5854 1.2476 -0.0055 0.1044  -0.0664 1640 ALA A O   
1400 C  CB  . ALA A 170 ? 1.0719 0.6190 1.2934 -0.0238 0.1050  -0.0343 1640 ALA A CB  
1401 N  N   . GLU A 171 ? 0.7567 0.3739 1.0135 -0.0255 0.1173  -0.0498 1641 GLU A N   
1402 C  CA  . GLU A 171 ? 0.8057 0.4560 1.0746 -0.0176 0.1213  -0.0569 1641 GLU A CA  
1403 C  C   . GLU A 171 ? 0.7352 0.3863 1.0043 -0.0206 0.1177  -0.0680 1641 GLU A C   
1404 O  O   . GLU A 171 ? 0.7800 0.4428 1.0508 -0.0094 0.1172  -0.0781 1641 GLU A O   
1405 C  CB  . GLU A 171 ? 0.8184 0.5001 1.0998 -0.0246 0.1300  -0.0485 1641 GLU A CB  
1406 C  CG  . GLU A 171 ? 0.8471 0.5396 1.1311 -0.0157 0.1343  -0.0423 1641 GLU A CG  
1407 C  CD  . GLU A 171 ? 1.0014 0.6772 1.2775 -0.0222 0.1353  -0.0313 1641 GLU A CD  
1408 O  OE1 . GLU A 171 ? 0.9707 0.6173 1.2351 -0.0293 0.1307  -0.0290 1641 GLU A OE1 
1409 O  OE2 . GLU A 171 ? 1.0461 0.7371 1.3264 -0.0205 0.1406  -0.0248 1641 GLU A OE2 
1410 N  N   . ARG A 172 ? 0.6283 0.2673 0.8952 -0.0362 0.1151  -0.0665 1642 ARG A N   
1411 C  CA  . ARG A 172 ? 0.8090 0.4443 1.0739 -0.0398 0.1098  -0.0777 1642 ARG A CA  
1412 C  C   . ARG A 172 ? 0.7018 0.3116 0.9548 -0.0264 0.1025  -0.0896 1642 ARG A C   
1413 O  O   . ARG A 172 ? 0.7503 0.3690 1.0028 -0.0194 0.1008  -0.1017 1642 ARG A O   
1414 C  CB  . ARG A 172 ? 0.6599 0.2818 0.9241 -0.0596 0.1069  -0.0741 1642 ARG A CB  
1415 C  CG  . ARG A 172 ? 0.7492 0.3668 1.0109 -0.0641 0.1001  -0.0864 1642 ARG A CG  
1416 C  CD  . ARG A 172 ? 0.8642 0.4663 1.1255 -0.0844 0.0958  -0.0841 1642 ARG A CD  
1417 N  NE  . ARG A 172 ? 1.1425 0.7161 1.3964 -0.0928 0.0955  -0.0738 1642 ARG A NE  
1418 C  CZ  . ARG A 172 ? 1.2627 0.8140 1.5127 -0.1108 0.0912  -0.0711 1642 ARG A CZ  
1419 N  NH1 . ARG A 172 ? 1.1742 0.7286 1.4284 -0.1221 0.0862  -0.0789 1642 ARG A NH1 
1420 N  NH2 . ARG A 172 ? 1.2935 0.8187 1.5346 -0.1182 0.0917  -0.0604 1642 ARG A NH2 
1421 N  N   . GLU A 173 ? 0.8326 0.4103 1.0753 -0.0221 0.0978  -0.0867 1643 GLU A N   
1422 C  CA  . GLU A 173 ? 0.8576 0.4080 1.0895 -0.0086 0.0895  -0.0988 1643 GLU A CA  
1423 C  C   . GLU A 173 ? 0.9470 0.5164 1.1836 0.0121  0.0923  -0.1062 1643 GLU A C   
1424 O  O   . GLU A 173 ? 0.8323 0.3956 1.0649 0.0240  0.0882  -0.1206 1643 GLU A O   
1425 C  CB  . GLU A 173 ? 0.7567 0.2651 0.9746 -0.0102 0.0819  -0.0925 1643 GLU A CB  
1426 C  CG  . GLU A 173 ? 0.9368 0.4209 1.1453 -0.0303 0.0764  -0.0884 1643 GLU A CG  
1427 C  CD  . GLU A 173 ? 1.0553 0.5383 1.2670 -0.0359 0.0736  -0.1024 1643 GLU A CD  
1428 O  OE1 . GLU A 173 ? 1.1702 0.6409 1.3750 -0.0220 0.0674  -0.1167 1643 GLU A OE1 
1429 O  OE2 . GLU A 173 ? 0.9691 0.4675 1.1880 -0.0534 0.0764  -0.0989 1643 GLU A OE2 
1430 N  N   . GLU A 174 ? 0.7578 0.3512 1.0034 0.0164  0.0993  -0.0976 1644 GLU A N   
1431 C  CA  . GLU A 174 ? 0.8363 0.4532 1.0890 0.0335  0.1028  -0.1047 1644 GLU A CA  
1432 C  C   . GLU A 174 ? 0.8303 0.4757 1.0885 0.0331  0.1075  -0.1137 1644 GLU A C   
1433 O  O   . GLU A 174 ? 0.8359 0.4884 1.0935 0.0461  0.1073  -0.1264 1644 GLU A O   
1434 C  CB  . GLU A 174 ? 0.7574 0.3949 1.0190 0.0359  0.1091  -0.0936 1644 GLU A CB  
1435 C  CG  . GLU A 174 ? 0.9458 0.5591 1.2010 0.0403  0.1044  -0.0859 1644 GLU A CG  
1436 C  CD  . GLU A 174 ? 1.2278 0.8632 1.4911 0.0397  0.1109  -0.0748 1644 GLU A CD  
1437 O  OE1 . GLU A 174 ? 1.3650 0.9925 1.6264 0.0499  0.1077  -0.0720 1644 GLU A OE1 
1438 O  OE2 . GLU A 174 ? 1.2219 0.8822 1.4933 0.0295  0.1184  -0.0694 1644 GLU A OE2 
1439 N  N   . VAL A 175 ? 0.7534 0.4155 1.0164 0.0184  0.1114  -0.1074 1645 VAL A N   
1440 C  CA  . VAL A 175 ? 0.7619 0.4482 1.0273 0.0169  0.1142  -0.1149 1645 VAL A CA  
1441 C  C   . VAL A 175 ? 0.8146 0.4811 1.0689 0.0192  0.1072  -0.1295 1645 VAL A C   
1442 O  O   . VAL A 175 ? 0.6705 0.3505 0.9223 0.0278  0.1087  -0.1411 1645 VAL A O   
1443 C  CB  . VAL A 175 ? 0.5951 0.2997 0.8678 0.0009  0.1175  -0.1055 1645 VAL A CB  
1444 C  CG1 . VAL A 175 ? 0.5909 0.3148 0.8628 -0.0011 0.1178  -0.1134 1645 VAL A CG1 
1445 C  CG2 . VAL A 175 ? 0.6378 0.3650 0.9215 0.0010  0.1249  -0.0934 1645 VAL A CG2 
1446 N  N   . ARG A 176 ? 0.6829 0.3162 0.9292 0.0113  0.0996  -0.1294 1646 ARG A N   
1447 C  CA  . ARG A 176 ? 0.7057 0.3163 0.9406 0.0126  0.0918  -0.1438 1646 ARG A CA  
1448 C  C   . ARG A 176 ? 0.7541 0.3562 0.9838 0.0332  0.0900  -0.1571 1646 ARG A C   
1449 O  O   . ARG A 176 ? 0.7312 0.3392 0.9556 0.0400  0.0893  -0.1718 1646 ARG A O   
1450 C  CB  . ARG A 176 ? 0.8588 0.4323 1.0863 -0.0006 0.0837  -0.1398 1646 ARG A CB  
1451 C  CG  . ARG A 176 ? 0.8893 0.4384 1.1052 -0.0032 0.0746  -0.1545 1646 ARG A CG  
1452 C  CD  . ARG A 176 ? 0.8717 0.3862 1.0814 -0.0206 0.0668  -0.1495 1646 ARG A CD  
1453 N  NE  . ARG A 176 ? 0.8969 0.4245 1.1164 -0.0393 0.0714  -0.1333 1646 ARG A NE  
1454 C  CZ  . ARG A 176 ? 0.9811 0.5257 1.2073 -0.0555 0.0717  -0.1321 1646 ARG A CZ  
1455 N  NH1 . ARG A 176 ? 0.8758 0.4259 1.0984 -0.0558 0.0671  -0.1455 1646 ARG A NH1 
1456 N  NH2 . ARG A 176 ? 1.0203 0.5781 1.2571 -0.0710 0.0764  -0.1180 1646 ARG A NH2 
1457 N  N   . ASP A 177 ? 0.8085 0.3998 1.0401 0.0439  0.0895  -0.1526 1647 ASP A N   
1458 C  CA  . ASP A 177 ? 0.7356 0.3229 0.9658 0.0650  0.0877  -0.1652 1647 ASP A CA  
1459 C  C   . ASP A 177 ? 0.7777 0.4049 1.0150 0.0736  0.0966  -0.1733 1647 ASP A C   
1460 O  O   . ASP A 177 ? 0.7734 0.4019 1.0058 0.0845  0.0958  -0.1897 1647 ASP A O   
1461 C  CB  . ASP A 177 ? 0.7334 0.3120 0.9678 0.0747  0.0865  -0.1569 1647 ASP A CB  
1462 C  CG  . ASP A 177 ? 0.9837 0.5227 1.2051 0.0681  0.0764  -0.1477 1647 ASP A CG  
1463 O  OD1 . ASP A 177 ? 0.7914 0.3023 1.0009 0.0592  0.0691  -0.1511 1647 ASP A OD1 
1464 O  OD2 . ASP A 177 ? 1.0472 0.5850 1.2678 0.0712  0.0751  -0.1358 1647 ASP A OD2 
1465 N  N   . TRP A 178 ? 0.7601 0.4198 1.0084 0.0686  0.1054  -0.1619 1648 TRP A N   
1466 C  CA  . TRP A 178 ? 0.6879 0.3851 0.9428 0.0757  0.1144  -0.1671 1648 TRP A CA  
1467 C  C   . TRP A 178 ? 0.6616 0.3687 0.9083 0.0707  0.1154  -0.1772 1648 TRP A C   
1468 O  O   . TRP A 178 ? 0.6975 0.4189 0.9413 0.0813  0.1189  -0.1904 1648 TRP A O   
1469 C  CB  . TRP A 178 ? 0.7952 0.5203 1.0620 0.0688  0.1222  -0.1517 1648 TRP A CB  
1470 C  CG  . TRP A 178 ? 0.8354 0.5975 1.1085 0.0741  0.1314  -0.1552 1648 TRP A CG  
1471 C  CD1 . TRP A 178 ? 0.8034 0.5821 1.0839 0.0882  0.1359  -0.1610 1648 TRP A CD1 
1472 C  CD2 . TRP A 178 ? 0.8376 0.6246 1.1096 0.0648  0.1369  -0.1527 1648 TRP A CD2 
1473 N  NE1 . TRP A 178 ? 0.7572 0.5693 1.0409 0.0869  0.1448  -0.1620 1648 TRP A NE1 
1474 C  CE2 . TRP A 178 ? 0.7260 0.5422 1.0033 0.0730  0.1452  -0.1566 1648 TRP A CE2 
1475 C  CE3 . TRP A 178 ? 0.6930 0.4807 0.9605 0.0504  0.1352  -0.1475 1648 TRP A CE3 
1476 C  CZ2 . TRP A 178 ? 0.7269 0.5701 1.0025 0.0667  0.1518  -0.1544 1648 TRP A CZ2 
1477 C  CZ3 . TRP A 178 ? 0.7551 0.5700 1.0218 0.0456  0.1407  -0.1459 1648 TRP A CZ3 
1478 C  CH2 . TRP A 178 ? 0.6760 0.5168 0.9453 0.0536  0.1489  -0.1489 1648 TRP A CH2 
1479 N  N   . VAL A 179 ? 0.6625 0.3629 0.9049 0.0546  0.1122  -0.1715 1649 VAL A N   
1480 C  CA  . VAL A 179 ? 0.6704 0.3800 0.9041 0.0490  0.1117  -0.1805 1649 VAL A CA  
1481 C  C   . VAL A 179 ? 0.7067 0.3942 0.9276 0.0586  0.1056  -0.1994 1649 VAL A C   
1482 O  O   . VAL A 179 ? 0.8586 0.5606 1.0718 0.0637  0.1083  -0.2120 1649 VAL A O   
1483 C  CB  . VAL A 179 ? 0.6667 0.3719 0.9005 0.0299  0.1076  -0.1711 1649 VAL A CB  
1484 C  CG1 . VAL A 179 ? 0.6871 0.3892 0.9090 0.0241  0.1023  -0.1828 1649 VAL A CG1 
1485 C  CG2 . VAL A 179 ? 0.6308 0.3664 0.8762 0.0225  0.1147  -0.1562 1649 VAL A CG2 
1486 N  N   . LEU A 180 ? 0.8434 0.4943 1.0605 0.0612  0.0972  -0.2019 1650 LEU A N   
1487 C  CA  . LEU A 180 ? 0.7705 0.3959 0.9754 0.0717  0.0902  -0.2207 1650 LEU A CA  
1488 C  C   . LEU A 180 ? 0.7916 0.4348 0.9987 0.0924  0.0962  -0.2336 1650 LEU A C   
1489 O  O   . LEU A 180 ? 0.9348 0.5838 1.1328 0.0997  0.0971  -0.2505 1650 LEU A O   
1490 C  CB  . LEU A 180 ? 0.7986 0.3793 0.9994 0.0709  0.0797  -0.2185 1650 LEU A CB  
1491 C  CG  . LEU A 180 ? 0.8538 0.4017 1.0408 0.0807  0.0704  -0.2381 1650 LEU A CG  
1492 C  CD1 . LEU A 180 ? 0.8581 0.4062 1.0342 0.0700  0.0673  -0.2481 1650 LEU A CD1 
1493 C  CD2 . LEU A 180 ? 0.8730 0.3744 1.0551 0.0799  0.0595  -0.2340 1650 LEU A CD2 
1494 N  N   . THR A 181 ? 0.8307 0.4845 1.0502 0.1018  0.1005  -0.2264 1651 THR A N   
1495 C  CA  . THR A 181 ? 0.8438 0.5192 1.0693 0.1209  0.1068  -0.2381 1651 THR A CA  
1496 C  C   . THR A 181 ? 0.8645 0.5796 1.0888 0.1193  0.1177  -0.2432 1651 THR A C   
1497 O  O   . THR A 181 ? 0.8629 0.5872 1.0814 0.1309  0.1207  -0.2608 1651 THR A O   
1498 C  CB  . THR A 181 ? 0.8349 0.5192 1.0756 0.1279  0.1095  -0.2270 1651 THR A CB  
1499 O  OG1 . THR A 181 ? 0.9894 0.6363 1.2281 0.1373  0.0988  -0.2292 1651 THR A OG1 
1500 C  CG2 . THR A 181 ? 0.9825 0.7054 1.2344 0.1417  0.1198  -0.2345 1651 THR A CG2 
1501 N  N   . VAL A 182 ? 0.7052 0.4433 0.9340 0.1050  0.1235  -0.2281 1652 VAL A N   
1502 C  CA  . VAL A 182 ? 0.7733 0.5480 0.9999 0.1023  0.1335  -0.2299 1652 VAL A CA  
1503 C  C   . VAL A 182 ? 0.8287 0.5978 1.0372 0.0986  0.1305  -0.2432 1652 VAL A C   
1504 O  O   . VAL A 182 ? 0.7863 0.5784 0.9876 0.1039  0.1377  -0.2538 1652 VAL A O   
1505 C  CB  . VAL A 182 ? 0.8050 0.6000 1.0397 0.0878  0.1382  -0.2099 1652 VAL A CB  
1506 C  CG1 . VAL A 182 ? 0.6631 0.4876 0.8903 0.0814  0.1454  -0.2103 1652 VAL A CG1 
1507 C  CG2 . VAL A 182 ? 0.6411 0.4490 0.8926 0.0932  0.1432  -0.1995 1652 VAL A CG2 
1508 N  N   . SER A 183 ? 0.7319 0.4712 0.9321 0.0887  0.1200  -0.2429 1653 SER A N   
1509 C  CA  . SER A 183 ? 0.7594 0.4883 0.9419 0.0845  0.1146  -0.2563 1653 SER A CA  
1510 C  C   . SER A 183 ? 0.9101 0.6348 1.0822 0.1014  0.1155  -0.2792 1653 SER A C   
1511 O  O   . SER A 183 ? 0.8756 0.5984 1.0312 0.0996  0.1131  -0.2924 1653 SER A O   
1512 C  CB  . SER A 183 ? 0.9135 0.6059 1.0919 0.0723  0.1019  -0.2533 1653 SER A CB  
1513 O  OG  . SER A 183 ? 1.1097 0.7702 1.2920 0.0801  0.0958  -0.2548 1653 SER A OG  
1514 N  N   . MET A 184 ? 0.9483 0.6709 1.1296 0.1182  0.1179  -0.2852 1654 MET A N   
1515 C  CA  . MET A 184 ? 1.1381 0.8548 1.3112 0.1360  0.1179  -0.3086 1654 MET A CA  
1516 C  C   . MET A 184 ? 1.2476 1.0049 1.4166 0.1426  0.1311  -0.3185 1654 MET A C   
1517 O  O   . MET A 184 ? 1.1837 0.9393 1.3416 0.1547  0.1319  -0.3397 1654 MET A O   
1518 C  CB  . MET A 184 ? 0.9153 0.6156 1.1010 0.1531  0.1146  -0.3122 1654 MET A CB  
1519 C  CG  . MET A 184 ? 0.9103 0.5610 1.0930 0.1506  0.0998  -0.3092 1654 MET A CG  
1520 S  SD  . MET A 184 ? 1.0613 0.6722 1.2216 0.1429  0.0871  -0.3234 1654 MET A SD  
1521 C  CE  . MET A 184 ? 1.0081 0.6224 1.1667 0.1142  0.0853  -0.3028 1654 MET A CE  
1522 N  N   . ASP A 185 ? 1.3452 1.1381 1.5222 0.1349  0.1415  -0.3040 1655 ASP A N   
1523 C  CA  . ASP A 185 ? 1.3660 1.1971 1.5365 0.1375  0.1545  -0.3110 1655 ASP A CA  
1524 C  C   . ASP A 185 ? 1.2314 1.0640 1.3794 0.1252  0.1527  -0.3142 1655 ASP A C   
1525 O  O   . ASP A 185 ? 1.2359 1.0654 1.3668 0.1320  0.1525  -0.3337 1655 ASP A O   
1526 C  CB  . ASP A 185 ? 1.3807 1.2464 1.5670 0.1330  0.1656  -0.2939 1655 ASP A CB  
1527 C  CG  . ASP A 185 ? 1.5123 1.3790 1.7208 0.1453  0.1668  -0.2915 1655 ASP A CG  
1528 O  OD1 . ASP A 185 ? 1.5582 1.3920 1.7717 0.1497  0.1559  -0.2911 1655 ASP A OD1 
1529 O  OD2 . ASP A 185 ? 1.5647 1.4649 1.7851 0.1504  0.1781  -0.2902 1655 ASP A OD2 
1530 N  N   . LEU A 188 ? 1.5112 1.4421 1.6902 0.0986  0.1829  -0.2562 1658 LEU A N   
1531 C  CA  . LEU A 188 ? 1.5322 1.4752 1.7111 0.0830  0.1839  -0.2361 1658 LEU A CA  
1532 C  C   . LEU A 188 ? 1.5807 1.5210 1.7365 0.0726  0.1792  -0.2374 1658 LEU A C   
1533 O  O   . LEU A 188 ? 1.5498 1.4693 1.6928 0.0742  0.1709  -0.2504 1658 LEU A O   
1534 C  CB  . LEU A 188 ? 1.4722 1.3974 1.6679 0.0766  0.1761  -0.2198 1658 LEU A CB  
1535 C  CG  . LEU A 188 ? 1.3584 1.2911 1.5769 0.0798  0.1802  -0.2084 1658 LEU A CG  
1536 C  CD1 . LEU A 188 ? 1.2055 1.1148 1.4341 0.0729  0.1708  -0.1953 1658 LEU A CD1 
1537 C  CD2 . LEU A 188 ? 1.2557 1.2206 1.4794 0.0746  0.1910  -0.1968 1658 LEU A CD2 
1538 N  N   . GLU A 189 ? 1.6322 1.5932 1.7821 0.0620  0.1838  -0.2241 1659 GLU A N   
1539 C  CA  . GLU A 189 ? 1.6656 1.6232 1.7965 0.0506  0.1768  -0.2204 1659 GLU A CA  
1540 C  C   . GLU A 189 ? 1.6272 1.5687 1.7703 0.0407  0.1661  -0.2051 1659 GLU A C   
1541 O  O   . GLU A 189 ? 1.6886 1.6376 1.8482 0.0372  0.1689  -0.1892 1659 GLU A O   
1542 C  CB  . GLU A 189 ? 1.7014 1.6870 1.8195 0.0443  0.1859  -0.2120 1659 GLU A CB  
1543 C  CG  . GLU A 189 ? 1.7301 1.7409 1.8491 0.0526  0.2015  -0.2193 1659 GLU A CG  
1544 C  CD  . GLU A 189 ? 1.7026 1.7314 1.8411 0.0497  0.2098  -0.2028 1659 GLU A CD  
1545 O  OE1 . GLU A 189 ? 1.7017 1.7552 1.8324 0.0453  0.2205  -0.1975 1659 GLU A OE1 
1546 O  OE2 . GLU A 189 ? 1.6149 1.6327 1.7755 0.0512  0.2058  -0.1952 1659 GLU A OE2 
1547 N  N   . GLN A 190 ? 1.4239 1.3451 1.5591 0.0355  0.1541  -0.2098 1660 GLN A N   
1548 C  CA  . GLN A 190 ? 1.2658 1.1734 1.4147 0.0262  0.1446  -0.1967 1660 GLN A CA  
1549 C  C   . GLN A 190 ? 1.1816 1.0968 1.3203 0.0144  0.1379  -0.1880 1660 GLN A C   
1550 O  O   . GLN A 190 ? 1.0551 0.9572 1.1869 0.0082  0.1269  -0.1927 1660 GLN A O   
1551 C  CB  . GLN A 190 ? 1.2870 1.1645 1.4400 0.0280  0.1353  -0.2068 1660 GLN A CB  
1552 C  CG  . GLN A 190 ? 1.1979 1.0648 1.3537 0.0424  0.1397  -0.2207 1660 GLN A CG  
1553 C  CD  . GLN A 190 ? 1.1913 1.0680 1.3666 0.0491  0.1482  -0.2116 1660 GLN A CD  
1554 O  OE1 . GLN A 190 ? 1.2418 1.1377 1.4260 0.0442  0.1538  -0.1964 1660 GLN A OE1 
1555 N  NE2 . GLN A 190 ? 0.9372 0.7990 1.1190 0.0608  0.1483  -0.2214 1660 GLN A NE2 
1556 N  N   . VAL A 191 ? 1.2113 1.1476 1.3504 0.0111  0.1441  -0.1744 1661 VAL A N   
1557 C  CA  . VAL A 191 ? 1.2319 1.1764 1.3643 0.0010  0.1376  -0.1627 1661 VAL A CA  
1558 C  C   . VAL A 191 ? 1.0102 0.9655 1.1603 -0.0017 0.1421  -0.1438 1661 VAL A C   
1559 O  O   . VAL A 191 ? 0.9976 0.9604 1.1573 0.0036  0.1523  -0.1409 1661 VAL A O   
1560 C  CB  . VAL A 191 ? 1.3670 1.3249 1.4714 -0.0001 0.1396  -0.1677 1661 VAL A CB  
1561 C  CG1 . VAL A 191 ? 1.3953 1.3742 1.4963 0.0022  0.1533  -0.1603 1661 VAL A CG1 
1562 C  CG2 . VAL A 191 ? 1.3324 1.2910 1.4266 -0.0098 0.1274  -0.1604 1661 VAL A CG2 
1563 N  N   . LEU A 192 ? 0.9345 0.8905 1.0898 -0.0096 0.1338  -0.1320 1662 LEU A N   
1564 C  CA  . LEU A 192 ? 0.8934 0.8580 1.0648 -0.0114 0.1375  -0.1152 1662 LEU A CA  
1565 C  C   . LEU A 192 ? 0.9818 0.9635 1.1391 -0.0121 0.1447  -0.1079 1662 LEU A C   
1566 O  O   . LEU A 192 ? 1.0861 1.0732 1.2205 -0.0145 0.1426  -0.1114 1662 LEU A O   
1567 C  CB  . LEU A 192 ? 0.8872 0.8487 1.0699 -0.0185 0.1266  -0.1052 1662 LEU A CB  
1568 C  CG  . LEU A 192 ? 0.6633 0.6094 0.8605 -0.0206 0.1197  -0.1106 1662 LEU A CG  
1569 C  CD1 . LEU A 192 ? 0.8340 0.7816 1.0367 -0.0285 0.1077  -0.1051 1662 LEU A CD1 
1570 C  CD2 . LEU A 192 ? 0.6118 0.5529 0.8303 -0.0176 0.1258  -0.1050 1662 LEU A CD2 
1571 N  N   . PRO A 193 ? 0.8629 0.8528 1.0320 -0.0108 0.1532  -0.0978 1663 PRO A N   
1572 C  CA  . PRO A 193 ? 0.8893 0.8947 1.0451 -0.0130 0.1609  -0.0903 1663 PRO A CA  
1573 C  C   . PRO A 193 ? 0.9088 0.9161 1.0539 -0.0203 0.1524  -0.0775 1663 PRO A C   
1574 O  O   . PRO A 193 ? 1.0120 1.0129 1.1704 -0.0227 0.1432  -0.0694 1663 PRO A O   
1575 C  CB  . PRO A 193 ? 0.8878 0.8985 1.0632 -0.0107 0.1699  -0.0824 1663 PRO A CB  
1576 C  CG  . PRO A 193 ? 0.8911 0.8892 1.0875 -0.0057 0.1676  -0.0878 1663 PRO A CG  
1577 C  CD  . PRO A 193 ? 0.6851 0.6698 0.8793 -0.0081 0.1559  -0.0927 1663 PRO A CD  
1578 N  N   . ARG A 194 ? 0.9484 0.9650 1.0688 -0.0235 0.1552  -0.0760 1664 ARG A N   
1579 C  CA  . ARG A 194 ? 1.0058 1.0236 1.1116 -0.0299 0.1469  -0.0632 1664 ARG A CA  
1580 C  C   . ARG A 194 ? 0.9669 0.9928 1.0707 -0.0336 0.1545  -0.0480 1664 ARG A C   
1581 O  O   . ARG A 194 ? 0.9352 0.9703 1.0405 -0.0325 0.1679  -0.0499 1664 ARG A O   
1582 C  CB  . ARG A 194 ? 1.1138 1.1339 1.1885 -0.0321 0.1428  -0.0711 1664 ARG A CB  
1583 C  CG  . ARG A 194 ? 1.1568 1.1685 1.2303 -0.0288 0.1364  -0.0886 1664 ARG A CG  
1584 C  CD  . ARG A 194 ? 1.2460 1.2572 1.2908 -0.0325 0.1267  -0.0932 1664 ARG A CD  
1585 N  NE  . ARG A 194 ? 1.3786 1.3830 1.4313 -0.0361 0.1100  -0.0869 1664 ARG A NE  
1586 C  CZ  . ARG A 194 ? 1.4202 1.4154 1.4906 -0.0355 0.1014  -0.0946 1664 ARG A CZ  
1587 N  NH1 . ARG A 194 ? 1.3565 1.3497 1.4355 -0.0393 0.0868  -0.0884 1664 ARG A NH1 
1588 N  NH2 . ARG A 194 ? 1.4389 1.4272 1.5189 -0.0313 0.1070  -0.1085 1664 ARG A NH2 
1589 N  N   . ASP A 195 ? 0.9924 1.0145 1.0942 -0.0379 0.1454  -0.0330 1665 ASP A N   
1590 C  CA  . ASP A 195 ? 1.0341 1.0594 1.1326 -0.0425 0.1504  -0.0172 1665 ASP A CA  
1591 C  C   . ASP A 195 ? 1.0310 1.0598 1.0955 -0.0487 0.1488  -0.0109 1665 ASP A C   
1592 O  O   . ASP A 195 ? 0.9337 0.9641 0.9769 -0.0488 0.1455  -0.0203 1665 ASP A O   
1593 C  CB  . ASP A 195 ? 0.9706 0.9872 1.0899 -0.0422 0.1414  -0.0041 1665 ASP A CB  
1594 C  CG  . ASP A 195 ? 1.0035 1.0133 1.1168 -0.0428 0.1244  0.0005  1665 ASP A CG  
1595 O  OD1 . ASP A 195 ? 1.0277 1.0388 1.1165 -0.0450 0.1188  -0.0031 1665 ASP A OD1 
1596 O  OD2 . ASP A 195 ? 0.9880 0.9921 1.1214 -0.0408 0.1164  0.0074  1665 ASP A OD2 
1597 N  N   . GLU A 196 ? 0.9484 0.9764 1.0063 -0.0544 0.1503  0.0057  1666 GLU A N   
1598 C  CA  . GLU A 196 ? 1.1014 1.1308 1.1250 -0.0615 0.1490  0.0146  1666 GLU A CA  
1599 C  C   . GLU A 196 ? 1.1054 1.1261 1.1132 -0.0612 0.1311  0.0168  1666 GLU A C   
1600 O  O   . GLU A 196 ? 1.2054 1.2271 1.1803 -0.0662 0.1287  0.0206  1666 GLU A O   
1601 C  CB  . GLU A 196 ? 1.2165 1.2426 1.2382 -0.0683 0.1526  0.0336  1666 GLU A CB  
1602 C  CG  . GLU A 196 ? 1.2364 1.2491 1.2813 -0.0656 0.1412  0.0449  1666 GLU A CG  
1603 C  CD  . GLU A 196 ? 1.2633 1.2686 1.3017 -0.0727 0.1422  0.0640  1666 GLU A CD  
1604 O  OE1 . GLU A 196 ? 1.2408 1.2417 1.3037 -0.0714 0.1445  0.0689  1666 GLU A OE1 
1605 O  OE2 . GLU A 196 ? 1.3100 1.3126 1.3174 -0.0799 0.1404  0.0742  1666 GLU A OE2 
1606 N  N   . ARG A 197 ? 1.0599 1.0735 1.0901 -0.0559 0.1185  0.0146  1667 ARG A N   
1607 C  CA  . ARG A 197 ? 1.0647 1.0730 1.0833 -0.0553 0.1007  0.0150  1667 ARG A CA  
1608 C  C   . ARG A 197 ? 1.1139 1.1264 1.1207 -0.0538 0.0988  -0.0031 1667 ARG A C   
1609 O  O   . ARG A 197 ? 1.0848 1.0943 1.0800 -0.0541 0.0838  -0.0047 1667 ARG A O   
1610 C  CB  . ARG A 197 ? 1.0059 1.0079 1.0544 -0.0507 0.0877  0.0192  1667 ARG A CB  
1611 C  CG  . ARG A 197 ? 1.0314 1.0265 1.0911 -0.0508 0.0855  0.0366  1667 ARG A CG  
1612 C  CD  . ARG A 197 ? 0.9875 0.9799 1.0824 -0.0448 0.0774  0.0361  1667 ARG A CD  
1613 N  NE  . ARG A 197 ? 0.9144 0.9116 1.0318 -0.0419 0.0857  0.0217  1667 ARG A NE  
1614 C  CZ  . ARG A 197 ? 0.8273 0.8246 0.9722 -0.0379 0.0798  0.0169  1667 ARG A CZ  
1615 N  NH1 . ARG A 197 ? 0.6001 0.5958 0.7557 -0.0355 0.0660  0.0243  1667 ARG A NH1 
1616 N  NH2 . ARG A 197 ? 0.7358 0.7351 0.8974 -0.0362 0.0877  0.0049  1667 ARG A NH2 
1617 N  N   . GLY A 198 ? 1.1282 1.1467 1.1387 -0.0518 0.1126  -0.0174 1668 GLY A N   
1618 C  CA  . GLY A 198 ? 1.3258 1.3446 1.3304 -0.0491 0.1095  -0.0359 1668 GLY A CA  
1619 C  C   . GLY A 198 ? 1.3461 1.3584 1.3794 -0.0456 0.0992  -0.0423 1668 GLY A C   
1620 O  O   . GLY A 198 ? 1.4592 1.4688 1.4872 -0.0451 0.0911  -0.0551 1668 GLY A O   
1621 N  N   . ALA A 199 ? 1.0762 1.0859 1.1388 -0.0438 0.0991  -0.0334 1669 ALA A N   
1622 C  CA  . ALA A 199 ? 0.9032 0.9084 0.9950 -0.0412 0.0918  -0.0382 1669 ALA A CA  
1623 C  C   . ALA A 199 ? 0.8724 0.8764 0.9874 -0.0376 0.1046  -0.0432 1669 ALA A C   
1624 O  O   . ALA A 199 ? 0.8361 0.8437 0.9508 -0.0368 0.1171  -0.0387 1669 ALA A O   
1625 C  CB  . ALA A 199 ? 0.9214 0.9253 1.0283 -0.0415 0.0797  -0.0243 1669 ALA A CB  
1626 N  N   . TYR A 200 ? 0.9452 0.9439 1.0798 -0.0359 0.1009  -0.0524 1670 TYR A N   
1627 C  CA  . TYR A 200 ? 0.9019 0.8971 1.0603 -0.0324 0.1100  -0.0556 1670 TYR A CA  
1628 C  C   . TYR A 200 ? 0.8483 0.8458 1.0224 -0.0316 0.1143  -0.0409 1670 TYR A C   
1629 O  O   . TYR A 200 ? 0.8296 0.8276 1.0112 -0.0330 0.1056  -0.0305 1670 TYR A O   
1630 C  CB  . TYR A 200 ? 0.7871 0.7752 0.9636 -0.0331 0.1020  -0.0633 1670 TYR A CB  
1631 C  CG  . TYR A 200 ? 0.6827 0.6656 0.8859 -0.0308 0.1076  -0.0627 1670 TYR A CG  
1632 C  CD1 . TYR A 200 ? 0.6530 0.6331 0.8595 -0.0264 0.1197  -0.0667 1670 TYR A CD1 
1633 C  CD2 . TYR A 200 ? 0.6375 0.6194 0.8622 -0.0331 0.1004  -0.0586 1670 TYR A CD2 
1634 C  CE1 . TYR A 200 ? 0.5447 0.5189 0.7731 -0.0244 0.1237  -0.0658 1670 TYR A CE1 
1635 C  CE2 . TYR A 200 ? 0.5049 0.4820 0.7513 -0.0317 0.1057  -0.0578 1670 TYR A CE2 
1636 C  CZ  . TYR A 200 ? 0.5447 0.5167 0.7916 -0.0274 0.1169  -0.0611 1670 TYR A CZ  
1637 O  OH  . TYR A 200 ? 0.5891 0.5553 0.8553 -0.0260 0.1212  -0.0596 1670 TYR A OH  
1638 N  N   . GLU A 201 ? 0.7810 0.7802 0.9601 -0.0290 0.1272  -0.0409 1671 GLU A N   
1639 C  CA  . GLU A 201 ? 0.6883 0.6901 0.8754 -0.0294 0.1321  -0.0272 1671 GLU A CA  
1640 C  C   . GLU A 201 ? 0.7700 0.7673 0.9816 -0.0283 0.1262  -0.0199 1671 GLU A C   
1641 O  O   . GLU A 201 ? 0.6174 0.6148 0.8330 -0.0290 0.1245  -0.0074 1671 GLU A O   
1642 C  CB  . GLU A 201 ? 0.7642 0.7702 0.9552 -0.0270 0.1465  -0.0303 1671 GLU A CB  
1643 C  CG  . GLU A 201 ? 0.9114 0.9126 1.1203 -0.0219 0.1506  -0.0409 1671 GLU A CG  
1644 C  CD  . GLU A 201 ? 0.9850 0.9914 1.2025 -0.0187 0.1630  -0.0416 1671 GLU A CD  
1645 O  OE1 . GLU A 201 ? 0.7809 0.7974 0.9854 -0.0195 0.1713  -0.0429 1671 GLU A OE1 
1646 O  OE2 . GLU A 201 ? 0.8825 0.8838 1.1201 -0.0156 0.1642  -0.0411 1671 GLU A OE2 
1647 N  N   . ALA A 202 ? 0.7020 0.6950 0.9291 -0.0269 0.1226  -0.0275 1672 ALA A N   
1648 C  CA  . ALA A 202 ? 0.5914 0.5824 0.8421 -0.0261 0.1182  -0.0222 1672 ALA A CA  
1649 C  C   . ALA A 202 ? 0.6331 0.6269 0.8865 -0.0281 0.1048  -0.0190 1672 ALA A C   
1650 O  O   . ALA A 202 ? 0.5113 0.5061 0.7852 -0.0272 0.1010  -0.0154 1672 ALA A O   
1651 C  CB  . ALA A 202 ? 0.5515 0.5368 0.8179 -0.0247 0.1222  -0.0309 1672 ALA A CB  
1652 N  N   . SER A 203 ? 0.6795 0.6756 0.9129 -0.0305 0.0975  -0.0204 1673 SER A N   
1653 C  CA  . SER A 203 ? 0.8075 0.8073 1.0441 -0.0322 0.0833  -0.0198 1673 SER A CA  
1654 C  C   . SER A 203 ? 0.7577 0.7600 0.9916 -0.0308 0.0758  -0.0062 1673 SER A C   
1655 O  O   . SER A 203 ? 0.6987 0.6991 0.9122 -0.0313 0.0782  0.0008  1673 SER A O   
1656 C  CB  . SER A 203 ? 0.9510 0.9508 1.1664 -0.0354 0.0773  -0.0297 1673 SER A CB  
1657 O  OG  . SER A 203 ? 1.1486 1.1532 1.3560 -0.0369 0.0630  -0.0251 1673 SER A OG  
1658 N  N   . LEU A 204 ? 0.7240 0.7305 0.9787 -0.0290 0.0669  -0.0025 1674 LEU A N   
1659 C  CA  . LEU A 204 ? 0.7414 0.7489 0.9954 -0.0260 0.0576  0.0097  1674 LEU A CA  
1660 C  C   . LEU A 204 ? 0.7399 0.7497 0.9730 -0.0278 0.0440  0.0107  1674 LEU A C   
1661 O  O   . LEU A 204 ? 0.7174 0.7236 0.9361 -0.0264 0.0376  0.0217  1674 LEU A O   
1662 C  CB  . LEU A 204 ? 0.6568 0.6700 0.9417 -0.0220 0.0525  0.0119  1674 LEU A CB  
1663 C  CG  . LEU A 204 ? 0.5914 0.6030 0.8982 -0.0199 0.0642  0.0111  1674 LEU A CG  
1664 C  CD1 . LEU A 204 ? 0.6945 0.7135 1.0284 -0.0152 0.0582  0.0140  1674 LEU A CD1 
1665 C  CD2 . LEU A 204 ? 0.6039 0.6064 0.9008 -0.0187 0.0747  0.0180  1674 LEU A CD2 
1666 N  N   . VAL A 205 ? 0.9264 0.9405 1.1559 -0.0313 0.0388  -0.0005 1675 VAL A N   
1667 C  CA  . VAL A 205 ? 1.0304 1.0467 1.2383 -0.0333 0.0253  -0.0012 1675 VAL A CA  
1668 C  C   . VAL A 205 ? 1.2555 1.2662 1.4303 -0.0368 0.0328  -0.0052 1675 VAL A C   
1669 O  O   . VAL A 205 ? 1.2190 1.2280 1.3922 -0.0388 0.0422  -0.0168 1675 VAL A O   
1670 C  CB  . VAL A 205 ? 0.9984 1.0233 1.2208 -0.0359 0.0140  -0.0118 1675 VAL A CB  
1671 C  CG1 . VAL A 205 ? 1.0134 1.0355 1.2420 -0.0401 0.0238  -0.0256 1675 VAL A CG1 
1672 C  CG2 . VAL A 205 ? 1.0594 1.0864 1.2574 -0.0380 -0.0010 -0.0129 1675 VAL A CG2 
1673 N  N   . ALA A 206 ? 1.4689 1.4766 1.6170 -0.0372 0.0290  0.0043  1676 ALA A N   
1674 C  CA  . ALA A 206 ? 1.6274 1.6328 1.7418 -0.0410 0.0350  -0.0003 1676 ALA A CA  
1675 C  C   . ALA A 206 ? 1.7088 1.7174 1.8104 -0.0434 0.0216  -0.0104 1676 ALA A C   
1676 O  O   . ALA A 206 ? 1.6469 1.6571 1.7393 -0.0432 0.0057  -0.0041 1676 ALA A O   
1677 C  CB  . ALA A 206 ? 1.6355 1.6362 1.7238 -0.0423 0.0367  0.0142  1676 ALA A CB  
1678 N  N   . ALA A 207 ? 1.8106 1.8194 1.9125 -0.0453 0.0267  -0.0263 1677 ALA A N   
1679 C  CA  . ALA A 207 ? 1.8792 1.8899 1.9698 -0.0483 0.0138  -0.0377 1677 ALA A CA  
1680 C  C   . ALA A 207 ? 1.8737 1.8839 1.9255 -0.0501 0.0064  -0.0335 1677 ALA A C   
1681 O  O   . ALA A 207 ? 1.9072 1.9202 1.9511 -0.0513 -0.0111 -0.0337 1677 ALA A O   
1682 C  CB  . ALA A 207 ? 1.9102 1.9170 2.0015 -0.0500 0.0222  -0.0554 1677 ALA A CB  
1683 N  N   . SER A 208 ? 1.7745 1.7819 1.8017 -0.0506 0.0195  -0.0291 1678 SER A N   
1684 C  CA  . SER A 208 ? 1.6812 1.6876 1.6682 -0.0532 0.0155  -0.0233 1678 SER A CA  
1685 C  C   . SER A 208 ? 1.7058 1.7106 1.6896 -0.0524 -0.0003 -0.0061 1678 SER A C   
1686 O  O   . SER A 208 ? 1.5660 1.5722 1.5393 -0.0529 -0.0185 -0.0070 1678 SER A O   
1687 C  CB  . SER A 208 ? 1.5231 1.5291 1.4913 -0.0546 0.0352  -0.0198 1678 SER A CB  
1688 O  OG  . SER A 208 ? 1.4372 1.4410 1.3758 -0.0577 0.0324  -0.0044 1678 SER A OG  
1689 N  N   . THR A 209 ? 1.8506 1.8520 1.8446 -0.0507 0.0054  0.0093  1679 THR A N   
1690 C  CA  . THR A 209 ? 1.8705 1.8672 1.8601 -0.0489 -0.0093 0.0266  1679 THR A CA  
1691 C  C   . THR A 209 ? 1.8820 1.8837 1.9020 -0.0442 -0.0272 0.0249  1679 THR A C   
1692 O  O   . THR A 209 ? 1.9883 1.9918 1.9966 -0.0437 -0.0460 0.0259  1679 THR A O   
1693 C  CB  . THR A 209 ? 1.7657 1.7556 1.7619 -0.0483 0.0016  0.0418  1679 THR A CB  
1694 O  OG1 . THR A 209 ? 1.7394 1.7313 1.7776 -0.0434 0.0044  0.0406  1679 THR A OG1 
1695 C  CG2 . THR A 209 ? 1.6775 1.6677 1.6552 -0.0533 0.0229  0.0394  1679 THR A CG2 
1696 N  N   . GLY A 210 ? 1.7450 1.7504 1.8040 -0.0408 -0.0218 0.0220  1680 GLY A N   
1697 C  CA  . GLY A 210 ? 1.6070 1.6199 1.6987 -0.0364 -0.0360 0.0208  1680 GLY A CA  
1698 C  C   . GLY A 210 ? 1.5878 1.5977 1.7003 -0.0301 -0.0391 0.0349  1680 GLY A C   
1699 O  O   . GLY A 210 ? 1.5503 1.5667 1.6826 -0.0252 -0.0549 0.0372  1680 GLY A O   
1700 N  N   . VAL A 211 ? 1.5873 1.5882 1.6967 -0.0300 -0.0249 0.0438  1681 VAL A N   
1701 C  CA  . VAL A 211 ? 1.4631 1.4592 1.5944 -0.0241 -0.0251 0.0551  1681 VAL A CA  
1702 C  C   . VAL A 211 ? 1.3699 1.3706 1.5333 -0.0232 -0.0100 0.0472  1681 VAL A C   
1703 O  O   . VAL A 211 ? 1.4286 1.4283 1.5863 -0.0275 0.0061  0.0406  1681 VAL A O   
1704 C  CB  . VAL A 211 ? 1.3761 1.3572 1.4815 -0.0258 -0.0206 0.0711  1681 VAL A CB  
1705 C  CG1 . VAL A 211 ? 1.1896 1.1633 1.3182 -0.0194 -0.0214 0.0815  1681 VAL A CG1 
1706 C  CG2 . VAL A 211 ? 1.3954 1.3702 1.4649 -0.0275 -0.0356 0.0799  1681 VAL A CG2 
1707 N  N   . ARG A 212 ? 1.2005 1.2068 1.3973 -0.0170 -0.0154 0.0475  1682 ARG A N   
1708 C  CA  . ARG A 212 ? 0.9213 0.9316 1.1482 -0.0158 -0.0022 0.0413  1682 ARG A CA  
1709 C  C   . ARG A 212 ? 0.8170 0.8155 1.0432 -0.0138 0.0082  0.0517  1682 ARG A C   
1710 O  O   . ARG A 212 ? 0.8972 0.8889 1.1254 -0.0086 0.0000  0.0628  1682 ARG A O   
1711 C  CB  . ARG A 212 ? 0.8436 0.8667 1.1053 -0.0106 -0.0116 0.0370  1682 ARG A CB  
1712 C  CG  . ARG A 212 ? 0.8944 0.9305 1.1647 -0.0151 -0.0161 0.0237  1682 ARG A CG  
1713 C  CD  . ARG A 212 ? 1.0557 1.0927 1.3397 -0.0194 0.0003  0.0139  1682 ARG A CD  
1714 N  NE  . ARG A 212 ? 1.0427 1.0824 1.3557 -0.0146 0.0071  0.0163  1682 ARG A NE  
1715 C  CZ  . ARG A 212 ? 1.1117 1.1654 1.4556 -0.0129 0.0029  0.0115  1682 ARG A CZ  
1716 N  NH1 . ARG A 212 ? 1.0987 1.1652 1.4499 -0.0162 -0.0085 0.0043  1682 ARG A NH1 
1717 N  NH2 . ARG A 212 ? 1.1018 1.1576 1.4691 -0.0083 0.0103  0.0135  1682 ARG A NH2 
1718 N  N   . ALA A 213 ? 0.7122 0.7075 0.9339 -0.0180 0.0253  0.0480  1683 ALA A N   
1719 C  CA  . ALA A 213 ? 0.8109 0.7966 1.0349 -0.0172 0.0358  0.0562  1683 ALA A CA  
1720 C  C   . ALA A 213 ? 0.6696 0.6582 0.9276 -0.0115 0.0387  0.0539  1683 ALA A C   
1721 O  O   . ALA A 213 ? 0.7112 0.7100 0.9899 -0.0107 0.0396  0.0438  1683 ALA A O   
1722 C  CB  . ALA A 213 ? 0.8492 0.8332 1.0586 -0.0232 0.0525  0.0521  1683 ALA A CB  
1723 N  N   . LEU A 214 ? 0.7398 0.7185 1.0021 -0.0083 0.0406  0.0635  1684 LEU A N   
1724 C  CA  . LEU A 214 ? 0.5750 0.5554 0.8666 -0.0029 0.0448  0.0610  1684 LEU A CA  
1725 C  C   . LEU A 214 ? 0.6949 0.6771 0.9927 -0.0066 0.0616  0.0532  1684 LEU A C   
1726 O  O   . LEU A 214 ? 0.7083 0.6859 0.9881 -0.0120 0.0708  0.0543  1684 LEU A O   
1727 C  CB  . LEU A 214 ? 0.6355 0.6024 0.9281 0.0018  0.0413  0.0727  1684 LEU A CB  
1728 C  CG  . LEU A 214 ? 0.7387 0.7005 1.0269 0.0076  0.0234  0.0815  1684 LEU A CG  
1729 C  CD1 . LEU A 214 ? 0.7684 0.7143 1.0612 0.0131  0.0206  0.0914  1684 LEU A CD1 
1730 C  CD2 . LEU A 214 ? 0.6143 0.5926 0.9254 0.0136  0.0132  0.0732  1684 LEU A CD2 
1731 N  N   . PRO A 215 ? 0.6178 0.6073 0.9406 -0.0039 0.0658  0.0454  1685 PRO A N   
1732 C  CA  . PRO A 215 ? 0.5550 0.5440 0.8829 -0.0067 0.0805  0.0391  1685 PRO A CA  
1733 C  C   . PRO A 215 ? 0.6563 0.6364 0.9904 -0.0042 0.0873  0.0447  1685 PRO A C   
1734 O  O   . PRO A 215 ? 0.5845 0.5630 0.9338 0.0016  0.0828  0.0480  1685 PRO A O   
1735 C  CB  . PRO A 215 ? 0.5643 0.5639 0.9142 -0.0058 0.0807  0.0293  1685 PRO A CB  
1736 C  CG  . PRO A 215 ? 0.5725 0.5785 0.9376 -0.0002 0.0686  0.0323  1685 PRO A CG  
1737 C  CD  . PRO A 215 ? 0.4584 0.4590 0.8043 0.0008  0.0572  0.0410  1685 PRO A CD  
1738 N  N   . CYS A 216 ? 0.4484 0.4239 0.7723 -0.0082 0.0982  0.0448  1686 CYS A N   
1739 C  CA  . CYS A 216 ? 0.4291 0.3964 0.7583 -0.0070 0.1043  0.0496  1686 CYS A CA  
1740 C  C   . CYS A 216 ? 0.5165 0.4863 0.8691 -0.0024 0.1082  0.0437  1686 CYS A C   
1741 O  O   . CYS A 216 ? 0.4442 0.4208 0.8045 -0.0032 0.1127  0.0350  1686 CYS A O   
1742 C  CB  . CYS A 216 ? 0.4351 0.4008 0.7507 -0.0128 0.1154  0.0492  1686 CYS A CB  
1743 S  SG  . CYS A 216 ? 0.5573 0.5157 0.8814 -0.0129 0.1241  0.0525  1686 CYS A SG  
1744 N  N   . LEU A 217 ? 0.4495 0.4126 0.8121 0.0022  0.1061  0.0484  1687 LEU A N   
1745 C  CA  . LEU A 217 ? 0.4122 0.3779 0.7952 0.0069  0.1099  0.0429  1687 LEU A CA  
1746 C  C   . LEU A 217 ? 0.3753 0.3397 0.7592 0.0041  0.1217  0.0381  1687 LEU A C   
1747 O  O   . LEU A 217 ? 0.4214 0.3891 0.8190 0.0066  0.1260  0.0324  1687 LEU A O   
1748 C  CB  . LEU A 217 ? 0.4385 0.3956 0.8297 0.0132  0.1047  0.0483  1687 LEU A CB  
1749 C  CG  . LEU A 217 ? 0.5138 0.4754 0.9162 0.0203  0.0933  0.0492  1687 LEU A CG  
1750 C  CD1 . LEU A 217 ? 0.5539 0.5025 0.9607 0.0273  0.0873  0.0551  1687 LEU A CD1 
1751 C  CD2 . LEU A 217 ? 0.6086 0.5856 1.0311 0.0231  0.0958  0.0398  1687 LEU A CD2 
1752 N  N   . ILE A 218 ? 0.3798 0.3405 0.7496 -0.0009 0.1269  0.0402  1688 ILE A N   
1753 C  CA  . ILE A 218 ? 0.3831 0.3433 0.7541 -0.0027 0.1368  0.0359  1688 ILE A CA  
1754 C  C   . ILE A 218 ? 0.4107 0.3775 0.7773 -0.0052 0.1413  0.0281  1688 ILE A C   
1755 O  O   . ILE A 218 ? 0.4372 0.4045 0.8109 -0.0041 0.1467  0.0221  1688 ILE A O   
1756 C  CB  . ILE A 218 ? 0.4509 0.4050 0.8125 -0.0064 0.1401  0.0420  1688 ILE A CB  
1757 C  CG1 . ILE A 218 ? 0.4777 0.4213 0.8434 -0.0041 0.1347  0.0495  1688 ILE A CG1 
1758 C  CG2 . ILE A 218 ? 0.4268 0.3831 0.7910 -0.0078 0.1495  0.0367  1688 ILE A CG2 
1759 C  CD1 . ILE A 218 ? 0.4138 0.3541 0.7959 0.0018  0.1355  0.0455  1688 ILE A CD1 
1760 N  N   . THR A 219 ? 0.3763 0.3467 0.7296 -0.0083 0.1387  0.0281  1689 THR A N   
1761 C  CA  . THR A 219 ? 0.3998 0.3744 0.7476 -0.0101 0.1425  0.0198  1689 THR A CA  
1762 C  C   . THR A 219 ? 0.5568 0.5356 0.9042 -0.0108 0.1358  0.0156  1689 THR A C   
1763 O  O   . THR A 219 ? 0.4895 0.4694 0.8343 -0.0122 0.1381  0.0077  1689 THR A O   
1764 C  CB  . THR A 219 ? 0.4665 0.4433 0.7977 -0.0136 0.1471  0.0200  1689 THR A CB  
1765 O  OG1 . THR A 219 ? 0.4209 0.3987 0.7382 -0.0163 0.1408  0.0256  1689 THR A OG1 
1766 C  CG2 . THR A 219 ? 0.5344 0.5096 0.8671 -0.0145 0.1538  0.0238  1689 THR A CG2 
1767 N  N   . GLY A 220 ? 0.5197 0.5005 0.8695 -0.0098 0.1268  0.0204  1690 GLY A N   
1768 C  CA  . GLY A 220 ? 0.4119 0.3984 0.7615 -0.0111 0.1193  0.0164  1690 GLY A CA  
1769 C  C   . GLY A 220 ? 0.4995 0.4872 0.8283 -0.0144 0.1153  0.0165  1690 GLY A C   
1770 O  O   . GLY A 220 ? 0.4767 0.4691 0.8037 -0.0154 0.1062  0.0148  1690 GLY A O   
1771 N  N   . TYR A 221 ? 0.4577 0.4428 0.7709 -0.0164 0.1217  0.0179  1691 TYR A N   
1772 C  CA  . TYR A 221 ? 0.5519 0.5389 0.8429 -0.0199 0.1200  0.0170  1691 TYR A CA  
1773 C  C   . TYR A 221 ? 0.5482 0.5342 0.8287 -0.0205 0.1099  0.0268  1691 TYR A C   
1774 O  O   . TYR A 221 ? 0.5604 0.5422 0.8489 -0.0181 0.1063  0.0355  1691 TYR A O   
