data_9GLQ
# 
_entry.id   9GLQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9GLQ         pdb_00009glq 10.2210/pdb9glq/pdb 
WWPDB D_1292141358 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_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                        9GLQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-27 
_pdbx_database_status.SG_entry                        Y 
_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              chaikuad@pharmchem.uni-frankfurt.de 
_pdbx_contact_author.name_first         Apirat 
_pdbx_contact_author.name_last          Chaikuad 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1120-2209 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chaikuad, A.'                         1 ? 
'Strubel, A.'                          2 ? 
'Doetsch, V.'                          3 ? 
'Knapp, S.'                            4 ? 
'Structural Genomics Consortium (SGC)' 5 ? 
# 
_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            'Cell Death Dis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-4889 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                909 
_citation.page_last                 909 
_citation.title                     'DARPins as a novel tool to detect and degrade p73.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41419-024-07304-2 
_citation.pdbx_database_id_PubMed   39695090 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Munick, P.'     1  0000-0002-0548-0897 
primary 'Zielinski, J.'  2  ?                   
primary 'Strubel, A.'    3  0000-0002-8175-962X 
primary 'Gutfreund, N.'  4  ?                   
primary 'Dreier, B.'     5  ?                   
primary 'Schaefer, J.V.' 6  0000-0002-8332-4371 
primary 'Schafer, B.'    7  ?                   
primary 'Gebel, J.'      8  ?                   
primary 'Osterburg, C.'  9  ?                   
primary 'Chaikuad, A.'   10 ?                   
primary 'Knapp, S.'      11 0000-0001-5995-6494 
primary 'Pluckthun, A.'  12 0000-0003-4191-5306 
primary 'Dotsch, V.'     13 0000-0001-5720-212X 
# 
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 'Tumor protein p73' 6034.894  2  ? ? ? ? 
2 polymer     man 'Darpins 1800'      13273.813 1  ? ? ? ? 
3 non-polymer syn 'COBALT (II) ION'   58.933    1  ? ? ? ? 
4 non-polymer syn GLYCEROL            92.094    1  ? ? ? ? 
5 water       nat water               18.015    49 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'p53-like transcription factor,p53-related protein' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no GSDEDTYYLQVRGRKNFEILMKLKESLELMELVPQPLVDSYRQQQQLLQR GSDEDTYYLQVRGRKNFEILMKLKESLELMELVPQPLVDSYRQQQQLLQR A,B 
? 
2 'polypeptide(L)' no no 
;GSDLGKKLLEAAAVGQDDEVRILMANGADVNAMDQNGETPLHLAAMNGHLEIVEVLLKTGADVNASDFHGDTPLHLAAMA
GHLEIVEVLLKHGADVNAQDTWGYIPFDLAAWAGNEDIAEVLQKAA
;
;GSDLGKKLLEAAAVGQDDEVRILMANGADVNAMDQNGETPLHLAAMNGHLEIVEVLLKTGADVNASDFHGDTPLHLAAMA
GHLEIVEVLLKHGADVNAQDTWGYIPFDLAAWAGNEDIAEVLQKAA
;
C   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'COBALT (II) ION' CO  
4 GLYCEROL          GOL 
5 water             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ASP n 
1 4   GLU n 
1 5   ASP n 
1 6   THR n 
1 7   TYR n 
1 8   TYR n 
1 9   LEU n 
1 10  GLN n 
1 11  VAL n 
1 12  ARG n 
1 13  GLY n 
1 14  ARG n 
1 15  LYS n 
1 16  ASN n 
1 17  PHE n 
1 18  GLU n 
1 19  ILE n 
1 20  LEU n 
1 21  MET n 
1 22  LYS n 
1 23  LEU n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  LEU n 
1 28  GLU n 
1 29  LEU n 
1 30  MET n 
1 31  GLU n 
1 32  LEU n 
1 33  VAL n 
1 34  PRO n 
1 35  GLN n 
1 36  PRO n 
1 37  LEU n 
1 38  VAL n 
1 39  ASP n 
1 40  SER n 
1 41  TYR n 
1 42  ARG n 
1 43  GLN n 
1 44  GLN n 
1 45  GLN n 
1 46  GLN n 
1 47  LEU n 
1 48  LEU n 
1 49  GLN n 
1 50  ARG n 
2 1   GLY n 
2 2   SER n 
2 3   ASP n 
2 4   LEU n 
2 5   GLY n 
2 6   LYS n 
2 7   LYS n 
2 8   LEU n 
2 9   LEU n 
2 10  GLU n 
2 11  ALA n 
2 12  ALA n 
2 13  ALA n 
2 14  VAL n 
2 15  GLY n 
2 16  GLN n 
2 17  ASP n 
2 18  ASP n 
2 19  GLU n 
2 20  VAL n 
2 21  ARG n 
2 22  ILE n 
2 23  LEU n 
2 24  MET n 
2 25  ALA n 
2 26  ASN n 
2 27  GLY n 
2 28  ALA n 
2 29  ASP n 
2 30  VAL n 
2 31  ASN n 
2 32  ALA n 
2 33  MET n 
2 34  ASP n 
2 35  GLN n 
2 36  ASN n 
2 37  GLY n 
2 38  GLU n 
2 39  THR n 
2 40  PRO n 
2 41  LEU n 
2 42  HIS n 
2 43  LEU n 
2 44  ALA n 
2 45  ALA n 
2 46  MET n 
2 47  ASN n 
2 48  GLY n 
2 49  HIS n 
2 50  LEU n 
2 51  GLU n 
2 52  ILE n 
2 53  VAL n 
2 54  GLU n 
2 55  VAL n 
2 56  LEU n 
2 57  LEU n 
2 58  LYS n 
2 59  THR n 
2 60  GLY n 
2 61  ALA n 
2 62  ASP n 
2 63  VAL n 
2 64  ASN n 
2 65  ALA n 
2 66  SER n 
2 67  ASP n 
2 68  PHE n 
2 69  HIS n 
2 70  GLY n 
2 71  ASP n 
2 72  THR n 
2 73  PRO n 
2 74  LEU n 
2 75  HIS n 
2 76  LEU n 
2 77  ALA n 
2 78  ALA n 
2 79  MET n 
2 80  ALA n 
2 81  GLY n 
2 82  HIS n 
2 83  LEU n 
2 84  GLU n 
2 85  ILE n 
2 86  VAL n 
2 87  GLU n 
2 88  VAL n 
2 89  LEU n 
2 90  LEU n 
2 91  LYS n 
2 92  HIS n 
2 93  GLY n 
2 94  ALA n 
2 95  ASP n 
2 96  VAL n 
2 97  ASN n 
2 98  ALA n 
2 99  GLN n 
2 100 ASP n 
2 101 THR n 
2 102 TRP n 
2 103 GLY n 
2 104 TYR n 
2 105 ILE n 
2 106 PRO n 
2 107 PHE n 
2 108 ASP n 
2 109 LEU n 
2 110 ALA n 
2 111 ALA n 
2 112 TRP n 
2 113 ALA n 
2 114 GLY n 
2 115 ASN n 
2 116 GLU n 
2 117 ASP n 
2 118 ILE n 
2 119 ALA n 
2 120 GLU n 
2 121 VAL n 
2 122 LEU n 
2 123 GLN n 
2 124 LYS n 
2 125 ALA n 
2 126 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 50  human ? 'TP73, P73' ? ? ? ? ? ? 'Homo sapiens'        9606  ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 126 ?     ? ?           ? ? ? ? ? ? 'synthetic construct' 32630 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
CO  non-polymer         . 'COBALT (II) ION' ?                               'Co 2'           58.933  
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  
GOL non-polymer         . GLYCEROL          'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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   GLY 1   349 ?   ?   ?   A . n 
A 1 2   SER 2   350 ?   ?   ?   A . n 
A 1 3   ASP 3   351 ?   ?   ?   A . n 
A 1 4   GLU 4   352 352 GLU GLU A . n 
A 1 5   ASP 5   353 353 ASP ASP A . n 
A 1 6   THR 6   354 354 THR THR A . n 
A 1 7   TYR 7   355 355 TYR TYR A . n 
A 1 8   TYR 8   356 356 TYR TYR A . n 
A 1 9   LEU 9   357 357 LEU LEU A . n 
A 1 10  GLN 10  358 358 GLN GLN A . n 
A 1 11  VAL 11  359 359 VAL VAL A . n 
A 1 12  ARG 12  360 360 ARG ARG A . n 
A 1 13  GLY 13  361 361 GLY GLY A . n 
A 1 14  ARG 14  362 362 ARG ARG A . n 
A 1 15  LYS 15  363 363 LYS LYS A . n 
A 1 16  ASN 16  364 364 ASN ASN A . n 
A 1 17  PHE 17  365 365 PHE PHE A . n 
A 1 18  GLU 18  366 366 GLU GLU A . n 
A 1 19  ILE 19  367 367 ILE ILE A . n 
A 1 20  LEU 20  368 368 LEU LEU A . n 
A 1 21  MET 21  369 369 MET MET A . n 
A 1 22  LYS 22  370 370 LYS LYS A . n 
A 1 23  LEU 23  371 371 LEU LEU A . n 
A 1 24  LYS 24  372 372 LYS LYS A . n 
A 1 25  GLU 25  373 373 GLU GLU A . n 
A 1 26  SER 26  374 374 SER SER A . n 
A 1 27  LEU 27  375 375 LEU LEU A . n 
A 1 28  GLU 28  376 376 GLU GLU A . n 
A 1 29  LEU 29  377 377 LEU LEU A . n 
A 1 30  MET 30  378 378 MET MET A . n 
A 1 31  GLU 31  379 379 GLU GLU A . n 
A 1 32  LEU 32  380 380 LEU LEU A . n 
A 1 33  VAL 33  381 381 VAL VAL A . n 
A 1 34  PRO 34  382 382 PRO PRO A . n 
A 1 35  GLN 35  383 383 GLN GLN A . n 
A 1 36  PRO 36  384 384 PRO PRO A . n 
A 1 37  LEU 37  385 385 LEU LEU A . n 
A 1 38  VAL 38  386 386 VAL VAL A . n 
A 1 39  ASP 39  387 387 ASP ASP A . n 
A 1 40  SER 40  388 388 SER SER A . n 
A 1 41  TYR 41  389 389 TYR TYR A . n 
A 1 42  ARG 42  390 390 ARG ARG A . n 
A 1 43  GLN 43  391 391 GLN GLN A . n 
A 1 44  GLN 44  392 392 GLN GLN A . n 
A 1 45  GLN 45  393 393 GLN GLN A . n 
A 1 46  GLN 46  394 394 GLN GLN A . n 
A 1 47  LEU 47  395 395 LEU LEU A . n 
A 1 48  LEU 48  396 396 LEU LEU A . n 
A 1 49  GLN 49  397 397 GLN GLN A . n 
A 1 50  ARG 50  398 ?   ?   ?   A . n 
B 1 1   GLY 1   349 ?   ?   ?   B . n 
B 1 2   SER 2   350 ?   ?   ?   B . n 
B 1 3   ASP 3   351 ?   ?   ?   B . n 
B 1 4   GLU 4   352 ?   ?   ?   B . n 
B 1 5   ASP 5   353 353 ASP ASP B . n 
B 1 6   THR 6   354 354 THR THR B . n 
B 1 7   TYR 7   355 355 TYR TYR B . n 
B 1 8   TYR 8   356 356 TYR TYR B . n 
B 1 9   LEU 9   357 357 LEU LEU B . n 
B 1 10  GLN 10  358 358 GLN GLN B . n 
B 1 11  VAL 11  359 359 VAL VAL B . n 
B 1 12  ARG 12  360 360 ARG ARG B . n 
B 1 13  GLY 13  361 361 GLY GLY B . n 
B 1 14  ARG 14  362 362 ARG ARG B . n 
B 1 15  LYS 15  363 363 LYS LYS B . n 
B 1 16  ASN 16  364 364 ASN ASN B . n 
B 1 17  PHE 17  365 365 PHE PHE B . n 
B 1 18  GLU 18  366 366 GLU GLU B . n 
B 1 19  ILE 19  367 367 ILE ILE B . n 
B 1 20  LEU 20  368 368 LEU LEU B . n 
B 1 21  MET 21  369 369 MET MET B . n 
B 1 22  LYS 22  370 370 LYS LYS B . n 
B 1 23  LEU 23  371 371 LEU LEU B . n 
B 1 24  LYS 24  372 372 LYS LYS B . n 
B 1 25  GLU 25  373 373 GLU GLU B . n 
B 1 26  SER 26  374 374 SER SER B . n 
B 1 27  LEU 27  375 375 LEU LEU B . n 
B 1 28  GLU 28  376 376 GLU GLU B . n 
B 1 29  LEU 29  377 377 LEU LEU B . n 
B 1 30  MET 30  378 378 MET MET B . n 
B 1 31  GLU 31  379 379 GLU GLU B . n 
B 1 32  LEU 32  380 380 LEU LEU B . n 
B 1 33  VAL 33  381 381 VAL VAL B . n 
B 1 34  PRO 34  382 382 PRO PRO B . n 
B 1 35  GLN 35  383 383 GLN GLN B . n 
B 1 36  PRO 36  384 384 PRO PRO B . n 
B 1 37  LEU 37  385 385 LEU LEU B . n 
B 1 38  VAL 38  386 386 VAL VAL B . n 
B 1 39  ASP 39  387 387 ASP ASP B . n 
B 1 40  SER 40  388 388 SER SER B . n 
B 1 41  TYR 41  389 389 TYR TYR B . n 
B 1 42  ARG 42  390 390 ARG ARG B . n 
B 1 43  GLN 43  391 391 GLN GLN B . n 
B 1 44  GLN 44  392 392 GLN GLN B . n 
B 1 45  GLN 45  393 393 GLN GLN B . n 
B 1 46  GLN 46  394 394 GLN GLN B . n 
B 1 47  LEU 47  395 395 LEU LEU B . n 
B 1 48  LEU 48  396 396 LEU LEU B . n 
B 1 49  GLN 49  397 ?   ?   ?   B . n 
B 1 50  ARG 50  398 ?   ?   ?   B . n 
C 2 1   GLY 1   1   1   GLY GLY C . n 
C 2 2   SER 2   2   2   SER SER C . n 
C 2 3   ASP 3   3   3   ASP ASP C . n 
C 2 4   LEU 4   4   4   LEU LEU C . n 
C 2 5   GLY 5   5   5   GLY GLY C . n 
C 2 6   LYS 6   6   6   LYS LYS C . n 
C 2 7   LYS 7   7   7   LYS LYS C . n 
C 2 8   LEU 8   8   8   LEU LEU C . n 
C 2 9   LEU 9   9   9   LEU LEU C . n 
C 2 10  GLU 10  10  10  GLU GLU C . n 
C 2 11  ALA 11  11  11  ALA ALA C . n 
C 2 12  ALA 12  12  12  ALA ALA C . n 
C 2 13  ALA 13  13  13  ALA ALA C . n 
C 2 14  VAL 14  14  14  VAL VAL C . n 
C 2 15  GLY 15  15  15  GLY GLY C . n 
C 2 16  GLN 16  16  16  GLN GLN C . n 
C 2 17  ASP 17  17  17  ASP ASP C . n 
C 2 18  ASP 18  18  18  ASP ASP C . n 
C 2 19  GLU 19  19  19  GLU GLU C . n 
C 2 20  VAL 20  20  20  VAL VAL C . n 
C 2 21  ARG 21  21  21  ARG ARG C . n 
C 2 22  ILE 22  22  22  ILE ILE C . n 
C 2 23  LEU 23  23  23  LEU LEU C . n 
C 2 24  MET 24  24  24  MET MET C . n 
C 2 25  ALA 25  25  25  ALA ALA C . n 
C 2 26  ASN 26  26  26  ASN ASN C . n 
C 2 27  GLY 27  27  27  GLY GLY C . n 
C 2 28  ALA 28  28  28  ALA ALA C . n 
C 2 29  ASP 29  29  29  ASP ASP C . n 
C 2 30  VAL 30  30  30  VAL VAL C . n 
C 2 31  ASN 31  31  31  ASN ASN C . n 
C 2 32  ALA 32  32  32  ALA ALA C . n 
C 2 33  MET 33  33  33  MET MET C . n 
C 2 34  ASP 34  34  34  ASP ASP C . n 
C 2 35  GLN 35  35  35  GLN GLN C . n 
C 2 36  ASN 36  36  36  ASN ASN C . n 
C 2 37  GLY 37  37  37  GLY GLY C . n 
C 2 38  GLU 38  38  38  GLU GLU C . n 
C 2 39  THR 39  39  39  THR THR C . n 
C 2 40  PRO 40  40  40  PRO PRO C . n 
C 2 41  LEU 41  41  41  LEU LEU C . n 
C 2 42  HIS 42  42  42  HIS HIS C . n 
C 2 43  LEU 43  43  43  LEU LEU C . n 
C 2 44  ALA 44  44  44  ALA ALA C . n 
C 2 45  ALA 45  45  45  ALA ALA C . n 
C 2 46  MET 46  46  46  MET MET C . n 
C 2 47  ASN 47  47  47  ASN ASN C . n 
C 2 48  GLY 48  48  48  GLY GLY C . n 
C 2 49  HIS 49  49  49  HIS HIS C . n 
C 2 50  LEU 50  50  50  LEU LEU C . n 
C 2 51  GLU 51  51  51  GLU GLU C . n 
C 2 52  ILE 52  52  52  ILE ILE C . n 
C 2 53  VAL 53  53  53  VAL VAL C . n 
C 2 54  GLU 54  54  54  GLU GLU C . n 
C 2 55  VAL 55  55  55  VAL VAL C . n 
C 2 56  LEU 56  56  56  LEU LEU C . n 
C 2 57  LEU 57  57  57  LEU LEU C . n 
C 2 58  LYS 58  58  58  LYS LYS C . n 
C 2 59  THR 59  59  59  THR THR C . n 
C 2 60  GLY 60  60  60  GLY GLY C . n 
C 2 61  ALA 61  61  61  ALA ALA C . n 
C 2 62  ASP 62  62  62  ASP ASP C . n 
C 2 63  VAL 63  63  63  VAL VAL C . n 
C 2 64  ASN 64  64  64  ASN ASN C . n 
C 2 65  ALA 65  65  65  ALA ALA C . n 
C 2 66  SER 66  66  66  SER SER C . n 
C 2 67  ASP 67  67  67  ASP ASP C . n 
C 2 68  PHE 68  68  68  PHE PHE C . n 
C 2 69  HIS 69  69  69  HIS HIS C . n 
C 2 70  GLY 70  70  70  GLY GLY C . n 
C 2 71  ASP 71  71  71  ASP ASP C . n 
C 2 72  THR 72  72  72  THR THR C . n 
C 2 73  PRO 73  73  73  PRO PRO C . n 
C 2 74  LEU 74  74  74  LEU LEU C . n 
C 2 75  HIS 75  75  75  HIS HIS C . n 
C 2 76  LEU 76  76  76  LEU LEU C . n 
C 2 77  ALA 77  77  77  ALA ALA C . n 
C 2 78  ALA 78  78  78  ALA ALA C . n 
C 2 79  MET 79  79  79  MET MET C . n 
C 2 80  ALA 80  80  80  ALA ALA C . n 
C 2 81  GLY 81  81  81  GLY GLY C . n 
C 2 82  HIS 82  82  82  HIS HIS C . n 
C 2 83  LEU 83  83  83  LEU LEU C . n 
C 2 84  GLU 84  84  84  GLU GLU C . n 
C 2 85  ILE 85  85  85  ILE ILE C . n 
C 2 86  VAL 86  86  86  VAL VAL C . n 
C 2 87  GLU 87  87  87  GLU GLU C . n 
C 2 88  VAL 88  88  88  VAL VAL C . n 
C 2 89  LEU 89  89  89  LEU LEU C . n 
C 2 90  LEU 90  90  90  LEU LEU C . n 
C 2 91  LYS 91  91  91  LYS LYS C . n 
C 2 92  HIS 92  92  92  HIS HIS C . n 
C 2 93  GLY 93  93  93  GLY GLY C . n 
C 2 94  ALA 94  94  94  ALA ALA C . n 
C 2 95  ASP 95  95  95  ASP ASP C . n 
C 2 96  VAL 96  96  96  VAL VAL C . n 
C 2 97  ASN 97  97  97  ASN ASN C . n 
C 2 98  ALA 98  98  98  ALA ALA C . n 
C 2 99  GLN 99  99  99  GLN GLN C . n 
C 2 100 ASP 100 100 100 ASP ASP C . n 
C 2 101 THR 101 101 101 THR THR C . n 
C 2 102 TRP 102 102 102 TRP TRP C . n 
C 2 103 GLY 103 103 103 GLY GLY C . n 
C 2 104 TYR 104 104 104 TYR TYR C . n 
C 2 105 ILE 105 105 105 ILE ILE C . n 
C 2 106 PRO 106 106 106 PRO PRO C . n 
C 2 107 PHE 107 107 107 PHE PHE C . n 
C 2 108 ASP 108 108 108 ASP ASP C . n 
C 2 109 LEU 109 109 109 LEU LEU C . n 
C 2 110 ALA 110 110 110 ALA ALA C . n 
C 2 111 ALA 111 111 111 ALA ALA C . n 
C 2 112 TRP 112 112 112 TRP TRP C . n 
C 2 113 ALA 113 113 113 ALA ALA C . n 
C 2 114 GLY 114 114 114 GLY GLY C . n 
C 2 115 ASN 115 115 115 ASN ASN C . n 
C 2 116 GLU 116 116 116 GLU GLU C . n 
C 2 117 ASP 117 117 117 ASP ASP C . n 
C 2 118 ILE 118 118 118 ILE ILE C . n 
C 2 119 ALA 119 119 119 ALA ALA C . n 
C 2 120 GLU 120 120 120 GLU GLU C . n 
C 2 121 VAL 121 121 121 VAL VAL C . n 
C 2 122 LEU 122 122 122 LEU LEU C . n 
C 2 123 GLN 123 123 123 GLN GLN C . n 
C 2 124 LYS 124 124 124 LYS LYS C . n 
C 2 125 ALA 125 125 125 ALA ALA C . n 
C 2 126 ALA 126 126 126 ALA ALA C . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 3 CO  1  401 1  CO  CO  A . 
E 4 GOL 1  401 6  GOL GOL B . 
F 5 HOH 1  501 44 HOH HOH A . 
F 5 HOH 2  502 34 HOH HOH A . 
F 5 HOH 3  503 3  HOH HOH A . 
F 5 HOH 4  504 22 HOH HOH A . 
F 5 HOH 5  505 23 HOH HOH A . 
F 5 HOH 6  506 17 HOH HOH A . 
F 5 HOH 7  507 37 HOH HOH A . 
F 5 HOH 8  508 4  HOH HOH A . 
F 5 HOH 9  509 49 HOH HOH A . 
F 5 HOH 10 510 35 HOH HOH A . 
F 5 HOH 11 511 60 HOH HOH A . 
F 5 HOH 12 512 42 HOH HOH A . 
F 5 HOH 13 513 38 HOH HOH A . 
F 5 HOH 14 514 66 HOH HOH A . 
F 5 HOH 15 515 39 HOH HOH A . 
F 5 HOH 16 516 33 HOH HOH A . 
F 5 HOH 17 517 30 HOH HOH A . 
G 5 HOH 1  501 68 HOH HOH B . 
G 5 HOH 2  502 36 HOH HOH B . 
G 5 HOH 3  503 51 HOH HOH B . 
G 5 HOH 4  504 52 HOH HOH B . 
H 5 HOH 1  201 43 HOH HOH C . 
H 5 HOH 2  202 54 HOH HOH C . 
H 5 HOH 3  203 5  HOH HOH C . 
H 5 HOH 4  204 53 HOH HOH C . 
H 5 HOH 5  205 45 HOH HOH C . 
H 5 HOH 6  206 57 HOH HOH C . 
H 5 HOH 7  207 27 HOH HOH C . 
H 5 HOH 8  208 13 HOH HOH C . 
H 5 HOH 9  209 41 HOH HOH C . 
H 5 HOH 10 210 32 HOH HOH C . 
H 5 HOH 11 211 19 HOH HOH C . 
H 5 HOH 12 212 56 HOH HOH C . 
H 5 HOH 13 213 10 HOH HOH C . 
H 5 HOH 14 214 50 HOH HOH C . 
H 5 HOH 15 215 67 HOH HOH C . 
H 5 HOH 16 216 46 HOH HOH C . 
H 5 HOH 17 217 18 HOH HOH C . 
H 5 HOH 18 218 59 HOH HOH C . 
H 5 HOH 19 219 40 HOH HOH C . 
H 5 HOH 20 220 63 HOH HOH C . 
H 5 HOH 21 221 21 HOH HOH C . 
H 5 HOH 22 222 14 HOH HOH C . 
H 5 HOH 23 223 64 HOH HOH C . 
H 5 HOH 24 224 8  HOH HOH C . 
H 5 HOH 25 225 65 HOH HOH C . 
H 5 HOH 26 226 61 HOH HOH C . 
H 5 HOH 27 227 29 HOH HOH C . 
H 5 HOH 28 228 12 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLU 352 ? CG  ? A GLU 4 CG  
2 1 Y 1 A GLU 352 ? CD  ? A GLU 4 CD  
3 1 Y 1 A GLU 352 ? OE1 ? A GLU 4 OE1 
4 1 Y 1 A GLU 352 ? OE2 ? A GLU 4 OE2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9GLQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.763 
_cell.length_a_esd                 ? 
_cell.length_b                     94.816 
_cell.length_b_esd                 ? 
_cell.length_c                     96.433 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9GLQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   9GLQ 
_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             2.83 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.54 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '30% PEG2000MME, 0.15M potassium bromide' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-02-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99999 
_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 X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99999 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GLQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               48.22 
_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                                     17152 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.060 
_reflns.pdbx_Rpim_I_all                                0.022 
_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                              0.053 
_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                                    2.10 
_reflns_shell.d_res_low                                     2.17 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1653 
_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                               7.7 
_reflns_shell.pdbx_chi_squared                              1.08 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.056 
_reflns_shell.pdbx_Rpim_I_all                               0.375 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.938 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.913 
_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]                            -0.67 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            3.93 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -3.27 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               65.216 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9GLQ 
_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                            2.10 
_refine.ls_d_res_low                             47.41 
_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                     16349 
_refine.ls_number_reflns_R_free                  799 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.81 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20430 
_refine.ls_R_factor_R_free                       0.24782 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20224 
_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                    MASK 
_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                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.187 
_refine.pdbx_overall_ESU_R_Free                  0.173 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                 ? 
_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                             12.458 
_refine.overall_SU_ML                            0.155 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        47.41 
_refine_hist.number_atoms_solvent             49 
_refine_hist.number_atoms_total               1752 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1696 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         7 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
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' ? 0.007  0.013  1728 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  1621 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.189  1.631  2333 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.243  1.578  3769 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.622  5.000  213  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.252 24.891 92   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.085 15.000 311  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.501 15.000 7    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.058  0.200  215  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1924 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  313  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.895  4.247  861  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.893  4.245  860  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.993  6.344  1071 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.992  6.347  1072 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.803  4.686  867  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.801  4.691  868  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.099  6.886  1263 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.570  50.835 1928 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.560  50.666 1919 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             67 
_refine_ls_shell.number_reflns_R_work             1183 
_refine_ls_shell.percent_reflns_obs               99.92 
_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                  0.288 
_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   20 
_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                  0.362 
# 
_struct.entry_id                     9GLQ 
_struct.title                        'Crystal structure of p73 tetramerisation domain in complex with darpins 1800' 
_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        9GLQ 
_struct_keywords.text            
'TP73, tetramerisation domain, darpins, Structural Genomics, Structural Genomics Consortium, SGC, DNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'DNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP P73_HUMAN O15350 ? 1 DEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQR 351 
2 PDB 9GLQ      9GLQ   ? 2 ?                                                1   
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9GLQ A 3 ? 50  ? O15350 351 ? 398 ? 351 398 
2 1 9GLQ B 3 ? 50  ? O15350 351 ? 398 ? 351 398 
3 2 9GLQ C 1 ? 126 ? 9GLQ   1   ? 126 ? 1   126 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GLQ GLY A 1  ? UNP O15350 ?   ?   'expression tag' 349 1 
1 9GLQ SER A 2  ? UNP O15350 ?   ?   'expression tag' 350 2 
1 9GLQ LYS A 15 ? UNP O15350 GLU 363 conflict         363 3 
2 9GLQ GLY B 1  ? UNP O15350 ?   ?   'expression tag' 349 4 
2 9GLQ SER B 2  ? UNP O15350 ?   ?   'expression tag' 350 5 
2 9GLQ LYS B 15 ? UNP O15350 GLU 363 conflict         363 6 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13350 ? 
1 MORE         -106  ? 
1 'SSA (A^2)'  19980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_556 -x,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 96.4330000000 
# 
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 GLY A 13  ? GLU A 31  ? GLY A 361 GLU A 379 1 ? 19 
HELX_P HELX_P2  AA2 PRO A 34  ? GLN A 49  ? PRO A 382 GLN A 397 1 ? 16 
HELX_P HELX_P3  AA3 GLY B 13  ? MET B 30  ? GLY B 361 MET B 378 1 ? 18 
HELX_P HELX_P4  AA4 GLU B 31  ? VAL B 33  ? GLU B 379 VAL B 381 5 ? 3  
HELX_P HELX_P5  AA5 PRO B 34  ? GLN B 46  ? PRO B 382 GLN B 394 1 ? 13 
HELX_P HELX_P6  AA6 SER C 2   ? GLY C 15  ? SER C 2   GLY C 15  1 ? 14 
HELX_P HELX_P7  AA7 GLN C 16  ? ASN C 26  ? GLN C 16  ASN C 26  1 ? 11 
HELX_P HELX_P8  AA8 THR C 39  ? ASN C 47  ? THR C 39  ASN C 47  1 ? 9  
HELX_P HELX_P9  AA9 HIS C 49  ? THR C 59  ? HIS C 49  THR C 59  1 ? 11 
HELX_P HELX_P10 AB1 THR C 72  ? GLY C 81  ? THR C 72  GLY C 81  1 ? 10 
HELX_P HELX_P11 AB2 HIS C 82  ? HIS C 92  ? HIS C 82  HIS C 92  1 ? 11 
HELX_P HELX_P12 AB3 ILE C 105 ? GLY C 114 ? ILE C 105 GLY C 114 1 ? 10 
HELX_P HELX_P13 AB4 ASN C 115 ? ALA C 126 ? ASN C 115 ALA C 126 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A LYS 15 NZ  ? ? ? 1_555 D CO  .  CO  ? ? A LYS 363 A CO  401 1_555 ? ? ? ? ? ? ? 2.004 ? ? 
metalc2 metalc ? ? A GLU 18 OE1 ? ? ? 1_555 D CO  .  CO  ? ? A GLU 366 A CO  401 1_555 ? ? ? ? ? ? ? 1.890 ? ? 
metalc3 metalc ? ? D CO  .  CO  ? ? ? 1_555 F HOH .  O   ? ? A CO  401 A HOH 503 1_555 ? ? ? ? ? ? ? 2.116 ? ? 
metalc4 metalc ? ? D CO  .  CO  ? ? ? 1_555 F HOH .  O   ? ? A CO  401 A HOH 508 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc5 metalc ? ? D CO  .  CO  ? ? ? 6_554 C ASP 29 OD1 ? ? A CO  401 C ASP 29  1_555 ? ? ? ? ? ? ? 2.065 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NZ  ? A LYS 15 ? A LYS 363 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 OE1 ? A GLU 18 ? A GLU 366 ? 1_555 162.9 ? 
2  NZ  ? A LYS 15 ? A LYS 363 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 O   ? F HOH .  ? A HOH 503 ? 1_555 96.7  ? 
3  OE1 ? A GLU 18 ? A GLU 366 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 O   ? F HOH .  ? A HOH 503 ? 1_555 89.6  ? 
4  NZ  ? A LYS 15 ? A LYS 363 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 O   ? F HOH .  ? A HOH 508 ? 1_555 75.2  ? 
5  OE1 ? A GLU 18 ? A GLU 366 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 O   ? F HOH .  ? A HOH 508 ? 1_555 98.4  ? 
6  O   ? F HOH .  ? A HOH 503 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 O   ? F HOH .  ? A HOH 508 ? 1_555 171.8 ? 
7  NZ  ? A LYS 15 ? A LYS 363 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 OD1 ? C ASP 29 ? C ASP 29  ? 1_555 131.4 ? 
8  OE1 ? A GLU 18 ? A GLU 366 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 OD1 ? C ASP 29 ? C ASP 29  ? 1_555 45.8  ? 
9  O   ? F HOH .  ? A HOH 503 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 OD1 ? C ASP 29 ? C ASP 29  ? 1_555 131.8 ? 
10 O   ? F HOH .  ? A HOH 508 ? 1_555 CO ? D CO . ? A CO 401 ? 1_555 OD1 ? C ASP 29 ? C ASP 29  ? 1_555 56.3  ? 
# 
_pdbx_entry_details.entry_id                   9GLQ 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLN B 394 ? ? -54.34  -4.02 
2 1 HIS C 49  ? ? -100.67 78.94 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          ? 
_pdbx_SG_project.full_name_of_center   'Structural Genomics Consortium' 
_pdbx_SG_project.initial_of_center     SGC 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 6.3674  27.4076 44.1971 0.2776 ? 0.0377 ? -0.0021 ? 0.1984 ? 0.0010  ? 0.0647 ? 0.8057 ? -0.0795 ? 
-0.4142 ? 0.7646 ? 0.0894 ? 1.4532 ? -0.1850 ? -0.0707 ? 0.1643  ? 0.0111  ? 0.1014 ? -0.0757 ? 0.1657 ? 0.1925 ? 0.0836 ? 
2 'X-RAY DIFFRACTION' ? refined 6.9329  23.9211 46.3179 0.3058 ? 0.0364 ? 0.0337  ? 0.1652 ? -0.0053 ? 0.0120 ? 3.5637 ? 0.3510  ? 
-0.4176 ? 0.3817 ? 0.5491 ? 4.1496 ? -0.3598 ? 0.1326  ? -0.0360 ? -0.0904 ? 0.2046 ? -0.0187 ? 0.5353 ? 0.3615 ? 0.1552 ? 
3 'X-RAY DIFFRACTION' ? refined 21.8985 11.8809 27.6360 0.2862 ? 0.1157 ? 0.0783  ? 0.1254 ? 0.0369  ? 0.0588 ? 1.3662 ? -0.5056 ? 
-1.9255 ? 0.7832 ? 1.2284 ? 6.7538 ? -0.2769 ? -0.1319 ? -0.0411 ? 0.1272  ? 0.1444 ? -0.0498 ? 0.6890 ? 0.3346 ? 0.1325 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1 'X-RAY DIFFRACTION' 1 ? ? A 352 ? ? ? A 397 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 353 ? ? ? B 396 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? C 1   ? ? ? C 126 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 349 ? A GLY 1  
2  1 Y 1 A SER 350 ? A SER 2  
3  1 Y 1 A ASP 351 ? A ASP 3  
4  1 Y 1 A ARG 398 ? A ARG 50 
5  1 Y 1 B GLY 349 ? B GLY 1  
6  1 Y 1 B SER 350 ? B SER 2  
7  1 Y 1 B ASP 351 ? B ASP 3  
8  1 Y 1 B GLU 352 ? B GLU 4  
9  1 Y 1 B GLN 397 ? B GLN 49 
10 1 Y 1 B ARG 398 ? B ARG 50 
# 
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  
CO  CO   CO N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
GOL C1   C  N N 124 
GOL O1   O  N N 125 
GOL C2   C  N N 126 
GOL O2   O  N N 127 
GOL C3   C  N N 128 
GOL O3   O  N N 129 
GOL H11  H  N N 130 
GOL H12  H  N N 131 
GOL HO1  H  N N 132 
GOL H2   H  N N 133 
GOL HO2  H  N N 134 
GOL H31  H  N N 135 
GOL H32  H  N N 136 
GOL HO3  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
GOL C1  O1   sing N N 116 
GOL C1  C2   sing N N 117 
GOL C1  H11  sing N N 118 
GOL C1  H12  sing N N 119 
GOL O1  HO1  sing N N 120 
GOL C2  O2   sing N N 121 
GOL C2  C3   sing N N 122 
GOL C2  H2   sing N N 123 
GOL O2  HO2  sing N N 124 
GOL C3  O3   sing N N 125 
GOL C3  H31  sing N N 126 
GOL C3  H32  sing N N 127 
GOL O3  HO3  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.entity_id_list 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
_pdbx_initial_refinement_model.details 
1 ? 'experimental model' PDB 5hob ? 
2 ? 'experimental model' PDB 6fp7 ? 
# 
_atom_sites.entry_id                    9GLQ 
_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]   0.015933 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010547 
_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]   0.010370 
_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  
CO 
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   . GLU A 1 4   ? 6.440   38.199 33.394 1.00 92.76  ? 352 GLU A N   1 
ATOM   2    C  CA  . GLU A 1 4   ? 7.249   39.061 34.310 1.00 92.49  ? 352 GLU A CA  1 
ATOM   3    C  C   . GLU A 1 4   ? 6.340   40.076 35.019 1.00 91.80  ? 352 GLU A C   1 
ATOM   4    O  O   . GLU A 1 4   ? 6.884   40.995 35.659 1.00 98.48  ? 352 GLU A O   1 
ATOM   5    C  CB  . GLU A 1 4   ? 8.353   39.777 33.525 1.00 92.83  ? 352 GLU A CB  1 
ATOM   6    N  N   . ASP A 1 5   ? 5.015   39.904 34.927 1.00 87.11  ? 353 ASP A N   1 
ATOM   7    C  CA  . ASP A 1 5   ? 3.995   40.857 35.444 1.00 83.04  ? 353 ASP A CA  1 
ATOM   8    C  C   . ASP A 1 5   ? 3.732   40.541 36.928 1.00 79.07  ? 353 ASP A C   1 
ATOM   9    O  O   . ASP A 1 5   ? 3.754   39.349 37.301 1.00 75.28  ? 353 ASP A O   1 
ATOM   10   C  CB  . ASP A 1 5   ? 2.729   40.790 34.585 1.00 86.10  ? 353 ASP A CB  1 
ATOM   11   C  CG  . ASP A 1 5   ? 2.013   42.116 34.394 1.00 88.89  ? 353 ASP A CG  1 
ATOM   12   O  OD1 . ASP A 1 5   ? 2.623   43.173 34.679 1.00 96.91  ? 353 ASP A OD1 1 
ATOM   13   O  OD2 . ASP A 1 5   ? 0.855   42.077 33.942 1.00 88.86  ? 353 ASP A OD2 1 
ATOM   14   N  N   . THR A 1 6   ? 3.511   41.574 37.740 1.00 73.02  ? 354 THR A N   1 
ATOM   15   C  CA  . THR A 1 6   ? 3.533   41.517 39.222 1.00 71.89  ? 354 THR A CA  1 
ATOM   16   C  C   . THR A 1 6   ? 2.111   41.669 39.762 1.00 68.67  ? 354 THR A C   1 
ATOM   17   O  O   . THR A 1 6   ? 1.448   42.663 39.419 1.00 67.45  ? 354 THR A O   1 
ATOM   18   C  CB  . THR A 1 6   ? 4.459   42.594 39.800 1.00 75.02  ? 354 THR A CB  1 
ATOM   19   O  OG1 . THR A 1 6   ? 5.797   42.293 39.403 1.00 79.11  ? 354 THR A OG1 1 
ATOM   20   C  CG2 . THR A 1 6   ? 4.398   42.674 41.307 1.00 76.17  ? 354 THR A CG2 1 
ATOM   21   N  N   . TYR A 1 7   ? 1.675   40.725 40.597 1.00 64.74  ? 355 TYR A N   1 
ATOM   22   C  CA  . TYR A 1 7   ? 0.332   40.720 41.219 1.00 63.71  ? 355 TYR A CA  1 
ATOM   23   C  C   . TYR A 1 7   ? 0.496   40.830 42.728 1.00 64.62  ? 355 TYR A C   1 
ATOM   24   O  O   . TYR A 1 7   ? 1.559   40.461 43.264 1.00 66.75  ? 355 TYR A O   1 
ATOM   25   C  CB  . TYR A 1 7   ? -0.455  39.475 40.811 1.00 60.96  ? 355 TYR A CB  1 
ATOM   26   C  CG  . TYR A 1 7   ? -0.782  39.406 39.345 1.00 59.78  ? 355 TYR A CG  1 
ATOM   27   C  CD1 . TYR A 1 7   ? 0.104   38.835 38.453 1.00 57.36  ? 355 TYR A CD1 1 
ATOM   28   C  CD2 . TYR A 1 7   ? -1.977  39.909 38.845 1.00 59.20  ? 355 TYR A CD2 1 
ATOM   29   C  CE1 . TYR A 1 7   ? -0.176  38.764 37.104 1.00 57.36  ? 355 TYR A CE1 1 
ATOM   30   C  CE2 . TYR A 1 7   ? -2.275  39.841 37.494 1.00 58.26  ? 355 TYR A CE2 1 
ATOM   31   C  CZ  . TYR A 1 7   ? -1.369  39.266 36.621 1.00 58.34  ? 355 TYR A CZ  1 
ATOM   32   O  OH  . TYR A 1 7   ? -1.626  39.196 35.283 1.00 59.41  ? 355 TYR A OH  1 
ATOM   33   N  N   . TYR A 1 8   ? -0.519  41.376 43.380 1.00 67.92  ? 356 TYR A N   1 
ATOM   34   C  CA  . TYR A 1 8   ? -0.557  41.596 44.842 1.00 72.57  ? 356 TYR A CA  1 
ATOM   35   C  C   . TYR A 1 8   ? -1.692  40.750 45.409 1.00 70.30  ? 356 TYR A C   1 
ATOM   36   O  O   . TYR A 1 8   ? -2.780  40.748 44.806 1.00 72.45  ? 356 TYR A O   1 
ATOM   37   C  CB  . TYR A 1 8   ? -0.680  43.091 45.136 1.00 78.09  ? 356 TYR A CB  1 
ATOM   38   C  CG  . TYR A 1 8   ? 0.439   43.913 44.547 1.00 85.10  ? 356 TYR A CG  1 
ATOM   39   C  CD1 . TYR A 1 8   ? 1.617   44.131 45.250 1.00 87.83  ? 356 TYR A CD1 1 
ATOM   40   C  CD2 . TYR A 1 8   ? 0.342   44.435 43.264 1.00 88.34  ? 356 TYR A CD2 1 