1775 C  CB  . TYR A 221 ? 0.5098 0.4970 0.7889 -0.0219 0.1310  0.0162  1691 TYR A CB  
1776 C  CG  . TYR A 221 ? 0.5943 0.5835 0.8727 -0.0213 0.1378  0.0039  1691 TYR A CG  
1777 C  CD1 . TYR A 221 ? 0.5851 0.5715 0.8796 -0.0189 0.1383  -0.0029 1691 TYR A CD1 
1778 C  CD2 . TYR A 221 ? 0.6007 0.5941 0.8616 -0.0230 0.1438  -0.0010 1691 TYR A CD2 
1779 C  CE1 . TYR A 221 ? 0.5367 0.5215 0.8298 -0.0178 0.1432  -0.0136 1691 TYR A CE1 
1780 C  CE2 . TYR A 221 ? 0.7141 0.7080 0.9750 -0.0208 0.1492  -0.0132 1691 TYR A CE2 
1781 C  CZ  . TYR A 221 ? 0.5696 0.5576 0.8464 -0.0181 0.1482  -0.0192 1691 TYR A CZ  
1782 O  OH  . TYR A 221 ? 0.5008 0.4857 0.7770 -0.0154 0.1521  -0.0308 1691 TYR A OH  
1783 N  N   . PRO A 222 ? 0.5467 0.5352 0.8079 -0.0233 0.1044  0.0256  1692 PRO A N   
1784 C  CA  . PRO A 222 ? 0.4965 0.4822 0.7437 -0.0240 0.0940  0.0360  1692 PRO A CA  
1785 C  C   . PRO A 222 ? 0.6838 0.6628 0.9192 -0.0264 0.0993  0.0472  1692 PRO A C   
1786 O  O   . PRO A 222 ? 0.6078 0.5886 0.8328 -0.0303 0.1105  0.0456  1692 PRO A O   
1787 C  CB  . PRO A 222 ? 0.6133 0.6031 0.8388 -0.0273 0.0895  0.0305  1692 PRO A CB  
1788 C  CG  . PRO A 222 ? 0.6711 0.6639 0.8936 -0.0290 0.1018  0.0189  1692 PRO A CG  
1789 C  CD  . PRO A 222 ? 0.5381 0.5303 0.7872 -0.0257 0.1071  0.0144  1692 PRO A CD  
1790 N  N   . ILE A 223 ? 0.7123 0.6838 0.9504 -0.0243 0.0909  0.0584  1693 ILE A N   
1791 C  CA  . ILE A 223 ? 0.7973 0.7594 1.0224 -0.0280 0.0938  0.0705  1693 ILE A CA  
1792 C  C   . ILE A 223 ? 0.8065 0.7675 1.0002 -0.0337 0.0900  0.0765  1693 ILE A C   
1793 O  O   . ILE A 223 ? 0.8161 0.7741 1.0006 -0.0319 0.0765  0.0809  1693 ILE A O   
1794 C  CB  . ILE A 223 ? 0.8528 0.8040 1.0908 -0.0230 0.0851  0.0800  1693 ILE A CB  
1795 C  CG1 . ILE A 223 ? 0.6859 0.6405 0.9539 -0.0168 0.0883  0.0723  1693 ILE A CG1 
1796 C  CG2 . ILE A 223 ? 0.8214 0.7606 1.0473 -0.0283 0.0893  0.0920  1693 ILE A CG2 
1797 C  CD1 . ILE A 223 ? 0.5919 0.5365 0.8740 -0.0109 0.0814  0.0793  1693 ILE A CD1 
1798 N  N   . LEU A 224 ? 0.7849 0.7495 0.9619 -0.0405 0.1021  0.0760  1694 LEU A N   
1799 C  CA  . LEU A 224 ? 0.8790 0.8441 1.0237 -0.0470 0.1011  0.0809  1694 LEU A CA  
1800 C  C   . LEU A 224 ? 0.8929 0.8480 1.0208 -0.0541 0.1032  0.0966  1694 LEU A C   
1801 O  O   . LEU A 224 ? 0.9644 0.9149 1.0639 -0.0591 0.0980  0.1053  1694 LEU A O   
1802 C  CB  . LEU A 224 ? 0.8431 0.8214 0.9779 -0.0502 0.1139  0.0685  1694 LEU A CB  
1803 C  CG  . LEU A 224 ? 0.8039 0.7898 0.9505 -0.0448 0.1122  0.0526  1694 LEU A CG  
1804 C  CD1 . LEU A 224 ? 0.7236 0.7194 0.8525 -0.0478 0.1222  0.0417  1694 LEU A CD1 
1805 C  CD2 . LEU A 224 ? 0.8938 0.8763 1.0381 -0.0417 0.0953  0.0539  1694 LEU A CD2 
1806 N  N   . ARG A 225 ? 0.7343 0.6851 0.8778 -0.0552 0.1105  0.1004  1695 ARG A N   
1807 C  CA  . ARG A 225 ? 0.8769 0.8171 1.0070 -0.0635 0.1132  0.1151  1695 ARG A CA  
1808 C  C   . ARG A 225 ? 0.8300 0.7613 0.9858 -0.0603 0.1137  0.1177  1695 ARG A C   
1809 O  O   . ARG A 225 ? 0.7586 0.6962 0.9396 -0.0535 0.1167  0.1068  1695 ARG A O   
1810 C  CB  . ARG A 225 ? 0.8261 0.7786 0.9406 -0.0734 0.1294  0.1134  1695 ARG A CB  
1811 C  CG  . ARG A 225 ? 0.8654 0.8312 1.0040 -0.0714 0.1430  0.1008  1695 ARG A CG  
1812 C  CD  . ARG A 225 ? 0.9519 0.9362 1.0796 -0.0773 0.1585  0.0930  1695 ARG A CD  
1813 N  NE  . ARG A 225 ? 1.1473 1.1381 1.2485 -0.0789 0.1574  0.0895  1695 ARG A NE  
1814 C  CZ  . ARG A 225 ? 1.3269 1.3348 1.4176 -0.0817 0.1699  0.0796  1695 ARG A CZ  
1815 N  NH1 . ARG A 225 ? 1.2973 1.3185 1.4038 -0.0826 0.1839  0.0725  1695 ARG A NH1 
1816 N  NH2 . ARG A 225 ? 1.4133 1.4256 1.4780 -0.0828 0.1681  0.0760  1695 ARG A NH2 
1817 N  N   . ASN A 226 ? 0.8987 0.8140 1.0463 -0.0658 0.1107  0.1322  1696 ASN A N   
1818 C  CA  . ASN A 226 ? 0.7533 0.6585 0.9221 -0.0644 0.1118  0.1349  1696 ASN A CA  
1819 C  C   . ASN A 226 ? 0.7389 0.6384 0.9315 -0.0514 0.1010  0.1298  1696 ASN A C   
1820 O  O   . ASN A 226 ? 0.8021 0.7033 1.0184 -0.0470 0.1054  0.1230  1696 ASN A O   
1821 C  CB  . ASN A 226 ? 0.6476 0.5672 0.8308 -0.0681 0.1280  0.1257  1696 ASN A CB  
1822 C  CG  . ASN A 226 ? 0.9165 0.8373 1.0848 -0.0817 0.1382  0.1341  1696 ASN A CG  
1823 O  OD1 . ASN A 226 ? 0.9957 0.9030 1.1420 -0.0896 0.1335  0.1485  1696 ASN A OD1 
1824 N  ND2 . ASN A 226 ? 0.9558 0.8928 1.1360 -0.0849 0.1521  0.1254  1696 ASN A ND2 
1825 N  N   . LYS A 227 ? 0.6943 0.5886 0.8808 -0.0453 0.0869  0.1327  1697 LYS A N   
1826 C  CA  . LYS A 227 ? 0.8173 0.7098 1.0277 -0.0330 0.0771  0.1274  1697 LYS A CA  
1827 C  C   . LYS A 227 ? 0.9164 0.7896 1.1368 -0.0300 0.0718  0.1353  1697 LYS A C   
1828 O  O   . LYS A 227 ? 0.9742 0.8293 1.1769 -0.0352 0.0663  0.1491  1697 LYS A O   
1829 C  CB  . LYS A 227 ? 0.8027 0.6962 1.0050 -0.0273 0.0623  0.1286  1697 LYS A CB  
1830 C  CG  . LYS A 227 ? 0.9277 0.8219 1.1554 -0.0146 0.0512  0.1235  1697 LYS A CG  
1831 C  CD  . LYS A 227 ? 0.9879 0.8914 1.2113 -0.0101 0.0389  0.1206  1697 LYS A CD  
1832 C  CE  . LYS A 227 ? 0.9441 0.8320 1.1555 -0.0055 0.0206  0.1332  1697 LYS A CE  
1833 N  NZ  . LYS A 227 ? 0.8875 0.7866 1.1002 0.0005  0.0067  0.1290  1697 LYS A NZ  
1834 N  N   . ILE A 228 ? 0.8317 0.7075 1.0790 -0.0222 0.0738  0.1267  1698 ILE A N   
1835 C  CA  . ILE A 228 ? 0.8016 0.6598 1.0611 -0.0161 0.0667  0.1312  1698 ILE A CA  
1836 C  C   . ILE A 228 ? 0.7508 0.6151 1.0317 -0.0025 0.0575  0.1233  1698 ILE A C   
1837 O  O   . ILE A 228 ? 0.6936 0.5770 0.9887 0.0007  0.0627  0.1115  1698 ILE A O   
1838 C  CB  . ILE A 228 ? 0.8022 0.6576 1.0738 -0.0198 0.0780  0.1278  1698 ILE A CB  
1839 C  CG1 . ILE A 228 ? 0.5939 0.4688 0.8862 -0.0155 0.0878  0.1127  1698 ILE A CG1 
1840 C  CG2 . ILE A 228 ? 1.0220 0.8745 1.2747 -0.0341 0.0871  0.1355  1698 ILE A CG2 
1841 C  CD1 . ILE A 228 ? 0.6987 0.5702 1.0045 -0.0166 0.0961  0.1086  1698 ILE A CD1 
1842 N  N   . GLU A 229 ? 0.7550 0.6033 1.0381 0.0054  0.0435  0.1301  1699 GLU A N   
1843 C  CA  . GLU A 229 ? 0.8066 0.6621 1.1081 0.0188  0.0323  0.1243  1699 GLU A CA  
1844 C  C   . GLU A 229 ? 0.7076 0.5560 1.0324 0.0288  0.0310  0.1194  1699 GLU A C   
1845 O  O   . GLU A 229 ? 0.8840 0.7109 1.2042 0.0279  0.0296  0.1262  1699 GLU A O   
1846 C  CB  . GLU A 229 ? 0.8922 0.7368 1.1781 0.0224  0.0147  0.1350  1699 GLU A CB  
1847 C  CG  . GLU A 229 ? 1.0846 0.9475 1.3634 0.0216  0.0103  0.1317  1699 GLU A CG  
1848 C  CD  . GLU A 229 ? 1.2899 1.1394 1.5439 0.0215  -0.0058 0.1447  1699 GLU A CD  
1849 O  OE1 . GLU A 229 ? 1.2907 1.1155 1.5349 0.0235  -0.0150 0.1567  1699 GLU A OE1 
1850 O  OE2 . GLU A 229 ? 1.3311 1.1934 1.5746 0.0195  -0.0102 0.1429  1699 GLU A OE2 
1851 N  N   . PHE A 230 ? 0.6309 0.4974 0.9801 0.0378  0.0319  0.1074  1700 PHE A N   
1852 C  CA  . PHE A 230 ? 0.7298 0.5936 1.1021 0.0489  0.0307  0.1008  1700 PHE A CA  
1853 C  C   . PHE A 230 ? 0.7525 0.6124 1.1341 0.0625  0.0135  0.1027  1700 PHE A C   
1854 O  O   . PHE A 230 ? 0.7067 0.5702 1.0799 0.0636  0.0025  0.1076  1700 PHE A O   
1855 C  CB  . PHE A 230 ? 0.6967 0.5836 1.0902 0.0504  0.0427  0.0865  1700 PHE A CB  
1856 C  CG  . PHE A 230 ? 0.6562 0.5452 1.0436 0.0399  0.0582  0.0837  1700 PHE A CG  
1857 C  CD1 . PHE A 230 ? 0.5547 0.4536 0.9288 0.0299  0.0647  0.0839  1700 PHE A CD1 
1858 C  CD2 . PHE A 230 ? 0.6777 0.5585 1.0725 0.0407  0.0655  0.0802  1700 PHE A CD2 
1859 C  CE1 . PHE A 230 ? 0.6719 0.5733 1.0418 0.0216  0.0781  0.0808  1700 PHE A CE1 
1860 C  CE2 . PHE A 230 ? 0.6604 0.5438 1.0503 0.0316  0.0785  0.0776  1700 PHE A CE2 
1861 C  CZ  . PHE A 230 ? 0.6824 0.5765 1.0606 0.0225  0.0847  0.0780  1700 PHE A CZ  
1862 N  N   . LYS A 231 ? 0.7061 0.5588 1.1055 0.0736  0.0108  0.0981  1701 LYS A N   
1863 C  CA  . LYS A 231 ? 0.8349 0.6827 1.2448 0.0883  -0.0061 0.0993  1701 LYS A CA  
1864 C  C   . LYS A 231 ? 0.8378 0.7159 1.2677 0.0953  -0.0098 0.0901  1701 LYS A C   
1865 O  O   . LYS A 231 ? 0.7831 0.6621 1.2133 0.1028  -0.0255 0.0942  1701 LYS A O   
1866 C  CB  . LYS A 231 ? 0.8368 0.6697 1.2611 0.0995  -0.0077 0.0948  1701 LYS A CB  
1867 C  CG  . LYS A 231 ? 1.0570 0.8525 1.4602 0.0966  -0.0151 0.1077  1701 LYS A CG  
1868 C  CD  . LYS A 231 ? 1.1469 0.9276 1.5566 0.0976  -0.0074 0.1025  1701 LYS A CD  
1869 C  CE  . LYS A 231 ? 1.2513 1.0014 1.6612 0.1096  -0.0225 0.1068  1701 LYS A CE  
1870 N  NZ  . LYS A 231 ? 1.2025 0.9409 1.6230 0.1140  -0.0165 0.0981  1701 LYS A NZ  
1871 N  N   . ARG A 232 ? 0.7569 0.6598 1.2028 0.0921  0.0039  0.0783  1702 ARG A N   
1872 C  CA  . ARG A 232 ? 0.6816 0.6132 1.1443 0.0952  0.0006  0.0708  1702 ARG A CA  
1873 C  C   . ARG A 232 ? 0.8285 0.7616 1.2696 0.0857  -0.0049 0.0782  1702 ARG A C   
1874 O  O   . ARG A 232 ? 0.9273 0.8520 1.3464 0.0732  0.0037  0.0831  1702 ARG A O   
1875 C  CB  . ARG A 232 ? 0.7964 0.7523 1.2777 0.0915  0.0166  0.0579  1702 ARG A CB  
1876 C  CG  . ARG A 232 ? 0.6330 0.6188 1.1299 0.0909  0.0139  0.0508  1702 ARG A CG  
1877 C  CD  . ARG A 232 ? 0.5916 0.5994 1.1052 0.0855  0.0295  0.0392  1702 ARG A CD  
1878 N  NE  . ARG A 232 ? 0.6631 0.6744 1.1963 0.0940  0.0366  0.0317  1702 ARG A NE  
1879 C  CZ  . ARG A 232 ? 0.7758 0.8078 1.3366 0.1044  0.0335  0.0233  1702 ARG A CZ  
1880 N  NH1 . ARG A 232 ? 0.4938 0.5458 1.0676 0.1071  0.0230  0.0215  1702 ARG A NH1 
1881 N  NH2 . ARG A 232 ? 0.7086 0.7429 1.2844 0.1119  0.0411  0.0160  1702 ARG A NH2 
1882 N  N   . PRO A 233 ? 0.9468 0.8910 1.3932 0.0917  -0.0195 0.0788  1703 PRO A N   
1883 C  CA  . PRO A 233 ? 1.0615 1.0072 1.4855 0.0828  -0.0254 0.0850  1703 PRO A CA  
1884 C  C   . PRO A 233 ? 0.9944 0.9613 1.4207 0.0718  -0.0127 0.0761  1703 PRO A C   
1885 O  O   . PRO A 233 ? 0.8822 0.8702 1.3336 0.0735  -0.0054 0.0647  1703 PRO A O   
1886 C  CB  . PRO A 233 ? 1.0213 0.9752 1.4553 0.0942  -0.0458 0.0861  1703 PRO A CB  
1887 C  CG  . PRO A 233 ? 0.9836 0.9521 1.4530 0.1076  -0.0461 0.0758  1703 PRO A CG  
1888 C  CD  . PRO A 233 ? 0.9048 0.8565 1.3748 0.1081  -0.0335 0.0752  1703 PRO A CD  
1889 N  N   . GLY A 234 ? 0.9023 0.8630 1.3011 0.0604  -0.0106 0.0816  1704 GLY A N   
1890 C  CA  . GLY A 234 ? 0.8195 0.7948 1.2150 0.0497  0.0008  0.0740  1704 GLY A CA  
1891 C  C   . GLY A 234 ? 0.7528 0.7247 1.1479 0.0428  0.0198  0.0701  1704 GLY A C   
1892 O  O   . GLY A 234 ? 0.8720 0.8561 1.2692 0.0358  0.0294  0.0622  1704 GLY A O   
1893 N  N   . LYS A 235 ? 0.5333 0.4881 0.9258 0.0447  0.0245  0.0751  1705 LYS A N   
1894 C  CA  . LYS A 235 ? 0.4972 0.4490 0.8910 0.0392  0.0411  0.0712  1705 LYS A CA  
1895 C  C   . LYS A 235 ? 0.6287 0.5613 0.9965 0.0314  0.0450  0.0810  1705 LYS A C   
1896 O  O   . LYS A 235 ? 0.7242 0.6384 1.0844 0.0342  0.0383  0.0903  1705 LYS A O   
1897 C  CB  . LYS A 235 ? 0.6539 0.6049 1.0703 0.0478  0.0446  0.0663  1705 LYS A CB  
1898 C  CG  . LYS A 235 ? 0.7745 0.7479 1.2182 0.0538  0.0449  0.0554  1705 LYS A CG  
1899 C  CD  . LYS A 235 ? 0.7342 0.7233 1.1792 0.0447  0.0550  0.0478  1705 LYS A CD  
1900 C  CE  . LYS A 235 ? 0.7222 0.7343 1.1931 0.0485  0.0542  0.0382  1705 LYS A CE  
1901 N  NZ  . LYS A 235 ? 0.5091 0.5345 0.9770 0.0397  0.0552  0.0337  1705 LYS A NZ  
1902 N  N   . ALA A 236 ? 0.6187 0.5556 0.9739 0.0216  0.0558  0.0786  1706 ALA A N   
1903 C  CA  . ALA A 236 ? 0.6525 0.5763 0.9845 0.0131  0.0610  0.0869  1706 ALA A CA  
1904 C  C   . ALA A 236 ? 0.6713 0.6021 1.0035 0.0062  0.0769  0.0798  1706 ALA A C   
1905 O  O   . ALA A 236 ? 0.5641 0.5083 0.9094 0.0071  0.0825  0.0695  1706 ALA A O   
1906 C  CB  . ALA A 236 ? 0.5927 0.5142 0.8995 0.0081  0.0532  0.0944  1706 ALA A CB  
1907 N  N   . ALA A 237 ? 0.5070 0.4281 0.8252 -0.0007 0.0836  0.0858  1707 ALA A N   
1908 C  CA  . ALA A 237 ? 0.5029 0.4312 0.8193 -0.0070 0.0976  0.0798  1707 ALA A CA  
1909 C  C   . ALA A 237 ? 0.6188 0.5434 0.9112 -0.0165 0.1014  0.0873  1707 ALA A C   
1910 O  O   . ALA A 237 ? 0.5863 0.4983 0.8645 -0.0192 0.0948  0.0988  1707 ALA A O   
1911 C  CB  . ALA A 237 ? 0.5591 0.4835 0.8911 -0.0052 0.1051  0.0764  1707 ALA A CB  
1912 N  N   . ASN A 238 ? 0.6024 0.5379 0.8903 -0.0215 0.1123  0.0806  1708 ASN A N   
1913 C  CA  . ASN A 238 ? 0.4870 0.4225 0.7554 -0.0308 0.1191  0.0862  1708 ASN A CA  
1914 C  C   . ASN A 238 ? 0.4825 0.4112 0.7580 -0.0343 0.1256  0.0899  1708 ASN A C   
1915 O  O   . ASN A 238 ? 0.6401 0.5729 0.9330 -0.0312 0.1317  0.0821  1708 ASN A O   
1916 C  CB  . ASN A 238 ? 0.5226 0.4733 0.7846 -0.0336 0.1282  0.0763  1708 ASN A CB  
1917 C  CG  . ASN A 238 ? 0.6580 0.6132 0.9073 -0.0423 0.1391  0.0789  1708 ASN A CG  
1918 O  OD1 . ASN A 238 ? 0.5667 0.5257 0.8276 -0.0435 0.1479  0.0754  1708 ASN A OD1 
1919 N  ND2 . ASN A 238 ? 0.5565 0.5124 0.7819 -0.0488 0.1384  0.0854  1708 ASN A ND2 
1920 N  N   . LYS A 239 ? 0.5051 0.4224 0.7664 -0.0413 0.1238  0.1020  1709 LYS A N   
1921 C  CA  . LYS A 239 ? 0.5064 0.4148 0.7750 -0.0454 0.1277  0.1063  1709 LYS A CA  
1922 C  C   . LYS A 239 ? 0.4853 0.4083 0.7631 -0.0489 0.1412  0.0976  1709 LYS A C   
1923 O  O   . LYS A 239 ? 0.6048 0.5245 0.8979 -0.0477 0.1438  0.0950  1709 LYS A O   
1924 C  CB  . LYS A 239 ? 0.5974 0.4915 0.8460 -0.0551 0.1246  0.1215  1709 LYS A CB  
1925 C  CG  . LYS A 239 ? 0.6811 0.5652 0.9354 -0.0621 0.1286  0.1266  1709 LYS A CG  
1926 C  CD  . LYS A 239 ? 0.8315 0.6963 1.0654 -0.0720 0.1231  0.1433  1709 LYS A CD  
1927 C  CE  . LYS A 239 ? 0.8330 0.7069 1.0551 -0.0875 0.1353  0.1481  1709 LYS A CE  
1928 N  NZ  . LYS A 239 ? 0.9985 0.8860 1.1988 -0.0928 0.1401  0.1497  1709 LYS A NZ  
1929 N  N   . ASP A 240 ? 0.5629 0.5023 0.8324 -0.0519 0.1492  0.0917  1710 ASP A N   
1930 C  CA  . ASP A 240 ? 0.5667 0.5208 0.8462 -0.0537 0.1611  0.0827  1710 ASP A CA  
1931 C  C   . ASP A 240 ? 0.5915 0.5489 0.8911 -0.0440 0.1614  0.0711  1710 ASP A C   
1932 O  O   . ASP A 240 ? 0.4684 0.4282 0.7817 -0.0436 0.1664  0.0670  1710 ASP A O   
1933 C  CB  . ASP A 240 ? 0.4749 0.4454 0.7399 -0.0583 0.1694  0.0785  1710 ASP A CB  
1934 C  CG  . ASP A 240 ? 0.6897 0.6603 0.9355 -0.0704 0.1731  0.0897  1710 ASP A CG  
1935 O  OD1 . ASP A 240 ? 0.8241 0.7842 1.0720 -0.0767 0.1722  0.0991  1710 ASP A OD1 
1936 O  OD2 . ASP A 240 ? 0.7805 0.7609 1.0081 -0.0743 0.1773  0.0890  1710 ASP A OD2 
1937 N  N   . ASN A 241 ? 0.4558 0.4132 0.7571 -0.0369 0.1557  0.0661  1711 ASN A N   
1938 C  CA  . ASN A 241 ? 0.4861 0.4443 0.8053 -0.0289 0.1555  0.0570  1711 ASN A CA  
1939 C  C   . ASN A 241 ? 0.4070 0.3536 0.7392 -0.0259 0.1514  0.0605  1711 ASN A C   
1940 O  O   . ASN A 241 ? 0.4129 0.3601 0.7586 -0.0225 0.1549  0.0545  1711 ASN A O   
1941 C  CB  . ASN A 241 ? 0.4297 0.3898 0.7490 -0.0236 0.1494  0.0523  1711 ASN A CB  
1942 C  CG  . ASN A 241 ? 0.5553 0.5250 0.8604 -0.0260 0.1519  0.0477  1711 ASN A CG  
1943 O  OD1 . ASN A 241 ? 0.5138 0.4840 0.8135 -0.0243 0.1451  0.0465  1711 ASN A OD1 
1944 N  ND2 . ASN A 241 ? 0.5702 0.5482 0.8697 -0.0297 0.1611  0.0441  1711 ASN A ND2 
1945 N  N   . TRP A 242 ? 0.4220 0.3565 0.7493 -0.0261 0.1431  0.0698  1712 TRP A N   
1946 C  CA  . TRP A 242 ? 0.4419 0.3637 0.7804 -0.0224 0.1385  0.0724  1712 TRP A CA  
1947 C  C   . TRP A 242 ? 0.5002 0.4202 0.8433 -0.0274 0.1451  0.0724  1712 TRP A C   
1948 O  O   . TRP A 242 ? 0.4756 0.3946 0.8322 -0.0231 0.1469  0.0664  1712 TRP A O   
1949 C  CB  . TRP A 242 ? 0.4425 0.3497 0.7723 -0.0224 0.1281  0.0832  1712 TRP A CB  
1950 C  CG  . TRP A 242 ? 0.6868 0.5793 1.0281 -0.0164 0.1218  0.0848  1712 TRP A CG  
1951 C  CD1 . TRP A 242 ? 0.7506 0.6263 1.0887 -0.0202 0.1187  0.0925  1712 TRP A CD1 
1952 C  CD2 . TRP A 242 ? 0.5529 0.4461 0.9104 -0.0058 0.1180  0.0777  1712 TRP A CD2 
1953 N  NE1 . TRP A 242 ? 0.7250 0.5899 1.0760 -0.0114 0.1128  0.0899  1712 TRP A NE1 
1954 C  CE2 . TRP A 242 ? 0.6406 0.5173 1.0037 -0.0024 0.1128  0.0807  1712 TRP A CE2 
1955 C  CE3 . TRP A 242 ? 0.5421 0.4484 0.9099 0.0005  0.1189  0.0690  1712 TRP A CE3 
1956 C  CZ2 . TRP A 242 ? 0.5541 0.4290 0.9327 0.0082  0.1092  0.0744  1712 TRP A CZ2 
1957 C  CZ3 . TRP A 242 ? 0.6726 0.5780 1.0561 0.0095  0.1157  0.0638  1712 TRP A CZ3 
1958 C  CH2 . TRP A 242 ? 0.4944 0.3849 0.8831 0.0138  0.1112  0.0662  1712 TRP A CH2 
1959 N  N   . ASN A 243 ? 0.5506 0.4719 0.8821 -0.0371 0.1489  0.0789  1713 ASN A N   
1960 C  CA  . ASN A 243 ? 0.5177 0.4396 0.8542 -0.0436 0.1549  0.0793  1713 ASN A CA  
1961 C  C   . ASN A 243 ? 0.4920 0.4288 0.8404 -0.0407 0.1628  0.0679  1713 ASN A C   
1962 O  O   . ASN A 243 ? 0.5424 0.4775 0.9018 -0.0408 0.1644  0.0650  1713 ASN A O   
1963 C  CB  . ASN A 243 ? 0.5348 0.4589 0.8566 -0.0559 0.1587  0.0883  1713 ASN A CB  
1964 C  CG  . ASN A 243 ? 0.5705 0.4738 0.8807 -0.0602 0.1499  0.1017  1713 ASN A CG  
1965 O  OD1 . ASN A 243 ? 0.5876 0.4750 0.9029 -0.0529 0.1405  0.1032  1713 ASN A OD1 
1966 N  ND2 . ASN A 243 ? 0.5480 0.4513 0.8422 -0.0721 0.1528  0.1113  1713 ASN A ND2 
1967 N  N   . LYS A 244 ? 0.4206 0.3709 0.7663 -0.0378 0.1669  0.0611  1714 LYS A N   
1968 C  CA  . LYS A 244 ? 0.3957 0.3573 0.7519 -0.0339 0.1731  0.0504  1714 LYS A CA  
1969 C  C   . LYS A 244 ? 0.4249 0.3786 0.7938 -0.0260 0.1696  0.0456  1714 LYS A C   
1970 O  O   . LYS A 244 ? 0.4570 0.4127 0.8355 -0.0248 0.1723  0.0409  1714 LYS A O   
1971 C  CB  . LYS A 244 ? 0.5713 0.5444 0.9214 -0.0312 0.1765  0.0437  1714 LYS A CB  
1972 C  CG  . LYS A 244 ? 0.6415 0.6251 1.0004 -0.0270 0.1824  0.0330  1714 LYS A CG  
1973 C  CD  . LYS A 244 ? 0.9330 0.9298 1.2831 -0.0276 0.1879  0.0275  1714 LYS A CD  
1974 C  CE  . LYS A 244 ? 1.0052 1.0142 1.3644 -0.0246 0.1944  0.0182  1714 LYS A CE  
1975 N  NZ  . LYS A 244 ? 0.7894 0.8153 1.1432 -0.0301 0.2023  0.0170  1714 LYS A NZ  
1976 N  N   . PHE A 245 ? 0.4511 0.3967 0.8202 -0.0209 0.1633  0.0468  1715 PHE A N   
1977 C  CA  . PHE A 245 ? 0.5348 0.4745 0.9151 -0.0138 0.1610  0.0420  1715 PHE A CA  
1978 C  C   . PHE A 245 ? 0.4279 0.3567 0.8138 -0.0145 0.1588  0.0449  1715 PHE A C   
1979 O  O   . PHE A 245 ? 0.5246 0.4522 0.9187 -0.0113 0.1604  0.0394  1715 PHE A O   
1980 C  CB  . PHE A 245 ? 0.4858 0.4226 0.8665 -0.0087 0.1552  0.0425  1715 PHE A CB  
1981 C  CG  . PHE A 245 ? 0.3578 0.2944 0.7491 -0.0021 0.1553  0.0360  1715 PHE A CG  
1982 C  CD1 . PHE A 245 ? 0.4561 0.4002 0.8488 -0.0005 0.1588  0.0293  1715 PHE A CD1 
1983 C  CD2 . PHE A 245 ? 0.5387 0.4667 0.9376 0.0023  0.1519  0.0364  1715 PHE A CD2 
1984 C  CE1 . PHE A 245 ? 0.4752 0.4189 0.8762 0.0040  0.1596  0.0243  1715 PHE A CE1 
1985 C  CE2 . PHE A 245 ? 0.6615 0.5910 1.0690 0.0077  0.1532  0.0303  1715 PHE A CE2 
1986 C  CZ  . PHE A 245 ? 0.5070 0.4446 0.9152 0.0080  0.1573  0.0248  1715 PHE A CZ  
1987 N  N   . LEU A 246 ? 0.3763 0.2955 0.7565 -0.0189 0.1544  0.0535  1716 LEU A N   
1988 C  CA  . LEU A 246 ? 0.5440 0.4502 0.9286 -0.0203 0.1513  0.0561  1716 LEU A CA  
1989 C  C   . LEU A 246 ? 0.6467 0.5593 1.0354 -0.0262 0.1570  0.0533  1716 LEU A C   
1990 O  O   . LEU A 246 ? 0.5388 0.4456 0.9351 -0.0244 0.1560  0.0495  1716 LEU A O   
1991 C  CB  . LEU A 246 ? 0.5212 0.4135 0.8971 -0.0247 0.1449  0.0668  1716 LEU A CB  
1992 C  CG  . LEU A 246 ? 0.5344 0.4179 0.9086 -0.0173 0.1365  0.0697  1716 LEU A CG  
1993 C  CD1 . LEU A 246 ? 0.5774 0.4412 0.9444 -0.0203 0.1283  0.0800  1716 LEU A CD1 
1994 C  CD2 . LEU A 246 ? 0.6148 0.4978 1.0016 -0.0068 0.1351  0.0613  1716 LEU A CD2 
1995 N  N   . MET A 247 ? 0.4921 0.4182 0.8763 -0.0327 0.1629  0.0542  1717 MET A N   
1996 C  CA  . MET A 247 ? 0.4218 0.3583 0.8124 -0.0377 0.1684  0.0506  1717 MET A CA  
1997 C  C   . MET A 247 ? 0.6314 0.5738 1.0313 -0.0299 0.1702  0.0405  1717 MET A C   
1998 O  O   . MET A 247 ? 0.4800 0.4238 0.8878 -0.0311 0.1706  0.0370  1717 MET A O   
1999 C  CB  . MET A 247 ? 0.4134 0.3663 0.7981 -0.0448 0.1752  0.0522  1717 MET A CB  
2000 C  CG  . MET A 247 ? 0.6769 0.6253 1.0537 -0.0568 0.1752  0.0629  1717 MET A CG  
2001 S  SD  . MET A 247 ? 0.9011 0.8472 1.2895 -0.0649 0.1752  0.0634  1717 MET A SD  
2002 C  CE  . MET A 247 ? 0.6129 0.5860 1.0139 -0.0626 0.1836  0.0517  1717 MET A CE  
2003 N  N   . ALA A 248 ? 0.4103 0.3559 0.8087 -0.0225 0.1708  0.0358  1718 ALA A N   
2004 C  CA  . ALA A 248 ? 0.3550 0.3035 0.7599 -0.0158 0.1721  0.0274  1718 ALA A CA  
2005 C  C   . ALA A 248 ? 0.4585 0.3944 0.8681 -0.0120 0.1679  0.0261  1718 ALA A C   
2006 O  O   . ALA A 248 ? 0.4748 0.4115 0.8892 -0.0093 0.1683  0.0206  1718 ALA A O   
2007 C  CB  . ALA A 248 ? 0.3285 0.2808 0.7299 -0.0104 0.1734  0.0233  1718 ALA A CB  
2008 N  N   . ILE A 249 ? 0.4076 0.3318 0.8154 -0.0110 0.1633  0.0305  1719 ILE A N   
2009 C  CA  . ILE A 249 ? 0.4686 0.3806 0.8805 -0.0070 0.1595  0.0285  1719 ILE A CA  
2010 C  C   . ILE A 249 ? 0.5970 0.5043 1.0116 -0.0130 0.1580  0.0295  1719 ILE A C   
2011 O  O   . ILE A 249 ? 0.5568 0.4610 0.9753 -0.0106 0.1571  0.0241  1719 ILE A O   
2012 C  CB  . ILE A 249 ? 0.4559 0.3570 0.8666 -0.0033 0.1544  0.0321  1719 ILE A CB  
2013 C  CG1 . ILE A 249 ? 0.6303 0.5373 1.0419 0.0031  0.1555  0.0290  1719 ILE A CG1 
2014 C  CG2 . ILE A 249 ? 0.5649 0.4522 0.9793 0.0001  0.1503  0.0299  1719 ILE A CG2 
2015 C  CD1 . ILE A 249 ? 0.4557 0.3566 0.8680 0.0071  0.1500  0.0326  1719 ILE A CD1 
2016 N  N   . LYS A 250 ? 0.5294 0.4362 0.9413 -0.0215 0.1576  0.0365  1720 LYS A N   
2017 C  CA  . LYS A 250 ? 0.6144 0.5173 1.0296 -0.0295 0.1561  0.0383  1720 LYS A CA  
2018 C  C   . LYS A 250 ? 0.6624 0.5791 1.0850 -0.0304 0.1596  0.0314  1720 LYS A C   
2019 O  O   . LYS A 250 ? 0.8104 0.7222 1.2380 -0.0318 0.1566  0.0281  1720 LYS A O   
2020 C  CB  . LYS A 250 ? 0.6514 0.5547 1.0613 -0.0404 0.1569  0.0477  1720 LYS A CB  
2021 C  CG  . LYS A 250 ? 0.7681 0.6707 1.1830 -0.0510 0.1565  0.0494  1720 LYS A CG  
2022 C  CD  . LYS A 250 ? 0.7714 0.6773 1.1804 -0.0638 0.1592  0.0592  1720 LYS A CD  
2023 C  CE  . LYS A 250 ? 0.7622 0.6645 1.1770 -0.0758 0.1578  0.0616  1720 LYS A CE  
2024 N  NZ  . LYS A 250 ? 0.8293 0.7455 1.2413 -0.0895 0.1642  0.0687  1720 LYS A NZ  
2025 N  N   . THR A 251 ? 0.7056 0.6391 1.1287 -0.0291 0.1651  0.0287  1721 THR A N   
2026 C  CA  . THR A 251 ? 0.6801 0.6276 1.1110 -0.0288 0.1675  0.0221  1721 THR A CA  
2027 C  C   . THR A 251 ? 0.6670 0.6111 1.0989 -0.0190 0.1656  0.0146  1721 THR A C   
2028 O  O   . THR A 251 ? 0.7306 0.6798 1.1685 -0.0181 0.1642  0.0095  1721 THR A O   
2029 C  CB  . THR A 251 ? 0.8674 0.8340 1.2985 -0.0304 0.1739  0.0213  1721 THR A CB  
2030 O  OG1 . THR A 251 ? 0.9772 0.9571 1.4169 -0.0269 0.1752  0.0136  1721 THR A OG1 
2031 C  CG2 . THR A 251 ? 0.7766 0.7421 1.1999 -0.0240 0.1755  0.0208  1721 THR A CG2 
2032 N  N   . SER A 252 ? 0.4936 0.4298 0.9196 -0.0120 0.1653  0.0140  1722 SER A N   
2033 C  CA  . SER A 252 ? 0.4772 0.4110 0.9022 -0.0041 0.1647  0.0078  1722 SER A CA  
2034 C  C   . SER A 252 ? 0.5978 0.5172 1.0201 0.0001  0.1614  0.0064  1722 SER A C   
2035 O  O   . SER A 252 ? 0.5480 0.4647 0.9684 0.0050  0.1607  0.0014  1722 SER A O   
2036 C  CB  . SER A 252 ? 0.5455 0.4842 0.9663 0.0004  0.1682  0.0066  1722 SER A CB  
2037 O  OG  . SER A 252 ? 0.4002 0.3318 0.8170 0.0019  0.1679  0.0096  1722 SER A OG  
2038 N  N   . HIS A 253 ? 0.5055 0.4155 0.9268 -0.0012 0.1594  0.0105  1723 HIS A N   
2039 C  CA  . HIS A 253 ? 0.6666 0.5643 1.0861 0.0044  0.1569  0.0081  1723 HIS A CA  
2040 C  C   . HIS A 253 ? 0.5512 0.4516 0.9678 0.0111  0.1602  0.0046  1723 HIS A C   
2041 O  O   . HIS A 253 ? 0.5614 0.4558 0.9761 0.0159  0.1599  0.0003  1723 HIS A O   
2042 C  CB  . HIS A 253 ? 0.4455 0.3351 0.8657 0.0041  0.1532  0.0038  1723 HIS A CB  
2043 C  CG  . HIS A 253 ? 0.5232 0.4082 0.9469 -0.0038 0.1495  0.0075  1723 HIS A CG  
2044 N  ND1 . HIS A 253 ? 0.5521 0.4422 0.9800 -0.0094 0.1480  0.0057  1723 HIS A ND1 
2045 C  CD2 . HIS A 253 ? 0.5004 0.3762 0.9239 -0.0079 0.1468  0.0136  1723 HIS A CD2 
2046 C  CE1 . HIS A 253 ? 0.6290 0.5135 1.0595 -0.0178 0.1452  0.0104  1723 HIS A CE1 
2047 N  NE2 . HIS A 253 ? 0.6539 0.5282 1.0807 -0.0170 0.1443  0.0157  1723 HIS A NE2 
2048 N  N   . SER A 254 ? 0.4450 0.3546 0.8607 0.0107  0.1634  0.0062  1724 SER A N   
2049 C  CA  . SER A 254 ? 0.4017 0.3138 0.8150 0.0148  0.1664  0.0042  1724 SER A CA  
2050 C  C   . SER A 254 ? 0.4966 0.4038 0.9116 0.0189  0.1659  0.0035  1724 SER A C   
2051 O  O   . SER A 254 ? 0.3886 0.2952 0.8067 0.0187  0.1636  0.0071  1724 SER A O   
2052 C  CB  . SER A 254 ? 0.4115 0.3317 0.8243 0.0126  0.1683  0.0070  1724 SER A CB  
2053 O  OG  . SER A 254 ? 0.4760 0.3981 0.8868 0.0152  0.1709  0.0046  1724 SER A OG  
2054 N  N   . PRO A 255 ? 0.3836 0.2880 0.7966 0.0229  0.1678  -0.0011 1725 PRO A N   
2055 C  CA  . PRO A 255 ? 0.5309 0.4349 0.9474 0.0274  0.1686  -0.0029 1725 PRO A CA  
2056 C  C   . PRO A 255 ? 0.4541 0.3671 0.8745 0.0271  0.1705  -0.0009 1725 PRO A C   
2057 O  O   . PRO A 255 ? 0.4857 0.4004 0.9125 0.0302  0.1687  -0.0005 1725 PRO A O   
2058 C  CB  . PRO A 255 ? 0.4988 0.4004 0.9100 0.0304  0.1719  -0.0086 1725 PRO A CB  
2059 C  CG  . PRO A 255 ? 0.5223 0.4195 0.9275 0.0282  0.1702  -0.0093 1725 PRO A CG  
2060 C  CD  . PRO A 255 ? 0.5077 0.4100 0.9147 0.0238  0.1692  -0.0050 1725 PRO A CD  
2061 N  N   . VAL A 256 ? 0.4407 0.3592 0.8579 0.0239  0.1731  -0.0001 1726 VAL A N   
2062 C  CA  . VAL A 256 ? 0.3647 0.2914 0.7861 0.0231  0.1741  0.0011  1726 VAL A CA  
2063 C  C   . VAL A 256 ? 0.3893 0.3177 0.8132 0.0216  0.1695  0.0057  1726 VAL A C   
2064 O  O   . VAL A 256 ? 0.4202 0.3536 0.8500 0.0231  0.1674  0.0068  1726 VAL A O   
2065 C  CB  . VAL A 256 ? 0.4630 0.3924 0.8793 0.0198  0.1776  0.0002  1726 VAL A CB  
2066 C  CG1 . VAL A 256 ? 0.3725 0.2990 0.7844 0.0206  0.1820  -0.0030 1726 VAL A CG1 
2067 C  CG2 . VAL A 256 ? 0.4434 0.3704 0.8539 0.0173  0.1765  0.0013  1726 VAL A CG2 
2068 N  N   . CYS A 257 ? 0.3879 0.3128 0.8077 0.0186  0.1677  0.0086  1727 CYS A N   
2069 C  CA  . CYS A 257 ? 0.3193 0.2445 0.7389 0.0164  0.1636  0.0140  1727 CYS A CA  
2070 C  C   . CYS A 257 ? 0.3620 0.2799 0.7858 0.0198  0.1587  0.0161  1727 CYS A C   
2071 O  O   . CYS A 257 ? 0.4166 0.3350 0.8418 0.0205  0.1543  0.0201  1727 CYS A O   
2072 C  CB  . CYS A 257 ? 0.3196 0.2450 0.7339 0.0113  0.1640  0.0166  1727 CYS A CB  
2073 S  SG  . CYS A 257 ? 0.5081 0.4414 0.9180 0.0093  0.1688  0.0128  1727 CYS A SG  
2074 N  N   A GLN A 258 ? 0.3452 0.2551 0.7704 0.0224  0.1585  0.0133  1728 GLN A N   
2075 N  N   B GLN A 258 ? 0.3536 0.2636 0.7788 0.0224  0.1586  0.0133  1728 GLN A N   
2076 C  CA  A GLN A 258 ? 0.4304 0.3312 0.8596 0.0269  0.1533  0.0141  1728 GLN A CA  
2077 C  CA  B GLN A 258 ? 0.4280 0.3288 0.8572 0.0269  0.1535  0.0139  1728 GLN A CA  
2078 C  C   A GLN A 258 ? 0.4760 0.3834 0.9132 0.0336  0.1531  0.0110  1728 GLN A C   
2079 C  C   B GLN A 258 ? 0.4757 0.3829 0.9128 0.0336  0.1531  0.0109  1728 GLN A C   
2080 O  O   A GLN A 258 ? 0.5405 0.4445 0.9821 0.0377  0.1473  0.0133  1728 GLN A O   
2081 O  O   B GLN A 258 ? 0.5385 0.4419 0.9799 0.0377  0.1473  0.0133  1728 GLN A O   
2082 C  CB  A GLN A 258 ? 0.3974 0.2877 0.8259 0.0286  0.1530  0.0101  1728 GLN A CB  
2083 C  CB  B GLN A 258 ? 0.4274 0.3181 0.8555 0.0283  0.1535  0.0098  1728 GLN A CB  
2084 C  CG  A GLN A 258 ? 0.5975 0.4759 1.0225 0.0234  0.1483  0.0148  1728 GLN A CG  
2085 C  CG  B GLN A 258 ? 0.6118 0.4980 1.0349 0.0211  0.1528  0.0127  1728 GLN A CG  
2086 C  CD  A GLN A 258 ? 0.5464 0.4125 0.9728 0.0257  0.1410  0.0194  1728 GLN A CD  
2087 C  CD  B GLN A 258 ? 0.5404 0.4153 0.9629 0.0218  0.1507  0.0087  1728 GLN A CD  
2088 O  OE1 A GLN A 258 ? 0.6031 0.4694 1.0347 0.0333  0.1387  0.0176  1728 GLN A OE1 
2089 O  OE1 B GLN A 258 ? 0.4491 0.3263 0.8693 0.0207  0.1532  0.0045  1728 GLN A OE1 
2090 N  NE2 A GLN A 258 ? 0.5132 0.3686 0.9353 0.0190  0.1371  0.0254  1728 GLN A NE2 
2091 N  NE2 B GLN A 258 ? 0.6170 0.4786 1.0410 0.0241  0.1450  0.0097  1728 GLN A NE2 
2092 N  N   . ASP A 259 ? 0.4802 0.3975 0.9195 0.0346  0.1590  0.0059  1729 ASP A N   
2093 C  CA  . ASP A 259 ? 0.5110 0.4387 0.9598 0.0393  0.1598  0.0029  1729 ASP A CA  
2094 C  C   . ASP A 259 ? 0.3870 0.3219 0.8388 0.0377  0.1554  0.0075  1729 ASP A C   
2095 O  O   . ASP A 259 ? 0.4311 0.3698 0.8917 0.0431  0.1506  0.0075  1729 ASP A O   
2096 C  CB  . ASP A 259 ? 0.3325 0.2691 0.7812 0.0380  0.1677  -0.0021 1729 ASP A CB  
2097 C  CG  . ASP A 259 ? 0.4801 0.4293 0.9407 0.0427  0.1700  -0.0067 1729 ASP A CG  
2098 O  OD1 . ASP A 259 ? 0.6306 0.5780 1.0966 0.0498  0.1696  -0.0110 1729 ASP A OD1 
2099 O  OD2 . ASP A 259 ? 0.3983 0.3597 0.8636 0.0394  0.1720  -0.0066 1729 ASP A OD2 
2100 N  N   . VAL A 260 ? 0.4957 0.4325 0.9401 0.0310  0.1563  0.0109  1730 VAL A N   
2101 C  CA  . VAL A 260 ? 0.3778 0.3204 0.8221 0.0290  0.1515  0.0151  1730 VAL A CA  
2102 C  C   . VAL A 260 ? 0.4071 0.3412 0.8509 0.0319  0.1432  0.0207  1730 VAL A C   
2103 O  O   . VAL A 260 ? 0.4298 0.3685 0.8794 0.0356  0.1371  0.0223  1730 VAL A O   
2104 C  CB  . VAL A 260 ? 0.3639 0.3075 0.7978 0.0217  0.1538  0.0172  1730 VAL A CB  
2105 C  CG1 . VAL A 260 ? 0.3295 0.2758 0.7592 0.0195  0.1480  0.0221  1730 VAL A CG1 
2106 C  CG2 . VAL A 260 ? 0.3151 0.2657 0.7494 0.0192  0.1598  0.0122  1730 VAL A CG2 
2107 N  N   . LEU A 261 ? 0.3508 0.2719 0.7877 0.0300  0.1423  0.0240  1731 LEU A N   
2108 C  CA  . LEU A 261 ? 0.3821 0.2910 0.8159 0.0313  0.1343  0.0305  1731 LEU A CA  
2109 C  C   . LEU A 261 ? 0.5042 0.4098 0.9488 0.0413  0.1287  0.0279  1731 LEU A C   
2110 O  O   . LEU A 261 ? 0.4032 0.3060 0.8493 0.0450  0.1203  0.0323  1731 LEU A O   
2111 C  CB  . LEU A 261 ? 0.4779 0.3738 0.9043 0.0263  0.1353  0.0333  1731 LEU A CB  
2112 C  CG  . LEU A 261 ? 0.6343 0.5161 1.0540 0.0242  0.1274  0.0423  1731 LEU A CG  
2113 C  CD1 . LEU A 261 ? 0.7725 0.6608 1.1836 0.0191  0.1257  0.0488  1731 LEU A CD1 
2114 C  CD2 . LEU A 261 ? 0.7489 0.6189 1.1631 0.0178  0.1288  0.0447  1731 LEU A CD2 
2115 N  N   . LYS A 262 ? 0.3638 0.2701 0.8156 0.0463  0.1331  0.0202  1732 LYS A N   
2116 C  CA  . LYS A 262 ? 0.4169 0.3235 0.8805 0.0569  0.1296  0.0151  1732 LYS A CA  
2117 C  C   . LYS A 262 ? 0.4971 0.4202 0.9715 0.0610  0.1267  0.0142  1732 LYS A C   
2118 O  O   . LYS A 262 ? 0.6075 0.5284 1.0891 0.0689  0.1182  0.0153  1732 LYS A O   
2119 C  CB  . LYS A 262 ? 0.5119 0.4216 0.9796 0.0601  0.1375  0.0059  1732 LYS A CB  
2120 C  CG  . LYS A 262 ? 0.9020 0.8238 1.3847 0.0703  0.1384  -0.0021 1732 LYS A CG  
2121 C  CD  . LYS A 262 ? 0.9678 0.8992 1.4521 0.0704  0.1492  -0.0106 1732 LYS A CD  
2122 C  CE  . LYS A 262 ? 0.8650 0.8195 1.3628 0.0729  0.1542  -0.0157 1732 LYS A CE  
2123 N  NZ  . LYS A 262 ? 0.7041 0.6706 1.1990 0.0630  0.1591  -0.0126 1732 LYS A NZ  
2124 N  N   . PHE A 263 ? 0.5426 0.4818 1.0184 0.0557  0.1330  0.0122  1733 PHE A N   
2125 C  CA  . PHE A 263 ? 0.3905 0.3472 0.8779 0.0581  0.1302  0.0106  1733 PHE A CA  
2126 C  C   . PHE A 263 ? 0.4132 0.3663 0.8960 0.0576  0.1196  0.0184  1733 PHE A C   
2127 O  O   . PHE A 263 ? 0.4885 0.4492 0.9823 0.0645  0.1120  0.0180  1733 PHE A O   
2128 C  CB  . PHE A 263 ? 0.3812 0.3526 0.8692 0.0508  0.1385  0.0074  1733 PHE A CB  
2129 C  CG  . PHE A 263 ? 0.3355 0.3237 0.8335 0.0505  0.1345  0.0067  1733 PHE A CG  
2130 C  CD1 . PHE A 263 ? 0.3831 0.3877 0.8998 0.0568  0.1345  0.0007  1733 PHE A CD1 
2131 C  CD2 . PHE A 263 ? 0.4258 0.4146 0.9151 0.0439  0.1304  0.0116  1733 PHE A CD2 
2132 C  CE1 . PHE A 263 ? 0.3391 0.3614 0.8673 0.0561  0.1299  -0.0002 1733 PHE A CE1 
2133 C  CE2 . PHE A 263 ? 0.3361 0.3399 0.8340 0.0432  0.1256  0.0106  1733 PHE A CE2 
2134 C  CZ  . PHE A 263 ? 0.4384 0.4595 0.9568 0.0491  0.1248  0.0048  1733 PHE A CZ  
2135 N  N   . ILE A 264 ? 0.3632 0.3067 0.8298 0.0496  0.1190  0.0253  1734 ILE A N   
2136 C  CA  . ILE A 264 ? 0.4367 0.3760 0.8953 0.0482  0.1093  0.0333  1734 ILE A CA  
2137 C  C   . ILE A 264 ? 0.4589 0.3840 0.9194 0.0565  0.0989  0.0376  1734 ILE A C   
2138 O  O   . ILE A 264 ? 0.4580 0.3847 0.9212 0.0614  0.0885  0.0411  1734 ILE A O   
2139 C  CB  . ILE A 264 ? 0.4718 0.4033 0.9116 0.0380  0.1121  0.0396  1734 ILE A CB  
2140 C  CG1 . ILE A 264 ? 0.4944 0.4387 0.9320 0.0312  0.1204  0.0350  1734 ILE A CG1 
2141 C  CG2 . ILE A 264 ? 0.5031 0.4273 0.9313 0.0365  0.1020  0.0490  1734 ILE A CG2 
2142 C  CD1 . ILE A 264 ? 0.4259 0.3646 0.8471 0.0225  0.1247  0.0390  1734 ILE A CD1 
2143 N  N   . SER A 265 ? 0.4453 0.3552 0.9045 0.0588  0.1006  0.0370  1735 SER A N   
2144 C  CA  . SER A 265 ? 0.5269 0.4195 0.9873 0.0670  0.0901  0.0405  1735 SER A CA  
2145 C  C   . SER A 265 ? 0.4954 0.3995 0.9756 0.0803  0.0850  0.0334  1735 SER A C   
2146 O  O   . SER A 265 ? 0.4536 0.3541 0.9365 0.0872  0.0731  0.0375  1735 SER A O   
2147 C  CB  . SER A 265 ? 0.6457 0.5192 1.1009 0.0660  0.0929  0.0400  1735 SER A CB  
2148 O  OG  . SER A 265 ? 1.0293 0.9050 1.4983 0.0758  0.0953  0.0299  1735 SER A OG  
2149 N  N   . GLN A 266 ? 0.4063 0.3258 0.9002 0.0838  0.0941  0.0227  1736 GLN A N   
2150 C  CA  . GLN A 266 ? 0.6101 0.5452 1.1250 0.0960  0.0914  0.0145  1736 GLN A CA  
2151 C  C   . GLN A 266 ? 0.5230 0.4763 1.0463 0.0969  0.0846  0.0164  1736 GLN A C   
2152 O  O   . GLN A 266 ? 0.5369 0.4940 1.0729 0.1081  0.0743  0.0152  1736 GLN A O   
2153 C  CB  . GLN A 266 ? 0.5614 0.5125 1.0865 0.0963  0.1047  0.0036  1736 GLN A CB  
2154 C  CG  . GLN A 266 ? 0.7891 0.7627 1.3376 0.1070  0.1050  -0.0060 1736 GLN A CG  
2155 C  CD  . GLN A 266 ? 0.9311 0.9254 1.4870 0.1026  0.1196  -0.0145 1736 GLN A CD  
2156 O  OE1 . GLN A 266 ? 0.9053 0.8994 1.4495 0.0909  0.1278  -0.0123 1736 GLN A OE1 
2157 N  NE2 . GLN A 266 ? 0.9034 0.9157 1.4788 0.1121  0.1229  -0.0245 1736 GLN A NE2 
2158 N  N   . TRP A 267 ? 0.5717 0.5351 1.0875 0.0856  0.0890  0.0191  1737 TRP A N   
2159 C  CA  . TRP A 267 ? 0.3907 0.3733 0.9142 0.0845  0.0838  0.0192  1737 TRP A CA  
2160 C  C   . TRP A 267 ? 0.4751 0.4465 0.9882 0.0862  0.0690  0.0289  1737 TRP A C   
2161 O  O   . TRP A 267 ? 0.5733 0.5569 1.0983 0.0928  0.0589  0.0282  1737 TRP A O   
2162 C  CB  . TRP A 267 ? 0.3997 0.3924 0.9158 0.0715  0.0935  0.0183  1737 TRP A CB  
2163 C  CG  . TRP A 267 ? 0.5598 0.5697 1.0803 0.0675  0.0887  0.0182  1737 TRP A CG  
2164 C  CD1 . TRP A 267 ? 0.5838 0.6117 1.1228 0.0743  0.0803  0.0149  1737 TRP A CD1 
2165 C  CD2 . TRP A 267 ? 0.4697 0.4815 0.9767 0.0559  0.0918  0.0204  1737 TRP A CD2 
2166 N  NE1 . TRP A 267 ? 0.5023 0.5428 1.0396 0.0665  0.0776  0.0152  1737 TRP A NE1 
2167 C  CE2 . TRP A 267 ? 0.5531 0.5830 1.0702 0.0554  0.0847  0.0183  1737 TRP A CE2 
2168 C  CE3 . TRP A 267 ? 0.6891 0.6898 1.1775 0.0465  0.0995  0.0231  1737 TRP A CE3 
2169 C  CZ2 . TRP A 267 ? 0.6244 0.6592 1.1316 0.0455  0.0849  0.0187  1737 TRP A CZ2 
2170 C  CZ3 . TRP A 267 ? 0.6178 0.6241 1.0971 0.0377  0.1002  0.0231  1737 TRP A CZ3 
2171 C  CH2 . TRP A 267 ? 0.6036 0.6256 1.0915 0.0371  0.0929  0.0208  1737 TRP A CH2 
2172 N  N   . CYS A 268 ? 0.5506 0.4993 1.0418 0.0802  0.0672  0.0383  1738 CYS A N   
2173 C  CA  . CYS A 268 ? 0.6701 0.6067 1.1466 0.0795  0.0542  0.0489  1738 CYS A CA  
2174 C  C   . CYS A 268 ? 0.6866 0.5982 1.1584 0.0876  0.0441  0.0553  1738 CYS A C   
2175 O  O   . CYS A 268 ? 0.7548 0.6515 1.2114 0.0868  0.0327  0.0659  1738 CYS A O   
2176 C  CB  . CYS A 268 ? 0.6896 0.6196 1.1425 0.0655  0.0594  0.0559  1738 CYS A CB  
2177 S  SG  . CYS A 268 ? 0.7149 0.6674 1.1701 0.0556  0.0719  0.0482  1738 CYS A SG  
2178 N  N   . GLY A 269 ? 0.6141 0.5197 1.0976 0.0955  0.0473  0.0489  1739 GLY A N   
2179 C  CA  . GLY A 269 ? 0.6847 0.5680 1.1685 0.1063  0.0357  0.0523  1739 GLY A CA  
2180 C  C   . GLY A 269 ? 0.8285 0.6815 1.2911 0.0986  0.0357  0.0615  1739 GLY A C   
2181 O  O   . GLY A 269 ? 0.9464 0.7761 1.3975 0.1010  0.0231  0.0714  1739 GLY A O   
2182 N  N   . GLY A 270 ? 0.9149 0.7675 1.3720 0.0890  0.0490  0.0588  1740 GLY A N   
2183 C  CA  . GLY A 270 ? 0.9971 0.8238 1.4375 0.0811  0.0497  0.0661  1740 GLY A CA  
2184 C  C   . GLY A 270 ? 1.1387 0.9654 1.5594 0.0651  0.0551  0.0751  1740 GLY A C   
2185 O  O   . GLY A 270 ? 0.9955 0.8350 1.4105 0.0612  0.0538  0.0787  1740 GLY A O   
2186 N  N   . LEU A 271 ? 1.3272 1.1409 1.7381 0.0557  0.0616  0.0777  1741 LEU A N   
2187 C  CA  . LEU A 271 ? 1.3496 1.1650 1.7436 0.0406  0.0681  0.0850  1741 LEU A CA  
2188 C  C   . LEU A 271 ? 1.2855 1.0880 1.6613 0.0361  0.0581  0.0988  1741 LEU A C   
2189 O  O   . LEU A 271 ? 1.4895 1.2709 1.8621 0.0420  0.0458  0.1052  1741 LEU A O   
2190 C  CB  . LEU A 271 ? 1.3686 1.1722 1.7582 0.0322  0.0752  0.0851  1741 LEU A CB  
2191 C  CG  . LEU A 271 ? 1.3584 1.1734 1.7614 0.0346  0.0855  0.0724  1741 LEU A CG  
2192 C  CD1 . LEU A 271 ? 1.4192 1.2190 1.8322 0.0446  0.0809  0.0664  1741 LEU A CD1 
2193 C  CD2 . LEU A 271 ? 1.2506 1.0693 1.6467 0.0220  0.0957  0.0729  1741 LEU A CD2 
2194 N  N   . PRO A 272 ? 0.8965 0.7104 1.2588 0.0260  0.0627  0.1036  1742 PRO A N   
2195 C  CA  . PRO A 272 ? 0.9250 0.7306 1.2683 0.0222  0.0534  0.1159  1742 PRO A CA  
2196 C  C   . PRO A 272 ? 0.9639 0.7437 1.2879 0.0122  0.0502  0.1293  1742 PRO A C   
2197 O  O   . PRO A 272 ? 1.0992 0.8707 1.4261 0.0070  0.0566  0.1279  1742 PRO A O   
2198 C  CB  . PRO A 272 ? 0.8736 0.7016 1.2094 0.0142  0.0622  0.1136  1742 PRO A CB  
2199 C  CG  . PRO A 272 ? 0.8418 0.6789 1.1839 0.0078  0.0769  0.1062  1742 PRO A CG  
2200 C  CD  . PRO A 272 ? 0.8343 0.6672 1.1962 0.0172  0.0769  0.0977  1742 PRO A CD  
2201 N  N   . ASN B 7   ? 1.1904 1.4784 1.9159 0.0485  0.0350  -0.1203 1477 ASN B N   
2202 C  CA  . ASN B 7   ? 1.1106 1.4410 1.8721 0.0533  0.0272  -0.1309 1477 ASN B CA  
2203 C  C   . ASN B 7   ? 1.1548 1.4902 1.9193 0.0773  0.0212  -0.1368 1477 ASN B C   
2204 O  O   . ASN B 7   ? 1.0681 1.4429 1.8651 0.0842  0.0197  -0.1463 1477 ASN B O   
2205 C  CB  . ASN B 7   ? 1.0529 1.4226 1.8448 0.0375  0.0420  -0.1329 1477 ASN B CB  
2206 C  CG  . ASN B 7   ? 1.0462 1.4159 1.8420 0.0140  0.0431  -0.1289 1477 ASN B CG  
2207 O  OD1 . ASN B 7   ? 1.0310 1.3827 1.8170 0.0111  0.0294  -0.1287 1477 ASN B OD1 
2208 N  ND2 . ASN B 7   ? 1.0407 1.4289 1.8492 -0.0032 0.0592  -0.1256 1477 ASN B ND2 
2209 N  N   . PHE B 8   ? 1.1477 1.4424 1.8781 0.0890  0.0181  -0.1310 1478 PHE B N   
2210 C  CA  . PHE B 8   ? 1.0564 1.3383 1.7770 0.1117  0.0093  -0.1337 1478 PHE B CA  
2211 C  C   . PHE B 8   ? 0.8130 1.0766 1.5165 0.1181  0.0227  -0.1296 1478 PHE B C   
2212 O  O   . PHE B 8   ? 0.7284 0.9639 1.4064 0.1088  0.0326  -0.1206 1478 PHE B O   
2213 C  CB  . PHE B 8   ? 1.1082 1.4293 1.8637 0.1255  -0.0009 -0.1458 1478 PHE B CB  
2214 N  N   A ASN B 9   ? 0.6577 0.9394 1.3770 0.1334  0.0233  -0.1372 1479 ASN B N   
2215 N  N   B ASN B 9   ? 0.6630 0.9414 1.3801 0.1353  0.0208  -0.1371 1479 ASN B N   
2216 C  CA  A ASN B 9   ? 0.5540 0.8090 1.2515 0.1452  0.0285  -0.1344 1479 ASN B CA  
2217 C  CA  B ASN B 9   ? 0.5615 0.8265 1.2671 0.1460  0.0296  -0.1368 1479 ASN B CA  
2218 C  C   A ASN B 9   ? 0.4737 0.7179 1.1572 0.1318  0.0481  -0.1274 1479 ASN B C   
2219 C  C   B ASN B 9   ? 0.4708 0.7171 1.1562 0.1321  0.0475  -0.1280 1479 ASN B C   
2220 O  O   A ASN B 9   ? 0.4153 0.6239 1.0696 0.1347  0.0508  -0.1206 1479 ASN B O   
2221 O  O   B ASN B 9   ? 0.4478 0.6560 1.1023 0.1349  0.0483  -0.1206 1479 ASN B O   
2222 C  CB  A ASN B 9   ? 0.6198 0.8987 1.3398 0.1642  0.0258  -0.1457 1479 ASN B CB  
2223 C  CB  B ASN B 9   ? 0.6113 0.9187 1.3515 0.1559  0.0341  -0.1491 1479 ASN B CB  
2224 C  CG  A ASN B 9   ? 0.7173 0.9640 1.4133 0.1778  0.0275  -0.1436 1479 ASN B CG  
2225 C  CG  B ASN B 9   ? 0.6944 0.9916 1.4322 0.1807  0.0233  -0.1554 1479 ASN B CG  
2226 O  OD1 A ASN B 9   ? 0.8020 1.0156 1.4758 0.1895  0.0139  -0.1400 1479 ASN B OD1 
2227 O  OD1 B ASN B 9   ? 0.7620 1.0169 1.4685 0.1888  0.0163  -0.1488 1479 ASN B OD1 
2228 N  ND2 A ASN B 9   ? 0.7339 0.9889 1.4326 0.1753  0.0440  -0.1454 1479 ASN B ND2 
2229 N  ND2 B ASN B 9   ? 0.5704 0.9002 1.3268 0.1892  0.0217  -0.1651 1479 ASN B ND2 
2230 N  N   . ILE B 10  ? 0.3539 0.6280 1.0572 0.1169  0.0616  -0.1287 1480 ILE B N   
2231 C  CA  . ILE B 10  ? 0.4193 0.6814 1.1072 0.1046  0.0788  -0.1214 1480 ILE B CA  
2232 C  C   . ILE B 10  ? 0.3743 0.5968 1.0312 0.0951  0.0775  -0.1100 1480 ILE B C   
2233 O  O   . ILE B 10  ? 0.3694 0.5627 1.0011 0.0963  0.0831  -0.1037 1480 ILE B O   
2234 C  CB  . ILE B 10  ? 0.3320 0.6316 1.0444 0.0887  0.0927  -0.1233 1480 ILE B CB  
2235 C  CG1 . ILE B 10  ? 0.7142 1.0545 1.4561 0.0989  0.0970  -0.1354 1480 ILE B CG1 
2236 C  CG2 . ILE B 10  ? 0.3516 0.6355 1.0451 0.0753  0.1083  -0.1143 1480 ILE B CG2 
2237 C  CD1 . ILE B 10  ? 0.7151 1.0434 1.4390 0.1101  0.1042  -0.1369 1480 ILE B CD1 
2238 N  N   . TYR B 11  ? 0.4381 0.6597 1.0968 0.0859  0.0695  -0.1080 1481 TYR B N   
2239 C  CA  . TYR B 11  ? 0.3496 0.5367 0.9808 0.0767  0.0690  -0.0986 1481 TYR B CA  
2240 C  C   . TYR B 11  ? 0.5115 0.6629 1.1145 0.0898  0.0595  -0.0955 1481 TYR B C   
2241 O  O   . TYR B 11  ? 0.4568 0.5780 1.0335 0.0866  0.0650  -0.0878 1481 TYR B O   
2242 C  CB  . TYR B 11  ? 0.3515 0.5471 0.9924 0.0644  0.0621  -0.0991 1481 TYR B CB  
2243 C  CG  . TYR B 11  ? 0.3716 0.5981 1.0371 0.0481  0.0726  -0.1001 1481 TYR B CG  
2244 C  CD1 . TYR B 11  ? 0.3892 0.6050 1.0446 0.0331  0.0852  -0.0923 1481 TYR B CD1 
2245 C  CD2 . TYR B 11  ? 0.4849 0.7521 1.1840 0.0476  0.0699  -0.1087 1481 TYR B CD2 
2246 C  CE1 . TYR B 11  ? 0.3293 0.5708 1.0045 0.0172  0.0947  -0.0918 1481 TYR B CE1 
2247 C  CE2 . TYR B 11  ? 0.4452 0.7412 1.1660 0.0310  0.0805  -0.1088 1481 TYR B CE2 
2248 C  CZ  . TYR B 11  ? 0.4634 0.7450 1.1709 0.0153  0.0929  -0.0998 1481 TYR B CZ  
2249 O  OH  . TYR B 11  ? 0.3816 0.6895 1.1082 -0.0022 0.1033  -0.0987 1481 TYR B OH  
2250 N  N   . LYS B 12  ? 0.3876 0.5421 0.9954 0.1045  0.0452  -0.1011 1482 LYS B N   
2251 C  CA  . LYS B 12  ? 0.6041 0.7238 1.1837 0.1167  0.0361  -0.0972 1482 LYS B CA  
2252 C  C   . LYS B 12  ? 0.4500 0.5528 1.0155 0.1225  0.0457  -0.0941 1482 LYS B C   
2253 O  O   . LYS B 12  ? 0.4151 0.4844 0.9519 0.1226  0.0466  -0.0867 1482 LYS B O   
2254 C  CB  . LYS B 12  ? 0.6866 0.8131 1.2746 0.1324  0.0180  -0.1036 1482 LYS B CB  
2255 C  CG  . LYS B 12  ? 0.8145 0.9020 1.3700 0.1437  0.0075  -0.0981 1482 LYS B CG  
2256 C  CD  . LYS B 12  ? 0.8581 0.9443 1.4123 0.1524  -0.0128 -0.1009 1482 LYS B CD  
2257 C  CE  . LYS B 12  ? 0.8336 0.8806 1.3542 0.1643  -0.0233 -0.0947 1482 LYS B CE  
2258 N  NZ  . LYS B 12  ? 0.9104 0.9574 1.4380 0.1825  -0.0293 -0.0988 1482 LYS B NZ  
2259 N  N   . ARG B 13  ? 0.3815 0.5082 0.9672 0.1266  0.0534  -0.1002 1483 ARG B N   
2260 C  CA  . ARG B 13  ? 0.4076 0.5192 0.9809 0.1320  0.0620  -0.0986 1483 ARG B CA  
2261 C  C   . ARG B 13  ? 0.4649 0.5615 1.0216 0.1174  0.0759  -0.0902 1483 ARG B C   
2262 O  O   . ARG B 13  ? 0.5473 0.6172 1.0823 0.1196  0.0795  -0.0854 1483 ARG B O   
2263 C  CB  . ARG B 13  ? 0.4759 0.6191 1.0751 0.1400  0.0673  -0.1087 1483 ARG B CB  
2264 C  CG  . ARG B 13  ? 0.6818 0.8203 1.2836 0.1608  0.0546  -0.1155 1483 ARG B CG  
2265 C  CD  . ARG B 13  ? 0.8745 0.9707 1.4448 0.1669  0.0532  -0.1091 1483 ARG B CD  
2266 N  NE  . ARG B 13  ? 0.9537 1.0457 1.5164 0.1587  0.0693  -0.1066 1483 ARG B NE  
2267 C  CZ  . ARG B 13  ? 0.8758 0.9804 1.4487 0.1660  0.0761  -0.1142 1483 ARG B CZ  
2268 N  NH1 . ARG B 13  ? 0.6120 0.7329 1.1979 0.1805  0.0679  -0.1238 1483 ARG B NH1 
2269 N  NH2 . ARG B 13  ? 0.8689 0.9688 1.4327 0.1577  0.0899  -0.1117 1483 ARG B NH2 
2270 N  N   . ILE B 14  ? 0.5329 0.6453 1.0996 0.1022  0.0832  -0.0882 1484 ILE B N   
2271 C  CA  . ILE B 14  ? 0.3658 0.4619 0.9162 0.0893  0.0944  -0.0799 1484 ILE B CA  
2272 C  C   . ILE B 14  ? 0.3588 0.4197 0.8815 0.0891  0.0889  -0.0728 1484 ILE B C   
2273 O  O   . ILE B 14  ? 0.3822 0.4213 0.8857 0.0867  0.0954  -0.0669 1484 ILE B O   
2274 C  CB  . ILE B 14  ? 0.4091 0.5255 0.9742 0.0732  0.1013  -0.0786 1484 ILE B CB  
2275 C  CG1 . ILE B 14  ? 0.6434 0.7924 1.2307 0.0703  0.1116  -0.0835 1484 ILE B CG1 
2276 C  CG2 . ILE B 14  ? 0.3779 0.4712 0.9233 0.0616  0.1081  -0.0695 1484 ILE B CG2 
2277 C  CD1 . ILE B 14  ? 0.5054 0.6783 1.1110 0.0544  0.1160  -0.0829 1484 ILE B CD1 
2278 N  N   . PHE B 15  ? 0.3681 0.4247 0.8886 0.0910  0.0769  -0.0736 1485 PHE B N   
2279 C  CA  . PHE B 15  ? 0.4167 0.4419 0.9101 0.0909  0.0717  -0.0676 1485 PHE B CA  
2280 C  C   . PHE B 15  ? 0.5093 0.5100 0.9826 0.1018  0.0695  -0.0649 1485 PHE B C   
2281 O  O   . PHE B 15  ? 0.4975 0.4748 0.9495 0.0980  0.0753  -0.0584 1485 PHE B O   
2282 C  CB  . PHE B 15  ? 0.3901 0.4177 0.8852 0.0923  0.0581  -0.0705 1485 PHE B CB  
2283 C  CG  . PHE B 15  ? 0.4062 0.4028 0.8718 0.0939  0.0516  -0.0654 1485 PHE B CG  
2284 C  CD1 . PHE B 15  ? 0.4055 0.3906 0.8588 0.0833  0.0549  -0.0620 1485 PHE B CD1 
2285 C  CD2 . PHE B 15  ? 0.6675 0.6459 1.1165 0.1062  0.0419  -0.0642 1485 PHE B CD2 
2286 C  CE1 . PHE B 15  ? 0.4550 0.4137 0.8805 0.0848  0.0501  -0.0582 1485 PHE B CE1 
2287 C  CE2 . PHE B 15  ? 0.4857 0.4358 0.9051 0.1065  0.0369  -0.0589 1485 PHE B CE2 
2288 C  CZ  . PHE B 15  ? 0.4487 0.3904 0.8566 0.0958  0.0416  -0.0563 1485 PHE B CZ  
2289 N  N   . THR B 16  ? 0.4181 0.4232 0.8981 0.1154  0.0601  -0.0699 1486 THR B N   
2290 C  CA  . THR B 16  ? 0.4193 0.3978 0.8793 0.1259  0.0560  -0.0671 1486 THR B CA  
2291 C  C   . THR B 16  ? 0.4417 0.4124 0.8959 0.1224  0.0690  -0.0645 1486 THR B C   
2292 O  O   . THR B 16  ? 0.6312 0.5741 1.0620 0.1214  0.0710  -0.0581 1486 THR B O   
2293 C  CB  . THR B 16  ? 0.6418 0.6282 1.1136 0.1422  0.0437  -0.0741 1486 THR B CB  
2294 O  OG1 . THR B 16  ? 0.7989 0.8152 1.2978 0.1448  0.0505  -0.0821 1486 THR B OG1 
2295 C  CG2 . THR B 16  ? 0.4558 0.4508 0.9339 0.1466  0.0288  -0.0771 1486 THR B CG2 
2296 N  N   . ASP B 17  ? 0.4138 0.4099 0.8891 0.1200  0.0781  -0.0696 1487 ASP B N   
2297 C  CA  . ASP B 17  ? 0.4448 0.4352 0.9144 0.1161  0.0901  -0.0677 1487 ASP B CA  
2298 C  C   . ASP B 17  ? 0.6443 0.6176 1.0964 0.1034  0.0977  -0.0590 1487 ASP B C   
2299 O  O   . ASP B 17  ? 0.5068 0.4587 0.9417 0.1027  0.1014  -0.0546 1487 ASP B O   
2300 C  CB  . ASP B 17  ? 0.4050 0.4277 0.8986 0.1134  0.0992  -0.0741 1487 ASP B CB  
2301 C  CG  . ASP B 17  ? 0.8893 0.9279 1.3992 0.1279  0.0945  -0.0841 1487 ASP B CG  
2302 O  OD1 . ASP B 17  ? 0.9395 1.0073 1.4696 0.1268  0.1021  -0.0905 1487 ASP B OD1 
2303 O  OD2 . ASP B 17  ? 0.9994 1.0212 1.5015 0.1406  0.0830  -0.0855 1487 ASP B OD2 
2304 N  N   . MET B 18  ? 0.3928 0.3751 0.8497 0.0936  0.0994  -0.0569 1488 MET B N   
2305 C  CA  . MET B 18  ? 0.3670 0.3363 0.8106 0.0826  0.1069  -0.0500 1488 MET B CA  
2306 C  C   . MET B 18  ? 0.3984 0.3385 0.8170 0.0843  0.1029  -0.0445 1488 MET B C   
2307 O  O   . MET B 18  ? 0.3808 0.3064 0.7862 0.0797  0.1099  -0.0396 1488 MET B O   
2308 C  CB  . MET B 18  ? 0.4873 0.4700 0.9412 0.0730  0.1077  -0.0499 1488 MET B CB  
2309 C  CG  . MET B 18  ? 0.8058 0.7764 1.2484 0.0630  0.1150  -0.0438 1488 MET B CG  
2310 S  SD  . MET B 18  ? 0.9338 0.9213 1.3895 0.0540  0.1270  -0.0426 1488 MET B SD  
2311 C  CE  . MET B 18  ? 0.7772 0.7520 1.2207 0.0585  0.1328  -0.0408 1488 MET B CE  
2312 N  N   . VAL B 19  ? 0.4127 0.3450 0.8244 0.0905  0.0917  -0.0453 1489 VAL B N   
2313 C  CA  . VAL B 19  ? 0.4122 0.3175 0.7979 0.0908  0.0882  -0.0396 1489 VAL B CA  
2314 C  C   . VAL B 19  ? 0.5712 0.4561 0.9422 0.0975  0.0866  -0.0368 1489 VAL B C   
2315 O  O   . VAL B 19  ? 0.5426 0.4042 0.8907 0.0957  0.0864  -0.0308 1489 VAL B O   
2316 C  CB  . VAL B 19  ? 0.4268 0.3286 0.8063 0.0949  0.0758  -0.0408 1489 VAL B CB  
2317 C  CG1 . VAL B 19  ? 0.5628 0.4809 0.9544 0.0872  0.0761  -0.0437 1489 VAL B CG1 
2318 C  CG2 . VAL B 19  ? 0.4383 0.3456 0.8264 0.1077  0.0636  -0.0456 1489 VAL B CG2 
2319 N  N   . SER B 20  ? 0.4261 0.3187 0.8092 0.1050  0.0855  -0.0414 1490 SER B N   
2320 C  CA  . SER B 20  ? 0.6160 0.4884 0.9866 0.1100  0.0852  -0.0394 1490 SER B CA  
2321 C  C   . SER B 20  ? 0.6319 0.5087 1.0072 0.1038  0.0973  -0.0394 1490 SER B C   
2322 O  O   . SER B 20  ? 0.5852 0.4463 0.9518 0.1067  0.0979  -0.0387 1490 SER B O   
2323 C  CB  . SER B 20  ? 0.5636 0.4377 0.9423 0.1245  0.0743  -0.0454 1490 SER B CB  
2324 O  OG  . SER B 20  ? 0.6481 0.5456 1.0493 0.1276  0.0795  -0.0532 1490 SER B OG  
2325 N  N   . SER B 21  ? 0.5314 0.4271 0.9191 0.0955  0.1058  -0.0402 1491 SER B N   
2326 C  CA  . SER B 21  ? 0.4565 0.3575 0.8486 0.0906  0.1158  -0.0406 1491 SER B CA  
2327 C  C   . SER B 21  ? 0.6963 0.5798 1.0720 0.0817  0.1223  -0.0335 1491 SER B C   
2328 O  O   . SER B 21  ? 0.4883 0.3647 0.8547 0.0765  0.1226  -0.0288 1491 SER B O   
2329 C  CB  . SER B 21  ? 0.4906 0.4195 0.9025 0.0851  0.1223  -0.0438 1491 SER B CB  
2330 O  OG  . SER B 21  ? 0.6885 0.6192 1.0992 0.0766  0.1321  -0.0411 1491 SER B OG  
2331 N  N   . PRO B 22  ? 0.5580 0.4366 0.9311 0.0798  0.1278  -0.0335 1492 PRO B N   
2332 C  CA  . PRO B 22  ? 0.5262 0.3920 0.8871 0.0710  0.1339  -0.0275 1492 PRO B CA  
2333 C  C   . PRO B 22  ? 0.6454 0.5265 1.0146 0.0622  0.1418  -0.0258 1492 PRO B C   
2334 O  O   . PRO B 22  ? 0.4720 0.3724 0.8556 0.0617  0.1436  -0.0289 1492 PRO B O   
2335 C  CB  . PRO B 22  ? 0.6160 0.4734 0.9739 0.0724  0.1355  -0.0295 1492 PRO B CB  
2336 C  CG  . PRO B 22  ? 0.6748 0.5510 1.0486 0.0791  0.1350  -0.0375 1492 PRO B CG  
2337 C  CD  . PRO B 22  ? 0.6292 0.5140 1.0106 0.0861  0.1280  -0.0399 1492 PRO B CD  
2338 N  N   . GLY B 23  ? 0.6172 0.4890 0.9770 0.0552  0.1462  -0.0206 1493 GLY B N   
2339 C  CA  . GLY B 23  ? 0.4946 0.3778 0.8613 0.0479  0.1529  -0.0188 1493 GLY B CA  
2340 C  C   . GLY B 23  ? 0.6211 0.5133 0.9938 0.0462  0.1522  -0.0187 1493 GLY B C   
2341 O  O   . GLY B 23  ? 0.5237 0.4274 0.9054 0.0417  0.1561  -0.0182 1493 GLY B O   
2342 N  N   . THR B 24  ? 0.5305 0.4161 0.8969 0.0495  0.1467  -0.0188 1494 THR B N   
2343 C  CA  . THR B 24  ? 0.4575 0.3502 0.8290 0.0480  0.1447  -0.0197 1494 THR B CA  
2344 C  C   . THR B 24  ? 0.6114 0.4932 0.9706 0.0451  0.1461  -0.0171 1494 THR B C   
2345 O  O   . THR B 24  ? 0.4763 0.3614 0.8379 0.0436  0.1444  -0.0185 1494 THR B O   
2346 C  CB  . THR B 24  ? 0.4330 0.3293 0.8080 0.0541  0.1363  -0.0234 1494 THR B CB  
2347 O  OG1 . THR B 24  ? 0.4527 0.3317 0.8117 0.0592  0.1312  -0.0219 1494 THR B OG1 
2348 C  CG2 . THR B 24  ? 0.5266 0.4395 0.9178 0.0571  0.1358  -0.0276 1494 THR B CG2 
2349 N  N   . ASN B 25  ? 0.4287 0.2978 0.7746 0.0439  0.1492  -0.0139 1495 ASN B N   
2350 C  CA  . ASN B 25  ? 0.4685 0.3290 0.8020 0.0413  0.1517  -0.0120 1495 ASN B CA  
2351 C  C   . ASN B 25  ? 0.5929 0.4594 0.9323 0.0360  0.1597  -0.0109 1495 ASN B C   
2352 O  O   . ASN B 25  ? 0.4962 0.3574 0.8283 0.0330  0.1648  -0.0084 1495 ASN B O   
2353 C  CB  . ASN B 25  ? 0.4883 0.3322 0.8031 0.0420  0.1508  -0.0086 1495 ASN B CB  
2354 C  CG  . ASN B 25  ? 0.5611 0.3976 0.8610 0.0394  0.1539  -0.0071 1495 ASN B CG  
2355 O  OD1 . ASN B 25  ? 0.5835 0.4254 0.8857 0.0395  0.1538  -0.0101 1495 ASN B OD1 
2356 N  ND2 . ASN B 25  ? 0.4930 0.3168 0.7769 0.0366  0.1567  -0.0028 1495 ASN B ND2 
2357 N  N   . CYS B 26  ? 0.5383 0.4162 0.8917 0.0348  0.1602  -0.0126 1496 CYS B N   
2358 C  CA  . CYS B 26  ? 0.5303 0.4133 0.8899 0.0311  0.1659  -0.0115 1496 CYS B CA  
2359 C  C   . CYS B 26  ? 0.4210 0.3104 0.7907 0.0303  0.1640  -0.0133 1496 CYS B C   
2360 O  O   . CYS B 26  ? 0.4765 0.3699 0.8515 0.0310  0.1593  -0.0149 1496 CYS B O   
2361 C  CB  . CYS B 26  ? 0.4609 0.3489 0.8266 0.0288  0.1693  -0.0095 1496 CYS B CB  
2362 S  SG  . CYS B 26  ? 0.5843 0.4828 0.9616 0.0294  0.1666  -0.0107 1496 CYS B SG  
2363 N  N   . ALA B 27  ? 0.3994 0.2899 0.7724 0.0287  0.1675  -0.0129 1497 ALA B N   
2364 C  CA  . ALA B 27  ? 0.4150 0.3078 0.7964 0.0275  0.1653  -0.0139 1497 ALA B CA  
2365 C  C   . ALA B 27  ? 0.5797 0.4808 0.9715 0.0246  0.1636  -0.0119 1497 ALA B C   
2366 O  O   . ALA B 27  ? 0.3869 0.2898 0.7842 0.0227  0.1599  -0.0127 1497 ALA B O   
2367 C  CB  . ALA B 27  ? 0.3373 0.2295 0.7214 0.0276  0.1688  -0.0136 1497 ALA B CB  
2368 N  N   . GLU B 28  ? 0.4903 0.3969 0.8844 0.0236  0.1664  -0.0095 1498 GLU B N   
2369 C  CA  . GLU B 28  ? 0.5097 0.4256 0.9118 0.0207  0.1662  -0.0078 1498 GLU B CA  
2370 C  C   . GLU B 28  ? 0.5364 0.4581 0.9418 0.0215  0.1631  -0.0104 1498 GLU B C   
2371 O  O   . GLU B 28  ? 0.6176 0.5492 1.0307 0.0183  0.1634  -0.0097 1498 GLU B O   
2372 C  CB  . GLU B 28  ? 0.4894 0.4092 0.8909 0.0201  0.1695  -0.0060 1498 GLU B CB  
2373 C  CG  . GLU B 28  ? 0.5803 0.4999 0.9835 0.0182  0.1714  -0.0029 1498 GLU B CG  
2374 C  CD  . GLU B 28  ? 0.5172 0.4309 0.9166 0.0202  0.1732  -0.0038 1498 GLU B CD  
2375 O  OE1 . GLU B 28  ? 0.4319 0.3406 0.8245 0.0222  0.1739  -0.0058 1498 GLU B OE1 
2376 O  OE2 . GLU B 28  ? 0.4596 0.3742 0.8625 0.0200  0.1739  -0.0023 1498 GLU B OE2 
2377 N  N   . ALA B 29  ? 0.4355 0.3521 0.8350 0.0256  0.1601  -0.0132 1499 ALA B N   
2378 C  CA  . ALA B 29  ? 0.5009 0.4240 0.9051 0.0276  0.1557  -0.0164 1499 ALA B CA  
2379 C  C   . ALA B 29  ? 0.4455 0.3703 0.8550 0.0250  0.1515  -0.0180 1499 ALA B C   
2380 O  O   . ALA B 29  ? 0.3955 0.3278 0.8111 0.0262  0.1469  -0.0211 1499 ALA B O   
2381 C  CB  . ALA B 29  ? 0.3966 0.3117 0.7912 0.0337  0.1526  -0.0182 1499 ALA B CB  
2382 N  N   . TYR B 30  ? 0.4052 0.3233 0.8133 0.0218  0.1521  -0.0166 1500 TYR B N   
2383 C  CA  . TYR B 30  ? 0.3634 0.2794 0.7745 0.0194  0.1471  -0.0191 1500 TYR B CA  
2384 C  C   . TYR B 30  ? 0.3329 0.2627 0.7575 0.0146  0.1449  -0.0196 1500 TYR B C   
2385 O  O   . TYR B 30  ? 0.4270 0.3609 0.8556 0.0148  0.1391  -0.0234 1500 TYR B O   
2386 C  CB  . TYR B 30  ? 0.4526 0.3591 0.8622 0.0166  0.1481  -0.0177 1500 TYR B CB  
2387 C  CG  . TYR B 30  ? 0.3474 0.2511 0.7611 0.0128  0.1423  -0.0204 1500 TYR B CG  
2388 C  CD1 . TYR B 30  ? 0.3571 0.2535 0.7634 0.0160  0.1372  -0.0256 1500 TYR B CD1 
2389 C  CD2 . TYR B 30  ? 0.3474 0.2553 0.7715 0.0052  0.1414  -0.0177 1500 TYR B CD2 
2390 C  CE1 . TYR B 30  ? 0.4708 0.3641 0.8809 0.0120  0.1308  -0.0291 1500 TYR B CE1 
2391 C  CE2 . TYR B 30  ? 0.3685 0.2725 0.7968 0.0003  0.1355  -0.0203 1500 TYR B CE2 
2392 C  CZ  . TYR B 30  ? 0.4041 0.3011 0.8260 0.0039  0.1299  -0.0265 1500 TYR B CZ  
2393 O  OH  . TYR B 30  ? 0.3763 0.2693 0.8022 -0.0012 0.1231  -0.0299 1500 TYR B OH  
2394 N  N   . HIS B 31  ? 0.3983 0.3366 0.8300 0.0098  0.1494  -0.0159 1501 HIS B N   
2395 C  CA  . HIS B 31  ? 0.4328 0.3859 0.8774 0.0033  0.1490  -0.0158 1501 HIS B CA  
2396 C  C   . HIS B 31  ? 0.5497 0.5183 1.0015 0.0074  0.1480  -0.0201 1501 HIS B C   
2397 O  O   . HIS B 31  ? 0.3931 0.3759 0.8574 0.0033  0.1459  -0.0224 1501 HIS B O   
2398 C  CB  . HIS B 31  ? 0.3423 0.2992 0.7895 -0.0036 0.1544  -0.0099 1501 HIS B CB  
2399 C  CG  . HIS B 31  ? 0.5527 0.4971 0.9983 -0.0097 0.1525  -0.0060 1501 HIS B CG  
2400 N  ND1 . HIS B 31  ? 0.7512 0.6958 1.2039 -0.0173 0.1486  -0.0062 1501 HIS B ND1 
2401 C  CD2 . HIS B 31  ? 0.7719 0.7024 1.2102 -0.0090 0.1533  -0.0023 1501 HIS B CD2 
2402 C  CE1 . HIS B 31  ? 0.6694 0.5982 1.1178 -0.0207 0.1468  -0.0025 1501 HIS B CE1 
2403 N  NE2 . HIS B 31  ? 0.6551 0.5758 1.0952 -0.0151 0.1495  -0.0003 1501 HIS B NE2 
2404 N  N   . SER B 32  ? 0.4067 0.3725 0.8515 0.0156  0.1489  -0.0217 1502 SER B N   
2405 C  CA  . SER B 32  ? 0.3999 0.3777 0.8513 0.0215  0.1461  -0.0266 1502 SER B CA  
2406 C  C   . SER B 32  ? 0.3288 0.3040 0.7807 0.0245  0.1374  -0.0305 1502 SER B C   
2407 O  O   . SER B 32  ? 0.3349 0.3260 0.8002 0.0245  0.1335  -0.0346 1502 SER B O   
2408 C  CB  . SER B 32  ? 0.4665 0.4379 0.9087 0.0297  0.1476  -0.0273 1502 SER B CB  
2409 O  OG  . SER B 32  ? 0.4585 0.4314 0.8987 0.0275  0.1546  -0.0246 1502 SER B OG  
2410 N  N   . TRP B 33  ? 0.3336 0.2906 0.7718 0.0262  0.1345  -0.0297 1503 TRP B N   
2411 C  CA  . TRP B 33  ? 0.3723 0.3255 0.8080 0.0288  0.1257  -0.0335 1503 TRP B CA  
2412 C  C   . TRP B 33  ? 0.3943 0.3547 0.8415 0.0206  0.1223  -0.0352 1503 TRP B C   
2413 O  O   . TRP B 33  ? 0.4540 0.4244 0.9103 0.0209  0.1150  -0.0396 1503 TRP B O   
2414 C  CB  . TRP B 33  ? 0.3521 0.2842 0.7678 0.0323  0.1246  -0.0324 1503 TRP B CB  
2415 C  CG  . TRP B 33  ? 0.4156 0.3387 0.8186 0.0392  0.1263  -0.0307 1503 TRP B CG  
2416 C  CD1 . TRP B 33  ? 0.5105 0.4229 0.9026 0.0391  0.1329  -0.0269 1503 TRP B CD1 
2417 C  CD2 . TRP B 33  ? 0.4247 0.3476 0.8245 0.0468  0.1203  -0.0326 1503 TRP B CD2 
2418 N  NE1 . TRP B 33  ? 0.3608 0.2654 0.7426 0.0448  0.1319  -0.0260 1503 TRP B NE1 
2419 C  CE2 . TRP B 33  ? 0.4742 0.3836 0.8596 0.0502  0.1239  -0.0292 1503 TRP B CE2 
2420 C  CE3 . TRP B 33  ? 0.5270 0.4598 0.9354 0.0514  0.1116  -0.0369 1503 TRP B CE3 
2421 C  CZ2 . TRP B 33  ? 0.4190 0.3214 0.7966 0.0577  0.1188  -0.0295 1503 TRP B CZ2 
2422 C  CZ3 . TRP B 33  ? 0.4825 0.4098 0.8841 0.0602  0.1061  -0.0376 1503 TRP B CZ3 
2423 C  CH2 . TRP B 33  ? 0.4501 0.3607 0.8354 0.0633  0.1096  -0.0336 1503 TRP B CH2 
2424 N  N   . ALA B 34  ? 0.4426 0.3974 0.8899 0.0131  0.1267  -0.0317 1504 ALA B N   
2425 C  CA  . ALA B 34  ? 0.3479 0.3056 0.8047 0.0041  0.1232  -0.0326 1504 ALA B CA  
2426 C  C   . ALA B 34  ? 0.3739 0.3556 0.8503 -0.0008 0.1225  -0.0343 1504 ALA B C   
2427 O  O   . ALA B 34  ? 0.4061 0.3952 0.8918 -0.0042 0.1155  -0.0385 1504 ALA B O   
2428 C  CB  . ALA B 34  ? 0.3524 0.2995 0.8065 -0.0027 0.1280  -0.0275 1504 ALA B CB  
2429 N  N   . ASP B 35  ? 0.3954 0.3907 0.8784 -0.0012 0.1300  -0.0318 1505 ASP B N   
2430 C  CA  . ASP B 35  ? 0.3785 0.4001 0.8806 -0.0048 0.1312  -0.0344 1505 ASP B CA  
2431 C  C   . ASP B 35  ? 0.5122 0.5445 1.0219 0.0028  0.1227  -0.0416 1505 ASP B C   
2432 O  O   . ASP B 35  ? 0.3901 0.4379 0.9154 -0.0025 0.1178  -0.0453 1505 ASP B O   
2433 C  CB  . ASP B 35  ? 0.3714 0.4043 0.8752 -0.0032 0.1405  -0.0322 1505 ASP B CB  
2434 C  CG  . ASP B 35  ? 0.5801 0.6437 1.1043 -0.0051 0.1429  -0.0365 1505 ASP B CG  
2435 O  OD1 . ASP B 35  ? 0.4212 0.4955 0.9483 0.0042  0.1447  -0.0407 1505 ASP B OD1 
2436 O  OD2 . ASP B 35  ? 0.5494 0.6267 1.0871 -0.0160 0.1431  -0.0362 1505 ASP B OD2 
2437 N  N   . LEU B 36  ? 0.5098 0.5330 1.0083 0.0150  0.1200  -0.0434 1506 LEU B N   
2438 C  CA  . LEU B 36  ? 0.4047 0.4348 0.9080 0.0234  0.1102  -0.0496 1506 LEU B CA  
2439 C  C   . LEU B 36  ? 0.3487 0.3734 0.8519 0.0190  0.1009  -0.0520 1506 LEU B C   
2440 O  O   . LEU B 36  ? 0.3512 0.3939 0.8710 0.0174  0.0940  -0.0571 1506 LEU B O   
2441 C  CB  . LEU B 36  ? 0.3437 0.3575 0.8298 0.0359  0.1079  -0.0494 1506 LEU B CB  
2442 C  CG  . LEU B 36  ? 0.3549 0.3667 0.8383 0.0458  0.0956  -0.0540 1506 LEU B CG  
2443 C  CD1 . LEU B 36  ? 0.4481 0.4861 0.9532 0.0517  0.0922  -0.0601 1506 LEU B CD1 
2444 C  CD2 . LEU B 36  ? 0.4335 0.4209 0.8931 0.0547  0.0942  -0.0511 1506 LEU B CD2 
2445 N  N   . ARG B 37  ? 0.3546 0.3557 0.8402 0.0166  0.1007  -0.0491 1507 ARG B N   
2446 C  CA  . ARG B 37  ? 0.4612 0.4540 0.9439 0.0122  0.0922  -0.0522 1507 ARG B CA  
2447 C  C   . ARG B 37  ? 0.4446 0.4552 0.9487 0.0002  0.0907  -0.0539 1507 ARG B C   
2448 O  O   . ARG B 37  ? 0.4574 0.4781 0.9716 -0.0012 0.0811  -0.0595 1507 ARG B O   
2449 C  CB  . ARG B 37  ? 0.3715 0.3387 0.8349 0.0103  0.0953  -0.0491 1507 ARG B CB  
2450 C  CG  . ARG B 37  ? 0.3866 0.3413 0.8430 0.0071  0.0864  -0.0536 1507 ARG B CG  
2451 C  CD  . ARG B 37  ? 0.3915 0.3247 0.8345 0.0041  0.0911  -0.0512 1507 ARG B CD  
2452 N  NE  . ARG B 37  ? 0.4925 0.4299 0.9471 -0.0051 0.0980  -0.0463 1507 ARG B NE  
2453 C  CZ  . ARG B 37  ? 0.6036 0.5282 1.0507 -0.0060 0.1051  -0.0416 1507 ARG B CZ  
2454 N  NH1 . ARG B 37  ? 0.3853 0.2941 0.8151 0.0016  0.1075  -0.0418 1507 ARG B NH1 
2455 N  NH2 . ARG B 37  ? 0.3785 0.3072 0.8358 -0.0148 0.1098  -0.0366 1507 ARG B NH2 
2456 N  N   . ASP B 38  ? 0.3586 0.3739 0.8699 -0.0091 0.1000  -0.0489 1508 ASP B N   
2457 C  CA  . ASP B 38  ? 0.3614 0.3904 0.8905 -0.0228 0.0992  -0.0492 1508 ASP B CA  
2458 C  C   . ASP B 38  ? 0.5043 0.5655 1.0567 -0.0227 0.0968  -0.0543 1508 ASP B C   
2459 O  O   . ASP B 38  ? 0.4597 0.5327 1.0264 -0.0294 0.0890  -0.0589 1508 ASP B O   
2460 C  CB  . ASP B 38  ? 0.3583 0.3834 0.8869 -0.0326 0.1096  -0.0414 1508 ASP B CB  
2461 C  CG  . ASP B 38  ? 0.6225 0.6166 1.1310 -0.0324 0.1102  -0.0374 1508 ASP B CG  
2462 O  OD1 . ASP B 38  ? 0.3740 0.3509 0.8710 -0.0277 0.1029  -0.0415 1508 ASP B OD1 
2463 O  OD2 . ASP B 38  ? 0.3626 0.3501 0.8666 -0.0364 0.1179  -0.0307 1508 ASP B OD2 
2464 N  N   . VAL B 39  ? 0.3971 0.4725 0.9535 -0.0136 0.1020  -0.0549 1509 VAL B N   
2465 C  CA  . VAL B 39  ? 0.3433 0.4513 0.9236 -0.0117 0.0999  -0.0610 1509 VAL B CA  
2466 C  C   . VAL B 39  ? 0.4113 0.5211 0.9949 -0.0049 0.0854  -0.0681 1509 VAL B C   
2467 O  O   . VAL B 39  ? 0.3735 0.5043 0.9777 -0.0118 0.0792  -0.0729 1509 VAL B O   
2468 C  CB  . VAL B 39  ? 0.3343 0.4536 0.9159 -0.0009 0.1072  -0.0617 1509 VAL B CB  
2469 C  CG1 . VAL B 39  ? 0.3956 0.5464 1.0009 0.0054  0.1026  -0.0700 1509 VAL B CG1 
2470 C  CG2 . VAL B 39  ? 0.3275 0.4512 0.9088 -0.0091 0.1212  -0.0557 1509 VAL B CG2 
2471 N  N   . LEU B 40  ? 0.4213 0.5066 0.9827 0.0064  0.0791  -0.0681 1510 LEU B N   
2472 C  CA  . LEU B 40  ? 0.4197 0.5050 0.9808 0.0135  0.0644  -0.0743 1510 LEU B CA  
2473 C  C   . LEU B 40  ? 0.3999 0.4818 0.9644 0.0019  0.0569  -0.0767 1510 LEU B C   
2474 O  O   . LEU B 40  ? 0.3846 0.4842 0.9653 0.0008  0.0462  -0.0831 1510 LEU B O   
2475 C  CB  . LEU B 40  ? 0.3766 0.4350 0.9102 0.0267  0.0601  -0.0727 1510 LEU B CB  
2476 C  CG  . LEU B 40  ? 0.4124 0.4748 0.9446 0.0406  0.0618  -0.0727 1510 LEU B CG  
2477 C  CD1 . LEU B 40  ? 0.3837 0.4159 0.8859 0.0506  0.0583  -0.0695 1510 LEU B CD1 
2478 C  CD2 . LEU B 40  ? 0.3745 0.4643 0.9296 0.0479  0.0527  -0.0801 1510 LEU B CD2 
2479 N  N   . PHE B 41  ? 0.3813 0.4420 0.9328 -0.0074 0.0623  -0.0719 1511 PHE B N   
2480 C  CA  . PHE B 41  ? 0.3936 0.4471 0.9467 -0.0187 0.0549  -0.0746 1511 PHE B CA  
2481 C  C   . PHE B 41  ? 0.3917 0.4751 0.9751 -0.0314 0.0537  -0.0773 1511 PHE B C   
2482 O  O   . PHE B 41  ? 0.4013 0.4944 0.9957 -0.0348 0.0418  -0.0839 1511 PHE B O   
2483 C  CB  . PHE B 41  ? 0.3974 0.4240 0.9340 -0.0258 0.0615  -0.0691 1511 PHE B CB  
2484 C  CG  . PHE B 41  ? 0.4120 0.4296 0.9514 -0.0383 0.0545  -0.0720 1511 PHE B CG  
2485 C  CD1 . PHE B 41  ? 0.4865 0.4930 1.0164 -0.0353 0.0414  -0.0791 1511 PHE B CD1 
2486 C  CD2 . PHE B 41  ? 0.5012 0.5200 1.0513 -0.0534 0.0602  -0.0676 1511 PHE B CD2 
2487 C  CE1 . PHE B 41  ? 0.4433 0.4401 0.9754 -0.0468 0.0340  -0.0829 1511 PHE B CE1 
2488 C  CE2 . PHE B 41  ? 0.5575 0.5654 1.1100 -0.0657 0.0528  -0.0703 1511 PHE B CE2 
2489 C  CZ  . PHE B 41  ? 0.6190 0.6159 1.1630 -0.0622 0.0396  -0.0785 1511 PHE B CZ  
2490 N  N   . ASN B 42  ? 0.3804 0.4804 0.9775 -0.0385 0.0660  -0.0726 1512 ASN B N   
2491 C  CA  . ASN B 42  ? 0.3804 0.5105 1.0062 -0.0525 0.0668  -0.0746 1512 ASN B CA  
2492 C  C   . ASN B 42  ? 0.3781 0.5386 1.0250 -0.0447 0.0579  -0.0833 1512 ASN B C   
2493 O  O   . ASN B 42  ? 0.3855 0.5629 1.0513 -0.0533 0.0489  -0.0888 1512 ASN B O   
2494 C  CB  . ASN B 42  ? 0.3701 0.5139 1.0044 -0.0606 0.0824  -0.0678 1512 ASN B CB  
2495 C  CG  . ASN B 42  ? 0.8035 0.9779 1.4660 -0.0781 0.0849  -0.0687 1512 ASN B CG  
2496 O  OD1 . ASN B 42  ? 0.8443 1.0157 1.5137 -0.0908 0.0772  -0.0704 1512 ASN B OD1 
2497 N  ND2 . ASN B 42  ? 0.8260 1.0303 1.5048 -0.0793 0.0959  -0.0681 1512 ASN B ND2 
2498 N  N   . LEU B 43  ? 0.3710 0.5349 1.0128 -0.0273 0.0580  -0.0850 1513 LEU B N   
2499 C  CA  . LEU B 43  ? 0.5802 0.7717 1.2418 -0.0175 0.0483  -0.0935 1513 LEU B CA  
2500 C  C   . LEU B 43  ? 0.3859 0.5691 1.0440 -0.0164 0.0306  -0.0993 1513 LEU B C   
2501 O  O   . LEU B 43  ? 0.3898 0.5998 1.0729 -0.0214 0.0218  -0.1061 1513 LEU B O   
2502 C  CB  . LEU B 43  ? 0.4184 0.6070 1.0703 0.0020  0.0500  -0.0939 1513 LEU B CB  
2503 C  CG  . LEU B 43  ? 0.5865 0.8001 1.2563 0.0166  0.0402  -0.1022 1513 LEU B CG  
2504 C  CD1 . LEU B 43  ? 0.7286 0.9328 1.3855 0.0320  0.0464  -0.1001 1513 LEU B CD1 
2505 C  CD2 . LEU B 43  ? 0.5699 0.7730 1.2319 0.0244  0.0213  -0.1069 1513 LEU B CD2 
2506 N  N   . CYS B 44  ? 0.3957 0.5426 1.0230 -0.0116 0.0257  -0.0969 1514 CYS B N   
2507 C  CA  . CYS B 44  ? 0.4565 0.5949 1.0770 -0.0089 0.0085  -0.1030 1514 CYS B CA  
2508 C  C   . CYS B 44  ? 0.4211 0.5636 1.0540 -0.0268 0.0036  -0.1060 1514 CYS B C   
2509 O  O   . CYS B 44  ? 0.5342 0.6811 1.1716 -0.0272 -0.0118 -0.1131 1514 CYS B O   
2510 C  CB  . CYS B 44  ? 0.5933 0.6925 1.1760 0.0003  0.0057  -0.1001 1514 CYS B CB  
2511 S  SG  . CYS B 44  ? 0.5863 0.6746 1.1500 0.0204  0.0093  -0.0961 1514 CYS B SG  
2512 N  N   . GLU B 45  ? 0.4163 0.5556 1.0535 -0.0419 0.0155  -0.1004 1515 GLU B N   
2513 C  CA  . GLU B 45  ? 0.5389 0.6815 1.1894 -0.0608 0.0112  -0.1025 1515 GLU B CA  
2514 C  C   . GLU B 45  ? 0.6791 0.8650 1.3674 -0.0691 0.0081  -0.1079 1515 GLU B C   
2515 O  O   . GLU B 45  ? 0.7114 0.9050 1.4138 -0.0821 -0.0017 -0.1129 1515 GLU B O   
2516 C  CB  . GLU B 45  ? 0.7873 0.9118 1.4301 -0.0743 0.0244  -0.0939 1515 GLU B CB  
2517 C  CG  . GLU B 45  ? 0.8257 0.9080 1.4345 -0.0686 0.0258  -0.0902 1515 GLU B CG  
2518 C  CD  . GLU B 45  ? 0.9388 0.9982 1.5358 -0.0738 0.0128  -0.0961 1515 GLU B CD  
2519 O  OE1 . GLU B 45  ? 1.0884 1.1327 1.6849 -0.0881 0.0143  -0.0938 1515 GLU B OE1 
2520 O  OE2 . GLU B 45  ? 0.8531 0.9084 1.4402 -0.0634 0.0005  -0.1030 1515 GLU B OE2 
2521 N  N   . ASN B 46  ? 0.4076 0.6229 1.1134 -0.0620 0.0161  -0.1076 1516 ASN B N   
2522 C  CA  . ASN B 46  ? 0.4028 0.6641 1.1471 -0.0693 0.0157  -0.1131 1516 ASN B CA  
2523 C  C   . ASN B 46  ? 0.5476 0.8308 1.3065 -0.0555 -0.0006 -0.1233 1516 ASN B C   
2524 O  O   . ASN B 46  ? 0.7261 1.0475 1.5188 -0.0627 -0.0054 -0.1300 1516 ASN B O   