ATOM   41   C  CE1 . TYR A 1 8   ? 2.658   44.867 44.705 1.00 91.19  ? 356 TYR A CE1 1 
ATOM   42   C  CE2 . TYR A 1 8   ? 1.371   45.177 42.706 1.00 91.97  ? 356 TYR A CE2 1 
ATOM   43   C  CZ  . TYR A 1 8   ? 2.533   45.391 43.428 1.00 94.79  ? 356 TYR A CZ  1 
ATOM   44   O  OH  . TYR A 1 8   ? 3.544   46.122 42.873 1.00 102.14 ? 356 TYR A OH  1 
ATOM   45   N  N   . LEU A 1 9   ? -1.395  39.967 46.447 1.00 67.90  ? 357 LEU A N   1 
ATOM   46   C  CA  . LEU A 1 9   ? -2.397  39.242 47.271 1.00 65.00  ? 357 LEU A CA  1 
ATOM   47   C  C   . LEU A 1 9   ? -2.451  39.901 48.636 1.00 63.30  ? 357 LEU A C   1 
ATOM   48   O  O   . LEU A 1 9   ? -1.394  40.287 49.154 1.00 64.10  ? 357 LEU A O   1 
ATOM   49   C  CB  . LEU A 1 9   ? -2.018  37.771 47.453 1.00 64.23  ? 357 LEU A CB  1 
ATOM   50   C  CG  . LEU A 1 9   ? -2.016  36.912 46.202 1.00 64.08  ? 357 LEU A CG  1 
ATOM   51   C  CD1 . LEU A 1 9   ? -0.748  37.150 45.409 1.00 65.76  ? 357 LEU A CD1 1 
ATOM   52   C  CD2 . LEU A 1 9   ? -2.158  35.437 46.558 1.00 63.27  ? 357 LEU A CD2 1 
ATOM   53   N  N   . GLN A 1 10  ? -3.644  39.981 49.189 1.00 63.01  ? 358 GLN A N   1 
ATOM   54   C  CA  . GLN A 1 10  ? -3.900  40.345 50.594 1.00 63.15  ? 358 GLN A CA  1 
ATOM   55   C  C   . GLN A 1 10  ? -4.284  39.053 51.316 1.00 60.45  ? 358 GLN A C   1 
ATOM   56   O  O   . GLN A 1 10  ? -5.094  38.286 50.750 1.00 56.53  ? 358 GLN A O   1 
ATOM   57   C  CB  . GLN A 1 10  ? -4.994  41.407 50.620 1.00 67.79  ? 358 GLN A CB  1 
ATOM   58   C  CG  . GLN A 1 10  ? -5.344  41.906 52.005 1.00 72.53  ? 358 GLN A CG  1 
ATOM   59   C  CD  . GLN A 1 10  ? -6.381  42.997 51.922 1.00 76.06  ? 358 GLN A CD  1 
ATOM   60   O  OE1 . GLN A 1 10  ? -7.094  43.117 50.930 1.00 79.74  ? 358 GLN A OE1 1 
ATOM   61   N  NE2 . GLN A 1 10  ? -6.456  43.820 52.957 1.00 78.12  ? 358 GLN A NE2 1 
ATOM   62   N  N   . VAL A 1 11  ? -3.665  38.789 52.465 1.00 58.31  ? 359 VAL A N   1 
ATOM   63   C  CA  . VAL A 1 11  ? -3.869  37.555 53.274 1.00 59.50  ? 359 VAL A CA  1 
ATOM   64   C  C   . VAL A 1 11  ? -4.230  37.974 54.698 1.00 59.07  ? 359 VAL A C   1 
ATOM   65   O  O   . VAL A 1 11  ? -3.508  38.807 55.250 1.00 57.59  ? 359 VAL A O   1 
ATOM   66   C  CB  . VAL A 1 11  ? -2.604  36.677 53.263 1.00 60.99  ? 359 VAL A CB  1 
ATOM   67   C  CG1 . VAL A 1 11  ? -2.784  35.403 54.064 1.00 61.70  ? 359 VAL A CG1 1 
ATOM   68   C  CG2 . VAL A 1 11  ? -2.175  36.357 51.845 1.00 64.92  ? 359 VAL A CG2 1 
ATOM   69   N  N   . ARG A 1 12  ? -5.296  37.391 55.253 1.00 60.16  ? 360 ARG A N   1 
ATOM   70   C  CA  . ARG A 1 12  ? -5.684  37.521 56.677 1.00 63.68  ? 360 ARG A CA  1 
ATOM   71   C  C   . ARG A 1 12  ? -5.083  36.352 57.462 1.00 58.58  ? 360 ARG A C   1 
ATOM   72   O  O   . ARG A 1 12  ? -5.313  35.179 57.079 1.00 56.71  ? 360 ARG A O   1 
ATOM   73   C  CB  . ARG A 1 12  ? -7.208  37.560 56.815 1.00 72.21  ? 360 ARG A CB  1 
ATOM   74   C  CG  . ARG A 1 12  ? -7.711  38.508 57.896 1.00 82.88  ? 360 ARG A CG  1 
ATOM   75   C  CD  . ARG A 1 12  ? -9.173  38.889 57.706 1.00 91.85  ? 360 ARG A CD  1 
ATOM   76   N  NE  . ARG A 1 12  ? -10.031 37.720 57.527 1.00 99.62  ? 360 ARG A NE  1 
ATOM   77   C  CZ  . ARG A 1 12  ? -11.348 37.758 57.324 1.00 105.41 ? 360 ARG A CZ  1 
ATOM   78   N  NH1 . ARG A 1 12  ? -11.990 38.914 57.277 1.00 107.28 ? 360 ARG A NH1 1 
ATOM   79   N  NH2 . ARG A 1 12  ? -12.022 36.630 57.174 1.00 107.86 ? 360 ARG A NH2 1 
ATOM   80   N  N   . GLY A 1 13  ? -4.318  36.671 58.504 1.00 57.14  ? 361 GLY A N   1 
ATOM   81   C  CA  . GLY A 1 13  ? -3.832  35.703 59.500 1.00 55.48  ? 361 GLY A CA  1 
ATOM   82   C  C   . GLY A 1 13  ? -2.387  35.345 59.230 1.00 54.39  ? 361 GLY A C   1 
ATOM   83   O  O   . GLY A 1 13  ? -2.054  35.051 58.064 1.00 50.67  ? 361 GLY A O   1 
ATOM   84   N  N   . ARG A 1 14  ? -1.555  35.438 60.265 1.00 50.44  ? 362 ARG A N   1 
ATOM   85   C  CA  . ARG A 1 14  ? -0.091  35.261 60.187 1.00 49.13  ? 362 ARG A CA  1 
ATOM   86   C  C   . ARG A 1 14  ? 0.192   33.874 59.631 1.00 45.46  ? 362 ARG A C   1 
ATOM   87   O  O   . ARG A 1 14  ? 1.112   33.772 58.857 1.00 43.64  ? 362 ARG A O   1 
ATOM   88   C  CB  . ARG A 1 14  ? 0.567   35.447 61.568 1.00 50.25  ? 362 ARG A CB  1 
ATOM   89   C  CG  . ARG A 1 14  ? 2.056   35.117 61.597 1.00 50.61  ? 362 ARG A CG  1 
ATOM   90   C  CD  . ARG A 1 14  ? 2.931   36.138 60.880 1.00 50.34  ? 362 ARG A CD  1 
ATOM   91   N  NE  . ARG A 1 14  ? 4.245   35.606 60.541 1.00 50.42  ? 362 ARG A NE  1 
ATOM   92   C  CZ  . ARG A 1 14  ? 5.195   36.284 59.902 1.00 50.87  ? 362 ARG A CZ  1 
ATOM   93   N  NH1 . ARG A 1 14  ? 4.985   37.542 59.557 1.00 51.99  ? 362 ARG A NH1 1 
ATOM   94   N  NH2 . ARG A 1 14  ? 6.356   35.710 59.618 1.00 49.36  ? 362 ARG A NH2 1 
ATOM   95   N  N   . LYS A 1 15  ? -0.518  32.843 60.103 1.00 45.05  ? 363 LYS A N   1 
ATOM   96   C  CA  . LYS A 1 15  ? -0.249  31.440 59.715 1.00 47.48  ? 363 LYS A CA  1 
ATOM   97   C  C   . LYS A 1 15  ? -0.558  31.282 58.215 1.00 45.08  ? 363 LYS A C   1 
ATOM   98   O  O   . LYS A 1 15  ? 0.130   30.526 57.567 1.00 44.48  ? 363 LYS A O   1 
ATOM   99   C  CB  . LYS A 1 15  ? -1.035  30.448 60.577 1.00 51.91  ? 363 LYS A CB  1 
ATOM   100  C  CG  . LYS A 1 15  ? -0.611  30.393 62.053 1.00 59.55  ? 363 LYS A CG  1 
ATOM   101  C  CD  . LYS A 1 15  ? 0.876   30.070 62.278 1.00 63.87  ? 363 LYS A CD  1 
ATOM   102  C  CE  . LYS A 1 15  ? 1.150   28.683 62.840 1.00 70.11  ? 363 LYS A CE  1 
ATOM   103  N  NZ  . LYS A 1 15  ? 2.513   28.581 63.431 1.00 68.44  ? 363 LYS A NZ  1 
ATOM   104  N  N   . ASN A 1 16  ? -1.551  31.995 57.694 1.00 43.39  ? 364 ASN A N   1 
ATOM   105  C  CA  . ASN A 1 16  ? -1.881  31.948 56.248 1.00 43.51  ? 364 ASN A CA  1 
ATOM   106  C  C   . ASN A 1 16  ? -0.762  32.631 55.466 1.00 42.88  ? 364 ASN A C   1 
ATOM   107  O  O   . ASN A 1 16  ? -0.364  32.076 54.412 1.00 45.02  ? 364 ASN A O   1 
ATOM   108  C  CB  . ASN A 1 16  ? -3.257  32.544 55.967 1.00 43.20  ? 364 ASN A CB  1 
ATOM   109  C  CG  . ASN A 1 16  ? -4.364  31.663 56.500 1.00 44.19  ? 364 ASN A CG  1 
ATOM   110  O  OD1 . ASN A 1 16  ? -4.212  30.437 56.571 1.00 44.42  ? 364 ASN A OD1 1 
ATOM   111  N  ND2 . ASN A 1 16  ? -5.464  32.280 56.894 1.00 43.58  ? 364 ASN A ND2 1 
ATOM   112  N  N   . PHE A 1 17  ? -0.253  33.765 55.963 1.00 41.46  ? 365 PHE A N   1 
ATOM   113  C  CA  . PHE A 1 17  ? 0.873   34.494 55.335 1.00 42.65  ? 365 PHE A CA  1 
ATOM   114  C  C   . PHE A 1 17  ? 2.103   33.577 55.256 1.00 42.60  ? 365 PHE A C   1 
ATOM   115  O  O   . PHE A 1 17  ? 2.711   33.461 54.192 1.00 41.40  ? 365 PHE A O   1 
ATOM   116  C  CB  . PHE A 1 17  ? 1.164   35.800 56.062 1.00 43.75  ? 365 PHE A CB  1 
ATOM   117  C  CG  . PHE A 1 17  ? 2.405   36.514 55.597 1.00 45.02  ? 365 PHE A CG  1 
ATOM   118  C  CD1 . PHE A 1 17  ? 2.426   37.180 54.382 1.00 46.26  ? 365 PHE A CD1 1 
ATOM   119  C  CD2 . PHE A 1 17  ? 3.547   36.523 56.375 1.00 45.99  ? 365 PHE A CD2 1 
ATOM   120  C  CE1 . PHE A 1 17  ? 3.567   37.856 53.966 1.00 47.08  ? 365 PHE A CE1 1 
ATOM   121  C  CE2 . PHE A 1 17  ? 4.690   37.185 55.956 1.00 47.46  ? 365 PHE A CE2 1 
ATOM   122  C  CZ  . PHE A 1 17  ? 4.697   37.857 54.755 1.00 48.38  ? 365 PHE A CZ  1 
ATOM   123  N  N   . GLU A 1 18  ? 2.464   32.942 56.354 1.00 43.35  ? 366 GLU A N   1 
ATOM   124  C  CA  . GLU A 1 18  ? 3.623   32.021 56.417 1.00 44.02  ? 366 GLU A CA  1 
ATOM   125  C  C   . GLU A 1 18  ? 3.480   30.914 55.362 1.00 43.26  ? 366 GLU A C   1 
ATOM   126  O  O   . GLU A 1 18  ? 4.444   30.660 54.663 1.00 44.39  ? 366 GLU A O   1 
ATOM   127  C  CB  . GLU A 1 18  ? 3.737   31.410 57.802 1.00 44.98  ? 366 GLU A CB  1 
ATOM   128  C  CG  . GLU A 1 18  ? 4.205   32.407 58.846 1.00 47.14  ? 366 GLU A CG  1 
ATOM   129  C  CD  . GLU A 1 18  ? 4.050   31.950 60.289 1.00 46.15  ? 366 GLU A CD  1 
ATOM   130  O  OE1 . GLU A 1 18  ? 3.843   30.741 60.533 1.00 53.25  ? 366 GLU A OE1 1 
ATOM   131  O  OE2 . GLU A 1 18  ? 4.152   32.823 61.172 1.00 48.38  ? 366 GLU A OE2 1 
ATOM   132  N  N   . ILE A 1 19  ? 2.334   30.248 55.296 1.00 42.83  ? 367 ILE A N   1 
ATOM   133  C  CA  . ILE A 1 19  ? 2.107   29.131 54.332 1.00 43.96  ? 367 ILE A CA  1 
ATOM   134  C  C   . ILE A 1 19  ? 2.278   29.671 52.911 1.00 41.24  ? 367 ILE A C   1 
ATOM   135  O  O   . ILE A 1 19  ? 3.026   29.071 52.137 1.00 39.25  ? 367 ILE A O   1 
ATOM   136  C  CB  . ILE A 1 19  ? 0.728   28.479 54.540 1.00 46.78  ? 367 ILE A CB  1 
ATOM   137  C  CG1 . ILE A 1 19  ? 0.670   27.735 55.875 1.00 49.83  ? 367 ILE A CG1 1 
ATOM   138  C  CG2 . ILE A 1 19  ? 0.403   27.556 53.372 1.00 50.22  ? 367 ILE A CG2 1 
ATOM   139  C  CD1 . ILE A 1 19  ? -0.722  27.594 56.457 1.00 51.55  ? 367 ILE A CD1 1 
ATOM   140  N  N   . LEU A 1 20  ? 1.615   30.778 52.598 1.00 40.49  ? 368 LEU A N   1 
ATOM   141  C  CA  . LEU A 1 20  ? 1.597   31.347 51.232 1.00 40.47  ? 368 LEU A CA  1 
ATOM   142  C  C   . LEU A 1 20  ? 2.980   31.884 50.864 1.00 40.91  ? 368 LEU A C   1 
ATOM   143  O  O   . LEU A 1 20  ? 3.368   31.704 49.711 1.00 40.49  ? 368 LEU A O   1 
ATOM   144  C  CB  . LEU A 1 20  ? 0.516   32.430 51.139 1.00 40.56  ? 368 LEU A CB  1 
ATOM   145  C  CG  . LEU A 1 20  ? -0.910  31.900 51.174 1.00 40.93  ? 368 LEU A CG  1 
ATOM   146  C  CD1 . LEU A 1 20  ? -1.900  33.038 51.295 1.00 41.56  ? 368 LEU A CD1 1 
ATOM   147  C  CD2 . LEU A 1 20  ? -1.205  31.050 49.941 1.00 41.57  ? 368 LEU A CD2 1 
ATOM   148  N  N   . MET A 1 21  ? 3.714   32.485 51.801 1.00 41.82  ? 369 MET A N   1 
ATOM   149  C  CA  . MET A 1 21  ? 5.083   32.991 51.526 1.00 43.23  ? 369 MET A CA  1 
ATOM   150  C  C   . MET A 1 21  ? 6.005   31.817 51.183 1.00 44.29  ? 369 MET A C   1 
ATOM   151  O  O   . MET A 1 21  ? 6.826   31.948 50.277 1.00 43.81  ? 369 MET A O   1 
ATOM   152  C  CB  . MET A 1 21  ? 5.661   33.759 52.710 1.00 44.31  ? 369 MET A CB  1 
ATOM   153  C  CG  . MET A 1 21  ? 5.122   35.147 52.820 1.00 46.78  ? 369 MET A CG  1 
ATOM   154  S  SD  . MET A 1 21  ? 5.487   36.129 51.328 1.00 48.27  ? 369 MET A SD  1 
ATOM   155  C  CE  . MET A 1 21  ? 7.223   36.503 51.537 1.00 48.13  ? 369 MET A CE  1 
ATOM   156  N  N   . LYS A 1 22  ? 5.864   30.713 51.891 1.00 45.66  ? 370 LYS A N   1 
ATOM   157  C  CA  . LYS A 1 22  ? 6.652   29.483 51.657 1.00 47.66  ? 370 LYS A CA  1 
ATOM   158  C  C   . LYS A 1 22  ? 6.385   28.983 50.226 1.00 45.98  ? 370 LYS A C   1 
ATOM   159  O  O   . LYS A 1 22  ? 7.342   28.732 49.477 1.00 43.50  ? 370 LYS A O   1 
ATOM   160  C  CB  . LYS A 1 22  ? 6.291   28.475 52.754 1.00 49.88  ? 370 LYS A CB  1 
ATOM   161  C  CG  . LYS A 1 22  ? 6.912   27.101 52.596 1.00 53.88  ? 370 LYS A CG  1 
ATOM   162  C  CD  . LYS A 1 22  ? 8.395   27.145 52.486 1.00 57.64  ? 370 LYS A CD  1 
ATOM   163  C  CE  . LYS A 1 22  ? 9.044   25.806 52.759 1.00 60.75  ? 370 LYS A CE  1 
ATOM   164  N  NZ  . LYS A 1 22  ? 10.102  25.529 51.752 1.00 63.31  ? 370 LYS A NZ  1 
ATOM   165  N  N   . LEU A 1 23  ? 5.123   28.869 49.841 1.00 45.21  ? 371 LEU A N   1 
ATOM   166  C  CA  . LEU A 1 23  ? 4.753   28.378 48.495 1.00 45.16  ? 371 LEU A CA  1 
ATOM   167  C  C   . LEU A 1 23  ? 5.201   29.403 47.447 1.00 44.99  ? 371 LEU A C   1 
ATOM   168  O  O   . LEU A 1 23  ? 5.701   28.977 46.395 1.00 41.96  ? 371 LEU A O   1 
ATOM   169  C  CB  . LEU A 1 23  ? 3.252   28.122 48.448 1.00 45.04  ? 371 LEU A CB  1 
ATOM   170  C  CG  . LEU A 1 23  ? 2.782   27.066 49.440 1.00 47.87  ? 371 LEU A CG  1 
ATOM   171  C  CD1 . LEU A 1 23  ? 1.276   27.031 49.512 1.00 48.18  ? 371 LEU A CD1 1 
ATOM   172  C  CD2 . LEU A 1 23  ? 3.342   25.708 49.077 1.00 50.91  ? 371 LEU A CD2 1 
ATOM   173  N  N   . LYS A 1 24  ? 5.002   30.693 47.707 1.00 44.19  ? 372 LYS A N   1 
ATOM   174  C  CA  . LYS A 1 24  ? 5.351   31.742 46.726 1.00 46.92  ? 372 LYS A CA  1 
ATOM   175  C  C   . LYS A 1 24  ? 6.846   31.627 46.447 1.00 47.12  ? 372 LYS A C   1 
ATOM   176  O  O   . LYS A 1 24  ? 7.244   31.642 45.260 1.00 44.38  ? 372 LYS A O   1 
ATOM   177  C  CB  . LYS A 1 24  ? 4.984   33.136 47.222 1.00 48.31  ? 372 LYS A CB  1 
ATOM   178  C  CG  . LYS A 1 24  ? 5.500   34.273 46.352 1.00 51.72  ? 372 LYS A CG  1 
ATOM   179  C  CD  . LYS A 1 24  ? 5.348   35.624 47.013 1.00 57.21  ? 372 LYS A CD  1 
ATOM   180  C  CE  . LYS A 1 24  ? 6.620   36.444 47.007 1.00 59.71  ? 372 LYS A CE  1 
ATOM   181  N  NZ  . LYS A 1 24  ? 7.575   35.943 48.011 1.00 64.16  ? 372 LYS A NZ  1 
ATOM   182  N  N   . GLU A 1 25  ? 7.635   31.475 47.511 1.00 46.35  ? 373 GLU A N   1 
ATOM   183  C  CA  . GLU A 1 25  ? 9.108   31.410 47.420 1.00 48.12  ? 373 GLU A CA  1 
ATOM   184  C  C   . GLU A 1 25  ? 9.503   30.201 46.574 1.00 47.54  ? 373 GLU A C   1 
ATOM   185  O  O   . GLU A 1 25  ? 10.375  30.364 45.679 1.00 46.57  ? 373 GLU A O   1 
ATOM   186  C  CB  . GLU A 1 25  ? 9.741   31.340 48.803 1.00 50.31  ? 373 GLU A CB  1 
ATOM   187  C  CG  . GLU A 1 25  ? 11.192  30.960 48.743 1.00 52.02  ? 373 GLU A CG  1 
ATOM   188  C  CD  . GLU A 1 25  ? 11.849  30.937 50.101 1.00 54.65  ? 373 GLU A CD  1 
ATOM   189  O  OE1 . GLU A 1 25  ? 11.972  32.033 50.732 1.00 56.85  ? 373 GLU A OE1 1 
ATOM   190  O  OE2 . GLU A 1 25  ? 12.195  29.829 50.541 1.00 56.01  ? 373 GLU A OE2 1 
ATOM   191  N  N   . SER A 1 26  ? 8.883   29.050 46.829 1.00 44.77  ? 374 SER A N   1 
ATOM   192  C  CA  . SER A 1 26  ? 9.155   27.793 46.104 1.00 45.55  ? 374 SER A CA  1 
ATOM   193  C  C   . SER A 1 26  ? 8.817   27.974 44.603 1.00 46.32  ? 374 SER A C   1 
ATOM   194  O  O   . SER A 1 26  ? 9.620   27.539 43.754 1.00 45.99  ? 374 SER A O   1 
ATOM   195  C  CB  . SER A 1 26  ? 8.423   26.639 46.746 1.00 46.39  ? 374 SER A CB  1 
ATOM   196  O  OG  . SER A 1 26  ? 7.040   26.658 46.424 1.00 48.33  ? 374 SER A OG  1 
ATOM   197  N  N   . LEU A 1 27  ? 7.723   28.655 44.273 1.00 43.81  ? 375 LEU A N   1 
ATOM   198  C  CA  . LEU A 1 27  ? 7.296   28.842 42.862 1.00 46.35  ? 375 LEU A CA  1 
ATOM   199  C  C   . LEU A 1 27  ? 8.257   29.788 42.145 1.00 47.48  ? 375 LEU A C   1 
ATOM   200  O  O   . LEU A 1 27  ? 8.613   29.493 41.023 1.00 48.35  ? 375 LEU A O   1 
ATOM   201  C  CB  . LEU A 1 27  ? 5.872   29.383 42.825 1.00 45.09  ? 375 LEU A CB  1 
ATOM   202  C  CG  . LEU A 1 27  ? 4.797   28.361 43.163 1.00 44.14  ? 375 LEU A CG  1 
ATOM   203  C  CD1 . LEU A 1 27  ? 3.499   29.069 43.476 1.00 43.17  ? 375 LEU A CD1 1 
ATOM   204  C  CD2 . LEU A 1 27  ? 4.626   27.362 42.026 1.00 45.73  ? 375 LEU A CD2 1 
ATOM   205  N  N   . GLU A 1 28  ? 8.686   30.858 42.801 1.00 47.45  ? 376 GLU A N   1 
ATOM   206  C  CA  . GLU A 1 28  ? 9.581   31.865 42.198 1.00 49.59  ? 376 GLU A CA  1 
ATOM   207  C  C   . GLU A 1 28  ? 10.998  31.284 42.080 1.00 50.47  ? 376 GLU A C   1 
ATOM   208  O  O   . GLU A 1 28  ? 11.607  31.436 41.004 1.00 50.92  ? 376 GLU A O   1 
ATOM   209  C  CB  . GLU A 1 28  ? 9.497   33.164 42.986 1.00 50.82  ? 376 GLU A CB  1 
ATOM   210  C  CG  . GLU A 1 28  ? 8.202   33.908 42.721 1.00 53.81  ? 376 GLU A CG  1 
ATOM   211  C  CD  . GLU A 1 28  ? 8.139   35.316 43.289 1.00 55.21  ? 376 GLU A CD  1 
ATOM   212  O  OE1 . GLU A 1 28  ? 9.045   35.674 44.053 1.00 59.06  ? 376 GLU A OE1 1 
ATOM   213  O  OE2 . GLU A 1 28  ? 7.175   36.037 42.979 1.00 56.75  ? 376 GLU A OE2 1 
ATOM   214  N  N   . LEU A 1 29  ? 11.482  30.593 43.101 1.00 50.33  ? 377 LEU A N   1 
ATOM   215  C  CA  . LEU A 1 29  ? 12.840  29.990 43.090 1.00 53.65  ? 377 LEU A CA  1 
ATOM   216  C  C   . LEU A 1 29  ? 12.903  28.849 42.069 1.00 54.39  ? 377 LEU A C   1 
ATOM   217  O  O   . LEU A 1 29  ? 13.956  28.675 41.474 1.00 54.98  ? 377 LEU A O   1 
ATOM   218  C  CB  . LEU A 1 29  ? 13.209  29.495 44.489 1.00 54.15  ? 377 LEU A CB  1 
ATOM   219  C  CG  . LEU A 1 29  ? 13.572  30.593 45.479 1.00 55.85  ? 377 LEU A CG  1 
ATOM   220  C  CD1 . LEU A 1 29  ? 13.877  30.011 46.850 1.00 56.60  ? 377 LEU A CD1 1 
ATOM   221  C  CD2 . LEU A 1 29  ? 14.743  31.413 44.968 1.00 57.61  ? 377 LEU A CD2 1 
ATOM   222  N  N   . MET A 1 30  ? 11.817  28.103 41.893 1.00 55.54  ? 378 MET A N   1 
ATOM   223  C  CA  . MET A 1 30  ? 11.740  26.981 40.930 1.00 56.72  ? 378 MET A CA  1 
ATOM   224  C  C   . MET A 1 30  ? 12.036  27.502 39.520 1.00 56.40  ? 378 MET A C   1 
ATOM   225  O  O   . MET A 1 30  ? 12.580  26.747 38.723 1.00 53.80  ? 378 MET A O   1 
ATOM   226  C  CB  . MET A 1 30  ? 10.355  26.349 40.939 1.00 59.13  ? 378 MET A CB  1 
ATOM   227  C  CG  . MET A 1 30  ? 10.353  24.957 40.407 1.00 63.30  ? 378 MET A CG  1 
ATOM   228  S  SD  . MET A 1 30  ? 8.713   24.456 39.888 1.00 66.68  ? 378 MET A SD  1 
ATOM   229  C  CE  . MET A 1 30  ? 8.896   24.693 38.118 1.00 65.12  ? 378 MET A CE  1 
ATOM   230  N  N   . GLU A 1 31  ? 11.734  28.769 39.261 1.00 55.49  ? 379 GLU A N   1 
ATOM   231  C  CA  . GLU A 1 31  ? 11.901  29.407 37.936 1.00 56.63  ? 379 GLU A CA  1 
ATOM   232  C  C   . GLU A 1 31  ? 13.386  29.574 37.604 1.00 56.19  ? 379 GLU A C   1 
ATOM   233  O  O   . GLU A 1 31  ? 13.688  29.771 36.423 1.00 56.32  ? 379 GLU A O   1 
ATOM   234  C  CB  . GLU A 1 31  ? 11.159  30.740 37.905 1.00 59.79  ? 379 GLU A CB  1 
ATOM   235  C  CG  . GLU A 1 31  ? 9.650   30.561 37.867 1.00 63.05  ? 379 GLU A CG  1 
ATOM   236  C  CD  . GLU A 1 31  ? 8.840   31.848 37.938 1.00 68.21  ? 379 GLU A CD  1 
ATOM   237  O  OE1 . GLU A 1 31  ? 9.402   32.926 37.649 1.00 71.64  ? 379 GLU A OE1 1 
ATOM   238  O  OE2 . GLU A 1 31  ? 7.651   31.771 38.297 1.00 71.46  ? 379 GLU A OE2 1 
ATOM   239  N  N   . LEU A 1 32  ? 14.273  29.511 38.598 1.00 53.95  ? 380 LEU A N   1 
ATOM   240  C  CA  . LEU A 1 32  ? 15.739  29.619 38.397 1.00 54.42  ? 380 LEU A CA  1 
ATOM   241  C  C   . LEU A 1 32  ? 16.296  28.272 37.924 1.00 53.63  ? 380 LEU A C   1 
ATOM   242  O  O   . LEU A 1 32  ? 17.433  28.247 37.427 1.00 52.03  ? 380 LEU A O   1 
ATOM   243  C  CB  . LEU A 1 32  ? 16.400  30.049 39.708 1.00 55.69  ? 380 LEU A CB  1 
ATOM   244  C  CG  . LEU A 1 32  ? 15.935  31.394 40.261 1.00 55.92  ? 380 LEU A CG  1 
ATOM   245  C  CD1 . LEU A 1 32  ? 16.822  31.833 41.409 1.00 57.24  ? 380 LEU A CD1 1 
ATOM   246  C  CD2 . LEU A 1 32  ? 15.910  32.454 39.166 1.00 56.47  ? 380 LEU A CD2 1 
ATOM   247  N  N   . VAL A 1 33  ? 15.540  27.192 38.106 1.00 49.93  ? 381 VAL A N   1 
ATOM   248  C  CA  . VAL A 1 33  ? 16.022  25.818 37.809 1.00 50.95  ? 381 VAL A CA  1 
ATOM   249  C  C   . VAL A 1 33  ? 15.968  25.622 36.292 1.00 49.27  ? 381 VAL A C   1 
ATOM   250  O  O   . VAL A 1 33  ? 14.907  25.749 35.678 1.00 49.82  ? 381 VAL A O   1 
ATOM   251  C  CB  . VAL A 1 33  ? 15.223  24.740 38.560 1.00 49.85  ? 381 VAL A CB  1 
ATOM   252  C  CG1 . VAL A 1 33  ? 15.763  23.351 38.256 1.00 50.73  ? 381 VAL A CG1 1 
ATOM   253  C  CG2 . VAL A 1 33  ? 15.204  24.984 40.065 1.00 50.07  ? 381 VAL A CG2 1 
ATOM   254  N  N   . PRO A 1 34  ? 17.105  25.303 35.646 1.00 49.47  ? 382 PRO A N   1 
ATOM   255  C  CA  . PRO A 1 34  ? 17.125  25.063 34.204 1.00 49.07  ? 382 PRO A CA  1 
ATOM   256  C  C   . PRO A 1 34  ? 16.077  24.028 33.791 1.00 46.95  ? 382 PRO A C   1 
ATOM   257  O  O   . PRO A 1 34  ? 15.874  23.067 34.504 1.00 47.34  ? 382 PRO A O   1 
ATOM   258  C  CB  . PRO A 1 34  ? 18.549  24.551 33.964 1.00 51.06  ? 382 PRO A CB  1 
ATOM   259  C  CG  . PRO A 1 34  ? 19.348  25.215 35.045 1.00 51.47  ? 382 PRO A CG  1 
ATOM   260  C  CD  . PRO A 1 34  ? 18.439  25.146 36.258 1.00 51.04  ? 382 PRO A CD  1 
ATOM   261  N  N   . GLN A 1 35  ? 15.438  24.248 32.656 1.00 45.94  ? 383 GLN A N   1 
ATOM   262  C  CA  . GLN A 1 35  ? 14.286  23.433 32.205 1.00 46.38  ? 383 GLN A CA  1 
ATOM   263  C  C   . GLN A 1 35  ? 14.688  21.961 32.125 1.00 46.60  ? 383 GLN A C   1 
ATOM   264  O  O   . GLN A 1 35  ? 13.867  21.089 32.409 1.00 47.19  ? 383 GLN A O   1 
ATOM   265  C  CB  . GLN A 1 35  ? 13.747  23.965 30.875 1.00 46.68  ? 383 GLN A CB  1 
ATOM   266  C  CG  . GLN A 1 35  ? 12.398  23.380 30.485 1.00 47.87  ? 383 GLN A CG  1 
ATOM   267  C  CD  . GLN A 1 35  ? 11.344  23.736 31.510 1.00 49.40  ? 383 GLN A CD  1 
ATOM   268  O  OE1 . GLN A 1 35  ? 11.251  24.875 31.935 1.00 50.54  ? 383 GLN A OE1 1 
ATOM   269  N  NE2 . GLN A 1 35  ? 10.538  22.766 31.913 1.00 48.78  ? 383 GLN A NE2 1 
ATOM   270  N  N   . PRO A 1 36  ? 15.925  21.608 31.690 1.00 48.30  ? 384 PRO A N   1 
ATOM   271  C  CA  . PRO A 1 36  ? 16.289  20.201 31.550 1.00 48.44  ? 384 PRO A CA  1 
ATOM   272  C  C   . PRO A 1 36  ? 16.243  19.464 32.895 1.00 47.95  ? 384 PRO A C   1 
ATOM   273  O  O   . PRO A 1 36  ? 15.839  18.327 32.909 1.00 47.23  ? 384 PRO A O   1 
ATOM   274  C  CB  . PRO A 1 36  ? 17.695  20.248 30.927 1.00 50.35  ? 384 PRO A CB  1 
ATOM   275  C  CG  . PRO A 1 36  ? 17.727  21.584 30.217 1.00 50.35  ? 384 PRO A CG  1 
ATOM   276  C  CD  . PRO A 1 36  ? 16.959  22.503 31.142 1.00 49.38  ? 384 PRO A CD  1 
ATOM   277  N  N   . LEU A 1 37  ? 16.594  20.140 33.988 1.00 47.88  ? 385 LEU A N   1 
ATOM   278  C  CA  . LEU A 1 37  ? 16.484  19.565 35.354 1.00 49.31  ? 385 LEU A CA  1 
ATOM   279  C  C   . LEU A 1 37  ? 15.011  19.471 35.743 1.00 48.27  ? 385 LEU A C   1 
ATOM   280  O  O   . LEU A 1 37  ? 14.616  18.414 36.240 1.00 47.96  ? 385 LEU A O   1 
ATOM   281  C  CB  . LEU A 1 37  ? 17.300  20.397 36.342 1.00 50.11  ? 385 LEU A CB  1 
ATOM   282  C  CG  . LEU A 1 37  ? 18.788  20.460 36.020 1.00 53.43  ? 385 LEU A CG  1 
ATOM   283  C  CD1 . LEU A 1 37  ? 19.565  21.113 37.145 1.00 55.00  ? 385 LEU A CD1 1 
ATOM   284  C  CD2 . LEU A 1 37  ? 19.339  19.073 35.713 1.00 55.04  ? 385 LEU A CD2 1 
ATOM   285  N  N   . VAL A 1 38  ? 14.205  20.479 35.417 1.00 48.10  ? 386 VAL A N   1 
ATOM   286  C  CA  . VAL A 1 38  ? 12.736  20.416 35.657 1.00 48.31  ? 386 VAL A CA  1 
ATOM   287  C  C   . VAL A 1 38  ? 12.161  19.219 34.884 1.00 48.55  ? 386 VAL A C   1 
ATOM   288  O  O   . VAL A 1 38  ? 11.409  18.441 35.474 1.00 49.13  ? 386 VAL A O   1 
ATOM   289  C  CB  . VAL A 1 38  ? 12.019  21.726 35.291 1.00 47.90  ? 386 VAL A CB  1 
ATOM   290  C  CG1 . VAL A 1 38  ? 10.532  21.620 35.566 1.00 47.61  ? 386 VAL A CG1 1 
ATOM   291  C  CG2 . VAL A 1 38  ? 12.606  22.910 36.036 1.00 49.42  ? 386 VAL A CG2 1 
ATOM   292  N  N   . ASP A 1 39  ? 12.524  19.048 33.621 1.00 48.76  ? 387 ASP A N   1 
ATOM   293  C  CA  . ASP A 1 39  ? 11.945  17.974 32.769 1.00 49.32  ? 387 ASP A CA  1 
ATOM   294  C  C   . ASP A 1 39  ? 12.426  16.602 33.250 1.00 49.54  ? 387 ASP A C   1 
ATOM   295  O  O   . ASP A 1 39  ? 11.652  15.631 33.124 1.00 50.58  ? 387 ASP A O   1 
ATOM   296  C  CB  . ASP A 1 39  ? 12.281  18.197 31.298 1.00 49.77  ? 387 ASP A CB  1 
ATOM   297  C  CG  . ASP A 1 39  ? 11.645  19.453 30.736 1.00 50.60  ? 387 ASP A CG  1 
ATOM   298  O  OD1 . ASP A 1 39  ? 10.681  19.949 31.355 1.00 53.73  ? 387 ASP A OD1 1 
ATOM   299  O  OD2 . ASP A 1 39  ? 12.148  19.946 29.718 1.00 53.60  ? 387 ASP A OD2 1 
ATOM   300  N  N   . SER A 1 40  ? 13.673  16.519 33.714 1.00 49.25  ? 388 SER A N   1 
ATOM   301  C  CA  . SER A 1 40  ? 14.271  15.304 34.327 1.00 51.53  ? 388 SER A CA  1 
ATOM   302  C  C   . SER A 1 40  ? 13.482  14.937 35.584 1.00 52.34  ? 388 SER A C   1 
ATOM   303  O  O   . SER A 1 40  ? 13.112  13.764 35.750 1.00 52.13  ? 388 SER A O   1 
ATOM   304  C  CB  . SER A 1 40  ? 15.726  15.501 34.635 1.00 51.31  ? 388 SER A CB  1 
ATOM   305  O  OG  . SER A 1 40  ? 16.489  15.549 33.444 1.00 52.44  ? 388 SER A OG  1 
ATOM   306  N  N   . TYR A 1 41  ? 13.204  15.913 36.430 1.00 54.77  ? 389 TYR A N   1 
ATOM   307  C  CA  . TYR A 1 41  ? 12.383  15.707 37.645 1.00 55.16  ? 389 TYR A CA  1 
ATOM   308  C  C   . TYR A 1 41  ? 11.011  15.160 37.222 1.00 56.35  ? 389 TYR A C   1 
ATOM   309  O  O   . TYR A 1 41  ? 10.581  14.144 37.791 1.00 57.24  ? 389 TYR A O   1 
ATOM   310  C  CB  . TYR A 1 41  ? 12.292  16.995 38.455 1.00 54.11  ? 389 TYR A CB  1 
ATOM   311  C  CG  . TYR A 1 41  ? 11.309  16.931 39.589 1.00 55.28  ? 389 TYR A CG  1 
ATOM   312  C  CD1 . TYR A 1 41  ? 9.984   17.284 39.393 1.00 55.14  ? 389 TYR A CD1 1 
ATOM   313  C  CD2 . TYR A 1 41  ? 11.701  16.522 40.855 1.00 55.42  ? 389 TYR A CD2 1 
ATOM   314  C  CE1 . TYR A 1 41  ? 9.069   17.236 40.424 1.00 54.82  ? 389 TYR A CE1 1 
ATOM   315  C  CE2 . TYR A 1 41  ? 10.793  16.463 41.897 1.00 56.41  ? 389 TYR A CE2 1 
ATOM   316  C  CZ  . TYR A 1 41  ? 9.472   16.815 41.676 1.00 55.37  ? 389 TYR A CZ  1 
ATOM   317  O  OH  . TYR A 1 41  ? 8.565   16.778 42.687 1.00 58.89  ? 389 TYR A OH  1 
ATOM   318  N  N   . ARG A 1 42  ? 10.375  15.774 36.219 1.00 55.34  ? 390 ARG A N   1 
ATOM   319  C  CA  . ARG A 1 42  ? 9.028   15.360 35.732 1.00 56.69  ? 390 ARG A CA  1 
ATOM   320  C  C   . ARG A 1 42  ? 9.065   13.946 35.149 1.00 58.46  ? 390 ARG A C   1 
ATOM   321  O  O   . ARG A 1 42  ? 8.082   13.215 35.365 1.00 60.71  ? 390 ARG A O   1 
ATOM   322  C  CB  . ARG A 1 42  ? 8.477   16.365 34.729 1.00 56.48  ? 390 ARG A CB  1 
ATOM   323  C  CG  . ARG A 1 42  ? 8.011   17.636 35.409 1.00 56.84  ? 390 ARG A CG  1 
ATOM   324  C  CD  . ARG A 1 42  ? 7.528   18.673 34.439 1.00 58.75  ? 390 ARG A CD  1 
ATOM   325  N  NE  . ARG A 1 42  ? 7.159   19.857 35.187 1.00 58.98  ? 390 ARG A NE  1 
ATOM   326  C  CZ  . ARG A 1 42  ? 7.063   21.064 34.673 1.00 57.96  ? 390 ARG A CZ  1 
ATOM   327  N  NH1 . ARG A 1 42  ? 7.334   21.261 33.397 1.00 57.06  ? 390 ARG A NH1 1 
ATOM   328  N  NH2 . ARG A 1 42  ? 6.736   22.084 35.446 1.00 55.79  ? 390 ARG A NH2 1 
ATOM   329  N  N   . GLN A 1 43  ? 10.147  13.558 34.467 1.00 58.87  ? 391 GLN A N   1 
ATOM   330  C  CA  . GLN A 1 43  ? 10.347  12.153 34.005 1.00 61.15  ? 391 GLN A CA  1 
ATOM   331  C  C   . GLN A 1 43  ? 10.319  11.224 35.217 1.00 63.03  ? 391 GLN A C   1 
ATOM   332  O  O   . GLN A 1 43  ? 9.681   10.169 35.146 1.00 63.28  ? 391 GLN A O   1 
ATOM   333  C  CB  . GLN A 1 43  ? 11.669  11.988 33.257 1.00 60.46  ? 391 GLN A CB  1 
ATOM   334  C  CG  . GLN A 1 43  ? 11.598  12.491 31.830 1.00 61.15  ? 391 GLN A CG  1 
ATOM   335  C  CD  . GLN A 1 43  ? 10.749  11.575 30.980 1.00 62.25  ? 391 GLN A CD  1 
ATOM   336  O  OE1 . GLN A 1 43  ? 11.030  10.384 30.842 1.00 64.35  ? 391 GLN A OE1 1 
ATOM   337  N  NE2 . GLN A 1 43  ? 9.685   12.123 30.419 1.00 60.42  ? 391 GLN A NE2 1 
ATOM   338  N  N   . GLN A 1 44  ? 11.021  11.607 36.280 1.00 65.79  ? 392 GLN A N   1 
ATOM   339  C  CA  . GLN A 1 44  ? 11.131  10.807 37.523 1.00 68.35  ? 392 GLN A CA  1 
ATOM   340  C  C   . GLN A 1 44  ? 9.742   10.651 38.149 1.00 68.48  ? 392 GLN A C   1 
ATOM   341  O  O   . GLN A 1 44  ? 9.443   9.542  38.621 1.00 71.32  ? 392 GLN A O   1 
ATOM   342  C  CB  . GLN A 1 44  ? 12.115  11.443 38.501 1.00 68.93  ? 392 GLN A CB  1 
ATOM   343  C  CG  . GLN A 1 44  ? 12.703  10.427 39.471 1.00 71.78  ? 392 GLN A CG  1 
ATOM   344  C  CD  . GLN A 1 44  ? 12.765  10.926 40.891 1.00 70.54  ? 392 GLN A CD  1 
ATOM   345  O  OE1 . GLN A 1 44  ? 12.231  11.983 41.233 1.00 72.92  ? 392 GLN A OE1 1 
ATOM   346  N  NE2 . GLN A 1 44  ? 13.433  10.160 41.733 1.00 74.30  ? 392 GLN A NE2 1 
ATOM   347  N  N   . GLN A 1 45  ? 8.935   11.719 38.142 1.00 70.12  ? 393 GLN A N   1 
ATOM   348  C  CA  . GLN A 1 45  ? 7.558   11.738 38.711 1.00 71.79  ? 393 GLN A CA  1 
ATOM   349  C  C   . GLN A 1 45  ? 6.700   10.772 37.913 1.00 73.97  ? 393 GLN A C   1 
ATOM   350  O  O   . GLN A 1 45  ? 5.993   9.968  38.529 1.00 75.32  ? 393 GLN A O   1 
ATOM   351  C  CB  . GLN A 1 45  ? 6.925   13.133 38.662 1.00 69.87  ? 393 GLN A CB  1 
ATOM   352  C  CG  . GLN A 1 45  ? 7.632   14.158 39.527 1.00 68.49  ? 393 GLN A CG  1 
ATOM   353  C  CD  . GLN A 1 45  ? 8.065   13.579 40.852 1.00 69.78  ? 393 GLN A CD  1 
ATOM   354  O  OE1 . GLN A 1 45  ? 7.257   13.375 41.756 1.00 67.75  ? 393 GLN A OE1 1 
ATOM   355  N  NE2 . GLN A 1 45  ? 9.354   13.306 40.970 1.00 71.59  ? 393 GLN A NE2 1 
ATOM   356  N  N   . GLN A 1 46  ? 6.808   10.843 36.589 1.00 76.71  ? 394 GLN A N   1 
ATOM   357  C  CA  . GLN A 1 46  ? 6.088   9.956  35.644 1.00 80.87  ? 394 GLN A CA  1 
ATOM   358  C  C   . GLN A 1 46  ? 6.426   8.493  35.957 1.00 83.08  ? 394 GLN A C   1 
ATOM   359  O  O   . GLN A 1 46  ? 5.498   7.670  35.895 1.00 86.42  ? 394 GLN A O   1 
ATOM   360  C  CB  . GLN A 1 46  ? 6.443   10.328 34.207 1.00 81.60  ? 394 GLN A CB  1 
ATOM   361  C  CG  . GLN A 1 46  ? 5.386   9.916  33.201 1.00 84.09  ? 394 GLN A CG  1 
ATOM   362  C  CD  . GLN A 1 46  ? 5.903   10.008 31.788 1.00 87.59  ? 394 GLN A CD  1 
ATOM   363  O  OE1 . GLN A 1 46  ? 5.328   10.689 30.942 1.00 91.95  ? 394 GLN A OE1 1 
ATOM   364  N  NE2 . GLN A 1 46  ? 7.009   9.328  31.525 1.00 86.57  ? 394 GLN A NE2 1 
ATOM   365  N  N   . LEU A 1 47  ? 7.688   8.195  36.307 1.00 85.50  ? 395 LEU A N   1 
ATOM   366  C  CA  . LEU A 1 47  ? 8.178   6.817  36.623 1.00 89.12  ? 395 LEU A CA  1 
ATOM   367  C  C   . LEU A 1 47  ? 7.546   6.320  37.931 1.00 93.97  ? 395 LEU A C   1 
ATOM   368  O  O   . LEU A 1 47  ? 7.208   5.128  38.002 1.00 96.31  ? 395 LEU A O   1 
ATOM   369  C  CB  . LEU A 1 47  ? 9.709   6.803  36.735 1.00 88.80  ? 395 LEU A CB  1 
ATOM   370  C  CG  . LEU A 1 47  ? 10.490  6.821  35.416 1.00 88.81  ? 395 LEU A CG  1 
ATOM   371  C  CD1 . LEU A 1 47  ? 11.989  6.719  35.676 1.00 88.23  ? 395 LEU A CD1 1 
ATOM   372  C  CD2 . LEU A 1 47  ? 10.038  5.704  34.483 1.00 89.08  ? 395 LEU A CD2 1 
ATOM   373  N  N   . LEU A 1 48  ? 7.420   7.195  38.932 1.00 97.58  ? 396 LEU A N   1 
ATOM   374  C  CA  . LEU A 1 48  ? 6.866   6.857  40.272 1.00 97.77  ? 396 LEU A CA  1 
ATOM   375  C  C   . LEU A 1 48  ? 5.346   6.651  40.172 1.00 101.35 ? 396 LEU A C   1 
ATOM   376  O  O   . LEU A 1 48  ? 4.843   5.741  40.854 1.00 110.01 ? 396 LEU A O   1 
ATOM   377  C  CB  . LEU A 1 48  ? 7.223   7.970  41.261 1.00 94.19  ? 396 LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 48  ? 8.713   8.121  41.569 1.00 93.00  ? 396 LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 48  ? 9.011   9.495  42.145 1.00 92.38  ? 396 LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 48  ? 9.191   7.033  42.521 1.00 92.33  ? 396 LEU A CD2 1 
ATOM   381  N  N   . GLN A 1 49  ? 4.650   7.455  39.354 1.00 102.01 ? 397 GLN A N   1 
ATOM   382  C  CA  . GLN A 1 49  ? 3.181   7.350  39.108 1.00 100.48 ? 397 GLN A CA  1 
ATOM   383  C  C   . GLN A 1 49  ? 2.942   6.741  37.722 1.00 97.52  ? 397 GLN A C   1 
ATOM   384  O  O   . GLN A 1 49  ? 3.420   5.656  37.422 1.00 94.36  ? 397 GLN A O   1 
ATOM   385  C  CB  . GLN A 1 49  ? 2.504   8.721  39.218 1.00 101.00 ? 397 GLN A CB  1 
ATOM   386  C  CG  . GLN A 1 49  ? 2.606   9.566  37.952 1.00 102.55 ? 397 GLN A CG  1 
ATOM   387  C  CD  . GLN A 1 49  ? 2.061   10.964 38.129 1.00 102.27 ? 397 GLN A CD  1 
ATOM   388  O  OE1 . GLN A 1 49  ? 1.366   11.263 39.098 1.00 101.29 ? 397 GLN A OE1 1 
ATOM   389  N  NE2 . GLN A 1 49  ? 2.367   11.834 37.179 1.00 102.53 ? 397 GLN A NE2 1 
ATOM   390  N  N   . ASP B 1 5   ? 11.204  8.812  55.340 1.00 112.71 ? 353 ASP B N   1 
ATOM   391  C  CA  . ASP B 1 5   ? 11.338  10.245 54.929 1.00 109.86 ? 353 ASP B CA  1 
ATOM   392  C  C   . ASP B 1 5   ? 10.497  10.523 53.665 1.00 106.63 ? 353 ASP B C   1 
ATOM   393  O  O   . ASP B 1 5   ? 10.374  11.719 53.300 1.00 106.94 ? 353 ASP B O   1 
ATOM   394  C  CB  . ASP B 1 5   ? 12.810  10.619 54.725 1.00 111.80 ? 353 ASP B CB  1 
ATOM   395  C  CG  . ASP B 1 5   ? 13.111  12.084 55.001 1.00 109.97 ? 353 ASP B CG  1 
ATOM   396  O  OD1 . ASP B 1 5   ? 12.877  12.525 56.143 1.00 109.02 ? 353 ASP B OD1 1 
ATOM   397  O  OD2 . ASP B 1 5   ? 13.566  12.775 54.069 1.00 110.71 ? 353 ASP B OD2 1 
ATOM   398  N  N   . THR B 1 6   ? 9.960   9.477  53.015 1.00 103.97 ? 354 THR B N   1 
ATOM   399  C  CA  . THR B 1 6   ? 8.913   9.569  51.957 1.00 100.17 ? 354 THR B CA  1 
ATOM   400  C  C   . THR B 1 6   ? 7.543   9.274  52.571 1.00 97.40  ? 354 THR B C   1 
ATOM   401  O  O   . THR B 1 6   ? 7.305   8.122  52.963 1.00 99.15  ? 354 THR B O   1 
ATOM   402  C  CB  . THR B 1 6   ? 9.183   8.617  50.785 1.00 103.69 ? 354 THR B CB  1 
ATOM   403  O  OG1 . THR B 1 6   ? 10.194  9.211  49.971 1.00 104.26 ? 354 THR B OG1 1 
ATOM   404  C  CG2 . THR B 1 6   ? 7.960   8.347  49.933 1.00 103.08 ? 354 THR B CG2 1 
ATOM   405  N  N   . TYR B 1 7   ? 6.671   10.280 52.601 1.00 92.53  ? 355 TYR B N   1 
ATOM   406  C  CA  . TYR B 1 7   ? 5.269   10.182 53.075 1.00 89.86  ? 355 TYR B CA  1 
ATOM   407  C  C   . TYR B 1 7   ? 4.355   10.169 51.853 1.00 87.14  ? 355 TYR B C   1 
ATOM   408  O  O   . TYR B 1 7   ? 4.760   10.656 50.776 1.00 84.08  ? 355 TYR B O   1 
ATOM   409  C  CB  . TYR B 1 7   ? 4.932   11.331 54.027 1.00 86.44  ? 355 TYR B CB  1 
ATOM   410  C  CG  . TYR B 1 7   ? 5.959   11.564 55.104 1.00 88.13  ? 355 TYR B CG  1 
ATOM   411  C  CD1 . TYR B 1 7   ? 7.176   12.157 54.808 1.00 88.23  ? 355 TYR B CD1 1 
ATOM   412  C  CD2 . TYR B 1 7   ? 5.719   11.196 56.418 1.00 92.21  ? 355 TYR B CD2 1 
ATOM   413  C  CE1 . TYR B 1 7   ? 8.130   12.378 55.785 1.00 90.61  ? 355 TYR B CE1 1 
ATOM   414  C  CE2 . TYR B 1 7   ? 6.662   11.410 57.411 1.00 94.60  ? 355 TYR B CE2 1 
ATOM   415  C  CZ  . TYR B 1 7   ? 7.873   12.004 57.092 1.00 95.29  ? 355 TYR B CZ  1 
ATOM   416  O  OH  . TYR B 1 7   ? 8.814   12.220 58.056 1.00 98.33  ? 355 TYR B OH  1 
ATOM   417  N  N   . TYR B 1 8   ? 3.169   9.598  52.013 1.00 88.10  ? 356 TYR B N   1 
ATOM   418  C  CA  . TYR B 1 8   ? 2.163   9.458  50.940 1.00 90.20  ? 356 TYR B CA  1 
ATOM   419  C  C   . TYR B 1 8   ? 0.947   10.291 51.305 1.00 86.51  ? 356 TYR B C   1 
ATOM   420  O  O   . TYR B 1 8   ? 0.576   10.349 52.477 1.00 85.96  ? 356 TYR B O   1 
ATOM   421  C  CB  . TYR B 1 8   ? 1.801   7.993  50.722 1.00 96.65  ? 356 TYR B CB  1 
ATOM   422  C  CG  . TYR B 1 8   ? 2.899   7.188  50.082 1.00 101.90 ? 356 TYR B CG  1 
ATOM   423  C  CD1 . TYR B 1 8   ? 3.982   6.741  50.822 1.00 105.41 ? 356 TYR B CD1 1 
ATOM   424  C  CD2 . TYR B 1 8   ? 2.864   6.888  48.732 1.00 105.03 ? 356 TYR B CD2 1 
ATOM   425  C  CE1 . TYR B 1 8   ? 4.998   6.000  50.240 1.00 109.65 ? 356 TYR B CE1 1 
ATOM   426  C  CE2 . TYR B 1 8   ? 3.869   6.145  48.133 1.00 109.19 ? 356 TYR B CE2 1 
ATOM   427  C  CZ  . TYR B 1 8   ? 4.940   5.700  48.889 1.00 111.15 ? 356 TYR B CZ  1 
ATOM   428  O  OH  . TYR B 1 8   ? 5.929   4.961  48.307 1.00 115.92 ? 356 TYR B OH  1 
ATOM   429  N  N   . LEU B 1 9   ? 0.359   10.917 50.298 1.00 84.87  ? 357 LEU B N   1 
ATOM   430  C  CA  . LEU B 1 9   ? -0.759  11.863 50.450 1.00 83.03  ? 357 LEU B CA  1 
ATOM   431  C  C   . LEU B 1 9   ? -1.901  11.382 49.560 1.00 82.03  ? 357 LEU B C   1 
ATOM   432  O  O   . LEU B 1 9   ? -1.639  11.033 48.398 1.00 82.84  ? 357 LEU B O   1 
ATOM   433  C  CB  . LEU B 1 9   ? -0.251  13.252 50.058 1.00 83.83  ? 357 LEU B CB  1 
ATOM   434  C  CG  . LEU B 1 9   ? -1.264  14.386 50.145 1.00 84.95  ? 357 LEU B CG  1 
ATOM   435  C  CD1 . LEU B 1 9   ? -1.886  14.448 51.515 1.00 88.57  ? 357 LEU B CD1 1 
ATOM   436  C  CD2 . LEU B 1 9   ? -0.611  15.714 49.816 1.00 87.39  ? 357 LEU B CD2 1 
ATOM   437  N  N   . GLN B 1 10  ? -3.099  11.298 50.123 1.00 80.45  ? 358 GLN B N   1 
ATOM   438  C  CA  . GLN B 1 10  ? -4.338  10.921 49.406 1.00 82.67  ? 358 GLN B CA  1 
ATOM   439  C  C   . GLN B 1 10  ? -5.070  12.206 49.016 1.00 78.83  ? 358 GLN B C   1 
ATOM   440  O  O   . GLN B 1 10  ? -5.217  13.074 49.889 1.00 77.20  ? 358 GLN B O   1 
ATOM   441  C  CB  . GLN B 1 10  ? -5.172  10.026 50.319 1.00 85.95  ? 358 GLN B CB  1 
ATOM   442  C  CG  . GLN B 1 10  ? -6.365  9.383  49.636 1.00 89.69  ? 358 GLN B CG  1 
ATOM   443  C  CD  . GLN B 1 10  ? -6.711  8.055  50.262 1.00 93.77  ? 358 GLN B CD  1 
ATOM   444  O  OE1 . GLN B 1 10  ? -6.356  7.771  51.405 1.00 93.86  ? 358 GLN B OE1 1 
ATOM   445  N  NE2 . GLN B 1 10  ? -7.389  7.214  49.501 1.00 96.31  ? 358 GLN B NE2 1 
ATOM   446  N  N   . VAL B 1 11  ? -5.484  12.341 47.753 1.00 78.94  ? 359 VAL B N   1 
ATOM   447  C  CA  . VAL B 1 11  ? -6.218  13.545 47.259 1.00 78.51  ? 359 VAL B CA  1 
ATOM   448  C  C   . VAL B 1 11  ? -7.401  13.104 46.399 1.00 81.20  ? 359 VAL B C   1 
ATOM   449  O  O   . VAL B 1 11  ? -7.179  12.554 45.306 1.00 82.61  ? 359 VAL B O   1 
ATOM   450  C  CB  . VAL B 1 11  ? -5.314  14.513 46.470 1.00 76.27  ? 359 VAL B CB  1 
ATOM   451  C  CG1 . VAL B 1 11  ? -5.971  15.877 46.348 1.00 75.73  ? 359 VAL B CG1 1 
ATOM   452  C  CG2 . VAL B 1 11  ? -3.928  14.638 47.076 1.00 76.27  ? 359 VAL B CG2 1 
ATOM   453  N  N   . ARG B 1 12  ? -8.609  13.385 46.874 1.00 86.52  ? 360 ARG B N   1 
ATOM   454  C  CA  . ARG B 1 12  ? -9.858  13.336 46.078 1.00 91.02  ? 360 ARG B CA  1 
ATOM   455  C  C   . ARG B 1 12  ? -9.999  14.696 45.394 1.00 90.13  ? 360 ARG B C   1 
ATOM   456  O  O   . ARG B 1 12  ? -9.900  15.733 46.110 1.00 92.20  ? 360 ARG B O   1 
ATOM   457  C  CB  . ARG B 1 12  ? -11.063 13.025 46.975 1.00 96.65  ? 360 ARG B CB  1 
ATOM   458  C  CG  . ARG B 1 12  ? -10.872 11.831 47.906 1.00 101.47 ? 360 ARG B CG  1 
ATOM   459  C  CD  . ARG B 1 12  ? -11.805 11.816 49.107 1.00 104.79 ? 360 ARG B CD  1 
ATOM   460  N  NE  . ARG B 1 12  ? -12.102 13.157 49.600 1.00 107.02 ? 360 ARG B NE  1 
ATOM   461  C  CZ  . ARG B 1 12  ? -13.281 13.771 49.497 1.00 109.28 ? 360 ARG B CZ  1 
ATOM   462  N  NH1 . ARG B 1 12  ? -14.308 13.158 48.929 1.00 111.51 ? 360 ARG B NH1 1 
ATOM   463  N  NH2 . ARG B 1 12  ? -13.430 14.998 49.975 1.00 106.61 ? 360 ARG B NH2 1 
ATOM   464  N  N   . GLY B 1 13  ? -10.178 14.692 44.073 1.00 87.51  ? 361 GLY B N   1 
ATOM   465  C  CA  . GLY B 1 13  ? -10.264 15.905 43.243 1.00 86.95  ? 361 GLY B CA  1 
ATOM   466  C  C   . GLY B 1 13  ? -9.084  15.996 42.294 1.00 87.64  ? 361 GLY B C   1 
ATOM   467  O  O   . GLY B 1 13  ? -7.975  16.294 42.768 1.00 91.26  ? 361 GLY B O   1 
ATOM   468  N  N   . ARG B 1 14  ? -9.308  15.713 41.009 1.00 85.23  ? 362 ARG B N   1 
ATOM   469  C  CA  . ARG B 1 14  ? -8.275  15.748 39.939 1.00 83.17  ? 362 ARG B CA  1 
ATOM   470  C  C   . ARG B 1 14  ? -7.607  17.128 39.915 1.00 75.71  ? 362 ARG B C   1 
ATOM   471  O  O   . ARG B 1 14  ? -6.376  17.194 39.785 1.00 73.03  ? 362 ARG B O   1 
ATOM   472  C  CB  . ARG B 1 14  ? -8.922  15.445 38.586 1.00 88.75  ? 362 ARG B CB  1 
ATOM   473  C  CG  . ARG B 1 14  ? -8.015  15.684 37.388 1.00 91.47  ? 362 ARG B CG  1 
ATOM   474  C  CD  . ARG B 1 14  ? -6.756  14.844 37.441 1.00 95.67  ? 362 ARG B CD  1 
ATOM   475  N  NE  . ARG B 1 14  ? -5.798  15.235 36.416 1.00 98.94  ? 362 ARG B NE  1 
ATOM   476  C  CZ  . ARG B 1 14  ? -4.751  14.505 36.032 1.00 103.13 ? 362 ARG B CZ  1 
ATOM   477  N  NH1 . ARG B 1 14  ? -4.516  13.323 36.582 1.00 104.21 ? 362 ARG B NH1 1 
ATOM   478  N  NH2 . ARG B 1 14  ? -3.945  14.959 35.087 1.00 105.78 ? 362 ARG B NH2 1 
ATOM   479  N  N   . LYS B 1 15  ? -8.419  18.178 39.981 1.00 70.08  ? 363 LYS B N   1 
ATOM   480  C  CA  . LYS B 1 15  ? -7.993  19.595 40.072 1.00 68.23  ? 363 LYS B CA  1 
ATOM   481  C  C   . LYS B 1 15  ? -7.087  19.779 41.306 1.00 63.52  ? 363 LYS B C   1 
ATOM   482  O  O   . LYS B 1 15  ? -6.021  20.354 41.159 1.00 63.63  ? 363 LYS B O   1 
ATOM   483  C  CB  . LYS B 1 15  ? -9.242  20.478 40.142 1.00 68.90  ? 363 LYS B CB  1 
ATOM   484  C  CG  . LYS B 1 15  ? -9.005  21.970 39.976 1.00 69.66  ? 363 LYS B CG  1 
ATOM   485  C  CD  . LYS B 1 15  ? -10.260 22.779 40.191 1.00 69.91  ? 363 LYS B CD  1 
ATOM   486  C  CE  . LYS B 1 15  ? -9.960  24.211 40.564 1.00 70.77  ? 363 LYS B CE  1 
ATOM   487  N  NZ  . LYS B 1 15  ? -11.191 24.910 40.999 1.00 75.49  ? 363 LYS B NZ  1 
ATOM   488  N  N   . ASN B 1 16  ? -7.502  19.294 42.475 1.00 60.35  ? 364 ASN B N   1 
ATOM   489  C  CA  . ASN B 1 16  ? -6.736  19.421 43.750 1.00 57.97  ? 364 ASN B CA  1 
ATOM   490  C  C   . ASN B 1 16  ? -5.421  18.642 43.626 1.00 56.14  ? 364 ASN B C   1 
ATOM   491  O  O   . ASN B 1 16  ? -4.379  19.174 44.026 1.00 52.25  ? 364 ASN B O   1 
ATOM   492  C  CB  . ASN B 1 16  ? -7.579  18.984 44.946 1.00 58.45  ? 364 ASN B CB  1 
ATOM   493  C  CG  . ASN B 1 16  ? -8.744  19.917 45.187 1.00 58.60  ? 364 ASN B CG  1 
ATOM   494  O  OD1 . ASN B 1 16  ? -8.747  21.041 44.687 1.00 62.06  ? 364 ASN B OD1 1 
ATOM   495  N  ND2 . ASN B 1 16  ? -9.732  19.465 45.942 1.00 61.23  ? 364 ASN B ND2 1 
ATOM   496  N  N   . PHE B 1 17  ? -5.449  17.470 43.000 1.00 58.69  ? 365 PHE B N   1 
ATOM   497  C  CA  . PHE B 1 17  ? -4.242  16.638 42.780 1.00 61.45  ? 365 PHE B CA  1 
ATOM   498  C  C   . PHE B 1 17  ? -3.217  17.436 41.965 1.00 60.82  ? 365 PHE B C   1 
ATOM   499  O  O   . PHE B 1 17  ? -2.040  17.467 42.348 1.00 60.65  ? 365 PHE B O   1 
ATOM   500  C  CB  . PHE B 1 17  ? -4.578  15.317 42.082 1.00 65.33  ? 365 PHE B CB  1 
ATOM   501  C  CG  . PHE B 1 17  ? -3.351  14.565 41.638 1.00 67.66  ? 365 PHE B CG  1 
ATOM   502  C  CD1 . PHE B 1 17  ? -2.518  13.968 42.571 1.00 69.23  ? 365 PHE B CD1 1 
ATOM   503  C  CD2 . PHE B 1 17  ? -2.973  14.540 40.303 1.00 70.25  ? 365 PHE B CD2 1 
ATOM   504  C  CE1 . PHE B 1 17  ? -1.372  13.300 42.170 1.00 71.73  ? 365 PHE B CE1 1 
ATOM   505  C  CE2 . PHE B 1 17  ? -1.810  13.897 39.908 1.00 71.66  ? 365 PHE B CE2 1 
ATOM   506  C  CZ  . PHE B 1 17  ? -1.022  13.262 40.840 1.00 72.22  ? 365 PHE B CZ  1 
ATOM   507  N  N   . GLU B 1 18  ? -3.662  18.052 40.869 1.00 61.82  ? 366 GLU B N   1 
ATOM   508  C  CA  . GLU B 1 18  ? -2.805  18.835 39.944 1.00 61.23  ? 366 GLU B CA  1 
ATOM   509  C  C   . GLU B 1 18  ? -2.190  20.017 40.692 1.00 56.60  ? 366 GLU B C   1 
ATOM   510  O  O   . GLU B 1 18  ? -0.974  20.242 40.531 1.00 55.13  ? 366 GLU B O   1 
ATOM   511  C  CB  . GLU B 1 18  ? -3.613  19.316 38.743 1.00 64.95  ? 366 GLU B CB  1 
ATOM   512  C  CG  . GLU B 1 18  ? -4.015  18.189 37.819 1.00 71.18  ? 366 GLU B CG  1 
ATOM   513  C  CD  . GLU B 1 18  ? -4.631  18.646 36.509 1.00 77.60  ? 366 GLU B CD  1 
ATOM   514  O  OE1 . GLU B 1 18  ? -5.259  19.736 36.490 1.00 78.80  ? 366 GLU B OE1 1 
ATOM   515  O  OE2 . GLU B 1 18  ? -4.464  17.921 35.505 1.00 87.61  ? 366 GLU B OE2 1 
ATOM   516  N  N   . ILE B 1 19  ? -2.979  20.733 41.496 1.00 54.07  ? 367 ILE B N   1 
ATOM   517  C  CA  . ILE B 1 19  ? -2.459  21.888 42.290 1.00 54.28  ? 367 ILE B CA  1 
ATOM   518  C  C   . ILE B 1 19  ? -1.394  21.377 43.260 1.00 49.17  ? 367 ILE B C   1 
ATOM   519  O  O   . ILE B 1 19  ? -0.322  21.983 43.351 1.00 47.44  ? 367 ILE B O   1 
ATOM   520  C  CB  . ILE B 1 19  ? -3.573  22.644 43.031 1.00 57.42  ? 367 ILE B CB  1 
ATOM   521  C  CG1 . ILE B 1 19  ? -4.598  23.240 42.061 1.00 61.90  ? 367 ILE B CG1 1 
ATOM   522  C  CG2 . ILE B 1 19  ? -2.963  23.720 43.911 1.00 58.12  ? 367 ILE B CG2 1 
ATOM   523  C  CD1 . ILE B 1 19  ? -5.895  23.683 42.730 1.00 64.72  ? 367 ILE B CD1 1 
ATOM   524  N  N   . LEU B 1 20  ? -1.685  20.308 43.982 1.00 49.70  ? 368 LEU B N   1 
ATOM   525  C  CA  . LEU B 1 20  ? -0.762  19.782 45.017 1.00 49.51  ? 368 LEU B CA  1 
ATOM   526  C  C   . LEU B 1 20  ? 0.493   19.226 44.346 1.00 48.75  ? 368 LEU B C   1 
ATOM   527  O  O   . LEU B 1 20  ? 1.580   19.412 44.903 1.00 46.43  ? 368 LEU B O   1 
ATOM   528  C  CB  . LEU B 1 20  ? -1.487  18.727 45.854 1.00 50.06  ? 368 LEU B CB  1 
ATOM   529  C  CG  . LEU B 1 20  ? -2.621  19.268 46.717 1.00 49.16  ? 368 LEU B CG  1 
ATOM   530  C  CD1 . LEU B 1 20  ? -3.286  18.142 47.477 1.00 50.78  ? 368 LEU B CD1 1 
ATOM   531  C  CD2 . LEU B 1 20  ? -2.116  20.341 47.665 1.00 47.61  ? 368 LEU B CD2 1 
ATOM   532  N  N   . MET B 1 21  ? 0.359   18.639 43.157 1.00 52.88  ? 369 MET B N   1 
ATOM   533  C  CA  . MET B 1 21  ? 1.522   18.163 42.357 1.00 55.56  ? 369 MET B CA  1 
ATOM   534  C  C   . MET B 1 21  ? 2.415   19.342 41.956 1.00 51.94  ? 369 MET B C   1 
ATOM   535  O  O   . MET B 1 21  ? 3.656   19.226 42.111 1.00 51.22  ? 369 MET B O   1 
ATOM   536  C  CB  . MET B 1 21  ? 1.071   17.403 41.113 1.00 61.32  ? 369 MET B CB  1 
ATOM   537  C  CG  . MET B 1 21  ? 0.829   15.936 41.402 1.00 69.90  ? 369 MET B CG  1 
ATOM   538  S  SD  . MET B 1 21  ? 2.280   15.102 42.128 1.00 79.05  ? 369 MET B SD  1 
ATOM   539  C  CE  . MET B 1 21  ? 3.088   14.479 40.652 1.00 77.39  ? 369 MET B CE  1 
ATOM   540  N  N   . LYS B 1 22  ? 1.817   20.446 41.513 1.00 50.72  ? 370 LYS B N   1 
ATOM   541  C  CA  . LYS B 1 22  ? 2.569   21.675 41.156 1.00 53.08  ? 370 LYS B CA  1 
ATOM   542  C  C   . LYS B 1 22  ? 3.365   22.148 42.375 1.00 49.02  ? 370 LYS B C   1 
ATOM   543  O  O   . LYS B 1 22  ? 4.570   22.448 42.236 1.00 46.20  ? 370 LYS B O   1 
ATOM   544  C  CB  . LYS B 1 22  ? 1.622   22.753 40.621 1.00 57.39  ? 370 LYS B CB  1 
ATOM   545  C  CG  . LYS B 1 22  ? 1.004   22.414 39.270 1.00 67.61  ? 370 LYS B CG  1 
ATOM   546  C  CD  . LYS B 1 22  ? -0.036  23.407 38.774 1.00 74.49  ? 370 LYS B CD  1 
ATOM   547  C  CE  . LYS B 1 22  ? 0.575   24.656 38.172 1.00 80.98  ? 370 LYS B CE  1 
ATOM   548  N  NZ  . LYS B 1 22  ? 1.144   24.412 36.823 1.00 83.59  ? 370 LYS B NZ  1 
ATOM   549  N  N   . LEU B 1 23  ? 2.735   22.192 43.542 1.00 47.41  ? 371 LEU B N   1 
ATOM   550  C  CA  . LEU B 1 23  ? 3.395   22.732 44.755 1.00 46.47  ? 371 LEU B CA  1 
ATOM   551  C  C   . LEU B 1 23  ? 4.447   21.748 45.241 1.00 45.43  ? 371 LEU B C   1 
ATOM   552  O  O   . LEU B 1 23  ? 5.537   22.201 45.632 1.00 45.45  ? 371 LEU B O   1 
ATOM   553  C  CB  . LEU B 1 23  ? 2.341   23.015 45.818 1.00 47.28  ? 371 LEU B CB  1 
ATOM   554  C  CG  . LEU B 1 23  ? 1.375   24.125 45.436 1.00 47.43  ? 371 LEU B CG  1 
ATOM   555  C  CD1 . LEU B 1 23  ? 0.203   24.151 46.395 1.00 51.57  ? 371 LEU B CD1 1 
ATOM   556  C  CD2 . LEU B 1 23  ? 2.093   25.456 45.406 1.00 46.95  ? 371 LEU B CD2 1 
ATOM   557  N  N   . LYS B 1 24  ? 4.137   20.455 45.218 1.00 47.56  ? 372 LYS B N   1 
ATOM   558  C  CA  . LYS B 1 24  ? 5.141   19.395 45.506 1.00 50.26  ? 372 LYS B CA  1 
ATOM   559  C  C   . LYS B 1 24  ? 6.374   19.693 44.656 1.00 50.23  ? 372 LYS B C   1 
ATOM   560  O  O   . LYS B 1 24  ? 7.477   19.799 45.213 1.00 49.76  ? 372 LYS B O   1 
ATOM   561  C  CB  . LYS B 1 24  ? 4.603   18.001 45.187 1.00 53.95  ? 372 LYS B CB  1 
ATOM   562  C  CG  . LYS B 1 24  ? 5.545   16.859 45.548 1.00 59.47  ? 372 LYS B CG  1 
ATOM   563  C  CD  . LYS B 1 24  ? 5.398   15.625 44.668 1.00 62.93  ? 372 LYS B CD  1 
ATOM   564  C  CE  . LYS B 1 24  ? 6.715   14.918 44.430 1.00 66.09  ? 372 LYS B CE  1 
ATOM   565  N  NZ  . LYS B 1 24  ? 6.557   13.450 44.315 1.00 69.52  ? 372 LYS B NZ  1 
ATOM   566  N  N   . GLU B 1 25  ? 6.167   19.882 43.351 1.00 48.79  ? 373 GLU B N   1 
ATOM   567  C  CA  . GLU B 1 25  ? 7.265   20.069 42.381 1.00 50.56  ? 373 GLU B CA  1 
ATOM   568  C  C   . GLU B 1 25  ? 8.098   21.270 42.838 1.00 49.27  ? 373 GLU B C   1 
ATOM   569  O  O   . GLU B 1 25  ? 9.329   21.136 42.960 1.00 51.06  ? 373 GLU B O   1 
ATOM   570  C  CB  . GLU B 1 25  ? 6.681   20.235 40.984 1.00 51.21  ? 373 GLU B CB  1 
ATOM   571  C  CG  . GLU B 1 25  ? 7.657   20.745 39.954 1.00 53.31  ? 373 GLU B CG  1 
ATOM   572  C  CD  . GLU B 1 25  ? 7.032   20.720 38.566 1.00 55.70  ? 373 GLU B CD  1 
ATOM   573  O  OE1 . GLU B 1 25  ? 6.798   19.612 38.045 1.00 56.09  ? 373 GLU B OE1 1 
ATOM   574  O  OE2 . GLU B 1 25  ? 6.688   21.800 38.063 1.00 57.53  ? 373 GLU B OE2 1 
ATOM   575  N  N   . SER B 1 26  ? 7.444   22.402 43.095 1.00 47.19  ? 374 SER B N   1 
ATOM   576  C  CA  . SER B 1 26  ? 8.131   23.670 43.437 1.00 45.50  ? 374 SER B CA  1 
ATOM   577  C  C   . SER B 1 26  ? 8.855   23.506 44.785 1.00 46.19  ? 374 SER B C   1 
ATOM   578  O  O   . SER B 1 26  ? 10.028  23.903 44.889 1.00 46.05  ? 374 SER B O   1 
ATOM   579  C  CB  . SER B 1 26  ? 7.171   24.827 43.425 1.00 45.91  ? 374 SER B CB  1 
ATOM   580  O  OG  . SER B 1 26  ? 6.270   24.766 44.536 1.00 47.26  ? 374 SER B OG  1 
ATOM   581  N  N   . LEU B 1 27  ? 8.199   22.915 45.777 1.00 45.75  ? 375 LEU B N   1 
ATOM   582  C  CA  . LEU B 1 27  ? 8.824   22.675 47.104 1.00 47.91  ? 375 LEU B CA  1 
ATOM   583  C  C   . LEU B 1 27  ? 10.088  21.826 46.923 1.00 50.27  ? 375 LEU B C   1 
ATOM   584  O  O   . LEU B 1 27  ? 11.109  22.186 47.495 1.00 53.70  ? 375 LEU B O   1 
ATOM   585  C  CB  . LEU B 1 27  ? 7.817   22.015 48.048 1.00 46.92  ? 375 LEU B CB  1 
ATOM   586  C  CG  . LEU B 1 27  ? 6.718   22.949 48.551 1.00 44.78  ? 375 LEU B CG  1 
ATOM   587  C  CD1 . LEU B 1 27  ? 5.634   22.173 49.275 1.00 44.31  ? 375 LEU B CD1 1 
ATOM   588  C  CD2 . LEU B 1 27  ? 7.303   24.033 49.440 1.00 44.81  ? 375 LEU B CD2 1 
ATOM   589  N  N   . GLU B 1 28  ? 10.053  20.800 46.079 1.00 50.71  ? 376 GLU B N   1 
ATOM   590  C  CA  . GLU B 1 28  ? 11.218  19.900 45.908 1.00 52.78  ? 376 GLU B CA  1 
ATOM   591  C  C   . GLU B 1 28  ? 12.295  20.598 45.076 1.00 51.29  ? 376 GLU B C   1 
ATOM   592  O  O   . GLU B 1 28  ? 13.421  20.678 45.551 1.00 50.12  ? 376 GLU B O   1 
ATOM   593  C  CB  . GLU B 1 28  ? 10.750  18.557 45.368 1.00 55.02  ? 376 GLU B CB  1 
ATOM   594  C  CG  . GLU B 1 28  ? 9.943   17.806 46.408 1.00 57.12  ? 376 GLU B CG  1 
ATOM   595  C  CD  . GLU B 1 28  ? 9.579   16.379 46.058 1.00 62.03  ? 376 GLU B CD  1 
ATOM   596  O  OE1 . GLU B 1 28  ? 9.594   16.041 44.860 1.00 64.17  ? 376 GLU B OE1 1 
ATOM   597  O  OE2 . GLU B 1 28  ? 9.253   15.619 46.987 1.00 65.61  ? 376 GLU B OE2 1 
ATOM   598  N  N   . LEU B 1 29  ? 11.951  21.142 43.909 1.00 49.99  ? 377 LEU B N   1 
ATOM   599  C  CA  . LEU B 1 29  ? 12.959  21.641 42.942 1.00 50.69  ? 377 LEU B CA  1 
ATOM   600  C  C   . LEU B 1 29  ? 13.650  22.884 43.510 1.00 50.57  ? 377 LEU B C   1 
ATOM   601  O  O   . LEU B 1 29  ? 14.809  23.124 43.159 1.00 49.05  ? 377 LEU B O   1 
ATOM   602  C  CB  . LEU B 1 29  ? 12.284  21.919 41.598 1.00 51.01  ? 377 LEU B CB  1 
ATOM   603  C  CG  . LEU B 1 29  ? 11.946  20.679 40.773 1.00 52.70  ? 377 LEU B CG  1 
ATOM   604  C  CD1 . LEU B 1 29  ? 11.128  21.059 39.558 1.00 53.55  ? 377 LEU B CD1 1 
ATOM   605  C  CD2 . LEU B 1 29  ? 13.213  19.937 40.342 1.00 54.27  ? 377 LEU B CD2 1 
ATOM   606  N  N   . MET B 1 30  ? 13.009  23.596 44.436 1.00 52.27  ? 378 MET B N   1 
ATOM   607  C  CA  . MET B 1 30  ? 13.593  24.831 45.017 1.00 54.01  ? 378 MET B CA  1 
ATOM   608  C  C   . MET B 1 30  ? 14.832  24.466 45.838 1.00 51.62  ? 378 MET B C   1 
ATOM   609  O  O   . MET B 1 30  ? 15.704  25.319 45.989 1.00 51.57  ? 378 MET B O   1 
ATOM   610  C  CB  . MET B 1 30  ? 12.592  25.558 45.907 1.00 57.94  ? 378 MET B CB  1 
ATOM   611  C  CG  . MET B 1 30  ? 12.402  24.892 47.251 1.00 65.29  ? 378 MET B CG  1 
ATOM   612  S  SD  . MET B 1 30  ? 11.954  26.094 48.473 1.00 78.51  ? 378 MET B SD  1 
ATOM   613  C  CE  . MET B 1 30  ? 13.547  26.855 48.775 1.00 72.15  ? 378 MET B CE  1 
ATOM   614  N  N   . GLU B 1 31  ? 14.895  23.234 46.331 1.00 51.73  ? 379 GLU B N   1 
ATOM   615  C  CA  . GLU B 1 31  ? 16.034  22.717 47.133 1.00 55.18  ? 379 GLU B CA  1 
ATOM   616  C  C   . GLU B 1 31  ? 17.320  22.735 46.296 1.00 55.87  ? 379 GLU B C   1 
ATOM   617  O  O   . GLU B 1 31  ? 18.397  22.852 46.892 1.00 57.09  ? 379 GLU B O   1 
ATOM   618  C  CB  . GLU B 1 31  ? 15.758  21.288 47.616 1.00 57.18  ? 379 GLU B CB  1 
ATOM   619  C  CG  . GLU B 1 31  ? 14.640  21.178 48.637 1.00 56.50  ? 379 GLU B CG  1 
ATOM   620  C  CD  . GLU B 1 31  ? 14.268  19.748 49.013 1.00 58.82  ? 379 GLU B CD  1 
ATOM   621  O  OE1 . GLU B 1 31  ? 14.892  18.806 48.499 1.00 63.29  ? 379 GLU B OE1 1 
ATOM   622  O  OE2 . GLU B 1 31  ? 13.356  19.582 49.806 1.00 60.32  ? 379 GLU B OE2 1 
ATOM   623  N  N   . LEU B 1 32  ? 17.223  22.604 44.968 1.00 56.36  ? 380 LEU B N   1 
ATOM   624  C  CA  . LEU B 1 32  ? 18.403  22.540 44.065 1.00 57.42  ? 380 LEU B CA  1 
ATOM   625  C  C   . LEU B 1 32  ? 19.077  23.912 43.984 1.00 57.46  ? 380 LEU B C   1 
ATOM   626  O  O   . LEU B 1 32  ? 20.254  23.962 43.593 1.00 58.01  ? 380 LEU B O   1 
ATOM   627  C  CB  . LEU B 1 32  ? 17.972  22.080 42.672 1.00 59.27  ? 380 LEU B CB  1 
ATOM   628  C  CG  . LEU B 1 32  ? 17.504  20.632 42.549 1.00 61.75  ? 380 LEU B CG  1 
ATOM   629  C  CD1 . LEU B 1 32  ? 17.166  20.310 41.099 1.00 62.56  ? 380 LEU B CD1 1 
ATOM   630  C  CD2 . LEU B 1 32  ? 18.549  19.661 43.077 1.00 64.12  ? 380 LEU B CD2 1 
ATOM   631  N  N   . VAL B 1 33  ? 18.362  24.987 44.318 1.00 57.25  ? 381 VAL B N   1 
ATOM   632  C  CA  . VAL B 1 33  ? 18.837  26.376 44.059 1.00 58.66  ? 381 VAL B CA  1 
ATOM   633  C  C   . VAL B 1 33  ? 19.941  26.691 45.058 1.00 60.47  ? 381 VAL B C   1 
ATOM   634  O  O   . VAL B 1 33  ? 19.779  26.477 46.250 1.00 61.99  ? 381 VAL B O   1 
ATOM   635  C  CB  . VAL B 1 33  ? 17.693  27.406 44.115 1.00 56.30  ? 381 VAL B CB  1 
ATOM   636  C  CG1 . VAL B 1 33  ? 18.216  28.830 44.008 1.00 56.76  ? 381 VAL B CG1 1 
ATOM   637  C  CG2 . VAL B 1 33  ? 16.658  27.141 43.029 1.00 55.05  ? 381 VAL B CG2 1 
ATOM   638  N  N   . PRO B 1 34  ? 21.113  27.165 44.592 1.00 64.85  ? 382 PRO B N   1 
ATOM   639  C  CA  . PRO B 1 34  ? 22.198  27.547 45.493 1.00 66.74  ? 382 PRO B CA  1 
ATOM   640  C  C   . PRO B 1 34  ? 21.719  28.521 46.578 1.00 65.69  ? 382 PRO B C   1 
ATOM   641  O  O   . PRO B 1 34  ? 21.024  29.470 46.252 1.00 63.07  ? 382 PRO B O   1 
ATOM   642  C  CB  . PRO B 1 34  ? 23.209  28.234 44.562 1.00 67.42  ? 382 PRO B CB  1 
ATOM   643  C  CG  . PRO B 1 34  ? 22.944  27.621 43.209 1.00 68.62  ? 382 PRO B CG  1 
ATOM   644  C  CD  . PRO B 1 34  ? 21.461  27.337 43.177 1.00 65.68  ? 382 PRO B CD  1 
ATOM   645  N  N   . GLN B 1 35  ? 22.126  28.279 47.823 1.00 68.67  ? 383 GLN B N   1 
ATOM   646  C  CA  . GLN B 1 35  ? 21.769  29.110 49.004 1.00 69.36  ? 383 GLN B CA  1 
ATOM   647  C  C   . GLN B 1 35  ? 21.991  30.592 48.696 1.00 70.47  ? 383 GLN B C   1 
ATOM   648  O  O   . GLN B 1 35  ? 21.136  31.418 49.005 1.00 70.41  ? 383 GLN B O   1 
ATOM   649  C  CB  . GLN B 1 35  ? 22.568  28.670 50.232 1.00 71.56  ? 383 GLN B CB  1 
ATOM   650  C  CG  . GLN B 1 35  ? 21.967  29.149 51.545 1.00 71.46  ? 383 GLN B CG  1 
ATOM   651  C  CD  . GLN B 1 35  ? 20.550  28.661 51.718 1.00 70.80  ? 383 GLN B CD  1 
ATOM   652  O  OE1 . GLN B 1 35  ? 20.259  27.489 51.500 1.00 73.55  ? 383 GLN B OE1 1 
ATOM   653  N  NE2 . GLN B 1 35  ? 19.655  29.560 52.109 1.00 65.91  ? 383 GLN B NE2 1 
ATOM   654  N  N   . PRO B 1 36  ? 23.146  30.997 48.120 1.00 73.38  ? 384 PRO B N   1 
ATOM   655  C  CA  . PRO B 1 36  ? 23.399  32.413 47.846 1.00 74.91  ? 384 PRO B CA  1 
ATOM   656  C  C   . PRO B 1 36  ? 22.251  33.096 47.091 1.00 73.31  ? 384 PRO B C   1 
ATOM   657  O  O   . PRO B 1 36  ? 21.910  34.207 47.451 1.00 74.92  ? 384 PRO B O   1 
ATOM   658  C  CB  . PRO B 1 36  ? 24.689  32.387 47.008 1.00 76.52  ? 384 PRO B CB  1 
ATOM   659  C  CG  . PRO B 1 36  ? 25.409  31.151 47.504 1.00 77.68  ? 384 PRO B CG  1 
ATOM   660  C  CD  . PRO B 1 36  ? 24.302  30.150 47.778 1.00 75.99  ? 384 PRO B CD  1 
ATOM   661  N  N   . LEU B 1 37  ? 21.677  32.413 46.097 1.00 70.17  ? 385 LEU B N   1 
ATOM   662  C  CA  . LEU B 1 37  ? 20.547  32.922 45.276 1.00 68.36  ? 385 LEU B CA  1 
ATOM   663  C  C   . LEU B 1 37  ? 19.265  32.926 46.109 1.00 65.50  ? 385 LEU B C   1 
ATOM   664  O  O   . LEU B 1 37  ? 18.447  33.847 45.924 1.00 65.81  ? 385 LEU B O   1 
ATOM   665  C  CB  . LEU B 1 37  ? 20.382  32.050 44.025 1.00 66.60  ? 385 LEU B CB  1 
ATOM   666  C  CG  . LEU B 1 37  ? 21.558  32.082 43.054 1.00 70.18  ? 385 LEU B CG  1 
ATOM   667  C  CD1 . LEU B 1 37  ? 21.274  31.221 41.831 1.00 68.98  ? 385 LEU B CD1 1 
ATOM   668  C  CD2 . LEU B 1 37  ? 21.891  33.513 42.638 1.00 71.40  ? 385 LEU B CD2 1 
ATOM   669  N  N   . VAL B 1 38  ? 19.067  31.916 46.957 1.00 63.75  ? 386 VAL B N   1 
ATOM   670  C  CA  . VAL B 1 38  ? 17.900  31.875 47.886 1.00 62.42  ? 386 VAL B CA  1 
ATOM   671  C  C   . VAL B 1 38  ? 18.007  33.081 48.820 1.00 64.38  ? 386 VAL B C   1 
ATOM   672  O  O   . VAL B 1 38  ? 16.985  33.761 49.041 1.00 63.51  ? 386 VAL B O   1 
ATOM   673  C  CB  . VAL B 1 38  ? 17.824  30.563 48.686 1.00 60.53  ? 386 VAL B CB  1 
ATOM   674  C  CG1 . VAL B 1 38  ? 16.665  30.593 49.668 1.00 59.21  ? 386 VAL B CG1 1 
ATOM   675  C  CG2 . VAL B 1 38  ? 17.729  29.345 47.778 1.00 60.63  ? 386 VAL B CG2 1 
ATOM   676  N  N   . ASP B 1 39  ? 19.208  33.317 49.351 1.00 68.23  ? 387 ASP B N   1 
ATOM   677  C  CA  . ASP B 1 39  ? 19.473  34.356 50.379 1.00 69.73  ? 387 ASP B CA  1 
ATOM   678  C  C   . ASP B 1 39  ? 19.286  35.726 49.732 1.00 71.27  ? 387 ASP B C   1 
ATOM   679  O  O   . ASP B 1 39  ? 18.504  36.537 50.271 1.00 71.60  ? 387 ASP B O   1 
ATOM   680  C  CB  . ASP B 1 39  ? 20.858  34.166 50.994 1.00 71.21  ? 387 ASP B CB  1 
ATOM   681  C  CG  . ASP B 1 39  ? 20.962  32.945 51.897 1.00 71.13  ? 387 ASP B CG  1 
ATOM   682  O  OD1 . ASP B 1 39  ? 19.913  32.370 52.254 1.00 71.20  ? 387 ASP B OD1 1 
ATOM   683  O  OD2 . ASP B 1 39  ? 22.088  32.579 52.235 1.00 74.75  ? 387 ASP B OD2 1 
ATOM   684  N  N   . SER B 1 40  ? 19.940  35.943 48.595 1.00 72.91  ? 388 SER B N   1 
ATOM   685  C  CA  . SER B 1 40  ? 19.719  37.109 47.705 1.00 75.78  ? 388 SER B CA  1 
ATOM   686  C  C   . SER B 1 40  ? 18.215  37.357 47.560 1.00 73.51  ? 388 SER B C   1 
ATOM   687  O  O   . SER B 1 40  ? 17.764  38.482 47.839 1.00 78.07  ? 388 SER B O   1 
ATOM   688  C  CB  . SER B 1 40  ? 20.374  36.898 46.370 1.00 77.28  ? 388 SER B CB  1 
ATOM   689  O  OG  . SER B 1 40  ? 19.731  37.672 45.373 1.00 80.95  ? 388 SER B OG  1 
ATOM   690  N  N   . TYR B 1 41  ? 17.465  36.328 47.174 1.00 70.49  ? 389 TYR B N   1 
ATOM   691  C  CA  . TYR B 1 41  ? 16.015  36.409 46.860 1.00 67.06  ? 389 TYR B CA  1 
ATOM   692  C  C   . TYR B 1 41  ? 15.221  36.821 48.108 1.00 65.21  ? 389 TYR B C   1 
ATOM   693  O  O   . TYR B 1 41  ? 14.256  37.588 47.989 1.00 66.10  ? 389 TYR B O   1 
ATOM   694  C  CB  . TYR B 1 41  ? 15.519  35.074 46.304 1.00 64.82  ? 389 TYR B CB  1 
ATOM   695  C  CG  . TYR B 1 41  ? 14.022  34.926 46.308 1.00 62.06  ? 389 TYR B CG  1 
ATOM   696  C  CD1 . TYR B 1 41  ? 13.358  34.396 47.405 1.00 58.95  ? 389 TYR B CD1 1 
ATOM   697  C  CD2 . TYR B 1 41  ? 13.268  35.339 45.226 1.00 60.05  ? 389 TYR B CD2 1 
ATOM   698  C  CE1 . TYR B 1 41  ? 11.980  34.288 47.428 1.00 57.83  ? 389 TYR B CE1 1 
ATOM   699  C  CE2 . TYR B 1 41  ? 11.890  35.224 45.227 1.00 58.45  ? 389 TYR B CE2 1 
ATOM   700  C  CZ  . TYR B 1 41  ? 11.243  34.692 46.328 1.00 57.43  ? 389 TYR B CZ  1 
ATOM   701  O  OH  . TYR B 1 41  ? 9.884   34.588 46.328 1.00 56.00  ? 389 TYR B OH  1 
ATOM   702  N  N   . ARG B 1 42  ? 15.587  36.293 49.271 1.00 64.78  ? 390 ARG B N   1 
ATOM   703  C  CA  . ARG B 1 42  ? 14.894  36.590 50.551 1.00 63.49  ? 390 ARG B CA  1 
ATOM   704  C  C   . ARG B 1 42  ? 15.207  38.016 51.013 1.00 66.35  ? 390 ARG B C   1 
ATOM   705  O  O   . ARG B 1 42  ? 14.302  38.657 51.574 1.00 65.13  ? 390 ARG B O   1 
ATOM   706  C  CB  . ARG B 1 42  ? 15.287  35.570 51.611 1.00 61.47  ? 390 ARG B CB  1 
ATOM   707  C  CG  . ARG B 1 42  ? 14.559  34.252 51.448 1.00 58.13  ? 390 ARG B CG  1 
ATOM   708  C  CD  . ARG B 1 42  ? 15.148  33.222 52.359 1.00 56.94  ? 390 ARG B CD  1 
ATOM   709  N  NE  . ARG B 1 42  ? 14.452  31.971 52.199 1.00 54.69  ? 390 ARG B NE  1 
ATOM   710  C  CZ  . ARG B 1 42  ? 14.904  30.816 52.647 1.00 56.85  ? 390 ARG B CZ  1 
ATOM   711  N  NH1 . ARG B 1 42  ? 16.026  30.773 53.346 1.00 60.23  ? 390 ARG B NH1 1 
ATOM   712  N  NH2 . ARG B 1 42  ? 14.208  29.714 52.445 1.00 55.05  ? 390 ARG B NH2 1 
ATOM   713  N  N   . GLN B 1 43  ? 16.440  38.476 50.802 1.00 72.22  ? 391 GLN B N   1 
ATOM   714  C  CA  . GLN B 1 43  ? 16.873  39.862 51.121 1.00 80.88  ? 391 GLN B CA  1 
ATOM   715  C  C   . GLN B 1 43  ? 16.071  40.826 50.238 1.00 84.31  ? 391 GLN B C   1 
ATOM   716  O  O   . GLN B 1 43  ? 15.748  41.932 50.708 1.00 86.24  ? 391 GLN B O   1 
ATOM   717  C  CB  . GLN B 1 43  ? 18.394  39.985 50.970 1.00 83.46  ? 391 GLN B CB  1 
ATOM   718  C  CG  . GLN B 1 43  ? 19.151  39.325 52.120 1.00 86.29  ? 391 GLN B CG  1 
ATOM   719  C  CD  . GLN B 1 43  ? 20.565  38.901 51.795 1.00 90.94  ? 391 GLN B CD  1 
ATOM   720  O  OE1 . GLN B 1 43  ? 21.095  39.181 50.719 1.00 97.93  ? 391 GLN B OE1 1 
ATOM   721  N  NE2 . GLN B 1 43  ? 21.190  38.206 52.736 1.00 88.72  ? 391 GLN B NE2 1 
ATOM   722  N  N   . GLN B 1 44  ? 15.681  40.369 49.047 1.00 87.77  ? 392 GLN B N   1 
ATOM   723  C  CA  . GLN B 1 44  ? 14.846  41.129 48.081 1.00 91.63  ? 392 GLN B CA  1 
ATOM   724  C  C   . GLN B 1 44  ? 13.404  41.237 48.605 1.00 93.24  ? 392 GLN B C   1 
ATOM   725  O  O   . GLN B 1 44  ? 12.806  42.311 48.432 1.00 93.06  ? 392 GLN B O   1 
ATOM   726  C  CB  . GLN B 1 44  ? 14.893  40.451 46.714 1.00 93.41  ? 392 GLN B CB  1 
ATOM   727  C  CG  . GLN B 1 44  ? 14.816  41.424 45.552 1.00 98.83  ? 392 GLN B CG  1 
ATOM   728  C  CD  . GLN B 1 44  ? 14.487  40.727 44.255 1.00 102.80 ? 392 GLN B CD  1 
ATOM   729  O  OE1 . GLN B 1 44  ? 14.596  39.504 44.134 1.00 105.74 ? 392 GLN B OE1 1 
ATOM   730  N  NE2 . GLN B 1 44  ? 14.077  41.507 43.268 1.00 105.92 ? 392 GLN B NE2 1 
ATOM   731  N  N   . GLN B 1 45  ? 12.872  40.174 49.231 1.00 95.03  ? 393 GLN B N   1 
ATOM   732  C  CA  . GLN B 1 45  ? 11.454  40.089 49.700 1.00 94.58  ? 393 GLN B CA  1 
ATOM   733  C  C   . GLN B 1 45  ? 11.150  41.205 50.704 1.00 100.23 ? 393 GLN B C   1 
ATOM   734  O  O   . GLN B 1 45  ? 9.970   41.582 50.812 1.00 98.73  ? 393 GLN B O   1 
ATOM   735  C  CB  . GLN B 1 45  ? 11.145  38.734 50.345 1.00 89.09  ? 393 GLN B CB  1 
ATOM   736  C  CG  . GLN B 1 45  ? 11.146  37.573 49.366 1.00 86.45  ? 393 GLN B CG  1 
ATOM   737  C  CD  . GLN B 1 45  ? 10.490  37.947 48.064 1.00 84.76  ? 393 GLN B CD  1 
ATOM   738  O  OE1 . GLN B 1 45  ? 9.347   38.392 48.036 1.00 81.57  ? 393 GLN B OE1 1 
ATOM   739  N  NE2 . GLN B 1 45  ? 11.223  37.781 46.977 1.00 86.74  ? 393 GLN B NE2 1 
ATOM   740  N  N   . GLN B 1 46  ? 12.171  41.723 51.392 1.00 109.70 ? 394 GLN B N   1 
ATOM   741  C  CA  . GLN B 1 46  ? 12.040  42.837 52.372 1.00 118.32 ? 394 GLN B CA  1 
ATOM   742  C  C   . GLN B 1 46  ? 11.350  44.053 51.726 1.00 126.10 ? 394 GLN B C   1 
ATOM   743  O  O   . GLN B 1 46  ? 11.107  45.035 52.459 1.00 132.35 ? 394 GLN B O   1 
ATOM   744  C  CB  . GLN B 1 46  ? 13.412  43.221 52.925 1.00 119.80 ? 394 GLN B CB  1 
ATOM   745  C  CG  . GLN B 1 46  ? 13.336  44.213 54.076 1.00 121.49 ? 394 GLN B CG  1 
ATOM   746  C  CD  . GLN B 1 46  ? 14.565  44.191 54.949 1.00 121.94 ? 394 GLN B CD  1 
ATOM   747  O  OE1 . GLN B 1 46  ? 15.300  43.208 54.993 1.00 119.18 ? 394 GLN B OE1 1 
ATOM   748  N  NE2 . GLN B 1 46  ? 14.784  45.278 55.672 1.00 123.72 ? 394 GLN B NE2 1 
ATOM   749  N  N   . LEU B 1 47  ? 11.049  43.996 50.419 1.00 128.74 ? 395 LEU B N   1 
ATOM   750  C  CA  . LEU B 1 47  ? 10.246  45.014 49.680 1.00 130.65 ? 395 LEU B CA  1 
ATOM   751  C  C   . LEU B 1 47  ? 9.084   45.502 50.563 1.00 130.98 ? 395 LEU B C   1 
ATOM   752  O  O   . LEU B 1 47  ? 9.001   46.727 50.792 1.00 130.20 ? 395 LEU B O   1 
ATOM   753  C  CB  . LEU B 1 47  ? 9.738   44.405 48.365 1.00 129.75 ? 395 LEU B CB  1 
ATOM   754  C  CG  . LEU B 1 47  ? 9.190   45.404 47.341 1.00 134.10 ? 395 LEU B CG  1 
ATOM   755  C  CD1 . LEU B 1 47  ? 9.543   44.983 45.921 1.00 132.08 ? 395 LEU B CD1 1 
ATOM   756  C  CD2 . LEU B 1 47  ? 7.683   45.579 47.487 1.00 135.31 ? 395 LEU B CD2 1 
ATOM   757  N  N   . LEU B 1 48  ? 8.244   44.579 51.059 1.00 129.28 ? 396 LEU B N   1 
ATOM   758  C  CA  . LEU B 1 48  ? 7.014   44.885 51.850 1.00 129.39 ? 396 LEU B CA  1 
ATOM   759  C  C   . LEU B 1 48  ? 7.254   44.587 53.338 1.00 123.59 ? 396 LEU B C   1 
ATOM   760  O  O   . LEU B 1 48  ? 8.159   43.850 53.730 1.00 115.56 ? 396 LEU B O   1 
ATOM   761  C  CB  . LEU B 1 48  ? 5.840   44.062 51.299 1.00 129.77 ? 396 LEU B CB  1 
ATOM   762  C  CG  . LEU B 1 48  ? 5.409   44.388 49.865 1.00 131.15 ? 396 LEU B CG  1 
ATOM   763  C  CD1 . LEU B 1 48  ? 4.342   43.419 49.374 1.00 128.18 ? 396 LEU B CD1 1 
ATOM   764  C  CD2 . LEU B 1 48  ? 4.914   45.824 49.750 1.00 134.44 ? 396 LEU B CD2 1 
ATOM   765  N  N   . GLY C 2 1   ? 22.569  26.356 14.354 1.00 88.02  ? 1   GLY C N   1 
ATOM   766  C  CA  . GLY C 2 1   ? 21.621  25.212 14.194 1.00 81.74  ? 1   GLY C CA  1 
ATOM   767  C  C   . GLY C 2 1   ? 21.572  24.708 12.760 1.00 78.04  ? 1   GLY C C   1 
ATOM   768  O  O   . GLY C 2 1   ? 22.147  25.376 11.862 1.00 81.16  ? 1   GLY C O   1 
ATOM   769  N  N   . SER C 2 2   ? 20.914  23.565 12.554 1.00 70.93  ? 2   SER C N   1 
ATOM   770  C  CA  . SER C 2 2   ? 20.720  22.891 11.244 1.00 68.56  ? 2   SER C CA  1 
ATOM   771  C  C   . SER C 2 2   ? 19.318  22.270 11.208 1.00 67.15  ? 2   SER C C   1 
ATOM   772  O  O   . SER C 2 2   ? 18.788  21.938 12.278 1.00 59.45  ? 2   SER C O   1 
ATOM   773  C  CB  . SER C 2 2   ? 21.803  21.852 10.994 1.00 67.27  ? 2   SER C CB  1 
ATOM   774  O  OG  . SER C 2 2   ? 21.556  20.662 11.732 1.00 62.51  ? 2   SER C OG  1 
ATOM   775  N  N   . ASP C 2 3   ? 18.749  22.119 10.014 1.00 68.64  ? 3   ASP C N   1 
ATOM   776  C  CA  . ASP C 2 3   ? 17.396  21.546 9.792  1.00 67.79  ? 3   ASP C CA  1 
ATOM   777  C  C   . ASP C 2 3   ? 17.338  20.105 10.312 1.00 61.74  ? 3   ASP C C   1 
ATOM   778  O  O   . ASP C 2 3   ? 16.384  19.788 11.042 1.00 60.84  ? 3   ASP C O   1 
ATOM   779  C  CB  . ASP C 2 3   ? 17.010  21.574 8.314  1.00 73.41  ? 3   ASP C CB  1 
ATOM   780  C  CG  . ASP C 2 3   ? 15.625  21.004 8.059  1.00 78.08  ? 3   ASP C CG  1 
ATOM   781  O  OD1 . ASP C 2 3   ? 14.755  21.166 8.942  1.00 84.20  ? 3   ASP C OD1 1 
ATOM   782  O  OD2 . ASP C 2 3   ? 15.422  20.405 6.987  1.00 85.20  ? 3   ASP C OD2 1 
ATOM   783  N  N   . LEU C 2 4   ? 18.267  19.249 9.879  1.00 56.76  ? 4   LEU C N   1 
ATOM   784  C  CA  . LEU C 2 4   ? 18.298  17.812 10.261 1.00 53.12  ? 4   LEU C CA  1 
ATOM   785  C  C   . LEU C 2 4   ? 18.593  17.702 11.762 1.00 50.05  ? 4   LEU C C   1 
ATOM   786  O  O   . LEU C 2 4   ? 18.110  16.745 12.376 1.00 49.14  ? 4   LEU C O   1 
ATOM   787  C  CB  . LEU C 2 4   ? 19.366  17.075 9.455  1.00 54.16  ? 4   LEU C CB  1 
ATOM   788  C  CG  . LEU C 2 4   ? 19.035  16.792 7.989  1.00 57.99  ? 4   LEU C CG  1 
ATOM   789  C  CD1 . LEU C 2 4   ? 20.090  15.890 7.381  1.00 58.55  ? 4   LEU C CD1 1 