2525 C  CB  . ASN B 46  ? 0.4875 0.7718 1.2446 -0.0693 0.0337  -0.1087 1516 ASN B CB  
2526 C  CG  . ASN B 46  ? 0.7741 1.0426 1.5215 -0.0862 0.0486  -0.0985 1516 ASN B CG  
2527 O  OD1 . ASN B 46  ? 0.8668 1.1180 1.6096 -0.1022 0.0455  -0.0959 1516 ASN B OD1 
2528 N  ND2 . ASN B 46  ? 0.9129 1.1857 1.6562 -0.0824 0.0640  -0.0929 1516 ASN B ND2 
2529 N  N   . LEU B 47  ? 0.6561 0.9175 1.3911 -0.0360 -0.0091 -0.1244 1517 LEU B N   
2530 C  CA  . LEU B 47  ? 0.7352 1.0130 1.4806 -0.0223 -0.0268 -0.1332 1517 LEU B CA  
2531 C  C   . LEU B 47  ? 0.9258 1.2066 1.6795 -0.0336 -0.0431 -0.1399 1517 LEU B C   
2532 O  O   . LEU B 47  ? 1.0525 1.3683 1.8364 -0.0339 -0.0543 -0.1483 1517 LEU B O   
2533 C  CB  . LEU B 47  ? 0.6874 0.9340 1.3993 -0.0014 -0.0327 -0.1311 1517 LEU B CB  
2534 C  CG  . LEU B 47  ? 0.7044 0.9429 1.4045 0.0104  -0.0183 -0.1249 1517 LEU B CG  
2535 C  CD1 . LEU B 47  ? 0.7470 0.9487 1.4101 0.0268  -0.0245 -0.1215 1517 LEU B CD1 
2536 C  CD2 . LEU B 47  ? 0.5934 0.8718 1.3250 0.0191  -0.0154 -0.1299 1517 LEU B CD2 
2537 N  N   . VAL B 48  ? 1.1797 1.4245 1.9073 -0.0426 -0.0452 -0.1369 1518 VAL B N   
2538 C  CA  . VAL B 48  ? 1.3251 1.5657 2.0553 -0.0542 -0.0607 -0.1435 1518 VAL B CA  
2539 C  C   . VAL B 48  ? 1.3058 1.5774 2.0724 -0.0769 -0.0583 -0.1460 1518 VAL B C   
2540 O  O   . VAL B 48  ? 1.1909 1.4651 1.9648 -0.0907 -0.0420 -0.1392 1518 VAL B O   
2541 C  CB  . VAL B 48  ? 1.3638 1.5553 2.0547 -0.0569 -0.0616 -0.1402 1518 VAL B CB  
2542 C  CG1 . VAL B 48  ? 1.2844 1.4475 1.9404 -0.0370 -0.0589 -0.1357 1518 VAL B CG1 
2543 C  CG2 . VAL B 48  ? 1.3651 1.5422 2.0546 -0.0751 -0.0469 -0.1333 1518 VAL B CG2 
2544 N  N   . SER B 55  ? 1.1808 1.3612 1.7865 0.0991  -0.1776 -0.1568 1525 SER B N   
2545 C  CA  . SER B 55  ? 1.1661 1.3622 1.7937 0.0986  -0.1574 -0.1534 1525 SER B CA  
2546 C  C   . SER B 55  ? 1.1935 1.3554 1.7874 0.1083  -0.1458 -0.1432 1525 SER B C   
2547 O  O   . SER B 55  ? 1.1510 1.2882 1.7227 0.0984  -0.1305 -0.1370 1525 SER B O   
2548 C  CB  . SER B 55  ? 1.1303 1.3378 1.7758 0.0769  -0.1401 -0.1536 1525 SER B CB  
2549 O  OG  . SER B 55  ? 1.1079 1.3398 1.7808 0.0770  -0.1232 -0.1521 1525 SER B OG  
2550 N  N   . PRO B 56  ? 1.1946 1.3537 1.7843 0.1276  -0.1535 -0.1416 1526 PRO B N   
2551 C  CA  . PRO B 56  ? 1.1999 1.3231 1.7549 0.1365  -0.1437 -0.1314 1526 PRO B CA  
2552 C  C   . PRO B 56  ? 1.1696 1.2960 1.7344 0.1305  -0.1193 -0.1270 1526 PRO B C   
2553 O  O   . PRO B 56  ? 1.1444 1.2390 1.6786 0.1291  -0.1071 -0.1184 1526 PRO B O   
2554 C  CB  . PRO B 56  ? 1.1583 1.2829 1.7143 0.1582  -0.1603 -0.1324 1526 PRO B CB  
2555 C  CG  . PRO B 56  ? 1.0099 1.1851 1.6181 0.1602  -0.1666 -0.1436 1526 PRO B CG  
2556 C  CD  . PRO B 56  ? 1.0926 1.2865 1.7167 0.1413  -0.1680 -0.1495 1526 PRO B CD  
2557 N  N   . ALA B 57  ? 1.1542 1.3193 1.7606 0.1269  -0.1116 -0.1328 1527 ALA B N   
2558 C  CA  . ALA B 57  ? 1.0983 1.2666 1.7121 0.1211  -0.0889 -0.1288 1527 ALA B CA  
2559 C  C   . ALA B 57  ? 0.9614 1.1195 1.5668 0.1009  -0.0745 -0.1248 1527 ALA B C   
2560 O  O   . ALA B 57  ? 0.9756 1.1146 1.5647 0.0969  -0.0580 -0.1176 1527 ALA B O   
2561 C  CB  . ALA B 57  ? 1.0849 1.2984 1.7438 0.1240  -0.0847 -0.1364 1527 ALA B CB  
2562 N  N   . HIS B 58  ? 0.7542 0.9247 1.3714 0.0881  -0.0814 -0.1298 1528 HIS B N   
2563 C  CA  . HIS B 58  ? 0.8784 1.0322 1.4826 0.0704  -0.0716 -0.1264 1528 HIS B CA  
2564 C  C   . HIS B 58  ? 0.8457 0.9549 1.4044 0.0739  -0.0696 -0.1191 1528 HIS B C   
2565 O  O   . HIS B 58  ? 0.6859 0.7773 1.2306 0.0658  -0.0541 -0.1131 1528 HIS B O   
2566 C  CB  . HIS B 58  ? 0.7173 0.8866 1.3375 0.0581  -0.0836 -0.1338 1528 HIS B CB  
2567 N  N   . GLU B 59  ? 0.8695 0.9608 1.4042 0.0861  -0.0854 -0.1193 1529 GLU B N   
2568 C  CA  . GLU B 59  ? 0.8792 0.9300 1.3698 0.0883  -0.0831 -0.1126 1529 GLU B CA  
2569 C  C   . GLU B 59  ? 0.8041 0.8383 1.2802 0.0946  -0.0681 -0.1040 1529 GLU B C   
2570 O  O   . GLU B 59  ? 0.7475 0.7565 1.1987 0.0893  -0.0563 -0.0981 1529 GLU B O   
2571 C  CB  . GLU B 59  ? 0.8595 0.8952 1.3259 0.0994  -0.1036 -0.1141 1529 GLU B CB  
2572 C  CG  . GLU B 59  ? 0.9582 0.9996 1.4262 0.0922  -0.1189 -0.1221 1529 GLU B CG  
2573 C  CD  . GLU B 59  ? 1.1301 1.1535 1.5819 0.0773  -0.1096 -0.1222 1529 GLU B CD  
2574 O  OE1 . GLU B 59  ? 1.2123 1.2080 1.6351 0.0771  -0.0970 -0.1154 1529 GLU B OE1 
2575 O  OE2 . GLU B 59  ? 1.1500 1.1866 1.6184 0.0659  -0.1155 -0.1296 1529 GLU B OE2 
2576 N  N   . GLU B 60  ? 0.6836 0.7325 1.1766 0.1057  -0.0682 -0.1039 1530 GLU B N   
2577 C  CA  . GLU B 60  ? 0.6313 0.6642 1.1116 0.1106  -0.0543 -0.0965 1530 GLU B CA  
2578 C  C   . GLU B 60  ? 0.5847 0.6261 1.0784 0.0979  -0.0341 -0.0945 1530 GLU B C   
2579 O  O   . GLU B 60  ? 0.6066 0.6262 1.0801 0.0958  -0.0213 -0.0875 1530 GLU B O   
2580 C  CB  . GLU B 60  ? 0.6976 0.7414 1.1911 0.1267  -0.0602 -0.0980 1530 GLU B CB  
2581 C  CG  . GLU B 60  ? 0.8604 0.8845 1.3386 0.1318  -0.0471 -0.0907 1530 GLU B CG  
2582 C  CD  . GLU B 60  ? 0.9299 0.9619 1.4205 0.1484  -0.0531 -0.0930 1530 GLU B CD  
2583 O  OE1 . GLU B 60  ? 0.7575 0.7633 1.2233 0.1603  -0.0628 -0.0886 1530 GLU B OE1 
2584 O  OE2 . GLU B 60  ? 0.8703 0.9338 1.3946 0.1496  -0.0477 -0.0993 1530 GLU B OE2 
2585 N  N   . PHE B 61  ? 0.4596 0.5319 0.9862 0.0882  -0.0312 -0.1000 1531 PHE B N   
2586 C  CA  . PHE B 61  ? 0.6001 0.6776 1.1360 0.0749  -0.0130 -0.0970 1531 PHE B CA  
2587 C  C   . PHE B 61  ? 0.5950 0.6476 1.1083 0.0635  -0.0086 -0.0935 1531 PHE B C   
2588 O  O   . PHE B 61  ? 0.5603 0.6005 1.0645 0.0576  0.0060  -0.0878 1531 PHE B O   
2589 C  CB  . PHE B 61  ? 0.4870 0.6033 1.0623 0.0659  -0.0108 -0.1030 1531 PHE B CB  
2590 C  CG  . PHE B 61  ? 0.5599 0.7023 1.1591 0.0737  -0.0046 -0.1053 1531 PHE B CG  
2591 C  CD1 . PHE B 61  ? 0.7293 0.8644 1.3221 0.0746  0.0110  -0.1001 1531 PHE B CD1 
2592 C  CD2 . PHE B 61  ? 0.6388 0.8140 1.2674 0.0804  -0.0147 -0.1137 1531 PHE B CD2 
2593 C  CE1 . PHE B 61  ? 0.6595 0.8180 1.2728 0.0823  0.0167  -0.1035 1531 PHE B CE1 
2594 C  CE2 . PHE B 61  ? 0.6879 0.8881 1.3388 0.0888  -0.0085 -0.1172 1531 PHE B CE2 
2595 C  CZ  . PHE B 61  ? 0.5253 0.7162 1.1674 0.0897  0.0074  -0.1123 1531 PHE B CZ  
2596 N  N   . LYS B 62  ? 0.5327 0.5773 1.0360 0.0613  -0.0215 -0.0973 1532 LYS B N   
2597 C  CA  . LYS B 62  ? 0.6008 0.6196 1.0798 0.0530  -0.0184 -0.0954 1532 LYS B CA  
2598 C  C   . LYS B 62  ? 0.6055 0.5940 1.0505 0.0601  -0.0115 -0.0884 1532 LYS B C   
2599 O  O   . LYS B 62  ? 0.5124 0.4853 0.9451 0.0538  0.0008  -0.0844 1532 LYS B O   
2600 C  CB  . LYS B 62  ? 0.5671 0.5829 1.0397 0.0512  -0.0353 -0.1022 1532 LYS B CB  
2601 C  CG  . LYS B 62  ? 0.6814 0.7229 1.1853 0.0390  -0.0410 -0.1093 1532 LYS B CG  
2602 C  CD  . LYS B 62  ? 0.8209 0.8526 1.3122 0.0362  -0.0572 -0.1161 1532 LYS B CD  
2603 C  CE  . LYS B 62  ? 1.0068 1.0654 1.5208 0.0401  -0.0750 -0.1235 1532 LYS B CE  
2604 N  NZ  . LYS B 62  ? 1.0729 1.1251 1.5783 0.0351  -0.0914 -0.1312 1532 LYS B NZ  
2605 N  N   . THR B 63  ? 0.4888 0.4688 0.9190 0.0732  -0.0196 -0.0867 1533 THR B N   
2606 C  CA  . THR B 63  ? 0.5930 0.5449 0.9912 0.0787  -0.0130 -0.0794 1533 THR B CA  
2607 C  C   . THR B 63  ? 0.4935 0.4465 0.8988 0.0768  0.0042  -0.0739 1533 THR B C   
2608 O  O   . THR B 63  ? 0.5928 0.5274 0.9797 0.0730  0.0154  -0.0689 1533 THR B O   
2609 C  CB  . THR B 63  ? 0.6221 0.5640 1.0039 0.0924  -0.0259 -0.0777 1533 THR B CB  
2610 O  OG1 . THR B 63  ? 0.6654 0.6027 1.0349 0.0936  -0.0420 -0.0823 1533 THR B OG1 
2611 C  CG2 . THR B 63  ? 0.5275 0.4410 0.8774 0.0964  -0.0181 -0.0692 1533 THR B CG2 
2612 N  N   . MET B 64  ? 0.4892 0.4654 0.9220 0.0790  0.0065  -0.0754 1534 MET B N   
2613 C  CA  . MET B 64  ? 0.4809 0.4593 0.9202 0.0767  0.0222  -0.0710 1534 MET B CA  
2614 C  C   . MET B 64  ? 0.6120 0.5886 1.0534 0.0633  0.0341  -0.0693 1534 MET B C   
2615 O  O   . MET B 64  ? 0.4560 0.4192 0.8856 0.0611  0.0460  -0.0638 1534 MET B O   
2616 C  CB  . MET B 64  ? 0.4912 0.4978 0.9605 0.0809  0.0227  -0.0746 1534 MET B CB  
2617 C  CG  . MET B 64  ? 0.5985 0.6011 1.0631 0.0964  0.0147  -0.0748 1534 MET B CG  
2618 S  SD  . MET B 64  ? 0.6347 0.6750 1.1375 0.1045  0.0094  -0.0832 1534 MET B SD  
2619 C  CE  . MET B 64  ? 0.6338 0.6975 1.1604 0.0925  0.0283  -0.0835 1534 MET B CE  
2620 N  N   . LEU B 65  ? 0.5477 0.5365 1.0036 0.0543  0.0300  -0.0739 1535 LEU B N   
2621 C  CA  . LEU B 65  ? 0.4835 0.4672 0.9403 0.0420  0.0392  -0.0723 1535 LEU B CA  
2622 C  C   . LEU B 65  ? 0.4322 0.3867 0.8588 0.0425  0.0425  -0.0693 1535 LEU B C   
2623 O  O   . LEU B 65  ? 0.4347 0.3802 0.8563 0.0380  0.0542  -0.0650 1535 LEU B O   
2624 C  CB  . LEU B 65  ? 0.4762 0.4738 0.9508 0.0321  0.0317  -0.0782 1535 LEU B CB  
2625 C  CG  . LEU B 65  ? 0.4240 0.4113 0.8970 0.0195  0.0381  -0.0770 1535 LEU B CG  
2626 C  CD1 . LEU B 65  ? 0.4062 0.3994 0.8895 0.0137  0.0530  -0.0710 1535 LEU B CD1 
2627 C  CD2 . LEU B 65  ? 0.4319 0.4310 0.9217 0.0093  0.0281  -0.0835 1535 LEU B CD2 
2628 N  N   . LEU B 66  ? 0.4519 0.3928 0.8585 0.0479  0.0322  -0.0718 1536 LEU B N   
2629 C  CA  . LEU B 66  ? 0.4929 0.4084 0.8702 0.0484  0.0359  -0.0699 1536 LEU B CA  
2630 C  C   . LEU B 66  ? 0.5571 0.4614 0.9210 0.0528  0.0474  -0.0626 1536 LEU B C   
2631 O  O   . LEU B 66  ? 0.5216 0.4138 0.8746 0.0494  0.0576  -0.0601 1536 LEU B O   
2632 C  CB  . LEU B 66  ? 0.4895 0.3939 0.8458 0.0540  0.0224  -0.0736 1536 LEU B CB  
2633 C  CG  . LEU B 66  ? 0.6284 0.5080 0.9519 0.0550  0.0263  -0.0725 1536 LEU B CG  
2634 C  CD1 . LEU B 66  ? 0.5053 0.3789 0.8293 0.0466  0.0322  -0.0764 1536 LEU B CD1 
2635 C  CD2 . LEU B 66  ? 0.5335 0.4036 0.8349 0.0611  0.0121  -0.0754 1536 LEU B CD2 
2636 N  N   . ILE B 67  ? 0.4571 0.3658 0.8230 0.0606  0.0454  -0.0598 1537 ILE B N   
2637 C  CA  . ILE B 67  ? 0.4532 0.3514 0.8078 0.0642  0.0550  -0.0532 1537 ILE B CA  
2638 C  C   . ILE B 67  ? 0.5334 0.4398 0.9034 0.0577  0.0683  -0.0508 1537 ILE B C   
2639 O  O   . ILE B 67  ? 0.4999 0.3949 0.8585 0.0563  0.0785  -0.0462 1537 ILE B O   
2640 C  CB  . ILE B 67  ? 0.4579 0.3591 0.8146 0.0741  0.0483  -0.0518 1537 ILE B CB  
2641 C  CG1 . ILE B 67  ? 0.5235 0.4082 0.8556 0.0815  0.0362  -0.0511 1537 ILE B CG1 
2642 C  CG2 . ILE B 67  ? 0.4483 0.3447 0.8036 0.0759  0.0591  -0.0462 1537 ILE B CG2 
2643 C  CD1 . ILE B 67  ? 0.5942 0.4852 0.9340 0.0921  0.0246  -0.0521 1537 ILE B CD1 
2644 N  N   . ALA B 68  ? 0.4341 0.3612 0.8301 0.0535  0.0683  -0.0536 1538 ALA B N   
2645 C  CA  . ALA B 68  ? 0.4931 0.4276 0.9019 0.0468  0.0802  -0.0507 1538 ALA B CA  
2646 C  C   . ALA B 68  ? 0.5071 0.4298 0.9080 0.0394  0.0856  -0.0498 1538 ALA B C   
2647 O  O   . ALA B 68  ? 0.4154 0.3337 0.8147 0.0366  0.0958  -0.0457 1538 ALA B O   
2648 C  CB  . ALA B 68  ? 0.4068 0.3667 0.8435 0.0427  0.0794  -0.0536 1538 ALA B CB  
2649 N  N   . HIS B 69  ? 0.4125 0.3299 0.8088 0.0368  0.0782  -0.0543 1539 HIS B N   
2650 C  CA  . HIS B 69  ? 0.4725 0.3766 0.8604 0.0314  0.0822  -0.0549 1539 HIS B CA  
2651 C  C   . HIS B 69  ? 0.4851 0.3717 0.8499 0.0362  0.0888  -0.0521 1539 HIS B C   
2652 O  O   . HIS B 69  ? 0.4343 0.3148 0.7973 0.0335  0.0974  -0.0500 1539 HIS B O   
2653 C  CB  . HIS B 69  ? 0.4321 0.3324 0.8178 0.0284  0.0718  -0.0617 1539 HIS B CB  
2654 C  CG  . HIS B 69  ? 0.6398 0.5213 1.0085 0.0273  0.0741  -0.0641 1539 HIS B CG  
2655 N  ND1 . HIS B 69  ? 0.4392 0.3155 0.8137 0.0216  0.0807  -0.0631 1539 HIS B ND1 
2656 C  CD2 . HIS B 69  ? 0.4628 0.3293 0.8083 0.0318  0.0706  -0.0679 1539 HIS B CD2 
2657 C  CE1 . HIS B 69  ? 0.5501 0.4098 0.9075 0.0235  0.0811  -0.0671 1539 HIS B CE1 
2658 N  NE2 . HIS B 69  ? 0.5893 0.4436 0.9286 0.0293  0.0756  -0.0703 1539 HIS B NE2 
2659 N  N   . TYR B 70  ? 0.4354 0.3146 0.7829 0.0430  0.0845  -0.0518 1540 TYR B N   
2660 C  CA  . TYR B 70  ? 0.4699 0.3342 0.7954 0.0461  0.0916  -0.0484 1540 TYR B CA  
2661 C  C   . TYR B 70  ? 0.4816 0.3490 0.8137 0.0453  0.1027  -0.0425 1540 TYR B C   
2662 O  O   . TYR B 70  ? 0.5148 0.3758 0.8404 0.0436  0.1115  -0.0408 1540 TYR B O   
2663 C  CB  . TYR B 70  ? 0.4607 0.3162 0.7664 0.0525  0.0849  -0.0472 1540 TYR B CB  
2664 C  CG  . TYR B 70  ? 0.4824 0.3299 0.7721 0.0539  0.0751  -0.0525 1540 TYR B CG  
2665 C  CD1 . TYR B 70  ? 0.4897 0.3312 0.7736 0.0503  0.0763  -0.0580 1540 TYR B CD1 
2666 C  CD2 . TYR B 70  ? 0.4984 0.3428 0.7775 0.0596  0.0636  -0.0525 1540 TYR B CD2 
2667 C  CE1 . TYR B 70  ? 0.5122 0.3456 0.7792 0.0518  0.0668  -0.0638 1540 TYR B CE1 
2668 C  CE2 . TYR B 70  ? 0.5688 0.4056 0.8312 0.0610  0.0536  -0.0573 1540 TYR B CE2 
2669 C  CZ  . TYR B 70  ? 0.5837 0.4153 0.8398 0.0568  0.0553  -0.0633 1540 TYR B CZ  
2670 O  OH  . TYR B 70  ? 0.5719 0.3956 0.8097 0.0585  0.0444  -0.0689 1540 TYR B OH  
2671 N  N   . TYR B 71  ? 0.4727 0.3507 0.8179 0.0469  0.1019  -0.0401 1541 TYR B N   
2672 C  CA  . TYR B 71  ? 0.4026 0.2832 0.7530 0.0462  0.1115  -0.0352 1541 TYR B CA  
2673 C  C   . TYR B 71  ? 0.4468 0.3331 0.8099 0.0398  0.1187  -0.0346 1541 TYR B C   
2674 O  O   . TYR B 71  ? 0.4745 0.3564 0.8338 0.0386  0.1270  -0.0314 1541 TYR B O   
2675 C  CB  . TYR B 71  ? 0.4361 0.3276 0.7986 0.0498  0.1086  -0.0346 1541 TYR B CB  
2676 C  CG  . TYR B 71  ? 0.4087 0.2898 0.7566 0.0570  0.1046  -0.0324 1541 TYR B CG  
2677 C  CD1 . TYR B 71  ? 0.4210 0.2891 0.7544 0.0572  0.1114  -0.0275 1541 TYR B CD1 
2678 C  CD2 . TYR B 71  ? 0.4183 0.3024 0.7678 0.0633  0.0936  -0.0351 1541 TYR B CD2 
2679 C  CE1 . TYR B 71  ? 0.4346 0.2901 0.7535 0.0628  0.1072  -0.0246 1541 TYR B CE1 
2680 C  CE2 . TYR B 71  ? 0.4330 0.3049 0.7686 0.0705  0.0886  -0.0325 1541 TYR B CE2 
2681 C  CZ  . TYR B 71  ? 0.5416 0.3977 0.8609 0.0699  0.0954  -0.0269 1541 TYR B CZ  
2682 O  OH  . TYR B 71  ? 0.5058 0.3468 0.8099 0.0762  0.0897  -0.0236 1541 TYR B OH  
2683 N  N   . ALA B 72  ? 0.3847 0.2805 0.7630 0.0354  0.1151  -0.0374 1542 ALA B N   
2684 C  CA  . ALA B 72  ? 0.4738 0.3720 0.8621 0.0291  0.1207  -0.0358 1542 ALA B CA  
2685 C  C   . ALA B 72  ? 0.3839 0.2677 0.7600 0.0289  0.1237  -0.0369 1542 ALA B C   
2686 O  O   . ALA B 72  ? 0.3812 0.2628 0.7590 0.0275  0.1306  -0.0340 1542 ALA B O   
2687 C  CB  . ALA B 72  ? 0.3738 0.2830 0.7791 0.0228  0.1158  -0.0381 1542 ALA B CB  
2688 N  N   . THR B 73  ? 0.3989 0.2736 0.7628 0.0311  0.1182  -0.0416 1543 THR B N   
2689 C  CA  . THR B 73  ? 0.4088 0.2710 0.7606 0.0322  0.1214  -0.0443 1543 THR B CA  
2690 C  C   . THR B 73  ? 0.4078 0.2661 0.7480 0.0358  0.1301  -0.0409 1543 THR B C   
2691 O  O   . THR B 73  ? 0.4081 0.2624 0.7467 0.0360  0.1362  -0.0415 1543 THR B O   
2692 C  CB  . THR B 73  ? 0.4511 0.3049 0.7900 0.0340  0.1134  -0.0509 1543 THR B CB  
2693 O  OG1 . THR B 73  ? 0.4371 0.2960 0.7888 0.0295  0.1046  -0.0542 1543 THR B OG1 
2694 C  CG2 . THR B 73  ? 0.4690 0.3106 0.7960 0.0356  0.1171  -0.0556 1543 THR B CG2 
2695 N  N   . ARG B 74  ? 0.4080 0.2675 0.7411 0.0384  0.1304  -0.0376 1544 ARG B N   
2696 C  CA  . ARG B 74  ? 0.4079 0.2639 0.7313 0.0397  0.1385  -0.0337 1544 ARG B CA  
2697 C  C   . ARG B 74  ? 0.4535 0.3167 0.7908 0.0372  0.1456  -0.0300 1544 ARG B C   
2698 O  O   . ARG B 74  ? 0.4499 0.3116 0.7845 0.0370  0.1527  -0.0293 1544 ARG B O   
2699 C  CB  . ARG B 74  ? 0.4808 0.3338 0.7940 0.0424  0.1359  -0.0303 1544 ARG B CB  
2700 C  CG  . ARG B 74  ? 0.5229 0.3705 0.8246 0.0420  0.1442  -0.0256 1544 ARG B CG  
2701 C  CD  . ARG B 74  ? 0.4261 0.2672 0.7176 0.0444  0.1403  -0.0215 1544 ARG B CD  
2702 N  NE  . ARG B 74  ? 0.5097 0.3589 0.8175 0.0452  0.1384  -0.0200 1544 ARG B NE  
2703 C  CZ  . ARG B 74  ? 0.4179 0.2625 0.7218 0.0486  0.1339  -0.0176 1544 ARG B CZ  
2704 N  NH1 . ARG B 74  ? 0.4384 0.2686 0.7218 0.0509  0.1304  -0.0151 1544 ARG B NH1 
2705 N  NH2 . ARG B 74  ? 0.4057 0.2590 0.7248 0.0498  0.1332  -0.0178 1544 ARG B NH2 
2706 N  N   . SER B 75  ? 0.3789 0.2511 0.7311 0.0352  0.1437  -0.0279 1545 SER B N   
2707 C  CA  . SER B 75  ? 0.4859 0.3642 0.8491 0.0326  0.1497  -0.0244 1545 SER B CA  
2708 C  C   . SER B 75  ? 0.3814 0.2572 0.7494 0.0310  0.1514  -0.0259 1545 SER B C   
2709 O  O   . SER B 75  ? 0.5626 0.4390 0.9326 0.0310  0.1570  -0.0241 1545 SER B O   
2710 C  CB  . SER B 75  ? 0.3548 0.2439 0.7314 0.0305  0.1480  -0.0224 1545 SER B CB  
2711 O  OG  . SER B 75  ? 0.5150 0.4056 0.8880 0.0335  0.1474  -0.0213 1545 SER B OG  
2712 N  N   . ALA B 76  ? 0.4569 0.3290 0.8267 0.0299  0.1458  -0.0298 1546 ALA B N   
2713 C  CA  . ALA B 76  ? 0.5477 0.4133 0.9201 0.0294  0.1459  -0.0322 1546 ALA B CA  
2714 C  C   . ALA B 76  ? 0.5614 0.4214 0.9234 0.0341  0.1513  -0.0350 1546 ALA B C   
2715 O  O   . ALA B 76  ? 0.4292 0.2889 0.7962 0.0354  0.1551  -0.0347 1546 ALA B O   
2716 C  CB  . ALA B 76  ? 0.3981 0.2579 0.7712 0.0274  0.1381  -0.0371 1546 ALA B CB  
2717 N  N   . ALA B 77  ? 0.4096 0.2658 0.7570 0.0368  0.1514  -0.0381 1547 ALA B N   
2718 C  CA  . ALA B 77  ? 0.4313 0.2844 0.7673 0.0403  0.1578  -0.0410 1547 ALA B CA  
2719 C  C   . ALA B 77  ? 0.5855 0.4460 0.9252 0.0398  0.1660  -0.0361 1547 ALA B C   
2720 O  O   . ALA B 77  ? 0.5502 0.4130 0.8912 0.0420  0.1720  -0.0381 1547 ALA B O   
2721 C  CB  . ALA B 77  ? 0.4365 0.2838 0.7534 0.0419  0.1560  -0.0436 1547 ALA B CB  
2722 N  N   . GLN B 78  ? 0.5383 0.4033 0.8806 0.0373  0.1659  -0.0303 1548 GLN B N   
2723 C  CA  . GLN B 78  ? 0.5453 0.4166 0.8913 0.0358  0.1725  -0.0259 1548 GLN B CA  
2724 C  C   . GLN B 78  ? 0.4258 0.3034 0.7871 0.0354  0.1742  -0.0248 1548 GLN B C   
2725 O  O   . GLN B 78  ? 0.4846 0.3684 0.8500 0.0345  0.1794  -0.0224 1548 GLN B O   
2726 C  CB  . GLN B 78  ? 0.4925 0.3653 0.8384 0.0337  0.1705  -0.0212 1548 GLN B CB  
2727 C  CG  . GLN B 78  ? 0.4007 0.2659 0.7302 0.0345  0.1690  -0.0206 1548 GLN B CG  
2728 C  CD  . GLN B 78  ? 0.4742 0.3390 0.8047 0.0346  0.1642  -0.0176 1548 GLN B CD  
2729 O  OE1 . GLN B 78  ? 0.4206 0.2922 0.7643 0.0343  0.1611  -0.0174 1548 GLN B OE1 
2730 N  NE2 . GLN B 78  ? 0.5036 0.3600 0.8196 0.0352  0.1636  -0.0153 1548 GLN B NE2 
2731 N  N   . SER B 79  ? 0.3648 0.2404 0.7343 0.0354  0.1692  -0.0259 1549 SER B N   
2732 C  CA  . SER B 79  ? 0.4778 0.3569 0.8596 0.0353  0.1697  -0.0238 1549 SER B CA  
2733 C  C   . SER B 79  ? 0.5480 0.4253 0.9319 0.0401  0.1720  -0.0284 1549 SER B C   
2734 O  O   . SER B 79  ? 0.5745 0.4549 0.9684 0.0412  0.1720  -0.0265 1549 SER B O   
2735 C  CB  . SER B 79  ? 0.5298 0.4064 0.9192 0.0321  0.1635  -0.0216 1549 SER B CB  
2736 O  OG  . SER B 79  ? 0.6881 0.5558 1.0740 0.0329  0.1587  -0.0264 1549 SER B OG  
2737 N  N   A VAL B 80  ? 0.5120 0.3847 0.8865 0.0435  0.1737  -0.0346 1550 VAL B N   
2738 N  N   B VAL B 80  ? 0.4931 0.3657 0.8673 0.0435  0.1737  -0.0346 1550 VAL B N   
2739 C  CA  A VAL B 80  ? 0.5252 0.3977 0.9024 0.0494  0.1765  -0.0405 1550 VAL B CA  
2740 C  CA  B VAL B 80  ? 0.5403 0.4116 0.9160 0.0495  0.1762  -0.0411 1550 VAL B CA  
2741 C  C   A VAL B 80  ? 0.5504 0.4273 0.9163 0.0512  0.1843  -0.0448 1550 VAL B C   
2742 C  C   B VAL B 80  ? 0.5656 0.4425 0.9308 0.0511  0.1845  -0.0448 1550 VAL B C   
2743 O  O   A VAL B 80  ? 0.5389 0.4104 0.8902 0.0501  0.1840  -0.0465 1550 VAL B O   
2744 O  O   B VAL B 80  ? 0.4708 0.3430 0.8211 0.0497  0.1847  -0.0461 1550 VAL B O   
2745 C  CB  A VAL B 80  ? 0.5343 0.3943 0.9119 0.0524  0.1698  -0.0458 1550 VAL B CB  
2746 C  CB  B VAL B 80  ? 0.5447 0.4029 0.9172 0.0521  0.1697  -0.0472 1550 VAL B CB  
2747 C  CG1 A VAL B 80  ? 0.4936 0.3503 0.8843 0.0515  0.1644  -0.0413 1550 VAL B CG1 
2748 C  CG1 B VAL B 80  ? 0.4704 0.3266 0.8460 0.0598  0.1717  -0.0548 1550 VAL B CG1 
2749 C  CG2 A VAL B 80  ? 0.5521 0.4041 0.9201 0.0490  0.1644  -0.0470 1550 VAL B CG2 
2750 C  CG2 B VAL B 80  ? 0.5353 0.3871 0.9162 0.0478  0.1616  -0.0425 1550 VAL B CG2 
2751 N  N   . LYS B 81  ? 0.6516 0.5391 1.0243 0.0538  0.1911  -0.0463 1551 LYS B N   
2752 C  CA  . LYS B 81  ? 0.5319 0.4276 0.8956 0.0529  0.2006  -0.0482 1551 LYS B CA  
2753 C  C   . LYS B 81  ? 0.4709 0.3601 0.8187 0.0563  0.2026  -0.0560 1551 LYS B C   
2754 O  O   . LYS B 81  ? 0.4265 0.3153 0.7580 0.0530  0.2073  -0.0552 1551 LYS B O   
2755 C  CB  . LYS B 81  ? 0.7837 0.6952 1.1616 0.0551  0.2073  -0.0496 1551 LYS B CB  
2756 N  N   . GLN B 82  ? 0.4262 0.3079 0.7762 0.0625  0.1981  -0.0633 1552 GLN B N   
2757 C  CA  . GLN B 82  ? 0.4912 0.3673 0.8245 0.0660  0.2004  -0.0719 1552 GLN B CA  
2758 C  C   . GLN B 82  ? 0.4701 0.3333 0.7867 0.0622  0.1936  -0.0703 1552 GLN B C   
2759 O  O   . GLN B 82  ? 0.5463 0.4037 0.8457 0.0643  0.1945  -0.0769 1552 GLN B O   
2760 C  CB  . GLN B 82  ? 0.6164 0.4878 0.9562 0.0750  0.1982  -0.0823 1552 GLN B CB  
2761 C  CG  . GLN B 82  ? 0.8955 0.7521 1.2432 0.0760  0.1864  -0.0821 1552 GLN B CG  
2762 C  CD  . GLN B 82  ? 0.9666 0.8269 1.3348 0.0773  0.1836  -0.0770 1552 GLN B CD  
2763 O  OE1 . GLN B 82  ? 0.7354 0.6095 1.1122 0.0746  0.1885  -0.0707 1552 GLN B OE1 
2764 N  NE2 . GLN B 82  ? 0.8079 0.6546 1.1830 0.0807  0.1748  -0.0794 1552 GLN B NE2 
2765 N  N   . LEU B 83  ? 0.4634 0.3234 0.7841 0.0569  0.1870  -0.0622 1553 LEU B N   
2766 C  CA  . LEU B 83  ? 0.4889 0.3400 0.7959 0.0537  0.1804  -0.0604 1553 LEU B CA  
2767 C  C   . LEU B 83  ? 0.5531 0.4076 0.8502 0.0490  0.1839  -0.0529 1553 LEU B C   
2768 O  O   . LEU B 83  ? 0.5028 0.3510 0.7912 0.0469  0.1774  -0.0499 1553 LEU B O   
2769 C  CB  . LEU B 83  ? 0.4535 0.2992 0.7724 0.0515  0.1701  -0.0580 1553 LEU B CB  
2770 C  CG  . LEU B 83  ? 0.4742 0.3112 0.7996 0.0546  0.1643  -0.0648 1553 LEU B CG  
2771 C  CD1 . LEU B 83  ? 0.4365 0.2697 0.7729 0.0498  0.1553  -0.0607 1553 LEU B CD1 
2772 C  CD2 . LEU B 83  ? 0.4669 0.2945 0.7757 0.0581  0.1621  -0.0746 1553 LEU B CD2 
2773 N  N   . GLU B 84  ? 0.4401 0.3039 0.7388 0.0473  0.1935  -0.0499 1554 GLU B N   
2774 C  CA  . GLU B 84  ? 0.4409 0.3050 0.7296 0.0421  0.1965  -0.0425 1554 GLU B CA  
2775 C  C   . GLU B 84  ? 0.5485 0.4019 0.8123 0.0416  0.1941  -0.0428 1554 GLU B C   
2776 O  O   . GLU B 84  ? 0.4917 0.3381 0.7478 0.0392  0.1885  -0.0370 1554 GLU B O   
2777 C  CB  . GLU B 84  ? 0.5646 0.4403 0.8568 0.0394  0.2080  -0.0408 1554 GLU B CB  
2778 C  CG  . GLU B 84  ? 0.7292 0.6026 1.0112 0.0327  0.2107  -0.0325 1554 GLU B CG  
2779 C  CD  . GLU B 84  ? 0.8275 0.7137 1.1174 0.0280  0.2210  -0.0301 1554 GLU B CD  
2780 O  OE1 . GLU B 84  ? 0.7524 0.6506 1.0488 0.0301  0.2287  -0.0358 1554 GLU B OE1 
2781 O  OE2 . GLU B 84  ? 0.8944 0.7788 1.1846 0.0222  0.2209  -0.0229 1554 GLU B OE2 
2782 N  N   . THR B 85  ? 0.4796 0.3312 0.7294 0.0444  0.1978  -0.0499 1555 THR B N   
2783 C  CA  . THR B 85  ? 0.5626 0.4035 0.7858 0.0434  0.1952  -0.0494 1555 THR B CA  
2784 C  C   . THR B 85  ? 0.6217 0.4526 0.8429 0.0456  0.1814  -0.0508 1555 THR B C   
2785 O  O   . THR B 85  ? 0.5775 0.3996 0.7823 0.0444  0.1755  -0.0468 1555 THR B O   
2786 C  CB  . THR B 85  ? 0.6303 0.4720 0.8357 0.0455  0.2031  -0.0571 1555 THR B CB  
2787 O  OG1 . THR B 85  ? 0.7375 0.5747 0.9437 0.0514  0.1971  -0.0673 1555 THR B OG1 
2788 C  CG2 . THR B 85  ? 0.6553 0.5123 0.8704 0.0445  0.2170  -0.0586 1555 THR B CG2 
2789 N  N   . VAL B 86  ? 0.6820 0.5139 0.9203 0.0485  0.1755  -0.0560 1556 VAL B N   
2790 C  CA  . VAL B 86  ? 0.5056 0.3312 0.7462 0.0488  0.1626  -0.0565 1556 VAL B CA  
2791 C  C   . VAL B 86  ? 0.5624 0.3895 0.8087 0.0460  0.1586  -0.0476 1556 VAL B C   
2792 O  O   . VAL B 86  ? 0.4997 0.3208 0.7351 0.0464  0.1504  -0.0458 1556 VAL B O   
2793 C  CB  . VAL B 86  ? 0.5178 0.3442 0.7778 0.0500  0.1577  -0.0617 1556 VAL B CB  
2794 C  CG1 . VAL B 86  ? 0.4806 0.3048 0.7480 0.0480  0.1452  -0.0603 1556 VAL B CG1 
2795 C  CG2 . VAL B 86  ? 0.5824 0.4029 0.8337 0.0540  0.1583  -0.0723 1556 VAL B CG2 
2796 N  N   . ALA B 87  ? 0.4603 0.2954 0.7230 0.0439  0.1639  -0.0424 1557 ALA B N   
2797 C  CA  . ALA B 87  ? 0.4499 0.2864 0.7183 0.0420  0.1606  -0.0352 1557 ALA B CA  
2798 C  C   . ALA B 87  ? 0.6213 0.4492 0.8680 0.0415  0.1604  -0.0307 1557 ALA B C   
2799 O  O   . ALA B 87  ? 0.5183 0.3414 0.7613 0.0428  0.1518  -0.0280 1557 ALA B O   
2800 C  CB  . ALA B 87  ? 0.4309 0.2764 0.7164 0.0396  0.1673  -0.0310 1557 ALA B CB  
2801 N  N   . ALA B 88  ? 0.5181 0.3438 0.7495 0.0398  0.1693  -0.0303 1558 ALA B N   
2802 C  CA  . ALA B 88  ? 0.5927 0.4083 0.8012 0.0377  0.1699  -0.0244 1558 ALA B CA  
2803 C  C   . ALA B 88  ? 0.5354 0.3401 0.7255 0.0410  0.1592  -0.0263 1558 ALA B C   
2804 O  O   . ALA B 88  ? 0.5539 0.3495 0.7343 0.0418  0.1517  -0.0210 1558 ALA B O   
2805 C  CB  . ALA B 88  ? 0.5355 0.3530 0.7312 0.0339  0.1827  -0.0240 1558 ALA B CB  
2806 N  N   . ARG B 89  ? 0.5262 0.3316 0.7129 0.0437  0.1570  -0.0345 1559 ARG B N   
2807 C  CA  . ARG B 89  ? 0.6350 0.4306 0.8035 0.0466  0.1459  -0.0372 1559 ARG B CA  
2808 C  C   . ARG B 89  ? 0.5607 0.3572 0.7433 0.0491  0.1327  -0.0359 1559 ARG B C   
2809 O  O   . ARG B 89  ? 0.5984 0.3864 0.7666 0.0515  0.1227  -0.0336 1559 ARG B O   
2810 C  CB  . ARG B 89  ? 0.5562 0.3522 0.7199 0.0487  0.1456  -0.0476 1559 ARG B CB  
2811 C  CG  . ARG B 89  ? 0.6549 0.4480 0.7948 0.0478  0.1564  -0.0502 1559 ARG B CG  
2812 C  CD  . ARG B 89  ? 0.6220 0.4166 0.7618 0.0511  0.1571  -0.0625 1559 ARG B CD  
2813 N  NE  . ARG B 89  ? 1.0101 0.8108 1.1450 0.0510  0.1717  -0.0667 1559 ARG B NE  
2814 C  CZ  . ARG B 89  ? 1.0790 0.8771 1.1867 0.0496  0.1797  -0.0670 1559 ARG B CZ  
2815 N  NH1 . ARG B 89  ? 1.0509 0.8374 1.1314 0.0480  0.1738  -0.0620 1559 ARG B NH1 
2816 N  NH2 . ARG B 89  ? 1.0385 0.8463 1.1461 0.0500  0.1938  -0.0722 1559 ARG B NH2 
2817 N  N   . LEU B 90  ? 0.6185 0.4259 0.8290 0.0487  0.1326  -0.0370 1560 LEU B N   
2818 C  CA  . LEU B 90  ? 0.5326 0.3441 0.7575 0.0507  0.1214  -0.0366 1560 LEU B CA  
2819 C  C   . LEU B 90  ? 0.5497 0.3562 0.7689 0.0522  0.1189  -0.0290 1560 LEU B C   
2820 O  O   . LEU B 90  ? 0.5146 0.3178 0.7299 0.0562  0.1073  -0.0286 1560 LEU B O   
2821 C  CB  . LEU B 90  ? 0.4759 0.3003 0.7298 0.0487  0.1229  -0.0387 1560 LEU B CB  
2822 C  CG  . LEU B 90  ? 0.4764 0.3024 0.7368 0.0476  0.1210  -0.0466 1560 LEU B CG  
2823 C  CD1 . LEU B 90  ? 0.4554 0.2902 0.7391 0.0446  0.1260  -0.0465 1560 LEU B CD1 
2824 C  CD2 . LEU B 90  ? 0.5386 0.3646 0.8000 0.0486  0.1078  -0.0514 1560 LEU B CD2 
2825 N  N   . SER B 91  ? 0.5272 0.3314 0.7433 0.0494  0.1288  -0.0233 1561 SER B N   
2826 C  CA  . SER B 91  ? 0.6685 0.4652 0.8793 0.0508  0.1255  -0.0164 1561 SER B CA  
2827 C  C   . SER B 91  ? 0.6805 0.4606 0.8618 0.0528  0.1192  -0.0131 1561 SER B C   
2828 O  O   . SER B 91  ? 0.6332 0.4066 0.8108 0.0578  0.1078  -0.0109 1561 SER B O   
2829 C  CB  . SER B 91  ? 0.5685 0.3651 0.7822 0.0461  0.1368  -0.0111 1561 SER B CB  
2830 O  OG  . SER B 91  ? 0.5621 0.3722 0.8021 0.0454  0.1398  -0.0126 1561 SER B OG  
2831 N  N   . VAL B 92  ? 0.5549 0.3297 0.7159 0.0501  0.1244  -0.0145 1562 VAL B N   
2832 C  CA  . VAL B 92  ? 0.6495 0.4083 0.7791 0.0515  0.1180  -0.0114 1562 VAL B CA  
2833 C  C   . VAL B 92  ? 0.6917 0.4502 0.8219 0.0578  0.1021  -0.0162 1562 VAL B C   
2834 O  O   . VAL B 92  ? 0.6721 0.4198 0.7902 0.0623  0.0905  -0.0121 1562 VAL B O   
2835 C  CB  . VAL B 92  ? 0.6734 0.4292 0.7812 0.0470  0.1286  -0.0131 1562 VAL B CB  
2836 C  CG1 . VAL B 92  ? 0.6409 0.3807 0.7140 0.0484  0.1212  -0.0109 1562 VAL B CG1 
2837 C  CG2 . VAL B 92  ? 0.6141 0.3707 0.7209 0.0402  0.1435  -0.0071 1562 VAL B CG2 
2838 N  N   . SER B 93  ? 0.5954 0.3665 0.7429 0.0585  0.1001  -0.0250 1563 SER B N   
2839 C  CA  . SER B 93  ? 0.5890 0.3604 0.7358 0.0633  0.0846  -0.0298 1563 SER B CA  
2840 C  C   . SER B 93  ? 0.6036 0.3815 0.7710 0.0679  0.0746  -0.0280 1563 SER B C   
2841 O  O   . SER B 93  ? 0.5914 0.3662 0.7530 0.0733  0.0602  -0.0290 1563 SER B O   
2842 C  CB  . SER B 93  ? 0.6795 0.4610 0.8390 0.0617  0.0839  -0.0399 1563 SER B CB  
2843 O  OG  . SER B 93  ? 0.6654 0.4438 0.8123 0.0583  0.0954  -0.0431 1563 SER B OG  
2844 N  N   . LEU B 94  ? 0.5530 0.3393 0.7419 0.0667  0.0818  -0.0252 1564 LEU B N   
2845 C  CA  . LEU B 94  ? 0.6029 0.3969 0.8111 0.0720  0.0727  -0.0250 1564 LEU B CA  
2846 C  C   . LEU B 94  ? 0.7503 0.5281 0.9390 0.0781  0.0633  -0.0191 1564 LEU B C   
2847 O  O   . LEU B 94  ? 0.6241 0.4071 0.8253 0.0851  0.0518  -0.0205 1564 LEU B O   
2848 C  CB  . LEU B 94  ? 0.5512 0.3568 0.7839 0.0696  0.0823  -0.0238 1564 LEU B CB  
2849 C  CG  . LEU B 94  ? 0.5060 0.3309 0.7658 0.0663  0.0845  -0.0302 1564 LEU B CG  
2850 C  CD1 . LEU B 94  ? 0.4691 0.3018 0.7449 0.0620  0.0968  -0.0280 1564 LEU B CD1 
2851 C  CD2 . LEU B 94  ? 0.4867 0.3258 0.7662 0.0707  0.0723  -0.0349 1564 LEU B CD2 
2852 N  N   . LEU B 95  ? 0.5914 0.3498 0.7494 0.0756  0.0674  -0.0126 1565 LEU B N   
2853 C  CA  . LEU B 95  ? 0.7740 0.5125 0.9094 0.0806  0.0579  -0.0054 1565 LEU B CA  
2854 C  C   . LEU B 95  ? 0.8719 0.6088 1.0003 0.0882  0.0398  -0.0088 1565 LEU B C   
2855 O  O   . LEU B 95  ? 0.9122 0.6391 1.0353 0.0960  0.0274  -0.0052 1565 LEU B O   
2856 C  CB  . LEU B 95  ? 0.6561 0.3749 0.7578 0.0743  0.0666  0.0024  1565 LEU B CB  
2857 C  CG  . LEU B 95  ? 0.6902 0.4089 0.7965 0.0664  0.0833  0.0069  1565 LEU B CG  
2858 C  CD1 . LEU B 95  ? 0.6582 0.3618 0.7316 0.0587  0.0927  0.0133  1565 LEU B CD1 
2859 C  CD2 . LEU B 95  ? 0.6268 0.3396 0.7444 0.0694  0.0808  0.0117  1565 LEU B CD2 
2860 N  N   . ARG B 96  ? 0.7286 0.4752 0.8585 0.0867  0.0370  -0.0162 1566 ARG B N   
2861 C  CA  . ARG B 96  ? 0.6556 0.4017 0.7796 0.0935  0.0186  -0.0200 1566 ARG B CA  
2862 C  C   . ARG B 96  ? 0.7236 0.4886 0.8816 0.1003  0.0082  -0.0250 1566 ARG B C   
2863 O  O   . ARG B 96  ? 0.7768 0.5435 0.9342 0.1074  -0.0087 -0.0279 1566 ARG B O   
2864 C  CB  . ARG B 96  ? 0.6930 0.4430 0.8080 0.0897  0.0174  -0.0274 1566 ARG B CB  
2865 C  CG  . ARG B 96  ? 0.6323 0.4057 0.7814 0.0864  0.0195  -0.0372 1566 ARG B CG  
2866 C  CD  . ARG B 96  ? 0.8351 0.6078 0.9719 0.0832  0.0161  -0.0451 1566 ARG B CD  
2867 N  NE  . ARG B 96  ? 0.8501 0.6108 0.9621 0.0779  0.0300  -0.0436 1566 ARG B NE  
2868 C  CZ  . ARG B 96  ? 0.8410 0.6086 0.9640 0.0722  0.0430  -0.0482 1566 ARG B CZ  
2869 N  NH1 . ARG B 96  ? 0.6400 0.4241 0.7963 0.0700  0.0437  -0.0535 1566 ARG B NH1 
2870 N  NH2 . ARG B 96  ? 0.6691 0.4272 0.7695 0.0687  0.0553  -0.0473 1566 ARG B NH2 
2871 N  N   . HIS B 97  ? 0.7085 0.4891 0.8961 0.0982  0.0179  -0.0266 1567 HIS B N   
2872 C  CA  . HIS B 97  ? 0.7465 0.5482 0.9679 0.1036  0.0111  -0.0318 1567 HIS B CA  
2873 C  C   . HIS B 97  ? 0.7462 0.5428 0.9733 0.1104  0.0108  -0.0272 1567 HIS B C   
2874 O  O   . HIS B 97  ? 0.5811 0.3969 0.8382 0.1128  0.0124  -0.0313 1567 HIS B O   
2875 C  CB  . HIS B 97  ? 0.5585 0.3827 0.8092 0.0961  0.0215  -0.0378 1567 HIS B CB  
2876 C  CG  . HIS B 97  ? 0.5560 0.3863 0.8064 0.0907  0.0185  -0.0442 1567 HIS B CG  
2877 N  ND1 . HIS B 97  ? 0.5742 0.4162 0.8349 0.0937  0.0036  -0.0507 1567 HIS B ND1 
2878 C  CD2 . HIS B 97  ? 0.6319 0.4573 0.8723 0.0828  0.0278  -0.0456 1567 HIS B CD2 
2879 C  CE1 . HIS B 97  ? 0.6437 0.4863 0.9002 0.0872  0.0038  -0.0560 1567 HIS B CE1 
2880 N  NE2 . HIS B 97  ? 0.5610 0.3931 0.8049 0.0811  0.0183  -0.0532 1567 HIS B NE2 
2881 N  N   . THR B 98  ? 0.6111 0.3815 0.8093 0.1127  0.0096  -0.0187 1568 THR B N   
2882 C  CA  . THR B 98  ? 0.6650 0.4265 0.8667 0.1187  0.0094  -0.0144 1568 THR B CA  
2883 C  C   . THR B 98  ? 0.7989 0.5664 1.0146 0.1323  -0.0078 -0.0182 1568 THR B C   
2884 O  O   . THR B 98  ? 0.8313 0.5937 1.0543 0.1390  -0.0090 -0.0169 1568 THR B O   
2885 C  CB  . THR B 98  ? 0.6767 0.4063 0.8427 0.1159  0.0126  -0.0036 1568 THR B CB  
2886 O  OG1 . THR B 98  ? 0.7836 0.4968 0.9181 0.1161  0.0038  0.0000  1568 THR B OG1 
2887 C  CG2 . THR B 98  ? 0.6302 0.3594 0.7937 0.1040  0.0319  -0.0006 1568 THR B CG2 
2888 N  N   . GLN B 99  ? 0.7550 0.5343 0.9765 0.1369  -0.0213 -0.0239 1569 GLN B N   
2889 C  CA  . GLN B 99  ? 0.8405 0.6348 1.0853 0.1496  -0.0361 -0.0299 1569 GLN B CA  
2890 C  C   . GLN B 99  ? 0.8732 0.6987 1.1586 0.1491  -0.0278 -0.0378 1569 GLN B C   
2891 O  O   . GLN B 99  ? 0.8056 0.6447 1.1126 0.1603  -0.0368 -0.0430 1569 GLN B O   
2892 C  CB  . GLN B 99  ? 0.8251 0.6283 1.0693 0.1534  -0.0527 -0.0349 1569 GLN B CB  
2893 C  CG  . GLN B 99  ? 1.1492 0.9274 1.3643 0.1639  -0.0713 -0.0295 1569 GLN B CG  
2894 C  CD  . GLN B 99  ? 1.2400 1.0147 1.4351 0.1613  -0.0821 -0.0307 1569 GLN B CD  
2895 O  OE1 . GLN B 99  ? 1.2275 1.0152 1.4276 0.1508  -0.0744 -0.0355 1569 GLN B OE1 
2896 N  NE2 . GLN B 99  ? 1.2074 0.9634 1.3790 0.1713  -0.1010 -0.0268 1569 GLN B NE2 
2897 N  N   . LEU B 100 ? 0.6148 0.4518 0.9104 0.1370  -0.0110 -0.0388 1570 LEU B N   
2898 C  CA  . LEU B 100 ? 0.5746 0.4405 0.9057 0.1349  -0.0024 -0.0453 1570 LEU B CA  
2899 C  C   . LEU B 100 ? 0.7174 0.5779 1.0481 0.1286  0.0148  -0.0414 1570 LEU B C   
2900 O  O   . LEU B 100 ? 0.6245 0.5073 0.9810 0.1253  0.0237  -0.0459 1570 LEU B O   