ATOM   790  C  CD2 . LEU C 2 4   ? 17.661  16.166 7.840  1.00 59.07  ? 4   LEU C CD2 1 
ATOM   791  N  N   . GLY C 2 5   ? 19.414  18.612 12.287 1.00 48.14  ? 5   GLY C N   1 
ATOM   792  C  CA  . GLY C 2 5   ? 19.747  18.724 13.716 1.00 51.03  ? 5   GLY C CA  1 
ATOM   793  C  C   . GLY C 2 5   ? 18.505  18.913 14.555 1.00 49.59  ? 5   GLY C C   1 
ATOM   794  O  O   . GLY C 2 5   ? 18.315  18.139 15.495 1.00 49.75  ? 5   GLY C O   1 
ATOM   795  N  N   . LYS C 2 6   ? 17.663  19.875 14.179 1.00 53.36  ? 6   LYS C N   1 
ATOM   796  C  CA  . LYS C 2 6   ? 16.355  20.144 14.831 1.00 57.08  ? 6   LYS C CA  1 
ATOM   797  C  C   . LYS C 2 6   ? 15.445  18.911 14.728 1.00 54.30  ? 6   LYS C C   1 
ATOM   798  O  O   . LYS C 2 6   ? 14.832  18.566 15.722 1.00 52.33  ? 6   LYS C O   1 
ATOM   799  C  CB  . LYS C 2 6   ? 15.721  21.402 14.233 1.00 62.83  ? 6   LYS C CB  1 
ATOM   800  C  CG  . LYS C 2 6   ? 16.430  22.680 14.647 1.00 69.68  ? 6   LYS C CG  1 
ATOM   801  C  CD  . LYS C 2 6   ? 15.874  23.943 14.027 1.00 76.09  ? 6   LYS C CD  1 
ATOM   802  C  CE  . LYS C 2 6   ? 16.761  25.143 14.283 1.00 80.14  ? 6   LYS C CE  1 
ATOM   803  N  NZ  . LYS C 2 6   ? 16.353  26.309 13.460 1.00 86.48  ? 6   LYS C NZ  1 
ATOM   804  N  N   . LYS C 2 7   ? 15.371  18.253 13.577 1.00 54.19  ? 7   LYS C N   1 
ATOM   805  C  CA  . LYS C 2 7   ? 14.555  17.018 13.438 1.00 55.37  ? 7   LYS C CA  1 
ATOM   806  C  C   . LYS C 2 7   ? 15.121  15.933 14.359 1.00 51.85  ? 7   LYS C C   1 
ATOM   807  O  O   . LYS C 2 7   ? 14.310  15.157 14.896 1.00 54.82  ? 7   LYS C O   1 
ATOM   808  C  CB  . LYS C 2 7   ? 14.491  16.532 11.984 1.00 59.22  ? 7   LYS C CB  1 
ATOM   809  C  CG  . LYS C 2 7   ? 13.572  17.345 11.081 1.00 62.92  ? 7   LYS C CG  1 
ATOM   810  C  CD  . LYS C 2 7   ? 13.516  16.841 9.653  1.00 66.59  ? 7   LYS C CD  1 
ATOM   811  C  CE  . LYS C 2 7   ? 12.491  17.570 8.811  1.00 70.22  ? 7   LYS C CE  1 
ATOM   812  N  NZ  . LYS C 2 7   ? 12.510  17.120 7.394  1.00 74.57  ? 7   LYS C NZ  1 
ATOM   813  N  N   . LEU C 2 8   ? 16.447  15.860 14.520 1.00 48.07  ? 8   LEU C N   1 
ATOM   814  C  CA  . LEU C 2 8   ? 17.095  14.778 15.308 1.00 48.06  ? 8   LEU C CA  1 
ATOM   815  C  C   . LEU C 2 8   ? 16.866  15.047 16.802 1.00 48.11  ? 8   LEU C C   1 
ATOM   816  O  O   . LEU C 2 8   ? 16.482  14.120 17.520 1.00 47.14  ? 8   LEU C O   1 
ATOM   817  C  CB  . LEU C 2 8   ? 18.585  14.677 14.968 1.00 46.55  ? 8   LEU C CB  1 
ATOM   818  C  CG  . LEU C 2 8   ? 19.354  13.611 15.755 1.00 46.04  ? 8   LEU C CG  1 
ATOM   819  C  CD1 . LEU C 2 8   ? 18.731  12.235 15.579 1.00 46.24  ? 8   LEU C CD1 1 
ATOM   820  C  CD2 . LEU C 2 8   ? 20.818  13.586 15.361 1.00 46.75  ? 8   LEU C CD2 1 
ATOM   821  N  N   . LEU C 2 9   ? 17.038  16.290 17.231 1.00 48.29  ? 9   LEU C N   1 
ATOM   822  C  CA  . LEU C 2 9   ? 16.683  16.730 18.599 1.00 47.18  ? 9   LEU C CA  1 
ATOM   823  C  C   . LEU C 2 9   ? 15.250  16.271 18.906 1.00 50.38  ? 9   LEU C C   1 
ATOM   824  O  O   . LEU C 2 9   ? 15.047  15.594 19.933 1.00 49.87  ? 9   LEU C O   1 
ATOM   825  C  CB  . LEU C 2 9   ? 16.834  18.248 18.684 1.00 46.37  ? 9   LEU C CB  1 
ATOM   826  C  CG  . LEU C 2 9   ? 18.277  18.761 18.766 1.00 46.54  ? 9   LEU C CG  1 
ATOM   827  C  CD1 . LEU C 2 9   ? 18.335  20.258 18.476 1.00 46.74  ? 9   LEU C CD1 1 
ATOM   828  C  CD2 . LEU C 2 9   ? 18.883  18.464 20.129 1.00 47.36  ? 9   LEU C CD2 1 
ATOM   829  N  N   . GLU C 2 10  ? 14.298  16.572 18.024 1.00 54.23  ? 10  GLU C N   1 
ATOM   830  C  CA  . GLU C 2 10  ? 12.863  16.245 18.230 1.00 58.05  ? 10  GLU C CA  1 
ATOM   831  C  C   . GLU C 2 10  ? 12.658  14.719 18.253 1.00 57.65  ? 10  GLU C C   1 
ATOM   832  O  O   . GLU C 2 10  ? 11.959  14.247 19.148 1.00 57.41  ? 10  GLU C O   1 
ATOM   833  C  CB  . GLU C 2 10  ? 12.004  16.927 17.165 1.00 62.56  ? 10  GLU C CB  1 
ATOM   834  C  CG  . GLU C 2 10  ? 10.515  16.686 17.337 1.00 68.11  ? 10  GLU C CG  1 
ATOM   835  C  CD  . GLU C 2 10  ? 9.904   17.173 18.650 1.00 72.33  ? 10  GLU C CD  1 
ATOM   836  O  OE1 . GLU C 2 10  ? 10.639  17.741 19.492 1.00 73.16  ? 10  GLU C OE1 1 
ATOM   837  O  OE2 . GLU C 2 10  ? 8.681   16.991 18.827 1.00 78.19  ? 10  GLU C OE2 1 
ATOM   838  N  N   . ALA C 2 11  ? 13.216  13.977 17.295 1.00 56.20  ? 11  ALA C N   1 
ATOM   839  C  CA  . ALA C 2 11  ? 13.060  12.503 17.193 1.00 57.35  ? 11  ALA C CA  1 
ATOM   840  C  C   . ALA C 2 11  ? 13.626  11.817 18.446 1.00 55.75  ? 11  ALA C C   1 
ATOM   841  O  O   . ALA C 2 11  ? 12.951  10.936 19.006 1.00 56.41  ? 11  ALA C O   1 
ATOM   842  C  CB  . ALA C 2 11  ? 13.733  11.992 15.948 1.00 58.51  ? 11  ALA C CB  1 
ATOM   843  N  N   . ALA C 2 12  ? 14.843  12.176 18.837 1.00 54.28  ? 12  ALA C N   1 
ATOM   844  C  CA  . ALA C 2 12  ? 15.548  11.646 20.026 1.00 53.22  ? 12  ALA C CA  1 
ATOM   845  C  C   . ALA C 2 12  ? 14.736  11.914 21.299 1.00 54.30  ? 12  ALA C C   1 
ATOM   846  O  O   . ALA C 2 12  ? 14.680  11.022 22.166 1.00 54.44  ? 12  ALA C O   1 
ATOM   847  C  CB  . ALA C 2 12  ? 16.921  12.258 20.104 1.00 51.97  ? 12  ALA C CB  1 
ATOM   848  N  N   . ALA C 2 13  ? 14.123  13.094 21.405 1.00 54.78  ? 13  ALA C N   1 
ATOM   849  C  CA  . ALA C 2 13  ? 13.382  13.546 22.604 1.00 54.35  ? 13  ALA C CA  1 
ATOM   850  C  C   . ALA C 2 13  ? 12.088  12.739 22.761 1.00 59.37  ? 13  ALA C C   1 
ATOM   851  O  O   . ALA C 2 13  ? 11.774  12.344 23.897 1.00 59.63  ? 13  ALA C O   1 
ATOM   852  C  CB  . ALA C 2 13  ? 13.084  15.020 22.513 1.00 54.39  ? 13  ALA C CB  1 
ATOM   853  N  N   . VAL C 2 14  ? 11.341  12.546 21.675 1.00 61.14  ? 14  VAL C N   1 
ATOM   854  C  CA  . VAL C 2 14  ? 9.993   11.903 21.706 1.00 65.03  ? 14  VAL C CA  1 
ATOM   855  C  C   . VAL C 2 14  ? 10.126  10.392 21.460 1.00 65.44  ? 14  VAL C C   1 
ATOM   856  O  O   . VAL C 2 14  ? 9.127   9.693  21.637 1.00 69.68  ? 14  VAL C O   1 
ATOM   857  C  CB  . VAL C 2 14  ? 9.025   12.567 20.710 1.00 67.30  ? 14  VAL C CB  1 
ATOM   858  C  CG1 . VAL C 2 14  ? 8.934   14.067 20.944 1.00 67.56  ? 14  VAL C CG1 1 
ATOM   859  C  CG2 . VAL C 2 14  ? 9.380   12.262 19.262 1.00 68.48  ? 14  VAL C CG2 1 
ATOM   860  N  N   . GLY C 2 15  ? 11.309  9.913  21.072 1.00 64.33  ? 15  GLY C N   1 
ATOM   861  C  CA  . GLY C 2 15  ? 11.649  8.475  21.059 1.00 65.66  ? 15  GLY C CA  1 
ATOM   862  C  C   . GLY C 2 15  ? 11.340  7.784  19.732 1.00 68.94  ? 15  GLY C C   1 
ATOM   863  O  O   . GLY C 2 15  ? 11.127  6.552  19.760 1.00 67.29  ? 15  GLY C O   1 
ATOM   864  N  N   . GLN C 2 16  ? 11.370  8.513  18.606 1.00 67.42  ? 16  GLN C N   1 
ATOM   865  C  CA  . GLN C 2 16  ? 11.188  7.941  17.243 1.00 68.57  ? 16  GLN C CA  1 
ATOM   866  C  C   . GLN C 2 16  ? 12.493  7.264  16.797 1.00 67.11  ? 16  GLN C C   1 
ATOM   867  O  O   . GLN C 2 16  ? 13.281  7.911  16.079 1.00 65.69  ? 16  GLN C O   1 
ATOM   868  C  CB  . GLN C 2 16  ? 10.776  9.034  16.257 1.00 73.01  ? 16  GLN C CB  1 
ATOM   869  C  CG  . GLN C 2 16  ? 9.407   9.631  16.540 1.00 77.21  ? 16  GLN C CG  1 
ATOM   870  C  CD  . GLN C 2 16  ? 9.190   10.950 15.833 1.00 82.03  ? 16  GLN C CD  1 
ATOM   871  O  OE1 . GLN C 2 16  ? 10.132  11.675 15.491 1.00 82.11  ? 16  GLN C OE1 1 
ATOM   872  N  NE2 . GLN C 2 16  ? 7.926   11.287 15.632 1.00 85.15  ? 16  GLN C NE2 1 
ATOM   873  N  N   . ASP C 2 17  ? 12.697  6.000  17.185 1.00 69.35  ? 17  ASP C N   1 
ATOM   874  C  CA  . ASP C 2 17  ? 13.915  5.190  16.885 1.00 72.23  ? 17  ASP C CA  1 
ATOM   875  C  C   . ASP C 2 17  ? 14.222  5.214  15.380 1.00 70.14  ? 17  ASP C C   1 
ATOM   876  O  O   . ASP C 2 17  ? 15.396  5.394  15.019 1.00 66.62  ? 17  ASP C O   1 
ATOM   877  C  CB  . ASP C 2 17  ? 13.751  3.731  17.322 1.00 78.36  ? 17  ASP C CB  1 
ATOM   878  C  CG  . ASP C 2 17  ? 13.571  3.549  18.817 1.00 84.97  ? 17  ASP C CG  1 
ATOM   879  O  OD1 . ASP C 2 17  ? 12.428  3.697  19.293 1.00 90.72  ? 17  ASP C OD1 1 
ATOM   880  O  OD2 . ASP C 2 17  ? 14.575  3.262  19.494 1.00 89.55  ? 17  ASP C OD2 1 
ATOM   881  N  N   . ASP C 2 18  ? 13.208  5.001  14.541 1.00 70.94  ? 18  ASP C N   1 
ATOM   882  C  CA  . ASP C 2 18  ? 13.369  4.854  13.069 1.00 71.86  ? 18  ASP C CA  1 
ATOM   883  C  C   . ASP C 2 18  ? 13.780  6.199  12.473 1.00 67.72  ? 18  ASP C C   1 
ATOM   884  O  O   . ASP C 2 18  ? 14.736  6.229  11.684 1.00 67.35  ? 18  ASP C O   1 
ATOM   885  C  CB  . ASP C 2 18  ? 12.088  4.333  12.415 1.00 77.45  ? 18  ASP C CB  1 
ATOM   886  C  CG  . ASP C 2 18  ? 11.764  2.901  12.800 1.00 83.94  ? 18  ASP C CG  1 
ATOM   887  O  OD1 . ASP C 2 18  ? 12.718  2.123  13.017 1.00 85.97  ? 18  ASP C OD1 1 
ATOM   888  O  OD2 . ASP C 2 18  ? 10.559  2.578  12.902 1.00 91.31  ? 18  ASP C OD2 1 
ATOM   889  N  N   . GLU C 2 19  ? 13.070  7.261  12.835 1.00 65.79  ? 19  GLU C N   1 
ATOM   890  C  CA  . GLU C 2 19  ? 13.348  8.630  12.353 1.00 64.78  ? 19  GLU C CA  1 
ATOM   891  C  C   . GLU C 2 19  ? 14.775  9.015  12.763 1.00 61.97  ? 19  GLU C C   1 
ATOM   892  O  O   . GLU C 2 19  ? 15.458  9.640  11.931 1.00 61.74  ? 19  GLU C O   1 
ATOM   893  C  CB  . GLU C 2 19  ? 12.288  9.592  12.882 1.00 66.35  ? 19  GLU C CB  1 
ATOM   894  C  CG  . GLU C 2 19  ? 12.440  11.007 12.364 1.00 68.24  ? 19  GLU C CG  1 
ATOM   895  C  CD  . GLU C 2 19  ? 12.254  11.182 10.865 1.00 72.21  ? 19  GLU C CD  1 
ATOM   896  O  OE1 . GLU C 2 19  ? 12.004  10.175 10.177 1.00 72.60  ? 19  GLU C OE1 1 
ATOM   897  O  OE2 . GLU C 2 19  ? 12.353  12.332 10.395 1.00 73.75  ? 19  GLU C OE2 1 
ATOM   898  N  N   . VAL C 2 20  ? 15.206  8.643  13.981 1.00 60.80  ? 20  VAL C N   1 
ATOM   899  C  CA  . VAL C 2 20  ? 16.602  8.850  14.478 1.00 57.82  ? 20  VAL C CA  1 
ATOM   900  C  C   . VAL C 2 20  ? 17.579  8.176  13.511 1.00 58.04  ? 20  VAL C C   1 
ATOM   901  O  O   . VAL C 2 20  ? 18.520  8.855  13.068 1.00 54.83  ? 20  VAL C O   1 
ATOM   902  C  CB  . VAL C 2 20  ? 16.821  8.343  15.919 1.00 56.78  ? 20  VAL C CB  1 
ATOM   903  C  CG1 . VAL C 2 20  ? 18.299  8.126  16.212 1.00 55.39  ? 20  VAL C CG1 1 
ATOM   904  C  CG2 . VAL C 2 20  ? 16.216  9.280  16.957 1.00 55.69  ? 20  VAL C CG2 1 
ATOM   905  N  N   . ARG C 2 21  ? 17.386  6.893  13.214 1.00 61.11  ? 21  ARG C N   1 
ATOM   906  C  CA  . ARG C 2 21  ? 18.287  6.123  12.309 1.00 64.18  ? 21  ARG C CA  1 
ATOM   907  C  C   . ARG C 2 21  ? 18.288  6.758  10.913 1.00 62.59  ? 21  ARG C C   1 
ATOM   908  O  O   . ARG C 2 21  ? 19.390  6.892  10.348 1.00 60.31  ? 21  ARG C O   1 
ATOM   909  C  CB  . ARG C 2 21  ? 17.888  4.648  12.261 1.00 69.53  ? 21  ARG C CB  1 
ATOM   910  C  CG  . ARG C 2 21  ? 18.114  3.927  13.583 1.00 73.20  ? 21  ARG C CG  1 
ATOM   911  C  CD  . ARG C 2 21  ? 17.989  2.421  13.487 1.00 78.09  ? 21  ARG C CD  1 
ATOM   912  N  NE  . ARG C 2 21  ? 17.625  1.852  14.774 1.00 83.38  ? 21  ARG C NE  1 
ATOM   913  C  CZ  . ARG C 2 21  ? 16.378  1.691  15.214 1.00 88.71  ? 21  ARG C CZ  1 
ATOM   914  N  NH1 . ARG C 2 21  ? 15.346  2.033  14.456 1.00 90.91  ? 21  ARG C NH1 1 
ATOM   915  N  NH2 . ARG C 2 21  ? 16.166  1.170  16.413 1.00 92.99  ? 21  ARG C NH2 1 
ATOM   916  N  N   . ILE C 2 22  ? 17.119  7.161  10.391 1.00 61.22  ? 22  ILE C N   1 
ATOM   917  C  CA  . ILE C 2 22  ? 17.021  7.808  9.048  1.00 62.36  ? 22  ILE C CA  1 
ATOM   918  C  C   . ILE C 2 22  ? 17.875  9.075  9.076  1.00 58.41  ? 22  ILE C C   1 
ATOM   919  O  O   . ILE C 2 22  ? 18.658  9.272  8.148  1.00 54.17  ? 22  ILE C O   1 
ATOM   920  C  CB  . ILE C 2 22  ? 15.576  8.149  8.621  1.00 66.87  ? 22  ILE C CB  1 
ATOM   921  C  CG1 . ILE C 2 22  ? 14.649  6.932  8.597  1.00 71.78  ? 22  ILE C CG1 1 
ATOM   922  C  CG2 . ILE C 2 22  ? 15.603  8.837  7.263  1.00 68.04  ? 22  ILE C CG2 1 
ATOM   923  C  CD1 . ILE C 2 22  ? 13.177  7.287  8.426  1.00 74.73  ? 22  ILE C CD1 1 
ATOM   924  N  N   . LEU C 2 23  ? 17.714  9.900  10.118 1.00 55.30  ? 23  LEU C N   1 
ATOM   925  C  CA  . LEU C 2 23  ? 18.351  11.236 10.200 1.00 53.76  ? 23  LEU C CA  1 
ATOM   926  C  C   . LEU C 2 23  ? 19.870  11.064 10.287 1.00 52.34  ? 23  LEU C C   1 
ATOM   927  O  O   . LEU C 2 23  ? 20.587  11.752 9.538  1.00 47.67  ? 23  LEU C O   1 
ATOM   928  C  CB  . LEU C 2 23  ? 17.771  11.992 11.399 1.00 54.20  ? 23  LEU C CB  1 
ATOM   929  C  CG  . LEU C 2 23  ? 16.303  12.389 11.250 1.00 55.18  ? 23  LEU C CG  1 
ATOM   930  C  CD1 . LEU C 2 23  ? 15.734  12.892 12.568 1.00 55.36  ? 23  LEU C CD1 1 
ATOM   931  C  CD2 . LEU C 2 23  ? 16.130  13.435 10.163 1.00 57.30  ? 23  LEU C CD2 1 
ATOM   932  N  N   . MET C 2 24  ? 20.329  10.110 11.091 1.00 51.15  ? 24  MET C N   1 
ATOM   933  C  CA  . MET C 2 24  ? 21.769  9.800  11.263 1.00 54.79  ? 24  MET C CA  1 
ATOM   934  C  C   . MET C 2 24  ? 22.394  9.417  9.920  1.00 53.29  ? 24  MET C C   1 
ATOM   935  O  O   . MET C 2 24  ? 23.454  9.945  9.593  1.00 52.13  ? 24  MET C O   1 
ATOM   936  C  CB  . MET C 2 24  ? 21.943  8.632  12.218 1.00 59.20  ? 24  MET C CB  1 
ATOM   937  C  CG  . MET C 2 24  ? 21.293  8.894  13.518 1.00 68.03  ? 24  MET C CG  1 
ATOM   938  S  SD  . MET C 2 24  ? 22.331  9.951  14.459 1.00 79.44  ? 24  MET C SD  1 
ATOM   939  C  CE  . MET C 2 24  ? 23.056  8.665  15.473 1.00 72.83  ? 24  MET C CE  1 
ATOM   940  N  N   . ALA C 2 25  ? 21.778  8.478  9.214  1.00 52.13  ? 25  ALA C N   1 
ATOM   941  C  CA  . ALA C 2 25  ? 22.241  7.980  7.899  1.00 53.06  ? 25  ALA C CA  1 
ATOM   942  C  C   . ALA C 2 25  ? 22.265  9.140  6.897  1.00 51.23  ? 25  ALA C C   1 
ATOM   943  O  O   . ALA C 2 25  ? 23.008  9.075  5.925  1.00 50.97  ? 25  ALA C O   1 
ATOM   944  C  CB  . ALA C 2 25  ? 21.341  6.864  7.440  1.00 55.29  ? 25  ALA C CB  1 
ATOM   945  N  N   . ASN C 2 26  ? 21.493  10.191 7.146  1.00 50.39  ? 26  ASN C N   1 
ATOM   946  C  CA  . ASN C 2 26  ? 21.426  11.356 6.236  1.00 51.27  ? 26  ASN C CA  1 
ATOM   947  C  C   . ASN C 2 26  ? 22.407  12.427 6.704  1.00 49.91  ? 26  ASN C C   1 
ATOM   948  O  O   . ASN C 2 26  ? 22.430  13.481 6.087  1.00 51.41  ? 26  ASN C O   1 
ATOM   949  C  CB  . ASN C 2 26  ? 19.993  11.831 6.091  1.00 53.83  ? 26  ASN C CB  1 
ATOM   950  C  CG  . ASN C 2 26  ? 19.287  11.066 4.998  1.00 56.47  ? 26  ASN C CG  1 
ATOM   951  O  OD1 . ASN C 2 26  ? 19.429  11.408 3.827  1.00 61.37  ? 26  ASN C OD1 1 
ATOM   952  N  ND2 . ASN C 2 26  ? 18.575  10.009 5.360  1.00 54.39  ? 26  ASN C ND2 1 
ATOM   953  N  N   . GLY C 2 27  ? 23.243  12.104 7.692  1.00 49.09  ? 27  GLY C N   1 
ATOM   954  C  CA  . GLY C 2 27  ? 24.265  13.005 8.255  1.00 49.61  ? 27  GLY C CA  1 
ATOM   955  C  C   . GLY C 2 27  ? 23.673  14.078 9.165  1.00 48.20  ? 27  GLY C C   1 
ATOM   956  O  O   . GLY C 2 27  ? 24.264  15.172 9.234  1.00 47.27  ? 27  GLY C O   1 
ATOM   957  N  N   . ALA C 2 28  ? 22.546  13.808 9.834  1.00 47.00  ? 28  ALA C N   1 
ATOM   958  C  CA  . ALA C 2 28  ? 21.978  14.734 10.848 1.00 46.93  ? 28  ALA C CA  1 
ATOM   959  C  C   . ALA C 2 28  ? 23.062  15.022 11.880 1.00 45.79  ? 28  ALA C C   1 
ATOM   960  O  O   . ALA C 2 28  ? 23.853  14.100 12.194 1.00 46.28  ? 28  ALA C O   1 
ATOM   961  C  CB  . ALA C 2 28  ? 20.738  14.188 11.494 1.00 46.62  ? 28  ALA C CB  1 
ATOM   962  N  N   . ASP C 2 29  ? 23.125  16.267 12.338 1.00 45.95  ? 29  ASP C N   1 
ATOM   963  C  CA  . ASP C 2 29  ? 24.151  16.754 13.288 1.00 46.11  ? 29  ASP C CA  1 
ATOM   964  C  C   . ASP C 2 29  ? 23.929  16.047 14.629 1.00 45.55  ? 29  ASP C C   1 
ATOM   965  O  O   . ASP C 2 29  ? 23.012  16.417 15.349 1.00 45.69  ? 29  ASP C O   1 
ATOM   966  C  CB  . ASP C 2 29  ? 24.104  18.275 13.376 1.00 47.10  ? 29  ASP C CB  1 
ATOM   967  C  CG  . ASP C 2 29  ? 25.147  18.829 14.318 1.00 50.91  ? 29  ASP C CG  1 
ATOM   968  O  OD1 . ASP C 2 29  ? 26.077  18.079 14.662 1.00 51.21  ? 29  ASP C OD1 1 
ATOM   969  O  OD2 . ASP C 2 29  ? 25.003  19.993 14.713 1.00 55.85  ? 29  ASP C OD2 1 
ATOM   970  N  N   . VAL C 2 30  ? 24.720  15.026 14.928 1.00 48.36  ? 30  VAL C N   1 
ATOM   971  C  CA  . VAL C 2 30  ? 24.542  14.193 16.154 1.00 49.17  ? 30  VAL C CA  1 
ATOM   972  C  C   . VAL C 2 30  ? 24.784  15.055 17.402 1.00 48.69  ? 30  VAL C C   1 
ATOM   973  O  O   . VAL C 2 30  ? 24.264  14.694 18.460 1.00 49.17  ? 30  VAL C O   1 
ATOM   974  C  CB  . VAL C 2 30  ? 25.447  12.942 16.137 1.00 52.43  ? 30  VAL C CB  1 
ATOM   975  C  CG1 . VAL C 2 30  ? 26.889  13.272 16.453 1.00 54.62  ? 30  VAL C CG1 1 
ATOM   976  C  CG2 . VAL C 2 30  ? 24.949  11.884 17.096 1.00 55.81  ? 30  VAL C CG2 1 
ATOM   977  N  N   . ASN C 2 31  ? 25.537  16.148 17.289 1.00 47.60  ? 31  ASN C N   1 
ATOM   978  C  CA  . ASN C 2 31  ? 25.828  17.064 18.425 1.00 47.56  ? 31  ASN C CA  1 
ATOM   979  C  C   . ASN C 2 31  ? 25.057  18.378 18.238 1.00 47.22  ? 31  ASN C C   1 
ATOM   980  O  O   . ASN C 2 31  ? 25.500  19.406 18.748 1.00 49.77  ? 31  ASN C O   1 
ATOM   981  C  CB  . ASN C 2 31  ? 27.340  17.207 18.599 1.00 49.96  ? 31  ASN C CB  1 
ATOM   982  C  CG  . ASN C 2 31  ? 27.976  15.883 18.993 1.00 52.32  ? 31  ASN C CG  1 
ATOM   983  O  OD1 . ASN C 2 31  ? 27.588  15.260 20.001 1.00 50.95  ? 31  ASN C OD1 1 
ATOM   984  N  ND2 . ASN C 2 31  ? 28.910  15.410 18.180 1.00 53.75  ? 31  ASN C ND2 1 
ATOM   985  N  N   . ALA C 2 32  ? 23.908  18.341 17.561 1.00 45.87  ? 32  ALA C N   1 
ATOM   986  C  CA  . ALA C 2 32  ? 22.999  19.502 17.465 1.00 44.96  ? 32  ALA C CA  1 
ATOM   987  C  C   . ALA C 2 32  ? 22.621  19.914 18.888 1.00 47.13  ? 32  ALA C C   1 
ATOM   988  O  O   . ALA C 2 32  ? 22.637  19.037 19.801 1.00 44.24  ? 32  ALA C O   1 
ATOM   989  C  CB  . ALA C 2 32  ? 21.785  19.172 16.645 1.00 44.23  ? 32  ALA C CB  1 
ATOM   990  N  N   . MET C 2 33  ? 22.288  21.181 19.073 1.00 46.34  ? 33  MET C N   1 
ATOM   991  C  CA  . MET C 2 33  ? 21.963  21.752 20.398 1.00 49.34  ? 33  MET C CA  1 
ATOM   992  C  C   . MET C 2 33  ? 20.619  22.457 20.300 1.00 48.09  ? 33  MET C C   1 
ATOM   993  O  O   . MET C 2 33  ? 20.375  23.051 19.267 1.00 47.70  ? 33  MET C O   1 
ATOM   994  C  CB  . MET C 2 33  ? 23.071  22.693 20.857 1.00 51.66  ? 33  MET C CB  1 
ATOM   995  C  CG  . MET C 2 33  ? 24.253  21.917 21.434 1.00 54.80  ? 33  MET C CG  1 
ATOM   996  S  SD  . MET C 2 33  ? 25.494  22.968 22.184 1.00 61.49  ? 33  MET C SD  1 
ATOM   997  C  CE  . MET C 2 33  ? 26.007  23.887 20.737 1.00 62.71  ? 33  MET C CE  1 
ATOM   998  N  N   . ASP C 2 34  ? 19.729  22.207 21.263 1.00 47.82  ? 34  ASP C N   1 
ATOM   999  C  CA  . ASP C 2 34  ? 18.474  22.982 21.419 1.00 48.91  ? 34  ASP C CA  1 
ATOM   1000 C  C   . ASP C 2 34  ? 18.810  24.245 22.223 1.00 50.19  ? 34  ASP C C   1 
ATOM   1001 O  O   . ASP C 2 34  ? 19.991  24.479 22.517 1.00 49.41  ? 34  ASP C O   1 
ATOM   1002 C  CB  . ASP C 2 34  ? 17.349  22.119 22.009 1.00 47.08  ? 34  ASP C CB  1 
ATOM   1003 C  CG  . ASP C 2 34  ? 17.420  21.870 23.507 1.00 46.91  ? 34  ASP C CG  1 
ATOM   1004 O  OD1 . ASP C 2 34  ? 18.348  22.392 24.161 1.00 46.22  ? 34  ASP C OD1 1 
ATOM   1005 O  OD2 . ASP C 2 34  ? 16.540  21.138 24.011 1.00 47.85  ? 34  ASP C OD2 1 
ATOM   1006 N  N   . GLN C 2 35  ? 17.804  25.033 22.559 1.00 53.02  ? 35  GLN C N   1 
ATOM   1007 C  CA  . GLN C 2 35  ? 17.981  26.394 23.121 1.00 58.49  ? 35  GLN C CA  1 
ATOM   1008 C  C   . GLN C 2 35  ? 18.518  26.339 24.559 1.00 55.34  ? 35  GLN C C   1 
ATOM   1009 O  O   . GLN C 2 35  ? 18.880  27.404 25.067 1.00 59.24  ? 35  GLN C O   1 
ATOM   1010 C  CB  . GLN C 2 35  ? 16.665  27.172 23.059 1.00 63.36  ? 35  GLN C CB  1 
ATOM   1011 C  CG  . GLN C 2 35  ? 15.499  26.465 23.744 1.00 67.72  ? 35  GLN C CG  1 
ATOM   1012 C  CD  . GLN C 2 35  ? 14.897  25.337 22.932 1.00 72.04  ? 35  GLN C CD  1 
ATOM   1013 O  OE1 . GLN C 2 35  ? 15.420  24.912 21.893 1.00 73.04  ? 35  GLN C OE1 1 
ATOM   1014 N  NE2 . GLN C 2 35  ? 13.766  24.843 23.403 1.00 77.44  ? 35  GLN C NE2 1 
ATOM   1015 N  N   . ASN C 2 36  ? 18.594  25.165 25.189 1.00 50.78  ? 36  ASN C N   1 
ATOM   1016 C  CA  . ASN C 2 36  ? 19.175  25.019 26.549 1.00 49.73  ? 36  ASN C CA  1 
ATOM   1017 C  C   . ASN C 2 36  ? 20.551  24.356 26.462 1.00 49.35  ? 36  ASN C C   1 
ATOM   1018 O  O   . ASN C 2 36  ? 21.165  24.120 27.502 1.00 50.29  ? 36  ASN C O   1 
ATOM   1019 C  CB  . ASN C 2 36  ? 18.227  24.246 27.455 1.00 49.53  ? 36  ASN C CB  1 
ATOM   1020 C  CG  . ASN C 2 36  ? 17.000  25.058 27.777 1.00 50.78  ? 36  ASN C CG  1 
ATOM   1021 O  OD1 . ASN C 2 36  ? 17.120  26.221 28.125 1.00 54.37  ? 36  ASN C OD1 1 
ATOM   1022 N  ND2 . ASN C 2 36  ? 15.829  24.471 27.619 1.00 50.02  ? 36  ASN C ND2 1 
ATOM   1023 N  N   . GLY C 2 37  ? 20.998  24.028 25.263 1.00 46.73  ? 37  GLY C N   1 
ATOM   1024 C  CA  . GLY C 2 37  ? 22.302  23.382 25.037 1.00 46.31  ? 37  GLY C CA  1 
ATOM   1025 C  C   . GLY C 2 37  ? 22.171  21.879 24.962 1.00 44.64  ? 37  GLY C C   1 
ATOM   1026 O  O   . GLY C 2 37  ? 23.192  21.221 25.001 1.00 44.83  ? 37  GLY C O   1 
ATOM   1027 N  N   . GLU C 2 38  ? 20.945  21.353 24.966 1.00 43.71  ? 38  GLU C N   1 
ATOM   1028 C  CA  . GLU C 2 38  ? 20.716  19.889 24.983 1.00 42.87  ? 38  GLU C CA  1 
ATOM   1029 C  C   . GLU C 2 38  ? 21.082  19.326 23.604 1.00 42.13  ? 38  GLU C C   1 
ATOM   1030 O  O   . GLU C 2 38  ? 20.642  19.881 22.610 1.00 40.85  ? 38  GLU C O   1 
ATOM   1031 C  CB  . GLU C 2 38  ? 19.268  19.532 25.309 1.00 43.52  ? 38  GLU C CB  1 
ATOM   1032 C  CG  . GLU C 2 38  ? 18.716  20.179 26.559 1.00 45.89  ? 38  GLU C CG  1 
ATOM   1033 C  CD  . GLU C 2 38  ? 19.659  20.134 27.743 1.00 49.13  ? 38  GLU C CD  1 
ATOM   1034 O  OE1 . GLU C 2 38  ? 19.910  19.033 28.244 1.00 52.22  ? 38  GLU C OE1 1 
ATOM   1035 O  OE2 . GLU C 2 38  ? 20.153  21.209 28.136 1.00 55.62  ? 38  GLU C OE2 1 
ATOM   1036 N  N   . THR C 2 39  ? 21.836  18.239 23.577 1.00 42.79  ? 39  THR C N   1 
ATOM   1037 C  CA  . THR C 2 39  ? 22.090  17.414 22.373 1.00 41.99  ? 39  THR C CA  1 
ATOM   1038 C  C   . THR C 2 39  ? 21.040  16.316 22.295 1.00 42.69  ? 39  THR C C   1 
ATOM   1039 O  O   . THR C 2 39  ? 20.346  16.031 23.273 1.00 39.91  ? 39  THR C O   1 
ATOM   1040 C  CB  . THR C 2 39  ? 23.498  16.829 22.431 1.00 43.23  ? 39  THR C CB  1 
ATOM   1041 O  OG1 . THR C 2 39  ? 23.509  15.917 23.525 1.00 41.86  ? 39  THR C OG1 1 
ATOM   1042 C  CG2 . THR C 2 39  ? 24.570  17.878 22.620 1.00 44.40  ? 39  THR C CG2 1 
ATOM   1043 N  N   . PRO C 2 40  ? 20.904  15.635 21.142 1.00 42.19  ? 40  PRO C N   1 
ATOM   1044 C  CA  . PRO C 2 40  ? 20.007  14.492 21.049 1.00 42.76  ? 40  PRO C CA  1 
ATOM   1045 C  C   . PRO C 2 40  ? 20.227  13.506 22.198 1.00 42.83  ? 40  PRO C C   1 
ATOM   1046 O  O   . PRO C 2 40  ? 19.254  12.957 22.686 1.00 44.04  ? 40  PRO C O   1 
ATOM   1047 C  CB  . PRO C 2 40  ? 20.384  13.876 19.701 1.00 43.66  ? 40  PRO C CB  1 
ATOM   1048 C  CG  . PRO C 2 40  ? 20.786  15.082 18.881 1.00 43.08  ? 40  PRO C CG  1 
ATOM   1049 C  CD  . PRO C 2 40  ? 21.544  15.953 19.863 1.00 43.71  ? 40  PRO C CD  1 
ATOM   1050 N  N   . LEU C 2 41  ? 21.486  13.306 22.589 1.00 43.27  ? 41  LEU C N   1 
ATOM   1051 C  CA  . LEU C 2 41  ? 21.858  12.352 23.654 1.00 45.02  ? 41  LEU C CA  1 
ATOM   1052 C  C   . LEU C 2 41  ? 21.299  12.850 24.994 1.00 45.39  ? 41  LEU C C   1 
ATOM   1053 O  O   . LEU C 2 41  ? 20.736  12.024 25.737 1.00 45.90  ? 41  LEU C O   1 
ATOM   1054 C  CB  . LEU C 2 41  ? 23.377  12.187 23.709 1.00 44.41  ? 41  LEU C CB  1 
ATOM   1055 C  CG  . LEU C 2 41  ? 23.852  11.103 24.668 1.00 46.04  ? 41  LEU C CG  1 
ATOM   1056 C  CD1 . LEU C 2 41  ? 23.215  9.759  24.333 1.00 46.31  ? 41  LEU C CD1 1 
ATOM   1057 C  CD2 . LEU C 2 41  ? 25.359  11.002 24.667 1.00 48.39  ? 41  LEU C CD2 1 
ATOM   1058 N  N   . HIS C 2 42  ? 21.432  14.143 25.298 1.00 45.53  ? 42  HIS C N   1 
ATOM   1059 C  CA  . HIS C 2 42  ? 20.789  14.737 26.502 1.00 43.70  ? 42  HIS C CA  1 
ATOM   1060 C  C   . HIS C 2 42  ? 19.323  14.317 26.489 1.00 45.53  ? 42  HIS C C   1 
ATOM   1061 O  O   . HIS C 2 42  ? 18.858  13.737 27.457 1.00 45.69  ? 42  HIS C O   1 
ATOM   1062 C  CB  . HIS C 2 42  ? 20.898  16.260 26.530 1.00 43.69  ? 42  HIS C CB  1 
ATOM   1063 C  CG  . HIS C 2 42  ? 22.208  16.808 26.999 1.00 44.57  ? 42  HIS C CG  1 
ATOM   1064 N  ND1 . HIS C 2 42  ? 23.203  17.172 26.120 1.00 43.64  ? 42  HIS C ND1 1 
ATOM   1065 C  CD2 . HIS C 2 42  ? 22.646  17.158 28.233 1.00 44.27  ? 42  HIS C CD2 1 
ATOM   1066 C  CE1 . HIS C 2 42  ? 24.208  17.701 26.793 1.00 45.17  ? 42  HIS C CE1 1 
ATOM   1067 N  NE2 . HIS C 2 42  ? 23.888  17.709 28.095 1.00 44.29  ? 42  HIS C NE2 1 
ATOM   1068 N  N   . LEU C 2 43  ? 18.619  14.588 25.391 1.00 47.80  ? 43  LEU C N   1 
ATOM   1069 C  CA  . LEU C 2 43  ? 17.146  14.460 25.355 1.00 46.21  ? 43  LEU C CA  1 
ATOM   1070 C  C   . LEU C 2 43  ? 16.748  12.983 25.462 1.00 48.32  ? 43  LEU C C   1 
ATOM   1071 O  O   . LEU C 2 43  ? 15.885  12.678 26.295 1.00 49.10  ? 43  LEU C O   1 
ATOM   1072 C  CB  . LEU C 2 43  ? 16.625  15.154 24.101 1.00 46.53  ? 43  LEU C CB  1 
ATOM   1073 C  CG  . LEU C 2 43  ? 16.936  16.648 24.056 1.00 46.51  ? 43  LEU C CG  1 
ATOM   1074 C  CD1 . LEU C 2 43  ? 16.482  17.256 22.752 1.00 47.92  ? 43  LEU C CD1 1 
ATOM   1075 C  CD2 . LEU C 2 43  ? 16.295  17.384 25.236 1.00 46.66  ? 43  LEU C CD2 1 
ATOM   1076 N  N   . ALA C 2 44  ? 17.411  12.086 24.733 1.00 47.32  ? 44  ALA C N   1 
ATOM   1077 C  CA  . ALA C 2 44  ? 17.107  10.638 24.763 1.00 49.33  ? 44  ALA C CA  1 
ATOM   1078 C  C   . ALA C 2 44  ? 17.414  10.063 26.158 1.00 49.28  ? 44  ALA C C   1 
ATOM   1079 O  O   . ALA C 2 44  ? 16.625  9.233  26.649 1.00 49.93  ? 44  ALA C O   1 
ATOM   1080 C  CB  . ALA C 2 44  ? 17.870  9.926  23.680 1.00 50.01  ? 44  ALA C CB  1 
ATOM   1081 N  N   . ALA C 2 45  ? 18.536  10.468 26.753 1.00 48.81  ? 45  ALA C N   1 
ATOM   1082 C  CA  . ALA C 2 45  ? 18.980  10.051 28.099 1.00 49.11  ? 45  ALA C CA  1 
ATOM   1083 C  C   . ALA C 2 45  ? 17.941  10.486 29.124 1.00 50.68  ? 45  ALA C C   1 
ATOM   1084 O  O   . ALA C 2 45  ? 17.459  9.622  29.915 1.00 52.11  ? 45  ALA C O   1 
ATOM   1085 C  CB  . ALA C 2 45  ? 20.328  10.644 28.404 1.00 49.99  ? 45  ALA C CB  1 
ATOM   1086 N  N   . MET C 2 46  ? 17.582  11.770 29.078 1.00 49.13  ? 46  MET C N   1 
ATOM   1087 C  CA  . MET C 2 46  ? 16.562  12.385 29.952 1.00 50.80  ? 46  MET C CA  1 
ATOM   1088 C  C   . MET C 2 46  ? 15.242  11.622 29.865 1.00 54.01  ? 46  MET C C   1 
ATOM   1089 O  O   . MET C 2 46  ? 14.576  11.476 30.923 1.00 53.40  ? 46  MET C O   1 
ATOM   1090 C  CB  . MET C 2 46  ? 16.287  13.830 29.555 1.00 50.61  ? 46  MET C CB  1 
ATOM   1091 C  CG  . MET C 2 46  ? 15.205  14.447 30.406 1.00 53.52  ? 46  MET C CG  1 
ATOM   1092 S  SD  . MET C 2 46  ? 15.074  16.207 30.186 1.00 54.93  ? 46  MET C SD  1 
ATOM   1093 C  CE  . MET C 2 46  ? 14.253  16.253 28.592 1.00 56.38  ? 46  MET C CE  1 
ATOM   1094 N  N   . ASN C 2 47  ? 14.811  11.277 28.649 1.00 53.39  ? 47  ASN C N   1 
ATOM   1095 C  CA  . ASN C 2 47  ? 13.432  10.792 28.388 1.00 54.17  ? 47  ASN C CA  1 
ATOM   1096 C  C   . ASN C 2 47  ? 13.420  9.263  28.379 1.00 55.97  ? 47  ASN C C   1 
ATOM   1097 O  O   . ASN C 2 47  ? 12.360  8.686  28.076 1.00 59.50  ? 47  ASN C O   1 
ATOM   1098 C  CB  . ASN C 2 47  ? 12.858  11.405 27.111 1.00 54.14  ? 47  ASN C CB  1 
ATOM   1099 C  CG  . ASN C 2 47  ? 12.440  12.848 27.293 1.00 54.64  ? 47  ASN C CG  1 
ATOM   1100 O  OD1 . ASN C 2 47  ? 12.196  13.301 28.413 1.00 56.38  ? 47  ASN C OD1 1 
ATOM   1101 N  ND2 . ASN C 2 47  ? 12.340  13.573 26.197 1.00 54.80  ? 47  ASN C ND2 1 
ATOM   1102 N  N   . GLY C 2 48  ? 14.545  8.637  28.734 1.00 55.77  ? 48  GLY C N   1 
ATOM   1103 C  CA  . GLY C 2 48  ? 14.636  7.183  28.935 1.00 57.92  ? 48  GLY C CA  1 
ATOM   1104 C  C   . GLY C 2 48  ? 14.508  6.417  27.628 1.00 61.22  ? 48  GLY C C   1 
ATOM   1105 O  O   . GLY C 2 48  ? 13.896  5.350  27.638 1.00 63.18  ? 48  GLY C O   1 
ATOM   1106 N  N   . HIS C 2 49  ? 15.066  6.931  26.527 1.00 61.50  ? 49  HIS C N   1 
ATOM   1107 C  CA  . HIS C 2 49  ? 14.986  6.282  25.192 1.00 62.13  ? 49  HIS C CA  1 
ATOM   1108 C  C   . HIS C 2 49  ? 16.308  5.555  24.926 1.00 63.35  ? 49  HIS C C   1 
ATOM   1109 O  O   . HIS C 2 49  ? 17.134  6.063  24.118 1.00 61.53  ? 49  HIS C O   1 
ATOM   1110 C  CB  . HIS C 2 49  ? 14.600  7.292  24.109 1.00 61.37  ? 49  HIS C CB  1 
ATOM   1111 C  CG  . HIS C 2 49  ? 13.259  7.923  24.303 1.00 63.99  ? 49  HIS C CG  1 
ATOM   1112 N  ND1 . HIS C 2 49  ? 12.125  7.188  24.592 1.00 68.17  ? 49  HIS C ND1 1 
ATOM   1113 C  CD2 . HIS C 2 49  ? 12.857  9.210  24.206 1.00 62.46  ? 49  HIS C CD2 1 
ATOM   1114 C  CE1 . HIS C 2 49  ? 11.088  7.999  24.682 1.00 68.38  ? 49  HIS C CE1 1 
ATOM   1115 N  NE2 . HIS C 2 49  ? 11.510  9.240  24.444 1.00 66.72  ? 49  HIS C NE2 1 
ATOM   1116 N  N   . LEU C 2 50  ? 16.450  4.375  25.531 1.00 63.52  ? 50  LEU C N   1 
ATOM   1117 C  CA  . LEU C 2 50  ? 17.713  3.602  25.645 1.00 66.85  ? 50  LEU C CA  1 
ATOM   1118 C  C   . LEU C 2 50  ? 18.245  3.237  24.257 1.00 67.88  ? 50  LEU C C   1 
ATOM   1119 O  O   . LEU C 2 50  ? 19.475  3.331  24.049 1.00 65.94  ? 50  LEU C O   1 
ATOM   1120 C  CB  . LEU C 2 50  ? 17.446  2.340  26.468 1.00 70.45  ? 50  LEU C CB  1 
ATOM   1121 C  CG  . LEU C 2 50  ? 18.559  1.296  26.429 1.00 73.18  ? 50  LEU C CG  1 
ATOM   1122 C  CD1 . LEU C 2 50  ? 19.849  1.868  26.995 1.00 72.39  ? 50  LEU C CD1 1 
ATOM   1123 C  CD2 . LEU C 2 50  ? 18.148  0.038  27.184 1.00 77.07  ? 50  LEU C CD2 1 
ATOM   1124 N  N   . GLU C 2 51  ? 17.367  2.777  23.368 1.00 70.14  ? 51  GLU C N   1 
ATOM   1125 C  CA  . GLU C 2 51  ? 17.757  2.340  22.006 1.00 72.46  ? 51  GLU C CA  1 
ATOM   1126 C  C   . GLU C 2 51  ? 18.375  3.545  21.287 1.00 66.90  ? 51  GLU C C   1 
ATOM   1127 O  O   . GLU C 2 51  ? 19.444  3.388  20.670 1.00 63.58  ? 51  GLU C O   1 
ATOM   1128 C  CB  . GLU C 2 51  ? 16.552  1.759  21.269 1.00 78.84  ? 51  GLU C CB  1 
ATOM   1129 C  CG  . GLU C 2 51  ? 16.879  1.262  19.866 1.00 89.94  ? 51  GLU C CG  1 
ATOM   1130 C  CD  . GLU C 2 51  ? 17.826  0.072  19.785 1.00 97.15  ? 51  GLU C CD  1 
ATOM   1131 O  OE1 . GLU C 2 51  ? 17.739  -0.821 20.666 1.00 106.57 ? 51  GLU C OE1 1 
ATOM   1132 O  OE2 . GLU C 2 51  ? 18.647  0.037  18.837 1.00 100.89 ? 51  GLU C OE2 1 
ATOM   1133 N  N   . ILE C 2 52  ? 17.758  4.719  21.421 1.00 62.52  ? 52  ILE C N   1 
ATOM   1134 C  CA  . ILE C 2 52  ? 18.222  5.959  20.739 1.00 59.59  ? 52  ILE C CA  1 
ATOM   1135 C  C   . ILE C 2 52  ? 19.548  6.386  21.365 1.00 56.83  ? 52  ILE C C   1 
ATOM   1136 O  O   . ILE C 2 52  ? 20.451  6.778  20.621 1.00 57.94  ? 52  ILE C O   1 
ATOM   1137 C  CB  . ILE C 2 52  ? 17.143  7.049  20.792 1.00 58.29  ? 52  ILE C CB  1 
ATOM   1138 C  CG1 . ILE C 2 52  ? 16.013  6.721  19.810 1.00 59.50  ? 52  ILE C CG1 1 
ATOM   1139 C  CG2 . ILE C 2 52  ? 17.752  8.418  20.535 1.00 55.70  ? 52  ILE C CG2 1 
ATOM   1140 C  CD1 . ILE C 2 52  ? 14.775  7.572  19.962 1.00 58.41  ? 52  ILE C CD1 1 
ATOM   1141 N  N   . VAL C 2 53  ? 19.682  6.229  22.676 1.00 59.09  ? 53  VAL C N   1 
ATOM   1142 C  CA  . VAL C 2 53  ? 20.930  6.542  23.432 1.00 58.70  ? 53  VAL C CA  1 
ATOM   1143 C  C   . VAL C 2 53  ? 22.094  5.721  22.861 1.00 60.83  ? 53  VAL C C   1 
ATOM   1144 O  O   . VAL C 2 53  ? 23.158  6.319  22.604 1.00 60.06  ? 53  VAL C O   1 
ATOM   1145 C  CB  . VAL C 2 53  ? 20.755  6.308  24.944 1.00 57.55  ? 53  VAL C CB  1 
ATOM   1146 C  CG1 . VAL C 2 53  ? 22.098  6.200  25.648 1.00 58.46  ? 53  VAL C CG1 1 
ATOM   1147 C  CG2 . VAL C 2 53  ? 19.900  7.399  25.585 1.00 55.99  ? 53  VAL C CG2 1 
ATOM   1148 N  N   . GLU C 2 54  ? 21.906  4.410  22.674 1.00 63.49  ? 54  GLU C N   1 
ATOM   1149 C  CA  . GLU C 2 54  ? 22.960  3.498  22.146 1.00 67.12  ? 54  GLU C CA  1 
ATOM   1150 C  C   . GLU C 2 54  ? 23.323  3.898  20.710 1.00 64.77  ? 54  GLU C C   1 
ATOM   1151 O  O   . GLU C 2 54  ? 24.519  4.060  20.439 1.00 62.34  ? 54  GLU C O   1 
ATOM   1152 C  CB  . GLU C 2 54  ? 22.507  2.044  22.218 1.00 72.56  ? 54  GLU C CB  1 
ATOM   1153 C  CG  . GLU C 2 54  ? 22.858  1.384  23.537 1.00 77.50  ? 54  GLU C CG  1 
ATOM   1154 C  CD  . GLU C 2 54  ? 21.912  0.279  23.955 1.00 82.34  ? 54  GLU C CD  1 
ATOM   1155 O  OE1 . GLU C 2 54  ? 20.863  0.127  23.299 1.00 86.41  ? 54  GLU C OE1 1 
ATOM   1156 O  OE2 . GLU C 2 54  ? 22.220  -0.417 24.941 1.00 87.04  ? 54  GLU C OE2 1 
ATOM   1157 N  N   . VAL C 2 55  ? 22.320  4.057  19.842 1.00 65.19  ? 55  VAL C N   1 
ATOM   1158 C  CA  . VAL C 2 55  ? 22.469  4.508  18.423 1.00 64.84  ? 55  VAL C CA  1 
ATOM   1159 C  C   . VAL C 2 55  ? 23.351  5.766  18.387 1.00 61.91  ? 55  VAL C C   1 
ATOM   1160 O  O   . VAL C 2 55  ? 24.313  5.798  17.597 1.00 61.60  ? 55  VAL C O   1 
ATOM   1161 C  CB  . VAL C 2 55  ? 21.099  4.785  17.771 1.00 67.64  ? 55  VAL C CB  1 
ATOM   1162 C  CG1 . VAL C 2 55  ? 21.236  5.554  16.466 1.00 70.59  ? 55  VAL C CG1 1 
ATOM   1163 C  CG2 . VAL C 2 55  ? 20.307  3.513  17.539 1.00 71.22  ? 55  VAL C CG2 1 
ATOM   1164 N  N   . LEU C 2 56  ? 23.006  6.778  19.188 1.00 57.07  ? 56  LEU C N   1 