2901 C  CB  . LEU B 100 ? 0.5733 0.4632 0.9229 0.1260  -0.0005 -0.0514 1570 LEU B CB  
2902 C  CG  . LEU B 100 ? 0.6880 0.5947 1.0509 0.1314  -0.0173 -0.0584 1570 LEU B CG  
2903 C  CD1 . LEU B 100 ? 0.5149 0.4376 0.8892 0.1198  -0.0148 -0.0631 1570 LEU B CD1 
2904 C  CD2 . LEU B 100 ? 0.5957 0.5274 0.9901 0.1418  -0.0240 -0.0651 1570 LEU B CD2 
2905 N  N   . LEU B 101 ? 0.6946 0.5269 0.9968 0.1260  0.0196  -0.0332 1571 LEU B N   
2906 C  CA  . LEU B 101 ? 0.5846 0.4105 0.8844 0.1190  0.0350  -0.0292 1571 LEU B CA  
2907 C  C   . LEU B 101 ? 0.6575 0.4582 0.9400 0.1252  0.0321  -0.0235 1571 LEU B C   
2908 O  O   . LEU B 101 ? 0.7457 0.5254 1.0065 0.1314  0.0204  -0.0193 1571 LEU B O   
2909 C  CB  . LEU B 101 ? 0.7622 0.5789 1.0444 0.1070  0.0458  -0.0246 1571 LEU B CB  
2910 C  CG  . LEU B 101 ? 0.6022 0.4329 0.8904 0.1005  0.0467  -0.0287 1571 LEU B CG  
2911 C  CD1 . LEU B 101 ? 0.6347 0.4506 0.9004 0.0914  0.0569  -0.0240 1571 LEU B CD1 
2912 C  CD2 . LEU B 101 ? 0.5579 0.4157 0.8780 0.0965  0.0532  -0.0347 1571 LEU B CD2 
2913 N  N   . PRO B 102 ? 0.5407 0.3414 0.8312 0.1235  0.0418  -0.0232 1572 PRO B N   
2914 C  CA  . PRO B 102 ? 0.7240 0.4966 0.9953 0.1269  0.0400  -0.0173 1572 PRO B CA  
2915 C  C   . PRO B 102 ? 0.6722 0.4200 0.9115 0.1179  0.0438  -0.0077 1572 PRO B C   
2916 O  O   . PRO B 102 ? 0.5777 0.3297 0.8150 0.1065  0.0570  -0.0056 1572 PRO B O   
2917 C  CB  . PRO B 102 ? 0.6952 0.4764 0.9824 0.1238  0.0518  -0.0200 1572 PRO B CB  
2918 C  CG  . PRO B 102 ? 0.6119 0.4256 0.9249 0.1182  0.0603  -0.0262 1572 PRO B CG  
2919 C  CD  . PRO B 102 ? 0.6120 0.4334 0.9227 0.1153  0.0561  -0.0265 1572 PRO B CD  
2920 N  N   . VAL B 103 ? 0.6398 0.3626 0.8538 0.1229  0.0323  -0.0018 1573 VAL B N   
2921 C  CA  . VAL B 103 ? 0.7910 0.4958 0.9745 0.1141  0.0355  0.0063  1573 VAL B CA  
2922 C  C   . VAL B 103 ? 0.7016 0.3888 0.8696 0.1034  0.0483  0.0139  1573 VAL B C   
2923 O  O   . VAL B 103 ? 0.7715 0.4550 0.9235 0.0928  0.0578  0.0184  1573 VAL B O   
2924 C  CB  . VAL B 103 ? 0.6614 0.3454 0.8211 0.1226  0.0183  0.0106  1573 VAL B CB  
2925 C  CG1 . VAL B 103 ? 0.7542 0.4120 0.9036 0.1305  0.0097  0.0155  1573 VAL B CG1 
2926 C  CG2 . VAL B 103 ? 0.8059 0.4743 0.9329 0.1137  0.0212  0.0179  1573 VAL B CG2 
2927 N  N   . ASP B 104 ? 0.8303 0.5092 1.0050 0.1057  0.0494  0.0144  1574 ASP B N   
2928 C  CA  . ASP B 104 ? 0.8018 0.4678 0.9663 0.0943  0.0617  0.0204  1574 ASP B CA  
2929 C  C   . ASP B 104 ? 0.7667 0.4578 0.9493 0.0844  0.0775  0.0165  1574 ASP B C   
2930 O  O   . ASP B 104 ? 0.7516 0.4390 0.9218 0.0731  0.0882  0.0214  1574 ASP B O   
2931 C  CB  . ASP B 104 ? 0.8484 0.4993 1.0168 0.0994  0.0579  0.0203  1574 ASP B CB  
2932 C  CG  . ASP B 104 ? 0.9170 0.5927 1.1183 0.1076  0.0578  0.0093  1574 ASP B CG  
2933 O  OD1 . ASP B 104 ? 0.7956 0.4930 1.0138 0.1152  0.0523  0.0025  1574 ASP B OD1 
2934 O  OD2 . ASP B 104 ? 0.8061 0.4800 1.0158 0.1058  0.0633  0.0074  1574 ASP B OD2 
2935 N  N   . LYS B 105 ? 0.7258 0.4429 0.9376 0.0886  0.0790  0.0077  1575 LYS B N   
2936 C  CA  . LYS B 105 ? 0.5739 0.3136 0.8020 0.0801  0.0921  0.0044  1575 LYS B CA  
2937 C  C   . LYS B 105 ? 0.5488 0.2926 0.7665 0.0743  0.0958  0.0059  1575 LYS B C   
2938 O  O   . LYS B 105 ? 0.5845 0.3325 0.8003 0.0649  0.1074  0.0076  1575 LYS B O   
2939 C  CB  . LYS B 105 ? 0.5325 0.2989 0.7907 0.0854  0.0917  -0.0044 1575 LYS B CB  
2940 C  CG  . LYS B 105 ? 0.5662 0.3529 0.8402 0.0768  0.1042  -0.0068 1575 LYS B CG  
2941 C  CD  . LYS B 105 ? 0.6004 0.4136 0.8993 0.0797  0.1030  -0.0142 1575 LYS B CD  
2942 C  CE  . LYS B 105 ? 0.6738 0.4934 0.9705 0.0781  0.1000  -0.0154 1575 LYS B CE  
2943 N  NZ  . LYS B 105 ? 0.4393 0.2838 0.7601 0.0775  0.1005  -0.0216 1575 LYS B NZ  
2944 N  N   . ALA B 106 ? 0.6027 0.3465 0.8146 0.0804  0.0854  0.0041  1576 ALA B N   
2945 C  CA  . ALA B 106 ? 0.6770 0.4257 0.8797 0.0757  0.0880  0.0035  1576 ALA B CA  
2946 C  C   . ALA B 106 ? 0.6206 0.3510 0.7949 0.0677  0.0951  0.0111  1576 ALA B C   
2947 O  O   . ALA B 106 ? 0.6040 0.3420 0.7763 0.0604  0.1054  0.0102  1576 ALA B O   
2948 C  CB  . ALA B 106 ? 0.6097 0.3596 0.8092 0.0837  0.0738  0.0002  1576 ALA B CB  
2949 N  N   . PHE B 107 ? 0.6713 0.3773 0.8234 0.0687  0.0898  0.0185  1577 PHE B N   
2950 C  CA  . PHE B 107 ? 0.7532 0.4427 0.8774 0.0594  0.0976  0.0264  1577 PHE B CA  
2951 C  C   . PHE B 107 ? 0.7199 0.4148 0.8528 0.0494  0.1125  0.0281  1577 PHE B C   
2952 O  O   . PHE B 107 ? 0.6110 0.3085 0.7341 0.0405  0.1238  0.0302  1577 PHE B O   
2953 C  CB  . PHE B 107 ? 0.7894 0.4490 0.8850 0.0619  0.0874  0.0352  1577 PHE B CB  
2954 C  CG  . PHE B 107 ? 0.7239 0.3753 0.7984 0.0671  0.0762  0.0360  1577 PHE B CG  
2955 C  CD1 . PHE B 107 ? 0.7620 0.4103 0.8126 0.0598  0.0827  0.0386  1577 PHE B CD1 
2956 C  CD2 . PHE B 107 ? 0.6931 0.3421 0.7725 0.0797  0.0591  0.0331  1577 PHE B CD2 
2957 C  CE1 . PHE B 107 ? 0.7787 0.4194 0.8081 0.0645  0.0719  0.0388  1577 PHE B CE1 
2958 C  CE2 . PHE B 107 ? 0.7164 0.3584 0.7762 0.0846  0.0474  0.0335  1577 PHE B CE2 
2959 C  CZ  . PHE B 107 ? 0.7591 0.3962 0.7929 0.0768  0.0536  0.0365  1577 PHE B CZ  
2960 N  N   . TYR B 108 ? 0.6676 0.3657 0.8195 0.0511  0.1127  0.0265  1578 TYR B N   
2961 C  CA  . TYR B 108 ? 0.6568 0.3629 0.8198 0.0420  0.1257  0.0270  1578 TYR B CA  
2962 C  C   . TYR B 108 ? 0.7204 0.4508 0.8982 0.0383  0.1356  0.0215  1578 TYR B C   
2963 O  O   . TYR B 108 ? 0.6332 0.3675 0.8069 0.0294  0.1470  0.0235  1578 TYR B O   
2964 C  CB  . TYR B 108 ? 0.5725 0.2814 0.7552 0.0458  0.1232  0.0239  1578 TYR B CB  
2965 C  CG  . TYR B 108 ? 0.6271 0.3456 0.8226 0.0369  0.1350  0.0236  1578 TYR B CG  
2966 C  CD1 . TYR B 108 ? 0.6916 0.3952 0.8730 0.0267  0.1411  0.0304  1578 TYR B CD1 
2967 C  CD2 . TYR B 108 ? 0.6769 0.4195 0.8981 0.0378  0.1397  0.0168  1578 TYR B CD2 
2968 C  CE1 . TYR B 108 ? 0.6521 0.3666 0.8469 0.0183  0.1511  0.0295  1578 TYR B CE1 
2969 C  CE2 . TYR B 108 ? 0.6942 0.4461 0.9267 0.0302  0.1492  0.0164  1578 TYR B CE2 
2970 C  CZ  . TYR B 108 ? 0.7692 0.5079 0.9894 0.0208  0.1545  0.0223  1578 TYR B CZ  
2971 O  OH  . TYR B 108 ? 0.6925 0.4425 0.9259 0.0135  0.1627  0.0213  1578 TYR B OH  
2972 N  N   . GLU B 109 ? 0.6233 0.3701 0.8188 0.0450  0.1310  0.0143  1579 GLU B N   
2973 C  CA  . GLU B 109 ? 0.6442 0.4118 0.8558 0.0421  0.1390  0.0090  1579 GLU B CA  
2974 C  C   . GLU B 109 ? 0.5213 0.2873 0.7157 0.0385  0.1437  0.0093  1579 GLU B C   
2975 O  O   . GLU B 109 ? 0.5602 0.3356 0.7585 0.0328  0.1545  0.0081  1579 GLU B O   
2976 C  CB  . GLU B 109 ? 0.5421 0.3253 0.7749 0.0489  0.1323  0.0020  1579 GLU B CB  
2977 C  CG  . GLU B 109 ? 0.5925 0.3834 0.8453 0.0514  0.1314  0.0002  1579 GLU B CG  
2978 C  CD  . GLU B 109 ? 0.5780 0.3872 0.8526 0.0562  0.1267  -0.0063 1579 GLU B CD  
2979 O  OE1 . GLU B 109 ? 0.5930 0.4070 0.8676 0.0582  0.1219  -0.0094 1579 GLU B OE1 
2980 O  OE2 . GLU B 109 ? 0.5526 0.3715 0.8441 0.0573  0.1281  -0.0084 1579 GLU B OE2 
2981 N  N   . ALA B 110 ? 0.5432 0.2977 0.7183 0.0424  0.1352  0.0102  1580 ALA B N   
2982 C  CA  . ALA B 110 ? 0.5600 0.3114 0.7147 0.0391  0.1396  0.0101  1580 ALA B CA  
2983 C  C   . ALA B 110 ? 0.6841 0.4281 0.8226 0.0299  0.1514  0.0165  1580 ALA B C   
2984 O  O   . ALA B 110 ? 0.6471 0.4006 0.7839 0.0251  0.1623  0.0140  1580 ALA B O   
2985 C  CB  . ALA B 110 ? 0.6102 0.3479 0.7436 0.0449  0.1268  0.0110  1580 ALA B CB  
2986 N  N   . GLY B 111 ? 0.8065 0.5340 0.9342 0.0270  0.1497  0.0244  1581 GLY B N   
2987 C  CA  . GLY B 111 ? 0.7762 0.4959 0.8877 0.0163  0.1606  0.0314  1581 GLY B CA  
2988 C  C   . GLY B 111 ? 0.6863 0.4249 0.8193 0.0097  0.1739  0.0286  1581 GLY B C   
2989 O  O   . GLY B 111 ? 0.6079 0.3535 0.7342 0.0023  0.1858  0.0292  1581 GLY B O   
2990 N  N   . ILE B 112 ? 0.7656 0.5142 0.9248 0.0127  0.1719  0.0251  1582 ILE B N   
2991 C  CA  . ILE B 112 ? 0.5892 0.3559 0.7695 0.0074  0.1825  0.0224  1582 ILE B CA  
2992 C  C   . ILE B 112 ? 0.7992 0.5849 0.9889 0.0091  0.1888  0.0153  1582 ILE B C   
2993 O  O   . ILE B 112 ? 0.6537 0.4513 0.8480 0.0033  0.2001  0.0143  1582 ILE B O   
2994 C  CB  . ILE B 112 ? 0.6427 0.4147 0.8459 0.0108  0.1778  0.0202  1582 ILE B CB  
2995 C  CG1 . ILE B 112 ? 0.9236 0.6757 1.1170 0.0085  0.1729  0.0264  1582 ILE B CG1 
2996 C  CG2 . ILE B 112 ? 0.7363 0.5276 0.9609 0.0063  0.1870  0.0171  1582 ILE B CG2 
2997 C  CD1 . ILE B 112 ? 0.7428 0.4926 0.9339 -0.0032 0.1821  0.0312  1582 ILE B CD1 
2998 N  N   . ALA B 113 ? 0.5713 0.3603 0.7652 0.0172  0.1814  0.0097  1583 ALA B N   
2999 C  CA  . ALA B 113 ? 0.6695 0.4732 0.8718 0.0193  0.1862  0.0024  1583 ALA B CA  
3000 C  C   . ALA B 113 ? 0.5973 0.3990 0.7782 0.0155  0.1944  0.0024  1583 ALA B C   
3001 O  O   . ALA B 113 ? 0.5981 0.4138 0.7866 0.0139  0.2042  -0.0022 1583 ALA B O   
3002 C  CB  . ALA B 113 ? 0.4956 0.3007 0.7047 0.0272  0.1758  -0.0032 1583 ALA B CB  
3003 N  N   . ALA B 114 ? 0.6273 0.4119 0.7808 0.0147  0.1901  0.0072  1584 ALA B N   
3004 C  CA  . ALA B 114 ? 0.7194 0.5012 0.8485 0.0101  0.1985  0.0080  1584 ALA B CA  
3005 C  C   . ALA B 114 ? 0.7598 0.5503 0.8919 0.0004  0.2129  0.0115  1584 ALA B C   
3006 O  O   . ALA B 114 ? 0.6392 0.4441 0.7726 -0.0017 0.2241  0.0065  1584 ALA B O   
3007 C  CB  . ALA B 114 ? 0.7571 0.5164 0.8543 0.0098  0.1905  0.0149  1584 ALA B CB  
3008 N  N   . LYS B 115 ? 0.7475 0.5304 0.8825 -0.0054 0.2123  0.0191  1585 LYS B N   
3009 C  CA  . LYS B 115 ? 0.9068 0.6981 1.0459 -0.0162 0.2251  0.0227  1585 LYS B CA  
3010 C  C   . LYS B 115 ? 0.9043 0.7220 1.0724 -0.0147 0.2332  0.0145  1585 LYS B C   
3011 O  O   . LYS B 115 ? 0.8225 0.6548 0.9922 -0.0205 0.2459  0.0127  1585 LYS B O   
3012 C  CB  . LYS B 115 ? 0.9433 0.7211 1.0842 -0.0218 0.2208  0.0308  1585 LYS B CB  
3013 C  CG  . LYS B 115 ? 1.0173 0.7985 1.1568 -0.0356 0.2326  0.0365  1585 LYS B CG  
3014 C  CD  . LYS B 115 ? 1.1311 0.9059 1.2848 -0.0391 0.2279  0.0401  1585 LYS B CD  
3015 C  CE  . LYS B 115 ? 1.1688 0.9515 1.3275 -0.0536 0.2394  0.0441  1585 LYS B CE  
3016 N  NZ  . LYS B 115 ? 1.1255 0.9015 1.2982 -0.0567 0.2339  0.0462  1585 LYS B NZ  
3017 N  N   . ALA B 116 ? 0.7496 0.5739 0.9403 -0.0066 0.2258  0.0093  1586 ALA B N   
3018 C  CA  . ALA B 116 ? 0.6853 0.5318 0.9029 -0.0045 0.2314  0.0024  1586 ALA B CA  
3019 C  C   . ALA B 116 ? 0.7648 0.6227 0.9806 -0.0001 0.2377  -0.0058 1586 ALA B C   
3020 O  O   . ALA B 116 ? 0.7179 0.5948 0.9500 -0.0005 0.2465  -0.0107 1586 ALA B O   
3021 C  CB  . ALA B 116 ? 0.7058 0.5541 0.9443 0.0025  0.2216  -0.0002 1586 ALA B CB  
3022 N  N   . VAL B 117 ? 0.5861 0.4334 0.7822 0.0046  0.2332  -0.0082 1587 VAL B N   
3023 C  CA  . VAL B 117 ? 0.7301 0.5877 0.9234 0.0088  0.2397  -0.0172 1587 VAL B CA  
3024 C  C   . VAL B 117 ? 0.6637 0.5214 0.8321 0.0022  0.2510  -0.0156 1587 VAL B C   
3025 O  O   . VAL B 117 ? 0.6229 0.4864 0.7822 0.0060  0.2563  -0.0234 1587 VAL B O   
3026 C  CB  . VAL B 117 ? 0.5643 0.4138 0.7537 0.0180  0.2291  -0.0237 1587 VAL B CB  
3027 C  CG1 . VAL B 117 ? 0.5904 0.4441 0.8065 0.0231  0.2210  -0.0259 1587 VAL B CG1 
3028 C  CG2 . VAL B 117 ? 0.6632 0.4927 0.8272 0.0177  0.2197  -0.0184 1587 VAL B CG2 
3029 N  N   . GLY B 118 ? 0.6919 0.5430 0.8484 -0.0080 0.2552  -0.0057 1588 GLY B N   
3030 C  CA  . GLY B 118 ? 0.6770 0.5290 0.8094 -0.0163 0.2672  -0.0030 1588 GLY B CA  
3031 C  C   . GLY B 118 ? 0.7817 0.6130 0.8782 -0.0155 0.2617  0.0001  1588 GLY B C   
3032 O  O   . GLY B 118 ? 0.6576 0.4911 0.7313 -0.0199 0.2716  -0.0005 1588 GLY B O   
3033 N  N   . TRP B 119 ? 0.7426 0.5553 0.8338 -0.0096 0.2459  0.0029  1589 TRP B N   
3034 C  CA  . TRP B 119 ? 0.9216 0.7129 0.9789 -0.0083 0.2376  0.0068  1589 TRP B CA  
3035 C  C   . TRP B 119 ? 0.7082 0.4792 0.7476 -0.0167 0.2343  0.0206  1589 TRP B C   
3036 O  O   . TRP B 119 ? 0.8355 0.5908 0.8765 -0.0129 0.2207  0.0254  1589 TRP B O   
3037 C  CB  . TRP B 119 ? 0.8747 0.6592 0.9383 0.0032  0.2217  0.0011  1589 TRP B CB  
3038 C  CG  . TRP B 119 ? 0.9358 0.7352 1.0128 0.0107  0.2237  -0.0121 1589 TRP B CG  
3039 C  CD1 . TRP B 119 ? 0.8875 0.7021 0.9635 0.0101  0.2371  -0.0198 1589 TRP B CD1 
3040 C  CD2 . TRP B 119 ? 0.8413 0.6412 0.9348 0.0199  0.2118  -0.0194 1589 TRP B CD2 
3041 N  NE1 . TRP B 119 ? 1.0574 0.8793 1.1475 0.0192  0.2332  -0.0317 1589 TRP B NE1 
3042 C  CE2 . TRP B 119 ? 1.0446 0.8572 1.1453 0.0244  0.2178  -0.0311 1589 TRP B CE2 
3043 C  CE3 . TRP B 119 ? 0.7175 0.5090 0.8210 0.0246  0.1968  -0.0175 1589 TRP B CE3 
3044 C  CZ2 . TRP B 119 ? 0.9587 0.7728 1.0748 0.0323  0.2087  -0.0399 1589 TRP B CZ2 
3045 C  CZ3 . TRP B 119 ? 0.8026 0.5990 0.9225 0.0316  0.1890  -0.0262 1589 TRP B CZ3 
3046 C  CH2 . TRP B 119 ? 0.8275 0.6337 0.9529 0.0349  0.1946  -0.0369 1589 TRP B CH2 
3047 N  N   . ASP B 120 ? 0.7342 0.5053 0.7558 -0.0284 0.2472  0.0270  1590 ASP B N   
3048 C  CA  . ASP B 120 ? 0.9327 0.6866 0.9439 -0.0387 0.2464  0.0401  1590 ASP B CA  
3049 C  C   . ASP B 120 ? 0.8271 0.5497 0.8021 -0.0387 0.2344  0.0499  1590 ASP B C   
3050 O  O   . ASP B 120 ? 0.8490 0.5519 0.8218 -0.0405 0.2252  0.0587  1590 ASP B O   
3051 C  CB  . ASP B 120 ? 1.0754 0.8426 1.0841 -0.0532 0.2650  0.0437  1590 ASP B CB  
3052 C  CG  . ASP B 120 ? 1.1226 0.9185 1.1709 -0.0536 0.2738  0.0361  1590 ASP B CG  
3053 O  OD1 . ASP B 120 ? 1.1130 0.9278 1.1654 -0.0633 0.2898  0.0354  1590 ASP B OD1 
3054 O  OD2 . ASP B 120 ? 1.0523 0.8526 1.1275 -0.0444 0.2646  0.0309  1590 ASP B OD2 
3055 N  N   . ASN B 121 ? 0.8293 0.5458 0.7751 -0.0361 0.2336  0.0483  1591 ASN B N   
3056 C  CA  . ASN B 121 ? 0.8553 0.5418 0.7666 -0.0342 0.2196  0.0572  1591 ASN B CA  
3057 C  C   . ASN B 121 ? 1.0819 0.7585 1.0091 -0.0215 0.2000  0.0551  1591 ASN B C   
3058 O  O   . ASN B 121 ? 1.1867 0.8402 1.1048 -0.0210 0.1882  0.0644  1591 ASN B O   
3059 C  CB  . ASN B 121 ? 0.9079 0.5929 0.7873 -0.0322 0.2212  0.0534  1591 ASN B CB  
3060 C  CG  . ASN B 121 ? 1.3237 1.0142 1.1783 -0.0459 0.2403  0.0577  1591 ASN B CG  
3061 O  OD1 . ASN B 121 ? 1.3439 1.0336 1.1994 -0.0586 0.2504  0.0666  1591 ASN B OD1 
3062 N  ND2 . ASN B 121 ? 1.4213 1.1179 1.2533 -0.0438 0.2455  0.0510  1591 ASN B ND2 
3063 N  N   . MET B 122 ? 0.8429 0.5370 0.7938 -0.0111 0.1962  0.0427  1592 MET B N   
3064 C  CA  . MET B 122 ? 0.8634 0.5542 0.8343 0.0001  0.1797  0.0394  1592 MET B CA  
3065 C  C   . MET B 122 ? 0.7232 0.4126 0.7179 -0.0019 0.1785  0.0440  1592 MET B C   
3066 O  O   . MET B 122 ? 0.8602 0.5347 0.8566 0.0039  0.1646  0.0477  1592 MET B O   
3067 C  CB  . MET B 122 ? 0.8427 0.5550 0.8377 0.0083  0.1794  0.0255  1592 MET B CB  
3068 C  CG  . MET B 122 ? 0.9512 0.6648 0.9236 0.0108  0.1801  0.0189  1592 MET B CG  
3069 S  SD  . MET B 122 ? 1.0010 0.7351 1.0025 0.0204  0.1772  0.0027  1592 MET B SD  
3070 C  CE  . MET B 122 ? 0.6999 0.4223 0.7064 0.0298  0.1543  0.0031  1592 MET B CE  
3071 N  N   . ALA B 123 ? 0.7052 0.4106 0.7187 -0.0095 0.1927  0.0429  1593 ALA B N   
3072 C  CA  . ALA B 123 ? 0.6868 0.3917 0.7223 -0.0119 0.1918  0.0462  1593 ALA B CA  
3073 C  C   . ALA B 123 ? 0.7776 0.4536 0.7901 -0.0169 0.1853  0.0586  1593 ALA B C   
3074 O  O   . ALA B 123 ? 0.7790 0.4432 0.8006 -0.0113 0.1736  0.0604  1593 ALA B O   
3075 C  CB  . ALA B 123 ? 0.6720 0.3984 0.7273 -0.0206 0.2081  0.0438  1593 ALA B CB  
3076 N  N   . PHE B 124 ? 0.7751 0.4383 0.7562 -0.0272 0.1922  0.0670  1594 PHE B N   
3077 C  CA  . PHE B 124 ? 0.8730 0.5052 0.8295 -0.0334 0.1860  0.0801  1594 PHE B CA  
3078 C  C   . PHE B 124 ? 0.8824 0.4915 0.8235 -0.0213 0.1661  0.0825  1594 PHE B C   
3079 O  O   . PHE B 124 ? 0.9610 0.5505 0.9038 -0.0179 0.1548  0.0874  1594 PHE B O   
3080 C  CB  . PHE B 124 ? 1.0029 0.6264 0.9262 -0.0480 0.1981  0.0894  1594 PHE B CB  
3081 C  CG  . PHE B 124 ? 1.0006 0.5893 0.8966 -0.0566 0.1922  0.1043  1594 PHE B CG  
3082 C  CD1 . PHE B 124 ? 1.0422 0.6252 0.9503 -0.0667 0.1965  0.1095  1594 PHE B CD1 
3083 C  CD2 . PHE B 124 ? 1.0930 0.6528 0.9504 -0.0543 0.1811  0.1131  1594 PHE B CD2 
3084 C  CE1 . PHE B 124 ? 1.0193 0.5667 0.9014 -0.0749 0.1902  0.1234  1594 PHE B CE1 
3085 C  CE2 . PHE B 124 ? 1.0212 0.5453 0.8517 -0.0619 0.1745  0.1277  1594 PHE B CE2 
3086 C  CZ  . PHE B 124 ? 1.0105 0.5278 0.8537 -0.0723 0.1791  0.1327  1594 PHE B CZ  
3087 N  N   . ILE B 125 ? 0.9426 0.5540 0.8693 -0.0140 0.1608  0.0783  1595 ILE B N   
3088 C  CA  . ILE B 125 ? 0.9688 0.5591 0.8799 -0.0027 0.1409  0.0808  1595 ILE B CA  
3089 C  C   . ILE B 125 ? 0.9155 0.5129 0.8603 0.0098  0.1290  0.0737  1595 ILE B C   
3090 O  O   . ILE B 125 ? 0.9794 0.5563 0.9204 0.0163  0.1148  0.0784  1595 ILE B O   
3091 C  CB  . ILE B 125 ? 0.8719 0.4661 0.7629 0.0023  0.1373  0.0762  1595 ILE B CB  
3092 C  CG1 . ILE B 125 ? 0.9470 0.5285 0.7974 -0.0096 0.1471  0.0851  1595 ILE B CG1 
3093 C  CG2 . ILE B 125 ? 0.8582 0.4378 0.7430 0.0161  0.1152  0.0758  1595 ILE B CG2 
3094 C  CD1 . ILE B 125 ? 0.8986 0.4906 0.7319 -0.0073 0.1498  0.0781  1595 ILE B CD1 
3095 N  N   . PHE B 126 ? 0.7786 0.4050 0.7566 0.0135  0.1346  0.0622  1596 PHE B N   
3096 C  CA  . PHE B 126 ? 0.8316 0.4673 0.8412 0.0242  0.1248  0.0553  1596 PHE B CA  
3097 C  C   . PHE B 126 ? 0.8721 0.4993 0.8946 0.0215  0.1254  0.0595  1596 PHE B C   
3098 O  O   . PHE B 126 ? 0.8545 0.4740 0.8870 0.0309  0.1128  0.0585  1596 PHE B O   
3099 C  CB  . PHE B 126 ? 0.6898 0.3564 0.7297 0.0270  0.1312  0.0433  1596 PHE B CB  
3100 C  CG  . PHE B 126 ? 0.6950 0.3695 0.7245 0.0305  0.1293  0.0372  1596 PHE B CG  
3101 C  CD1 . PHE B 126 ? 0.7245 0.3829 0.7285 0.0359  0.1162  0.0397  1596 PHE B CD1 
3102 C  CD2 . PHE B 126 ? 0.7035 0.4005 0.7488 0.0287  0.1397  0.0284  1596 PHE B CD2 
3103 C  CE1 . PHE B 126 ? 0.8480 0.5132 0.8419 0.0387  0.1139  0.0331  1596 PHE B CE1 
3104 C  CE2 . PHE B 126 ? 0.7287 0.4311 0.7641 0.0319  0.1377  0.0218  1596 PHE B CE2 
3105 C  CZ  . PHE B 126 ? 0.7080 0.3950 0.7176 0.0365  0.1250  0.0238  1596 PHE B CZ  
3106 N  N   . LEU B 127 ? 0.7729 0.4023 0.7962 0.0090  0.1396  0.0634  1597 LEU B N   
3107 C  CA  . LEU B 127 ? 0.7400 0.3615 0.7759 0.0057  0.1399  0.0664  1597 LEU B CA  
3108 C  C   . LEU B 127 ? 0.7651 0.3506 0.7737 0.0045  0.1299  0.0773  1597 LEU B C   
3109 O  O   . LEU B 127 ? 0.8507 0.4238 0.8687 0.0093  0.1216  0.0776  1597 LEU B O   
3110 C  CB  . LEU B 127 ? 0.7594 0.3959 0.8063 -0.0077 0.1571  0.0666  1597 LEU B CB  
3111 C  CG  . LEU B 127 ? 0.9262 0.5963 1.0045 -0.0047 0.1648  0.0555  1597 LEU B CG  
3112 C  CD1 . LEU B 127 ? 0.8823 0.5689 0.9727 -0.0168 0.1807  0.0553  1597 LEU B CD1 
3113 C  CD2 . LEU B 127 ? 0.8096 0.4875 0.9147 0.0064  0.1554  0.0484  1597 LEU B CD2 
3114 N  N   . ASN B 128 ? 0.8669 0.4340 0.8406 -0.0011 0.1298  0.0862  1598 ASN B N   
3115 C  CA  . ASN B 128 ? 0.9810 0.5104 0.9252 -0.0010 0.1178  0.0976  1598 ASN B CA  
3116 C  C   . ASN B 128 ? 1.0644 0.5842 1.0119 0.0169  0.0978  0.0940  1598 ASN B C   
3117 O  O   . ASN B 128 ? 1.0833 0.5798 1.0289 0.0226  0.0860  0.0975  1598 ASN B O   
3118 C  CB  . ASN B 128 ? 0.9118 0.4254 0.8158 -0.0110 0.1222  0.1079  1598 ASN B CB  
3119 C  CG  . ASN B 128 ? 0.9297 0.4014 0.8008 -0.0151 0.1125  0.1221  1598 ASN B CG  
3120 O  OD1 . ASN B 128 ? 1.1260 0.5816 1.0037 -0.0184 0.1102  0.1259  1598 ASN B OD1 
3121 N  ND2 . ASN B 128 ? 1.0657 0.5178 0.8997 -0.0149 0.1058  0.1302  1598 ASN B ND2 
3122 N  N   . ARG B 129 ? 0.9168 0.4546 0.8698 0.0262  0.0933  0.0864  1599 ARG B N   
3123 C  CA  . ARG B 129 ? 0.9249 0.4612 0.8875 0.0432  0.0749  0.0810  1599 ARG B CA  
3124 C  C   . ARG B 129 ? 0.9794 0.5276 0.9781 0.0507  0.0725  0.0730  1599 ARG B C   
3125 O  O   . ARG B 129 ? 0.8134 0.3476 0.8153 0.0623  0.0578  0.0726  1599 ARG B O   
3126 C  CB  . ARG B 129 ? 0.8783 0.4368 0.8456 0.0492  0.0728  0.0727  1599 ARG B CB  
3127 C  CG  . ARG B 129 ? 1.0525 0.6168 1.0361 0.0656  0.0552  0.0655  1599 ARG B CG  
3128 C  CD  . ARG B 129 ? 1.1623 0.6936 1.1228 0.0739  0.0370  0.0737  1599 ARG B CD  
3129 N  NE  . ARG B 129 ? 1.2497 0.7865 1.2131 0.0881  0.0196  0.0682  1599 ARG B NE  
3130 C  CZ  . ARG B 129 ? 1.3502 0.8687 1.2814 0.0911  0.0076  0.0741  1599 ARG B CZ  
3131 N  NH1 . ARG B 129 ? 1.3895 0.8817 1.2813 0.0806  0.0120  0.0865  1599 ARG B NH1 
3132 N  NH2 . ARG B 129 ? 1.3457 0.8727 1.2840 0.1042  -0.0089 0.0677  1599 ARG B NH2 
3133 N  N   . PHE B 130 ? 0.7567 0.3306 0.7817 0.0445  0.0869  0.0665  1600 PHE B N   
3134 C  CA  . PHE B 130 ? 0.7912 0.3764 0.8476 0.0496  0.0865  0.0594  1600 PHE B CA  
3135 C  C   . PHE B 130 ? 0.8767 0.4327 0.9236 0.0487  0.0811  0.0658  1600 PHE B C   
3136 O  O   . PHE B 130 ? 0.9155 0.4665 0.9754 0.0605  0.0702  0.0613  1600 PHE B O   
3137 C  CB  . PHE B 130 ? 0.7263 0.3388 0.8055 0.0406  0.1031  0.0541  1600 PHE B CB  
3138 C  CG  . PHE B 130 ? 0.8013 0.4186 0.9035 0.0409  0.1055  0.0501  1600 PHE B CG  
3139 C  CD1 . PHE B 130 ? 0.6781 0.3073 0.8041 0.0532  0.0976  0.0415  1600 PHE B CD1 
3140 C  CD2 . PHE B 130 ? 0.7722 0.3836 0.8724 0.0284  0.1157  0.0545  1600 PHE B CD2 
3141 C  CE1 . PHE B 130 ? 0.6709 0.3049 0.8162 0.0537  0.1000  0.0370  1600 PHE B CE1 
3142 C  CE2 . PHE B 130 ? 0.6834 0.2988 0.8035 0.0286  0.1171  0.0501  1600 PHE B CE2 
3143 C  CZ  . PHE B 130 ? 0.7248 0.3510 0.8665 0.0416  0.1093  0.0412  1600 PHE B CZ  
3144 N  N   . LEU B 131 ? 0.8858 0.4234 0.9116 0.0345  0.0893  0.0756  1601 LEU B N   
3145 C  CA  . LEU B 131 ? 0.9781 0.4851 0.9938 0.0319  0.0841  0.0820  1601 LEU B CA  
3146 C  C   . LEU B 131 ? 0.9515 0.4285 0.9488 0.0450  0.0645  0.0860  1601 LEU B C   
3147 O  O   . LEU B 131 ? 0.9712 0.4342 0.9773 0.0544  0.0542  0.0831  1601 LEU B O   
3148 C  CB  . LEU B 131 ? 0.9712 0.4628 0.9641 0.0125  0.0958  0.0931  1601 LEU B CB  
3149 C  CG  . LEU B 131 ? 0.8312 0.3492 0.8427 -0.0014 0.1146  0.0899  1601 LEU B CG  
3150 C  CD1 . LEU B 131 ? 0.9090 0.4102 0.8953 -0.0207 0.1248  0.1019  1601 LEU B CD1 
3151 C  CD2 . LEU B 131 ? 0.7711 0.2996 0.8129 0.0012  0.1153  0.0816  1601 LEU B CD2 
3152 N  N   . ASP B 132 ? 0.8632 0.3308 0.8351 0.0468  0.0583  0.0920  1602 ASP B N   
3153 C  CA  . ASP B 132 ? 0.8994 0.3384 0.8525 0.0600  0.0380  0.0963  1602 ASP B CA  
3154 C  C   . ASP B 132 ? 0.9988 0.4552 0.9821 0.0797  0.0257  0.0837  1602 ASP B C   
3155 O  O   . ASP B 132 ? 1.1206 0.5554 1.1027 0.0922  0.0104  0.0836  1602 ASP B O   
3156 C  CB  . ASP B 132 ? 1.0935 0.5232 1.0139 0.0579  0.0342  0.1042  1602 ASP B CB  
3157 C  CG  . ASP B 132 ? 1.1927 0.6006 1.0782 0.0385  0.0452  0.1183  1602 ASP B CG  
3158 O  OD1 . ASP B 132 ? 1.1704 0.5727 1.0598 0.0258  0.0563  0.1216  1602 ASP B OD1 
3159 O  OD2 . ASP B 132 ? 1.1862 0.5833 1.0400 0.0354  0.0429  0.1258  1602 ASP B OD2 
3160 N  N   . LEU B 133 ? 0.8555 0.3509 0.8670 0.0826  0.0325  0.0726  1603 LEU B N   
3161 C  CA  . LEU B 133 ? 0.9134 0.4284 0.9543 0.0996  0.0222  0.0607  1603 LEU B CA  
3162 C  C   . LEU B 133 ? 0.9563 0.4730 1.0206 0.1034  0.0239  0.0544  1603 LEU B C   
3163 O  O   . LEU B 133 ? 0.9012 0.4155 0.9784 0.1190  0.0109  0.0482  1603 LEU B O   
3164 C  CB  . LEU B 133 ? 0.7696 0.3247 0.8339 0.0996  0.0295  0.0512  1603 LEU B CB  
3165 C  CG  . LEU B 133 ? 0.9500 0.5080 0.9958 0.0990  0.0256  0.0536  1603 LEU B CG  
3166 C  CD1 . LEU B 133 ? 0.8110 0.4043 0.8763 0.0931  0.0382  0.0457  1603 LEU B CD1 
3167 C  CD2 . LEU B 133 ? 0.8006 0.3520 0.8435 0.1153  0.0046  0.0516  1603 LEU B CD2 
3168 N  N   . THR B 134 ? 0.8586 0.3785 0.9274 0.0897  0.0391  0.0557  1604 THR B N   
3169 C  CA  . THR B 134 ? 0.7798 0.2990 0.8672 0.0918  0.0410  0.0498  1604 THR B CA  
3170 C  C   . THR B 134 ? 0.9752 0.4541 1.0447 0.0986  0.0271  0.0549  1604 THR B C   
3171 O  O   . THR B 134 ? 0.9227 0.4002 1.0087 0.1114  0.0193  0.0465  1604 THR B O   
3172 C  CB  . THR B 134 ? 0.9631 0.4898 1.0540 0.0742  0.0586  0.0519  1604 THR B CB  
3173 O  OG1 . THR B 134 ? 0.9654 0.5315 1.0824 0.0720  0.0699  0.0436  1604 THR B OG1 
3174 C  CG2 . THR B 134 ? 1.1402 0.6506 1.2365 0.0735  0.0579  0.0500  1604 THR B CG2 
3175 N  N   . ASP B 135 ? 1.0432 0.4882 1.0780 0.0903  0.0238  0.0684  1605 ASP B N   
3176 C  CA  . ASP B 135 ? 1.1916 0.5933 1.2060 0.0969  0.0087  0.0746  1605 ASP B CA  
3177 C  C   . ASP B 135 ? 1.2351 0.6331 1.2530 0.1190  -0.0110 0.0698  1605 ASP B C   
3178 O  O   . ASP B 135 ? 1.2158 0.5978 1.2408 0.1329  -0.0231 0.0646  1605 ASP B O   
3179 C  CB  . ASP B 135 ? 1.3188 0.6855 1.2931 0.0813  0.0102  0.0916  1605 ASP B CB  
3180 C  CG  . ASP B 135 ? 1.3496 0.7267 1.3234 0.0587  0.0308  0.0957  1605 ASP B CG  
3181 O  OD1 . ASP B 135 ? 1.0850 0.4879 1.0877 0.0559  0.0414  0.0860  1605 ASP B OD1 
3182 O  OD2 . ASP B 135 ? 1.2517 0.6126 1.1962 0.0439  0.0365  0.1084  1605 ASP B OD2 
3183 N  N   . ALA B 136 ? 1.2733 0.6883 1.2885 0.1233  -0.0146 0.0698  1606 ALA B N   
3184 C  CA  . ALA B 136 ? 1.2352 0.6489 1.2543 0.1440  -0.0342 0.0653  1606 ALA B CA  
3185 C  C   . ALA B 136 ? 1.2798 0.7248 1.3401 0.1594  -0.0366 0.0486  1606 ALA B C   
3186 O  O   . ALA B 136 ? 1.3355 0.7738 1.4028 0.1783  -0.0536 0.0434  1606 ALA B O   
3187 C  CB  . ALA B 136 ? 1.1480 0.5752 1.1558 0.1434  -0.0371 0.0683  1606 ALA B CB  
3188 N  N   . ILE B 137 ? 1.2686 0.7488 1.3562 0.1520  -0.0199 0.0400  1607 ILE B N   
3189 C  CA  . ILE B 137 ? 1.1845 0.6947 1.3095 0.1644  -0.0197 0.0247  1607 ILE B CA  
3190 C  C   . ILE B 137 ? 1.2435 0.7280 1.3693 0.1756  -0.0290 0.0212  1607 ILE B C   
3191 O  O   . ILE B 137 ? 1.1458 0.6366 1.2886 0.1947  -0.0415 0.0117  1607 ILE B O   
3192 C  CB  . ILE B 137 ? 1.0370 0.5811 1.1846 0.1519  0.0004  0.0187  1607 ILE B CB  
3193 C  CG1 . ILE B 137 ? 0.9020 0.4772 1.0570 0.1453  0.0078  0.0181  1607 ILE B CG1 
3194 C  CG2 . ILE B 137 ? 0.9258 0.4928 1.1060 0.1625  0.0019  0.0045  1607 ILE B CG2 
3195 C  CD1 . ILE B 137 ? 0.8809 0.4812 1.0508 0.1310  0.0272  0.0154  1607 ILE B CD1 
3196 N  N   . GLU B 138 ? 1.2030 0.6593 1.3120 0.1637  -0.0229 0.0280  1608 GLU B N   
3197 C  CA  . GLU B 138 ? 1.3792 0.8044 1.4846 0.1730  -0.0324 0.0253  1608 GLU B CA  
3198 C  C   . GLU B 138 ? 1.3715 0.7620 1.4567 0.1883  -0.0543 0.0307  1608 GLU B C   
3199 O  O   . GLU B 138 ? 1.1865 0.5825 1.2810 0.2047  -0.0630 0.0219  1608 GLU B O   
3200 C  CB  . GLU B 138 ? 1.3325 0.7314 1.4199 0.1543  -0.0224 0.0336  1608 GLU B CB  
3201 C  CG  . GLU B 138 ? 1.0988 0.5267 1.1933 0.1345  -0.0017 0.0355  1608 GLU B CG  
3202 C  CD  . GLU B 138 ? 1.3515 0.7616 1.4373 0.1174  0.0085  0.0399  1608 GLU B CD  
3203 O  OE1 . GLU B 138 ? 1.4273 0.7958 1.4844 0.1101  0.0030  0.0514  1608 GLU B OE1 
3204 O  OE2 . GLU B 138 ? 1.3444 0.7815 1.4517 0.1110  0.0215  0.0321  1608 GLU B OE2 
3205 N  N   . GLU B 139 ? 1.4283 0.7957 1.4814 0.1802  -0.0589 0.0456  1609 GLU B N   
3206 C  CA  . GLU B 139 ? 1.3389 0.6737 1.3697 0.1940  -0.0803 0.0522  1609 GLU B CA  
3207 C  C   . GLU B 139 ? 1.3454 0.7101 1.3994 0.2151  -0.0928 0.0412  1609 GLU B C   
3208 O  O   . GLU B 139 ? 1.4677 0.8199 1.5143 0.2294  -0.1088 0.0416  1609 GLU B O   
3209 C  CB  . GLU B 139 ? 1.2842 0.5893 1.2738 0.1799  -0.0819 0.0706  1609 GLU B CB  
3210 N  N   . GLY B 140 ? 1.2837 0.6937 1.3663 0.2152  -0.0841 0.0316  1610 GLY B N   
3211 C  CA  . GLY B 140 ? 1.1120 0.5528 1.2209 0.2341  -0.0954 0.0202  1610 GLY B CA  
3212 C  C   . GLY B 140 ? 1.1993 0.6371 1.2910 0.2382  -0.1090 0.0271  1610 GLY B C   
3213 O  O   . GLY B 140 ? 1.2734 0.7378 1.3879 0.2537  -0.1199 0.0175  1610 GLY B O   
3214 N  N   . THR B 141 ? 1.3721 0.7805 1.4249 0.2243  -0.1085 0.0430  1611 THR B N   
3215 C  CA  . THR B 141 ? 1.4016 0.8065 1.4338 0.2266  -0.1206 0.0500  1611 THR B CA  
3216 C  C   . THR B 141 ? 1.3926 0.7990 1.4012 0.2040  -0.1047 0.0601  1611 THR B C   
3217 O  O   . THR B 141 ? 1.3852 0.7820 1.3839 0.1869  -0.0879 0.0659  1611 THR B O   
3218 C  CB  . THR B 141 ? 1.4147 0.7704 1.4132 0.2380  -0.1437 0.0609  1611 THR B CB  
3219 O  OG1 . THR B 141 ? 1.3099 0.6652 1.2891 0.2411  -0.1564 0.0667  1611 THR B OG1 
3220 C  CG2 . THR B 141 ? 1.3929 0.7020 1.3532 0.2218  -0.1374 0.0768  1611 THR B CG2 
3221 N  N   . LEU B 142 ? 1.2231 0.6422 1.2230 0.2046  -0.1107 0.0615  1612 LEU B N   
3222 C  CA  . LEU B 142 ? 1.2235 0.6445 1.1991 0.1858  -0.0979 0.0698  1612 LEU B CA  
3223 C  C   . LEU B 142 ? 1.3530 0.7345 1.2802 0.1840  -0.1109 0.0852  1612 LEU B C   
3224 O  O   . LEU B 142 ? 1.2606 0.6432 1.1641 0.1703  -0.1023 0.0917  1612 LEU B O   
3225 C  CB  . LEU B 142 ? 1.2489 0.7159 1.2501 0.1852  -0.0923 0.0588  1612 LEU B CB  
3226 N  N   . ASP B 143 ? 1.4902 0.8365 1.4013 0.1980  -0.1318 0.0908  1613 ASP B N   
3227 C  CA  . ASP B 143 ? 1.6596 0.9675 1.5234 0.1980  -0.1469 0.1058  1613 ASP B CA  
3228 C  C   . ASP B 143 ? 1.6352 0.9035 1.4572 0.1784  -0.1362 0.1231  1613 ASP B C   
3229 O  O   . ASP B 143 ? 1.6354 0.8729 1.4135 0.1740  -0.1448 0.1372  1613 ASP B O   
3230 C  CB  . ASP B 143 ? 1.8751 1.1570 1.7357 0.2211  -0.1751 0.1064  1613 ASP B CB  
3231 C  CG  . ASP B 143 ? 1.9161 1.2329 1.8067 0.2404  -0.1908 0.0927  1613 ASP B CG  
3232 O  OD1 . ASP B 143 ? 1.9202 1.2821 1.8381 0.2357  -0.1791 0.0817  1613 ASP B OD1 
3233 O  OD2 . ASP B 143 ? 1.8705 1.1688 1.7573 0.2603  -0.2155 0.0930  1613 ASP B OD2 
3234 N  N   . GLY B 144 ? 1.5306 0.8002 1.3645 0.1656  -0.1175 0.1226  1614 GLY B N   
3235 C  CA  . GLY B 144 ? 1.6401 0.8769 1.4370 0.1448  -0.1058 0.1385  1614 GLY B CA  
3236 C  C   . GLY B 144 ? 1.6873 0.9476 1.4754 0.1245  -0.0837 0.1408  1614 GLY B C   
3237 O  O   . GLY B 144 ? 1.7361 0.9720 1.4870 0.1071  -0.0753 0.1551  1614 GLY B O   
3238 N  N   . LEU B 145 ? 1.7218 1.0293 1.5434 0.1266  -0.0743 0.1266  1615 LEU B N   
3239 C  CA  . LEU B 145 ? 1.6590 0.9926 1.4808 0.1086  -0.0516 0.1256  1615 LEU B CA  
3240 C  C   . LEU B 145 ? 1.6740 1.0052 1.4620 0.1043  -0.0541 0.1316  1615 LEU B C   
3241 O  O   . LEU B 145 ? 1.6170 0.9455 1.3974 0.1182  -0.0731 0.1301  1615 LEU B O   
3242 C  CB  . LEU B 145 ? 1.5394 0.9212 1.4098 0.1122  -0.0408 0.1084  1615 LEU B CB  
3243 C  CG  . LEU B 145 ? 1.4870 0.8721 1.3860 0.1115  -0.0329 0.1033  1615 LEU B CG  
3244 C  CD1 . LEU B 145 ? 1.2923 0.7228 1.2301 0.1068  -0.0154 0.0903  1615 LEU B CD1 
3245 C  CD2 . LEU B 145 ? 1.3708 0.7199 1.2431 0.0963  -0.0255 0.1168  1615 LEU B CD2 
3246 N  N   . ASP B 146 ? 1.6204 0.9545 1.3888 0.0849  -0.0346 0.1378  1616 ASP B N   
3247 C  CA  . ASP B 146 ? 1.6295 0.9632 1.3639 0.0782  -0.0327 0.1428  1616 ASP B CA  
3248 C  C   . ASP B 146 ? 1.5435 0.9224 1.3040 0.0764  -0.0195 0.1285  1616 ASP B C   
3249 O  O   . ASP B 146 ? 1.4344 0.8362 1.2170 0.0659  0.0007  0.1233  1616 ASP B O   
3250 C  CB  . ASP B 146 ? 1.6995 1.0069 1.3930 0.0578  -0.0192 0.1587  1616 ASP B CB  
3251 C  CG  . ASP B 146 ? 1.8011 1.1218 1.4692 0.0469  -0.0071 0.1597  1616 ASP B CG  
3252 O  OD1 . ASP B 146 ? 1.7928 1.1261 1.4596 0.0298  0.0156  0.1610  1616 ASP B OD1 
3253 O  OD2 . ASP B 146 ? 1.8488 1.1683 1.4986 0.0559  -0.0208 0.1585  1616 ASP B OD2 
3254 N  N   . HIS B 147 ? 1.5059 0.8957 1.2621 0.0863  -0.0319 0.1226  1617 HIS B N   
3255 C  CA  . HIS B 147 ? 1.4744 0.9036 1.2544 0.0866  -0.0236 0.1084  1617 HIS B CA  
3256 C  C   . HIS B 147 ? 1.4405 0.8704 1.1860 0.0753  -0.0138 0.1114  1617 HIS B C   
3257 O  O   . HIS B 147 ? 1.4382 0.8946 1.1952 0.0773  -0.0116 0.1000  1617 HIS B O   
3258 C  CB  . HIS B 147 ? 1.5170 0.9617 1.3198 0.1048  -0.0440 0.0976  1617 HIS B CB  
3259 C  CG  . HIS B 147 ? 1.6050 1.0447 1.4344 0.1188  -0.0578 0.0954  1617 HIS B CG  
3260 N  ND1 . HIS B 147 ? 1.6415 1.0764 1.4739 0.1362  -0.0822 0.0928  1617 HIS B ND1 
3261 C  CD2 . HIS B 147 ? 1.6016 1.0416 1.4561 0.1187  -0.0510 0.0944  1617 HIS B CD2 
3262 C  CE1 . HIS B 147 ? 1.6295 1.0621 1.4880 0.1467  -0.0891 0.0900  1617 HIS B CE1 
3263 N  NE2 . HIS B 147 ? 1.6045 1.0392 1.4757 0.1363  -0.0704 0.0909  1617 HIS B NE2 
3264 N  N   . SER B 148 ? 1.3673 0.7681 1.0696 0.0633  -0.0083 0.1262  1618 SER B N   
3265 C  CA  . SER B 148 ? 1.4040 0.8040 1.0689 0.0535  0.0001  0.1292  1618 SER B CA  
3266 C  C   . SER B 148 ? 1.2391 0.6760 0.9264 0.0454  0.0221  0.1169  1618 SER B C   
3267 O  O   . SER B 148 ? 1.3459 0.7939 1.0173 0.0444  0.0245  0.1111  1618 SER B O   
3268 C  CB  . SER B 148 ? 1.4397 0.8047 1.0576 0.0391  0.0064  0.1478  1618 SER B CB  
3269 O  OG  . SER B 148 ? 1.4121 0.7803 1.0448 0.0257  0.0261  0.1514  1618 SER B OG  
3270 N  N   . ASP B 149 ? 1.0592 0.5145 0.7828 0.0405  0.0372  0.1122  1619 ASP B N   
3271 C  CA  . ASP B 149 ? 1.1400 0.6278 0.8841 0.0327  0.0581  0.1017  1619 ASP B CA  
3272 C  C   . ASP B 149 ? 1.2075 0.7224 0.9743 0.0429  0.0524  0.0858  1619 ASP B C   
3273 O  O   . ASP B 149 ? 1.1063 0.6432 0.8794 0.0376  0.0670  0.0771  1619 ASP B O   
3274 C  CB  . ASP B 149 ? 1.0811 0.5826 0.8616 0.0272  0.0721  0.0997  1619 ASP B CB  
3275 C  CG  . ASP B 149 ? 1.2107 0.6968 0.9700 0.0105  0.0876  0.1123  1619 ASP B CG  