ATOM   1165 C  CA  . LEU C 2 56  ? 23.703  8.087  19.188 1.00 53.62  ? 56  LEU C CA  1 
ATOM   1166 C  C   . LEU C 2 56  ? 25.169  7.878  19.574 1.00 53.61  ? 56  LEU C C   1 
ATOM   1167 O  O   . LEU C 2 56  ? 26.053  8.397  18.882 1.00 51.47  ? 56  LEU C O   1 
ATOM   1168 C  CB  . LEU C 2 56  ? 22.989  9.051  20.140 1.00 52.00  ? 56  LEU C CB  1 
ATOM   1169 C  CG  . LEU C 2 56  ? 21.673  9.625  19.623 1.00 51.73  ? 56  LEU C CG  1 
ATOM   1170 C  CD1 . LEU C 2 56  ? 20.944  10.371 20.723 1.00 52.33  ? 56  LEU C CD1 1 
ATOM   1171 C  CD2 . LEU C 2 56  ? 21.901  10.535 18.421 1.00 52.10  ? 56  LEU C CD2 1 
ATOM   1172 N  N   . LEU C 2 57  ? 25.429  7.104  20.619 1.00 56.02  ? 57  LEU C N   1 
ATOM   1173 C  CA  . LEU C 2 57  ? 26.815  6.879  21.096 1.00 59.04  ? 57  LEU C CA  1 
ATOM   1174 C  C   . LEU C 2 57  ? 27.643  6.145  20.032 1.00 61.37  ? 57  LEU C C   1 
ATOM   1175 O  O   . LEU C 2 57  ? 28.830  6.497  19.874 1.00 61.38  ? 57  LEU C O   1 
ATOM   1176 C  CB  . LEU C 2 57  ? 26.758  6.116  22.410 1.00 59.74  ? 57  LEU C CB  1 
ATOM   1177 C  CG  . LEU C 2 57  ? 26.298  6.965  23.589 1.00 58.11  ? 57  LEU C CG  1 
ATOM   1178 C  CD1 . LEU C 2 57  ? 25.826  6.080  24.725 1.00 61.48  ? 57  LEU C CD1 1 
ATOM   1179 C  CD2 . LEU C 2 57  ? 27.411  7.893  24.039 1.00 57.57  ? 57  LEU C CD2 1 
ATOM   1180 N  N   . LYS C 2 58  ? 27.031  5.227  19.284 1.00 63.34  ? 58  LYS C N   1 
ATOM   1181 C  CA  . LYS C 2 58  ? 27.728  4.463  18.217 1.00 68.85  ? 58  LYS C CA  1 
ATOM   1182 C  C   . LYS C 2 58  ? 27.979  5.369  17.002 1.00 68.10  ? 58  LYS C C   1 
ATOM   1183 O  O   . LYS C 2 58  ? 28.853  5.027  16.186 1.00 70.38  ? 58  LYS C O   1 
ATOM   1184 C  CB  . LYS C 2 58  ? 26.931  3.219  17.811 1.00 72.75  ? 58  LYS C CB  1 
ATOM   1185 C  CG  . LYS C 2 58  ? 27.597  2.403  16.712 1.00 78.92  ? 58  LYS C CG  1 
ATOM   1186 C  CD  . LYS C 2 58  ? 27.080  0.993  16.533 1.00 85.17  ? 58  LYS C CD  1 
ATOM   1187 C  CE  . LYS C 2 58  ? 27.948  0.198  15.574 1.00 88.06  ? 58  LYS C CE  1 
ATOM   1188 N  NZ  . LYS C 2 58  ? 27.444  -1.180 15.382 1.00 92.58  ? 58  LYS C NZ  1 
ATOM   1189 N  N   . THR C 2 59  ? 27.260  6.485  16.873 1.00 64.61  ? 59  THR C N   1 
ATOM   1190 C  CA  . THR C 2 59  ? 27.324  7.357  15.672 1.00 64.42  ? 59  THR C CA  1 
ATOM   1191 C  C   . THR C 2 59  ? 27.958  8.706  16.017 1.00 61.51  ? 59  THR C C   1 
ATOM   1192 O  O   . THR C 2 59  ? 27.613  9.700  15.348 1.00 60.82  ? 59  THR C O   1 
ATOM   1193 C  CB  . THR C 2 59  ? 25.930  7.527  15.074 1.00 65.93  ? 59  THR C CB  1 
ATOM   1194 O  OG1 . THR C 2 59  ? 25.294  6.251  15.148 1.00 70.08  ? 59  THR C OG1 1 
ATOM   1195 C  CG2 . THR C 2 59  ? 25.952  8.013  13.644 1.00 67.54  ? 59  THR C CG2 1 
ATOM   1196 N  N   . GLY C 2 60  ? 28.821  8.745  17.030 1.00 59.00  ? 60  GLY C N   1 
ATOM   1197 C  CA  . GLY C 2 60  ? 29.711  9.891  17.309 1.00 59.01  ? 60  GLY C CA  1 
ATOM   1198 C  C   . GLY C 2 60  ? 29.157  10.893 18.325 1.00 55.30  ? 60  GLY C C   1 
ATOM   1199 O  O   . GLY C 2 60  ? 29.746  11.973 18.435 1.00 56.35  ? 60  GLY C O   1 
ATOM   1200 N  N   . ALA C 2 61  ? 28.089  10.588 19.064 1.00 53.84  ? 61  ALA C N   1 
ATOM   1201 C  CA  . ALA C 2 61  ? 27.505  11.551 20.045 1.00 51.93  ? 61  ALA C CA  1 
ATOM   1202 C  C   . ALA C 2 61  ? 28.521  11.795 21.164 1.00 52.25  ? 61  ALA C C   1 
ATOM   1203 O  O   . ALA C 2 61  ? 29.138  10.822 21.629 1.00 53.06  ? 61  ALA C O   1 
ATOM   1204 C  CB  . ALA C 2 61  ? 26.186  11.065 20.587 1.00 52.20  ? 61  ALA C CB  1 
ATOM   1205 N  N   . ASP C 2 62  ? 28.753  13.052 21.530 1.00 51.46  ? 62  ASP C N   1 
ATOM   1206 C  CA  . ASP C 2 62  ? 29.644  13.386 22.668 1.00 53.74  ? 62  ASP C CA  1 
ATOM   1207 C  C   . ASP C 2 62  ? 28.968  12.934 23.965 1.00 53.74  ? 62  ASP C C   1 
ATOM   1208 O  O   . ASP C 2 62  ? 27.918  13.507 24.333 1.00 52.60  ? 62  ASP C O   1 
ATOM   1209 C  CB  . ASP C 2 62  ? 29.991  14.868 22.695 1.00 56.23  ? 62  ASP C CB  1 
ATOM   1210 C  CG  . ASP C 2 62  ? 31.018  15.229 23.751 1.00 61.47  ? 62  ASP C CG  1 
ATOM   1211 O  OD1 . ASP C 2 62  ? 31.363  14.345 24.587 1.00 61.73  ? 62  ASP C OD1 1 
ATOM   1212 O  OD2 . ASP C 2 62  ? 31.454  16.398 23.747 1.00 66.51  ? 62  ASP C OD2 1 
ATOM   1213 N  N   . VAL C 2 63  ? 29.562  11.958 24.648 1.00 56.02  ? 63  VAL C N   1 
ATOM   1214 C  CA  . VAL C 2 63  ? 28.964  11.311 25.850 1.00 55.82  ? 63  VAL C CA  1 
ATOM   1215 C  C   . VAL C 2 63  ? 28.912  12.333 26.980 1.00 53.99  ? 63  VAL C C   1 
ATOM   1216 O  O   . VAL C 2 63  ? 28.082  12.162 27.869 1.00 54.03  ? 63  VAL C O   1 
ATOM   1217 C  CB  . VAL C 2 63  ? 29.734  10.059 26.297 1.00 58.51  ? 63  VAL C CB  1 
ATOM   1218 C  CG1 . VAL C 2 63  ? 31.193  10.368 26.605 1.00 59.33  ? 63  VAL C CG1 1 
ATOM   1219 C  CG2 . VAL C 2 63  ? 29.046  9.403  27.493 1.00 58.60  ? 63  VAL C CG2 1 
ATOM   1220 N  N   . ASN C 2 64  ? 29.789  13.333 26.932 1.00 54.78  ? 64  ASN C N   1 
ATOM   1221 C  CA  . ASN C 2 64  ? 30.001  14.313 28.021 1.00 57.27  ? 64  ASN C CA  1 
ATOM   1222 C  C   . ASN C 2 64  ? 29.697  15.712 27.498 1.00 55.84  ? 64  ASN C C   1 
ATOM   1223 O  O   . ASN C 2 64  ? 30.185  16.689 28.094 1.00 59.02  ? 64  ASN C O   1 
ATOM   1224 C  CB  . ASN C 2 64  ? 31.414  14.185 28.596 1.00 62.02  ? 64  ASN C CB  1 
ATOM   1225 C  CG  . ASN C 2 64  ? 31.598  12.895 29.359 1.00 64.19  ? 64  ASN C CG  1 
ATOM   1226 O  OD1 . ASN C 2 64  ? 30.780  12.556 30.207 1.00 67.68  ? 64  ASN C OD1 1 
ATOM   1227 N  ND2 . ASN C 2 64  ? 32.665  12.172 29.067 1.00 67.23  ? 64  ASN C ND2 1 
ATOM   1228 N  N   . ALA C 2 65  ? 28.873  15.807 26.456 1.00 54.05  ? 65  ALA C N   1 
ATOM   1229 C  CA  . ALA C 2 65  ? 28.325  17.089 25.970 1.00 52.12  ? 65  ALA C CA  1 
ATOM   1230 C  C   . ALA C 2 65  ? 27.702  17.833 27.155 1.00 52.71  ? 65  ALA C C   1 
ATOM   1231 O  O   . ALA C 2 65  ? 26.955  17.229 27.966 1.00 51.52  ? 65  ALA C O   1 
ATOM   1232 C  CB  . ALA C 2 65  ? 27.329  16.868 24.869 1.00 50.72  ? 65  ALA C CB  1 
ATOM   1233 N  N   . SER C 2 66  ? 27.995  19.116 27.208 1.00 52.95  ? 66  SER C N   1 
ATOM   1234 C  CA  . SER C 2 66  ? 27.672  20.040 28.296 1.00 55.08  ? 66  SER C CA  1 
ATOM   1235 C  C   . SER C 2 66  ? 26.649  21.037 27.765 1.00 53.77  ? 66  SER C C   1 
ATOM   1236 O  O   . SER C 2 66  ? 26.973  21.708 26.797 1.00 52.71  ? 66  SER C O   1 
ATOM   1237 C  CB  . SER C 2 66  ? 28.943  20.703 28.740 1.00 57.54  ? 66  SER C CB  1 
ATOM   1238 O  OG  . SER C 2 66  ? 28.766  21.343 29.968 1.00 59.30  ? 66  SER C OG  1 
ATOM   1239 N  N   . ASP C 2 67  ? 25.450  21.091 28.348 1.00 51.61  ? 67  ASP C N   1 
ATOM   1240 C  CA  . ASP C 2 67  ? 24.402  22.057 27.937 1.00 51.02  ? 67  ASP C CA  1 
ATOM   1241 C  C   . ASP C 2 67  ? 24.729  23.416 28.568 1.00 52.77  ? 67  ASP C C   1 
ATOM   1242 O  O   . ASP C 2 67  ? 25.763  23.515 29.230 1.00 54.54  ? 67  ASP C O   1 
ATOM   1243 C  CB  . ASP C 2 67  ? 23.009  21.535 28.282 1.00 50.22  ? 67  ASP C CB  1 
ATOM   1244 C  CG  . ASP C 2 67  ? 22.714  21.423 29.774 1.00 50.99  ? 67  ASP C CG  1 
ATOM   1245 O  OD1 . ASP C 2 67  ? 23.429  22.053 30.571 1.00 53.44  ? 67  ASP C OD1 1 
ATOM   1246 O  OD2 . ASP C 2 67  ? 21.778  20.697 30.117 1.00 48.78  ? 67  ASP C OD2 1 
ATOM   1247 N  N   . PHE C 2 68  ? 23.862  24.414 28.396 1.00 53.57  ? 68  PHE C N   1 
ATOM   1248 C  CA  . PHE C 2 68  ? 24.108  25.815 28.827 1.00 57.28  ? 68  PHE C CA  1 
ATOM   1249 C  C   . PHE C 2 68  ? 24.252  25.896 30.352 1.00 57.94  ? 68  PHE C C   1 
ATOM   1250 O  O   . PHE C 2 68  ? 24.850  26.862 30.800 1.00 59.02  ? 68  PHE C O   1 
ATOM   1251 C  CB  . PHE C 2 68  ? 23.032  26.755 28.273 1.00 58.83  ? 68  PHE C CB  1 
ATOM   1252 C  CG  . PHE C 2 68  ? 23.046  26.887 26.763 1.00 60.67  ? 68  PHE C CG  1 
ATOM   1253 C  CD1 . PHE C 2 68  ? 24.129  26.443 26.014 1.00 61.00  ? 68  PHE C CD1 1 
ATOM   1254 C  CD2 . PHE C 2 68  ? 21.982  27.464 26.086 1.00 63.23  ? 68  PHE C CD2 1 
ATOM   1255 C  CE1 . PHE C 2 68  ? 24.142  26.554 24.628 1.00 63.40  ? 68  PHE C CE1 1 
ATOM   1256 C  CE2 . PHE C 2 68  ? 21.993  27.569 24.699 1.00 65.97  ? 68  PHE C CE2 1 
ATOM   1257 C  CZ  . PHE C 2 68  ? 23.073  27.112 23.970 1.00 63.75  ? 68  PHE C CZ  1 
ATOM   1258 N  N   . HIS C 2 69  ? 23.787  24.895 31.109 1.00 56.35  ? 69  HIS C N   1 
ATOM   1259 C  CA  . HIS C 2 69  ? 23.911  24.860 32.592 1.00 56.62  ? 69  HIS C CA  1 
ATOM   1260 C  C   . HIS C 2 69  ? 25.049  23.923 33.021 1.00 56.30  ? 69  HIS C C   1 
ATOM   1261 O  O   . HIS C 2 69  ? 25.207  23.705 34.239 1.00 57.79  ? 69  HIS C O   1 
ATOM   1262 C  CB  . HIS C 2 69  ? 22.583  24.464 33.239 1.00 57.92  ? 69  HIS C CB  1 
ATOM   1263 C  CG  . HIS C 2 69  ? 22.570  24.660 34.720 1.00 58.56  ? 69  HIS C CG  1 
ATOM   1264 N  ND1 . HIS C 2 69  ? 22.506  23.593 35.607 1.00 58.41  ? 69  HIS C ND1 1 
ATOM   1265 C  CD2 . HIS C 2 69  ? 22.631  25.782 35.472 1.00 60.47  ? 69  HIS C CD2 1 
ATOM   1266 C  CE1 . HIS C 2 69  ? 22.502  24.052 36.844 1.00 60.24  ? 69  HIS C CE1 1 
ATOM   1267 N  NE2 . HIS C 2 69  ? 22.576  25.398 36.792 1.00 61.61  ? 69  HIS C NE2 1 
ATOM   1268 N  N   . GLY C 2 70  ? 25.818  23.392 32.065 1.00 53.60  ? 70  GLY C N   1 
ATOM   1269 C  CA  . GLY C 2 70  ? 26.930  22.471 32.341 1.00 52.31  ? 70  GLY C CA  1 
ATOM   1270 C  C   . GLY C 2 70  ? 26.435  21.079 32.672 1.00 50.71  ? 70  GLY C C   1 
ATOM   1271 O  O   . GLY C 2 70  ? 27.241  20.270 33.108 1.00 54.08  ? 70  GLY C O   1 
ATOM   1272 N  N   . ASP C 2 71  ? 25.156  20.784 32.451 1.00 48.72  ? 71  ASP C N   1 
ATOM   1273 C  CA  . ASP C 2 71  ? 24.617  19.410 32.643 1.00 48.17  ? 71  ASP C CA  1 
ATOM   1274 C  C   . ASP C 2 71  ? 25.001  18.536 31.447 1.00 49.11  ? 71  ASP C C   1 
ATOM   1275 O  O   . ASP C 2 71  ? 24.940  19.012 30.300 1.00 51.34  ? 71  ASP C O   1 
ATOM   1276 C  CB  . ASP C 2 71  ? 23.116  19.425 32.916 1.00 47.68  ? 71  ASP C CB  1 
ATOM   1277 C  CG  . ASP C 2 71  ? 22.814  20.012 34.280 1.00 50.23  ? 71  ASP C CG  1 
ATOM   1278 O  OD1 . ASP C 2 71  ? 23.276  19.401 35.277 1.00 51.12  ? 71  ASP C OD1 1 
ATOM   1279 O  OD2 . ASP C 2 71  ? 22.206  21.120 34.330 1.00 49.80  ? 71  ASP C OD2 1 
ATOM   1280 N  N   . THR C 2 72  ? 25.397  17.306 31.747 1.00 49.17  ? 72  THR C N   1 
ATOM   1281 C  CA  . THR C 2 72  ? 25.744  16.233 30.802 1.00 49.24  ? 72  THR C CA  1 
ATOM   1282 C  C   . THR C 2 72  ? 24.565  15.270 30.726 1.00 47.71  ? 72  THR C C   1 
ATOM   1283 O  O   . THR C 2 72  ? 23.683  15.286 31.589 1.00 47.72  ? 72  THR C O   1 
ATOM   1284 C  CB  . THR C 2 72  ? 27.040  15.541 31.255 1.00 52.40  ? 72  THR C CB  1 
ATOM   1285 O  OG1 . THR C 2 72  ? 26.761  14.792 32.440 1.00 51.05  ? 72  THR C OG1 1 
ATOM   1286 C  CG2 . THR C 2 72  ? 28.151  16.529 31.530 1.00 53.27  ? 72  THR C CG2 1 
ATOM   1287 N  N   . PRO C 2 73  ? 24.504  14.413 29.687 1.00 47.83  ? 73  PRO C N   1 
ATOM   1288 C  CA  . PRO C 2 73  ? 23.476  13.383 29.613 1.00 47.80  ? 73  PRO C CA  1 
ATOM   1289 C  C   . PRO C 2 73  ? 23.399  12.544 30.897 1.00 49.93  ? 73  PRO C C   1 
ATOM   1290 O  O   . PRO C 2 73  ? 22.322  12.059 31.224 1.00 49.34  ? 73  PRO C O   1 
ATOM   1291 C  CB  . PRO C 2 73  ? 23.918  12.525 28.422 1.00 47.88  ? 73  PRO C CB  1 
ATOM   1292 C  CG  . PRO C 2 73  ? 24.701  13.478 27.546 1.00 47.57  ? 73  PRO C CG  1 
ATOM   1293 C  CD  . PRO C 2 73  ? 25.371  14.440 28.493 1.00 47.73  ? 73  PRO C CD  1 
ATOM   1294 N  N   . LEU C 2 74  ? 24.531  12.362 31.582 1.00 53.31  ? 74  LEU C N   1 
ATOM   1295 C  CA  . LEU C 2 74  ? 24.590  11.539 32.819 1.00 54.09  ? 74  LEU C CA  1 
ATOM   1296 C  C   . LEU C 2 74  ? 23.839  12.264 33.951 1.00 53.40  ? 74  LEU C C   1 
ATOM   1297 O  O   . LEU C 2 74  ? 23.058  11.598 34.673 1.00 52.73  ? 74  LEU C O   1 
ATOM   1298 C  CB  . LEU C 2 74  ? 26.052  11.252 33.172 1.00 57.08  ? 74  LEU C CB  1 
ATOM   1299 C  CG  . LEU C 2 74  ? 26.264  10.300 34.350 1.00 59.68  ? 74  LEU C CG  1 
ATOM   1300 C  CD1 . LEU C 2 74  ? 25.563  8.964  34.112 1.00 59.93  ? 74  LEU C CD1 1 
ATOM   1301 C  CD2 . LEU C 2 74  ? 27.746  10.092 34.607 1.00 61.54  ? 74  LEU C CD2 1 
ATOM   1302 N  N   . HIS C 2 75  ? 24.001  13.582 34.065 1.00 51.89  ? 75  HIS C N   1 
ATOM   1303 C  CA  . HIS C 2 75  ? 23.224  14.414 35.016 1.00 50.94  ? 75  HIS C CA  1 
ATOM   1304 C  C   . HIS C 2 75  ? 21.744  14.112 34.831 1.00 50.05  ? 75  HIS C C   1 
ATOM   1305 O  O   . HIS C 2 75  ? 21.085  13.780 35.809 1.00 51.31  ? 75  HIS C O   1 
ATOM   1306 C  CB  . HIS C 2 75  ? 23.490  15.902 34.807 1.00 51.36  ? 75  HIS C CB  1 
ATOM   1307 C  CG  . HIS C 2 75  ? 24.781  16.374 35.373 1.00 52.27  ? 75  HIS C CG  1 
ATOM   1308 N  ND1 . HIS C 2 75  ? 25.908  16.523 34.599 1.00 52.60  ? 75  HIS C ND1 1 
ATOM   1309 C  CD2 . HIS C 2 75  ? 25.113  16.764 36.626 1.00 52.58  ? 75  HIS C CD2 1 
ATOM   1310 C  CE1 . HIS C 2 75  ? 26.888  16.981 35.349 1.00 55.80  ? 75  HIS C CE1 1 
ATOM   1311 N  NE2 . HIS C 2 75  ? 26.416  17.158 36.601 1.00 53.86  ? 75  HIS C NE2 1 
ATOM   1312 N  N   . LEU C 2 76  ? 21.243  14.244 33.605 1.00 48.27  ? 76  LEU C N   1 
ATOM   1313 C  CA  . LEU C 2 76  ? 19.791  14.187 33.335 1.00 47.28  ? 76  LEU C CA  1 
ATOM   1314 C  C   . LEU C 2 76  ? 19.288  12.769 33.617 1.00 48.77  ? 76  LEU C C   1 
ATOM   1315 O  O   . LEU C 2 76  ? 18.243  12.647 34.274 1.00 51.55  ? 76  LEU C O   1 
ATOM   1316 C  CB  . LEU C 2 76  ? 19.505  14.605 31.894 1.00 45.54  ? 76  LEU C CB  1 
ATOM   1317 C  CG  . LEU C 2 76  ? 19.971  16.007 31.493 1.00 45.90  ? 76  LEU C CG  1 
ATOM   1318 C  CD1 . LEU C 2 76  ? 19.324  16.419 30.180 1.00 46.50  ? 76  LEU C CD1 1 
ATOM   1319 C  CD2 . LEU C 2 76  ? 19.679  17.044 32.567 1.00 45.51  ? 76  LEU C CD2 1 
ATOM   1320 N  N   . ALA C 2 77  ? 19.970  11.745 33.099 1.00 48.74  ? 77  ALA C N   1 
ATOM   1321 C  CA  . ALA C 2 77  ? 19.545  10.336 33.228 1.00 52.98  ? 77  ALA C CA  1 
ATOM   1322 C  C   . ALA C 2 77  ? 19.488  9.969  34.722 1.00 56.05  ? 77  ALA C C   1 
ATOM   1323 O  O   . ALA C 2 77  ? 18.526  9.276  35.145 1.00 55.30  ? 77  ALA C O   1 
ATOM   1324 C  CB  . ALA C 2 77  ? 20.486  9.434  32.466 1.00 54.02  ? 77  ALA C CB  1 
ATOM   1325 N  N   . ALA C 2 78  ? 20.487  10.428 35.485 1.00 56.47  ? 78  ALA C N   1 
ATOM   1326 C  CA  . ALA C 2 78  ? 20.667  10.134 36.923 1.00 56.85  ? 78  ALA C CA  1 
ATOM   1327 C  C   . ALA C 2 78  ? 19.545  10.801 37.728 1.00 56.04  ? 78  ALA C C   1 
ATOM   1328 O  O   . ALA C 2 78  ? 19.032  10.174 38.669 1.00 57.08  ? 78  ALA C O   1 
ATOM   1329 C  CB  . ALA C 2 78  ? 22.026  10.613 37.364 1.00 57.92  ? 78  ALA C CB  1 
ATOM   1330 N  N   . MET C 2 79  ? 19.185  12.027 37.360 1.00 53.92  ? 79  MET C N   1 
ATOM   1331 C  CA  . MET C 2 79  ? 18.092  12.802 37.993 1.00 54.47  ? 79  MET C CA  1 
ATOM   1332 C  C   . MET C 2 79  ? 16.738  12.179 37.627 1.00 55.15  ? 79  MET C C   1 
ATOM   1333 O  O   . MET C 2 79  ? 15.853  12.141 38.506 1.00 53.61  ? 79  MET C O   1 
ATOM   1334 C  CB  . MET C 2 79  ? 18.137  14.260 37.536 1.00 54.25  ? 79  MET C CB  1 
ATOM   1335 C  CG  . MET C 2 79  ? 16.985  15.102 38.052 1.00 55.62  ? 79  MET C CG  1 
ATOM   1336 S  SD  . MET C 2 79  ? 17.487  16.823 38.172 1.00 61.46  ? 79  MET C SD  1 
ATOM   1337 C  CE  . MET C 2 79  ? 16.065  17.516 39.014 1.00 61.71  ? 79  MET C CE  1 
ATOM   1338 N  N   . ALA C 2 80  ? 16.586  11.694 36.390 1.00 54.86  ? 80  ALA C N   1 
ATOM   1339 C  CA  . ALA C 2 80  ? 15.296  11.207 35.839 1.00 56.84  ? 80  ALA C CA  1 
ATOM   1340 C  C   . ALA C 2 80  ? 14.963  9.819  36.408 1.00 59.70  ? 80  ALA C C   1 
ATOM   1341 O  O   . ALA C 2 80  ? 13.771  9.525  36.540 1.00 64.18  ? 80  ALA C O   1 
ATOM   1342 C  CB  . ALA C 2 80  ? 15.337  11.194 34.329 1.00 55.20  ? 80  ALA C CB  1 
ATOM   1343 N  N   . GLY C 2 81  ? 15.979  9.006  36.720 1.00 61.26  ? 81  GLY C N   1 
ATOM   1344 C  CA  . GLY C 2 81  ? 15.823  7.658  37.305 1.00 64.22  ? 81  GLY C CA  1 
ATOM   1345 C  C   . GLY C 2 81  ? 15.924  6.548  36.260 1.00 67.31  ? 81  GLY C C   1 
ATOM   1346 O  O   . GLY C 2 81  ? 15.321  5.478  36.477 1.00 69.50  ? 81  GLY C O   1 
ATOM   1347 N  N   . HIS C 2 82  ? 16.673  6.772  35.173 1.00 66.31  ? 82  HIS C N   1 
ATOM   1348 C  CA  . HIS C 2 82  ? 16.842  5.799  34.054 1.00 66.52  ? 82  HIS C CA  1 
ATOM   1349 C  C   . HIS C 2 82  ? 18.147  5.020  34.265 1.00 66.55  ? 82  HIS C C   1 
ATOM   1350 O  O   . HIS C 2 82  ? 19.196  5.452  33.754 1.00 62.84  ? 82  HIS C O   1 
ATOM   1351 C  CB  . HIS C 2 82  ? 16.744  6.529  32.708 1.00 63.94  ? 82  HIS C CB  1 
ATOM   1352 C  CG  . HIS C 2 82  ? 15.390  7.113  32.460 1.00 63.79  ? 82  HIS C CG  1 
ATOM   1353 N  ND1 . HIS C 2 82  ? 15.195  8.458  32.152 1.00 60.07  ? 82  HIS C ND1 1 
ATOM   1354 C  CD2 . HIS C 2 82  ? 14.160  6.553  32.501 1.00 64.62  ? 82  HIS C CD2 1 
ATOM   1355 C  CE1 . HIS C 2 82  ? 13.902  8.684  31.996 1.00 60.14  ? 82  HIS C CE1 1 
ATOM   1356 N  NE2 . HIS C 2 82  ? 13.246  7.536  32.217 1.00 62.87  ? 82  HIS C NE2 1 
ATOM   1357 N  N   . LEU C 2 83  ? 18.090  3.935  35.046 1.00 68.50  ? 83  LEU C N   1 
ATOM   1358 C  CA  . LEU C 2 83  ? 19.295  3.195  35.505 1.00 69.96  ? 83  LEU C CA  1 
ATOM   1359 C  C   . LEU C 2 83  ? 20.040  2.610  34.299 1.00 68.23  ? 83  LEU C C   1 
ATOM   1360 O  O   . LEU C 2 83  ? 21.260  2.849  34.200 1.00 68.97  ? 83  LEU C O   1 
ATOM   1361 C  CB  . LEU C 2 83  ? 18.887  2.094  36.488 1.00 74.26  ? 83  LEU C CB  1 
ATOM   1362 C  CG  . LEU C 2 83  ? 20.015  1.153  36.908 1.00 77.29  ? 83  LEU C CG  1 
ATOM   1363 C  CD1 . LEU C 2 83  ? 21.066  1.891  37.732 1.00 76.45  ? 83  LEU C CD1 1 
ATOM   1364 C  CD2 . LEU C 2 83  ? 19.463  -0.037 37.679 1.00 81.88  ? 83  LEU C CD2 1 
ATOM   1365 N  N   . GLU C 2 84  ? 19.345  1.852  33.444 1.00 68.54  ? 84  GLU C N   1 
ATOM   1366 C  CA  . GLU C 2 84  ? 19.938  1.205  32.236 1.00 73.79  ? 84  GLU C CA  1 
ATOM   1367 C  C   . GLU C 2 84  ? 20.724  2.249  31.425 1.00 72.01  ? 84  GLU C C   1 
ATOM   1368 O  O   . GLU C 2 84  ? 21.826  1.927  30.938 1.00 71.83  ? 84  GLU C O   1 
ATOM   1369 C  CB  . GLU C 2 84  ? 18.850  0.567  31.362 1.00 78.40  ? 84  GLU C CB  1 
ATOM   1370 C  CG  . GLU C 2 84  ? 18.318  -0.749 31.909 1.00 86.20  ? 84  GLU C CG  1 
ATOM   1371 C  CD  . GLU C 2 84  ? 17.382  -1.537 30.997 1.00 92.54  ? 84  GLU C CD  1 
ATOM   1372 O  OE1 . GLU C 2 84  ? 16.968  -1.008 29.952 1.00 97.27  ? 84  GLU C OE1 1 
ATOM   1373 O  OE2 . GLU C 2 84  ? 17.066  -2.691 31.346 1.00 103.71 ? 84  GLU C OE2 1 
ATOM   1374 N  N   . ILE C 2 85  ? 20.171  3.454  31.262 1.00 67.37  ? 85  ILE C N   1 
ATOM   1375 C  CA  . ILE C 2 85  ? 20.808  4.530  30.450 1.00 64.92  ? 85  ILE C CA  1 
ATOM   1376 C  C   . ILE C 2 85  ? 22.060  5.030  31.175 1.00 63.92  ? 85  ILE C C   1 
ATOM   1377 O  O   . ILE C 2 85  ? 23.090  5.243  30.511 1.00 61.03  ? 85  ILE C O   1 
ATOM   1378 C  CB  . ILE C 2 85  ? 19.805  5.652  30.137 1.00 63.69  ? 85  ILE C CB  1 
ATOM   1379 C  CG1 . ILE C 2 85  ? 18.837  5.198  29.041 1.00 65.42  ? 85  ILE C CG1 1 
ATOM   1380 C  CG2 . ILE C 2 85  ? 20.535  6.941  29.759 1.00 62.60  ? 85  ILE C CG2 1 
ATOM   1381 C  CD1 . ILE C 2 85  ? 17.677  6.117  28.822 1.00 64.88  ? 85  ILE C CD1 1 
ATOM   1382 N  N   . VAL C 2 86  ? 21.983  5.204  32.491 1.00 65.91  ? 86  VAL C N   1 
ATOM   1383 C  CA  . VAL C 2 86  ? 23.155  5.606  33.321 1.00 66.88  ? 86  VAL C CA  1 
ATOM   1384 C  C   . VAL C 2 86  ? 24.315  4.640  33.043 1.00 69.60  ? 86  VAL C C   1 
ATOM   1385 O  O   . VAL C 2 86  ? 25.446  5.118  32.844 1.00 70.76  ? 86  VAL C O   1 
ATOM   1386 C  CB  . VAL C 2 86  ? 22.788  5.651  34.811 1.00 66.52  ? 86  VAL C CB  1 
ATOM   1387 C  CG1 . VAL C 2 86  ? 24.024  5.626  35.699 1.00 68.25  ? 86  VAL C CG1 1 
ATOM   1388 C  CG2 . VAL C 2 86  ? 21.917  6.858  35.116 1.00 63.52  ? 86  VAL C CG2 1 
ATOM   1389 N  N   . GLU C 2 87  ? 24.043  3.337  33.026 1.00 72.91  ? 87  GLU C N   1 
ATOM   1390 C  CA  . GLU C 2 87  ? 25.086  2.283  32.875 1.00 77.45  ? 87  GLU C CA  1 
ATOM   1391 C  C   . GLU C 2 87  ? 25.716  2.411  31.485 1.00 74.57  ? 87  GLU C C   1 
ATOM   1392 O  O   . GLU C 2 87  ? 26.950  2.504  31.393 1.00 76.51  ? 87  GLU C O   1 
ATOM   1393 C  CB  . GLU C 2 87  ? 24.487  0.895  33.096 1.00 82.51  ? 87  GLU C CB  1 
ATOM   1394 C  CG  . GLU C 2 87  ? 24.262  0.569  34.568 1.00 88.86  ? 87  GLU C CG  1 
ATOM   1395 C  CD  . GLU C 2 87  ? 23.403  -0.657 34.833 1.00 93.82  ? 87  GLU C CD  1 
ATOM   1396 O  OE1 . GLU C 2 87  ? 22.859  -1.218 33.856 1.00 99.41  ? 87  GLU C OE1 1 
ATOM   1397 O  OE2 . GLU C 2 87  ? 23.279  -1.049 36.010 1.00 96.73  ? 87  GLU C OE2 1 
ATOM   1398 N  N   . VAL C 2 88  ? 24.891  2.456  30.446 1.00 70.56  ? 88  VAL C N   1 
ATOM   1399 C  CA  . VAL C 2 88  ? 25.359  2.621  29.034 1.00 68.70  ? 88  VAL C CA  1 
ATOM   1400 C  C   . VAL C 2 88  ? 26.251  3.868  28.946 1.00 64.80  ? 88  VAL C C   1 
ATOM   1401 O  O   . VAL C 2 88  ? 27.346  3.760  28.403 1.00 64.89  ? 88  VAL C O   1 
ATOM   1402 C  CB  . VAL C 2 88  ? 24.177  2.686  28.052 1.00 66.89  ? 88  VAL C CB  1 
ATOM   1403 C  CG1 . VAL C 2 88  ? 24.648  2.899  26.626 1.00 68.92  ? 88  VAL C CG1 1 
ATOM   1404 C  CG2 . VAL C 2 88  ? 23.312  1.436  28.139 1.00 68.77  ? 88  VAL C CG2 1 
ATOM   1405 N  N   . LEU C 2 89  ? 25.822  5.002  29.505 1.00 63.25  ? 89  LEU C N   1 
ATOM   1406 C  CA  . LEU C 2 89  ? 26.613  6.262  29.452 1.00 63.32  ? 89  LEU C CA  1 
ATOM   1407 C  C   . LEU C 2 89  ? 27.983  6.017  30.099 1.00 65.27  ? 89  LEU C C   1 
ATOM   1408 O  O   . LEU C 2 89  ? 29.003  6.427  29.513 1.00 64.74  ? 89  LEU C O   1 
ATOM   1409 C  CB  . LEU C 2 89  ? 25.858  7.394  30.163 1.00 60.05  ? 89  LEU C CB  1 
ATOM   1410 C  CG  . LEU C 2 89  ? 24.586  7.885  29.471 1.00 57.83  ? 89  LEU C CG  1 
ATOM   1411 C  CD1 . LEU C 2 89  ? 23.849  8.864  30.358 1.00 56.98  ? 89  LEU C CD1 1 
ATOM   1412 C  CD2 . LEU C 2 89  ? 24.893  8.519  28.127 1.00 58.17  ? 89  LEU C CD2 1 
ATOM   1413 N  N   . LEU C 2 90  ? 27.995  5.384  31.270 1.00 67.64  ? 90  LEU C N   1 
ATOM   1414 C  CA  . LEU C 2 90  ? 29.237  5.052  32.017 1.00 72.88  ? 90  LEU C CA  1 
ATOM   1415 C  C   . LEU C 2 90  ? 30.164  4.195  31.148 1.00 74.27  ? 90  LEU C C   1 
ATOM   1416 O  O   . LEU C 2 90  ? 31.360  4.525  31.100 1.00 75.48  ? 90  LEU C O   1 
ATOM   1417 C  CB  . LEU C 2 90  ? 28.866  4.345  33.323 1.00 74.87  ? 90  LEU C CB  1 
ATOM   1418 C  CG  . LEU C 2 90  ? 28.256  5.251  34.389 1.00 75.39  ? 90  LEU C CG  1 
ATOM   1419 C  CD1 . LEU C 2 90  ? 27.888  4.455  35.632 1.00 77.44  ? 90  LEU C CD1 1 
ATOM   1420 C  CD2 . LEU C 2 90  ? 29.202  6.391  34.743 1.00 75.90  ? 90  LEU C CD2 1 
ATOM   1421 N  N   . LYS C 2 91  ? 29.628  3.169  30.472 1.00 76.43  ? 91  LYS C N   1 
ATOM   1422 C  CA  . LYS C 2 91  ? 30.390  2.260  29.560 1.00 82.89  ? 91  LYS C CA  1 
ATOM   1423 C  C   . LYS C 2 91  ? 31.120  3.071  28.479 1.00 80.13  ? 91  LYS C C   1 
ATOM   1424 O  O   . LYS C 2 91  ? 32.264  2.708  28.129 1.00 81.11  ? 91  LYS C O   1 
ATOM   1425 C  CB  . LYS C 2 91  ? 29.459  1.270  28.853 1.00 87.82  ? 91  LYS C CB  1 
ATOM   1426 C  CG  . LYS C 2 91  ? 28.874  0.171  29.727 1.00 93.90  ? 91  LYS C CG  1 
ATOM   1427 C  CD  . LYS C 2 91  ? 27.933  -0.746 28.964 1.00 97.18  ? 91  LYS C CD  1 
ATOM   1428 C  CE  . LYS C 2 91  ? 27.603  -2.015 29.722 1.00 100.89 ? 91  LYS C CE  1 
ATOM   1429 N  NZ  . LYS C 2 91  ? 26.978  -1.717 31.031 1.00 101.80 ? 91  LYS C NZ  1 
ATOM   1430 N  N   . HIS C 2 92  ? 30.467  4.110  27.949 1.00 75.44  ? 92  HIS C N   1 
ATOM   1431 C  CA  . HIS C 2 92  ? 30.981  4.954  26.841 1.00 72.82  ? 92  HIS C CA  1 
ATOM   1432 C  C   . HIS C 2 92  ? 31.751  6.155  27.403 1.00 69.48  ? 92  HIS C C   1 
ATOM   1433 O  O   . HIS C 2 92  ? 32.023  7.085  26.633 1.00 70.14  ? 92  HIS C O   1 
ATOM   1434 C  CB  . HIS C 2 92  ? 29.829  5.334  25.908 1.00 72.49  ? 92  HIS C CB  1 
ATOM   1435 C  CG  . HIS C 2 92  ? 29.317  4.176  25.117 1.00 75.76  ? 92  HIS C CG  1 
ATOM   1436 N  ND1 . HIS C 2 92  ? 28.456  3.232  25.659 1.00 78.25  ? 92  HIS C ND1 1 
ATOM   1437 C  CD2 . HIS C 2 92  ? 29.559  3.785  23.843 1.00 75.24  ? 92  HIS C CD2 1 
ATOM   1438 C  CE1 . HIS C 2 92  ? 28.184  2.316  24.745 1.00 79.05  ? 92  HIS C CE1 1 
ATOM   1439 N  NE2 . HIS C 2 92  ? 28.846  2.636  23.624 1.00 77.20  ? 92  HIS C NE2 1 
ATOM   1440 N  N   . GLY C 2 93  ? 32.121  6.113  28.682 1.00 68.53  ? 93  GLY C N   1 
ATOM   1441 C  CA  . GLY C 2 93  ? 33.081  7.052  29.295 1.00 70.37  ? 93  GLY C CA  1 
ATOM   1442 C  C   . GLY C 2 93  ? 32.419  8.330  29.798 1.00 68.63  ? 93  GLY C C   1 
ATOM   1443 O  O   . GLY C 2 93  ? 33.090  9.387  29.799 1.00 69.60  ? 93  GLY C O   1 
ATOM   1444 N  N   . ALA C 2 94  ? 31.158  8.261  30.234 1.00 66.41  ? 94  ALA C N   1 
ATOM   1445 C  CA  . ALA C 2 94  ? 30.462  9.414  30.851 1.00 67.34  ? 94  ALA C CA  1 
ATOM   1446 C  C   . ALA C 2 94  ? 31.253  9.827  32.094 1.00 69.06  ? 94  ALA C C   1 
ATOM   1447 O  O   . ALA C 2 94  ? 31.750  8.926  32.784 1.00 72.08  ? 94  ALA C O   1 
ATOM   1448 C  CB  . ALA C 2 94  ? 29.035  9.067  31.174 1.00 65.72  ? 94  ALA C CB  1 
ATOM   1449 N  N   . ASP C 2 95  ? 31.404  11.133 32.328 1.00 68.01  ? 95  ASP C N   1 
ATOM   1450 C  CA  . ASP C 2 95  ? 32.317  11.707 33.356 1.00 70.87  ? 95  ASP C CA  1 
ATOM   1451 C  C   . ASP C 2 95  ? 31.533  11.952 34.661 1.00 69.94  ? 95  ASP C C   1 
ATOM   1452 O  O   . ASP C 2 95  ? 30.749  12.934 34.735 1.00 67.81  ? 95  ASP C O   1 
ATOM   1453 C  CB  . ASP C 2 95  ? 32.995  12.952 32.782 1.00 72.12  ? 95  ASP C CB  1 
ATOM   1454 C  CG  . ASP C 2 95  ? 33.800  13.762 33.777 1.00 76.60  ? 95  ASP C CG  1 
ATOM   1455 O  OD1 . ASP C 2 95  ? 34.088  13.242 34.884 1.00 78.49  ? 95  ASP C OD1 1 
ATOM   1456 O  OD2 . ASP C 2 95  ? 34.116  14.920 33.443 1.00 79.05  ? 95  ASP C OD2 1 
ATOM   1457 N  N   . VAL C 2 96  ? 31.745  11.106 35.673 1.00 72.11  ? 96  VAL C N   1 
ATOM   1458 C  CA  . VAL C 2 96  ? 30.945  11.103 36.940 1.00 71.12  ? 96  VAL C CA  1 
ATOM   1459 C  C   . VAL C 2 96  ? 31.363  12.292 37.812 1.00 70.91  ? 96  VAL C C   1 
ATOM   1460 O  O   . VAL C 2 96  ? 30.629  12.612 38.760 1.00 68.25  ? 96  VAL C O   1 
ATOM   1461 C  CB  . VAL C 2 96  ? 31.060  9.767  37.696 1.00 75.97  ? 96  VAL C CB  1 
ATOM   1462 C  CG1 . VAL C 2 96  ? 30.633  8.602  36.815 1.00 76.81  ? 96  VAL C CG1 1 
ATOM   1463 C  CG2 . VAL C 2 96  ? 32.452  9.531  38.278 1.00 80.22  ? 96  VAL C CG2 1 
ATOM   1464 N  N   . ASN C 2 97  ? 32.472  12.943 37.463 1.00 74.11  ? 97  ASN C N   1 
ATOM   1465 C  CA  . ASN C 2 97  ? 33.015  14.132 38.164 1.00 76.85  ? 97  ASN C CA  1 
ATOM   1466 C  C   . ASN C 2 97  ? 32.566  15.411 37.451 1.00 73.24  ? 97  ASN C C   1 
ATOM   1467 O  O   . ASN C 2 97  ? 33.027  16.483 37.842 1.00 73.84  ? 97  ASN C O   1 
ATOM   1468 C  CB  . ASN C 2 97  ? 34.542  14.071 38.233 1.00 82.32  ? 97  ASN C CB  1 
ATOM   1469 C  CG  . ASN C 2 97  ? 35.088  14.408 39.597 1.00 87.28  ? 97  ASN C CG  1 
ATOM   1470 O  OD1 . ASN C 2 97  ? 34.338  14.497 40.564 1.00 91.85  ? 97  ASN C OD1 1 
ATOM   1471 N  ND2 . ASN C 2 97  ? 36.396  14.592 39.684 1.00 92.90  ? 97  ASN C ND2 1 
ATOM   1472 N  N   . ALA C 2 98  ? 31.731  15.303 36.417 1.00 70.99  ? 98  ALA C N   1 
ATOM   1473 C  CA  . ALA C 2 98  ? 31.207  16.469 35.672 1.00 69.26  ? 98  ALA C CA  1 
ATOM   1474 C  C   . ALA C 2 98  ? 30.288  17.274 36.603 1.00 67.34  ? 98  ALA C C   1 
ATOM   1475 O  O   . ALA C 2 98  ? 29.320  16.699 37.123 1.00 64.20  ? 98  ALA C O   1 
ATOM   1476 C  CB  . ALA C 2 98  ? 30.495  16.026 34.412 1.00 68.26  ? 98  ALA C CB  1 
ATOM   1477 N  N   . GLN C 2 99  ? 30.655  18.532 36.854 1.00 68.53  ? 99  GLN C N   1 
ATOM   1478 C  CA  . GLN C 2 99  ? 29.907  19.508 37.679 1.00 70.95  ? 99  GLN C CA  1 
ATOM   1479 C  C   . GLN C 2 99  ? 29.173  20.456 36.732 1.00 67.80  ? 99  GLN C C   1 
ATOM   1480 O  O   . GLN C 2 99  ? 29.840  21.002 35.835 1.00 67.64  ? 99  GLN C O   1 
ATOM   1481 C  CB  . GLN C 2 99  ? 30.861  20.323 38.557 1.00 75.46  ? 99  GLN C CB  1 
ATOM   1482 C  CG  . GLN C 2 99  ? 31.188  19.691 39.900 1.00 79.47  ? 99  GLN C CG  1 
ATOM   1483 C  CD  . GLN C 2 99  ? 31.845  20.700 40.811 1.00 82.01  ? 99  GLN C CD  1 
ATOM   1484 O  OE1 . GLN C 2 99  ? 32.663  21.509 40.382 1.00 83.96  ? 99  GLN C OE1 1 
ATOM   1485 N  NE2 . GLN C 2 99  ? 31.469  20.682 42.076 1.00 85.26  ? 99  GLN C NE2 1 
ATOM   1486 N  N   . ASP C 2 100 ? 27.863  20.642 36.917 1.00 63.07  ? 100 ASP C N   1 
ATOM   1487 C  CA  . ASP C 2 100 ? 27.103  21.716 36.229 1.00 61.74  ? 100 ASP C CA  1 
ATOM   1488 C  C   . ASP C 2 100 ? 27.462  23.032 36.922 1.00 63.35  ? 100 ASP C C   1 
ATOM   1489 O  O   . ASP C 2 100 ? 28.228  22.982 37.887 1.00 64.53  ? 100 ASP C O   1 
ATOM   1490 C  CB  . ASP C 2 100 ? 25.610  21.398 36.181 1.00 59.14  ? 100 ASP C CB  1 
ATOM   1491 C  CG  . ASP C 2 100 ? 24.934  21.262 37.533 1.00 58.80  ? 100 ASP C CG  1 
ATOM   1492 O  OD1 . ASP C 2 100 ? 25.451  21.834 38.527 1.00 59.05  ? 100 ASP C OD1 1 
ATOM   1493 O  OD2 . ASP C 2 100 ? 23.888  20.591 37.577 1.00 57.76  ? 100 ASP C OD2 1 
ATOM   1494 N  N   . THR C 2 101 ? 26.947  24.160 36.442 1.00 63.94  ? 101 THR C N   1 
ATOM   1495 C  CA  . THR C 2 101 ? 27.377  25.507 36.887 1.00 67.16  ? 101 THR C CA  1 
ATOM   1496 C  C   . THR C 2 101 ? 26.831  25.801 38.294 1.00 66.99  ? 101 THR C C   1 
ATOM   1497 O  O   . THR C 2 101 ? 27.213  26.838 38.849 1.00 70.43  ? 101 THR C O   1 
ATOM   1498 C  CB  . THR C 2 101 ? 27.008  26.574 35.851 1.00 68.26  ? 101 THR C CB  1 
ATOM   1499 O  OG1 . THR C 2 101 ? 25.595  26.610 35.681 1.00 70.24  ? 101 THR C OG1 1 
ATOM   1500 C  CG2 . THR C 2 101 ? 27.660  26.320 34.514 1.00 68.26  ? 101 THR C CG2 1 
ATOM   1501 N  N   . TRP C 2 102 ? 26.002  24.913 38.861 1.00 64.62  ? 102 TRP C N   1 
ATOM   1502 C  CA  . TRP C 2 102 ? 25.568  24.962 40.287 1.00 62.55  ? 102 TRP C CA  1 
ATOM   1503 C  C   . TRP C 2 102 ? 26.385  23.965 41.119 1.00 63.71  ? 102 TRP C C   1 
ATOM   1504 O  O   . TRP C 2 102 ? 26.072  23.811 42.297 1.00 63.02  ? 102 TRP C O   1 
ATOM   1505 C  CB  . TRP C 2 102 ? 24.054  24.706 40.425 1.00 59.19  ? 102 TRP C CB  1 
ATOM   1506 C  CG  . TRP C 2 102 ? 23.182  25.879 40.081 1.00 56.51  ? 102 TRP C CG  1 
ATOM   1507 C  CD1 . TRP C 2 102 ? 23.581  27.140 39.734 1.00 57.51  ? 102 TRP C CD1 1 
ATOM   1508 C  CD2 . TRP C 2 102 ? 21.741  25.901 40.058 1.00 53.07  ? 102 TRP C CD2 1 
ATOM   1509 N  NE1 . TRP C 2 102 ? 22.494  27.939 39.499 1.00 56.44  ? 102 TRP C NE1 1 
ATOM   1510 C  CE2 . TRP C 2 102 ? 21.352  27.211 39.701 1.00 53.49  ? 102 TRP C CE2 1 
ATOM   1511 C  CE3 . TRP C 2 102 ? 20.748  24.949 40.307 1.00 49.89  ? 102 TRP C CE3 1 
ATOM   1512 C  CZ2 . TRP C 2 102 ? 20.016  27.590 39.607 1.00 51.78  ? 102 TRP C CZ2 1 
ATOM   1513 C  CZ3 . TRP C 2 102 ? 19.430  25.332 40.229 1.00 50.04  ? 102 TRP C CZ3 1 
ATOM   1514 C  CH2 . TRP C 2 102 ? 19.072  26.630 39.880 1.00 50.16  ? 102 TRP C CH2 1 
ATOM   1515 N  N   . GLY C 2 103 ? 27.387  23.317 40.524 1.00 63.26  ? 103 GLY C N   1 
ATOM   1516 C  CA  . GLY C 2 103 ? 28.375  22.497 41.245 1.00 64.69  ? 103 GLY C CA  1 
ATOM   1517 C  C   . GLY C 2 103 ? 27.893  21.081 41.511 1.00 63.77  ? 103 GLY C C   1 
ATOM   1518 O  O   . GLY C 2 103 ? 28.575  20.364 42.259 1.00 68.46  ? 103 GLY C O   1 
ATOM   1519 N  N   . TYR C 2 104 ? 26.784  20.664 40.909 1.00 61.72  ? 104 TYR C N   1 
ATOM   1520 C  CA  . TYR C 2 104 ? 26.238  19.290 41.062 1.00 60.87  ? 104 TYR C CA  1 
ATOM   1521 C  C   . TYR C 2 104 ? 26.967  18.330 40.114 1.00 61.38  ? 104 TYR C C   1 
ATOM   1522 O  O   . TYR C 2 104 ? 27.191  18.673 38.935 1.00 58.89  ? 104 TYR C O   1 
ATOM   1523 C  CB  . TYR C 2 104 ? 24.730  19.275 40.827 1.00 59.61  ? 104 TYR C CB  1 
ATOM   1524 C  CG  . TYR C 2 104 ? 23.933  20.037 41.853 1.00 59.57  ? 104 TYR C CG  1 
ATOM   1525 C  CD1 . TYR C 2 104 ? 23.901  19.634 43.183 1.00 62.61  ? 104 TYR C CD1 1 
ATOM   1526 C  CD2 . TYR C 2 104 ? 23.212  21.166 41.501 1.00 59.16  ? 104 TYR C CD2 1 
ATOM   1527 C  CE1 . TYR C 2 104 ? 23.166  20.330 44.135 1.00 60.69  ? 104 TYR C CE1 1 
ATOM   1528 C  CE2 . TYR C 2 104 ? 22.463  21.865 42.433 1.00 59.16  ? 104 TYR C CE2 1 
ATOM   1529 C  CZ  . TYR C 2 104 ? 22.440  21.447 43.757 1.00 60.70  ? 104 TYR C CZ  1 
ATOM   1530 O  OH  . TYR C 2 104 ? 21.713  22.146 44.681 1.00 61.46  ? 104 TYR C OH  1 
ATOM   1531 N  N   . ILE C 2 105 ? 27.359  17.171 40.639 1.00 60.21  ? 105 ILE C N   1 
ATOM   1532 C  CA  . ILE C 2 105 ? 27.743  15.982 39.827 1.00 61.07  ? 105 ILE C CA  1 
ATOM   1533 C  C   . ILE C 2 105 ? 26.518  15.082 39.719 1.00 58.38  ? 105 ILE C C   1 
ATOM   1534 O  O   . ILE C 2 105 ? 25.547  15.257 40.451 1.00 56.50  ? 105 ILE C O   1 
ATOM   1535 C  CB  . ILE C 2 105 ? 28.978  15.258 40.414 1.00 63.37  ? 105 ILE C CB  1 
ATOM   1536 C  CG1 . ILE C 2 105 ? 28.694  14.585 41.761 1.00 65.29  ? 105 ILE C CG1 1 
ATOM   1537 C  CG2 . ILE C 2 105 ? 30.145  16.228 40.502 1.00 66.40  ? 105 ILE C CG2 1 
ATOM   1538 C  CD1 . ILE C 2 105 ? 29.860  13.779 42.314 1.00 67.18  ? 105 ILE C CD1 1 
ATOM   1539 N  N   . PRO C 2 106 ? 26.481  14.161 38.737 1.00 58.68  ? 106 PRO C N   1 
ATOM   1540 C  CA  . PRO C 2 106 ? 25.326  13.279 38.566 1.00 58.57  ? 106 PRO C CA  1 
ATOM   1541 C  C   . PRO C 2 106 ? 24.846  12.584 39.843 1.00 60.01  ? 106 PRO C C   1 
ATOM   1542 O  O   . PRO C 2 106 ? 23.662  12.577 40.072 1.00 59.03  ? 106 PRO C O   1 
ATOM   1543 C  CB  . PRO C 2 106 ? 25.848  12.298 37.520 1.00 59.35  ? 106 PRO C CB  1 
ATOM   1544 C  CG  . PRO C 2 106 ? 26.691  13.188 36.634 1.00 58.67  ? 106 PRO C CG  1 
ATOM   1545 C  CD  . PRO C 2 106 ? 27.441  14.053 37.627 1.00 58.25  ? 106 PRO C CD  1 
ATOM   1546 N  N   . PHE C 2 107 ? 25.770  12.036 40.641 1.00 64.94  ? 107 PHE C N   1 
ATOM   1547 C  CA  . PHE C 2 107 ? 25.469  11.381 41.940 1.00 65.12  ? 107 PHE C CA  1 
ATOM   1548 C  C   . PHE C 2 107 ? 24.616  12.314 42.812 1.00 62.30  ? 107 PHE C C   1 
ATOM   1549 O  O   . PHE C 2 107 ? 23.601  11.840 43.386 1.00 62.63  ? 107 PHE C O   1 
ATOM   1550 C  CB  . PHE C 2 107 ? 26.758  10.996 42.670 1.00 69.26  ? 107 PHE C CB  1 
ATOM   1551 C  CG  . PHE C 2 107 ? 26.527  10.575 44.094 1.00 70.10  ? 107 PHE C CG  1 
ATOM   1552 C  CD1 . PHE C 2 107 ? 26.100  9.290  44.386 1.00 72.31  ? 107 PHE C CD1 1 
ATOM   1553 C  CD2 . PHE C 2 107 ? 26.654  11.485 45.133 1.00 71.84  ? 107 PHE C CD2 1 
ATOM   1554 C  CE1 . PHE C 2 107 ? 25.853  8.904  45.697 1.00 73.20  ? 107 PHE C CE1 1 
ATOM   1555 C  CE2 . PHE C 2 107 ? 26.401  11.101 46.443 1.00 73.71  ? 107 PHE C CE2 1 
ATOM   1556 C  CZ  . PHE C 2 107 ? 26.006  9.810  46.722 1.00 74.39  ? 107 PHE C CZ  1 
ATOM   1557 N  N   . ASP C 2 108 ? 25.019  13.589 42.922 1.00 60.32  ? 108 ASP C N   1 
ATOM   1558 C  CA  . ASP C 2 108 ? 24.315  14.613 43.745 1.00 59.21  ? 108 ASP C CA  1 
ATOM   1559 C  C   . ASP C 2 108 ? 22.838  14.622 43.359 1.00 57.91  ? 108 ASP C C   1 
ATOM   1560 O  O   . ASP C 2 108 ? 22.003  14.531 44.253 1.00 59.97  ? 108 ASP C O   1 
ATOM   1561 C  CB  . ASP C 2 108 ? 24.919  16.015 43.586 1.00 59.46  ? 108 ASP C CB  1 
ATOM   1562 C  CG  . ASP C 2 108 ? 26.347  16.135 44.089 1.00 64.08  ? 108 ASP C CG  1 
ATOM   1563 O  OD1 . ASP C 2 108 ? 26.689  15.397 45.033 1.00 68.98  ? 108 ASP C OD1 1 
ATOM   1564 O  OD2 . ASP C 2 108 ? 27.106  16.970 43.545 1.00 64.53  ? 108 ASP C OD2 1 
ATOM   1565 N  N   . LEU C 2 109 ? 22.528  14.703 42.059 1.00 54.66  ? 109 LEU C N   1 
ATOM   1566 C  CA  . LEU C 2 109 ? 21.130  14.734 41.567 1.00 52.28  ? 109 LEU C CA  1 
ATOM   1567 C  C   . LEU C 2 109 ? 20.436  13.391 41.859 1.00 51.94  ? 109 LEU C C   1 
ATOM   1568 O  O   . LEU C 2 109 ? 19.282  13.424 42.311 1.00 52.97  ? 109 LEU C O   1 
ATOM   1569 C  CB  . LEU C 2 109 ? 21.109  15.080 40.071 1.00 51.60  ? 109 LEU C CB  1 
ATOM   1570 C  CG  . LEU C 2 109 ? 21.708  16.437 39.702 1.00 51.14  ? 109 LEU C CG  1 
ATOM   1571 C  CD1 . LEU C 2 109 ? 21.530  16.729 38.225 1.00 50.37  ? 109 LEU C CD1 1 
ATOM   1572 C  CD2 . LEU C 2 109 ? 21.090  17.543 40.530 1.00 51.45  ? 109 LEU C CD2 1 
ATOM   1573 N  N   . ALA C 2 110 ? 21.078  12.255 41.596 1.00 52.32  ? 110 ALA C N   1 
ATOM   1574 C  CA  . ALA C 2 110 ? 20.504  10.916 41.869 1.00 56.53  ? 110 ALA C CA  1 
ATOM   1575 C  C   . ALA C 2 110 ? 20.182  10.812 43.363 1.00 59.77  ? 110 ALA C C   1 
ATOM   1576 O  O   . ALA C 2 110 ? 19.056  10.409 43.699 1.00 63.18  ? 110 ALA C O   1 
ATOM   1577 C  CB  . ALA C 2 110 ? 21.461  9.819  41.448 1.00 59.06  ? 110 ALA C CB  1 
ATOM   1578 N  N   . ALA C 2 111 ? 21.127  11.204 44.220 1.00 60.98  ? 111 ALA C N   1 
ATOM   1579 C  CA  . ALA C 2 111 ? 21.025  11.068 45.693 1.00 63.80  ? 111 ALA C CA  1 
ATOM   1580 C  C   . ALA C 2 111 ? 19.902  11.982 46.185 1.00 64.07  ? 111 ALA C C   1 
ATOM   1581 O  O   . ALA C 2 111 ? 18.954  11.474 46.807 1.00 62.71  ? 111 ALA C O   1 
ATOM   1582 C  CB  . ALA C 2 111 ? 22.349  11.386 46.346 1.00 64.34  ? 111 ALA C CB  1 
ATOM   1583 N  N   . TRP C 2 112 ? 19.960  13.267 45.827 1.00 65.17  ? 112 TRP C N   1 
ATOM   1584 C  CA  . TRP C 2 112 ? 18.883  14.252 46.117 1.00 63.83  ? 112 TRP C CA  1 
ATOM   1585 C  C   . TRP C 2 112 ? 17.520  13.704 45.663 1.00 62.24  ? 112 TRP C C   1 
ATOM   1586 O  O   . TRP C 2 112 ? 16.547  13.868 46.409 1.00 60.30  ? 112 TRP C O   1 
ATOM   1587 C  CB  . TRP C 2 112 ? 19.179  15.605 45.466 1.00 63.53  ? 112 TRP C CB  1 
ATOM   1588 C  CG  . TRP C 2 112 ? 17.999  16.520 45.533 1.00 62.75  ? 112 TRP C CG  1 
ATOM   1589 C  CD1 . TRP C 2 112 ? 17.643  17.320 46.575 1.00 62.06  ? 112 TRP C CD1 1 
ATOM   1590 C  CD2 . TRP C 2 112 ? 16.955  16.643 44.552 1.00 62.16  ? 112 TRP C CD2 1 
ATOM   1591 N  NE1 . TRP C 2 112 ? 16.463  17.955 46.298 1.00 64.20  ? 112 TRP C NE1 1 
ATOM   1592 C  CE2 . TRP C 2 112 ? 16.020  17.566 45.062 1.00 62.42  ? 112 TRP C CE2 1 
ATOM   1593 C  CE3 . TRP C 2 112 ? 16.729  16.085 43.289 1.00 62.03  ? 112 TRP C CE3 1 
ATOM   1594 C  CZ2 . TRP C 2 112 ? 14.882  17.942 44.351 1.00 62.46  ? 112 TRP C CZ2 1 
ATOM   1595 C  CZ3 . TRP C 2 112 ? 15.601  16.452 42.587 1.00 60.32  ? 112 TRP C CZ3 1 
ATOM   1596 C  CH2 . TRP C 2 112 ? 14.688  17.364 43.117 1.00 62.91  ? 112 TRP C CH2 1 
ATOM   1597 N  N   . ALA C 2 113 ? 17.452  13.094 44.477 1.00 59.72  ? 113 ALA C N   1 
ATOM   1598 C  CA  . ALA C 2 113 ? 16.190  12.642 43.839 1.00 59.76  ? 113 ALA C CA  1 
ATOM   1599 C  C   . ALA C 2 113 ? 15.649  11.381 44.524 1.00 61.52  ? 113 ALA C C   1 
ATOM   1600 O  O   . ALA C 2 113 ? 14.452  11.100 44.361 1.00 62.91  ? 113 ALA C O   1 
ATOM   1601 C  CB  . ALA C 2 113 ? 16.409  12.406 42.355 1.00 58.65  ? 113 ALA C CB  1 
ATOM   1602 N  N   . GLY C 2 114 ? 16.499  10.627 45.227 1.00 64.34  ? 114 GLY C N   1 
ATOM   1603 C  CA  . GLY C 2 114 ? 16.131  9.331  45.823 1.00 65.18  ? 114 GLY C CA  1 
ATOM   1604 C  C   . GLY C 2 114 ? 16.176  8.219  44.789 1.00 65.54  ? 114 GLY C C   1 
ATOM   1605 O  O   . GLY C 2 114 ? 15.358  7.296  44.883 1.00 67.55  ? 114 GLY C O   1 
ATOM   1606 N  N   . ASN C 2 115 ? 17.084  8.323  43.815 1.00 65.20  ? 115 ASN C N   1 
ATOM   1607 C  CA  . ASN C 2 115 ? 17.355  7.270  42.800 1.00 65.76  ? 115 ASN C CA  1 
ATOM   1608 C  C   . ASN C 2 115 ? 18.517  6.425  43.329 1.00 68.07  ? 115 ASN C C   1 
ATOM   1609 O  O   . ASN C 2 115 ? 19.633  6.542  42.799 1.00 68.04  ? 115 ASN C O   1 
ATOM   1610 C  CB  . ASN C 2 115 ? 17.596  7.877  41.406 1.00 64.82  ? 115 ASN C CB  1 
ATOM   1611 C  CG  . ASN C 2 115 ? 16.393  8.631  40.870 1.00 63.05  ? 115 ASN C CG  1 
ATOM   1612 O  OD1 . ASN C 2 115 ? 15.243  8.225  41.082 1.00 62.66  ? 115 ASN C OD1 1 
ATOM   1613 N  ND2 . ASN C 2 115 ? 16.644  9.730  40.167 1.00 61.01  ? 115 ASN C ND2 1 
ATOM   1614 N  N   . GLU C 2 116 ? 18.253  5.633  44.378 1.00 73.08  ? 116 GLU C N   1 
ATOM   1615 C  CA  . GLU C 2 116 ? 19.288  4.978  45.223 1.00 76.70  ? 116 GLU C CA  1 
ATOM   1616 C  C   . GLU C 2 116 ? 20.127  4.017  44.377 1.00 76.48  ? 116 GLU C C   1 
ATOM   1617 O  O   . GLU C 2 116 ? 21.374  4.085  44.481 1.00 77.28  ? 116 GLU C O   1 
ATOM   1618 C  CB  . GLU C 2 116 ? 18.640  4.262  46.409 1.00 81.65  ? 116 GLU C CB  1 
ATOM   1619 C  CG  . GLU C 2 116 ? 18.104  5.226  47.455 1.00 83.73  ? 116 GLU C CG  1 
ATOM   1620 C  CD  . GLU C 2 116 ? 18.101  4.704  48.881 1.00 88.80  ? 116 GLU C CD  1 
ATOM   1621 O  OE1 . GLU C 2 116 ? 18.295  3.482  49.067 1.00 94.39  ? 116 GLU C OE1 1 
ATOM   1622 O  OE2 . GLU C 2 116 ? 17.911  5.526  49.805 1.00 93.80  ? 116 GLU C OE2 1 
ATOM   1623 N  N   . ASP C 2 117 ? 19.478  3.194  43.546 1.00 77.38  ? 117 ASP C N   1 
ATOM   1624 C  CA  . ASP C 2 117 ? 20.156  2.244  42.619 1.00 81.27  ? 117 ASP C CA  1 
ATOM   1625 C  C   . ASP C 2 117 ? 21.210  2.986  41.785 1.00 80.49  ? 117 ASP C C   1 
ATOM   1626 O  O   . ASP C 2 117 ? 22.313  2.420  41.611 1.00 81.12  ? 117 ASP C O   1 
ATOM   1627 C  CB  . ASP C 2 117 ? 19.162  1.534  41.693 1.00 84.09  ? 117 ASP C CB  1 
ATOM   1628 C  CG  . ASP C 2 117 ? 18.429  0.375  42.346 1.00 89.64  ? 117 ASP C CG  1 
ATOM   1629 O  OD1 . ASP C 2 117 ? 18.458  0.286  43.583 1.00 92.15  ? 117 ASP C OD1 1 
ATOM   1630 O  OD2 . ASP C 2 117 ? 17.844  -0.432 41.608 1.00 95.54  ? 117 ASP C OD2 1 
ATOM   1631 N  N   . ILE C 2 118 ? 20.881  4.183  41.264 1.00 74.73  ? 118 ILE C N   1 
ATOM   1632 C  CA  . ILE C 2 118 ? 21.793  4.970  40.379 1.00 71.28  ? 118 ILE C CA  1 
ATOM   1633 C  C   . ILE C 2 118 ? 22.875  5.636  41.234 1.00 70.02  ? 118 ILE C C   1 
ATOM   1634 O  O   . ILE C 2 118 ? 24.036  5.664  40.776 1.00 69.60  ? 118 ILE C O   1 
ATOM   1635 C  CB  . ILE C 2 118 ? 21.023  6.015  39.539 1.00 69.43  ? 118 ILE C CB  1 
ATOM   1636 C  CG1 . ILE C 2 118 ? 20.286  5.364  38.363 1.00 69.60  ? 118 ILE C CG1 1 
ATOM   1637 C  CG2 . ILE C 2 118 ? 21.963  7.122  39.073 1.00 64.94  ? 118 ILE C CG2 1 
ATOM   1638 C  CD1 . ILE C 2 118 ? 18.962  6.017  38.025 1.00 68.66  ? 118 ILE C CD1 1 
ATOM   1639 N  N   . ALA C 2 119 ? 22.491  6.236  42.367 1.00 67.26  ? 119 ALA C N   1 
ATOM   1640 C  CA  . ALA C 2 119 ? 23.419  6.879  43.333 1.00 71.74  ? 119 ALA C CA  1 
ATOM   1641 C  C   . ALA C 2 119 ? 24.581  5.914  43.626 1.00 75.48  ? 119 ALA C C   1 
ATOM   1642 O  O   . ALA C 2 119 ? 25.760  6.349  43.574 1.00 75.40  ? 119 ALA C O   1 
ATOM   1643 C  CB  . ALA C 2 119 ? 22.685  7.249  44.609 1.00 72.52  ? 119 ALA C CB  1 
ATOM   1644 N  N   . GLU C 2 120 ? 24.248  4.643  43.876 1.00 79.04  ? 120 GLU C N   1 
ATOM   1645 C  CA  . GLU C 2 120 ? 25.196  3.574  44.302 1.00 84.77  ? 120 GLU C CA  1 
ATOM   1646 C  C   . GLU C 2 120 ? 26.163  3.261  43.151 1.00 83.93  ? 120 GLU C C   1 
ATOM   1647 O  O   . GLU C 2 120 ? 27.380  3.150  43.403 1.00 82.55  ? 120 GLU C O   1 
ATOM   1648 C  CB  . GLU C 2 120 ? 24.403  2.337  44.727 1.00 89.56  ? 120 GLU C CB  1 
ATOM   1649 C  CG  . GLU C 2 120 ? 25.262  1.184  45.211 1.00 96.60  ? 120 GLU C CG  1 
ATOM   1650 C  CD  . GLU C 2 120 ? 24.470  -0.019 45.692 1.00 100.56 ? 120 GLU C CD  1 
ATOM   1651 O  OE1 . GLU C 2 120 ? 23.370  0.183  46.238 1.00 104.06 ? 120 GLU C OE1 1 
ATOM   1652 O  OE2 . GLU C 2 120 ? 24.955  -1.151 45.523 1.00 106.62 ? 120 GLU C OE2 1 
ATOM   1653 N  N   . VAL C 2 121 ? 25.644  3.165  41.927 1.00 82.77  ? 121 VAL C N   1 
ATOM   1654 C  CA  . VAL C 2 121 ? 26.450  2.863  40.707 1.00 81.15  ? 121 VAL C CA  1 
ATOM   1655 C  C   . VAL C 2 121 ? 27.448  4.004  40.492 1.00 78.18  ? 121 VAL C C   1 
ATOM   1656 O  O   . VAL C 2 121 ? 28.612  3.716  40.195 1.00 82.09  ? 121 VAL C O   1 
ATOM   1657 C  CB  . VAL C 2 121 ? 25.546  2.636  39.484 1.00 80.48  ? 121 VAL C CB  1 
ATOM   1658 C  CG1 . VAL C 2 121 ? 26.347  2.541  38.188 1.00 80.78  ? 121 VAL C CG1 1 
ATOM   1659 C  CG2 . VAL C 2 121 ? 24.683  1.398  39.663 1.00 82.85  ? 121 VAL C CG2 1 
ATOM   1660 N  N   . LEU C 2 122 ? 27.017  5.244  40.707 1.00 76.64  ? 122 LEU C N   1 
ATOM   1661 C  CA  . LEU C 2 122 ? 27.834  6.466  40.468 1.00 75.69  ? 122 LEU C CA  1 
ATOM   1662 C  C   . LEU C 2 122 ? 28.917  6.595  41.546 1.00 77.94  ? 122 LEU C C   1 
ATOM   1663 O  O   . LEU C 2 122 ? 30.067  6.939  41.193 1.00 76.64  ? 122 LEU C O   1 
ATOM   1664 C  CB  . LEU C 2 122 ? 26.912  7.688  40.453 1.00 72.22  ? 122 LEU C CB  1 
ATOM   1665 C  CG  . LEU C 2 122 ? 25.910  7.730  39.296 1.00 71.34  ? 122 LEU C CG  1 
ATOM   1666 C  CD1 . LEU C 2 122 ? 24.990  8.932  39.416 1.00 68.20  ? 122 LEU C CD1 1 
ATOM   1667 C  CD2 . LEU C 2 122 ? 26.614  7.736  37.945 1.00 71.41  ? 122 LEU C CD2 1 
ATOM   1668 N  N   . GLN C 2 123 ? 28.568  6.361  42.813 1.00 79.76  ? 123 GLN C N   1 
ATOM   1669 C  CA  . GLN C 2 123 ? 29.551  6.384  43.928 1.00 86.06  ? 123 GLN C CA  1 
ATOM   1670 C  C   . GLN C 2 123 ? 30.642  5.345  43.629 1.00 89.56  ? 123 GLN C C   1 
ATOM   1671 O  O   . GLN C 2 123 ? 31.845  5.738  43.562 1.00 89.98  ? 123 GLN C O   1 
ATOM   1672 C  CB  . GLN C 2 123 ? 28.879  6.115  45.270 1.00 87.20  ? 123 GLN C CB  1 
ATOM   1673 C  CG  . GLN C 2 123 ? 29.809  6.353  46.449 1.00 92.83  ? 123 GLN C CG  1 
ATOM   1674 C  CD  . GLN C 2 123 ? 29.065  6.421  47.760 1.00 93.20  ? 123 GLN C CD  1 
ATOM   1675 O  OE1 . GLN C 2 123 ? 28.006  7.040  47.865 1.00 90.93  ? 123 GLN C OE1 1 
ATOM   1676 N  NE2 . GLN C 2 123 ? 29.625  5.791  48.779 1.00 101.43 ? 123 GLN C NE2 1 
ATOM   1677 N  N   . LYS C 2 124 ? 30.229  4.098  43.360 1.00 91.40  ? 124 LYS C N   1 
ATOM   1678 C  CA  . LYS C 2 124 ? 31.142  2.953  43.080 1.00 99.26  ? 124 LYS C CA  1 
ATOM   1679 C  C   . LYS C 2 124 ? 32.019  3.258  41.860 1.00 98.82  ? 124 LYS C C   1 
ATOM   1680 O  O   . LYS C 2 124 ? 33.175  2.802  41.851 1.00 100.12 ? 124 LYS C O   1 
ATOM   1681 C  CB  . LYS C 2 124 ? 30.335  1.666  42.883 1.00 102.13 ? 124 LYS C CB  1 
ATOM   1682 C  CG  . LYS C 2 124 ? 29.704  1.138  44.163 1.00 106.81 ? 124 LYS C CG  1 
ATOM   1683 C  CD  . LYS C 2 124 ? 29.212  -0.277 44.067 1.00 111.99 ? 124 LYS C CD  1 
ATOM   1684 C  CE  . LYS C 2 124 ? 28.011  -0.430 43.160 1.00 112.20 ? 124 LYS C CE  1 
ATOM   1685 N  NZ  . LYS C 2 124 ? 27.200  -1.605 43.562 1.00 117.96 ? 124 LYS C NZ  1 
ATOM   1686 N  N   . ALA C 2 125 ? 31.501  4.024  40.892 1.00 93.31  ? 125 ALA C N   1 
ATOM   1687 C  CA  . ALA C 2 125 ? 32.210  4.403  39.650 1.00 94.43  ? 125 ALA C CA  1 
ATOM   1688 C  C   . ALA C 2 125 ? 33.126  5.618  39.887 1.00 95.66  ? 125 ALA C C   1 
ATOM   1689 O  O   . ALA C 2 125 ? 33.955  5.886  39.002 1.00 95.67  ? 125 ALA C O   1 
ATOM   1690 C  CB  . ALA C 2 125 ? 31.207  4.673  38.555 1.00 91.66  ? 125 ALA C CB  1 
ATOM   1691 N  N   . ALA C 2 126 ? 32.989  6.318  41.026 1.00 97.62  ? 126 ALA C N   1 
ATOM   1692 C  CA  . ALA C 2 126 ? 33.684  7.597  41.347 1.00 99.70  ? 126 ALA C CA  1 
ATOM   1693 C  C   . ALA C 2 126 ? 35.124  7.572  40.821 1.00 104.18 ? 126 ALA C C   1 
ATOM   1694 O  O   . ALA C 2 126 ? 36.047  7.180  41.538 1.00 105.66 ? 126 ALA C O   1 
ATOM   1695 C  CB  . ALA C 2 126 ? 33.668  7.852  42.836 1.00 102.86 ? 126 ALA C CB  1 
ATOM   1696 O  OXT . ALA C 2 126 ? 35.391  7.948  39.672 1.00 105.10 ? 126 ALA C OXT 1 
HETATM 1697 CO CO  . CO  D 3 .   ? 3.443   29.739 62.085 1.00 63.73  ? 401 CO  A CO  1 
HETATM 1698 C  C1  . GOL E 4 .   ? 17.851  33.438 55.433 1.00 87.78  ? 401 GOL B C1  1 
HETATM 1699 O  O1  . GOL E 4 .   ? 18.078  32.764 54.196 1.00 78.53  ? 401 GOL B O1  1 
HETATM 1700 C  C2  . GOL E 4 .   ? 18.717  34.673 55.579 1.00 91.30  ? 401 GOL B C2  1 
HETATM 1701 O  O2  . GOL E 4 .   ? 20.071  34.291 55.821 1.00 90.99  ? 401 GOL B O2  1 
HETATM 1702 C  C3  . GOL E 4 .   ? 18.652  35.594 54.380 1.00 94.02  ? 401 GOL B C3  1 
HETATM 1703 O  O3  . GOL E 4 .   ? 17.467  36.383 54.398 1.00 96.90  ? 401 GOL B O3  1 
HETATM 1704 O  O   . HOH F 5 .   ? 9.797   15.240 31.464 1.00 60.21  ? 501 HOH A O   1 
HETATM 1705 O  O   . HOH F 5 .   ? 10.540  34.097 50.999 1.00 57.13  ? 502 HOH A O   1 
HETATM 1706 O  O   . HOH F 5 .   ? 3.364   31.532 63.206 1.00 53.48  ? 503 HOH A O   1 
HETATM 1707 O  O   . HOH F 5 .   ? 10.732  21.518 28.311 1.00 67.73  ? 504 HOH A O   1 
HETATM 1708 O  O   . HOH F 5 .   ? 8.237   34.065 49.598 1.00 63.35  ? 505 HOH A O   1 
HETATM 1709 O  O   . HOH F 5 .   ? 7.026   30.770 55.154 1.00 52.87  ? 506 HOH A O   1 
HETATM 1710 O  O   . HOH F 5 .   ? 12.164  26.333 36.127 1.00 49.19  ? 507 HOH A O   1 
HETATM 1711 O  O   . HOH F 5 .   ? 3.398   27.579 61.100 1.00 56.00  ? 508 HOH A O   1 
HETATM 1712 O  O   . HOH F 5 .   ? 8.018   19.612 31.065 1.00 55.10  ? 509 HOH A O   1 
HETATM 1713 O  O   . HOH F 5 .   ? 10.412  29.859 52.584 1.00 59.65  ? 510 HOH A O   1 
HETATM 1714 O  O   . HOH F 5 .   ? 6.098   39.849 58.579 1.00 57.55  ? 511 HOH A O   1 
HETATM 1715 O  O   . HOH F 5 .   ? 14.537  20.148 28.225 1.00 65.42  ? 512 HOH A O   1 
HETATM 1716 O  O   . HOH F 5 .   ? 16.522  26.669 31.393 1.00 66.58  ? 513 HOH A O   1 
HETATM 1717 O  O   . HOH F 5 .   ? -1.868  42.628 35.310 1.00 77.17  ? 514 HOH A O   1 
HETATM 1718 O  O   . HOH F 5 .   ? 15.577  28.721 33.673 1.00 72.94  ? 515 HOH A O   1 
HETATM 1719 O  O   . HOH F 5 .   ? 4.839   27.542 58.717 1.00 78.69  ? 516 HOH A O   1 
HETATM 1720 O  O   . HOH F 5 .   ? 12.702  21.420 26.008 1.00 79.51  ? 517 HOH A O   1 
HETATM 1721 O  O   . HOH G 5 .   ? 17.248  25.710 47.873 1.00 55.48  ? 501 HOH B O   1 
HETATM 1722 O  O   . HOH G 5 .   ? 5.432   23.535 39.913 1.00 64.26  ? 502 HOH B O   1 
HETATM 1723 O  O   . HOH G 5 .   ? 5.162   16.863 41.319 1.00 66.61  ? 503 HOH B O   1 
HETATM 1724 O  O   . HOH G 5 .   ? -10.406 18.864 42.909 1.00 61.78  ? 504 HOH B O   1 
HETATM 1725 O  O   . HOH H 5 .   ? 14.492  20.505 22.782 1.00 61.12  ? 201 HOH C O   1 
HETATM 1726 O  O   . HOH H 5 .   ? 22.183  18.495 10.669 1.00 49.83  ? 202 HOH C O   1 
HETATM 1727 O  O   . HOH H 5 .   ? 27.162  20.577 15.882 1.00 65.60  ? 203 HOH C O   1 
HETATM 1728 O  O   . HOH H 5 .   ? 22.964  21.396 13.977 1.00 55.95  ? 204 HOH C O   1 
HETATM 1729 O  O   . HOH H 5 .   ? 10.704  15.366 28.857 1.00 54.08  ? 205 HOH C O   1 
HETATM 1730 O  O   . HOH H 5 .   ? 28.854  13.189 32.509 1.00 59.90  ? 206 HOH C O   1 
HETATM 1731 O  O   . HOH H 5 .   ? 14.217  20.174 17.749 1.00 65.02  ? 207 HOH C O   1 
HETATM 1732 O  O   . HOH H 5 .   ? 24.090  13.758 20.949 1.00 43.94  ? 208 HOH C O   1 
HETATM 1733 O  O   . HOH H 5 .   ? 15.562  21.800 26.404 1.00 46.69  ? 209 HOH C O   1 
HETATM 1734 O  O   . HOH H 5 .   ? 22.688  15.893 4.975  1.00 52.40  ? 210 HOH C O   1 
HETATM 1735 O  O   . HOH H 5 .   ? 11.852  14.818 13.894 1.00 61.53  ? 211 HOH C O   1 
HETATM 1736 O  O   . HOH H 5 .   ? 27.359  12.272 30.451 1.00 57.72  ? 212 HOH C O   1 
HETATM 1737 O  O   . HOH H 5 .   ? 20.491  21.745 32.265 1.00 43.04  ? 213 HOH C O   1 
HETATM 1738 O  O   . HOH H 5 .   ? 16.083  3.981  43.977 1.00 75.31  ? 214 HOH C O   1 
HETATM 1739 O  O   . HOH H 5 .   ? 18.405  -2.467 43.749 1.00 89.33  ? 215 HOH C O   1 
HETATM 1740 O  O   . HOH H 5 .   ? 9.445   10.758 25.474 1.00 65.73  ? 216 HOH C O   1 
HETATM 1741 O  O   . HOH H 5 .   ? 25.812  14.520 22.818 1.00 47.00  ? 217 HOH C O   1 
HETATM 1742 O  O   . HOH H 5 .   ? 28.315  11.206 39.709 1.00 60.10  ? 218 HOH C O   1 
HETATM 1743 O  O   . HOH H 5 .   ? 20.587  23.939 30.272 1.00 60.43  ? 219 HOH C O   1 
HETATM 1744 O  O   . HOH H 5 .   ? 13.556  6.157  40.116 1.00 67.88  ? 220 HOH C O   1 
HETATM 1745 O  O   . HOH H 5 .   ? 15.309  2.804  35.507 1.00 74.49  ? 221 HOH C O   1 
HETATM 1746 O  O   . HOH H 5 .   ? 16.495  1.559  33.483 1.00 65.65  ? 222 HOH C O   1 
HETATM 1747 O  O   . HOH H 5 .   ? 15.009  4.431  22.280 1.00 67.08  ? 223 HOH C O   1 
HETATM 1748 O  O   . HOH H 5 .   ? 10.376  6.008  14.783 1.00 78.34  ? 224 HOH C O   1 
HETATM 1749 O  O   . HOH H 5 .   ? 12.728  4.624  22.187 1.00 79.78  ? 225 HOH C O   1 
HETATM 1750 O  O   . HOH H 5 .   ? 17.692  4.458  40.939 1.00 59.83  ? 226 HOH C O   1 
HETATM 1751 O  O   . HOH H 5 .   ? 16.698  3.474  31.714 1.00 67.97  ? 227 HOH C O   1 
HETATM 1752 O  O   . HOH H 5 .   ? 20.050  26.237 31.099 1.00 66.77  ? 228 HOH C 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   . GLU A 4   ? 1.2536 1.1582 1.1129 -0.0352 -0.0207 0.0472  352 GLU A N   
2    C CA  . GLU A 4   ? 1.2452 1.1517 1.1175 -0.0362 -0.0216 0.0419  352 GLU A CA  
3    C C   . GLU A 4   ? 1.2369 1.1354 1.1158 -0.0339 -0.0264 0.0403  352 GLU A C   
4    O O   . GLU A 4   ? 1.3186 1.2156 1.2076 -0.0360 -0.0273 0.0362  352 GLU A O   
5    C CB  . GLU A 4   ? 1.2478 1.1542 1.1250 -0.0435 -0.0183 0.0454  352 GLU A CB  
6    N N   . ASP A 5   ? 1.1807 1.0750 1.0542 -0.0300 -0.0290 0.0428  353 ASP A N   
7    C CA  . ASP A 5   ? 1.1298 1.0165 1.0088 -0.0267 -0.0332 0.0425  353 ASP A CA  
8    C C   . ASP A 5   ? 1.0769 0.9679 0.9596 -0.0212 -0.0349 0.0336  353 ASP A C   
9    O O   . ASP A 5   ? 1.0284 0.9269 0.9052 -0.0186 -0.0335 0.0304  353 ASP A O   
10   C CB  . ASP A 5   ? 1.1720 1.0553 1.0442 -0.0249 -0.0352 0.0497  353 ASP A CB  
11   C CG  . ASP A 5   ? 1.2090 1.0820 1.0862 -0.0233 -0.0382 0.0542  353 ASP A CG  
12   O OD1 . ASP A 5   ? 1.3108 1.1760 1.1954 -0.0254 -0.0376 0.0530  353 ASP A OD1 
13   O OD2 . ASP A 5   ? 1.2100 1.0829 1.0835 -0.0199 -0.0408 0.0589  353 ASP A OD2 
14   N N   . THR A 6   ? 0.9995 0.8846 0.8904 -0.0195 -0.0373 0.0298  354 THR A N   
15   C CA  . THR A 6   ? 0.9827 0.8712 0.8778 -0.0152 -0.0387 0.0204  354 THR A CA  
16   C C   . THR A 6   ? 0.9431 0.8281 0.8381 -0.0089 -0.0411 0.0197  354 THR A C   
17   O O   . THR A 6   ? 0.9294 0.8054 0.8279 -0.0081 -0.0427 0.0235  354 THR A O   
18   C CB  . THR A 6   ? 1.0203 0.9052 0.9248 -0.0189 -0.0391 0.0152  354 THR A CB  
19   O OG1 . THR A 6   ? 1.0693 0.9615 0.9749 -0.0245 -0.0366 0.0151  354 THR A OG1 
20   C CG2 . THR A 6   ? 1.0328 0.9204 0.9408 -0.0145 -0.0411 0.0054  354 THR A CG2 
21   N N   . TYR A 7   ? 0.8924 0.7842 0.7834 -0.0041 -0.0410 0.0150  355 TYR A N   
22   C CA  . TYR A 7   ? 0.8794 0.7706 0.7705 0.0019  -0.0425 0.0134  355 TYR A CA  
23   C C   . TYR A 7   ? 0.8897 0.7822 0.7835 0.0059  -0.0429 0.0041  355 TYR A C   
24   O O   . TYR A 7   ? 0.9153 0.8127 0.8083 0.0047  -0.0421 -0.0008 355 TYR A O   
25   C CB  . TYR A 7   ? 0.8453 0.7429 0.7279 0.0030  -0.0411 0.0165  355 TYR A CB  
26   C CG  . TYR A 7   ? 0.8318 0.7286 0.7108 -0.0007 -0.0414 0.0252  355 TYR A CG  
27   C CD1 . TYR A 7   ? 0.8027 0.7010 0.6757 -0.0058 -0.0391 0.0285  355 TYR A CD1 
28   C CD2 . TYR A 7   ? 0.8243 0.7198 0.7054 0.0013  -0.0439 0.0301  355 TYR A CD2 
29   C CE1 . TYR A 7   ? 0.8045 0.7021 0.6727 -0.0093 -0.0393 0.0362  355 TYR A CE1 
30   C CE2 . TYR A 7   ? 0.8136 0.7096 0.6904 -0.0018 -0.0448 0.0381  355 TYR A CE2 
31   C CZ  . TYR A 7   ? 0.8169 0.7134 0.6866 -0.0075 -0.0424 0.0411  355 TYR A CZ  
32   O OH  . TYR A 7   ? 0.8323 0.7290 0.6962 -0.0107 -0.0431 0.0487  355 TYR A OH  
33   N N   . TYR A 8   ? 0.9315 0.8205 0.8287 0.0110  -0.0442 0.0018  356 TYR A N   
34   C CA  . TYR A 8   ? 0.9897 0.8789 0.8888 0.0155  -0.0446 -0.0073 356 TYR A CA  
35   C C   . TYR A 8   ? 0.9607 0.8554 0.8550 0.0210  -0.0433 -0.0084 356 TYR A C   
36   O O   . TYR A 8   ? 0.9875 0.8825 0.8827 0.0223  -0.0434 -0.0031 356 TYR A O   
37   C CB  . TYR A 8   ? 1.0605 0.9389 0.9676 0.0162  -0.0463 -0.0097 356 TYR A CB  
38   C CG  . TYR A 8   ? 1.1500 1.0219 1.0614 0.0094  -0.0467 -0.0085 356 TYR A CG  
39   C CD1 . TYR A 8   ? 1.1832 1.0569 1.0969 0.0059  -0.0471 -0.0160 356 TYR A CD1 
40   C CD2 . TYR A 8   ? 1.1928 1.0580 1.1057 0.0060  -0.0467 0.0003  356 TYR A CD2 
41   C CE1 . TYR A 8   ? 1.2257 1.0948 1.1443 -0.0016 -0.0470 -0.0152 356 TYR A CE1 
42   C CE2 . TYR A 8   ? 1.2398 1.0984 1.1562 -0.0010 -0.0461 0.0017  356 TYR A CE2 
43   C CZ  . TYR A 8   ? 1.2737 1.1345 1.1935 -0.0053 -0.0461 -0.0062 356 TYR A CZ  
44   O OH  . TYR A 8   ? 1.3671 1.2225 1.2913 -0.0133 -0.0451 -0.0050 356 TYR A OH  
45   N N   . LEU A 9   ? 0.9303 0.8303 0.8193 0.0235  -0.0418 -0.0144 357 LEU A N   
46   C CA  . LEU A 9   ? 0.8939 0.7980 0.7780 0.0288  -0.0397 -0.0170 357 LEU A CA  
47   C C   . LEU A 9   ? 0.8723 0.7741 0.7588 0.0336  -0.0404 -0.0253 357 LEU A C   
48   O O   . LEU A 9   ? 0.8825 0.7833 0.7698 0.0325  -0.0419 -0.0305 357 LEU A O   
49   C CB  . LEU A 9   ? 0.8858 0.7956 0.7592 0.0286  -0.0366 -0.0171 357 LEU A CB  
50   C CG  . LEU A 9   ? 0.8849 0.7965 0.7533 0.0241  -0.0350 -0.0100 357 LEU A CG  
51   C CD1 . LEU A 9   ? 0.9059 0.8167 0.7760 0.0194  -0.0362 -0.0076 357 LEU A CD1 
52   C CD2 . LEU A 9   ? 0.8775 0.7921 0.7343 0.0254  -0.0307 -0.0105 357 LEU A CD2 
53   N N   . GLN A 10  ? 0.8682 0.7704 0.7555 0.0385  -0.0391 -0.0268 358 GLN A N   
54   C CA  . GLN A 10  ? 0.8706 0.7716 0.7572 0.0441  -0.0384 -0.0350 358 GLN A CA  
55   C C   . GLN A 10  ? 0.8375 0.7451 0.7142 0.0470  -0.0346 -0.0364 358 GLN A C   
56   O O   . GLN A 10  ? 0.7873 0.6988 0.6619 0.0460  -0.0322 -0.0312 358 GLN A O   
57   C CB  . GLN A 10  ? 0.9283 0.8244 0.8231 0.0480  -0.0388 -0.0349 358 GLN A CB  
58   C CG  . GLN A 10  ? 0.9892 0.8830 0.8836 0.0540  -0.0377 -0.0435 358 GLN A CG  
59   C CD  . GLN A 10  ? 1.0330 0.9212 0.9359 0.0586  -0.0376 -0.0430 358 GLN A CD  
60   O OE1 . GLN A 10  ? 1.0772 0.9669 0.9856 0.0585  -0.0381 -0.0355 358 GLN A OE1 
61   N NE2 . GLN A 10  ? 1.0608 0.9426 0.9646 0.0631  -0.0372 -0.0509 358 GLN A NE2 
62   N N   . VAL A 11  ? 0.8123 0.7209 0.6823 0.0498  -0.0342 -0.0431 359 VAL A N   
63   C CA  . VAL A 11  ? 0.8298 0.7428 0.6881 0.0532  -0.0301 -0.0445 359 VAL A CA  
64   C C   . VAL A 11  ? 0.8255 0.7377 0.6813 0.0593  -0.0292 -0.0523 359 VAL A C   
65   O O   . VAL A 11  ? 0.8067 0.7166 0.6648 0.0600  -0.0325 -0.0584 359 VAL A O   
66   C CB  . VAL A 11  ? 0.8507 0.7663 0.7005 0.0519  -0.0303 -0.0440 359 VAL A CB  
67   C CG1 . VAL A 11  ? 0.8636 0.7811 0.6997 0.0560  -0.0257 -0.0445 359 VAL A CG1 
68   C CG2 . VAL A 11  ? 0.8996 0.8155 0.7518 0.0460  -0.0309 -0.0369 359 VAL A CG2 
69   N N   . ARG A 12  ? 0.8403 0.7545 0.6912 0.0628  -0.0245 -0.0524 360 ARG A N   
70   C CA  . ARG A 12  ? 0.8867 0.8008 0.7319 0.0690  -0.0221 -0.0594 360 ARG A CA  
71   C C   . ARG A 12  ? 0.8265 0.7427 0.6566 0.0713  -0.0195 -0.0606 360 ARG A C   
72   O O   . ARG A 12  ? 0.8048 0.7221 0.6278 0.0697  -0.0155 -0.0551 360 ARG A O   
73   C CB  . ARG A 12  ? 0.9928 0.9090 0.8419 0.0714  -0.0177 -0.0584 360 ARG A CB  
74   C CG  . ARG A 12  ? 1.1279 1.0419 0.9792 0.0775  -0.0170 -0.0659 360 ARG A CG  
75   C CD  . ARG A 12  ? 1.2373 1.1545 1.0979 0.0798  -0.0138 -0.0641 360 ARG A CD  
76   N NE  . ARG A 12  ? 1.3345 1.2590 1.1915 0.0781  -0.0085 -0.0593 360 ARG A NE  
77   C CZ  . ARG A 12  ? 1.4029 1.3343 1.2677 0.0792  -0.0051 -0.0570 360 ARG A CZ  
78   N NH1 . ARG A 12  ? 1.4227 1.3542 1.2992 0.0835  -0.0065 -0.0587 360 ARG A NH1 
79   N NH2 . ARG A 12  ? 1.4332 1.3712 1.2939 0.0760  -0.0001 -0.0533 360 ARG A NH2 
80   N N   . GLY A 13  ? 0.8102 0.7263 0.6346 0.0751  -0.0218 -0.0676 361 GLY A N   
81   C CA  . GLY A 13  ? 0.7938 0.7119 0.6025 0.0797  -0.0196 -0.0695 361 GLY A CA  
82   C C   . GLY A 13  ? 0.7799 0.7012 0.5854 0.0785  -0.0237 -0.0686 361 GLY A C   
83   O O   . GLY A 13  ? 0.7311 0.6526 0.5415 0.0736  -0.0244 -0.0626 361 GLY A O   
84   N N   . ARG A 14  ? 0.7312 0.6560 0.5293 0.0828  -0.0265 -0.0748 362 ARG A N   
85   C CA  . ARG A 14  ? 0.7129 0.6441 0.5096 0.0826  -0.0314 -0.0756 362 ARG A CA  
86   C C   . ARG A 14  ? 0.6692 0.6008 0.4572 0.0835  -0.0276 -0.0675 362 ARG A C   
87   O O   . ARG A 14  ? 0.6434 0.5788 0.4360 0.0805  -0.0304 -0.0648 362 ARG A O   
88   C CB  . ARG A 14  ? 0.7282 0.6649 0.5160 0.0883  -0.0346 -0.0838 362 ARG A CB  
89   C CG  . ARG A 14  ? 0.7302 0.6770 0.5158 0.0894  -0.0396 -0.0845 362 ARG A CG  
90   C CD  . ARG A 14  ? 0.7200 0.6713 0.5215 0.0819  -0.0458 -0.0874 362 ARG A CD  
91   N NE  . ARG A 14  ? 0.7174 0.6794 0.5190 0.0820  -0.0489 -0.0853 362 ARG A NE  
92   C CZ  . ARG A 14  ? 0.7165 0.6852 0.5311 0.0755  -0.0537 -0.0871 362 ARG A CZ  
93   N NH1 . ARG A 14  ? 0.7282 0.6918 0.5555 0.0681  -0.0559 -0.0911 362 ARG A NH1 
94   N NH2 . ARG A 14  ? 0.6935 0.6738 0.5083 0.0765  -0.0558 -0.0849 362 ARG A NH2 
95   N N   . LYS A 15  ? 0.6699 0.5972 0.4445 0.0878  -0.0211 -0.0643 363 LYS A N   
96   C CA  . LYS A 15  ? 0.7054 0.6301 0.4685 0.0895  -0.0165 -0.0571 363 LYS A CA  
97   C C   . LYS A 15  ? 0.6732 0.5945 0.4453 0.0819  -0.0150 -0.0507 363 LYS A C   
98   O O   . LYS A 15  ? 0.6670 0.5881 0.4352 0.0814  -0.0141 -0.0461 363 LYS A O   
99   C CB  . LYS A 15  ? 0.7692 0.6876 0.5155 0.0948  -0.0090 -0.0554 363 LYS A CB  
100  C CG  . LYS A 15  ? 0.8693 0.7907 0.6026 0.1036  -0.0100 -0.0605 363 LYS A CG  
101  C CD  . LYS A 15  ? 0.9234 0.8522 0.6510 0.1089  -0.0150 -0.0608 363 LYS A CD  
102  C CE  . LYS A 15  ? 1.0108 0.9352 0.7177 0.1172  -0.0096 -0.0558 363 LYS A CE  
103  N NZ  . LYS A 15  ? 0.9882 0.9230 0.6892 0.1249  -0.0155 -0.0580 363 LYS A NZ  
104  N N   . ASN A 16  ? 0.6487 0.5680 0.4321 0.0766  -0.0148 -0.0506 364 ASN A N   
105  C CA  . ASN A 16  ? 0.6479 0.5654 0.4400 0.0693  -0.0143 -0.0447 364 ASN A CA  
106  C C   . ASN A 16  ? 0.6351 0.5566 0.4374 0.0658  -0.0204 -0.0447 364 ASN A C   
107  O O   . ASN A 16  ? 0.6626 0.5834 0.4647 0.0622  -0.0194 -0.0393 364 ASN A O   
108  C CB  . ASN A 16  ? 0.6414 0.5575 0.4427 0.0660  -0.0130 -0.0445 364 ASN A CB  
109  C CG  . ASN A 16  ? 0.6580 0.5713 0.4496 0.0675  -0.0057 -0.0432 364 ASN A CG  
110  O OD1 . ASN A 16  ? 0.6667 0.5761 0.4450 0.0684  -0.0007 -0.0400 364 ASN A OD1 
111  N ND2 . ASN A 16  ? 0.6477 0.5625 0.4457 0.0681  -0.0045 -0.0458 364 ASN A ND2 
112  N N   . PHE A 17  ? 0.6133 0.5385 0.4236 0.0664  -0.0259 -0.0509 365 PHE A N   
113  C CA  . PHE A 17  ? 0.6235 0.5531 0.4440 0.0623  -0.0314 -0.0518 365 PHE A CA  
114  C C   . PHE A 17  ? 0.6233 0.5587 0.4366 0.0646  -0.0314 -0.0498 365 PHE A C   
115  O O   . PHE A 17  ? 0.6060 0.5431 0.4241 0.0603  -0.0319 -0.0455 365 PHE A O   
116  C CB  . PHE A 17  ? 0.6342 0.5656 0.4625 0.0623  -0.0364 -0.0599 365 PHE A CB  
117  C CG  . PHE A 17  ? 0.6453 0.5820 0.4833 0.0574  -0.0416 -0.0620 365 PHE A CG  
118  C CD1 . PHE A 17  ? 0.6583 0.5915 0.5077 0.0503  -0.0427 -0.0581 365 PHE A CD1 
119  C CD2 . PHE A 17  ? 0.6553 0.6012 0.4910 0.0598  -0.0453 -0.0677 365 PHE A CD2 
120  C CE1 . PHE A 17  ? 0.6643 0.6020 0.5227 0.0450  -0.0466 -0.0599 365 PHE A CE1 
121  C CE2 . PHE A 17  ? 0.6684 0.6209 0.5142 0.0543  -0.0497 -0.0700 365 PHE A CE2 
122  C CZ  . PHE A 17  ? 0.6777 0.6256 0.5350 0.0466  -0.0500 -0.0662 365 PHE A CZ  
123  N N   . GLU A 18  ? 0.6357 0.5743 0.4372 0.0719  -0.0307 -0.0525 366 GLU A N   
124  C CA  . GLU A 18  ? 0.6447 0.5896 0.4382 0.0765  -0.0306 -0.0505 366 GLU A CA  
125  C C   . GLU A 18  ? 0.6391 0.5778 0.4268 0.0751  -0.0249 -0.0422 366 GLU A C   
126  O O   . GLU A 18  ? 0.6509 0.5944 0.4411 0.0741  -0.0258 -0.0396 366 GLU A O   
127  C CB  . GLU A 18  ? 0.6612 0.6080 0.4400 0.0860  -0.0296 -0.0535 366 GLU A CB  
128  C CG  . GLU A 18  ? 0.6843 0.6396 0.4672 0.0878  -0.0360 -0.0625 366 GLU A CG  
129  C CD  . GLU A 18  ? 0.6766 0.6327 0.4440 0.0969  -0.0350 -0.0659 366 GLU A CD  
130  O OE1 . GLU A 18  ? 0.7734 0.7243 0.5256 0.1031  -0.0294 -0.0607 366 GLU A OE1 
131  O OE2 . GLU A 18  ? 0.7026 0.6634 0.4723 0.0976  -0.0396 -0.0739 366 GLU A OE2 
132  N N   . ILE A 19  ? 0.6396 0.5684 0.4191 0.0748  -0.0189 -0.0387 367 ILE A N   
133  C CA  . ILE A 19  ? 0.6590 0.5802 0.4310 0.0726  -0.0129 -0.0317 367 ILE A CA  
134  C C   . ILE A 19  ? 0.6199 0.5426 0.4047 0.0643  -0.0152 -0.0288 367 ILE A C   
135  O O   . ILE A 19  ? 0.5954 0.5184 0.3776 0.0637  -0.0137 -0.0250 367 ILE A O   
136  C CB  . ILE A 19  ? 0.7010 0.6124 0.4641 0.0718  -0.0064 -0.0296 367 ILE A CB  
137  C CG1 . ILE A 19  ? 0.7460 0.6541 0.4932 0.0803  -0.0026 -0.0311 367 ILE A CG1 
138  C CG2 . ILE A 19  ? 0.7487 0.6524 0.5069 0.0666  -0.0011 -0.0235 367 ILE A CG2 
139  C CD1 . ILE A 19  ? 0.7714 0.6734 0.5139 0.0794  0.0024  -0.0318 367 ILE A CD1 
140  N N   . LEU A 20  ? 0.6059 0.5291 0.4033 0.0588  -0.0185 -0.0303 368 LEU A N   
141  C CA  . LEU A 20  ? 0.6021 0.5251 0.4105 0.0509  -0.0203 -0.0268 368 LEU A CA  
142  C C   . LEU A 20  ? 0.6025 0.5329 0.4188 0.0496  -0.0246 -0.0278 368 LEU A C   
143  O O   . LEU A 20  ? 0.5965 0.5268 0.4151 0.0452  -0.0237 -0.0232 368 LEU A O   
144  C CB  . LEU A 20  ? 0.6003 0.5215 0.4193 0.0473  -0.0227 -0.0281 368 LEU A CB  
145  C CG  . LEU A 20  ? 0.6083 0.5247 0.4223 0.0468  -0.0182 -0.0261 368 LEU A CG  
146  C CD1 . LEU A 20  ? 0.6123 0.5291 0.4375 0.0455  -0.0208 -0.0281 368 LEU A CD1 
147  C CD2 . LEU A 20  ? 0.6190 0.5320 0.4286 0.0415  -0.0147 -0.0198 368 LEU A CD2 
148  N N   . MET A 21  ? 0.6103 0.5479 0.4305 0.0529  -0.0288 -0.0337 369 MET A N   
149  C CA  . MET A 21  ? 0.6222 0.5693 0.4510 0.0509  -0.0328 -0.0355 369 MET A CA  
150  C C   . MET A 21  ? 0.6368 0.5883 0.4575 0.0547  -0.0297 -0.0317 369 MET A C   
151  O O   . MET A 21  ? 0.6270 0.5834 0.4542 0.0507  -0.0302 -0.0293 369 MET A O   
152  C CB  . MET A 21  ? 0.6317 0.5869 0.4648 0.0536  -0.0379 -0.0436 369 MET A CB  
153  C CG  . MET A 21  ? 0.6608 0.6119 0.5048 0.0486  -0.0414 -0.0478 369 MET A CG  
154  S SD  . MET A 21  ? 0.6753 0.6246 0.5341 0.0381  -0.0429 -0.0441 369 MET A SD  
155  C CE  . MET A 21  ? 0.6660 0.6300 0.5326 0.0359  -0.0470 -0.0491 369 MET A CE  
156  N N   . LYS A 22  ? 0.6599 0.6089 0.4662 0.0625  -0.0260 -0.0309 370 LYS A N   
157  C CA  . LYS A 22  ? 0.6882 0.6386 0.4841 0.0680  -0.0220 -0.0270 370 LYS A CA  
158  C C   . LYS A 22  ? 0.6700 0.6124 0.4645 0.0623  -0.0174 -0.0206 370 LYS A C   
159  O O   . LYS A 22  ? 0.6362 0.5838 0.4329 0.0618  -0.0166 -0.0181 370 LYS A O   
160  C CB  . LYS A 22  ? 0.7237 0.6687 0.5028 0.0773  -0.0183 -0.0270 370 LYS A CB  
161  C CG  . LYS A 22  ? 0.7799 0.7220 0.5451 0.0845  -0.0129 -0.0223 370 LYS A CG  
162  C CD  . LYS A 22  ? 0.8207 0.7776 0.5917 0.0885  -0.0161 -0.0230 370 LYS A CD  
163  C CE  . LYS A 22  ? 0.8658 0.8211 0.6213 0.0997  -0.0112 -0.0192 370 LYS A CE  
164  N NZ  . LYS A 22  ? 0.8942 0.8566 0.6547 0.0996  -0.0100 -0.0162 370 LYS A NZ  
165  N N   . LEU A 23  ? 0.6650 0.5965 0.4564 0.0578  -0.0145 -0.0183 371 LEU A N   
166  C CA  . LEU A 23  ? 0.6677 0.5917 0.4563 0.0517  -0.0104 -0.0127 371 LEU A CA  