3276 O  OD1 . ASP B 149 ? 1.1800 0.6483 0.8967 0.0021  0.0904  0.1218  1619 ASP B OD1 
3277 O  OD2 . ASP B 149 ? 1.1364 0.6290 0.9212 0.0050  0.0972  0.1124  1619 ASP B OD2 
3278 N  N   . PHE B 150 ? 1.2109 0.7253 0.9918 0.0572  0.0317  0.0813  1620 PHE B N   
3279 C  CA  . PHE B 150 ? 1.2540 0.7950 1.0620 0.0659  0.0256  0.0661  1620 PHE B CA  
3280 C  C   . PHE B 150 ? 1.4482 0.9794 1.2324 0.0750  0.0047  0.0649  1620 PHE B C   
3281 O  O   . PHE B 150 ? 1.4430 0.9896 1.2522 0.0855  -0.0090 0.0549  1620 PHE B O   
3282 C  CB  . PHE B 150 ? 1.1196 0.6785 0.9762 0.0741  0.0212  0.0587  1620 PHE B CB  
3283 C  CG  . PHE B 150 ? 1.0608 0.6216 0.9368 0.0671  0.0361  0.0625  1620 PHE B CG  
3284 C  CD1 . PHE B 150 ? 0.9701 0.5533 0.8665 0.0586  0.0559  0.0564  1620 PHE B CD1 
3285 C  CD2 . PHE B 150 ? 1.0406 0.5799 0.9141 0.0696  0.0294  0.0717  1620 PHE B CD2 
3286 C  CE1 . PHE B 150 ? 0.9601 0.5459 0.8742 0.0520  0.0686  0.0596  1620 PHE B CE1 
3287 C  CE2 . PHE B 150 ? 1.0839 0.6245 0.9745 0.0626  0.0424  0.0744  1620 PHE B CE2 
3288 C  CZ  . PHE B 150 ? 1.0124 0.5770 0.9233 0.0536  0.0619  0.0684  1620 PHE B CZ  
3289 N  N   . GLN B 151 ? 1.5949 1.1019 1.3304 0.0704  0.0022  0.0747  1621 GLN B N   
3290 C  CA  . GLN B 151 ? 1.7042 1.1953 1.4141 0.0803  -0.0216 0.0767  1621 GLN B CA  
3291 C  C   . GLN B 151 ? 1.6964 1.2071 1.4090 0.0845  -0.0278 0.0627  1621 GLN B C   
3292 O  O   . GLN B 151 ? 1.8226 1.3315 1.5354 0.0958  -0.0502 0.0594  1621 GLN B O   
3293 C  CB  . GLN B 151 ? 1.6910 1.1472 1.3439 0.0736  -0.0234 0.0929  1621 GLN B CB  
3294 N  N   . ASP B 152 ? 1.4594 0.9895 1.1769 0.0765  -0.0099 0.0536  1622 ASP B N   
3295 C  CA  . ASP B 152 ? 1.5605 1.1075 1.2813 0.0802  -0.0158 0.0393  1622 ASP B CA  
3296 C  C   . ASP B 152 ? 1.4674 1.0456 1.2370 0.0798  -0.0053 0.0252  1622 ASP B C   
3297 O  O   . ASP B 152 ? 1.4954 1.0879 1.2666 0.0769  0.0021  0.0139  1622 ASP B O   
3298 C  CB  . ASP B 152 ? 1.6784 1.2168 1.3531 0.0724  -0.0072 0.0395  1622 ASP B CB  
3299 C  CG  . ASP B 152 ? 1.8214 1.3291 1.4446 0.0738  -0.0220 0.0521  1622 ASP B CG  
3300 O  OD1 . ASP B 152 ? 1.8749 1.3658 1.4588 0.0638  -0.0095 0.0627  1622 ASP B OD1 
3301 O  OD2 . ASP B 152 ? 1.8406 1.3414 1.4629 0.0848  -0.0466 0.0517  1622 ASP B OD2 
3302 N  N   . THR B 153 ? 1.3010 0.8887 1.1099 0.0832  -0.0052 0.0258  1623 THR B N   
3303 C  CA  . THR B 153 ? 1.2501 0.8653 1.1052 0.0826  0.0043  0.0148  1623 THR B CA  
3304 C  C   . THR B 153 ? 1.1744 0.8032 1.0633 0.0930  -0.0140 0.0078  1623 THR B C   
3305 O  O   . THR B 153 ? 1.3222 0.9395 1.2035 0.1014  -0.0326 0.0125  1623 THR B O   
3306 C  CB  . THR B 153 ? 1.2119 0.8299 1.0857 0.0765  0.0219  0.0207  1623 THR B CB  
3307 O  OG1 . THR B 153 ? 0.9775 0.5888 0.8674 0.0832  0.0114  0.0269  1623 THR B OG1 
3308 C  CG2 . THR B 153 ? 1.2131 0.8142 1.0506 0.0663  0.0370  0.0309  1623 THR B CG2 
3309 N  N   . ASP B 154 ? 1.0148 0.6686 0.9418 0.0923  -0.0087 -0.0034 1624 ASP B N   
3310 C  CA  . ASP B 154 ? 0.9760 0.6472 0.9410 0.0999  -0.0220 -0.0099 1624 ASP B CA  
3311 C  C   . ASP B 154 ? 0.9565 0.6330 0.9505 0.1019  -0.0166 -0.0051 1624 ASP B C   
3312 O  O   . ASP B 154 ? 0.9048 0.6013 0.9363 0.1061  -0.0214 -0.0116 1624 ASP B O   
3313 C  CB  . ASP B 154 ? 1.0439 0.7382 1.0350 0.0971  -0.0197 -0.0236 1624 ASP B CB  
3314 C  CG  . ASP B 154 ? 1.0586 0.7632 1.0660 0.0888  0.0023  -0.0261 1624 ASP B CG  
3315 O  OD1 . ASP B 154 ? 1.0860 0.7808 1.0816 0.0845  0.0162  -0.0177 1624 ASP B OD1 
3316 O  OD2 . ASP B 154 ? 0.9198 0.6418 0.9521 0.0863  0.0049  -0.0362 1624 ASP B OD2 
3317 N  N   . ILE B 155 ? 0.8367 0.4960 0.8136 0.0980  -0.0062 0.0056  1625 ILE B N   
3318 C  CA  . ILE B 155 ? 0.8682 0.5277 0.8669 0.1001  -0.0025 0.0105  1625 ILE B CA  
3319 C  C   . ILE B 155 ? 1.0402 0.6851 1.0323 0.1114  -0.0224 0.0157  1625 ILE B C   
3320 O  O   . ILE B 155 ? 0.9405 0.5602 0.8948 0.1129  -0.0312 0.0241  1625 ILE B O   
3321 C  CB  . ILE B 155 ? 0.9433 0.5899 0.9266 0.0904  0.0159  0.0194  1625 ILE B CB  
3322 C  CG1 . ILE B 155 ? 0.8951 0.5585 0.8878 0.0810  0.0345  0.0130  1625 ILE B CG1 
3323 C  CG2 . ILE B 155 ? 0.7825 0.4264 0.7859 0.0928  0.0178  0.0240  1625 ILE B CG2 
3324 C  CD1 . ILE B 155 ? 0.7604 0.4185 0.7472 0.0712  0.0537  0.0198  1625 ILE B CD1 
3325 N  N   . PRO B 156 ? 1.0389 0.6990 1.0658 0.1202  -0.0309 0.0105  1626 PRO B N   
3326 C  CA  . PRO B 156 ? 1.0622 0.7102 1.0859 0.1331  -0.0511 0.0139  1626 PRO B CA  
3327 C  C   . PRO B 156 ? 0.9511 0.5739 0.9618 0.1344  -0.0486 0.0248  1626 PRO B C   
3328 O  O   . PRO B 156 ? 0.9645 0.5893 0.9866 0.1275  -0.0324 0.0266  1626 PRO B O   
3329 C  CB  . PRO B 156 ? 0.9782 0.6573 1.0485 0.1410  -0.0576 0.0024  1626 PRO B CB  
3330 C  CG  . PRO B 156 ? 1.0345 0.7337 1.1311 0.1311  -0.0367 -0.0021 1626 PRO B CG  
3331 C  CD  . PRO B 156 ? 0.9894 0.6800 1.0602 0.1188  -0.0227 0.0007  1626 PRO B CD  
3332 N  N   . PHE B 157 ? 1.3274 0.9249 1.3135 0.1433  -0.0662 0.0322  1627 PHE B N   
3333 C  CA  . PHE B 157 ? 1.4243 0.9933 1.3961 0.1451  -0.0666 0.0429  1627 PHE B CA  
3334 C  C   . PHE B 157 ? 1.3776 0.9527 1.3802 0.1597  -0.0785 0.0381  1627 PHE B C   
3335 O  O   . PHE B 157 ? 1.2816 0.8535 1.2983 0.1588  -0.0697 0.0392  1627 PHE B O   
3336 C  CB  . PHE B 157 ? 1.4950 1.0268 1.4170 0.1455  -0.0783 0.0558  1627 PHE B CB  
3337 C  CG  . PHE B 157 ? 1.4959 1.0218 1.3847 0.1318  -0.0668 0.0601  1627 PHE B CG  
3338 C  CD1 . PHE B 157 ? 1.2647 0.8049 1.1619 0.1180  -0.0431 0.0579  1627 PHE B CD1 
3339 C  CD2 . PHE B 157 ? 1.6144 1.1223 1.4644 0.1335  -0.0800 0.0654  1627 PHE B CD2 
3340 C  CE1 . PHE B 157 ? 1.4233 0.9605 1.2918 0.1066  -0.0320 0.0603  1627 PHE B CE1 
3341 C  CE2 . PHE B 157 ? 1.6656 1.1699 1.4845 0.1213  -0.0685 0.0681  1627 PHE B CE2 
3342 C  CZ  . PHE B 157 ? 1.6374 1.1569 1.4663 0.1081  -0.0440 0.0651  1627 PHE B CZ  
3343 N  N   . GLU B 158 ? 1.5111 1.0976 1.5264 0.1733  -0.0981 0.0315  1628 GLU B N   
3344 C  CA  . GLU B 158 ? 1.6270 1.2253 1.6757 0.1886  -0.1093 0.0246  1628 GLU B CA  
3345 C  C   . GLU B 158 ? 1.5090 1.1492 1.6042 0.1857  -0.0968 0.0115  1628 GLU B C   
3346 O  O   . GLU B 158 ? 1.6837 1.3517 1.7977 0.1860  -0.1005 0.0024  1628 GLU B O   
3347 C  CB  . GLU B 158 ? 1.7777 1.3736 1.8228 0.2044  -0.1358 0.0225  1628 GLU B CB  
3348 N  N   . VAL B 159 ? 1.1373 0.7810 1.2495 0.1820  -0.0820 0.0108  1629 VAL B N   
3349 C  CA  . VAL B 159 ? 1.1186 0.7995 1.2730 0.1793  -0.0698 -0.0004 1629 VAL B CA  
3350 C  C   . VAL B 159 ? 1.1693 0.8509 1.3450 0.1884  -0.0693 -0.0034 1629 VAL B C   
3351 O  O   . VAL B 159 ? 1.0876 0.7374 1.2429 0.1934  -0.0745 0.0041  1629 VAL B O   
3352 C  CB  . VAL B 159 ? 0.9598 0.6489 1.1129 0.1617  -0.0474 0.0007  1629 VAL B CB  
3353 C  CG1 . VAL B 159 ? 1.0592 0.7468 1.1904 0.1536  -0.0476 0.0023  1629 VAL B CG1 
3354 C  CG2 . VAL B 159 ? 1.0338 0.6981 1.1686 0.1543  -0.0349 0.0098  1629 VAL B CG2 
3355 N  N   . PRO B 160 ? 1.2956 1.0120 1.5113 0.1908  -0.0634 -0.0146 1630 PRO B N   
3356 C  CA  . PRO B 160 ? 1.3237 1.0426 1.5596 0.1997  -0.0618 -0.0191 1630 PRO B CA  
3357 C  C   . PRO B 160 ? 1.1141 0.8073 1.3315 0.1906  -0.0482 -0.0111 1630 PRO B C   
3358 O  O   . PRO B 160 ? 1.1351 0.8331 1.3493 0.1755  -0.0313 -0.0085 1630 PRO B O   
3359 C  CB  . PRO B 160 ? 1.3002 1.0636 1.5782 0.1980  -0.0526 -0.0312 1630 PRO B CB  
3360 C  CG  . PRO B 160 ? 1.2469 1.0250 1.5230 0.1842  -0.0453 -0.0309 1630 PRO B CG  
3361 C  CD  . PRO B 160 ? 1.2863 1.0409 1.5302 0.1857  -0.0589 -0.0240 1630 PRO B CD  
3362 N  N   . LEU B 161 ? 1.0713 0.7370 1.2775 0.2002  -0.0564 -0.0077 1631 LEU B N   
3363 C  CA  . LEU B 161 ? 1.0243 0.6648 1.2148 0.1919  -0.0452 -0.0009 1631 LEU B CA  
3364 C  C   . LEU B 161 ? 1.0080 0.6714 1.2304 0.1932  -0.0341 -0.0109 1631 LEU B C   
3365 O  O   . LEU B 161 ? 1.0507 0.7252 1.2951 0.2085  -0.0428 -0.0201 1631 LEU B O   
3366 C  CB  . LEU B 161 ? 1.0660 0.6633 1.2284 0.2004  -0.0595 0.0075  1631 LEU B CB  
3367 C  CG  . LEU B 161 ? 1.1027 0.6650 1.2311 0.1854  -0.0500 0.0207  1631 LEU B CG  
3368 C  CD1 . LEU B 161 ? 1.3216 0.8383 1.4165 0.1925  -0.0666 0.0313  1631 LEU B CD1 
3369 C  CD2 . LEU B 161 ? 0.9834 0.5496 1.1263 0.1786  -0.0349 0.0173  1631 LEU B CD2 
3370 N  N   . PRO B 162 ? 0.9213 0.5933 1.1474 0.1784  -0.0153 -0.0099 1632 PRO B N   
3371 C  CA  . PRO B 162 ? 0.9502 0.6458 1.2054 0.1791  -0.0047 -0.0195 1632 PRO B CA  
3372 C  C   . PRO B 162 ? 1.0796 0.7551 1.3346 0.1899  -0.0104 -0.0222 1632 PRO B C   
3373 O  O   . PRO B 162 ? 1.0189 0.6560 1.2469 0.1903  -0.0168 -0.0137 1632 PRO B O   
3374 C  CB  . PRO B 162 ? 0.9670 0.6658 1.2168 0.1605  0.0140  -0.0148 1632 PRO B CB  
3375 C  CG  . PRO B 162 ? 0.9678 0.6600 1.1966 0.1512  0.0144  -0.0068 1632 PRO B CG  
3376 C  CD  . PRO B 162 ? 0.9389 0.6027 1.1439 0.1608  -0.0031 -0.0009 1632 PRO B CD  
3377 N  N   . ALA B 163 ? 0.9602 0.6619 1.2453 0.1985  -0.0079 -0.0345 1633 ALA B N   
3378 C  CA  . ALA B 163 ? 1.1445 0.8298 1.4319 0.2097  -0.0123 -0.0396 1633 ALA B CA  
3379 C  C   . ALA B 163 ? 1.0014 0.6712 1.2785 0.1970  0.0011  -0.0362 1633 ALA B C   
3380 O  O   . ALA B 163 ? 0.9319 0.5719 1.1971 0.2021  -0.0039 -0.0357 1633 ALA B O   
3381 C  CB  . ALA B 163 ? 1.1421 0.8631 1.4651 0.2236  -0.0135 -0.0551 1633 ALA B CB  
3382 N  N   . LYS B 164 ? 0.7780 0.4666 1.0597 0.1809  0.0171  -0.0342 1634 LYS B N   
3383 C  CA  . LYS B 164 ? 0.8728 0.5519 1.1480 0.1685  0.0298  -0.0317 1634 LYS B CA  
3384 C  C   . LYS B 164 ? 0.9133 0.5860 1.1707 0.1506  0.0390  -0.0204 1634 LYS B C   
3385 O  O   . LYS B 164 ? 0.9641 0.6493 1.2206 0.1471  0.0390  -0.0173 1634 LYS B O   
3386 C  CB  . LYS B 164 ? 0.9293 0.6420 1.2316 0.1677  0.0415  -0.0426 1634 LYS B CB  
3387 N  N   . GLN B 165 ? 0.9497 0.6030 1.1933 0.1393  0.0465  -0.0149 1635 GLN B N   
3388 C  CA  . GLN B 165 ? 0.9417 0.5905 1.1702 0.1222  0.0566  -0.0051 1635 GLN B CA  
3389 C  C   . GLN B 165 ? 0.9320 0.6148 1.1808 0.1135  0.0708  -0.0096 1635 GLN B C   
3390 O  O   . GLN B 165 ? 0.8137 0.5080 1.0769 0.1128  0.0770  -0.0159 1635 GLN B O   
3391 C  CB  . GLN B 165 ? 0.9002 0.5163 1.1078 0.1129  0.0586  0.0023  1635 GLN B CB  
3392 C  CG  . GLN B 165 ? 1.0479 0.6293 1.2248 0.1106  0.0503  0.0140  1635 GLN B CG  
3393 C  CD  . GLN B 165 ? 1.1769 0.7252 1.3350 0.1013  0.0515  0.0208  1635 GLN B CD  
3394 O  OE1 . GLN B 165 ? 1.2426 0.7955 1.4006 0.0862  0.0641  0.0236  1635 GLN B OE1 
3395 N  NE2 . GLN B 165 ? 1.1374 0.6517 1.2800 0.1101  0.0378  0.0234  1635 GLN B NE2 
3396 N  N   . HIS B 166 ? 0.8948 0.5922 1.1432 0.1069  0.0754  -0.0062 1636 HIS B N   
3397 C  CA  . HIS B 166 ? 0.8103 0.5373 1.0769 0.0991  0.0876  -0.0098 1636 HIS B CA  
3398 C  C   . HIS B 166 ? 0.7569 0.4781 1.0174 0.0857  0.0989  -0.0054 1636 HIS B C   
3399 O  O   . HIS B 166 ? 0.6521 0.3909 0.9283 0.0822  0.1068  -0.0101 1636 HIS B O   
3400 C  CB  . HIS B 166 ? 0.7335 0.4755 1.0012 0.0965  0.0884  -0.0083 1636 HIS B CB  
3401 C  CG  . HIS B 166 ? 0.8392 0.6065 1.1223 0.0878  0.1002  -0.0106 1636 HIS B CG  
3402 N  ND1 . HIS B 166 ? 0.8966 0.6913 1.2035 0.0910  0.1019  -0.0180 1636 HIS B ND1 
3403 C  CD2 . HIS B 166 ? 0.9241 0.6931 1.2021 0.0761  0.1105  -0.0062 1636 HIS B CD2 
3404 C  CE1 . HIS B 166 ? 0.8837 0.6929 1.1977 0.0817  0.1119  -0.0173 1636 HIS B CE1 
3405 N  NE2 . HIS B 166 ? 0.9034 0.6981 1.2011 0.0734  0.1170  -0.0107 1636 HIS B NE2 
3406 N  N   . VAL B 167 ? 0.7001 0.3968 0.9379 0.0780  0.0995  0.0034  1637 VAL B N   
3407 C  CA  . VAL B 167 ? 0.6167 0.3139 0.8515 0.0639  0.1111  0.0075  1637 VAL B CA  
3408 C  C   . VAL B 167 ? 0.8177 0.4981 1.0499 0.0616  0.1108  0.0069  1637 VAL B C   
3409 O  O   . VAL B 167 ? 0.9033 0.5565 1.1216 0.0666  0.1016  0.0091  1637 VAL B O   
3410 C  CB  . VAL B 167 ? 0.7956 0.4810 1.0094 0.0544  0.1148  0.0168  1637 VAL B CB  
3411 C  CG1 . VAL B 167 ? 0.8904 0.5752 1.1018 0.0401  0.1260  0.0207  1637 VAL B CG1 
3412 C  CG2 . VAL B 167 ? 0.6840 0.3897 0.9029 0.0553  0.1171  0.0153  1637 VAL B CG2 
3413 N  N   . PRO B 168 ? 0.8756 0.5704 1.1208 0.0548  0.1194  0.0035  1638 PRO B N   
3414 C  CA  . PRO B 168 ? 1.0473 0.7266 1.2904 0.0523  0.1186  0.0018  1638 PRO B CA  
3415 C  C   . PRO B 168 ? 1.1376 0.7870 1.3584 0.0422  0.1179  0.0111  1638 PRO B C   
3416 O  O   . PRO B 168 ? 1.0739 0.7222 1.2840 0.0332  0.1230  0.0189  1638 PRO B O   
3417 C  CB  . PRO B 168 ? 0.9438 0.6474 1.2035 0.0448  0.1285  -0.0022 1638 PRO B CB  
3418 C  CG  . PRO B 168 ? 0.9415 0.6732 1.2157 0.0488  0.1319  -0.0052 1638 PRO B CG  
3419 C  CD  . PRO B 168 ? 0.9852 0.7109 1.2486 0.0511  0.1284  0.0000  1638 PRO B CD  
3420 N  N   . GLU B 169 ? 1.1155 0.7404 1.3291 0.0432  0.1119  0.0100  1639 GLU B N   
3421 C  CA  . GLU B 169 ? 1.0331 0.6241 1.2232 0.0343  0.1090  0.0195  1639 GLU B CA  
3422 C  C   . GLU B 169 ? 0.9033 0.5007 1.0905 0.0158  0.1207  0.0262  1639 GLU B C   
3423 O  O   . GLU B 169 ? 1.0361 0.6183 1.2046 0.0067  0.1226  0.0361  1639 GLU B O   
3424 C  CB  . GLU B 169 ? 1.0913 0.6548 1.2763 0.0383  0.1004  0.0158  1639 GLU B CB  
3425 N  N   . ALA B 170 ? 0.8484 0.4704 1.0542 0.0103  0.1289  0.0207  1640 ALA B N   
3426 C  CA  . ALA B 170 ? 0.9163 0.5472 1.1228 -0.0065 0.1395  0.0258  1640 ALA B CA  
3427 C  C   . ALA B 170 ? 1.0053 0.6510 1.2082 -0.0101 0.1467  0.0314  1640 ALA B C   
3428 O  O   . ALA B 170 ? 1.1785 0.8153 1.3676 -0.0221 0.1520  0.0396  1640 ALA B O   
3429 C  CB  . ALA B 170 ? 0.8880 0.5440 1.1160 -0.0096 0.1452  0.0182  1640 ALA B CB  
3430 N  N   . GLU B 171 ? 0.8615 0.5294 1.0760 0.0000  0.1471  0.0266  1641 GLU B N   
3431 C  CA  . GLU B 171 ? 1.0019 0.6835 1.2132 -0.0023 0.1532  0.0302  1641 GLU B CA  
3432 C  C   . GLU B 171 ? 0.9291 0.5865 1.1150 -0.0016 0.1483  0.0380  1641 GLU B C   
3433 O  O   . GLU B 171 ? 1.0064 0.6650 1.1804 -0.0097 0.1550  0.0440  1641 GLU B O   
3434 C  CB  . GLU B 171 ? 1.0684 0.7756 1.2971 0.0082  0.1531  0.0232  1641 GLU B CB  
3435 C  CG  . GLU B 171 ? 1.0833 0.8174 1.3346 0.0055  0.1600  0.0175  1641 GLU B CG  
3436 C  CD  . GLU B 171 ? 1.2290 0.9675 1.4935 0.0127  0.1552  0.0102  1641 GLU B CD  
3437 O  OE1 . GLU B 171 ? 1.2135 0.9320 1.4705 0.0167  0.1480  0.0093  1641 GLU B OE1 
3438 O  OE2 . GLU B 171 ? 1.2584 1.0200 1.5400 0.0147  0.1585  0.0053  1641 GLU B OE2 
3439 N  N   . ARG B 172 ? 0.8347 0.4707 1.0116 0.0087  0.1362  0.0378  1642 ARG B N   
3440 C  CA  . ARG B 172 ? 0.8698 0.4787 1.0202 0.0096  0.1294  0.0461  1642 ARG B CA  
3441 C  C   . ARG B 172 ? 0.9263 0.5138 1.0568 -0.0064 0.1345  0.0561  1642 ARG B C   
3442 O  O   . ARG B 172 ? 0.8533 0.4310 0.9625 -0.0126 0.1369  0.0644  1642 ARG B O   
3443 C  CB  . ARG B 172 ? 0.8003 0.3875 0.9456 0.0235  0.1145  0.0440  1642 ARG B CB  
3444 C  CG  . ARG B 172 ? 0.9320 0.4887 1.0476 0.0238  0.1065  0.0539  1642 ARG B CG  
3445 C  CD  . ARG B 172 ? 1.0658 0.5947 1.1743 0.0357  0.0915  0.0531  1642 ARG B CD  
3446 N  NE  . ARG B 172 ? 1.2675 0.7943 1.3907 0.0360  0.0915  0.0464  1642 ARG B NE  
3447 C  CZ  . ARG B 172 ? 1.3636 0.8636 1.4816 0.0449  0.0796  0.0444  1642 ARG B CZ  
3448 N  NH1 . ARG B 172 ? 1.3855 0.8586 1.4845 0.0545  0.0663  0.0494  1642 ARG B NH1 
3449 N  NH2 . ARG B 172 ? 1.3736 0.8730 1.5046 0.0448  0.0804  0.0371  1642 ARG B NH2 
3450 N  N   . GLU B 173 ? 1.0050 0.5855 1.1417 -0.0142 0.1363  0.0552  1643 GLU B N   
3451 C  CA  . GLU B 173 ? 1.0742 0.6341 1.1938 -0.0313 0.1409  0.0647  1643 GLU B CA  
3452 C  C   . GLU B 173 ? 1.0201 0.6049 1.1444 -0.0453 0.1563  0.0673  1643 GLU B C   
3453 O  O   . GLU B 173 ? 0.9939 0.5659 1.0995 -0.0593 0.1620  0.0769  1643 GLU B O   
3454 C  CB  . GLU B 173 ? 0.8335 0.3793 0.9598 -0.0358 0.1376  0.0618  1643 GLU B CB  
3455 C  CG  . GLU B 173 ? 0.9809 0.4954 1.0984 -0.0232 0.1223  0.0597  1643 GLU B CG  
3456 C  CD  . GLU B 173 ? 1.1669 0.6497 1.2557 -0.0193 0.1132  0.0694  1643 GLU B CD  
3457 O  OE1 . GLU B 173 ? 1.2455 0.7039 1.3115 -0.0336 0.1151  0.0808  1643 GLU B OE1 
3458 O  OE2 . GLU B 173 ? 1.2110 0.6939 1.2998 -0.0025 0.1039  0.0660  1643 GLU B OE2 
3459 N  N   . GLU B 174 ? 0.7642 0.3844 0.9130 -0.0419 0.1633  0.0592  1644 GLU B N   
3460 C  CA  . GLU B 174 ? 1.0004 0.6450 1.1539 -0.0522 0.1770  0.0607  1644 GLU B CA  
3461 C  C   . GLU B 174 ? 0.9915 0.6326 1.1245 -0.0505 0.1788  0.0660  1644 GLU B C   
3462 O  O   . GLU B 174 ? 0.9275 0.5703 1.0480 -0.0628 0.1886  0.0722  1644 GLU B O   
3463 C  CB  . GLU B 174 ? 1.1904 0.8704 1.3732 -0.0473 0.1822  0.0510  1644 GLU B CB  
3464 C  CG  . GLU B 174 ? 1.3574 1.0490 1.5581 -0.0570 0.1870  0.0481  1644 GLU B CG  
3465 C  CD  . GLU B 174 ? 1.4758 1.1532 1.6820 -0.0520 0.1773  0.0438  1644 GLU B CD  
3466 O  OE1 . GLU B 174 ? 1.4444 1.1312 1.6625 -0.0387 0.1719  0.0365  1644 GLU B OE1 
3467 O  OE2 . GLU B 174 ? 1.4983 1.1547 1.6962 -0.0616 0.1751  0.0473  1644 GLU B OE2 
3468 N  N   . VAL B 175 ? 0.9872 0.6240 1.1165 -0.0357 0.1692  0.0632  1645 VAL B N   
3469 C  CA  . VAL B 175 ? 0.9291 0.5592 1.0362 -0.0333 0.1684  0.0679  1645 VAL B CA  
3470 C  C   . VAL B 175 ? 1.0354 0.6313 1.1101 -0.0422 0.1655  0.0800  1645 VAL B C   
3471 O  O   . VAL B 175 ? 0.8642 0.4570 0.9177 -0.0504 0.1722  0.0867  1645 VAL B O   
3472 C  CB  . VAL B 175 ? 0.7365 0.3683 0.8478 -0.0157 0.1566  0.0621  1645 VAL B CB  
3473 C  CG1 . VAL B 175 ? 0.6883 0.3058 0.7725 -0.0127 0.1519  0.0677  1645 VAL B CG1 
3474 C  CG2 . VAL B 175 ? 0.8412 0.5071 0.9802 -0.0097 0.1616  0.0519  1645 VAL B CG2 
3475 N  N   . ARG B 176 ? 0.8071 0.3756 0.8762 -0.0409 0.1554  0.0829  1646 ARG B N   
3476 C  CA  . ARG B 176 ? 0.9383 0.4690 0.9756 -0.0488 0.1503  0.0951  1646 ARG B CA  
3477 C  C   . ARG B 176 ? 1.0689 0.6000 1.0970 -0.0704 0.1644  0.1030  1646 ARG B C   
3478 O  O   . ARG B 176 ? 0.9264 0.4411 0.9254 -0.0797 0.1675  0.1136  1646 ARG B O   
3479 C  CB  . ARG B 176 ? 0.8993 0.4020 0.9371 -0.0422 0.1367  0.0944  1646 ARG B CB  
3480 C  CG  . ARG B 176 ? 0.9762 0.4348 0.9806 -0.0487 0.1287  0.1072  1646 ARG B CG  
3481 C  CD  . ARG B 176 ? 1.0085 0.4393 1.0137 -0.0360 0.1123  0.1043  1646 ARG B CD  
3482 N  NE  . ARG B 176 ? 1.0982 0.5111 1.0870 -0.0200 0.0976  0.1064  1646 ARG B NE  
3483 C  CZ  . ARG B 176 ? 1.1542 0.5717 1.1588 -0.0001 0.0858  0.0966  1646 ARG B CZ  
3484 N  NH1 . ARG B 176 ? 1.1102 0.5483 1.1450 0.0055  0.0877  0.0845  1646 ARG B NH1 
3485 N  NH2 . ARG B 176 ? 1.1186 0.5213 1.1086 0.0138  0.0720  0.0988  1646 ARG B NH2 
3486 N  N   . ASP B 177 ? 1.0783 0.6298 1.1310 -0.0789 0.1733  0.0979  1647 ASP B N   
3487 C  CA  . ASP B 177 ? 1.0496 0.6091 1.0997 -0.0997 0.1877  0.1036  1647 ASP B CA  
3488 C  C   . ASP B 177 ? 0.9882 0.5692 1.0300 -0.1037 0.2001  0.1053  1647 ASP B C   
3489 O  O   . ASP B 177 ? 1.0760 0.6457 1.0933 -0.1178 0.2074  0.1155  1647 ASP B O   
3490 C  CB  . ASP B 177 ? 1.1001 0.6859 1.1833 -0.1049 0.1942  0.0952  1647 ASP B CB  
3491 C  CG  . ASP B 177 ? 1.0294 0.5927 1.1181 -0.1048 0.1838  0.0937  1647 ASP B CG  
3492 O  OD1 . ASP B 177 ? 0.8945 0.4198 0.9608 -0.1036 0.1730  0.1004  1647 ASP B OD1 
3493 O  OD2 . ASP B 177 ? 1.0532 0.6362 1.1683 -0.1053 0.1858  0.0853  1647 ASP B OD2 
3494 N  N   . TRP B 178 ? 0.8992 0.5104 0.9602 -0.0915 0.2025  0.0952  1648 TRP B N   
3495 C  CA  . TRP B 178 ? 0.9008 0.5349 0.9571 -0.0941 0.2146  0.0942  1648 TRP B CA  
3496 C  C   . TRP B 178 ? 0.8890 0.4998 0.9082 -0.0932 0.2109  0.1028  1648 TRP B C   
3497 O  O   . TRP B 178 ? 1.0098 0.6240 1.0102 -0.1048 0.2224  0.1085  1648 TRP B O   
3498 C  CB  . TRP B 178 ? 0.9123 0.5780 0.9956 -0.0800 0.2153  0.0815  1648 TRP B CB  
3499 C  CG  . TRP B 178 ? 0.9976 0.6854 1.0769 -0.0809 0.2267  0.0788  1648 TRP B CG  
3500 C  CD1 . TRP B 178 ? 0.9889 0.7036 1.0799 -0.0909 0.2423  0.0763  1648 TRP B CD1 
3501 C  CD2 . TRP B 178 ? 1.0129 0.6976 1.0748 -0.0711 0.2230  0.0774  1648 TRP B CD2 
3502 N  NE1 . TRP B 178 ? 1.0472 0.7754 1.1287 -0.0872 0.2492  0.0729  1648 TRP B NE1 
3503 C  CE2 . TRP B 178 ? 0.9987 0.7081 1.0614 -0.0755 0.2373  0.0736  1648 TRP B CE2 
3504 C  CE3 . TRP B 178 ? 1.0315 0.6960 1.0779 -0.0588 0.2085  0.0784  1648 TRP B CE3 
3505 C  CZ2 . TRP B 178 ? 1.0151 0.7277 1.0621 -0.0683 0.2375  0.0705  1648 TRP B CZ2 
3506 C  CZ3 . TRP B 178 ? 0.9773 0.6459 1.0089 -0.0523 0.2082  0.0759  1648 TRP B CZ3 
3507 C  CH2 . TRP B 178 ? 0.9494 0.6408 0.9804 -0.0571 0.2226  0.0718  1648 TRP B CH2 
3508 N  N   . VAL B 179 ? 0.8368 0.4250 0.8449 -0.0792 0.1948  0.1034  1649 VAL B N   
3509 C  CA  . VAL B 179 ? 0.8588 0.4235 0.8311 -0.0765 0.1884  0.1113  1649 VAL B CA  
3510 C  C   . VAL B 179 ? 1.0162 0.5503 0.9561 -0.0933 0.1909  0.1262  1649 VAL B C   
3511 O  O   . VAL B 179 ? 0.9232 0.4500 0.8332 -0.1003 0.1962  0.1338  1649 VAL B O   
3512 C  CB  . VAL B 179 ? 0.8286 0.3760 0.7995 -0.0576 0.1689  0.1085  1649 VAL B CB  
3513 C  CG1 . VAL B 179 ? 0.8729 0.3879 0.8036 -0.0560 0.1589  0.1191  1649 VAL B CG1 
3514 C  CG2 . VAL B 179 ? 0.7851 0.3630 0.7817 -0.0428 0.1674  0.0952  1649 VAL B CG2 
3515 N  N   . LEU B 180 ? 1.1463 0.6606 1.0901 -0.1005 0.1869  0.1307  1650 LEU B N   
3516 C  CA  . LEU B 180 ? 1.1565 0.6391 1.0696 -0.1184 0.1890  0.1456  1650 LEU B CA  
3517 C  C   . LEU B 180 ? 1.0089 0.5140 0.9181 -0.1381 0.2100  0.1493  1650 LEU B C   
3518 O  O   . LEU B 180 ? 1.0478 0.5386 0.9228 -0.1489 0.2153  0.1604  1650 LEU B O   
3519 C  CB  . LEU B 180 ? 1.0092 0.4688 0.9317 -0.1226 0.1811  0.1475  1650 LEU B CB  
3520 C  CG  . LEU B 180 ? 1.0264 0.4552 0.9425 -0.1041 0.1597  0.1467  1650 LEU B CG  
3521 C  CD1 . LEU B 180 ? 0.9538 0.3663 0.8858 -0.1047 0.1522  0.1439  1650 LEU B CD1 
3522 C  CD2 . LEU B 180 ? 1.0084 0.3969 0.8808 -0.1046 0.1497  0.1607  1650 LEU B CD2 
3523 N  N   . THR B 181 ? 1.1692 0.7120 1.1135 -0.1419 0.2221  0.1394  1651 THR B N   
3524 C  CA  . THR B 181 ? 1.3601 0.9307 1.3070 -0.1590 0.2426  0.1405  1651 THR B CA  
3525 C  C   . THR B 181 ? 1.3047 0.8853 1.2289 -0.1563 0.2500  0.1412  1651 THR B C   
3526 O  O   . THR B 181 ? 1.3596 0.9357 1.2574 -0.1723 0.2613  0.1507  1651 THR B O   
3527 C  CB  . THR B 181 ? 1.4742 1.0871 1.4654 -0.1573 0.2514  0.1271  1651 THR B CB  
3528 O  OG1 . THR B 181 ? 1.6234 1.2285 1.6324 -0.1648 0.2475  0.1275  1651 THR B OG1 
3529 C  CG2 . THR B 181 ? 1.2895 0.9377 1.2869 -0.1698 0.2721  0.1252  1651 THR B CG2 
3530 N  N   . VAL B 182 ? 0.9975 0.5913 0.9304 -0.1369 0.2436  0.1311  1652 VAL B N   
3531 C  CA  . VAL B 182 ? 0.9025 0.5084 0.8163 -0.1337 0.2507  0.1293  1652 VAL B CA  
3532 C  C   . VAL B 182 ? 1.0646 0.6328 0.9304 -0.1373 0.2434  0.1430  1652 VAL B C   
3533 O  O   . VAL B 182 ? 1.1045 0.6760 0.9434 -0.1461 0.2545  0.1477  1652 VAL B O   
3534 C  CB  . VAL B 182 ? 1.0721 0.6983 1.0070 -0.1127 0.2439  0.1151  1652 VAL B CB  
3535 C  CG1 . VAL B 182 ? 0.9198 0.5527 0.8310 -0.1083 0.2482  0.1129  1652 VAL B CG1 
3536 C  CG2 . VAL B 182 ? 1.0484 0.7124 1.0272 -0.1107 0.2527  0.1026  1652 VAL B CG2 
3537 N  N   . SER B 183 ? 1.1274 0.6587 0.9810 -0.1306 0.2247  0.1497  1653 SER B N   
3538 C  CA  . SER B 183 ? 1.3245 0.8148 1.1318 -0.1340 0.2152  0.1644  1653 SER B CA  
3539 C  C   . SER B 183 ? 1.4139 0.8960 1.1938 -0.1582 0.2305  0.1776  1653 SER B C   
3540 O  O   . SER B 183 ? 1.5821 1.0601 1.3279 -0.1636 0.2365  0.1838  1653 SER B O   
3541 C  CB  . SER B 183 ? 1.3619 0.8129 1.1649 -0.1263 0.1944  0.1702  1653 SER B CB  
3542 O  OG  . SER B 183 ? 1.4202 0.8829 1.2570 -0.1067 0.1826  0.1572  1653 SER B OG  
3543 N  N   . MET B 184 ? 1.3800 0.8632 1.1757 -0.1739 0.2381  0.1811  1654 MET B N   
3544 C  CA  . MET B 184 ? 1.4282 0.9038 1.1984 -0.1993 0.2532  0.1945  1654 MET B CA  
3545 C  C   . MET B 184 ? 1.6424 1.1642 1.4246 -0.2094 0.2773  0.1876  1654 MET B C   
3546 O  O   . MET B 184 ? 1.6211 1.1423 1.3811 -0.2306 0.2922  0.1979  1654 MET B O   
3547 C  CB  . MET B 184 ? 1.1937 0.6514 0.9728 -0.2159 0.2531  0.2021  1654 MET B CB  
3548 C  CG  . MET B 184 ? 1.2212 0.6230 0.9737 -0.2145 0.2328  0.2147  1654 MET B CG  
3549 S  SD  . MET B 184 ? 1.6362 1.0366 1.4250 -0.1882 0.2126  0.2004  1654 MET B SD  
3550 C  CE  . MET B 184 ? 1.5407 0.9808 1.3783 -0.1997 0.2275  0.1896  1654 MET B CE  
3551 N  N   . ASP B 185 ? 1.7028 1.2644 1.5196 -0.1950 0.2816  0.1705  1655 ASP B N   
3552 C  CA  . ASP B 185 ? 1.7367 1.3418 1.5656 -0.2029 0.3039  0.1630  1655 ASP B CA  
3553 C  C   . ASP B 185 ? 1.7667 1.3688 1.5540 -0.2079 0.3129  0.1686  1655 ASP B C   
3554 O  O   . ASP B 185 ? 1.8456 1.4813 1.6371 -0.2173 0.3334  0.1640  1655 ASP B O   
3555 C  CB  . ASP B 185 ? 1.6733 1.3160 1.5432 -0.1842 0.3041  0.1439  1655 ASP B CB  
3556 N  N   . GLN B 186 ? 1.6484 1.2119 1.3957 -0.2019 0.2982  0.1783  1656 GLN B N   
3557 C  CA  . GLN B 186 ? 1.7331 1.2844 1.4321 -0.2090 0.3043  0.1872  1656 GLN B CA  
3558 C  C   . GLN B 186 ? 1.8620 1.4565 1.5674 -0.2067 0.3229  0.1742  1656 GLN B C   
3559 O  O   . GLN B 186 ? 1.7756 1.3747 1.4495 -0.2203 0.3381  0.1801  1656 GLN B O   
3560 C  CB  . GLN B 186 ? 1.6685 1.1960 1.3361 -0.2354 0.3131  0.2063  1656 GLN B CB  
3561 N  N   . ARG B 187 ? 1.8985 1.5243 1.6441 -0.1897 0.3218  0.1562  1657 ARG B N   
3562 C  CA  . ARG B 187 ? 1.9377 1.6051 1.6962 -0.1848 0.3378  0.1413  1657 ARG B CA  
3563 C  C   . ARG B 187 ? 2.0405 1.7046 1.7866 -0.1642 0.3262  0.1319  1657 ARG B C   
3564 O  O   . ARG B 187 ? 2.0970 1.7694 1.8162 -0.1646 0.3354  0.1289  1657 ARG B O   
3565 C  CB  . ARG B 187 ? 1.8482 1.5545 1.6622 -0.1813 0.3456  0.1275  1657 ARG B CB  
3566 N  N   . LEU B 188 ? 2.0651 1.7170 1.8295 -0.1467 0.3061  0.1270  1658 LEU B N   
3567 C  CA  . LEU B 188 ? 2.0807 1.7337 1.8423 -0.1270 0.2943  0.1161  1658 LEU B CA  
3568 C  C   . LEU B 188 ? 2.1075 1.7192 1.8317 -0.1210 0.2737  0.1267  1658 LEU B C   
3569 O  O   . LEU B 188 ? 2.0820 1.6630 1.7965 -0.1257 0.2627  0.1398  1658 LEU B O   
3570 C  CB  . LEU B 188 ? 1.9891 1.6612 1.7991 -0.1112 0.2863  0.1021  1658 LEU B CB  
3571 N  N   . GLU B 189 ? 2.1278 1.7387 1.8311 -0.1100 0.2679  0.1203  1659 GLU B N   
3572 C  CA  . GLU B 189 ? 2.1335 1.7117 1.8105 -0.0990 0.2450  0.1258  1659 GLU B CA  
3573 C  C   . GLU B 189 ? 1.9998 1.5838 1.7152 -0.0805 0.2284  0.1148  1659 GLU B C   
3574 O  O   . GLU B 189 ? 2.0105 1.6252 1.7614 -0.0733 0.2345  0.1000  1659 GLU B O   
3575 C  CB  . GLU B 189 ? 2.1756 1.7513 1.8129 -0.0959 0.2454  0.1231  1659 GLU B CB  
3576 N  N   . GLN B 190 ? 1.8470 1.4015 1.5558 -0.0730 0.2074  0.1223  1660 GLN B N   
3577 C  CA  . GLN B 190 ? 1.6206 1.1798 1.3653 -0.0566 0.1916  0.1132  1660 GLN B CA  
3578 C  C   . GLN B 190 ? 1.4758 1.0285 1.2046 -0.0421 0.1752  0.1075  1660 GLN B C   
3579 O  O   . GLN B 190 ? 1.3453 0.8700 1.0536 -0.0355 0.1563  0.1151  1660 GLN B O   
3580 C  CB  . GLN B 190 ? 1.6858 1.2199 1.4380 -0.0568 0.1796  0.1232  1660 GLN B CB  
3581 N  N   . VAL B 191 ? 1.4028 0.9817 1.1408 -0.0372 0.1824  0.0936  1661 VAL B N   
3582 C  CA  . VAL B 191 ? 1.4025 0.9808 1.1314 -0.0239 0.1681  0.0850  1661 VAL B CA  
3583 C  C   . VAL B 191 ? 1.2967 0.9060 1.0675 -0.0147 0.1708  0.0674  1661 VAL B C   
3584 O  O   . VAL B 191 ? 1.1049 0.7381 0.8999 -0.0197 0.1879  0.0611  1661 VAL B O   
3585 C  CB  . VAL B 191 ? 1.4341 1.0053 1.1156 -0.0287 0.1729  0.0867  1661 VAL B CB  
3586 C  CG1 . VAL B 191 ? 1.4323 0.9933 1.0973 -0.0154 0.1523  0.0815  1661 VAL B CG1 
3587 C  CG2 . VAL B 191 ? 1.3287 0.8738 0.9683 -0.0433 0.1782  0.1052  1661 VAL B CG2 
3588 N  N   . LEU B 192 ? 1.2743 0.8828 1.0543 -0.0012 0.1529  0.0598  1662 LEU B N   
3589 C  CA  . LEU B 192 ? 1.2725 0.9060 1.0888 0.0075  0.1524  0.0440  1662 LEU B CA  
3590 C  C   . LEU B 192 ? 1.2110 0.8580 1.0136 0.0077  0.1613  0.0327  1662 LEU B C   
3591 O  O   . LEU B 192 ? 1.1582 0.7923 0.9203 0.0058  0.1595  0.0354  1662 LEU B O   
3592 C  CB  . LEU B 192 ? 1.2648 0.8930 1.0959 0.0203  0.1302  0.0404  1662 LEU B CB  
3593 C  CG  . LEU B 192 ? 1.1360 0.7501 0.9800 0.0238  0.1178  0.0492  1662 LEU B CG  
3594 C  CD1 . LEU B 192 ? 1.0546 0.6631 0.9030 0.0367  0.0950  0.0454  1662 LEU B CD1 
3595 C  CD2 . LEU B 192 ? 1.0502 0.6823 0.9366 0.0222  0.1272  0.0459  1662 LEU B CD2 
3596 N  N   . PRO B 193 ? 1.1999 0.8717 1.0344 0.0104  0.1704  0.0198  1663 PRO B N   
3597 C  CA  . PRO B 193 ? 1.1588 0.8428 0.9818 0.0118  0.1788  0.0074  1663 PRO B CA  
3598 C  C   . PRO B 193 ? 1.1161 0.7913 0.9243 0.0209  0.1611  0.0002  1663 PRO B C   
3599 O  O   . PRO B 193 ? 1.2301 0.9022 1.0576 0.0285  0.1442  -0.0013 1663 PRO B O   
3600 C  CB  . PRO B 193 ? 1.0084 0.7180 0.8743 0.0142  0.1891  -0.0039 1663 PRO B CB  
3601 C  CG  . PRO B 193 ? 1.0784 0.7899 0.9742 0.0119  0.1887  0.0039  1663 PRO B CG  
3602 C  CD  . PRO B 193 ? 1.0785 0.7668 0.9596 0.0129  0.1726  0.0156  1663 PRO B CD  
3603 N  N   . ARG B 194 ? 1.1874 0.8594 0.9606 0.0198  0.1650  -0.0045 1664 ARG B N   
3604 C  CA  . ARG B 194 ? 1.3027 0.9685 1.0605 0.0278  0.1495  -0.0138 1664 ARG B CA  
3605 C  C   . ARG B 194 ? 1.2724 0.9564 1.0424 0.0314  0.1587  -0.0318 1664 ARG B C   
3606 O  O   . ARG B 194 ? 1.2044 0.9027 0.9780 0.0270  0.1786  -0.0358 1664 ARG B O   
3607 C  CB  . ARG B 194 ? 1.3938 1.0383 1.0977 0.0248  0.1438  -0.0060 1664 ARG B CB  
3608 C  CG  . ARG B 194 ? 1.5328 1.1555 1.2222 0.0217  0.1340  0.0125  1664 ARG B CG  
3609 C  CD  . ARG B 194 ? 1.6733 1.2716 1.3122 0.0223  0.1200  0.0196  1664 ARG B CD  
3610 N  NE  . ARG B 194 ? 1.7574 1.3463 1.4032 0.0332  0.0939  0.0179  1664 ARG B NE  
3611 C  CZ  . ARG B 194 ? 1.7412 1.3203 1.4041 0.0373  0.0798  0.0270  1664 ARG B CZ  
3612 N  NH1 . ARG B 194 ? 1.6956 1.2701 1.3690 0.0313  0.0887  0.0387  1664 ARG B NH1 
3613 N  NH2 . ARG B 194 ? 1.6748 1.2494 1.3452 0.0477  0.0565  0.0237  1664 ARG B NH2 
3614 N  N   . ASP B 195 ? 1.2322 0.9158 1.0096 0.0395  0.1434  -0.0430 1665 ASP B N   
3615 C  CA  . ASP B 195 ? 1.2043 0.9009 0.9939 0.0439  0.1485  -0.0607 1665 ASP B CA  
3616 C  C   . ASP B 195 ? 1.2929 0.9807 1.0392 0.0454  0.1460  -0.0689 1665 ASP B C   
3617 O  O   . ASP B 195 ? 1.3945 1.0680 1.1001 0.0415  0.1440  -0.0596 1665 ASP B O   
3618 C  CB  . ASP B 195 ? 1.1607 0.8629 0.9897 0.0505  0.1343  -0.0683 1665 ASP B CB  
3619 C  CG  . ASP B 195 ? 1.1591 0.8484 0.9808 0.0544  0.1104  -0.0655 1665 ASP B CG  
3620 O  OD1 . ASP B 195 ? 1.1906 0.8652 0.9727 0.0541  0.1028  -0.0615 1665 ASP B OD1 
3621 O  OD2 . ASP B 195 ? 1.1095 0.8041 0.9653 0.0578  0.0990  -0.0672 1665 ASP B OD2 
3622 N  N   . GLU B 196 ? 1.1765 0.8714 0.9301 0.0508  0.1458  -0.0864 1666 GLU B N   
3623 C  CA  . GLU B 196 ? 1.1821 0.8694 0.8961 0.0530  0.1433  -0.0971 1666 GLU B CA  
3624 C  C   . GLU B 196 ? 1.2421 0.9110 0.9297 0.0551  0.1199  -0.0932 1666 GLU B C   
3625 O  O   . GLU B 196 ? 1.2545 0.9140 0.9004 0.0555  0.1169  -0.0983 1666 GLU B O   
3626 C  CB  . GLU B 196 ? 1.2949 0.9912 1.0274 0.0594  0.1446  -0.1175 1666 GLU B CB  
3627 C  CG  . GLU B 196 ? 1.3438 1.0407 1.1158 0.0637  0.1275  -0.1214 1666 GLU B CG  
3628 C  CD  . GLU B 196 ? 1.3871 1.0870 1.1725 0.0694  0.1252  -0.1411 1666 GLU B CD  
3629 O  OE1 . GLU B 196 ? 1.3481 1.0566 1.1744 0.0711  0.1263  -0.1445 1666 GLU B OE1 
3630 O  OE2 . GLU B 196 ? 1.5027 1.1951 1.2566 0.0720  0.1219  -0.1530 1666 GLU B OE2 
3631 N  N   . ARG B 197 ? 1.3532 1.0181 1.0645 0.0569  0.1030  -0.0851 1667 ARG B N   
3632 C  CA  . ARG B 197 ? 1.3102 0.9596 1.0000 0.0598  0.0797  -0.0807 1667 ARG B CA  
3633 C  C   . ARG B 197 ? 1.3922 1.0259 1.0468 0.0556  0.0787  -0.0625 1667 ARG B C   
3634 O  O   . ARG B 197 ? 1.4016 1.0201 1.0298 0.0583  0.0597  -0.0583 1667 ARG B O   
3635 C  CB  . ARG B 197 ? 1.2906 0.9444 1.0218 0.0641  0.0620  -0.0800 1667 ARG B CB  
3636 C  CG  . ARG B 197 ? 1.2896 0.9570 1.0593 0.0669  0.0609  -0.0951 1667 ARG B CG  
3637 C  CD  . ARG B 197 ? 1.2898 0.9686 1.1073 0.0665  0.0620  -0.0886 1667 ARG B CD  
3638 N  NE  . ARG B 197 ? 1.2240 0.9027 1.0610 0.0698  0.0411  -0.0856 1667 ARG B NE  
3639 C  CZ  . ARG B 197 ? 1.0781 0.7607 0.9396 0.0700  0.0388  -0.0745 1667 ARG B CZ  
3640 N  NH1 . ARG B 197 ? 0.9961 0.6810 0.8642 0.0664  0.0553  -0.0649 1667 ARG B NH1 
3641 N  NH2 . ARG B 197 ? 0.9383 0.6234 0.8182 0.0738  0.0199  -0.0736 1667 ARG B NH2 
3642 N  N   . GLY B 198 ? 1.3782 1.0142 1.0310 0.0487  0.0978  -0.0517 1668 GLY B N   
3643 C  CA  . GLY B 198 ? 1.4425 1.0614 1.0688 0.0440  0.0953  -0.0326 1668 GLY B CA  
3644 C  C   . GLY B 198 ? 1.4159 1.0298 1.0706 0.0474  0.0801  -0.0222 1668 GLY B C   
3645 O  O   . GLY B 198 ? 1.5200 1.1148 1.1508 0.0468  0.0697  -0.0080 1668 GLY B O   
3646 N  N   . ALA B 199 ? 1.2167 0.8465 0.9207 0.0516  0.0780  -0.0293 1669 ALA B N   
3647 C  CA  . ALA B 199 ? 1.0721 0.7014 0.8078 0.0552  0.0659  -0.0217 1669 ALA B CA  
3648 C  C   . ALA B 199 ? 1.0991 0.7414 0.8698 0.0508  0.0830  -0.0179 1669 ALA B C   
3649 O  O   . ALA B 199 ? 0.9327 0.5891 0.7145 0.0471  0.1011  -0.0250 1669 ALA B O   
3650 C  CB  . ALA B 199 ? 1.0760 0.7143 0.8404 0.0633  0.0473  -0.0330 1669 ALA B CB  