167  C C   . LEU A 23  ? 0.6589 0.5885 0.4619 0.0442  -0.0144 -0.0117 371 LEU A C   
168  O O   . LEU A 23  ? 0.6213 0.5503 0.4225 0.0416  -0.0117 -0.0077 371 LEU A O   
169  C CB  . LEU A 23  ? 0.6712 0.5852 0.4547 0.0482  -0.0074 -0.0115 371 LEU A CB  
170  C CG  . LEU A 23  ? 0.7146 0.6214 0.4828 0.0545  -0.0023 -0.0121 371 LEU A CG  
171  C CD1 . LEU A 23  ? 0.7212 0.6215 0.4879 0.0502  0.0001  -0.0120 371 LEU A CD1 
172  C CD2 . LEU A 23  ? 0.7604 0.6601 0.5138 0.0580  0.0042  -0.0085 371 LEU A CD2 
173  N N   . LYS A 24  ? 0.6433 0.5768 0.4591 0.0410  -0.0198 -0.0149 372 LYS A N   
174  C CA  . LYS A 24  ? 0.6724 0.6089 0.5012 0.0335  -0.0230 -0.0134 372 LYS A CA  
175  C C   . LYS A 24  ? 0.6707 0.6169 0.5028 0.0342  -0.0231 -0.0134 372 LYS A C   
176  O O   . LYS A 24  ? 0.6351 0.5814 0.4697 0.0292  -0.0215 -0.0092 372 LYS A O   
177  C CB  . LYS A 24  ? 0.6859 0.6231 0.5265 0.0310  -0.0282 -0.0175 372 LYS A CB  
178  C CG  . LYS A 24  ? 0.7243 0.6633 0.5777 0.0237  -0.0311 -0.0162 372 LYS A CG  
179  C CD  . LYS A 24  ? 0.7904 0.7290 0.6543 0.0221  -0.0357 -0.0215 372 LYS A CD  
180  C CE  . LYS A 24  ? 0.8161 0.7623 0.6904 0.0181  -0.0386 -0.0248 372 LYS A CE  
181  N NZ  . LYS A 24  ? 0.8693 0.8271 0.7413 0.0234  -0.0398 -0.0303 372 LYS A NZ  
182  N N   . GLU A 25  ? 0.6581 0.6132 0.4897 0.0407  -0.0249 -0.0180 373 GLU A N   
183  C CA  . GLU A 25  ? 0.6745 0.6428 0.5111 0.0423  -0.0257 -0.0190 373 GLU A CA  
184  C C   . GLU A 25  ? 0.6710 0.6372 0.4979 0.0449  -0.0196 -0.0134 373 GLU A C   
185  O O   . GLU A 25  ? 0.6543 0.6272 0.4878 0.0412  -0.0188 -0.0113 373 GLU A O   
186  C CB  . GLU A 25  ? 0.6988 0.6780 0.5346 0.0500  -0.0290 -0.0249 373 GLU A CB  
187  C CG  . GLU A 25  ? 0.7144 0.7090 0.5532 0.0539  -0.0291 -0.0252 373 GLU A CG  
188  C CD  . GLU A 25  ? 0.7434 0.7512 0.5818 0.0617  -0.0335 -0.0311 373 GLU A CD  
189  O OE1 . GLU A 25  ? 0.7656 0.7803 0.6143 0.0578  -0.0394 -0.0376 373 GLU A OE1 
190  O OE2 . GLU A 25  ? 0.7637 0.7739 0.5905 0.0719  -0.0308 -0.0294 373 GLU A OE2 
191  N N   . SER A 26  ? 0.6444 0.6007 0.4558 0.0506  -0.0150 -0.0113 374 SER A N   
192  C CA  . SER A 26  ? 0.6604 0.6109 0.4595 0.0537  -0.0082 -0.0065 374 SER A CA  
193  C C   . SER A 26  ? 0.6715 0.6156 0.4728 0.0443  -0.0059 -0.0020 374 SER A C   
194  O O   . SER A 26  ? 0.6669 0.6137 0.4667 0.0442  -0.0024 0.0008  374 SER A O   
195  C CB  . SER A 26  ? 0.6808 0.6192 0.4627 0.0602  -0.0034 -0.0056 374 SER A CB  
196  O OG  . SER A 26  ? 0.7107 0.6366 0.4888 0.0539  -0.0019 -0.0042 374 SER A OG  
197  N N   . LEU A 27  ? 0.6407 0.5781 0.4459 0.0371  -0.0081 -0.0015 375 LEU A N   
198  C CA  . LEU A 27  ? 0.6745 0.6061 0.4804 0.0286  -0.0066 0.0031  375 LEU A CA  
199  C C   . LEU A 27  ? 0.6813 0.6222 0.5003 0.0235  -0.0091 0.0040  375 LEU A C   
200  O O   . LEU A 27  ? 0.6937 0.6334 0.5099 0.0201  -0.0056 0.0079  375 LEU A O   
201  C CB  . LEU A 27  ? 0.6603 0.5848 0.4681 0.0236  -0.0091 0.0034  375 LEU A CB  
202  C CG  . LEU A 27  ? 0.6560 0.5707 0.4504 0.0256  -0.0052 0.0036  375 LEU A CG  
203  C CD1 . LEU A 27  ? 0.6426 0.5551 0.4425 0.0225  -0.0086 0.0025  375 LEU A CD1 
204  C CD2 . LEU A 27  ? 0.6828 0.5894 0.4652 0.0221  0.0004  0.0076  375 LEU A CD2 
205  N N   . GLU A 28  ? 0.6738 0.6233 0.5059 0.0229  -0.0143 0.0001  376 GLU A N   
206  C CA  . GLU A 28  ? 0.6936 0.6514 0.5391 0.0167  -0.0164 0.0005  376 GLU A CA  
207  C C   . GLU A 28  ? 0.7005 0.6704 0.5467 0.0204  -0.0135 0.0003  376 GLU A C   
208  O O   . GLU A 28  ? 0.7041 0.6769 0.5538 0.0154  -0.0109 0.0037  376 GLU A O   
209  C CB  . GLU A 28  ? 0.7040 0.6650 0.5621 0.0142  -0.0224 -0.0043 376 GLU A CB  
210  C CG  . GLU A 28  ? 0.7453 0.6945 0.6046 0.0097  -0.0245 -0.0025 376 GLU A CG  
211  C CD  . GLU A 28  ? 0.7588 0.7083 0.6305 0.0064  -0.0295 -0.0068 376 GLU A CD  
212  O OE1 . GLU A 28  ? 0.8021 0.7612 0.6808 0.0073  -0.0318 -0.0123 376 GLU A OE1 
213  O OE2 . GLU A 28  ? 0.7807 0.7209 0.6547 0.0032  -0.0310 -0.0047 376 GLU A OE2 
214  N N   . LEU A 29  ? 0.6977 0.6746 0.5399 0.0294  -0.0135 -0.0032 377 LEU A N   
215  C CA  . LEU A 29  ? 0.7349 0.7254 0.5781 0.0350  -0.0110 -0.0034 377 LEU A CA  
216  C C   . LEU A 29  ? 0.7510 0.7340 0.5815 0.0371  -0.0035 0.0020  377 LEU A C   
217  O O   . LEU A 29  ? 0.7539 0.7468 0.5883 0.0376  -0.0006 0.0035  377 LEU A O   
218  C CB  . LEU A 29  ? 0.7396 0.7384 0.5794 0.0456  -0.0131 -0.0078 377 LEU A CB  
219  C CG  . LEU A 29  ? 0.7524 0.7638 0.6058 0.0439  -0.0205 -0.0144 377 LEU A CG  
220  C CD1 . LEU A 29  ? 0.7613 0.7806 0.6087 0.0551  -0.0227 -0.0183 377 LEU A CD1 
221  C CD2 . LEU A 29  ? 0.7639 0.7915 0.6338 0.0373  -0.0222 -0.0158 377 LEU A CD2 
222  N N   . MET A 30  ? 0.7759 0.7423 0.5920 0.0379  -0.0002 0.0045  378 MET A N   
223  C CA  . MET A 30  ? 0.7990 0.7552 0.6009 0.0390  0.0072  0.0088  378 MET A CA  
224  C C   . MET A 30  ? 0.7927 0.7502 0.6000 0.0300  0.0087  0.0123  378 MET A C   
225  O O   . MET A 30  ? 0.7626 0.7188 0.5626 0.0317  0.0148  0.0150  378 MET A O   
226  C CB  . MET A 30  ? 0.8402 0.7785 0.6279 0.0378  0.0094  0.0100  378 MET A CB  
227  C CG  . MET A 30  ? 0.9027 0.8295 0.6728 0.0416  0.0174  0.0125  378 MET A CG  
228  S SD  . MET A 30  ? 0.9565 0.8640 0.7131 0.0345  0.0199  0.0141  378 MET A SD  
229  C CE  . MET A 30  ? 0.9369 0.8434 0.6938 0.0252  0.0221  0.0180  378 MET A CE  
230  N N   . GLU A 31  ? 0.7763 0.7360 0.5959 0.0215  0.0038  0.0124  379 GLU A N   
231  C CA  . GLU A 31  ? 0.7894 0.7488 0.6136 0.0124  0.0049  0.0164  379 GLU A CA  
232  C C   . GLU A 31  ? 0.7756 0.7502 0.6092 0.0126  0.0072  0.0164  379 GLU A C   
233  O O   . GLU A 31  ? 0.7773 0.7515 0.6112 0.0066  0.0106  0.0203  379 GLU A O   
234  C CB  . GLU A 31  ? 0.8272 0.7833 0.6613 0.0046  -0.0010 0.0167  379 GLU A CB  
235  C CG  . GLU A 31  ? 0.8760 0.8185 0.7012 0.0033  -0.0023 0.0180  379 GLU A CG  
236  C CD  . GLU A 31  ? 0.9394 0.8785 0.7740 -0.0022 -0.0081 0.0183  379 GLU A CD  
237  O OE1 . GLU A 31  ? 0.9773 0.9210 0.8235 -0.0072 -0.0101 0.0190  379 GLU A OE1 
238  O OE2 . GLU A 31  ? 0.9844 0.9162 0.8148 -0.0013 -0.0101 0.0179  379 GLU A OE2 
239  N N   . LEU A 32  ? 0.7400 0.7287 0.5809 0.0192  0.0055  0.0122  380 LEU A N   
240  C CA  . LEU A 32  ? 0.7363 0.7435 0.5878 0.0202  0.0075  0.0114  380 LEU A CA  
241  C C   . LEU A 32  ? 0.7303 0.7376 0.5698 0.0283  0.0152  0.0139  380 LEU A C   
242  O O   . LEU A 32  ? 0.7030 0.7242 0.5495 0.0287  0.0187  0.0146  380 LEU A O   
243  C CB  . LEU A 32  ? 0.7428 0.7667 0.6066 0.0244  0.0019  0.0054  380 LEU A CB  
244  C CG  . LEU A 32  ? 0.7420 0.7653 0.6174 0.0168  -0.0052 0.0019  380 LEU A CG  
245  C CD1 . LEU A 32  ? 0.7480 0.7907 0.6362 0.0196  -0.0104 -0.0048 380 LEU A CD1 
246  C CD2 . LEU A 32  ? 0.7474 0.7669 0.6311 0.0044  -0.0046 0.0051  380 LEU A CD2 
247  N N   . VAL A 33  ? 0.6943 0.6865 0.5164 0.0346  0.0181  0.0149  381 VAL A N   
248  C CA  . VAL A 33  ? 0.7130 0.7018 0.5213 0.0439  0.0259  0.0167  381 VAL A CA  
249  C C   . VAL A 33  ? 0.6969 0.6772 0.4980 0.0372  0.0321  0.0209  381 VAL A C   
250  O O   . VAL A 33  ? 0.7113 0.6766 0.5048 0.0297  0.0318  0.0229  381 VAL A O   
251  C CB  . VAL A 33  ? 0.7099 0.6833 0.5010 0.0521  0.0277  0.0161  381 VAL A CB  
252  C CG1 . VAL A 33  ? 0.7280 0.6956 0.5041 0.0620  0.0364  0.0180  381 VAL A CG1 
253  C CG2 . VAL A 33  ? 0.7082 0.6893 0.5049 0.0584  0.0214  0.0121  381 VAL A CG2 
254  N N   . PRO A 34  ? 0.6952 0.6860 0.4986 0.0401  0.0379  0.0223  382 PRO A N   
255  C CA  . PRO A 34  ? 0.6955 0.6784 0.4905 0.0344  0.0445  0.0261  382 PRO A CA  
256  C C   . PRO A 34  ? 0.6840 0.6433 0.4566 0.0351  0.0488  0.0274  382 PRO A C   
257  O O   . PRO A 34  ? 0.6952 0.6465 0.4569 0.0441  0.0509  0.0258  382 PRO A O   
258  C CB  . PRO A 34  ? 0.7143 0.7126 0.5131 0.0422  0.0509  0.0263  382 PRO A CB  
259  C CG  . PRO A 34  ? 0.7055 0.7264 0.5237 0.0457  0.0448  0.0229  382 PRO A CG  
260  C CD  . PRO A 34  ? 0.7044 0.7166 0.5184 0.0493  0.0384  0.0202  382 PRO A CD  
261  N N   . GLN A 35  ? 0.6770 0.6257 0.4429 0.0253  0.0502  0.0301  383 GLN A N   
262  C CA  . GLN A 35  ? 0.6963 0.6236 0.4423 0.0228  0.0529  0.0307  383 GLN A CA  
263  C C   . GLN A 35  ? 0.7081 0.6258 0.4369 0.0323  0.0621  0.0299  383 GLN A C   
264  O O   . GLN A 35  ? 0.7263 0.6271 0.4396 0.0342  0.0642  0.0286  383 GLN A O   
265  C CB  . GLN A 35  ? 0.7032 0.6248 0.4456 0.0111  0.0528  0.0340  383 GLN A CB  
266  C CG  . GLN A 35  ? 0.7302 0.6331 0.4555 0.0062  0.0530  0.0339  383 GLN A CG  
267  C CD  . GLN A 35  ? 0.7489 0.6491 0.4790 0.0054  0.0457  0.0321  383 GLN A CD  
268  O OE1 . GLN A 35  ? 0.7549 0.6646 0.5009 0.0026  0.0387  0.0325  383 GLN A OE1 
269  N NE2 . GLN A 35  ? 0.7502 0.6369 0.4665 0.0076  0.0478  0.0299  383 GLN A NE2 
270  N N   . PRO A 36  ? 0.7262 0.6529 0.4560 0.0382  0.0686  0.0307  384 PRO A N   
271  C CA  . PRO A 36  ? 0.7377 0.6531 0.4498 0.0480  0.0781  0.0301  384 PRO A CA  
272  C C   . PRO A 36  ? 0.7343 0.6456 0.4420 0.0599  0.0778  0.0281  384 PRO A C   
273  O O   . PRO A 36  ? 0.7382 0.6300 0.4265 0.0645  0.0840  0.0275  384 PRO A O   
274  C CB  . PRO A 36  ? 0.7540 0.6855 0.4737 0.0523  0.0838  0.0314  384 PRO A CB  
275  C CG  . PRO A 36  ? 0.7451 0.6884 0.4796 0.0397  0.0790  0.0334  384 PRO A CG  
276  C CD  . PRO A 36  ? 0.7279 0.6740 0.4742 0.0348  0.0684  0.0323  384 PRO A CD  
277  N N   . LEU A 37  ? 0.7222 0.6503 0.4466 0.0639  0.0706  0.0269  385 LEU A N   
278  C CA  . LEU A 37  ? 0.7427 0.6680 0.4630 0.0749  0.0691  0.0253  385 LEU A CA  
279  C C   . LEU A 37  ? 0.7389 0.6456 0.4494 0.0688  0.0661  0.0243  385 LEU A C   
280  O O   . LEU A 37  ? 0.7461 0.6362 0.4399 0.0756  0.0707  0.0239  385 LEU A O   
281  C CB  . LEU A 37  ? 0.7373 0.6879 0.4786 0.0797  0.0618  0.0238  385 LEU A CB  
282  C CG  . LEU A 37  ? 0.7683 0.7406 0.5211 0.0860  0.0649  0.0244  385 LEU A CG  
283  C CD1 . LEU A 37  ? 0.7735 0.7711 0.5453 0.0916  0.0575  0.0220  385 LEU A CD1 
284  C CD2 . LEU A 37  ? 0.7974 0.7603 0.5334 0.0985  0.0754  0.0260  385 LEU A CD2 
285  N N   . VAL A 38  ? 0.7335 0.6415 0.4525 0.0561  0.0596  0.0242  386 VAL A N   
286  C CA  . VAL A 38  ? 0.7442 0.6364 0.4549 0.0494  0.0569  0.0233  386 VAL A CA  
287  C C   . VAL A 38  ? 0.7624 0.6322 0.4503 0.0474  0.0654  0.0237  386 VAL A C   
288  O O   . VAL A 38  ? 0.7792 0.6336 0.4541 0.0496  0.0677  0.0224  386 VAL A O   
289  C CB  . VAL A 38  ? 0.7327 0.6310 0.4565 0.0370  0.0489  0.0238  386 VAL A CB  
290  C CG1 . VAL A 38  ? 0.7359 0.6207 0.4523 0.0312  0.0464  0.0228  386 VAL A CG1 
291  C CG2 . VAL A 38  ? 0.7382 0.6562 0.4834 0.0381  0.0413  0.0227  386 VAL A CG2 
292  N N   . ASP A 39  ? 0.7675 0.6350 0.4500 0.0433  0.0703  0.0251  387 ASP A N   
293  C CA  . ASP A 39  ? 0.7894 0.6351 0.4496 0.0395  0.0782  0.0246  387 ASP A CA  
294  C C   . ASP A 39  ? 0.8021 0.6341 0.4459 0.0520  0.0874  0.0237  387 ASP A C   
295  O O   . ASP A 39  ? 0.8292 0.6392 0.4536 0.0497  0.0930  0.0221  387 ASP A O   
296  C CB  . ASP A 39  ? 0.7950 0.6427 0.4532 0.0323  0.0811  0.0261  387 ASP A CB  
297  C CG  . ASP A 39  ? 0.7986 0.6553 0.4688 0.0199  0.0728  0.0278  387 ASP A CG  
298  O OD1 . ASP A 39  ? 0.8361 0.6930 0.5123 0.0157  0.0657  0.0271  387 ASP A OD1 
299  O OD2 . ASP A 39  ? 0.8330 0.6969 0.5068 0.0154  0.0736  0.0300  387 ASP A OD2 
300  N N   . SER A 40  ? 0.7920 0.6365 0.4429 0.0644  0.0892  0.0247  388 SER A N   
301  C CA  . SER A 40  ? 0.8288 0.6630 0.4661 0.0794  0.0973  0.0247  388 SER A CA  
302  C C   . SER A 40  ? 0.8447 0.6682 0.4757 0.0830  0.0952  0.0238  388 SER A C   
303  O O   . SER A 40  ? 0.8568 0.6570 0.4670 0.0872  0.1032  0.0234  388 SER A O   
304  C CB  . SER A 40  ? 0.8145 0.6702 0.4648 0.0917  0.0975  0.0261  388 SER A CB  
305  O OG  . SER A 40  ? 0.8263 0.6881 0.4780 0.0899  0.1025  0.0270  388 SER A OG  
306  N N   . TYR A 41  ? 0.8650 0.7035 0.5126 0.0808  0.0855  0.0233  389 TYR A N   
307  C CA  . TYR A 41  ? 0.8742 0.7043 0.5172 0.0831  0.0829  0.0224  389 TYR A CA  
308  C C   . TYR A 41  ? 0.9024 0.7093 0.5294 0.0721  0.0865  0.0211  389 TYR A C   
309  O O   . TYR A 41  ? 0.9259 0.7133 0.5357 0.0767  0.0926  0.0208  389 TYR A O   
310  C CB  . TYR A 41  ? 0.8468 0.6978 0.5112 0.0808  0.0716  0.0215  389 TYR A CB  
311  C CG  . TYR A 41  ? 0.8656 0.7087 0.5260 0.0809  0.0687  0.0202  389 TYR A CG  
312  C CD1 . TYR A 41  ? 0.8665 0.7020 0.5267 0.0683  0.0658  0.0189  389 TYR A CD1 
313  C CD2 . TYR A 41  ? 0.8681 0.7125 0.5250 0.0939  0.0690  0.0204  389 TYR A CD2 
314  C CE1 . TYR A 41  ? 0.8654 0.6948 0.5227 0.0682  0.0638  0.0176  389 TYR A CE1 
315  C CE2 . TYR A 41  ? 0.8847 0.7217 0.5370 0.0939  0.0669  0.0194  389 TYR A CE2 
316  C CZ  . TYR A 41  ? 0.8739 0.7032 0.5267 0.0808  0.0647  0.0179  389 TYR A CZ  
317  O OH  . TYR A 41  ? 0.9218 0.7449 0.5709 0.0805  0.0633  0.0167  389 TYR A OH  
318  N N   . ARG A 42  ? 0.8873 0.6961 0.5191 0.0581  0.0832  0.0204  390 ARG A N   
319  C CA  . ARG A 42  ? 0.9146 0.7056 0.5336 0.0460  0.0853  0.0187  390 ARG A CA  
320  C C   . ARG A 42  ? 0.9534 0.7201 0.5478 0.0475  0.0971  0.0178  390 ARG A C   
321  O O   . ARG A 42  ? 0.9929 0.7409 0.5729 0.0426  0.1010  0.0159  390 ARG A O   
322  C CB  . ARG A 42  ? 0.9050 0.7061 0.5348 0.0323  0.0786  0.0188  390 ARG A CB  
323  C CG  . ARG A 42  ? 0.8972 0.7152 0.5472 0.0291  0.0679  0.0190  390 ARG A CG  
324  C CD  . ARG A 42  ? 0.9147 0.7423 0.5752 0.0174  0.0614  0.0200  390 ARG A CD  
325  N NE  . ARG A 42  ? 0.9068 0.7484 0.5859 0.0162  0.0521  0.0201  390 ARG A NE  
326  C CZ  . ARG A 42  ? 0.8848 0.7389 0.5785 0.0098  0.0451  0.0218  390 ARG A CZ  
327  N NH1 . ARG A 42  ? 0.8736 0.7290 0.5655 0.0040  0.0462  0.0239  390 ARG A NH1 
328  N NH2 . ARG A 42  ? 0.8487 0.7132 0.5579 0.0097  0.0375  0.0214  390 ARG A NH2 
329  N N   . GLN A 43  ? 0.9603 0.7268 0.5499 0.0540  0.1030  0.0189  391 GLN A N   
330  C CA  . GLN A 43  ? 1.0056 0.7472 0.5706 0.0582  0.1155  0.0179  391 GLN A CA  
331  C C   . GLN A 43  ? 1.0388 0.7648 0.5914 0.0696  0.1209  0.0183  391 GLN A C   
332  O O   . GLN A 43  ? 1.0578 0.7575 0.5891 0.0667  0.1292  0.0165  391 GLN A O   
333  C CB  . GLN A 43  ? 0.9949 0.7426 0.5596 0.0664  0.1208  0.0193  391 GLN A CB  
334  C CG  . GLN A 43  ? 1.0010 0.7542 0.5681 0.0543  0.1197  0.0186  391 GLN A CG  
335  C CD  . GLN A 43  ? 1.0313 0.7590 0.5751 0.0445  0.1269  0.0154  391 GLN A CD  
336  O OE1 . GLN A 43  ? 1.0718 0.7779 0.5952 0.0507  0.1379  0.0140  391 GLN A OE1 
337  N NE2 . GLN A 43  ? 1.0065 0.7363 0.5529 0.0290  0.1208  0.0139  391 GLN A NE2 
338  N N   . GLN A 44  ? 1.0644 0.8060 0.6293 0.0820  0.1166  0.0206  392 GLN A N   
339  C CA  . GLN A 44  ? 1.1045 0.8341 0.6583 0.0951  0.1210  0.0221  392 GLN A CA  
340  C C   . GLN A 44  ? 1.1132 0.8288 0.6601 0.0861  0.1200  0.0204  392 GLN A C   
341  O O   . GLN A 44  ? 1.1641 0.8550 0.6905 0.0908  0.1288  0.0207  392 GLN A O   
342  C CB  . GLN A 44  ? 1.0979 0.8521 0.6689 0.1085  0.1142  0.0244  392 GLN A CB  
343  C CG  . GLN A 44  ? 1.1428 0.8854 0.6993 0.1267  0.1210  0.0270  392 GLN A CG  
344  C CD  . GLN A 44  ? 1.1188 0.8760 0.6855 0.1345  0.1133  0.0282  392 GLN A CD  
345  O OE1 . GLN A 44  ? 1.1381 0.9111 0.7213 0.1257  0.1035  0.0264  392 GLN A OE1 
346  N NE2 . GLN A 44  ? 1.1717 0.9235 0.7277 0.1520  0.1179  0.0312  392 GLN A NE2 
347  N N   . GLN A 45  ? 1.1236 0.8540 0.6868 0.0739  0.1102  0.0189  393 GLN A N   
348  C CA  . GLN A 45  ? 1.1484 0.8705 0.7089 0.0643  0.1083  0.0171  393 GLN A CA  
349  C C   . GLN A 45  ? 1.1911 0.8880 0.7315 0.0533  0.1169  0.0145  393 GLN A C   
350  O O   . GLN A 45  ? 1.2196 0.8970 0.7453 0.0524  0.1229  0.0138  393 GLN A O   
351  C CB  . GLN A 45  ? 1.1091 0.8534 0.6921 0.0538  0.0963  0.0160  393 GLN A CB  
352  C CG  . GLN A 45  ? 1.0771 0.8452 0.6800 0.0625  0.0875  0.0174  393 GLN A CG  
353  C CD  . GLN A 45  ? 1.0976 0.8607 0.6929 0.0770  0.0905  0.0188  393 GLN A CD  
354  O OE1 . GLN A 45  ? 1.0764 0.8315 0.6663 0.0765  0.0909  0.0182  393 GLN A OE1 
355  N NE2 . GLN A 45  ? 1.1189 0.8876 0.7136 0.0905  0.0928  0.0209  393 GLN A NE2 
356  N N   . GLN A 46  ? 1.2259 0.9234 0.7653 0.0452  0.1177  0.0132  394 GLN A N   
357  C CA  . GLN A 46  ? 1.2925 0.9676 0.8125 0.0336  0.1255  0.0098  394 GLN A CA  
358  C C   . GLN A 46  ? 1.3388 0.9843 0.8334 0.0427  0.1389  0.0099  394 GLN A C   
359  O O   . GLN A 46  ? 1.3943 1.0173 0.8720 0.0336  0.1455  0.0069  394 GLN A O   
360  C CB  . GLN A 46  ? 1.2982 0.9811 0.8211 0.0268  0.1240  0.0090  394 GLN A CB  
361  C CG  . GLN A 46  ? 1.3383 1.0082 0.8486 0.0100  0.1265  0.0048  394 GLN A CG  
362  C CD  . GLN A 46  ? 1.3829 1.0553 0.8898 0.0059  0.1278  0.0040  394 GLN A CD  
363  O OE1 . GLN A 46  ? 1.4319 1.1159 0.9459 -0.0064 0.1212  0.0030  394 GLN A OE1 
364  N NE2 . GLN A 46  ? 1.3772 1.0393 0.8728 0.0169  0.1366  0.0049  394 GLN A NE2 
365  N N   . LEU A 47  ? 1.3701 1.0160 0.8625 0.0600  0.1428  0.0131  395 LEU A N   
366  C CA  . LEU A 47  ? 1.4335 1.0511 0.9016 0.0721  0.1560  0.0142  395 LEU A CA  
367  C C   . LEU A 47  ? 1.5026 1.1059 0.9618 0.0757  0.1588  0.0155  395 LEU A C   
368  O O   . LEU A 47  ? 1.5508 1.1227 0.9858 0.0757  0.1704  0.0146  395 LEU A O   
369  C CB  . LEU A 47  ? 1.4245 1.0528 0.8969 0.0910  0.1575  0.0180  395 LEU A CB  
370  C CG  . LEU A 47  ? 1.4231 1.0559 0.8955 0.0905  0.1604  0.0171  395 LEU A CG  
371  C CD1 . LEU A 47  ? 1.4104 1.0546 0.8874 0.1106  0.1628  0.0209  395 LEU A CD1 
372  C CD2 . LEU A 47  ? 1.4458 1.0466 0.8922 0.0827  0.1722  0.0133  395 LEU A CD2 
373  N N   . LEU A 48  ? 1.5354 1.1598 1.0125 0.0789  0.1491  0.0174  396 LEU A N   
374  C CA  . LEU A 48  ? 1.5434 1.1578 1.0137 0.0833  0.1508  0.0190  396 LEU A CA  
375  C C   . LEU A 48  ? 1.5953 1.1964 1.0593 0.0649  0.1527  0.0152  396 LEU A C   
376  O O   . LEU A 48  ? 1.7191 1.2960 1.1648 0.0660  0.1614  0.0157  396 LEU A O   
377  C CB  . LEU A 48  ? 1.4809 1.1245 0.9734 0.0911  0.1392  0.0213  396 LEU A CB  
378  C CG  . LEU A 48  ? 1.4586 1.1172 0.9576 0.1098  0.1372  0.0249  396 LEU A CG  
379  C CD1 . LEU A 48  ? 1.4307 1.1231 0.9563 0.1116  0.1236  0.0251  396 LEU A CD1 
380  C CD2 . LEU A 48  ? 1.4634 1.1023 0.9423 0.1270  0.1462  0.0288  396 LEU A CD2 
381  N N   . GLN A 49  ? 1.5937 1.2102 1.0719 0.0490  0.1451  0.0117  397 GLN A N   
382  C CA  . GLN A 49  ? 1.5779 1.1870 1.0531 0.0303  0.1455  0.0075  397 GLN A CA  
383  C C   . GLN A 49  ? 1.5497 1.1440 1.0117 0.0183  0.1514  0.0035  397 GLN A C   
384  O O   . GLN A 49  ? 1.5252 1.0943 0.9657 0.0231  0.1626  0.0032  397 GLN A O   
385  C CB  . GLN A 49  ? 1.5659 1.2046 1.0669 0.0219  0.1321  0.0067  397 GLN A CB  
386  C CG  . GLN A 49  ? 1.5748 1.2319 1.0896 0.0134  0.1243  0.0053  397 GLN A CG  
387  C CD  . GLN A 49  ? 1.5535 1.2387 1.0935 0.0078  0.1114  0.0055  397 GLN A CD  
388  O OE1 . GLN A 49  ? 1.5373 1.2274 1.0839 0.0072  0.1084  0.0054  397 GLN A OE1 
389  N NE2 . GLN A 49  ? 1.5467 1.2493 1.0999 0.0040  0.1041  0.0058  397 GLN A NE2 
390  N N   . ASP B 5   ? 1.8310 1.2263 1.2252 0.3572  0.1725  0.1190  353 ASP B N   
391  C CA  . ASP B 5   ? 1.7552 1.2322 1.1868 0.3382  0.1575  0.1010  353 ASP B CA  
392  C C   . ASP B 5   ? 1.7182 1.1766 1.1568 0.2981  0.1586  0.0788  353 ASP B C   
393  O O   . ASP B 5   ? 1.6933 1.2094 1.1607 0.2770  0.1465  0.0663  353 ASP B O   
394  C CB  . ASP B 5   ? 1.7545 1.2908 1.2027 0.3718  0.1515  0.0950  353 ASP B CB  
395  C CG  . ASP B 5   ? 1.6894 1.3162 1.1726 0.3608  0.1354  0.0877  353 ASP B CG  
396  O OD1 . ASP B 5   ? 1.6649 1.3234 1.1541 0.3599  0.1287  0.0999  353 ASP B OD1 
397  O OD2 . ASP B 5   ? 1.6795 1.3439 1.1831 0.3517  0.1300  0.0694  353 ASP B OD2 
398  N N   . THR B 6   ? 1.7185 1.1004 1.1316 0.2879  0.1726  0.0741  354 THR B N   
399  C CA  . THR B 6   ? 1.6776 1.0367 1.0918 0.2457  0.1755  0.0553  354 THR B CA  
400  C C   . THR B 6   ? 1.6598 0.9816 1.0594 0.2155  0.1798  0.0651  354 THR B C   
401  O O   . THR B 6   ? 1.7156 0.9677 1.0841 0.2215  0.1934  0.0769  354 THR B O   
402  C CB  . THR B 6   ? 1.7463 1.0510 1.1423 0.2498  0.1889  0.0390  354 THR B CB  
403  O OG1 . THR B 6   ? 1.7287 1.0869 1.1456 0.2637  0.1822  0.0241  354 THR B OG1 
404  C CG2 . THR B 6   ? 1.7547 1.0203 1.1414 0.2065  0.1958  0.0234  354 THR B CG2 
405  N N   . TYR B 7   ? 1.5763 0.9423 0.9972 0.1838  0.1691  0.0597  355 TYR B N   
406  C CA  . TYR B 7   ? 1.5516 0.8986 0.9640 0.1502  0.1716  0.0648  355 TYR B CA  
407  C C   . TYR B 7   ? 1.5221 0.8538 0.9348 0.1128  0.1749  0.0441  355 TYR B C   
408  O O   . TYR B 7   ? 1.4693 0.8274 0.8978 0.1110  0.1700  0.0274  355 TYR B O   
409  C CB  . TYR B 7   ? 1.4779 0.8913 0.9151 0.1446  0.1570  0.0720  355 TYR B CB  
410  C CG  . TYR B 7   ? 1.4859 0.9337 0.9288 0.1807  0.1512  0.0877  355 TYR B CG  
411  C CD1 . TYR B 7   ? 1.4660 0.9582 0.9282 0.2055  0.1432  0.0816  355 TYR B CD1 
412  C CD2 . TYR B 7   ? 1.5446 0.9859 0.9732 0.1887  0.1537  0.1086  355 TYR B CD2 
413  C CE1 . TYR B 7   ? 1.4811 1.0126 0.9491 0.2373  0.1379  0.0943  355 TYR B CE1 
414  C CE2 . TYR B 7   ? 1.5602 1.0404 0.9938 0.2218  0.1481  0.1228  355 TYR B CE2 
415  C CZ  . TYR B 7   ? 1.5467 1.0732 1.0005 0.2463  0.1400  0.1148  355 TYR B CZ  
416  O OH  . TYR B 7   ? 1.5683 1.1402 1.0276 0.2777  0.1345  0.1270  355 TYR B OH  
417  N N   . TYR B 8   ? 1.5532 0.8464 0.9477 0.0829  0.1835  0.0454  356 TYR B N   
418  C CA  . TYR B 8   ? 1.5856 0.8648 0.9769 0.0439  0.1882  0.0259  356 TYR B CA  
419  C C   . TYR B 8   ? 1.5175 0.8436 0.9259 0.0135  0.1786  0.0257  356 TYR B C   
420  O O   . TYR B 8   ? 1.5088 0.8425 0.9148 0.0143  0.1771  0.0415  356 TYR B O   
421  C CB  . TYR B 8   ? 1.7086 0.9014 1.0624 0.0321  0.2084  0.0240  356 TYR B CB  
422  C CG  . TYR B 8   ? 1.7958 0.9416 1.1344 0.0600  0.2184  0.0173  356 TYR B CG  
423  C CD1 . TYR B 8   ? 1.8514 0.9742 1.1797 0.1030  0.2213  0.0350  356 TYR B CD1 
424  C CD2 . TYR B 8   ? 1.8419 0.9717 1.1771 0.0450  0.2248  -0.0077 356 TYR B CD2 
425  C CE1 . TYR B 8   ? 1.9228 1.0054 1.2382 0.1322  0.2304  0.0278  356 TYR B CE1 
426  C CE2 . TYR B 8   ? 1.9124 1.0018 1.2344 0.0718  0.2345  -0.0167 356 TYR B CE2 
427  C CZ  . TYR B 8   ? 1.9487 1.0134 1.2611 0.1166  0.2374  0.0009  356 TYR B CZ  
428  O OH  . TYR B 8   ? 2.0257 1.0528 1.3259 0.1462  0.2470  -0.0089 356 TYR B OH  
429  N N   . LEU B 9   ? 1.4799 0.8398 0.9051 -0.0113 0.1722  0.0081  357 LEU B N   
430  C CA  . LEU B 9   ? 1.4315 0.8453 0.8780 -0.0367 0.1610  0.0050  357 LEU B CA  
431  C C   . LEU B 9   ? 1.4280 0.8260 0.8626 -0.0758 0.1689  -0.0107 357 LEU B C   
432  O O   . LEU B 9   ? 1.4461 0.8270 0.8744 -0.0816 0.1741  -0.0256 357 LEU B O   
433  C CB  . LEU B 9   ? 1.4083 0.8869 0.8900 -0.0244 0.1432  0.0006  357 LEU B CB  
434  C CG  . LEU B 9   ? 1.3946 0.9308 0.9023 -0.0433 0.1296  -0.0028 357 LEU B CG  
435  C CD1 . LEU B 9   ? 1.4372 0.9836 0.9445 -0.0449 0.1287  0.0086  357 LEU B CD1 
436  C CD2 . LEU B 9   ? 1.3975 0.9856 0.9371 -0.0282 0.1133  -0.0046 357 LEU B CD2 
437  N N   . GLN B 10  ? 1.4070 0.8124 0.8371 -0.1021 0.1708  -0.0083 358 GLN B N   
438  C CA  . GLN B 10  ? 1.4389 0.8425 0.8596 -0.1434 0.1775  -0.0237 358 GLN B CA  
439  C C   . GLN B 10  ? 1.3532 0.8352 0.8067 -0.1552 0.1605  -0.0315 358 GLN B C   
440  O O   . GLN B 10  ? 1.3116 0.8360 0.7856 -0.1438 0.1488  -0.0217 358 GLN B O   
441  C CB  . GLN B 10  ? 1.5014 0.8683 0.8963 -0.1650 0.1905  -0.0152 358 GLN B CB  
442  C CG  . GLN B 10  ? 1.5581 0.9129 0.9368 -0.2102 0.2015  -0.0319 358 GLN B CG  
443  C CD  . GLN B 10  ? 1.6465 0.9290 0.9874 -0.2285 0.2213  -0.0243 358 GLN B CD  
444  O OE1 . GLN B 10  ? 1.6601 0.9164 0.9898 -0.2107 0.2244  -0.0029 358 GLN B OE1 
445  N NE2 . GLN B 10  ? 1.6970 0.9456 1.0166 -0.2650 0.2353  -0.0415 358 GLN B NE2 
446  N N   . VAL B 11  ? 1.3465 0.8480 0.8047 -0.1753 0.1591  -0.0484 359 VAL B N   
447  C CA  . VAL B 11  ? 1.3065 0.8817 0.7946 -0.1851 0.1428  -0.0544 359 VAL B CA  
448  C C   . VAL B 11  ? 1.3399 0.9274 0.8180 -0.2245 0.1491  -0.0712 359 VAL B C   
449  O O   . VAL B 11  ? 1.3687 0.9360 0.8339 -0.2356 0.1568  -0.0847 359 VAL B O   
450  C CB  . VAL B 11  ? 1.2603 0.8659 0.7715 -0.1629 0.1295  -0.0548 359 VAL B CB  
451  C CG1 . VAL B 11  ? 1.2198 0.8945 0.7630 -0.1644 0.1112  -0.0536 359 VAL B CG1 
452  C CG2 . VAL B 11  ? 1.2666 0.8506 0.7806 -0.1270 0.1278  -0.0427 359 VAL B CG2 
453  N N   . ARG B 12  ? 1.3917 1.0185 0.8772 -0.2446 0.1456  -0.0717 360 ARG B N   
454  C CA  . ARG B 12  ? 1.4353 1.1021 0.9209 -0.2804 0.1462  -0.0875 360 ARG B CA  
455  C C   . ARG B 12  ? 1.3895 1.1267 0.9085 -0.2687 0.1262  -0.0880 360 ARG B C   
456  O O   . ARG B 12  ? 1.3966 1.1659 0.9406 -0.2451 0.1121  -0.0762 360 ARG B O   
457  C CB  . ARG B 12  ? 1.5038 1.1859 0.9826 -0.3055 0.1515  -0.0872 360 ARG B CB  
458  C CG  . ARG B 12  ? 1.5990 1.2103 1.0459 -0.3127 0.1696  -0.0795 360 ARG B CG  
459  C CD  . ARG B 12  ? 1.6339 1.2681 1.0797 -0.3268 0.1711  -0.0719 360 ARG B CD  
460  N NE  . ARG B 12  ? 1.6259 1.3334 1.1070 -0.3073 0.1518  -0.0667 360 ARG B NE  
461  C CZ  . ARG B 12  ? 1.6246 1.4035 1.1240 -0.3242 0.1434  -0.0756 360 ARG B CZ  
462  N NH1 . ARG B 12  ? 1.6525 1.4459 1.1382 -0.3638 0.1525  -0.0902 360 ARG B NH1 
463  N NH2 . ARG B 12  ? 1.5607 1.3976 1.0923 -0.3009 0.1263  -0.0711 360 ARG B NH2 
464  N N   . GLY B 13  ? 1.3493 1.1077 0.8679 -0.2837 0.1254  -0.1007 361 GLY B N   
465  C CA  . GLY B 13  ? 1.3123 1.1329 0.8585 -0.2735 0.1073  -0.0990 361 GLY B CA  
466  C C   . GLY B 13  ? 1.3274 1.1301 0.8725 -0.2583 0.1061  -0.0991 361 GLY B C   
467  O O   . GLY B 13  ? 1.3801 1.1562 0.9312 -0.2294 0.1030  -0.0877 361 GLY B O   
468  N N   . ARG B 14  ? 1.2934 1.1144 0.8306 -0.2785 0.1091  -0.1128 362 ARG B N   
469  C CA  . ARG B 14  ? 1.2705 1.0842 0.8053 -0.2688 0.1088  -0.1158 362 ARG B CA  
470  C C   . ARG B 14  ? 1.1560 1.0013 0.7191 -0.2389 0.0901  -0.0977 362 ARG B C   
471  O O   . ARG B 14  ? 1.1306 0.9508 0.6933 -0.2186 0.0906  -0.0929 362 ARG B O   
472  C CB  . ARG B 14  ? 1.3318 1.1821 0.8582 -0.2985 0.1117  -0.1333 362 ARG B CB  
473  C CG  . ARG B 14  ? 1.3618 1.2244 0.8894 -0.2904 0.1086  -0.1357 362 ARG B CG  
474  C CD  . ARG B 14  ? 1.4429 1.2400 0.9523 -0.2771 0.1223  -0.1417 362 ARG B CD  
475  N NE  . ARG B 14  ? 1.4762 1.2926 0.9906 -0.2654 0.1175  -0.1417 362 ARG B NE  
476  C CZ  . ARG B 14  ? 1.5476 1.3248 1.0462 -0.2573 0.1293  -0.1526 362 ARG B CZ  
477  N NH1 . ARG B 14  ? 1.5913 1.3010 1.0673 -0.2576 0.1467  -0.1635 362 ARG B NH1 
478  N NH2 . ARG B 14  ? 1.5692 1.3755 1.0743 -0.2484 0.1238  -0.1521 362 ARG B NH2 
479  N N   . LYS B 15  ? 1.0589 0.9587 0.6451 -0.2373 0.0747  -0.0891 363 LYS B N   
480  C CA  . LYS B 15  ? 1.0166 0.9445 0.6312 -0.2109 0.0563  -0.0712 363 LYS B CA  
481  C C   . LYS B 15  ? 0.9682 0.8567 0.5887 -0.1848 0.0564  -0.0612 363 LYS B C   
482  O O   . LYS B 15  ? 0.9686 0.8505 0.5984 -0.1654 0.0505  -0.0524 363 LYS B O   
483  C CB  . LYS B 15  ? 0.9991 0.9844 0.6343 -0.2143 0.0426  -0.0664 363 LYS B CB  
484  C CG  . LYS B 15  ? 0.9890 1.0053 0.6524 -0.1909 0.0234  -0.0491 363 LYS B CG  
485  C CD  . LYS B 15  ? 0.9683 1.0360 0.6520 -0.1895 0.0108  -0.0452 363 LYS B CD  
486  C CE  . LYS B 15  ? 0.9667 1.0437 0.6786 -0.1608 -0.0060 -0.0286 363 LYS B CE  
487  N NZ  . LYS B 15  ? 1.0052 1.1264 0.7368 -0.1551 -0.0167 -0.0273 363 LYS B NZ  
488  N N   . ASN B 16  ? 0.9371 0.8043 0.5515 -0.1861 0.0631  -0.0627 364 ASN B N   
489  C CA  . ASN B 16  ? 0.9158 0.7522 0.5346 -0.1623 0.0634  -0.0534 364 ASN B CA  
490  C C   . ASN B 16  ? 0.9153 0.7020 0.5156 -0.1517 0.0746  -0.0542 364 ASN B C   
491  O O   . ASN B 16  ? 0.8646 0.6446 0.4759 -0.1274 0.0693  -0.0452 364 ASN B O   
492  C CB  . ASN B 16  ? 0.9257 0.7563 0.5389 -0.1698 0.0691  -0.0546 364 ASN B CB  
493  C CG  . ASN B 16  ? 0.9013 0.7874 0.5376 -0.1730 0.0563  -0.0538 364 ASN B CG  
494  O OD1 . ASN B 16  ? 0.9258 0.8469 0.5851 -0.1617 0.0415  -0.0487 364 ASN B OD1 
495  N ND2 . ASN B 16  ? 0.9339 0.8286 0.5638 -0.1879 0.0620  -0.0585 364 ASN B ND2 
496  N N   . PHE B 17  ? 0.9662 0.7232 0.5406 -0.1693 0.0894  -0.0663 365 PHE B N   
497  C CA  . PHE B 17  ? 1.0233 0.7325 0.5790 -0.1578 0.1012  -0.0697 365 PHE B CA  
498  C C   . PHE B 17  ? 1.0026 0.7353 0.5731 -0.1418 0.0916  -0.0658 365 PHE B C   
499  O O   . PHE B 17  ? 1.0065 0.7200 0.5781 -0.1180 0.0924  -0.0598 365 PHE B O   
500  C CB  . PHE B 17  ? 1.0934 0.7690 0.6199 -0.1822 0.1185  -0.0870 365 PHE B CB  
501  C CG  . PHE B 17  ? 1.1427 0.7756 0.6526 -0.1682 0.1294  -0.0933 365 PHE B CG  
502  C CD1 . PHE B 17  ? 1.1832 0.7657 0.6814 -0.1452 0.1377  -0.0861 365 PHE B CD1 
503  C CD2 . PHE B 17  ? 1.1705 0.8204 0.6783 -0.1748 0.1302  -0.1054 365 PHE B CD2 
504  C CE1 . PHE B 17  ? 1.2313 0.7783 0.7157 -0.1282 0.1472  -0.0922 365 PHE B CE1 
505  C CE2 . PHE B 17  ? 1.2039 0.8203 0.6984 -0.1592 0.1399  -0.1127 365 PHE B CE2 
506  C CZ  . PHE B 17  ? 1.2324 0.7964 0.7154 -0.1352 0.1485  -0.1066 365 PHE B CZ  
507  N N   . GLU B 18  ? 0.9972 0.7738 0.5779 -0.1554 0.0830  -0.0684 366 GLU B N   
508  C CA  . GLU B 18  ? 0.9764 0.7805 0.5694 -0.1460 0.0739  -0.0634 366 GLU B CA  
509  C C   . GLU B 18  ? 0.9055 0.7222 0.5230 -0.1222 0.0605  -0.0468 366 GLU B C   
510  O O   . GLU B 18  ? 0.8872 0.6998 0.5077 -0.1067 0.0597  -0.0430 366 GLU B O   
511  C CB  . GLU B 18  ? 1.0053 0.8582 0.6042 -0.1663 0.0662  -0.0657 366 GLU B CB  
512  C CG  . GLU B 18  ? 1.0943 0.9410 0.6692 -0.1911 0.0798  -0.0854 366 GLU B CG  
513  C CD  . GLU B 18  ? 1.1555 1.0582 0.7349 -0.2100 0.0721  -0.0878 366 GLU B CD  
514  O OE1 . GLU B 18  ? 1.1496 1.0950 0.7496 -0.2079 0.0565  -0.0738 366 GLU B OE1 
515  O OE2 . GLU B 18  ? 1.2873 1.1918 0.8496 -0.2253 0.0818  -0.1038 366 GLU B OE2 
516  N N   . ILE B 19  ? 0.8624 0.6954 0.4966 -0.1200 0.0509  -0.0392 367 ILE B N   
517  C CA  . ILE B 19  ? 0.8537 0.6969 0.5119 -0.0988 0.0387  -0.0264 367 ILE B CA  
518  C C   . ILE B 19  ? 0.8029 0.6118 0.4536 -0.0800 0.0467  -0.0259 367 ILE B C   
519  O O   . ILE B 19  ? 0.7757 0.5894 0.4374 -0.0642 0.0416  -0.0199 367 ILE B O   
520  C CB  . ILE B 19  ? 0.8797 0.7456 0.5562 -0.0989 0.0286  -0.0223 367 ILE B CB  
521  C CG1 . ILE B 19  ? 0.9200 0.8259 0.6059 -0.1130 0.0190  -0.0207 367 ILE B CG1 
522  C CG2 . ILE B 19  ? 0.8798 0.7497 0.5789 -0.0777 0.0183  -0.0133 367 ILE B CG2 
523  C CD1 . ILE B 19  ? 0.9429 0.8737 0.6426 -0.1149 0.0120  -0.0209 367 ILE B CD1 
524  N N   . LEU B 20  ? 0.8264 0.6036 0.4584 -0.0820 0.0588  -0.0311 368 LEU B N   
525  C CA  . LEU B 20  ? 0.8371 0.5832 0.4607 -0.0616 0.0661  -0.0278 368 LEU B CA  
526  C C   . LEU B 20  ? 0.8377 0.5657 0.4487 -0.0513 0.0738  -0.0313 368 LEU B C   
527  O O   . LEU B 20  ? 0.8073 0.5335 0.4234 -0.0294 0.0727  -0.0260 368 LEU B O   
528  C CB  . LEU B 20  ? 0.8614 0.5757 0.4650 -0.0690 0.0778  -0.0300 368 LEU B CB  
529  C CG  . LEU B 20  ? 0.8377 0.5756 0.4544 -0.0762 0.0707  -0.0269 368 LEU B CG  
530  C CD1 . LEU B 20  ? 0.8764 0.5830 0.4700 -0.0871 0.0839  -0.0281 368 LEU B CD1 
531  C CD2 . LEU B 20  ? 0.8025 0.5632 0.4431 -0.0549 0.0591  -0.0188 368 LEU B CD2 
532  N N   . MET B 21  ? 0.8967 0.6190 0.4936 -0.0664 0.0806  -0.0414 369 MET B N   
533  C CA  . MET B 21  ? 0.9373 0.6501 0.5238 -0.0572 0.0876  -0.0478 369 MET B CA  
534  C C   . MET B 21  ? 0.8708 0.6235 0.4792 -0.0473 0.0751  -0.0404 369 MET B C   
535  O O   . MET B 21  ? 0.8630 0.6125 0.4705 -0.0276 0.0780  -0.0397 369 MET B O   
536  C CB  . MET B 21  ? 1.0183 0.7247 0.5871 -0.0789 0.0966  -0.0628 369 MET B CB  
537  C CG  . MET B 21  ? 1.1548 0.8059 0.6952 -0.0828 0.1144  -0.0734 369 MET B CG  
538  S SD  . MET B 21  ? 1.2905 0.8960 0.8170 -0.0479 0.1254  -0.0712 369 MET B SD  
539  C CE  . MET B 21  ? 1.2746 0.8779 0.7880 -0.0482 0.1349  -0.0902 369 MET B CE  
540  N N   . LYS B 22  ? 0.8370 0.6260 0.4641 -0.0598 0.0619  -0.0341 370 LYS B N   
541  C CA  . LYS B 22  ? 0.8486 0.6718 0.4966 -0.0540 0.0496  -0.0246 370 LYS B CA  
542  C C   . LYS B 22  ? 0.7939 0.6141 0.4545 -0.0328 0.0459  -0.0178 370 LYS B C   
543  O O   . LYS B 22  ? 0.7523 0.5853 0.4180 -0.0219 0.0449  -0.0161 370 LYS B O   
544  C CB  . LYS B 22  ? 0.8873 0.7415 0.5518 -0.0691 0.0361  -0.0165 370 LYS B CB  
545  C CG  . LYS B 22  ? 1.0149 0.8856 0.6683 -0.0899 0.0382  -0.0222 370 LYS B CG  
546  C CD  . LYS B 22  ? 1.0860 0.9899 0.7544 -0.1021 0.0247  -0.0124 370 LYS B CD  
547  C CE  . LYS B 22  ? 1.1537 1.0845 0.8387 -0.0996 0.0123  0.0026  370 LYS B CE  
548  N NZ  . LYS B 22  ? 1.1837 1.1351 0.8571 -0.1106 0.0159  0.0006  370 LYS B NZ  
549  N N   . LEU B 23  ? 0.7757 0.5845 0.4410 -0.0279 0.0443  -0.0153 371 LEU B N   
550  C CA  . LEU B 23  ? 0.7578 0.5711 0.4367 -0.0094 0.0398  -0.0100 371 LEU B CA  
551  C C   . LEU B 23  ? 0.7567 0.5502 0.4194 0.0095  0.0511  -0.0128 371 LEU B C   
552  O O   . LEU B 23  ? 0.7479 0.5584 0.4206 0.0244  0.0480  -0.0103 371 LEU B O   
553  C CB  . LEU B 23  ? 0.7657 0.5776 0.4531 -0.0107 0.0353  -0.0080 371 LEU B CB  
554  C CG  . LEU B 23  ? 0.7533 0.5886 0.4603 -0.0233 0.0226  -0.0049 371 LEU B CG  
555  C CD1 . LEU B 23  ? 0.8040 0.6397 0.5157 -0.0253 0.0208  -0.0064 371 LEU B CD1 