3651 N  N   . TYR B 200 ? 1.1693 0.8064 0.9569 0.0518  0.0767  -0.0071 1670 TYR B N   
3652 C  CA  . TYR B 200 ? 1.1269 0.7767 0.9513 0.0488  0.0894  -0.0046 1670 TYR B CA  
3653 C  C   . TYR B 200 ? 1.1179 0.7896 0.9810 0.0517  0.0929  -0.0189 1670 TYR B C   
3654 O  O   . TYR B 200 ? 1.0886 0.7650 0.9679 0.0580  0.0780  -0.0266 1670 TYR B O   
3655 C  CB  . TYR B 200 ? 0.9974 0.6384 0.8364 0.0522  0.0772  0.0057  1670 TYR B CB  
3656 C  CG  . TYR B 200 ? 0.8767 0.5324 0.7594 0.0519  0.0841  0.0053  1670 TYR B CG  
3657 C  CD1 . TYR B 200 ? 0.8239 0.4876 0.7162 0.0441  0.1040  0.0077  1670 TYR B CD1 
3658 C  CD2 . TYR B 200 ? 0.9149 0.5777 0.8293 0.0594  0.0704  0.0024  1670 TYR B CD2 
3659 C  CE1 . TYR B 200 ? 0.7912 0.4678 0.7218 0.0439  0.1092  0.0074  1670 TYR B CE1 
3660 C  CE2 . TYR B 200 ? 0.7847 0.4606 0.7364 0.0590  0.0766  0.0020  1670 TYR B CE2 
3661 C  CZ  . TYR B 200 ? 0.8908 0.5727 0.8497 0.0514  0.0955  0.0046  1670 TYR B CZ  
3662 O  OH  . TYR B 200 ? 0.8384 0.5331 0.8332 0.0512  0.1005  0.0040  1670 TYR B OH  
3663 N  N   . GLU B 201 ? 0.9979 0.6831 0.8757 0.0468  0.1122  -0.0224 1671 GLU B N   
3664 C  CA  . GLU B 201 ? 1.0381 0.7403 0.9429 0.0495  0.1162  -0.0366 1671 GLU B CA  
3665 C  C   . GLU B 201 ? 1.0684 0.7799 1.0139 0.0540  0.1054  -0.0396 1671 GLU B C   
3666 O  O   . GLU B 201 ? 0.8795 0.5997 0.8424 0.0569  0.1016  -0.0512 1671 GLU B O   
3667 C  CB  . GLU B 201 ? 0.9185 0.6337 0.8326 0.0447  0.1381  -0.0395 1671 GLU B CB  
3668 C  CG  . GLU B 201 ? 1.0175 0.7379 0.9512 0.0397  0.1483  -0.0294 1671 GLU B CG  
3669 C  CD  . GLU B 201 ? 1.0336 0.7707 0.9813 0.0360  0.1683  -0.0343 1671 GLU B CD  
3670 O  OE1 . GLU B 201 ? 0.8750 0.6145 0.8001 0.0339  0.1793  -0.0394 1671 GLU B OE1 
3671 O  OE2 . GLU B 201 ? 1.0628 0.8112 1.0439 0.0354  0.1728  -0.0334 1671 GLU B OE2 
3672 N  N   . ALA B 202 ? 1.0361 0.7454 0.9961 0.0544  0.1003  -0.0299 1672 ALA B N   
3673 C  CA  . ALA B 202 ? 0.8735 0.5935 0.8710 0.0583  0.0909  -0.0329 1672 ALA B CA  
3674 C  C   . ALA B 202 ? 0.9341 0.6490 0.9286 0.0644  0.0697  -0.0344 1672 ALA B C   
3675 O  O   . ALA B 202 ? 0.8719 0.5978 0.8973 0.0674  0.0612  -0.0377 1672 ALA B O   
3676 C  CB  . ALA B 202 ? 0.8090 0.5320 0.8273 0.0566  0.0963  -0.0237 1672 ALA B CB  
3677 N  N   . SER B 203 ? 0.9813 0.6815 0.9400 0.0660  0.0609  -0.0325 1673 SER B N   
3678 C  CA  . SER B 203 ? 0.9632 0.6584 0.9189 0.0724  0.0394  -0.0327 1673 SER B CA  
3679 C  C   . SER B 203 ? 0.8609 0.5629 0.8188 0.0742  0.0301  -0.0460 1673 SER B C   
3680 O  O   . SER B 203 ? 0.9699 0.6680 0.9057 0.0716  0.0364  -0.0524 1673 SER B O   
3681 C  CB  . SER B 203 ? 0.8958 0.5691 0.8104 0.0738  0.0320  -0.0222 1673 SER B CB  
3682 O  OG  . SER B 203 ? 1.0462 0.7137 0.9454 0.0796  0.0118  -0.0262 1673 SER B OG  
3683 N  N   . LEU B 204 ? 0.8883 0.6010 0.8737 0.0782  0.0154  -0.0508 1674 LEU B N   
3684 C  CA  . LEU B 204 ? 0.9154 0.6349 0.9070 0.0787  0.0048  -0.0636 1674 LEU B CA  
3685 C  C   . LEU B 204 ? 0.9093 0.6154 0.8648 0.0821  -0.0110 -0.0654 1674 LEU B C   
3686 O  O   . LEU B 204 ? 1.0324 0.7379 0.9772 0.0810  -0.0155 -0.0763 1674 LEU B O   
3687 C  CB  . LEU B 204 ? 0.8809 0.6183 0.9150 0.0803  -0.0052 -0.0674 1674 LEU B CB  
3688 C  CG  . LEU B 204 ? 0.7906 0.5415 0.8602 0.0770  0.0089  -0.0650 1674 LEU B CG  
3689 C  CD1 . LEU B 204 ? 0.8650 0.6347 0.9737 0.0776  -0.0008 -0.0696 1674 LEU B CD1 
3690 C  CD2 . LEU B 204 ? 0.8109 0.5625 0.8812 0.0715  0.0257  -0.0703 1674 LEU B CD2 
3691 N  N   . VAL B 205 ? 0.9798 0.6736 0.9147 0.0865  -0.0204 -0.0551 1675 VAL B N   
3692 C  CA  . VAL B 205 ? 1.1506 0.8299 1.0479 0.0901  -0.0366 -0.0552 1675 VAL B CA  
3693 C  C   . VAL B 205 ? 1.1645 0.8256 1.0163 0.0860  -0.0235 -0.0491 1675 VAL B C   
3694 O  O   . VAL B 205 ? 1.0740 0.7262 0.9164 0.0838  -0.0126 -0.0370 1675 VAL B O   
3695 C  CB  . VAL B 205 ? 1.2032 0.8779 1.1020 0.0981  -0.0561 -0.0473 1675 VAL B CB  
3696 C  CG1 . VAL B 205 ? 1.2671 0.9268 1.1266 0.1023  -0.0750 -0.0477 1675 VAL B CG1 
3697 C  CG2 . VAL B 205 ? 1.1914 0.8887 1.1394 0.1017  -0.0661 -0.0535 1675 VAL B CG2 
3698 N  N   . ALA B 206 ? 1.3112 0.9673 1.1353 0.0842  -0.0238 -0.0580 1676 ALA B N   
3699 C  CA  . ALA B 206 ? 1.5575 1.1974 1.3341 0.0804  -0.0128 -0.0531 1676 ALA B CA  
3700 C  C   . ALA B 206 ? 1.7736 1.3937 1.5117 0.0843  -0.0302 -0.0433 1676 ALA B C   
3701 O  O   . ALA B 206 ? 1.8186 1.4362 1.5464 0.0892  -0.0505 -0.0495 1676 ALA B O   
3702 C  CB  . ALA B 206 ? 1.6062 1.2488 1.3674 0.0778  -0.0058 -0.0678 1676 ALA B CB  
3703 N  N   . ALA B 207 ? 1.9166 1.5222 1.6351 0.0822  -0.0235 -0.0276 1677 ALA B N   
3704 C  CA  . ALA B 207 ? 2.0111 1.5941 1.6920 0.0860  -0.0402 -0.0157 1677 ALA B CA  
3705 C  C   . ALA B 207 ? 2.0379 1.6088 1.6704 0.0856  -0.0481 -0.0204 1677 ALA B C   
3706 O  O   . ALA B 207 ? 2.0541 1.6139 1.6672 0.0921  -0.0712 -0.0185 1677 ALA B O   
3707 C  CB  . ALA B 207 ? 2.0456 1.6122 1.7081 0.0808  -0.0276 0.0017  1677 ALA B CB  
3708 N  N   . SER B 208 ? 2.0154 1.5887 1.6274 0.0788  -0.0295 -0.0271 1678 SER B N   
3709 C  CA  . SER B 208 ? 1.9674 1.5303 1.5320 0.0782  -0.0350 -0.0333 1678 SER B CA  
3710 C  C   . SER B 208 ? 2.0103 1.5809 1.5876 0.0851  -0.0573 -0.0482 1678 SER B C   
3711 O  O   . SER B 208 ? 2.0592 1.6180 1.6153 0.0907  -0.0807 -0.0450 1678 SER B O   
3712 C  CB  . SER B 208 ? 1.8684 1.4374 1.4169 0.0707  -0.0092 -0.0409 1678 SER B CB  
3713 O  OG  . SER B 208 ? 1.7920 1.3826 1.3833 0.0712  -0.0003 -0.0563 1678 SER B OG  
3714 N  N   . THR B 209 ? 1.9939 1.5836 1.6056 0.0845  -0.0514 -0.0643 1679 THR B N   
3715 C  CA  . THR B 209 ? 2.0054 1.6026 1.6305 0.0891  -0.0720 -0.0791 1679 THR B CA  
3716 C  C   . THR B 209 ? 2.0104 1.6144 1.6699 0.0955  -0.0937 -0.0748 1679 THR B C   
3717 O  O   . THR B 209 ? 2.0620 1.6577 1.7029 0.1010  -0.1170 -0.0733 1679 THR B O   
3718 C  CB  . THR B 209 ? 1.9558 1.5693 1.6106 0.0862  -0.0603 -0.0965 1679 THR B CB  
3719 O  OG1 . THR B 209 ? 1.9495 1.5721 1.6288 0.0893  -0.0809 -0.1092 1679 THR B OG1 
3720 C  CG2 . THR B 209 ? 1.8673 1.4945 1.5641 0.0831  -0.0403 -0.0928 1679 THR B CG2 
3721 N  N   . GLY B 210 ? 1.9621 1.5816 1.6707 0.0953  -0.0863 -0.0729 1680 GLY B N   
3722 C  CA  . GLY B 210 ? 1.8439 1.4742 1.5892 0.1014  -0.1049 -0.0710 1680 GLY B CA  
3723 C  C   . GLY B 210 ? 1.6819 1.3346 1.4731 0.1001  -0.1088 -0.0859 1680 GLY B C   
3724 O  O   . GLY B 210 ? 1.6261 1.2902 1.4426 0.1046  -0.1286 -0.0895 1680 GLY B O   
3725 N  N   . VAL B 211 ? 1.6166 1.2760 1.4193 0.0939  -0.0903 -0.0945 1681 VAL B N   
3726 C  CA  . VAL B 211 ? 1.4909 1.1693 1.3383 0.0910  -0.0904 -0.1068 1681 VAL B CA  
3727 C  C   . VAL B 211 ? 1.4749 1.1655 1.3611 0.0888  -0.0737 -0.1000 1681 VAL B C   
3728 O  O   . VAL B 211 ? 1.5102 1.1946 1.3855 0.0865  -0.0542 -0.0925 1681 VAL B O   
3729 C  CB  . VAL B 211 ? 1.4215 1.0969 1.2560 0.0864  -0.0827 -0.1216 1681 VAL B CB  
3730 C  CG1 . VAL B 211 ? 1.3934 1.0619 1.2024 0.0882  -0.1039 -0.1323 1681 VAL B CG1 
3731 C  CG2 . VAL B 211 ? 1.3756 1.0397 1.1788 0.0840  -0.0597 -0.1181 1681 VAL B CG2 
3732 N  N   . ARG B 212 ? 1.4372 1.1458 1.3680 0.0892  -0.0816 -0.1023 1682 ARG B N   
3733 C  CA  . ARG B 212 ? 1.3746 1.0960 1.3432 0.0869  -0.0668 -0.0971 1682 ARG B CA  
3734 C  C   . ARG B 212 ? 1.3215 1.0491 1.3075 0.0802  -0.0532 -0.1070 1682 ARG B C   
3735 O  O   . ARG B 212 ? 1.3628 1.0994 1.3690 0.0773  -0.0623 -0.1180 1682 ARG B O   
3736 C  CB  . ARG B 212 ? 1.3358 1.0751 1.3434 0.0901  -0.0800 -0.0954 1682 ARG B CB  
3737 N  N   . ALA B 213 ? 1.1531 0.8756 1.1315 0.0777  -0.0322 -0.1033 1683 ALA B N   
3738 C  CA  . ALA B 213 ? 1.0460 0.7739 1.0431 0.0728  -0.0191 -0.1117 1683 ALA B CA  
3739 C  C   . ALA B 213 ? 0.9461 0.6910 0.9901 0.0703  -0.0163 -0.1091 1683 ALA B C   
3740 O  O   . ALA B 213 ? 0.8425 0.5944 0.9014 0.0725  -0.0175 -0.0994 1683 ALA B O   
3741 C  CB  . ALA B 213 ? 0.9213 0.6409 0.8971 0.0718  0.0021  -0.1090 1683 ALA B CB  
3742 N  N   . LEU B 214 ? 0.7836 0.5341 0.8498 0.0656  -0.0133 -0.1182 1684 LEU B N   
3743 C  CA  . LEU B 214 ? 0.8219 0.5877 0.9299 0.0619  -0.0092 -0.1156 1684 LEU B CA  
3744 C  C   . LEU B 214 ? 0.9570 0.7237 1.0711 0.0616  0.0106  -0.1070 1684 LEU B C   
3745 O  O   . LEU B 214 ? 0.9043 0.6615 0.9975 0.0623  0.0232  -0.1076 1684 LEU B O   
3746 C  CB  . LEU B 214 ? 0.8300 0.5982 0.9572 0.0560  -0.0124 -0.1269 1684 LEU B CB  
3747 C  CG  . LEU B 214 ? 0.9380 0.7102 1.0707 0.0539  -0.0331 -0.1355 1684 LEU B CG  
3748 C  CD1 . LEU B 214 ? 0.9728 0.7433 1.1220 0.0466  -0.0351 -0.1465 1684 LEU B CD1 
3749 C  CD2 . LEU B 214 ? 0.9601 0.7507 1.1196 0.0544  -0.0427 -0.1291 1684 LEU B CD2 
3750 N  N   . PRO B 215 ? 0.9482 0.7278 1.0912 0.0607  0.0137  -0.0995 1685 PRO B N   
3751 C  CA  . PRO B 215 ? 0.6421 0.4234 0.7928 0.0599  0.0314  -0.0920 1685 PRO B CA  
3752 C  C   . PRO B 215 ? 0.7194 0.5050 0.8920 0.0551  0.0404  -0.0966 1685 PRO B C   
3753 O  O   . PRO B 215 ? 0.7607 0.5546 0.9579 0.0511  0.0333  -0.1008 1685 PRO B O   
3754 C  CB  . PRO B 215 ? 0.8655 0.6581 1.0361 0.0616  0.0286  -0.0831 1685 PRO B CB  
3755 C  CG  . PRO B 215 ? 0.8796 0.6838 1.0707 0.0606  0.0124  -0.0887 1685 PRO B CG  
3756 C  CD  . PRO B 215 ? 0.8506 0.6449 1.0192 0.0610  0.0010  -0.0977 1685 PRO B CD  
3757 N  N   . CYS B 216 ? 0.6213 0.4015 0.7858 0.0553  0.0555  -0.0959 1686 CYS B N   
3758 C  CA  . CYS B 216 ? 0.6058 0.3882 0.7902 0.0521  0.0631  -0.0998 1686 CYS B CA  
3759 C  C   . CYS B 216 ? 0.6526 0.4483 0.8692 0.0487  0.0650  -0.0928 1686 CYS B C   
3760 O  O   . CYS B 216 ? 0.5708 0.3727 0.7911 0.0500  0.0695  -0.0838 1686 CYS B O   
3761 C  CB  . CYS B 216 ? 0.6085 0.3858 0.7801 0.0543  0.0789  -0.0996 1686 CYS B CB  
3762 S  SG  . CYS B 216 ? 0.6689 0.4486 0.8654 0.0523  0.0881  -0.1026 1686 CYS B SG  
3763 N  N   . LEU B 217 ? 0.5983 0.3975 0.8369 0.0438  0.0614  -0.0969 1687 LEU B N   
3764 C  CA  . LEU B 217 ? 0.5392 0.3515 0.8069 0.0395  0.0638  -0.0905 1687 LEU B CA  
3765 C  C   . LEU B 217 ? 0.5218 0.3356 0.7949 0.0403  0.0785  -0.0840 1687 LEU B C   
3766 O  O   . LEU B 217 ? 0.5005 0.3252 0.7936 0.0376  0.0819  -0.0775 1687 LEU B O   
3767 C  CB  . LEU B 217 ? 0.5378 0.3514 0.8251 0.0324  0.0572  -0.0959 1687 LEU B CB  
3768 C  CG  . LEU B 217 ? 0.6318 0.4552 0.9308 0.0285  0.0428  -0.0988 1687 LEU B CG  
3769 C  CD1 . LEU B 217 ? 0.7359 0.5546 1.0461 0.0207  0.0356  -0.1062 1687 LEU B CD1 
3770 C  CD2 . LEU B 217 ? 0.6953 0.5377 1.0167 0.0269  0.0441  -0.0910 1687 LEU B CD2 
3771 N  N   . ILE B 218 ? 0.5314 0.3358 0.7878 0.0437  0.0873  -0.0862 1688 ILE B N   
3772 C  CA  . ILE B 218 ? 0.5411 0.3481 0.8040 0.0445  0.1006  -0.0812 1688 ILE B CA  
3773 C  C   . ILE B 218 ? 0.5185 0.3284 0.7696 0.0472  0.1080  -0.0738 1688 ILE B C   
3774 O  O   . ILE B 218 ? 0.4959 0.3137 0.7602 0.0460  0.1141  -0.0664 1688 ILE B O   
3775 C  CB  . ILE B 218 ? 0.5281 0.3257 0.7840 0.0469  0.1064  -0.0887 1688 ILE B CB  
3776 C  CG1 . ILE B 218 ? 0.5658 0.3567 0.8333 0.0437  0.0982  -0.0958 1688 ILE B CG1 
3777 C  CG2 . ILE B 218 ? 0.5131 0.3155 0.7775 0.0483  0.1192  -0.0839 1688 ILE B CG2 
3778 C  CD1 . ILE B 218 ? 0.5136 0.3111 0.8073 0.0380  0.0974  -0.0898 1688 ILE B CD1 
3779 N  N   . THR B 219 ? 0.5343 0.3370 0.7596 0.0503  0.1070  -0.0754 1689 THR B N   
3780 C  CA  . THR B 219 ? 0.6240 0.4261 0.8345 0.0516  0.1143  -0.0679 1689 THR B CA  
3781 C  C   . THR B 219 ? 0.6816 0.4808 0.8800 0.0531  0.1049  -0.0633 1689 THR B C   
3782 O  O   . THR B 219 ? 0.5856 0.3828 0.7744 0.0535  0.1095  -0.0556 1689 THR B O   
3783 C  CB  . THR B 219 ? 0.5569 0.3523 0.7434 0.0534  0.1235  -0.0716 1689 THR B CB  
3784 O  OG1 . THR B 219 ? 0.6291 0.4152 0.7917 0.0553  0.1151  -0.0772 1689 THR B OG1 
3785 C  CG2 . THR B 219 ? 0.5517 0.3494 0.7488 0.0542  0.1317  -0.0783 1689 THR B CG2 
3786 N  N   . GLY B 220 ? 0.6227 0.4209 0.8209 0.0539  0.0911  -0.0679 1690 GLY B N   
3787 C  CA  . GLY B 220 ? 0.6974 0.4924 0.8833 0.0568  0.0801  -0.0646 1690 GLY B CA  
3788 C  C   . GLY B 220 ? 0.8148 0.5962 0.9652 0.0592  0.0770  -0.0662 1690 GLY B C   
3789 O  O   . GLY B 220 ? 0.7032 0.4803 0.8420 0.0622  0.0642  -0.0653 1690 GLY B O   
3790 N  N   . TYR B 221 ? 0.6653 0.4407 0.7982 0.0584  0.0882  -0.0688 1691 TYR B N   
3791 C  CA  . TYR B 221 ? 0.6473 0.4104 0.7438 0.0599  0.0876  -0.0700 1691 TYR B CA  
3792 C  C   . TYR B 221 ? 0.6682 0.4263 0.7536 0.0617  0.0737  -0.0798 1691 TYR B C   
3793 O  O   . TYR B 221 ? 0.7406 0.5040 0.8462 0.0607  0.0683  -0.0877 1691 TYR B O   
3794 C  CB  . TYR B 221 ? 0.6531 0.4153 0.7378 0.0584  0.1044  -0.0724 1691 TYR B CB  
3795 C  CG  . TYR B 221 ? 0.6999 0.4614 0.7761 0.0560  0.1159  -0.0617 1691 TYR B CG  
3796 C  CD1 . TYR B 221 ? 0.6503 0.4162 0.7457 0.0549  0.1156  -0.0525 1691 TYR B CD1 
3797 C  CD2 . TYR B 221 ? 0.7624 0.5189 0.8109 0.0543  0.1271  -0.0609 1691 TYR B CD2 
3798 C  CE1 . TYR B 221 ? 0.6467 0.4099 0.7338 0.0519  0.1253  -0.0427 1691 TYR B CE1 
3799 C  CE2 . TYR B 221 ? 0.7446 0.5001 0.7853 0.0503  0.1376  -0.0506 1691 TYR B CE2 
3800 C  CZ  . TYR B 221 ? 0.6828 0.4407 0.7430 0.0490  0.1360  -0.0414 1691 TYR B CZ  
3801 O  OH  . TYR B 221 ? 0.7865 0.5418 0.8389 0.0442  0.1459  -0.0317 1691 TYR B OH  
3802 N  N   . PRO B 222 ? 0.7006 0.4473 0.7523 0.0637  0.0676  -0.0795 1692 PRO B N   
3803 C  CA  . PRO B 222 ? 0.7242 0.4654 0.7618 0.0652  0.0547  -0.0902 1692 PRO B CA  
3804 C  C   . PRO B 222 ? 0.8848 0.6253 0.9219 0.0643  0.0629  -0.1022 1692 PRO B C   
3805 O  O   . PRO B 222 ? 0.8183 0.5579 0.8450 0.0640  0.0787  -0.1026 1692 PRO B O   
3806 C  CB  . PRO B 222 ? 0.7608 0.4886 0.7571 0.0672  0.0503  -0.0858 1692 PRO B CB  
3807 C  CG  . PRO B 222 ? 0.7596 0.4849 0.7444 0.0650  0.0677  -0.0757 1692 PRO B CG  
3808 C  CD  . PRO B 222 ? 0.7553 0.4923 0.7776 0.0638  0.0724  -0.0695 1692 PRO B CD  
3809 N  N   . ILE B 223 ? 0.8250 0.5664 0.8753 0.0638  0.0519  -0.1125 1693 ILE B N   
3810 C  CA  . ILE B 223 ? 0.8201 0.5568 0.8677 0.0639  0.0559  -0.1256 1693 ILE B CA  
3811 C  C   . ILE B 223 ? 0.8971 0.6220 0.9037 0.0666  0.0529  -0.1328 1693 ILE B C   
3812 O  O   . ILE B 223 ? 0.9860 0.7056 0.9797 0.0671  0.0365  -0.1368 1693 ILE B O   
3813 C  CB  . ILE B 223 ? 0.8028 0.5421 0.8774 0.0611  0.0439  -0.1334 1693 ILE B CB  
3814 C  CG1 . ILE B 223 ? 0.7009 0.4527 0.8133 0.0578  0.0477  -0.1251 1693 ILE B CG1 
3815 C  CG2 . ILE B 223 ? 1.0753 0.8056 1.1444 0.0619  0.0464  -0.1477 1693 ILE B CG2 
3816 C  CD1 . ILE B 223 ? 0.7958 0.5504 0.9356 0.0532  0.0388  -0.1314 1693 ILE B CD1 
3817 N  N   . LEU B 224 ? 0.9637 0.6856 0.9497 0.0683  0.0686  -0.1351 1694 LEU B N   
3818 C  CA  . LEU B 224 ? 1.0294 0.7409 0.9737 0.0705  0.0682  -0.1422 1694 LEU B CA  
3819 C  C   . LEU B 224 ? 1.0819 0.7882 1.0206 0.0731  0.0705  -0.1598 1694 LEU B C   
3820 O  O   . LEU B 224 ? 0.9196 0.6163 0.8263 0.0751  0.0645  -0.1692 1694 LEU B O   
3821 C  CB  . LEU B 224 ? 0.9288 0.6409 0.8484 0.0699  0.0846  -0.1330 1694 LEU B CB  
3822 C  CG  . LEU B 224 ? 0.9973 0.7099 0.9164 0.0675  0.0820  -0.1156 1694 LEU B CG  
3823 C  CD1 . LEU B 224 ? 1.1124 0.8210 0.9979 0.0655  0.0958  -0.1080 1694 LEU B CD1 
3824 C  CD2 . LEU B 224 ? 0.8454 0.5516 0.7590 0.0687  0.0597  -0.1133 1694 LEU B CD2 
3825 N  N   . ARG B 225 ? 1.1186 0.8300 1.0866 0.0737  0.0782  -0.1646 1695 ARG B N   
3826 C  CA  . ARG B 225 ? 1.2281 0.9327 1.1939 0.0773  0.0798  -0.1816 1695 ARG B CA  
3827 C  C   . ARG B 225 ? 1.1615 0.8691 1.1679 0.0763  0.0794  -0.1829 1695 ARG B C   
3828 O  O   . ARG B 225 ? 0.8799 0.5974 0.9124 0.0734  0.0834  -0.1706 1695 ARG B O   
3829 C  CB  . ARG B 225 ? 1.3002 1.0066 1.2427 0.0817  0.0985  -0.1872 1695 ARG B CB  
3830 C  CG  . ARG B 225 ? 1.3003 1.0204 1.2619 0.0816  0.1169  -0.1776 1695 ARG B CG  
3831 C  CD  . ARG B 225 ? 1.4752 1.1983 1.4420 0.0877  0.1304  -0.1907 1695 ARG B CD  
3832 N  NE  . ARG B 225 ? 1.6360 1.3517 1.5679 0.0922  0.1323  -0.2057 1695 ARG B NE  
3833 C  CZ  . ARG B 225 ? 1.6547 1.3698 1.5856 0.0994  0.1406  -0.2217 1695 ARG B CZ  
3834 N  NH1 . ARG B 225 ? 1.6567 1.3652 1.5531 0.1035  0.1422  -0.2357 1695 ARG B NH1 
3835 N  NH2 . ARG B 225 ? 1.5723 1.2928 1.5359 0.1032  0.1468  -0.2242 1695 ARG B NH2 
3836 N  N   . ASN B 226 ? 1.0755 0.7729 1.0854 0.0785  0.0741  -0.1980 1696 ASN B N   
3837 C  CA  . ASN B 226 ? 0.8813 0.5776 0.9256 0.0777  0.0740  -0.2000 1696 ASN B CA  
3838 C  C   . ASN B 226 ? 0.8354 0.5364 0.9082 0.0701  0.0622  -0.1897 1696 ASN B C   
3839 O  O   . ASN B 226 ? 0.8391 0.5464 0.9410 0.0679  0.0667  -0.1822 1696 ASN B O   
3840 C  CB  . ASN B 226 ? 0.8988 0.6046 0.9567 0.0817  0.0926  -0.1957 1696 ASN B CB  
3841 C  CG  . ASN B 226 ? 1.2413 0.9407 1.2877 0.0900  0.1015  -0.2114 1696 ASN B CG  
3842 O  OD1 . ASN B 226 ? 1.3457 1.0443 1.3612 0.0940  0.1074  -0.2189 1696 ASN B OD1 
3843 N  ND2 . ASN B 226 ? 1.2269 0.9214 1.2975 0.0929  0.1022  -0.2167 1696 ASN B ND2 
3844 N  N   . LYS B 227 ? 1.0663 0.7655 1.1307 0.0663  0.0468  -0.1897 1697 LYS B N   
3845 C  CA  . LYS B 227 ? 1.1133 0.8205 1.2051 0.0592  0.0357  -0.1811 1697 LYS B CA  
3846 C  C   . LYS B 227 ? 1.0306 0.7311 1.1485 0.0545  0.0292  -0.1874 1697 LYS B C   
3847 O  O   . LYS B 227 ? 1.1136 0.7992 1.2217 0.0555  0.0233  -0.2015 1697 LYS B O   
3848 C  CB  . LYS B 227 ? 1.2010 0.9087 1.2778 0.0572  0.0195  -0.1815 1697 LYS B CB  
3849 C  CG  . LYS B 227 ? 1.1908 0.9094 1.2963 0.0504  0.0066  -0.1749 1697 LYS B CG  
3850 C  CD  . LYS B 227 ? 1.2166 0.9411 1.3070 0.0517  -0.0045 -0.1699 1697 LYS B CD  
3851 C  CE  . LYS B 227 ? 1.2599 0.9773 1.3373 0.0499  -0.0237 -0.1818 1697 LYS B CE  
3852 N  NZ  . LYS B 227 ? 1.2503 0.9742 1.3156 0.0518  -0.0367 -0.1764 1697 LYS B NZ  
3853 N  N   . ILE B 228 ? 0.8327 0.5427 0.9822 0.0493  0.0309  -0.1772 1698 ILE B N   
3854 C  CA  . ILE B 228 ? 0.8397 0.5441 1.0141 0.0420  0.0225  -0.1805 1698 ILE B CA  
3855 C  C   . ILE B 228 ? 0.8879 0.6071 1.0842 0.0336  0.0127  -0.1718 1698 ILE B C   
3856 O  O   . ILE B 228 ? 0.7416 0.4765 0.9462 0.0340  0.0182  -0.1597 1698 ILE B O   
3857 C  CB  . ILE B 228 ? 0.9170 0.6173 1.1096 0.0429  0.0336  -0.1776 1698 ILE B CB  
3858 C  CG1 . ILE B 228 ? 0.8275 0.5448 1.0393 0.0416  0.0438  -0.1619 1698 ILE B CG1 
3859 C  CG2 . ILE B 228 ? 0.9245 0.6140 1.0969 0.0531  0.0441  -0.1871 1698 ILE B CG2 
3860 C  CD1 . ILE B 228 ? 0.7247 0.4378 0.9558 0.0415  0.0518  -0.1587 1698 ILE B CD1 
3861 N  N   . GLU B 229 ? 0.8737 0.5882 1.0793 0.0259  -0.0021 -0.1788 1699 GLU B N   
3862 C  CA  . GLU B 229 ? 0.9428 0.6732 1.1670 0.0181  -0.0138 -0.1740 1699 GLU B CA  
3863 C  C   . GLU B 229 ? 0.8129 0.5473 1.0702 0.0070  -0.0155 -0.1700 1699 GLU B C   
3864 O  O   . GLU B 229 ? 0.8696 0.5871 1.1308 0.0029  -0.0167 -0.1762 1699 GLU B O   
3865 C  CB  . GLU B 229 ? 0.9403 0.6660 1.1490 0.0167  -0.0311 -0.1853 1699 GLU B CB  
3866 C  CG  . GLU B 229 ? 1.1411 0.8779 1.3327 0.0228  -0.0353 -0.1813 1699 GLU B CG  
3867 C  CD  . GLU B 229 ? 1.3100 1.0353 1.4714 0.0258  -0.0482 -0.1936 1699 GLU B CD  
3868 O  OE1 . GLU B 229 ? 1.1841 0.8940 1.3404 0.0225  -0.0551 -0.2064 1699 GLU B OE1 
3869 O  OE2 . GLU B 229 ? 1.3932 1.1236 1.5350 0.0316  -0.0521 -0.1904 1699 GLU B OE2 
3870 N  N   . PHE B 230 ? 0.7568 0.5126 1.0369 0.0021  -0.0154 -0.1596 1700 PHE B N   
3871 C  CA  . PHE B 230 ? 0.9572 0.7204 1.2683 -0.0098 -0.0166 -0.1548 1700 PHE B CA  
3872 C  C   . PHE B 230 ? 0.8954 0.6667 1.2195 -0.0200 -0.0335 -0.1610 1700 PHE B C   
3873 O  O   . PHE B 230 ? 0.8841 0.6593 1.1955 -0.0164 -0.0444 -0.1672 1700 PHE B O   
3874 C  CB  . PHE B 230 ? 0.8819 0.6651 1.2109 -0.0095 -0.0053 -0.1409 1700 PHE B CB  
3875 C  CG  . PHE B 230 ? 0.9262 0.7017 1.2456 -0.0014 0.0106  -0.1351 1700 PHE B CG  
3876 C  CD1 . PHE B 230 ? 0.8321 0.6065 1.1289 0.0100  0.0170  -0.1344 1700 PHE B CD1 
3877 C  CD2 . PHE B 230 ? 0.8902 0.6591 1.2227 -0.0056 0.0184  -0.1303 1700 PHE B CD2 
3878 C  CE1 . PHE B 230 ? 0.8789 0.6484 1.1689 0.0164  0.0313  -0.1298 1700 PHE B CE1 
3879 C  CE2 . PHE B 230 ? 0.7783 0.5418 1.1037 0.0021  0.0317  -0.1256 1700 PHE B CE2 
3880 C  CZ  . PHE B 230 ? 0.7503 0.5153 1.0556 0.0129  0.0383  -0.1258 1700 PHE B CZ  
3881 N  N   . LYS B 231 ? 1.0130 0.7869 1.3624 -0.0334 -0.0362 -0.1591 1701 LYS B N   
3882 C  CA  . LYS B 231 ? 1.0772 0.8583 1.4406 -0.0449 -0.0523 -0.1660 1701 LYS B CA  
3883 C  C   . LYS B 231 ? 1.1437 0.9553 1.5200 -0.0438 -0.0582 -0.1628 1701 LYS B C   
3884 O  O   . LYS B 231 ? 1.2431 1.0609 1.6194 -0.0464 -0.0736 -0.1711 1701 LYS B O   
3885 C  CB  . LYS B 231 ? 0.8782 0.6567 1.2667 -0.0612 -0.0527 -0.1630 1701 LYS B CB  
3886 N  N   . ARG B 232 ? 1.1984 1.0286 1.5851 -0.0392 -0.0470 -0.1516 1702 ARG B N   
3887 C  CA  . ARG B 232 ? 1.2155 1.0722 1.6115 -0.0345 -0.0521 -0.1490 1702 ARG B CA  
3888 C  C   . ARG B 232 ? 1.2562 1.1043 1.6212 -0.0209 -0.0583 -0.1537 1702 ARG B C   
3889 O  O   . ARG B 232 ? 1.2833 1.1116 1.6215 -0.0122 -0.0500 -0.1534 1702 ARG B O   
3890 C  CB  . ARG B 232 ? 1.2933 1.1680 1.7045 -0.0315 -0.0379 -0.1367 1702 ARG B CB  
3891 N  N   . PRO B 233 ? 1.3067 1.1696 1.6744 -0.0189 -0.0730 -0.1580 1703 PRO B N   
3892 C  CA  . PRO B 233 ? 1.2963 1.1498 1.6320 -0.0065 -0.0803 -0.1616 1703 PRO B CA  
3893 C  C   . PRO B 233 ? 1.1633 1.0197 1.4872 0.0057  -0.0695 -0.1513 1703 PRO B C   
3894 O  O   . PRO B 233 ? 1.0571 0.9316 1.4030 0.0060  -0.0617 -0.1427 1703 PRO B O   
3895 C  CB  . PRO B 233 ? 1.3543 1.2264 1.7028 -0.0089 -0.1002 -0.1679 1703 PRO B CB  
3896 C  CG  . PRO B 233 ? 1.3548 1.2553 1.7455 -0.0182 -0.0980 -0.1632 1703 PRO B CG  
3897 C  CD  . PRO B 233 ? 1.3654 1.2554 1.7661 -0.0284 -0.0841 -0.1599 1703 PRO B CD  
3898 N  N   . GLY B 234 ? 1.1316 0.9695 1.4191 0.0155  -0.0687 -0.1526 1704 GLY B N   
3899 C  CA  . GLY B 234 ? 1.0384 0.8753 1.3104 0.0261  -0.0593 -0.1429 1704 GLY B CA  
3900 C  C   . GLY B 234 ? 1.0608 0.8922 1.3350 0.0265  -0.0390 -0.1350 1704 GLY B C   
3901 O  O   . GLY B 234 ? 1.0860 0.9188 1.3524 0.0336  -0.0304 -0.1262 1704 GLY B O   
3902 N  N   . LYS B 235 ? 0.9228 0.7472 1.2071 0.0190  -0.0318 -0.1377 1705 LYS B N   
3903 C  CA  . LYS B 235 ? 0.8583 0.6795 1.1487 0.0188  -0.0141 -0.1304 1705 LYS B CA  
3904 C  C   . LYS B 235 ? 0.8052 0.6034 1.0717 0.0213  -0.0072 -0.1360 1705 LYS B C   
3905 O  O   . LYS B 235 ? 0.9163 0.7034 1.1830 0.0160  -0.0128 -0.1451 1705 LYS B O   
3906 C  CB  . LYS B 235 ? 0.8270 0.6606 1.1517 0.0083  -0.0113 -0.1274 1705 LYS B CB  
3907 C  CG  . LYS B 235 ? 0.8399 0.7000 1.1909 0.0064  -0.0146 -0.1217 1705 LYS B CG  
3908 C  CD  . LYS B 235 ? 0.8841 0.7501 1.2285 0.0163  -0.0059 -0.1128 1705 LYS B CD  
3909 C  CE  . LYS B 235 ? 1.0257 0.9171 1.3930 0.0175  -0.0114 -0.1094 1705 LYS B CE  
3910 N  NZ  . LYS B 235 ? 0.8972 0.7887 1.2505 0.0293  -0.0091 -0.1032 1705 LYS B NZ  
3911 N  N   . ALA B 236 ? 0.7798 0.5715 1.0268 0.0291  0.0048  -0.1312 1706 ALA B N   
3912 C  CA  . ALA B 236 ? 0.7138 0.4872 0.9381 0.0330  0.0128  -0.1371 1706 ALA B CA  
3913 C  C   . ALA B 236 ? 0.7196 0.4936 0.9411 0.0375  0.0303  -0.1287 1706 ALA B C   
3914 O  O   . ALA B 236 ? 0.6999 0.4855 0.9296 0.0388  0.0353  -0.1185 1706 ALA B O   
3915 C  CB  . ALA B 236 ? 0.7449 0.5073 0.9353 0.0384  0.0054  -0.1449 1706 ALA B CB  
3916 N  N   . ALA B 237 ? 0.7778 0.5393 0.9881 0.0403  0.0390  -0.1341 1707 ALA B N   
3917 C  CA  . ALA B 237 ? 0.6764 0.4385 0.8820 0.0450  0.0553  -0.1283 1707 ALA B CA  
3918 C  C   . ALA B 237 ? 0.8039 0.5536 0.9811 0.0510  0.0608  -0.1373 1707 ALA B C   
3919 O  O   . ALA B 237 ? 0.9180 0.6564 1.0821 0.0515  0.0525  -0.1489 1707 ALA B O   
3920 C  CB  . ALA B 237 ? 0.6322 0.3966 0.8631 0.0419  0.0630  -0.1246 1707 ALA B CB  
3921 N  N   . ASN B 238 ? 0.8084 0.5610 0.9751 0.0554  0.0747  -0.1323 1708 ASN B N   
3922 C  CA  . ASN B 238 ? 0.6679 0.4126 0.8131 0.0609  0.0837  -0.1409 1708 ASN B CA  
3923 C  C   . ASN B 238 ? 0.6595 0.4012 0.8233 0.0623  0.0901  -0.1456 1708 ASN B C   
3924 O  O   . ASN B 238 ? 0.6608 0.4105 0.8475 0.0605  0.0960  -0.1370 1708 ASN B O   
3925 C  CB  . ASN B 238 ? 0.8345 0.5852 0.9621 0.0637  0.0966  -0.1336 1708 ASN B CB  
3926 C  CG  . ASN B 238 ? 0.8042 0.5526 0.9176 0.0690  0.1099  -0.1416 1708 ASN B CG  
3927 O  OD1 . ASN B 238 ? 0.7358 0.4901 0.8656 0.0707  0.1208  -0.1403 1708 ASN B OD1 
3928 N  ND2 . ASN B 238 ? 0.7397 0.4802 0.8225 0.0720  0.1088  -0.1506 1708 ASN B ND2 
3929 N  N   . LYS B 239 ? 0.8486 0.5776 1.0027 0.0658  0.0875  -0.1594 1709 LYS B N   
3930 C  CA  . LYS B 239 ? 0.8533 0.5757 1.0253 0.0679  0.0904  -0.1647 1709 LYS B CA  
3931 C  C   . LYS B 239 ? 0.7697 0.5015 0.9497 0.0728  0.1064  -0.1598 1709 LYS B C   
3932 O  O   . LYS B 239 ? 0.6488 0.3805 0.8516 0.0727  0.1082  -0.1569 1709 LYS B O   
3933 C  CB  . LYS B 239 ? 0.7640 0.4696 0.9208 0.0726  0.0854  -0.1818 1709 LYS B CB  
3934 C  CG  . LYS B 239 ? 0.8190 0.5129 0.9951 0.0742  0.0837  -0.1874 1709 LYS B CG  
3935 C  CD  . LYS B 239 ? 0.9892 0.6641 1.1486 0.0792  0.0774  -0.2056 1709 LYS B CD  
3936 C  CE  . LYS B 239 ? 0.9331 0.5927 1.1100 0.0818  0.0748  -0.2116 1709 LYS B CE  
3937 N  NZ  . LYS B 239 ? 0.9539 0.5966 1.1124 0.0908  0.0734  -0.2309 1709 LYS B NZ  
3938 N  N   . ASP B 240 ? 0.8103 0.5507 0.9721 0.0764  0.1177  -0.1585 1710 ASP B N   
3939 C  CA  . ASP B 240 ? 0.6543 0.4064 0.8254 0.0803  0.1329  -0.1544 1710 ASP B CA  
3940 C  C   . ASP B 240 ? 0.6591 0.4224 0.8524 0.0749  0.1349  -0.1390 1710 ASP B C   
3941 O  O   . ASP B 240 ? 0.6120 0.3805 0.8254 0.0765  0.1406  -0.1361 1710 ASP B O   
3942 C  CB  . ASP B 240 ? 0.7874 0.5465 0.9329 0.0836  0.1449  -0.1566 1710 ASP B CB  
3943 C  CG  . ASP B 240 ? 0.9588 0.7108 1.0874 0.0914  0.1484  -0.1735 1710 ASP B CG  
3944 O  OD1 . ASP B 240 ? 1.0920 0.8378 1.2354 0.0968  0.1473  -0.1824 1710 ASP B OD1 
3945 O  OD2 . ASP B 240 ? 1.0175 0.7689 1.1169 0.0923  0.1516  -0.1782 1710 ASP B OD2 
3946 N  N   . ASN B 241 ? 0.6865 0.4535 0.8765 0.0690  0.1293  -0.1297 1711 ASN B N   
3947 C  CA  . ASN B 241 ? 0.6463 0.4230 0.8576 0.0642  0.1298  -0.1166 1711 ASN B CA  
3948 C  C   . ASN B 241 ? 0.5710 0.3440 0.8072 0.0613  0.1227  -0.1162 1711 ASN B C   
3949 O  O   . ASN B 241 ? 0.6040 0.3839 0.8595 0.0600  0.1274  -0.1089 1711 ASN B O   
3950 C  CB  . ASN B 241 ? 0.7401 0.5196 0.9437 0.0598  0.1230  -0.1088 1711 ASN B CB  
3951 C  CG  . ASN B 241 ? 0.7672 0.5474 0.9439 0.0615  0.1288  -0.1070 1711 ASN B CG  
3952 O  OD1 . ASN B 241 ? 0.6983 0.4824 0.8670 0.0640  0.1416  -0.1078 1711 ASN B OD1 
3953 N  ND2 . ASN B 241 ? 0.6565 0.4334 0.8193 0.0598  0.1193  -0.1041 1711 ASN B ND2 
3954 N  N   . TRP B 242 ? 0.6974 0.4592 0.9324 0.0593  0.1108  -0.1235 1712 TRP B N   
3955 C  CA  . TRP B 242 ? 0.6592 0.4151 0.9156 0.0549  0.1036  -0.1232 1712 TRP B CA  
3956 C  C   . TRP B 242 ? 0.6219 0.3729 0.8884 0.0598  0.1102  -0.1257 1712 TRP B C   
3957 O  O   . TRP B 242 ? 0.5597 0.3146 0.8456 0.0571  0.1119  -0.1176 1712 TRP B O   
3958 C  CB  . TRP B 242 ? 0.8561 0.5989 1.1062 0.0519  0.0900  -0.1328 1712 TRP B CB  
3959 C  CG  . TRP B 242 ? 0.8737 0.6093 1.1442 0.0446  0.0810  -0.1319 1712 TRP B CG  
3960 C  CD1 . TRP B 242 ? 0.8468 0.5647 1.1202 0.0450  0.0761  -0.1402 1712 TRP B CD1 
3961 C  CD2 . TRP B 242 ? 0.8710 0.6163 1.1609 0.0352  0.0760  -0.1222 1712 TRP B CD2 
3962 N  NE1 . TRP B 242 ? 0.8452 0.5600 1.1378 0.0353  0.0683  -0.1351 1712 TRP B NE1 
3963 C  CE2 . TRP B 242 ? 0.8340 0.5671 1.1372 0.0290  0.0688  -0.1243 1712 TRP B CE2 
3964 C  CE3 . TRP B 242 ? 0.6610 0.4239 0.9580 0.0317  0.0772  -0.1124 1712 TRP B CE3 
3965 C  CZ2 . TRP B 242 ? 0.7783 0.5182 1.1014 0.0182  0.0638  -0.1164 1712 TRP B CZ2 
3966 C  CZ3 . TRP B 242 ? 0.7503 0.5210 1.0680 0.0226  0.0722  -0.1059 1712 TRP B CZ3 
3967 C  CH2 . TRP B 242 ? 0.6903 0.4506 1.0208 0.0154  0.0661  -0.1077 1712 TRP B CH2 
3968 N  N   . ASN B 243 ? 0.5989 0.3421 0.8517 0.0678  0.1140  -0.1373 1713 ASN B N   
3969 C  CA  . ASN B 243 ? 0.6184 0.3577 0.8813 0.0746  0.1196  -0.1411 1713 ASN B CA  
3970 C  C   . ASN B 243 ? 0.5762 0.3322 0.8511 0.0759  0.1309  -0.1309 1713 ASN B C   
3971 O  O   . ASN B 243 ? 0.5724 0.3273 0.8647 0.0773  0.1316  -0.1275 1713 ASN B O   
3972 C  CB  . ASN B 243 ? 0.8428 0.5751 1.0880 0.0841  0.1235  -0.1563 1713 ASN B CB  
3973 C  CG  . ASN B 243 ? 0.7471 0.4583 0.9858 0.0843  0.1113  -0.1682 1713 ASN B CG  
3974 O  OD1 . ASN B 243 ? 0.7307 0.4312 0.9826 0.0777  0.1008  -0.1650 1713 ASN B OD1 
3975 N  ND2 . ASN B 243 ? 0.7841 0.4891 1.0014 0.0909  0.1127  -0.1822 1713 ASN B ND2 
3976 N  N   . LYS B 244 ? 0.5956 0.3658 0.8606 0.0749  0.1389  -0.1255 1714 LYS B N   
3977 C  CA  . LYS B 244 ? 0.6947 0.4807 0.9707 0.0748  0.1491  -0.1161 1714 LYS B CA  
3978 C  C   . LYS B 244 ? 0.6603 0.4490 0.9566 0.0684  0.1445  -0.1046 1714 LYS B C   
3979 O  O   . LYS B 244 ? 0.7173 0.5121 1.0290 0.0698  0.1488  -0.0997 1714 LYS B O   
3980 C  CB  . LYS B 244 ? 0.7560 0.5526 1.0154 0.0728  0.1564  -0.1117 1714 LYS B CB  
3981 C  CG  . LYS B 244 ? 0.9516 0.7640 1.2168 0.0732  0.1688  -0.1050 1714 LYS B CG  
3982 C  CD  . LYS B 244 ? 0.9460 0.7641 1.1883 0.0724  0.1770  -0.1050 1714 LYS B CD  
3983 C  CE  . LYS B 244 ? 0.9043 0.7383 1.1514 0.0731  0.1912  -0.1019 1714 LYS B CE  
3984 N  NZ  . LYS B 244 ? 0.7551 0.5964 1.0250 0.0784  0.1949  -0.1050 1714 LYS B NZ  
3985 N  N   . PHE B 245 ? 0.6791 0.4642 0.9758 0.0615  0.1354  -0.1009 1715 PHE B N   
3986 C  CA  . PHE B 245 ? 0.5008 0.2898 0.8157 0.0547  0.1315  -0.0908 1715 PHE B CA  
3987 C  C   . PHE B 245 ? 0.5961 0.3737 0.9247 0.0545  0.1265  -0.0921 1715 PHE B C   
3988 O  O   . PHE B 245 ? 0.5986 0.3803 0.9415 0.0529  0.1285  -0.0843 1715 PHE B O   
3989 C  CB  . PHE B 245 ? 0.6395 0.4295 0.9519 0.0480  0.1231  -0.0883 1715 PHE B CB  
3990 C  CG  . PHE B 245 ? 0.6496 0.4517 0.9755 0.0421  0.1236  -0.0773 1715 PHE B CG  
3991 C  CD1 . PHE B 245 ? 0.6434 0.4448 0.9854 0.0355  0.1180  -0.0732 1715 PHE B CD1 
3992 C  CD2 . PHE B 245 ? 0.6536 0.4670 0.9752 0.0429  0.1298  -0.0713 1715 PHE B CD2 
3993 C  CE1 . PHE B 245 ? 0.5276 0.3416 0.8814 0.0304  0.1193  -0.0641 1715 PHE B CE1 
3994 C  CE2 . PHE B 245 ? 0.6740 0.4979 1.0076 0.0385  0.1300  -0.0626 1715 PHE B CE2 
3995 C  CZ  . PHE B 245 ? 0.6188 0.4440 0.9686 0.0326  0.1251  -0.0594 1715 PHE B CZ  
3996 N  N   . LEU B 246 ? 0.5273 0.2887 0.8501 0.0561  0.1193  -0.1020 1716 LEU B N   
3997 C  CA  . LEU B 246 ? 0.5547 0.3007 0.8882 0.0563  0.1136  -0.1037 1716 LEU B CA  
3998 C  C   . LEU B 246 ? 0.6090 0.3563 0.9489 0.0653  0.1206  -0.1042 1716 LEU B C   
3999 O  O   . LEU B 246 ? 0.5486 0.2900 0.9015 0.0645  0.1179  -0.0987 1716 LEU B O   
4000 C  CB  . LEU B 246 ? 0.6178 0.3445 0.9414 0.0579  0.1050  -0.1163 1716 LEU B CB  
4001 C  CG  . LEU B 246 ? 0.6750 0.3933 0.9990 0.0477  0.0934  -0.1168 1716 LEU B CG  
4002 C  CD1 . LEU B 246 ? 0.6982 0.4341 1.0218 0.0408  0.0935  -0.1099 1716 LEU B CD1 
4003 C  CD2 . LEU B 246 ? 0.7094 0.4100 1.0193 0.0509  0.0860  -0.1316 1716 LEU B CD2 
4004 N  N   . MET B 247 ? 0.6806 0.4366 1.0114 0.0738  0.1295  -0.1107 1717 MET B N   
4005 C  CA  . MET B 247 ? 0.7398 0.5017 1.0787 0.0829  0.1368  -0.1123 1717 MET B CA  
4006 C  C   . MET B 247 ? 0.6924 0.4691 1.0449 0.0792  0.1413  -0.0993 1717 MET B C   
4007 O  O   . MET B 247 ? 0.5760 0.3556 0.9372 0.0818  0.1394  -0.0953 1717 MET B O   
4008 C  CB  . MET B 247 ? 0.7232 0.4957 1.0495 0.0907  0.1471  -0.1214 1717 MET B CB  
4009 C  CG  . MET B 247 ? 1.0559 0.8149 1.3712 0.0993  0.1451  -0.1373 1717 MET B CG  
4010 S  SD  . MET B 247 ? 1.3524 1.1027 1.6783 0.1090  0.1393  -0.1422 1717 MET B SD  
4011 C  CE  . MET B 247 ? 0.8755 0.6516 1.2164 0.1105  0.1479  -0.1314 1717 MET B CE  
4012 N  N   . ALA B 248 ? 0.5955 0.3850 0.9447 0.0720  0.1446  -0.0914 1718 ALA B N   
4013 C  CA  . ALA B 248 ? 0.5224 0.3250 0.8835 0.0683  0.1484  -0.0800 1718 ALA B CA  
4014 C  C   . ALA B 248 ? 0.5060 0.3000 0.8791 0.0627  0.1404  -0.0725 1718 ALA B C   
4015 O  O   . ALA B 248 ? 0.6304 0.4311 1.0125 0.0626  0.1409  -0.0653 1718 ALA B O   
4016 C  CB  . ALA B 248 ? 0.4902 0.3054 0.8443 0.0623  0.1527  -0.0739 1718 ALA B CB  
4017 N  N   . ILE B 249 ? 0.5198 0.3009 0.8903 0.0570  0.1319  -0.0736 1719 ILE B N   
4018 C  CA  . ILE B 249 ? 0.6510 0.4229 1.0316 0.0501  0.1247  -0.0662 1719 ILE B CA  
4019 C  C   . ILE B 249 ? 0.7467 0.5085 1.1283 0.0556  0.1198  -0.0675 1719 ILE B C   
4020 O  O   . ILE B 249 ? 0.6853 0.4488 1.0740 0.0538  0.1180  -0.0588 1719 ILE B O   
4021 C  CB  . ILE B 249 ? 0.6413 0.4037 1.0191 0.0413  0.1164  -0.0676 1719 ILE B CB  
4022 C  CG1 . ILE B 249 ? 0.5656 0.3444 0.9420 0.0346  0.1184  -0.0632 1719 ILE B CG1 
4023 C  CG2 . ILE B 249 ? 0.7558 0.5054 1.1427 0.0339  0.1092  -0.0611 1719 ILE B CG2 
4024 C  CD1 . ILE B 249 ? 0.5603 0.3337 0.9333 0.0281  0.1104  -0.0675 1719 ILE B CD1 
4025 N  N   . LYS B 250 ? 0.7158 0.4665 1.0893 0.0632  0.1170  -0.0789 1720 LYS B N   
4026 C  CA  . LYS B 250 ? 0.6908 0.4299 1.0641 0.0702  0.1109  -0.0817 1720 LYS B CA  
4027 C  C   . LYS B 250 ? 0.6419 0.3959 1.0220 0.0770  0.1159  -0.0776 1720 LYS B C   
4028 O  O   . LYS B 250 ? 0.7846 0.5319 1.1698 0.0782  0.1098  -0.0719 1720 LYS B O   
4029 C  CB  . LYS B 250 ? 0.8127 0.5402 1.1752 0.0789  0.1089  -0.0967 1720 LYS B CB  
4030 C  CG  . LYS B 250 ? 0.7557 0.4712 1.1173 0.0887  0.1027  -0.1015 1720 LYS B CG  
4031 C  CD  . LYS B 250 ? 0.8568 0.5615 1.2068 0.0978  0.1015  -0.1176 1720 LYS B CD  
4032 C  CE  . LYS B 250 ? 0.8632 0.5500 1.2114 0.1068  0.0924  -0.1224 1720 LYS B CE  
4033 N  NZ  . LYS B 250 ? 0.9259 0.6257 1.2838 0.1150  0.0949  -0.1177 1720 LYS B NZ  
4034 N  N   . THR B 251 ? 0.5673 0.3408 0.9477 0.0811  0.1265  -0.0801 1721 THR B N   
4035 C  CA  . THR B 251 ? 0.7357 0.5250 1.1242 0.0875  0.1312  -0.0779 1721 THR B CA  
4036 C  C   . THR B 251 ? 0.7319 0.5327 1.1296 0.0806  0.1333  -0.0651 1721 THR B C   
4037 O  O   . THR B 251 ? 0.8255 0.6344 1.2317 0.0849  0.1331  -0.0617 1721 THR B O   
4038 C  CB  . THR B 251 ? 0.7335 0.5391 1.1188 0.0944  0.1423  -0.0868 1721 THR B CB  
4039 O  OG1 . THR B 251 ? 0.8262 0.6421 1.2084 0.0875  0.1504  -0.0833 1721 THR B OG1 
4040 C  CG2 . THR B 251 ? 0.7908 0.5847 1.1656 0.1021  0.1408  -0.1008 1721 THR B CG2 
4041 N  N   . SER B 252 ? 0.7353 0.5379 1.1323 0.0708  0.1350  -0.0585 1722 SER B N   
4042 C  CA  . SER B 252 ? 0.7231 0.5369 1.1279 0.0650  0.1377  -0.0477 1722 SER B CA  
4043 C  C   . SER B 252 ? 0.6438 0.4465 1.0515 0.0563  0.1309  -0.0386 1722 SER B C   
4044 O  O   . SER B 252 ? 0.6693 0.4787 1.0832 0.0526  0.1320  -0.0297 1722 SER B O   
4045 C  CB  . SER B 252 ? 0.7264 0.5540 1.1288 0.0611  0.1466  -0.0468 1722 SER B CB  
4046 O  OG  . SER B 252 ? 0.8267 0.6470 1.2251 0.0541  0.1444  -0.0455 1722 SER B OG  
4047 N  N   . HIS B 253 ? 0.6178 0.4041 1.0211 0.0523  0.1243  -0.0408 1723 HIS B N   
4048 C  CA  . HIS B 253 ? 0.8899 0.6668 1.2961 0.0416  0.1192  -0.0323 1723 HIS B CA  
4049 C  C   . HIS B 253 ? 0.9153 0.7061 1.3259 0.0338  0.1255  -0.0262 1723 HIS B C   
4050 O  O   . HIS B 253 ? 0.9796 0.7705 1.3940 0.0252  0.1240  -0.0172 1723 HIS B O   
4051 C  CB  . HIS B 253 ? 0.8795 0.6472 1.2888 0.0414  0.1132  -0.0243 1723 HIS B CB  
4052 C  CG  . HIS B 253 ? 1.0843 0.8355 1.4894 0.0495  0.1053  -0.0300 1723 HIS B CG  
4053 N  ND1 . HIS B 253 ? 1.1728 0.9016 1.5728 0.0452  0.0960  -0.0305 1723 HIS B ND1 
4054 C  CD2 . HIS B 253 ? 1.1110 0.8646 1.5163 0.0618  0.1051  -0.0362 1723 HIS B CD2 
4055 C  CE1 . HIS B 253 ? 1.1599 0.8762 1.5560 0.0554  0.0900  -0.0368 1723 HIS B CE1 
4056 N  NE2 . HIS B 253 ? 1.1177 0.8498 1.5176 0.0660  0.0955  -0.0406 1723 HIS B NE2 
4057 N  N   . SER B 254 ? 0.4777 0.2816 0.8853 0.0364  0.1321  -0.0309 1724 SER B N   
4058 C  CA  . SER B 254 ? 0.5916 0.4110 0.9986 0.0300  0.1361  -0.0265 1724 SER B CA  
4059 C  C   . SER B 254 ? 0.5507 0.3676 0.9598 0.0197  0.1312  -0.0229 1724 SER B C   
4060 O  O   . SER B 254 ? 0.4226 0.2332 0.8284 0.0179  0.1272  -0.0286 1724 SER B O   
4061 C  CB  . SER B 254 ? 0.6315 0.4585 1.0308 0.0340  0.1407  -0.0331 1724 SER B CB  
4062 O  OG  . SER B 254 ? 0.7198 0.5612 1.1190 0.0302  0.1446  -0.0285 1724 SER B OG  
4063 N  N   . PRO B 255 ? 0.5997 0.4230 1.0141 0.0124  0.1317  -0.0140 1725 PRO B N   
4064 C  CA  . PRO B 255 ? 0.4911 0.3169 0.9091 0.0017  0.1287  -0.0110 1725 PRO B CA  
4065 C  C   . PRO B 255 ? 0.6000 0.4389 1.0174 0.0011  0.1303  -0.0155 1725 PRO B C   
4066 O  O   . PRO B 255 ? 0.5264 0.3661 0.9470 -0.0054 0.1261  -0.0173 1725 PRO B O   
4067 C  CB  . PRO B 255 ? 0.5047 0.3386 0.9267 -0.0047 0.1314  -0.0010 1725 PRO B CB  
4068 C  CG  . PRO B 255 ? 0.6810 0.5115 1.1011 0.0027  0.1331  0.0016  1725 PRO B CG  
4069 C  CD  . PRO B 255 ? 0.6113 0.4429 1.0283 0.0131  0.1356  -0.0069 1725 PRO B CD  
4070 N  N   A VAL B 256 ? 0.4416 0.2907 0.8552 0.0076  0.1357  -0.0173 1726 VAL B N   
4071 N  N   B VAL B 256 ? 0.4727 0.3218 0.8862 0.0076  0.1357  -0.0172 1726 VAL B N   
4072 C  CA  A VAL B 256 ? 0.4987 0.3585 0.9106 0.0078  0.1362  -0.0205 1726 VAL B CA  
4073 C  CA  B VAL B 256 ? 0.5025 0.3623 0.9144 0.0078  0.1361  -0.0206 1726 VAL B CA  
4074 C  C   A VAL B 256 ? 0.5270 0.3777 0.9319 0.0109  0.1314  -0.0288 1726 VAL B C   
4075 C  C   B VAL B 256 ? 0.5228 0.3734 0.9277 0.0108  0.1313  -0.0288 1726 VAL B C   
4076 O  O   A VAL B 256 ? 0.5528 0.4076 0.9592 0.0075  0.1268  -0.0316 1726 VAL B O   
4077 O  O   B VAL B 256 ? 0.5452 0.3997 0.9517 0.0073  0.1267  -0.0316 1726 VAL B O   
4078 C  CB  A VAL B 256 ? 0.5931 0.4629 1.0015 0.0130  0.1427  -0.0190 1726 VAL B CB  
4079 C  CB  B VAL B 256 ? 0.5602 0.4300 0.9683 0.0131  0.1426  -0.0193 1726 VAL B CB  
4080 C  CG1 A VAL B 256 ? 0.6699 0.5434 1.0719 0.0164  0.1422  -0.0234 1726 VAL B CG1 
4081 C  CG1 B VAL B 256 ? 0.4546 0.3187 0.8575 0.0197  0.1463  -0.0205 1726 VAL B CG1 
4082 C  CG2 A VAL B 256 ? 0.3781 0.2599 0.7933 0.0085  0.1459  -0.0124 1726 VAL B CG2 
4083 C  CG2 B VAL B 256 ? 0.6381 0.5122 1.0408 0.0158  0.1416  -0.0235 1726 VAL B CG2 
4084 N  N   . CYS B 257 ? 0.5455 0.3846 0.9429 0.0173  0.1319  -0.0335 1727 CYS B N   
4085 C  CA  . CYS B 257 ? 0.4728 0.3018 0.8618 0.0200  0.1271  -0.0421 1727 CYS B CA  
4086 C  C   . CYS B 257 ? 0.4301 0.2481 0.8241 0.0134  0.1189  -0.0441 1727 CYS B C   
4087 O  O   . CYS B 257 ? 0.5330 0.3471 0.9229 0.0120  0.1129  -0.0504 1727 CYS B O   
4088 C  CB  . CYS B 257 ? 0.6809 0.5021 1.0610 0.0288  0.1309  -0.0476 1727 CYS B CB  
4089 S  SG  . CYS B 257 ? 1.0239 0.8575 1.3989 0.0346  0.1410  -0.0451 1727 CYS B SG  
4090 N  N   . GLN B 258 ? 0.4325 0.2444 0.8344 0.0088  0.1178  -0.0385 1728 GLN B N   
4091 C  CA  . GLN B 258 ? 0.6220 0.4224 1.0288 0.0002  0.1100  -0.0389 1728 GLN B CA  
4092 C  C   . GLN B 258 ? 0.5098 0.3246 0.9243 -0.0092 0.1076  -0.0371 1728 GLN B C   
4093 O  O   . GLN B 258 ? 0.5192 0.3289 0.9354 -0.0148 0.1003  -0.0418 1728 GLN B O   
4094 C  CB  . GLN B 258 ? 0.4729 0.2631 0.8850 -0.0039 0.1094  -0.0312 1728 GLN B CB  
4095 C  CG  . GLN B 258 ? 0.9487 0.7228 1.3560 0.0059  0.1093  -0.0339 1728 GLN B CG  
4096 C  CD  . GLN B 258 ? 1.0180 0.7850 1.4299 0.0032  0.1088  -0.0242 1728 GLN B CD  
4097 O  OE1 . GLN B 258 ? 0.9580 0.7239 1.3692 0.0118  0.1116  -0.0232 1728 GLN B OE1 
4098 N  NE2 . GLN B 258 ? 1.0926 0.8556 1.5090 -0.0091 0.1051  -0.0170 1728 GLN B NE2 
4099 N  N   . ASP B 259 ? 0.5312 0.3649 0.9512 -0.0106 0.1134  -0.0310 1729 ASP B N   
4100 C  CA  . ASP B 259 ? 0.5033 0.3545 0.9323 -0.0173 0.1120  -0.0304 1729 ASP B CA  
4101 C  C   . ASP B 259 ? 0.4178 0.2723 0.8415 -0.0124 0.1075  -0.0387 1729 ASP B C   
4102 O  O   . ASP B 259 ? 0.4557 0.3163 0.8862 -0.0184 0.1012  -0.0419 1729 ASP B O   
4103 C  CB  . ASP B 259 ? 0.3972 0.2667 0.8317 -0.0175 0.1195  -0.0237 1729 ASP B CB  
4104 C  CG  . ASP B 259 ? 0.5250 0.4152 0.9725 -0.0252 0.1188  -0.0228 1729 ASP B CG  
4105 O  OD1 . ASP B 259 ? 0.5210 0.4130 0.9778 -0.0364 0.1167  -0.0200 1729 ASP B OD1 
4106 O  OD2 . ASP B 259 ? 0.4849 0.3898 0.9337 -0.0200 0.1207  -0.0249 1729 ASP B OD2 
4107 N  N   . VAL B 260 ? 0.4906 0.3418 0.9018 -0.0022 0.1103  -0.0419 1730 VAL B N   
4108 C  CA  . VAL B 260 ? 0.4566 0.3081 0.8590 0.0024  0.1053  -0.0490 1730 VAL B CA  
4109 C  C   . VAL B 260 ? 0.4419 0.2802 0.8418 -0.0011 0.0964  -0.0563 1730 VAL B C   
4110 O  O   . VAL B 260 ? 0.5253 0.3684 0.9266 -0.0035 0.0888  -0.0611 1730 VAL B O   
4111 C  CB  . VAL B 260 ? 0.4356 0.2829 0.8221 0.0126  0.1105  -0.0508 1730 VAL B CB  
4112 C  CG1 . VAL B 260 ? 0.4347 0.2785 0.8082 0.0166  0.1043  -0.0579 1730 VAL B CG1 
4113 C  CG2 . VAL B 260 ? 0.4049 0.2649 0.7936 0.0151  0.1175  -0.0445 1730 VAL B CG2 
4114 N  N   . LEU B 261 ? 0.4770 0.2979 0.8731 -0.0006 0.0966  -0.0578 1731 LEU B N   
4115 C  CA  . LEU B 261 ? 0.5279 0.3323 0.9205 -0.0035 0.0879  -0.0655 1731 LEU B CA  
4116 C  C   . LEU B 261 ? 0.6055 0.4146 1.0127 -0.0164 0.0807  -0.0641 1731 LEU B C   
4117 O  O   . LEU B 261 ? 0.4919 0.2988 0.8982 -0.0197 0.0718  -0.0712 1731 LEU B O   
4118 C  CB  . LEU B 261 ? 0.5497 0.3346 0.9383 -0.0001 0.0897  -0.0664 1731 LEU B CB  
4119 C  CG  . LEU B 261 ? 0.7728 0.5384 1.1495 0.0039  0.0832  -0.0779 1731 LEU B CG  
4120 C  CD1 . LEU B 261 ? 0.8628 0.6336 1.2237 0.0132  0.0858  -0.0843 1731 LEU B CD1 
4121 C  CD2 . LEU B 261 ? 0.9396 0.6862 1.3144 0.0087  0.0845  -0.0792 1731 LEU B CD2 
4122 N  N   . LYS B 262 ? 0.5262 0.3417 0.9464 -0.0244 0.0844  -0.0550 1732 LYS B N   
4123 C  CA  . LYS B 262 ? 0.6426 0.4664 1.0782 -0.0383 0.0796  -0.0525 1732 LYS B CA  
4124 C  C   . LYS B 262 ? 0.6187 0.4643 1.0613 -0.0393 0.0761  -0.0561 1732 LYS B C   
4125 O  O   . LYS B 262 ? 0.4761 0.3243 0.9265 -0.0475 0.0675  -0.0608 1732 LYS B O   
4126 C  CB  . LYS B 262 ? 0.7000 0.5318 1.1461 -0.0461 0.0864  -0.0412 1732 LYS B CB  
4127 N  N   . PHE B 263 ? 0.4948 0.3559 0.9354 -0.0309 0.0819  -0.0542 1733 PHE B N   
4128 C  CA  . PHE B 263 ? 0.5111 0.3925 0.9588 -0.0300 0.0778  -0.0575 1733 PHE B CA  
4129 C  C   . PHE B 263 ? 0.5065 0.3792 0.9441 -0.0264 0.0673  -0.0672 1733 PHE B C   
4130 O  O   . PHE B 263 ? 0.5033 0.3875 0.9510 -0.0316 0.0588  -0.0716 1733 PHE B O   
4131 C  CB  . PHE B 263 ? 0.4237 0.3182 0.8681 -0.0202 0.0847  -0.0542 1733 PHE B CB  
4132 C  CG  . PHE B 263 ? 0.5151 0.4253 0.9632 -0.0162 0.0784  -0.0587 1733 PHE B CG  
4133 C  CD1 . PHE B 263 ? 0.4828 0.4161 0.9518 -0.0230 0.0760  -0.0585 1733 PHE B CD1 
4134 C  CD2 . PHE B 263 ? 0.4797 0.3814 0.9107 -0.0064 0.0737  -0.0637 1733 PHE B CD2 
4135 C  CE1 . PHE B 263 ? 0.5211 0.4696 0.9956 -0.0183 0.0685  -0.0635 1733 PHE B CE1 
4136 C  CE2 . PHE B 263 ? 0.4317 0.3462 0.8654 -0.0024 0.0658  -0.0675 1733 PHE B CE2 
4137 C  CZ  . PHE B 263 ? 0.5374 0.4752 0.9936 -0.0076 0.0627  -0.0677 1733 PHE B CZ  
4138 N  N   . ILE B 264 ? 0.4904 0.3446 0.9079 -0.0173 0.0680  -0.0711 1734 ILE B N   
4139 C  CA  . ILE B 264 ? 0.5306 0.3757 0.9346 -0.0135 0.0584  -0.0807 1734 ILE B CA  
4140 C  C   . ILE B 264 ? 0.5957 0.4321 1.0069 -0.0239 0.0486  -0.0864 1734 ILE B C   
4141 O  O   . ILE B 264 ? 0.5882 0.4266 0.9979 -0.0253 0.0378  -0.0939 1734 ILE B O   
4142 C  CB  . ILE B 264 ? 0.5589 0.3861 0.9395 -0.0028 0.0628  -0.0841 1734 ILE B CB  
4143 C  CG1 . ILE B 264 ? 0.5349 0.3711 0.9077 0.0061  0.0710  -0.0789 1734 ILE B CG1 
4144 C  CG2 . ILE B 264 ? 0.6301 0.4454 0.9946 0.0000  0.0531  -0.0948 1734 ILE B CG2 
4145 C  CD1 . ILE B 264 ? 0.6274 0.4496 0.9786 0.0151  0.0768  -0.0817 1734 ILE B CD1 
4146 N  N   . SER B 265 ? 0.5561 0.3813 0.9742 -0.0314 0.0512  -0.0829 1735 SER B N   
4147 C  CA  . SER B 265 ? 0.7744 0.5883 1.1994 -0.0430 0.0418  -0.0874 1735 SER B CA  
4148 C  C   . SER B 265 ? 0.6980 0.5349 1.1443 -0.0548 0.0360  -0.0865 1735 SER B C   
4149 O  O   . SER B 265 ? 0.5746 0.4107 1.0234 -0.0603 0.0245  -0.0945 1735 SER B O   
4150 C  CB  . SER B 265 ? 0.7553 0.5512 1.1828 -0.0485 0.0460  -0.0817 1735 SER B CB  
4151 O  OG  . SER B 265 ? 0.9730 0.7524 1.4043 -0.0595 0.0364  -0.0862 1735 SER B OG  
4152 N  N   . GLN B 266 ? 0.5955 0.4542 1.0577 -0.0589 0.0438  -0.0776 1736 GLN B N   
4153 C  CA  . GLN B 266 ? 0.6868 0.5720 1.1715 -0.0694 0.0396  -0.0774 1736 GLN B CA  
4154 C  C   . GLN B 266 ? 0.6652 0.5652 1.1491 -0.0617 0.0312  -0.0851 1736 GLN B C   
4155 O  O   . GLN B 266 ? 0.5944 0.5047 1.0904 -0.0694 0.0206  -0.0912 1736 GLN B O   
4156 C  CB  . GLN B 266 ? 0.5658 0.4736 1.0655 -0.0727 0.0508  -0.0676 1736 GLN B CB  
4157 C  CG  . GLN B 266 ? 0.7812 0.6766 1.2810 -0.0805 0.0590  -0.0583 1736 GLN B CG  
4158 C  CD  . GLN B 266 ? 1.0744 0.9947 1.5948 -0.0929 0.0654  -0.0509 1736 GLN B CD  
4159 O  OE1 . GLN B 266 ? 1.1087 1.0535 1.6368 -0.0879 0.0720  -0.0487 1736 GLN B OE1 
4160 N  NE2 . GLN B 266 ? 1.1319 1.0456 1.6608 -0.1097 0.0636  -0.0472 1736 GLN B NE2 
4161 N  N   . TRP B 267 ? 0.4907 0.3905 0.9598 -0.0470 0.0349  -0.0850 1737 TRP B N   
4162 C  CA  . TRP B 267 ? 0.5609 0.4753 1.0285 -0.0385 0.0276  -0.0899 1737 TRP B CA  
4163 C  C   . TRP B 267 ? 0.6341 0.5335 1.0865 -0.0363 0.0146  -0.1000 1737 TRP B C   
4164 O  O   . TRP B 267 ? 0.6010 0.5144 1.0604 -0.0365 0.0033  -0.1058 1737 TRP B O   
4165 C  CB  . TRP B 267 ? 0.4710 0.3857 0.9249 -0.0245 0.0361  -0.0853 1737 TRP B CB  
4166 C  CG  . TRP B 267 ? 0.7776 0.7032 1.2265 -0.0143 0.0289  -0.0886 1737 TRP B CG  
4167 C  CD1 . TRP B 267 ? 0.8073 0.7542 1.2727 -0.0158 0.0186  -0.0929 1737 TRP B CD1 
4168 C  CD2 . TRP B 267 ? 0.9296 0.8452 1.3558 -0.0010 0.0312  -0.0874 1737 TRP B CD2 
4169 N  NE1 . TRP B 267 ? 0.8944 0.8431 1.3475 -0.0031 0.0133  -0.0942 1737 TRP B NE1 
4170 C  CE2 . TRP B 267 ? 0.8192 0.7478 1.2472 0.0053  0.0211  -0.0904 1737 TRP B CE2 
4171 C  CE3 . TRP B 267 ? 0.9185 0.8156 1.3232 0.0056  0.0405  -0.0839 1737 TRP B CE3 
4172 C  CZ2 . TRP B 267 ? 0.7843 0.7050 1.1912 0.0175  0.0198  -0.0891 1737 TRP B CZ2 
4173 C  CZ3 . TRP B 267 ? 0.8105 0.7023 1.1958 0.0165  0.0404  -0.0828 1737 TRP B CZ3 
4174 C  CH2 . TRP B 267 ? 0.7739 0.6758 1.1591 0.0221  0.0299  -0.0850 1737 TRP B CH2 
4175 N  N   . CYS B 268 ? 0.5367 0.4087 0.9688 -0.0339 0.0156  -0.1030 1738 CYS B N   
4176 C  CA  . CYS B 268 ? 0.7197 0.5756 1.1317 -0.0293 0.0049  -0.1132 1738 CYS B CA  
4177 C  C   . CYS B 268 ? 0.7851 0.6239 1.1985 -0.0398 -0.0033 -0.1205 1738 CYS B C   
4178 O  O   . CYS B 268 ? 0.9122 0.7372 1.3090 -0.0371 -0.0133 -0.1305 1738 CYS B O   
4179 C  CB  . CYS B 268 ? 0.7954 0.6337 1.1797 -0.0163 0.0127  -0.1130 1738 CYS B CB  
4180 S  SG  . CYS B 268 ? 0.7442 0.5994 1.1239 -0.0047 0.0194  -0.1054 1738 CYS B SG  
4181 N  N   . GLY B 269 ? 0.7854 0.6239 1.2170 -0.0522 -0.0001 -0.1158 1739 GLY B N   
4182 C  CA  . GLY B 269 ? 1.1004 0.9259 1.5384 -0.0652 -0.0102 -0.1220 1739 GLY B CA  
4183 C  C   . GLY B 269 ? 1.1949 0.9857 1.6140 -0.0632 -0.0110 -0.1275 1739 GLY B C   
4184 O  O   . GLY B 269 ? 1.2731 1.0486 1.6863 -0.0679 -0.0229 -0.1378 1739 GLY B O   
4185 N  N   . GLY B 270 ? 1.0759 0.8541 1.4860 -0.0561 0.0007  -0.1218 1740 GLY B N   
4186 C  CA  . GLY B 270 ? 1.1347 0.8811 1.5306 -0.0536 0.0004  -0.1268 1740 GLY B CA  
4187 C  C   . GLY B 270 ? 1.3813 1.1155 1.7507 -0.0373 0.0028  -0.1348 1740 GLY B C   
4188 O  O   . GLY B 270 ? 1.4627 1.2057 1.8205 -0.0311 -0.0014 -0.1404 1740 GLY B O   
4189 N  N   . LEU B 271 ? 1.4207 1.1339 1.7799 -0.0305 0.0091  -0.1357 1741 LEU B N   
4190 C  CA  . LEU B 271 ? 1.3577 1.0608 1.6930 -0.0150 0.0145  -0.1429 1741 LEU B CA  
4191 C  C   . LEU B 271 ? 1.2475 0.9372 1.5629 -0.0113 0.0042  -0.1582 1741 LEU B C   
4192 O  O   . LEU B 271 ? 1.3115 0.9856 1.6289 -0.0192 -0.0074 -0.1661 1741 LEU B O   
4193 C  CB  . LEU B 271 ? 1.3520 1.0369 1.6852 -0.0090 0.0222  -0.1416 1741 LEU B CB  
4194 N  N1  . EPE C .   ? 1.1107 1.1400 1.3390 -0.0032 0.1945  -0.0686 1801 EPE A N1  
4195 C  C2  . EPE C .   ? 1.1254 1.1724 1.3458 -0.0077 0.2039  -0.0632 1801 EPE A C2  
4196 C  C3  . EPE C .   ? 1.1345 1.1800 1.3534 -0.0163 0.2005  -0.0455 1801 EPE A C3  
4197 N  N4  . EPE C .   ? 1.1962 1.2305 1.4350 -0.0153 0.1947  -0.0382 1801 EPE A N4  
4198 C  C5  . EPE C .   ? 1.1075 1.1281 1.3553 -0.0103 0.1873  -0.0447 1801 EPE A C5  
4199 C  C6  . EPE C .   ? 1.1422 1.1632 1.3911 -0.0028 0.1913  -0.0603 1801 EPE A C6  
4200 C  C7  . EPE C .   ? 1.2313 1.2645 1.4740 -0.0213 0.1931  -0.0228 1801 EPE A C7  
4201 C  C8  . EPE C .   ? 1.1945 1.2161 1.4572 -0.0188 0.1872  -0.0180 1801 EPE A C8  
4202 O  O8  . EPE C .   ? 1.0547 1.0658 1.3155 -0.0193 0.1768  -0.0153 1801 EPE A O8  
4203 C  C9  . EPE C .   ? 1.1723 1.2001 1.4027 0.0055  0.1975  -0.0848 1801 EPE A C9  
4204 C  C10 . EPE C .   ? 1.3450 1.3525 1.5836 0.0083  0.1879  -0.0885 1801 EPE A C10 
4205 S  S   . EPE C .   ? 1.3688 1.3652 1.6000 0.0167  0.1859  -0.1087 1801 EPE A S   
4206 O  O1S . EPE C .   ? 1.4022 1.4129 1.6303 0.0239  0.1958  -0.1195 1801 EPE A O1S 
4207 O  O2S . EPE C .   ? 1.3233 1.3137 1.5369 0.0121  0.1787  -0.1125 1801 EPE A O2S 
4208 O  O3S . EPE C .   ? 0.7989 0.7774 1.0448 0.0207  0.1805  -0.1105 1801 EPE A O3S 
4209 CL CL  . CL  D .   ? 0.6170 1.1316 1.5051 -0.0021 0.1460  -0.0941 1802 CL  A CL  
4210 N  N1  . EPE E .   ? 1.2911 1.0738 1.2609 0.0143  0.2317  -0.0289 1801 EPE B N1  
4211 C  C2  . EPE E .   ? 1.2735 1.0742 1.2445 0.0160  0.2464  -0.0411 1801 EPE B C2  
4212 C  C3  . EPE E .   ? 1.2934 1.0937 1.2672 0.0268  0.2379  -0.0558 1801 EPE B C3  
4213 N  N4  . EPE E .   ? 1.4206 1.2180 1.4235 0.0327  0.2234  -0.0572 1801 EPE B N4  
4214 C  C5  . EPE E .   ? 1.3610 1.1453 1.3656 0.0304  0.2109  -0.0451 1801 EPE B C5  
4215 C  C6  . EPE E .   ? 1.2530 1.0386 1.2573 0.0212  0.2203  -0.0324 1801 EPE B C6  
4216 C  C7  . EPE E .   ? 1.4375 1.2381 1.4552 0.0416  0.2173  -0.0711 1801 EPE B C7  
4217 C  C8  . EPE E .   ? 1.3986 1.1832 1.3929 0.0458  0.2027  -0.0762 1801 EPE B C8  
4218 O  O8  . EPE E .   ? 1.3829 1.1578 1.3871 0.0462  0.1864  -0.0690 1801 EPE B O8  
4219 C  C9  . EPE E .   ? 1.4049 1.1880 1.3760 0.0039  0.2403  -0.0163 1801 EPE B C9  
4220 C  C10 . EPE E .   ? 1.4809 1.2454 1.4537 0.0037  0.2251  -0.0051 1801 EPE B C10 
4221 S  S   . EPE E .   ? 1.3734 1.1231 1.3266 -0.0095 0.2301  0.0127  1801 EPE B S   
4222 O  O1S . EPE E .   ? 0.9918 0.7354 0.9682 -0.0085 0.2208  0.0188  1801 EPE B O1S 
4223 O  O2S . EPE E .   ? 1.4913 1.2577 1.4466 -0.0196 0.2502  0.0134  1801 EPE B O2S 
4224 O  O3S . EPE E .   ? 1.4284 1.1547 1.3399 -0.0109 0.2223  0.0200  1801 EPE B O3S 
4225 O  O   . HOH F .   ? 0.6929 0.6261 1.0112 0.0699  0.1785  -0.1270 1901 HOH A O   
4226 O  O   . HOH F .   ? 1.1395 1.0178 1.2904 -0.1121 0.1399  0.1720  1902 HOH A O   
4227 O  O   . HOH F .   ? 0.4844 0.4786 0.7832 -0.0327 0.0931  -0.0317 1903 HOH A O   
4228 O  O   . HOH F .   ? 0.8847 0.8900 1.1880 0.0785  0.2040  -0.1553 1904 HOH A O   
4229 O  O   . HOH F .   ? 0.3897 0.8808 1.2576 -0.0512 0.1503  -0.0842 1905 HOH A O   
4230 O  O   . HOH F .   ? 0.8573 0.8226 1.0606 -0.0681 0.1583  0.0951  1906 HOH A O   
4231 O  O   . HOH F .   ? 0.5676 0.5511 0.9568 -0.0260 0.1851  0.0277  1907 HOH A O   
4232 O  O   . HOH F .   ? 0.4562 0.4008 0.8841 -0.0663 0.1798  -0.0120 1908 HOH A O   
4233 O  O   . HOH F .   ? 0.4786 0.3924 0.8444 -0.0079 0.1639  -0.0278 1909 HOH A O   
4234 O  O   . HOH F .   ? 0.7650 0.5234 1.1005 -0.1084 0.1273  -0.0521 1910 HOH A O   
4235 O  O   . HOH F .   ? 0.6456 0.4722 1.0405 0.0636  0.0303  0.0965  1911 HOH A O   
4236 O  O   . HOH F .   ? 1.0949 1.0907 1.2153 -0.0417 0.0731  -0.0656 1912 HOH A O   
4237 O  O   . HOH F .   ? 0.8669 0.8701 1.1468 -0.0703 0.0246  -0.0862 1913 HOH A O   
4238 O  O   . HOH F .   ? 0.6694 0.3473 0.9663 -0.0991 0.1167  -0.0591 1914 HOH A O   
4239 O  O   . HOH F .   ? 0.6781 0.5820 1.0884 0.0154  0.1603  -0.0062 1915 HOH A O   
4240 O  O   . HOH F .   ? 0.6921 0.6794 1.1597 -0.1313 0.2100  -0.0041 1916 HOH A O   
4241 O  O   . HOH F .   ? 0.5165 0.5471 0.9842 -0.0175 0.2348  -0.0166 1917 HOH A O   
4242 O  O   . HOH F .   ? 0.3793 0.3221 0.7775 -0.0420 0.1479  -0.0286 1918 HOH A O   
4243 O  O   . HOH F .   ? 0.9406 0.8390 1.0807 -0.0148 0.1041  -0.1756 1919 HOH A O   
4244 O  O   . HOH F .   ? 0.9783 0.9167 1.1253 -0.0208 0.1098  -0.1413 1920 HOH A O   
4245 O  O   . HOH F .   ? 0.4163 0.8958 1.2218 -0.0449 0.2165  -0.0851 1921 HOH A O   
4246 O  O   . HOH F .   ? 0.5193 0.4505 0.9162 -0.0098 0.1740  -0.0090 1922 HOH A O   
4247 O  O   . HOH F .   ? 0.6494 0.4918 0.9610 -0.0502 0.1209  0.1185  1923 HOH A O   
4248 O  O   . HOH F .   ? 0.6805 0.6733 0.8884 -0.0356 0.1338  0.0322  1924 HOH A O   
4249 O  O   . HOH F .   ? 0.4914 0.4538 0.8606 -0.0842 0.0772  -0.0774 1925 HOH A O   
4250 O  O   . HOH F .   ? 0.4701 0.4944 0.8705 -0.0112 0.0862  0.0059  1926 HOH A O   
4251 O  O   . HOH F .   ? 0.4679 0.3937 0.8717 -0.0428 0.1678  -0.0172 1927 HOH A O   
4252 O  O   . HOH F .   ? 0.4676 0.4409 0.8356 0.0157  0.0623  0.0584  1928 HOH A O   
4253 O  O   . HOH F .   ? 0.6955 0.7328 1.0038 0.0611  0.2141  -0.1334 1929 HOH A O   
4254 O  O   . HOH F .   ? 0.5301 0.5060 0.8338 -0.0306 0.1122  -0.0429 1930 HOH A O   
4255 O  O   . HOH F .   ? 0.7554 0.7642 1.1274 -0.0019 0.1951  -0.0104 1931 HOH A O   
4256 O  O   . HOH F .   ? 0.6184 0.4666 0.9779 -0.0464 0.1631  -0.0233 1932 HOH A O   
4257 O  O   . HOH F .   ? 0.4488 0.4422 0.8424 0.0072  0.0910  0.0339  1933 HOH A O   
4258 O  O   . HOH F .   ? 0.7197 0.7226 0.9002 -0.0358 0.1335  0.0094  1934 HOH A O   
4259 O  O   . HOH F .   ? 1.0174 0.7314 1.2076 -0.0379 0.0658  -0.2054 1935 HOH A O   
4260 O  O   . HOH F .   ? 0.5406 0.4231 0.8892 -0.0037 0.1606  -0.0409 1936 HOH A O   
4261 O  O   . HOH F .   ? 0.5930 0.6399 1.1125 0.0421  0.2062  -0.0333 1937 HOH A O   
4262 O  O   . HOH F .   ? 0.8297 0.8896 1.3843 0.0985  -0.0007 0.0312  1938 HOH A O   
4263 O  O   . HOH F .   ? 0.3941 0.9830 1.2609 -0.0427 0.2276  -0.1024 1939 HOH A O   
4264 O  O   . HOH F .   ? 0.6747 0.6967 1.0090 -0.0014 0.0239  0.0354  1940 HOH A O   
4265 O  O   . HOH F .   ? 0.5945 0.4773 1.0008 0.0216  0.1575  -0.0111 1941 HOH A O   
4266 O  O   . HOH F .   ? 0.3185 0.2976 0.7759 0.0219  0.1491  0.0106  1942 HOH A O   
4267 O  O   . HOH F .   ? 0.4342 0.3723 0.8080 -0.0342 0.1415  -0.0362 1943 HOH A O   
4268 O  O   . HOH F .   ? 0.3234 0.5480 0.9974 0.0546  0.1813  -0.0591 1944 HOH A O   
4269 O  O   . HOH F .   ? 0.4682 0.5476 0.9989 0.0376  0.0691  0.0098  1945 HOH A O   
4270 O  O   . HOH F .   ? 0.3631 0.6365 1.0716 0.1029  0.1763  -0.0887 1946 HOH A O   
4271 O  O   . HOH F .   ? 0.4345 0.7377 1.1808 0.0747  0.1582  -0.0743 1947 HOH A O   
4272 O  O   . HOH F .   ? 0.3732 0.3243 0.7604 0.0154  0.1794  -0.0149 1948 HOH A O   
4273 O  O   . HOH F .   ? 0.7977 0.8273 1.2314 -0.0022 0.1929  -0.0112 1949 HOH A O   
4274 O  O   . HOH F .   ? 0.8425 0.4711 1.0767 -0.1045 0.0455  -0.1740 1950 HOH A O   
4275 O  O   . HOH F .   ? 0.7991 0.6208 1.2294 -0.2477 0.0971  -0.0666 1951 HOH A O   
4276 O  O   . HOH F .   ? 0.7206 0.7371 1.2231 -0.1638 0.2031  -0.0103 1952 HOH A O   
4277 O  O   . HOH F .   ? 0.6576 0.5396 1.0219 0.0147  0.1744  -0.0121 1953 HOH A O   
4278 O  O   . HOH F .   ? 0.5544 0.5258 0.7583 -0.0436 0.1300  0.0695  1954 HOH A O   
4279 O  O   . HOH F .   ? 0.9627 0.8012 1.2679 0.1185  0.1507  -0.1762 1955 HOH A O   
4280 O  O   . HOH F .   ? 0.5427 0.5227 0.8565 -0.0612 0.1846  0.0695  1956 HOH A O   
4281 O  O   . HOH F .   ? 0.7515 0.6624 1.1271 0.0223  0.1738  -0.0205 1957 HOH A O   
4282 O  O   . HOH F .   ? 0.8023 0.7982 1.2421 0.0104  0.2294  -0.0216 1958 HOH A O   
4283 O  O   . HOH F .   ? 0.6024 0.5237 0.9675 0.0058  0.1703  -0.0268 1959 HOH A O   
4284 O  O   . HOH F .   ? 0.7392 0.6806 1.1406 -0.0106 0.2112  -0.0033 1960 HOH A O   
4285 O  O   . HOH F .   ? 0.6355 0.5424 1.1692 0.1310  0.0549  0.0177  1961 HOH A O   
4286 O  O   . HOH F .   ? 0.7395 0.6164 1.1521 -0.1384 0.1439  -0.0358 1962 HOH A O   
4287 O  O   . HOH F .   ? 0.7578 0.6300 1.1147 0.0113  0.1694  -0.0231 1963 HOH A O   
4288 O  O   . HOH F .   ? 0.8463 0.7631 1.1945 -0.0986 0.0712  -0.0978 1964 HOH A O   
4289 O  O   . HOH F .   ? 0.7289 0.7452 1.2442 -0.2093 0.0559  -0.0923 1965 HOH A O   
4290 O  O   . HOH F .   ? 0.6337 0.4632 0.9758 -0.0212 0.1608  -0.0284 1966 HOH A O   
4291 O  O   . HOH F .   ? 0.4690 0.5581 0.9531 -0.0465 0.0686  -0.0301 1967 HOH A O   
4292 O  O   . HOH F .   ? 0.6843 0.5994 1.0768 0.0155  0.1829  -0.0031 1968 HOH A O   
4293 O  O   . HOH F .   ? 0.7707 0.7637 1.0239 -0.0423 0.1675  0.0479  1969 HOH A O   
4294 O  O   . HOH F .   ? 0.6800 0.4896 1.0233 -0.0667 0.1707  -0.0095 1970 HOH A O   
4295 O  O   . HOH F .   ? 0.4638 0.5395 1.0498 0.0806  0.1631  -0.0361 1971 HOH A O   
4296 O  O   . HOH F .   ? 0.5477 0.5521 0.9588 0.0183  0.0668  0.0388  1972 HOH A O   
4297 O  O   . HOH F .   ? 0.6593 0.7584 1.2614 0.0855  0.0640  -0.0005 1973 HOH A O   
4298 O  O   . HOH F .   ? 0.9375 0.7205 1.1033 -0.0235 0.0772  -0.2096 1974 HOH A O   
4299 O  O   . HOH F .   ? 0.7681 0.8495 1.3274 0.0675  0.0500  0.0133  1975 HOH A O   
4300 O  O   . HOH F .   ? 0.4128 0.7808 1.1968 0.1171  0.1609  -0.1050 1976 HOH A O   
4301 O  O   . HOH F .   ? 0.8155 0.6360 1.1328 0.1118  0.1441  -0.1501 1977 HOH A O   
4302 O  O   . HOH F .   ? 0.9287 0.6579 1.2081 0.0074  0.0217  0.1624  1978 HOH A O   
4303 O  O   . HOH F .   ? 0.8616 0.8294 1.2777 0.0233  0.2244  -0.0251 1979 HOH A O   
4304 O  O   . HOH F .   ? 0.7785 0.6560 1.1160 0.0720  0.1614  -0.1019 1980 HOH A O   
4305 O  O   . HOH F .   ? 0.6721 0.5683 1.0945 -0.1347 0.1597  -0.0244 1981 HOH A O   
4306 O  O   . HOH F .   ? 0.6569 0.6392 1.0078 -0.0616 0.1887  0.0621  1982 HOH A O   
4307 O  O   . HOH F .   ? 0.4117 0.6360 1.0749 0.1123  0.1874  -0.0919 1983 HOH A O   
4308 O  O   . HOH F .   ? 0.6746 0.7018 1.0909 0.0166  0.0479  0.0333  1984 HOH A O   
4309 O  O   . HOH F .   ? 0.6431 0.6555 0.9569 -0.0549 0.1980  0.0495  1985 HOH A O   
4310 O  O   . HOH F .   ? 0.7870 0.8250 1.0215 -0.0929 0.2168  0.0758  1986 HOH A O   
4311 O  O   . HOH F .   ? 0.6024 0.5366 0.9775 0.0174  0.1765  -0.0239 1987 HOH A O   
4312 O  O   . HOH F .   ? 0.6971 1.0745 1.4869 -0.1120 0.1543  -0.0639 1988 HOH A O   
4313 O  O   . HOH F .   ? 0.8167 0.8544 1.3000 -0.0894 0.2331  -0.0059 1989 HOH A O   
4314 O  O   . HOH F .   ? 0.6349 0.6216 1.1246 -0.1531 0.1444  -0.0372 1990 HOH A O   
4315 O  O   . HOH F .   ? 0.9760 0.8020 1.0665 0.0665  0.1290  -0.2958 1991 HOH A O   
4316 O  O   . HOH F .   ? 0.6111 0.7031 1.1798 -0.1628 0.1242  -0.0495 1992 HOH A O   
4317 O  O   . HOH G .   ? 0.7247 0.5839 1.1274 0.0324  0.1539  -0.0220 1901 HOH B O   
4318 O  O   . HOH G .   ? 0.6795 0.5026 0.9423 0.0384  0.1556  -0.0097 1902 HOH B O   
4319 O  O   . HOH G .   ? 0.7914 0.5789 1.0680 0.0030  -0.0458 -0.1637 1903 HOH B O   
4320 O  O   . HOH G .   ? 0.7512 0.4898 0.7445 0.0622  0.1085  -0.0949 1904 HOH B O   
4321 O  O   . HOH G .   ? 0.4113 0.2971 0.8079 0.0147  0.0968  -0.0526 1905 HOH B O   
4322 O  O   . HOH G .   ? 1.0588 0.7796 0.9905 0.0583  0.1103  -0.0742 1906 HOH B O   
4323 O  O   . HOH G .   ? 0.8470 0.4988 0.9194 0.1183  -0.0041 0.0210  1907 HOH B O   
4324 O  O   . HOH G .   ? 0.5178 0.3704 0.8444 0.0599  0.1244  -0.0177 1908 HOH B O   
4325 O  O   . HOH G .   ? 0.6934 0.6546 1.1225 0.0610  0.1448  -0.0392 1909 HOH B O   
4326 O  O   . HOH G .   ? 0.4468 0.3280 0.8112 0.0747  0.1146  -0.0282 1910 HOH B O   
4327 O  O   . HOH G .   ? 1.0665 0.7433 0.8739 -0.0161 0.2092  0.0359  1911 HOH B O   
4328 O  O   . HOH G .   ? 0.8571 0.5884 0.8911 0.0634  -0.0089 -0.1403 1912 HOH B O   
4329 O  O   . HOH G .   ? 0.8911 0.6287 1.1307 0.1511  0.0015  -0.0132 1913 HOH B O   
4330 O  O   . HOH G .   ? 0.8330 0.6885 1.2846 -0.0471 0.1124  -0.0125 1914 HOH B O   
4331 O  O   . HOH G .   ? 0.5087 0.4402 0.9319 0.0091  0.1595  -0.0071 1915 HOH B O   
4332 O  O   . HOH G .   ? 0.4833 0.2895 0.7428 0.0688  0.1007  -0.0127 1916 HOH B O   
4333 O  O   . HOH G .   ? 0.5583 0.4299 0.9016 0.0399  0.1453  -0.0204 1917 HOH B O   
4334 O  O   . HOH G .   ? 0.7241 0.3743 0.9159 0.0829  0.0820  0.0174  1918 HOH B O   
4335 O  O   . HOH G .   ? 0.7768 0.5855 0.9479 0.0581  0.1720  -0.0837 1919 HOH B O   
4336 O  O   . HOH G .   ? 0.6798 0.3954 0.7330 0.0650  0.0764  -0.0062 1920 HOH B O   
4337 O  O   . HOH G .   ? 0.7068 0.5939 1.0997 0.0244  0.1573  -0.0172 1921 HOH B O   
4338 O  O   . HOH G .   ? 0.7589 0.7882 1.2863 -0.0486 0.1329  -0.0242 1922 HOH B O   
4339 O  O   . HOH G .   ? 0.9830 0.4264 0.8500 0.0637  0.0226  0.1065  1923 HOH B O   
4340 O  O   . HOH G .   ? 0.4768 0.4139 0.8853 0.0518  0.1523  -0.0301 1924 HOH B O   
4341 O  O   . HOH G .   ? 0.7217 0.5350 0.9283 0.0711  0.0213  -0.0641 1925 HOH B O   
4342 O  O   . HOH G .   ? 0.7309 0.5765 0.9840 0.0581  0.1934  -0.0744 1926 HOH B O   
4343 O  O   . HOH G .   ? 1.0197 0.7590 1.0763 0.0835  0.1324  -0.1717 1927 HOH B O   
4344 O  O   . HOH G .   ? 0.7365 0.7125 1.1995 0.0076  -0.0138 -0.1043 1928 HOH B O   
4345 O  O   . HOH G .   ? 0.6855 0.4779 0.8940 0.1282  -0.0330 -0.0330 1929 HOH B O   
4346 O  O   . HOH G .   ? 0.6164 0.4213 0.8604 0.0288  0.1661  0.0032  1930 HOH B O   
4347 O  O   . HOH G .   ? 0.6488 0.5668 1.0163 0.0453  -0.0160 -0.0953 1931 HOH B O   
4348 O  O   . HOH G .   ? 1.0474 0.7854 1.4339 0.1021  0.1025  -0.0839 1932 HOH B O   
4349 O  O   . HOH G .   ? 0.7159 0.5645 0.9881 0.1152  -0.0243 -0.0506 1933 HOH B O   
4350 O  O   . HOH G .   ? 0.7710 0.4869 0.8087 0.0729  0.0521  -0.0181 1934 HOH B O   
4351 O  O   . HOH G .   ? 0.5512 0.3806 0.8122 0.0476  0.0373  -0.0849 1935 HOH B O   
4352 O  O   . HOH G .   ? 0.6012 0.4492 0.8690 0.0319  0.1884  -0.0220 1936 HOH B O   
4353 O  O   . HOH G .   ? 0.5276 0.3044 0.7363 0.0632  0.1037  -0.0054 1937 HOH B O   
4354 O  O   . HOH G .   ? 0.7177 0.6683 1.1349 0.0353  -0.0021 -0.0917 1938 HOH B O   
4355 O  O   . HOH G .   ? 0.7223 0.5324 0.9608 0.0405  0.0064  -0.1139 1939 HOH B O   
4356 O  O   . HOH G .   ? 0.7913 0.7732 1.2807 -0.0321 0.1354  -0.0186 1940 HOH B O   
4357 O  O   . HOH G .   ? 0.7662 0.5421 0.9719 0.0931  0.1624  -0.1548 1941 HOH B O   
4358 O  O   . HOH G .   ? 0.7324 0.5502 1.0577 0.0819  0.1690  -0.1015 1942 HOH B O   
4359 O  O   . HOH G .   ? 0.4109 0.6122 1.0712 -0.0333 0.0928  -0.0761 1943 HOH B O   
4360 O  O   . HOH G .   ? 0.4273 0.3190 0.7967 0.0261  0.1793  -0.0103 1944 HOH B O   
4361 O  O   . HOH G .   ? 0.7192 0.4572 0.9936 0.1290  0.0557  -0.0170 1945 HOH B O   
4362 O  O   . HOH G .   ? 0.9363 0.8274 1.3484 0.1548  0.0694  -0.0670 1946 HOH B O   
4363 O  O   . HOH G .   ? 0.6847 0.4413 0.7684 0.0623  0.1020  -0.1073 1947 HOH B O   
4364 O  O   . HOH G .   ? 0.6886 0.5026 0.9881 0.0526  0.1378  -0.0057 1948 HOH B O   
4365 O  O   . HOH G .   ? 0.8136 0.6579 1.0605 0.0206  0.2026  -0.0114 1949 HOH B O   
4366 O  O   . HOH G .   ? 1.0148 0.7427 1.1797 -0.0463 0.2065  0.0514  1950 HOH B O   
4367 O  O   . HOH G .   ? 0.6018 0.4134 0.8892 0.0357  0.1555  0.0013  1951 HOH B O   
4368 O  O   . HOH G .   ? 0.4882 0.4757 0.9679 -0.0232 0.1475  -0.0138 1952 HOH B O   
4369 O  O   . HOH G .   ? 0.5194 0.3964 0.8529 0.0398  0.1909  -0.0338 1953 HOH B O   
4370 O  O   . HOH G .   ? 0.6031 0.4442 0.8807 0.0322  0.1744  -0.0138 1954 HOH B O   
4371 O  O   . HOH G .   ? 0.7695 0.6266 1.0862 0.0247  0.1798  -0.0053 1955 HOH B O   
4372 O  O   . HOH G .   ? 0.8140 0.4105 0.8489 0.1129  0.0019  0.0415  1956 HOH B O   
4373 O  O   . HOH G .   ? 1.0135 0.7875 1.1138 0.0693  0.1509  -0.1217 1957 HOH B O   
4374 O  O   . HOH G .   ? 0.8793 0.7274 1.2123 0.0444  0.1515  -0.0101 1958 HOH B O   
4375 O  O   . HOH G .   ? 1.1096 0.8504 1.1786 0.1116  0.1626  -0.2174 1959 HOH B O   
4376 O  O   . HOH G .   ? 0.8002 0.7339 1.2267 0.1148  0.1074  -0.0600 1960 HOH B O   
4377 O  O   . HOH G .   ? 0.7909 0.6635 0.9485 0.0265  0.2555  -0.0511 1961 HOH B O   
4378 O  O   . HOH G .   ? 0.7630 0.6633 1.1425 0.0392  0.1924  -0.0274 1962 HOH B O   
4379 O  O   . HOH G .   ? 0.7893 0.6230 1.2100 0.0355  0.1405  -0.0107 1963 HOH B O   
4380 O  O   . HOH G .   ? 0.6296 0.8414 1.2646 0.0688  -0.2113 -0.1782 1964 HOH B O   
4381 O  O   . HOH G .   ? 1.5399 0.7314 1.3532 0.2880  -0.2708 0.1191  1965 HOH B O   
4382 O  O   . HOH G .   ? 0.6925 0.5549 1.1056 0.0193  0.1488  -0.0093 1966 HOH B O   
4383 O  O   . HOH G .   ? 0.6467 0.4193 0.7419 0.0592  0.1350  -0.0894 1967 HOH B O   
4384 O  O   . HOH G .   ? 0.7328 0.5728 1.0056 0.0443  0.0083  -0.0978 1968 HOH B O   
4385 O  O   . HOH G .   ? 0.5717 0.4523 0.9477 0.1432  0.0307  -0.0491 1969 HOH B O   
4386 O  O   . HOH G .   ? 0.8767 0.7475 1.1566 0.0867  -0.0333 -0.0759 1970 HOH B O   
4387 O  O   . HOH G .   ? 0.7619 0.6781 1.1575 0.1854  -0.0587 -0.0679 1971 HOH B O   
4388 O  O   . HOH G .   ? 1.3304 0.6500 1.2034 0.0604  0.0056  0.1276  1972 HOH B O   
4389 O  O   . HOH G .   ? 0.7132 0.5617 1.0283 0.0204  0.1793  -0.0002 1973 HOH B O   
4390 O  O   . HOH G .   ? 0.8217 0.6479 1.0388 0.0751  -0.0088 -0.0744 1974 HOH B O   
4391 O  O   . HOH G .   ? 0.7115 0.5928 1.0626 0.0233  0.1827  -0.0073 1975 HOH B O   
4392 O  O   . HOH G .   ? 0.5088 1.0171 1.3864 -0.0090 0.0989  -0.1387 1976 HOH B O   
4393 O  O   . HOH G .   ? 0.9775 0.6334 1.2266 0.0464  0.0477  -0.1802 1977 HOH B O   
4394 O  O   . HOH G .   ? 0.6047 0.4724 0.9154 0.0316  0.1901  -0.0217 1978 HOH B O   
4395 O  O   . HOH G .   ? 0.8518 0.6455 1.1756 0.1446  0.0487  -0.0347 1979 HOH B O   
4396 O  O   . HOH G .   ? 0.7649 0.5383 1.0435 0.0418  0.1436  0.0023  1980 HOH B O   
4397 O  O   . HOH G .   ? 0.9060 0.7061 1.1549 -0.0469 0.2178  0.0322  1981 HOH B O   
4398 O  O   . HOH G .   ? 1.1961 0.9694 1.3768 0.1288  0.1847  -0.2093 1982 HOH B O   
4399 O  O   . HOH G .   ? 0.5830 1.1227 1.5062 -0.0720 0.0845  -0.1348 1983 HOH B O   
4400 O  O   . HOH G .   ? 1.0006 0.8973 1.2197 0.0416  0.2534  -0.0670 1984 HOH B O   
4401 O  O   . HOH G .   ? 0.6444 1.2241 1.6150 0.0590  0.0000  -0.1863 1985 HOH B O   
# 