556  C CD2 . LEU B 23  ? 0.7324 0.5888 0.4626 -0.0173 0.0110  0.0009  371 LEU B CD2 
557  N N   . LYS B 24  ? 0.8032 0.5622 0.4416 0.0090  0.0640  -0.0179 372 LYS B N   
558  C CA  . LYS B 24  ? 0.8521 0.5859 0.4718 0.0297  0.0760  -0.0201 372 LYS B CA  
559  C C   . LYS B 24  ? 0.8415 0.6003 0.4668 0.0375  0.0747  -0.0235 372 LYS B C   
560  O O   . LYS B 24  ? 0.8294 0.6017 0.4595 0.0586  0.0743  -0.0208 372 LYS B O   
561  C CB  . LYS B 24  ? 0.9236 0.6113 0.5150 0.0229  0.0908  -0.0273 372 LYS B CB  
562  C CG  . LYS B 24  ? 1.0119 0.6650 0.5826 0.0474  0.1037  -0.0283 372 LYS B CG  
563  C CD  . LYS B 24  ? 1.0783 0.6896 0.6232 0.0404  0.1184  -0.0408 372 LYS B CD  
564  C CE  . LYS B 24  ? 1.1265 0.7245 0.6600 0.0676  0.1273  -0.0458 372 LYS B CE  
565  N NZ  . LYS B 24  ? 1.2011 0.7358 0.7044 0.0713  0.1446  -0.0537 372 LYS B NZ  
566  N N   . GLU B 25  ? 0.8189 0.5907 0.4443 0.0195  0.0734  -0.0291 373 GLU B N   
567  C CA  . GLU B 25  ? 0.8316 0.6302 0.4594 0.0228  0.0736  -0.0334 373 GLU B CA  
568  C C   . GLU B 25  ? 0.7949 0.6312 0.4459 0.0305  0.0623  -0.0249 373 GLU B C   
569  O O   . GLU B 25  ? 0.8124 0.6644 0.4635 0.0480  0.0654  -0.0270 373 GLU B O   
570  C CB  . GLU B 25  ? 0.8359 0.6485 0.4615 -0.0017 0.0720  -0.0383 373 GLU B CB  
571  C CG  . GLU B 25  ? 0.8474 0.6988 0.4795 -0.0043 0.0691  -0.0395 373 GLU B CG  
572  C CD  . GLU B 25  ? 0.8750 0.7407 0.5006 -0.0282 0.0691  -0.0446 373 GLU B CD  
573  O OE1 . GLU B 25  ? 0.8937 0.7382 0.4991 -0.0316 0.0811  -0.0590 373 GLU B OE1 
574  O OE2 . GLU B 25  ? 0.8834 0.7791 0.5235 -0.0437 0.0574  -0.0341 373 GLU B OE2 
575  N N   . SER B 26  ? 0.7573 0.6082 0.4274 0.0180  0.0501  -0.0167 374 SER B N   
576  C CA  . SER B 26  ? 0.7176 0.6008 0.4106 0.0196  0.0392  -0.0101 374 SER B CA  
577  C C   . SER B 26  ? 0.7250 0.6093 0.4209 0.0421  0.0413  -0.0104 374 SER B C   
578  O O   . SER B 26  ? 0.7107 0.6239 0.4150 0.0505  0.0397  -0.0110 374 SER B O   
579  C CB  . SER B 26  ? 0.7145 0.6042 0.4255 0.0035  0.0268  -0.0025 374 SER B CB  
580  O OG  . SER B 26  ? 0.7365 0.6085 0.4506 0.0081  0.0253  -0.0021 374 SER B OG  
581  N N   . LEU B 27  ? 0.7306 0.5890 0.4188 0.0506  0.0450  -0.0098 375 LEU B N   
582  C CA  . LEU B 27  ? 0.7567 0.6187 0.4451 0.0730  0.0472  -0.0084 375 LEU B CA  
583  C C   . LEU B 27  ? 0.7894 0.6560 0.4644 0.0939  0.0564  -0.0117 375 LEU B C   
584  O O   . LEU B 27  ? 0.8192 0.7173 0.5038 0.1080  0.0539  -0.0114 375 LEU B O   
585  C CB  . LEU B 27  ? 0.7582 0.5892 0.4355 0.0762  0.0513  -0.0056 375 LEU B CB  
586  C CG  . LEU B 27  ? 0.7229 0.5610 0.4176 0.0619  0.0413  -0.0037 375 LEU B CG  
587  C CD1 . LEU B 27  ? 0.7310 0.5410 0.4117 0.0606  0.0471  -0.0017 375 LEU B CD1 
588  C CD2 . LEU B 27  ? 0.7046 0.5762 0.4218 0.0690  0.0322  -0.0037 375 LEU B CD2 
589  N N   . GLU B 28  ? 0.8103 0.6513 0.4651 0.0950  0.0665  -0.0166 376 GLU B N   
590  C CA  . GLU B 28  ? 0.8407 0.6827 0.4818 0.1190  0.0763  -0.0214 376 GLU B CA  
591  C C   . GLU B 28  ? 0.8014 0.6917 0.4556 0.1159  0.0721  -0.0261 376 GLU B C   
592  O O   . GLU B 28  ? 0.7742 0.6961 0.4340 0.1353  0.0720  -0.0265 376 GLU B O   
593  C CB  . GLU B 28  ? 0.8944 0.6869 0.5092 0.1211  0.0894  -0.0274 376 GLU B CB  
594  C CG  . GLU B 28  ? 0.9410 0.6881 0.5410 0.1274  0.0950  -0.0205 376 GLU B CG  
595  C CD  . GLU B 28  ? 1.0320 0.7217 0.6032 0.1310  0.1099  -0.0260 376 GLU B CD  
596  O OE1 . GLU B 28  ? 1.0637 0.7470 0.6275 0.1208  0.1153  -0.0382 376 GLU B OE1 
597  O OE2 . GLU B 28  ? 1.0954 0.7466 0.6510 0.1423  0.1165  -0.0184 376 GLU B OE2 
598  N N   . LEU B 29  ? 0.7796 0.6808 0.4391 0.0912  0.0681  -0.0286 377 LEU B N   
599  C CA  . LEU B 29  ? 0.7711 0.7166 0.4383 0.0856  0.0664  -0.0328 377 LEU B CA  
600  C C   . LEU B 29  ? 0.7476 0.7360 0.4378 0.0825  0.0560  -0.0271 377 LEU B C   
601  O O   . LEU B 29  ? 0.7126 0.7430 0.4082 0.0863  0.0565  -0.0309 377 LEU B O   
602  C CB  . LEU B 29  ? 0.7756 0.7215 0.4410 0.0583  0.0643  -0.0339 377 LEU B CB  
603  C CG  . LEU B 29  ? 0.8142 0.7317 0.4566 0.0594  0.0763  -0.0452 377 LEU B CG  
604  C CD1 . LEU B 29  ? 0.8228 0.7471 0.4649 0.0301  0.0726  -0.0452 377 LEU B CD1 
605  C CD2 . LEU B 29  ? 0.8311 0.7670 0.4641 0.0798  0.0861  -0.0570 377 LEU B CD2 
606  N N   . MET B 30  ? 0.7676 0.7477 0.4707 0.0768  0.0479  -0.0203 378 MET B N   
607  C CA  . MET B 30  ? 0.7701 0.7865 0.4955 0.0709  0.0385  -0.0176 378 MET B CA  
608  C C   . MET B 30  ? 0.7294 0.7770 0.4549 0.0960  0.0426  -0.0223 378 MET B C   
609  O O   . MET B 30  ? 0.7093 0.8000 0.4503 0.0903  0.0377  -0.0241 378 MET B O   
610  C CB  . MET B 30  ? 0.8216 0.8200 0.5597 0.0629  0.0301  -0.0127 378 MET B CB  
611  C CG  . MET B 30  ? 0.9215 0.9057 0.6535 0.0845  0.0338  -0.0133 378 MET B CG  
612  S SD  . MET B 30  ? 1.0777 1.0726 0.8326 0.0778  0.0231  -0.0128 378 MET B SD  
613  C CE  . MET B 30  ? 0.9733 1.0242 0.7438 0.0805  0.0202  -0.0186 378 MET B CE  
614  N N   . GLU B 31  ? 0.7437 0.7703 0.4516 0.1222  0.0516  -0.0236 379 GLU B N   
615  C CA  . GLU B 31  ? 0.7786 0.8342 0.4836 0.1522  0.0560  -0.0260 379 GLU B CA  
616  C C   . GLU B 31  ? 0.7709 0.8738 0.4781 0.1562  0.0589  -0.0336 379 GLU B C   
617  O O   . GLU B 31  ? 0.7684 0.9181 0.4827 0.1725  0.0585  -0.0364 379 GLU B O   
618  C CB  . GLU B 31  ? 0.8261 0.8388 0.5077 0.1798  0.0662  -0.0233 379 GLU B CB  
619  C CG  . GLU B 31  ? 0.8311 0.8063 0.5092 0.1785  0.0644  -0.0153 379 GLU B CG  
620  C CD  . GLU B 31  ? 0.8862 0.8105 0.5381 0.2005  0.0755  -0.0104 379 GLU B CD  
621  O OE1 . GLU B 31  ? 0.9518 0.8651 0.5880 0.2198  0.0848  -0.0141 379 GLU B OE1 
622  O OE2 . GLU B 31  ? 0.9167 0.8117 0.5634 0.1977  0.0752  -0.0032 379 GLU B OE2 
623  N N   . LEU B 32  ? 0.7812 0.8783 0.4821 0.1419  0.0620  -0.0375 380 LEU B N   
624  C CA  . LEU B 32  ? 0.7785 0.9234 0.4798 0.1448  0.0659  -0.0460 380 LEU B CA  
625  C C   . LEU B 32  ? 0.7532 0.9536 0.4763 0.1217  0.0570  -0.0450 380 LEU B C   
626  O O   . LEU B 32  ? 0.7410 0.9955 0.4676 0.1262  0.0595  -0.0519 380 LEU B O   
627  C CB  . LEU B 32  ? 0.8131 0.9374 0.5016 0.1319  0.0713  -0.0508 380 LEU B CB  
628  C CG  . LEU B 32  ? 0.8697 0.9419 0.5346 0.1530  0.0827  -0.0564 380 LEU B CG  
629  C CD1 . LEU B 32  ? 0.8863 0.9500 0.5406 0.1358  0.0877  -0.0648 380 LEU B CD1 
630  C CD2 . LEU B 32  ? 0.8989 0.9828 0.5546 0.1933  0.0913  -0.0625 380 LEU B CD2 
631  N N   . VAL B 33  ? 0.7502 0.9378 0.4874 0.0974  0.0474  -0.0375 381 VAL B N   
632  C CA  . VAL B 33  ? 0.7486 0.9752 0.5050 0.0686  0.0393  -0.0356 381 VAL B CA  
633  C C   . VAL B 33  ? 0.7506 1.0281 0.5188 0.0800  0.0383  -0.0418 381 VAL B C   
634  O O   . VAL B 33  ? 0.7720 1.0415 0.5419 0.0980  0.0374  -0.0422 381 VAL B O   
635  C CB  . VAL B 33  ? 0.7271 0.9178 0.4943 0.0423  0.0298  -0.0263 381 VAL B CB  
636  C CG1 . VAL B 33  ? 0.7161 0.9382 0.5022 0.0146  0.0223  -0.0240 381 VAL B CG1 
637  C CG2 . VAL B 33  ? 0.7278 0.8802 0.4838 0.0298  0.0303  -0.0200 381 VAL B CG2 
638  N N   . PRO B 34  ? 0.7837 1.1208 0.5596 0.0696  0.0388  -0.0472 382 PRO B N   
639  C CA  . PRO B 34  ? 0.7840 1.1793 0.5725 0.0762  0.0375  -0.0547 382 PRO B CA  
640  C C   . PRO B 34  ? 0.7697 1.1523 0.5741 0.0626  0.0294  -0.0534 382 PRO B C   
641  O O   . PRO B 34  ? 0.7437 1.0964 0.5563 0.0334  0.0232  -0.0475 382 PRO B O   
642  C CB  . PRO B 34  ? 0.7711 1.2236 0.5671 0.0511  0.0378  -0.0586 382 PRO B CB  
643  C CG  . PRO B 34  ? 0.7971 1.2319 0.5782 0.0492  0.0429  -0.0558 382 PRO B CG  
644  C CD  . PRO B 34  ? 0.7885 1.1461 0.5609 0.0496  0.0409  -0.0468 382 PRO B CD  
645  N N   . GLN B 35  ? 0.7976 1.2059 0.6056 0.0847  0.0295  -0.0591 383 GLN B N   
646  C CA  . GLN B 35  ? 0.8023 1.2079 0.6252 0.0755  0.0228  -0.0619 383 GLN B CA  
647  C C   . GLN B 35  ? 0.8051 1.2259 0.6464 0.0348  0.0167  -0.0655 383 GLN B C   
648  O O   . GLN B 35  ? 0.8140 1.1961 0.6651 0.0167  0.0105  -0.0636 383 GLN B O   
649  C CB  . GLN B 35  ? 0.8125 1.2693 0.6370 0.1034  0.0246  -0.0693 383 GLN B CB  
650  C CG  . GLN B 35  ? 0.8117 1.2575 0.6458 0.1028  0.0191  -0.0720 383 GLN B CG  
651  C CD  . GLN B 35  ? 0.8310 1.2043 0.6546 0.1112  0.0187  -0.0619 383 GLN B CD  
652  O OE1 . GLN B 35  ? 0.8817 1.2265 0.6864 0.1357  0.0245  -0.0537 383 GLN B OE1 
653  N NE2 . GLN B 35  ? 0.7750 1.1183 0.6109 0.0906  0.0122  -0.0634 383 GLN B NE2 
654  N N   . PRO B 36  ? 0.8213 1.2987 0.6681 0.0189  0.0186  -0.0711 384 PRO B N   
655  C CA  . PRO B 36  ? 0.8319 1.3200 0.6945 -0.0227 0.0139  -0.0734 384 PRO B CA  
656  C C   . PRO B 36  ? 0.8345 1.2536 0.6975 -0.0474 0.0088  -0.0604 384 PRO B C   
657  O O   . PRO B 36  ? 0.8572 1.2554 0.7340 -0.0709 0.0030  -0.0617 384 PRO B O   
658  C CB  . PRO B 36  ? 0.8308 1.3849 0.6919 -0.0331 0.0189  -0.0775 384 PRO B CB  
659  C CG  . PRO B 36  ? 0.8326 1.4337 0.6851 0.0087  0.0249  -0.0848 384 PRO B CG  
660  C CD  . PRO B 36  ? 0.8373 1.3740 0.6759 0.0399  0.0257  -0.0764 384 PRO B CD  
661  N N   . LEU B 37  ? 0.8104 1.1971 0.6586 -0.0402 0.0110  -0.0491 385 LEU B N   
662  C CA  . LEU B 37  ? 0.8080 1.1351 0.6543 -0.0597 0.0061  -0.0348 385 LEU B CA  
663  C C   . LEU B 37  ? 0.7891 1.0612 0.6385 -0.0478 0.0013  -0.0330 385 LEU B C   
664  O O   . LEU B 37  ? 0.8038 1.0353 0.6614 -0.0673 -0.0054 -0.0255 385 LEU B O   
665  C CB  . LEU B 37  ? 0.7938 1.1143 0.6223 -0.0534 0.0109  -0.0268 385 LEU B CB  
666  C CG  . LEU B 37  ? 0.8217 1.1984 0.6467 -0.0672 0.0156  -0.0282 385 LEU B CG  
667  C CD1 . LEU B 37  ? 0.8151 1.1833 0.6225 -0.0610 0.0205  -0.0227 385 LEU B CD1 
668  C CD2 . LEU B 37  ? 0.8297 1.2163 0.6667 -0.1081 0.0106  -0.0216 385 LEU B CD2 
669  N N   . VAL B 38  ? 0.7699 1.0403 0.6120 -0.0164 0.0048  -0.0386 386 VAL B N   
670  C CA  . VAL B 38  ? 0.7666 0.9937 0.6114 -0.0051 0.0010  -0.0383 386 VAL B CA  
671  C C   . VAL B 38  ? 0.7815 1.0178 0.6470 -0.0205 -0.0051 -0.0474 386 VAL B C   
672  O O   . VAL B 38  ? 0.7815 0.9760 0.6558 -0.0296 -0.0112 -0.0451 386 VAL B O   
673  C CB  . VAL B 38  ? 0.7464 0.9753 0.5780 0.0298  0.0068  -0.0412 386 VAL B CB  
674  C CG1 . VAL B 38  ? 0.7409 0.9330 0.5757 0.0376  0.0031  -0.0410 386 VAL B CG1 
675  C CG2 . VAL B 38  ? 0.7599 0.9736 0.5704 0.0448  0.0141  -0.0350 386 VAL B CG2 
676  N N   . ASP B 39  ? 0.8090 1.1012 0.6822 -0.0225 -0.0031 -0.0591 387 ASP B N   
677  C CA  . ASP B 39  ? 0.8155 1.1264 0.7077 -0.0363 -0.0073 -0.0729 387 ASP B CA  
678  C C   . ASP B 39  ? 0.8401 1.1231 0.7447 -0.0727 -0.0125 -0.0698 387 ASP B C   
679  O O   . ASP B 39  ? 0.8522 1.0991 0.7691 -0.0810 -0.0180 -0.0738 387 ASP B O   
680  C CB  . ASP B 39  ? 0.8081 1.1940 0.7035 -0.0300 -0.0032 -0.0863 387 ASP B CB  
681  C CG  . ASP B 39  ? 0.8028 1.2124 0.6875 0.0088  0.0007  -0.0883 387 ASP B CG  
682  O OD1 . ASP B 39  ? 0.8210 1.1866 0.6977 0.0269  0.0001  -0.0816 387 ASP B OD1 
683  O OD2 . ASP B 39  ? 0.8276 1.3008 0.7116 0.0205  0.0044  -0.0958 387 ASP B OD2 
684  N N   . SER B 40  ? 0.8574 1.1551 0.7578 -0.0922 -0.0105 -0.0620 388 SER B N   
685  C CA  . SER B 40  ? 0.9027 1.1671 0.8093 -0.1264 -0.0149 -0.0517 388 SER B CA  
686  C C   . SER B 40  ? 0.8971 1.0915 0.8043 -0.1223 -0.0212 -0.0404 388 SER B C   
687  O O   . SER B 40  ? 0.9617 1.1217 0.8827 -0.1390 -0.0268 -0.0420 388 SER B O   
688  C CB  . SER B 40  ? 0.9179 1.2052 0.8131 -0.1398 -0.0111 -0.0399 388 SER B CB  
689  O OG  . SER B 40  ? 0.9802 1.2209 0.8747 -0.1630 -0.0159 -0.0221 388 SER B OG  
690  N N   . TYR B 41  ? 0.8701 1.0451 0.7630 -0.1001 -0.0199 -0.0309 389 TYR B N   
691  C CA  . TYR B 41  ? 0.8465 0.9640 0.7377 -0.0956 -0.0254 -0.0189 389 TYR B CA  
692  C C   . TYR B 41  ? 0.8265 0.9199 0.7313 -0.0859 -0.0299 -0.0301 389 TYR B C   
693  O O   . TYR B 41  ? 0.8494 0.8993 0.7627 -0.0926 -0.0366 -0.0241 389 TYR B O   
694  C CB  . TYR B 41  ? 0.8263 0.9383 0.6983 -0.0749 -0.0211 -0.0113 389 TYR B CB  
695  C CG  . TYR B 41  ? 0.8077 0.8726 0.6778 -0.0655 -0.0256 -0.0042 389 TYR B CG  
696  C CD1 . TYR B 41  ? 0.7713 0.8261 0.6422 -0.0444 -0.0250 -0.0130 389 TYR B CD1 
697  C CD2 . TYR B 41  ? 0.7929 0.8283 0.6604 -0.0783 -0.0304 0.0118  389 TYR B CD2 
698  C CE1 . TYR B 41  ? 0.7698 0.7877 0.6397 -0.0377 -0.0289 -0.0078 389 TYR B CE1 
699  C CE2 . TYR B 41  ? 0.7847 0.7847 0.6515 -0.0696 -0.0348 0.0175  389 TYR B CE2 
700  C CZ  . TYR B 41  ? 0.7739 0.7658 0.6423 -0.0499 -0.0338 0.0068  389 TYR B CZ  
701  O OH  . TYR B 41  ? 0.7655 0.7286 0.6335 -0.0430 -0.0378 0.0113  389 TYR B OH  
702  N N   . ARG B 42  ? 0.8103 0.9341 0.7168 -0.0684 -0.0265 -0.0454 390 ARG B N   
703  C CA  . ARG B 42  ? 0.7941 0.9055 0.7126 -0.0580 -0.0299 -0.0582 390 ARG B CA  
704  C C   . ARG B 42  ? 0.8243 0.9333 0.7635 -0.0807 -0.0341 -0.0708 390 ARG B C   
705  O O   . ARG B 42  ? 0.8154 0.8921 0.7669 -0.0795 -0.0393 -0.0771 390 ARG B O   
706  C CB  . ARG B 42  ? 0.7578 0.9082 0.6696 -0.0334 -0.0245 -0.0685 390 ARG B CB  
707  C CG  . ARG B 42  ? 0.7276 0.8605 0.6206 -0.0096 -0.0209 -0.0579 390 ARG B CG  
708  C CD  . ARG B 42  ? 0.7031 0.8738 0.5864 0.0146  -0.0149 -0.0638 390 ARG B CD  
709  N NE  . ARG B 42  ? 0.6893 0.8355 0.5532 0.0350  -0.0104 -0.0533 390 ARG B NE  
710  C CZ  . ARG B 42  ? 0.7151 0.8811 0.5638 0.0588  -0.0037 -0.0518 390 ARG B CZ  
711  N NH1 . ARG B 42  ? 0.7398 0.9570 0.5918 0.0679  -0.0017 -0.0601 390 ARG B NH1 
712  N NH2 . ARG B 42  ? 0.7091 0.8436 0.5390 0.0738  0.0010  -0.0423 390 ARG B NH2 
713  N N   . GLN B 43  ? 0.8859 1.0293 0.8287 -0.1007 -0.0314 -0.0760 391 GLN B N   
714  C CA  . GLN B 43  ? 0.9909 1.1304 0.9518 -0.1285 -0.0340 -0.0887 391 GLN B CA  
715  C C   . GLN B 43  ? 1.0543 1.1296 1.0195 -0.1456 -0.0400 -0.0733 391 GLN B C   
716  O O   . GLN B 43  ? 1.0839 1.1278 1.0650 -0.1580 -0.0439 -0.0834 391 GLN B O   
717  C CB  . GLN B 43  ? 1.0045 1.2013 0.9652 -0.1477 -0.0287 -0.0959 391 GLN B CB  
718  C CG  . GLN B 43  ? 1.0182 1.2804 0.9799 -0.1305 -0.0244 -0.1149 391 GLN B CG  
719  C CD  . GLN B 43  ? 1.0567 1.3867 1.0120 -0.1361 -0.0184 -0.1171 391 GLN B CD  
720  O OE1 . GLN B 43  ? 1.1456 1.4786 1.0966 -0.1576 -0.0168 -0.1067 391 GLN B OE1 
721  N NE2 . GLN B 43  ? 1.0091 1.3987 0.9633 -0.1155 -0.0151 -0.1302 391 GLN B NE2 
722  N N   . GLN B 44  ? 1.1091 1.1653 1.0603 -0.1432 -0.0407 -0.0504 392 GLN B N   
723  C CA  . GLN B 44  ? 1.1766 1.1763 1.1285 -0.1549 -0.0470 -0.0304 392 GLN B CA  
724  C C   . GLN B 44  ? 1.2087 1.1660 1.1682 -0.1346 -0.0531 -0.0320 392 GLN B C   
725  O O   . GLN B 44  ? 1.2183 1.1289 1.1886 -0.1438 -0.0592 -0.0269 392 GLN B O   
726  C CB  . GLN B 44  ? 1.2033 1.2093 1.1367 -0.1563 -0.0453 -0.0078 392 GLN B CB  
727  C CG  . GLN B 44  ? 1.2832 1.2561 1.2157 -0.1817 -0.0496 0.0139  392 GLN B CG  
728  C CD  . GLN B 44  ? 1.3387 1.3141 1.2532 -0.1785 -0.0495 0.0360  392 GLN B CD  
729  O OE1 . GLN B 44  ? 1.3697 1.3764 1.2716 -0.1618 -0.0444 0.0329  392 GLN B OE1 
730  N NE2 . GLN B 44  ? 1.3901 1.3319 1.3027 -0.1945 -0.0549 0.0587  392 GLN B NE2 
731  N N   . GLN B 45  ? 1.2280 1.2009 1.1817 -0.1080 -0.0511 -0.0387 393 GLN B N   
732  C CA  . GLN B 45  ? 1.2309 1.1732 1.1896 -0.0881 -0.0560 -0.0401 393 GLN B CA  
733  C C   . GLN B 45  ? 1.3017 1.2244 1.2821 -0.0908 -0.0603 -0.0587 393 GLN B C   
734  O O   . GLN B 45  ? 1.2916 1.1797 1.2799 -0.0802 -0.0661 -0.0573 393 GLN B O   
735  C CB  . GLN B 45  ? 1.1563 1.1248 1.1038 -0.0634 -0.0513 -0.0460 393 GLN B CB  
736  C CG  . GLN B 45  ? 1.1276 1.1038 1.0534 -0.0572 -0.0470 -0.0295 393 GLN B CG  
737  C CD  . GLN B 45  ? 1.1182 1.0621 1.0403 -0.0671 -0.0520 -0.0092 393 GLN B CD  
738  O OE1 . GLN B 45  ? 1.0858 0.9984 1.0150 -0.0624 -0.0584 -0.0048 393 GLN B OE1 
739  N NE2 . GLN B 45  ? 1.1429 1.0991 1.0537 -0.0804 -0.0493 0.0032  393 GLN B NE2 
740  N N   . GLN B 46  ? 1.4105 1.3572 1.4003 -0.1047 -0.0572 -0.0771 394 GLN B N   
741  C CA  . GLN B 46  ? 1.5179 1.4487 1.5288 -0.1110 -0.0599 -0.0998 394 GLN B CA  
742  C C   . GLN B 46  ? 1.6346 1.5011 1.6555 -0.1215 -0.0667 -0.0893 394 GLN B C   
743  O O   . GLN B 46  ? 1.7157 1.5582 1.7546 -0.1250 -0.0691 -0.1083 394 GLN B O   
744  C CB  . GLN B 46  ? 1.5216 1.4918 1.5385 -0.1315 -0.0547 -0.1189 394 GLN B CB  
745  C CG  . GLN B 46  ? 1.5385 1.5014 1.5762 -0.1378 -0.0559 -0.1480 394 GLN B CG  
746  C CD  . GLN B 46  ? 1.5226 1.5461 1.5645 -0.1499 -0.0500 -0.1719 394 GLN B CD  
747  O OE1 . GLN B 46  ? 1.4734 1.5517 1.5031 -0.1428 -0.0455 -0.1686 394 GLN B OE1 
748  N NE2 . GLN B 46  ? 1.5419 1.5574 1.6016 -0.1673 -0.0500 -0.1974 394 GLN B NE2 
749  N N   . LEU B 47  ? 1.6804 1.5209 1.6900 -0.1253 -0.0696 -0.0607 395 LEU B N   
750  C CA  . LEU B 47  ? 1.7229 1.5023 1.7388 -0.1293 -0.0772 -0.0438 395 LEU B CA  
751  C C   . LEU B 47  ? 1.7308 1.4819 1.7639 -0.1086 -0.0825 -0.0597 395 LEU B C   
752  O O   . LEU B 47  ? 1.7298 1.4387 1.7784 -0.1173 -0.0856 -0.0680 395 LEU B O   
753  C CB  . LEU B 47  ? 1.7192 1.4928 1.7180 -0.1239 -0.0798 -0.0126 395 LEU B CB  
754  C CG  . LEU B 47  ? 1.7917 1.5115 1.7921 -0.1318 -0.0872 0.0125  395 LEU B CG  
755  C CD1 . LEU B 47  ? 1.7688 1.5002 1.7496 -0.1446 -0.0865 0.0418  395 LEU B CD1 
756  C CD2 . LEU B 47  ? 1.8142 1.5038 1.8232 -0.1055 -0.0951 0.0154  395 LEU B CD2 
757  N N   . LEU B 48  ? 1.7025 1.4764 1.7330 -0.0830 -0.0829 -0.0650 396 LEU B N   
758  C CA  . LEU B 48  ? 1.7046 1.4616 1.7501 -0.0607 -0.0878 -0.0794 396 LEU B CA  
759  C C   . LEU B 48  ? 1.6152 1.4116 1.6691 -0.0536 -0.0831 -0.1114 396 LEU B C   
760  O O   . LEU B 48  ? 1.5016 1.3427 1.5464 -0.0589 -0.0765 -0.1183 396 LEU B O   
761  C CB  . LEU B 48  ? 1.7119 1.4714 1.7472 -0.0403 -0.0914 -0.0615 396 LEU B CB  
762  C CG  . LEU B 48  ? 1.7430 1.4689 1.7711 -0.0441 -0.0973 -0.0302 396 LEU B CG  
763  C CD1 . LEU B 48  ? 1.7041 1.4456 1.7207 -0.0268 -0.0994 -0.0162 396 LEU B CD1 
764  C CD2 . LEU B 48  ? 1.7969 1.4686 1.8425 -0.0429 -0.1050 -0.0281 396 LEU B CD2 
765  N N   . GLY C 1   ? 1.3571 0.9970 0.9905 0.0582  0.1432  0.0694  1   GLY C N   
766  C CA  . GLY C 1   ? 1.2504 0.9417 0.9137 0.0776  0.1249  0.0728  1   GLY C CA  
767  C C   . GLY C 1   ? 1.1994 0.9048 0.8607 0.0840  0.1235  0.0778  1   GLY C C   
768  O O   . GLY C 1   ? 1.2607 0.9305 0.8924 0.0787  0.1368  0.0817  1   GLY C O   
769  N N   . SER C 2   ? 1.0843 0.8376 0.7729 0.0924  0.1095  0.0768  2   SER C N   
770  C CA  . SER C 2   ? 1.0460 0.8223 0.7366 0.0979  0.1059  0.0793  2   SER C CA  
771  C C   . SER C 2   ? 1.0112 0.8290 0.7113 0.1159  0.0935  0.0795  2   SER C C   
772  O O   . SER C 2   ? 0.9016 0.7380 0.6192 0.1158  0.0867  0.0750  2   SER C O   
773  C CB  . SER C 2   ? 1.0135 0.8110 0.7316 0.0765  0.1049  0.0714  2   SER C CB  
774  O OG  . SER C 2   ? 0.9314 0.7636 0.6803 0.0725  0.0944  0.0643  2   SER C OG  
775  N N   . ASP C 3   ? 1.0280 0.8637 0.7162 0.1293  0.0914  0.0831  3   ASP C N   
776  C CA  . ASP C 3   ? 0.9975 0.8849 0.6932 0.1437  0.0806  0.0801  3   ASP C CA  
777  C C   . ASP C 3   ? 0.8968 0.8207 0.6285 0.1220  0.0734  0.0678  3   ASP C C   
778  O O   . ASP C 3   ? 0.8715 0.8257 0.6143 0.1245  0.0672  0.0626  3   ASP C O   
779  C CB  . ASP C 3   ? 1.0692 0.9741 0.7460 0.1585  0.0804  0.0840  3   ASP C CB  
780  C CG  . ASP C 3   ? 1.1038 1.0742 0.7888 0.1706  0.0697  0.0774  3   ASP C CG  
781  O OD1 . ASP C 3   ? 1.1722 1.1647 0.8624 0.1802  0.0647  0.0751  3   ASP C OD1 
782  O OD2 . ASP C 3   ? 1.1828 1.1856 0.8689 0.1688  0.0669  0.0731  3   ASP C OD2 
783  N N   . LEU C 4   ? 0.8307 0.7510 0.5751 0.1029  0.0757  0.0632  4   LEU C N   
784  C CA  . LEU C 4   ? 0.7700 0.7111 0.5372 0.0843  0.0726  0.0524  4   LEU C CA  
785  C C   . LEU C 4   ? 0.7310 0.6589 0.5118 0.0775  0.0722  0.0504  4   LEU C C   
786  O O   . LEU C 4   ? 0.7105 0.6544 0.5021 0.0685  0.0698  0.0430  4   LEU C O   
787  C CB  . LEU C 4   ? 0.7855 0.7168 0.5555 0.0719  0.0771  0.0499  4   LEU C CB  
788  C CG  . LEU C 4   ? 0.8311 0.7814 0.5908 0.0742  0.0770  0.0488  4   LEU C CG  
789  C CD1 . LEU C 4   ? 0.8403 0.7802 0.6039 0.0611  0.0818  0.0447  4   LEU C CD1 
790  C CD2 . LEU C 4   ? 0.8299 0.8231 0.5915 0.0730  0.0713  0.0400  4   LEU C CD2 
791  N N   . GLY C 5   ? 0.7179 0.6162 0.4950 0.0792  0.0762  0.0555  5   GLY C N   
792  C CA  . GLY C 5   ? 0.7544 0.6423 0.5421 0.0747  0.0758  0.0535  5   GLY C CA  
793  C C   . GLY C 5   ? 0.7313 0.6334 0.5197 0.0837  0.0706  0.0532  5   GLY C C   
794  O O   . GLY C 5   ? 0.7255 0.6376 0.5272 0.0765  0.0680  0.0478  5   GLY C O   
795  N N   . LYS C 6   ? 0.7842 0.6879 0.5552 0.1011  0.0701  0.0589  6   LYS C N   
796  C CA  . LYS C 6   ? 0.8241 0.7512 0.5937 0.1148  0.0650  0.0583  6   LYS C CA  
797  C C   . LYS C 6   ? 0.7680 0.7422 0.5529 0.1055  0.0597  0.0487  6   LYS C C   
798  O O   . LYS C 6   ? 0.7343 0.7249 0.5292 0.1014  0.0573  0.0436  6   LYS C O   
799  C CB  . LYS C 6   ? 0.9091 0.8285 0.6496 0.1418  0.0667  0.0672  6   LYS C CB  
800  C CG  . LYS C 6   ? 1.0224 0.8853 0.7397 0.1477  0.0755  0.0747  6   LYS C CG  
801  C CD  . LYS C 6   ? 1.1257 0.9640 0.8015 0.1778  0.0812  0.0853  6   LYS C CD  
802  C CE  . LYS C 6   ? 1.2109 0.9789 0.8553 0.1755  0.0951  0.0911  6   LYS C CE  
803  N NZ  . LYS C 6   ? 1.3215 1.0505 0.9138 0.2055  0.1047  0.1031  6   LYS C NZ  
804  N N   . LYS C 7   ? 0.7603 0.7541 0.5446 0.0995  0.0596  0.0451  7   LYS C N   
805  C CA  . LYS C 7   ? 0.7582 0.7931 0.5526 0.0835  0.0580  0.0326  7   LYS C CA  
806  C C   . LYS C 7   ? 0.7175 0.7302 0.5222 0.0618  0.0621  0.0269  7   LYS C C   
807  O O   . LYS C 7   ? 0.7466 0.7813 0.5551 0.0485  0.0632  0.0173  7   LYS C O   
808  C CB  . LYS C 7   ? 0.8021 0.8575 0.5905 0.0791  0.0585  0.0286  7   LYS C CB  
809  C CG  . LYS C 7   ? 0.8401 0.9347 0.6158 0.1024  0.0537  0.0313  7   LYS C CG  
810  C CD  . LYS C 7   ? 0.8804 0.9995 0.6501 0.0978  0.0537  0.0263  7   LYS C CD  
811  C CE  . LYS C 7   ? 0.9145 1.0836 0.6698 0.1247  0.0481  0.0278  7   LYS C CE  
812  N NZ  . LYS C 7   ? 0.9639 1.1573 0.7122 0.1210  0.0480  0.0230  7   LYS C NZ  
813  N N   . LEU C 8   ? 0.6825 0.6555 0.4882 0.0590  0.0655  0.0318  8   LEU C N   
814  C CA  . LEU C 8   ? 0.6887 0.6394 0.4977 0.0455  0.0701  0.0276  8   LEU C CA  
815  C C   . LEU C 8   ? 0.6893 0.6347 0.5038 0.0484  0.0685  0.0286  8   LEU C C   
816  O O   . LEU C 8   ? 0.6783 0.6220 0.4907 0.0376  0.0719  0.0227  8   LEU C O   
817  C CB  . LEU C 8   ? 0.6789 0.6023 0.4873 0.0467  0.0732  0.0317  8   LEU C CB  
818  C CG  . LEU C 8   ? 0.6806 0.5820 0.4869 0.0418  0.0780  0.0290  8   LEU C CG  
819  C CD1 . LEU C 8   ? 0.6892 0.5858 0.4818 0.0284  0.0845  0.0209  8   LEU C CD1 
820  C CD2 . LEU C 8   ? 0.6935 0.5821 0.5006 0.0467  0.0803  0.0317  8   LEU C CD2 
821  N N   . LEU C 9   ? 0.6927 0.6323 0.5098 0.0616  0.0650  0.0353  9   LEU C N   
822  C CA  . LEU C 9   ? 0.6778 0.6158 0.4990 0.0662  0.0629  0.0360  9   LEU C CA  
823  C C   . LEU C 9   ? 0.7074 0.6773 0.5295 0.0619  0.0617  0.0295  9   LEU C C   
824  O O   . LEU C 9   ? 0.7014 0.6679 0.5255 0.0530  0.0641  0.0254  9   LEU C O   
825  C CB  . LEU C 9   ? 0.6735 0.5994 0.4890 0.0809  0.0615  0.0429  9   LEU C CB  
826  C CG  . LEU C 9   ? 0.6857 0.5822 0.5003 0.0780  0.0651  0.0456  9   LEU C CG  
827  C CD1 . LEU C 9   ? 0.7010 0.5761 0.4988 0.0882  0.0683  0.0514  9   LEU C CD1 
828  C CD2 . LEU C 9   ? 0.6950 0.5852 0.5191 0.0728  0.0647  0.0423  9   LEU C CD2 
829  N N   . GLU C 10  ? 0.7460 0.7496 0.5650 0.0676  0.0591  0.0276  10  GLU C N   
830  C CA  . GLU C 10  ? 0.7779 0.8284 0.5995 0.0630  0.0578  0.0185  10  GLU C CA  
831  C C   . GLU C 10  ? 0.7718 0.8263 0.5923 0.0346  0.0650  0.0067  10  GLU C C   
832  O O   . GLU C 10  ? 0.7642 0.8313 0.5857 0.0228  0.0683  -0.0004 10  GLU C O   
833  C CB  . GLU C 10  ? 0.8222 0.9160 0.6387 0.0796  0.0530  0.0185  10  GLU C CB  
834  C CG  . GLU C 10  ? 0.8694 1.0280 0.6904 0.0768  0.0509  0.0069  10  GLU C CG  
835  C CD  . GLU C 10  ? 0.9182 1.0867 0.7435 0.0857  0.0492  0.0073  10  GLU C CD  
836  O OE1 . GLU C 10  ? 0.9450 1.0661 0.7687 0.0945  0.0494  0.0169  10  GLU C OE1 
837  O OE2 . GLU C 10  ? 0.9706 1.1993 0.8008 0.0830  0.0480  -0.0034 10  GLU C OE2 
838  N N   . ALA C 11  ? 0.7602 0.8008 0.5744 0.0232  0.0693  0.0041  11  ALA C N   
839  C CA  . ALA C 11  ? 0.7814 0.8133 0.5845 -0.0045 0.0797  -0.0077 11  ALA C CA  
840  C C   . ALA C 11  ? 0.7796 0.7645 0.5739 -0.0109 0.0871  -0.0057 11  ALA C C   
841  O O   . ALA C 11  ? 0.7925 0.7758 0.5751 -0.0316 0.0964  -0.0155 11  ALA C O   
842  C CB  . ALA C 11  ? 0.8037 0.8207 0.5986 -0.0097 0.0829  -0.0086 11  ALA C CB  
843  N N   . ALA C 12  ? 0.7720 0.7214 0.5688 0.0054  0.0844  0.0055  12  ALA C N   
844  C CA  . ALA C 12  ? 0.7751 0.6844 0.5627 0.0076  0.0895  0.0091  12  ALA C CA  
845  C C   . ALA C 12  ? 0.7835 0.7046 0.5750 0.0066  0.0886  0.0078  12  ALA C C   
846  O O   . ALA C 12  ? 0.8000 0.6942 0.5744 -0.0024 0.0978  0.0053  12  ALA C O   
847  C CB  . ALA C 12  ? 0.7626 0.6541 0.5579 0.0266  0.0841  0.0189  12  ALA C CB  
848  N N   . ALA C 13  ? 0.7724 0.7284 0.5808 0.0172  0.0792  0.0098  13  ALA C N   
849  C CA  . ALA C 13  ? 0.7601 0.7311 0.5740 0.0206  0.0771  0.0093  13  ALA C CA  
850  C C   . ALA C 13  ? 0.8169 0.8151 0.6239 -0.0018 0.0847  -0.0033 13  ALA C C   
851  O O   . ALA C 13  ? 0.8260 0.8135 0.6261 -0.0093 0.0903  -0.0055 13  ALA C O   
852  C CB  . ALA C 13  ? 0.7480 0.7440 0.5745 0.0410  0.0670  0.0147  13  ALA C CB  
853  N N   . VAL C 14  ? 0.8262 0.8626 0.6342 -0.0132 0.0854  -0.0124 14  VAL C N   
854  C CA  . VAL C 14  ? 0.8622 0.9425 0.6662 -0.0387 0.0928  -0.0287 14  VAL C CA  
855  C C   . VAL C 14  ? 0.8879 0.9323 0.6664 -0.0710 0.1095  -0.0388 14  VAL C C   
856  O O   . VAL C 14  ? 0.9370 1.0052 0.7054 -0.1002 0.1205  -0.0544 14  VAL C O   
857  C CB  . VAL C 14  ? 0.8620 1.0157 0.6795 -0.0323 0.0844  -0.0356 14  VAL C CB  
858  C CG1 . VAL C 14  ? 0.8539 1.0280 0.6851 0.0041  0.0710  -0.0238 14  VAL C CG1 
859  C CG2 . VAL C 14  ? 0.8776 1.0335 0.6908 -0.0369 0.0844  -0.0381 14  VAL C CG2 
860  N N   . GLY C 15  ? 0.8968 0.8856 0.6619 -0.0662 0.1131  -0.0314 15  GLY C N   
861  C CA  . GLY C 15  ? 0.9441 0.8764 0.6743 -0.0891 0.1314  -0.0374 15  GLY C CA  
862  C C   . GLY C 15  ? 0.9857 0.9298 0.7041 -0.1126 0.1390  -0.0506 15  GLY C C   
863  O O   . GLY C 15  ? 0.9890 0.8952 0.6727 -0.1420 0.1586  -0.0619 15  GLY C O   
864  N N   . GLN C 16  ? 0.9447 0.9319 0.6850 -0.1003 0.1261  -0.0492 16  GLN C N   
865  C CA  . GLN C 16  ? 0.9575 0.9597 0.6883 -0.1190 0.1313  -0.0611 16  GLN C CA  
866  C C   . GLN C 16  ? 0.9694 0.9020 0.6783 -0.1126 0.1383  -0.0534 16  GLN C C   
867  O O   . GLN C 16  ? 0.9452 0.8816 0.6692 -0.0892 0.1271  -0.0428 16  GLN C O   
868  C CB  . GLN C 16  ? 0.9810 1.0535 0.7397 -0.1019 0.1146  -0.0603 16  GLN C CB  
869  C CG  . GLN C 16  ? 1.0021 1.1533 0.7783 -0.1046 0.1083  -0.0699 16  GLN C CG  
870  C CD  . GLN C 16  ? 1.0378 1.2437 0.8354 -0.0717 0.0909  -0.0619 16  GLN C CD  
871  O OE1 . GLN C 16  ? 1.0475 1.2228 0.8493 -0.0441 0.0829  -0.0452 16  GLN C OE1 
872  N NE2 . GLN C 16  ? 1.0464 1.3348 0.8541 -0.0734 0.0862  -0.0742 16  GLN C NE2 
873  N N   . ASP C 17  ? 1.0316 0.9015 0.7017 -0.1320 0.1580  -0.0590 17  ASP C N   
874  C CA  . ASP C 17  ? 1.1025 0.8999 0.7421 -0.1224 0.1679  -0.0521 17  ASP C CA  
875  C C   . ASP C 17  ? 1.0682 0.8834 0.7133 -0.1227 0.1638  -0.0555 17  ASP C C   
876  O O   . ASP C 17  ? 1.0307 0.8221 0.6786 -0.0969 0.1583  -0.0431 17  ASP C O   
877  C CB  . ASP C 17  ? 1.2220 0.9486 0.8067 -0.1486 0.1944  -0.0618 17  ASP C CB  
878  C CG  . ASP C 17  ? 1.3215 1.0164 0.8907 -0.1470 0.2018  -0.0571 17  ASP C CG  
879  O OD1 . ASP C 17  ? 1.3786 1.1119 0.9565 -0.1710 0.2040  -0.0679 17  ASP C OD1 
880  O OD2 . ASP C 17  ? 1.4058 1.0426 0.9539 -0.1204 0.2054  -0.0431 17  ASP C OD2 
881  N N   . ASP C 18  ? 1.0636 0.9231 0.7089 -0.1518 0.1672  -0.0732 18  ASP C N   
882  C CA  . ASP C 18  ? 1.0699 0.9462 0.7142 -0.1571 0.1661  -0.0797 18  ASP C CA  
883  C C   . ASP C 18  ? 0.9883 0.9125 0.6722 -0.1242 0.1437  -0.0658 18  ASP C C   
884  O O   . ASP C 18  ? 0.9911 0.8946 0.6733 -0.1089 0.1412  -0.0581 18  ASP C O   
885  C CB  . ASP C 18  ? 1.1279 1.0516 0.7633 -0.1983 0.1750  -0.1049 18  ASP C CB  
886  C CG  . ASP C 18  ? 1.2470 1.1101 0.8322 -0.2380 0.2028  -0.1214 18  ASP C CG  
887  O OD1 . ASP C 18  ? 1.3146 1.0892 0.8627 -0.2300 0.2165  -0.1134 18  ASP C OD1 
888  O OD2 . ASP C 18  ? 1.3284 1.2326 0.9082 -0.2761 0.2120  -0.1427 18  ASP C OD2 
889  N N   . GLU C 19  ? 0.9346 0.9170 0.6482 -0.1137 0.1299  -0.0629 19  GLU C N   
890  C CA  . GLU C 19  ? 0.8999 0.9192 0.6421 -0.0820 0.1116  -0.0493 19  GLU C CA  
891  C C   . GLU C 19  ? 0.8805 0.8481 0.6259 -0.0559 0.1081  -0.0307 19  GLU C C   
892  O O   . GLU C 19  ? 0.8735 0.8448 0.6276 -0.0386 0.1011  -0.0221 19  GLU C O   
893  C CB  . GLU C 19  ? 0.8930 0.9720 0.6562 -0.0735 0.1011  -0.0498 19  GLU C CB  
894  C CG  . GLU C 19  ? 0.9010 1.0096 0.6822 -0.0401 0.0858  -0.0362 19  GLU C CG  
895  C CD  . GLU C 19  ? 0.9394 1.0852 0.7190 -0.0364 0.0817  -0.0401 19  GLU C CD  
896  O OE1 . GLU C 19  ? 0.9455 1.0997 0.7132 -0.0623 0.0899  -0.0552 19  GLU C OE1 
897  O OE2 . GLU C 19  ? 0.9511 1.1140 0.7372 -0.0077 0.0717  -0.0282 19  GLU C OE2 
898  N N   . VAL C 20  ? 0.8827 0.8076 0.6198 -0.0539 0.1138  -0.0260 20  VAL C N   
899  C CA  . VAL C 20  ? 0.8584 0.7419 0.5968 -0.0307 0.1118  -0.0117 20  VAL C CA  
900  C C   . VAL C 20  ? 0.8764 0.7300 0.5988 -0.0285 0.1181  -0.0114 20  VAL C C   
901  O O   . VAL C 20  ? 0.8298 0.6874 0.5660 -0.0101 0.1107  -0.0021 20  VAL C O   
902  C CB  . VAL C 20  ? 0.8622 0.7076 0.5874 -0.0287 0.1185  -0.0089 20  VAL C CB  
903  C CG1 . VAL C 20  ? 0.8604 0.6666 0.5777 -0.0071 0.1200  0.0011  20  VAL C CG1 
904  C CG2 . VAL C 20  ? 0.8322 0.7055 0.5783 -0.0224 0.1095  -0.0053 20  VAL C CG2 
905  N N   . ARG C 21  ? 0.9362 0.7582 0.6274 -0.0476 0.1329  -0.0218 21  ARG C N   
906  C CA  . ARG C 21  ? 0.9940 0.7814 0.6633 -0.0444 0.1412  -0.0224 21  ARG C CA  
907  C C   . ARG C 21  ? 0.9540 0.7825 0.6418 -0.0434 0.1322  -0.0232 21  ARG C C   
908  O O   . ARG C 21  ? 0.9281 0.7454 0.6180 -0.0265 0.1302  -0.0158 21  ARG C O   
909  C CB  . ARG C 21  ? 1.0929 0.8318 0.7170 -0.0688 0.1620  -0.0355 21  ARG C CB  
910  C CG  . ARG C 21  ? 1.1685 0.8503 0.7624 -0.0639 0.1742  -0.0318 21  ARG C CG  
911  C CD  . ARG C 21  ? 1.2734 0.8850 0.8086 -0.0832 0.1994  -0.0423 21  ARG C CD  
912  N NE  . ARG C 21  ? 1.3654 0.9324 0.8704 -0.0895 0.2127  -0.0425 21  ARG C NE  
913  C CZ  . ARG C 21  ? 1.4305 1.0098 0.9303 -0.1231 0.2203  -0.0551 21  ARG C CZ  
914  N NH1 . ARG C 21  ? 1.4296 1.0713 0.9532 -0.1523 0.2151  -0.0698 21  ARG C NH1 
915  N NH2 . ARG C 21  ? 1.5108 1.0430 0.9794 -0.1266 0.2337  -0.0536 21  ARG C NH2 
916  N N   . ILE C 22  ? 0.9159 0.7945 0.6158 -0.0585 0.1269  -0.0320 22  ILE C N   
917  C CA  . ILE C 22  ? 0.9118 0.8323 0.6252 -0.0540 0.1183  -0.0321 22  ILE C CA  
918  C C   . ILE C 22  ? 0.8524 0.7789 0.5881 -0.0255 0.1064  -0.0150 22  ILE C C   
919  O O   . ILE C 22  ? 0.7999 0.7225 0.5357 -0.0164 0.1053  -0.0102 22  ILE C O   
920  C CB  . ILE C 22  ? 0.9447 0.9291 0.6671 -0.0678 0.1129  -0.0437 22  ILE C CB  
921  C CG1 . ILE C 22  ? 1.0135 1.0004 0.7135 -0.1041 0.1267  -0.0651 22  ILE C CG1 
922  C CG2 . ILE C 22  ? 0.9441 0.9663 0.6749 -0.0559 0.1042  -0.0410 22  ILE C CG2 
923  C CD1 . ILE C 22  ? 1.0206 1.0855 0.7333 -0.1182 0.1210  -0.0790 22  ILE C CD1 
924  N N   . LEU C 23  ? 0.8052 0.7394 0.5565 -0.0146 0.0995  -0.0074 23  LEU C N   
925  C CA  . LEU C 23  ? 0.7784 0.7178 0.5466 0.0073  0.0905  0.0063  23  LEU C CA  
926  C C   . LEU C 23  ? 0.7722 0.6776 0.5390 0.0163  0.0942  0.0129  23  LEU C C   
927  O O   . LEU C 23  ? 0.7102 0.6192 0.4820 0.0252  0.0919  0.0191  23  LEU C O   
928  C CB  . LEU C 23  ? 0.7765 0.7266 0.5562 0.0137  0.0849  0.0102  23  LEU C CB  
929  C CG  . LEU C 23  ? 0.7724 0.7687 0.5554 0.0114  0.0798  0.0044  23  LEU C CG  
930  C CD1 . LEU C 23  ? 0.7696 0.7727 0.5612 0.0164  0.0763  0.0065  23  LEU C CD1 
931  C CD2 . LEU C 23  ? 0.7905 0.8125 0.5739 0.0279  0.0734  0.0106  23  LEU C CD2 
932  N N   . MET C 24  ? 0.7707 0.6459 0.5269 0.0145  0.1010  0.0107  24  MET C N   
933  C CA  . MET C 24  ? 0.8259 0.6776 0.5784 0.0275  0.1046  0.0153  24  MET C CA  
934  C C   . MET C 24  ? 0.8106 0.6596 0.5545 0.0278  0.1087  0.0136  24  MET C C   
935  O O   . MET C 24  ? 0.7904 0.6465 0.5440 0.0384  0.1067  0.0187  24  MET C O   
936  C CB  . MET C 24  ? 0.9007 0.7169 0.6317 0.0291  0.1134  0.0127  24  MET C CB  
937  C CG  . MET C 24  ? 1.0102 0.8276 0.7469 0.0275  0.1106  0.0137  24  MET C CG  
938  S SD  . MET C 24  ? 1.1425 0.9740 0.9020 0.0467  0.1019  0.0225  24  MET C SD  
939  C CE  . MET C 24  ? 1.0804 0.8743 0.8125 0.0612  0.1113  0.0229  24  MET C CE  
940  N N   . ALA C 25  ? 0.8058 0.6447 0.5301 0.0142  0.1157  0.0049  25  ALA C N   
941  C CA  . ALA C 25  ? 0.8234 0.6574 0.5354 0.0126  0.1207  0.0014  25  ALA C CA  
942  C C   . ALA C 25  ? 0.7823 0.6513 0.5129 0.0158  0.1122  0.0063  25  ALA C C   
943  O O   . ALA C 25  ? 0.7803 0.6488 0.5074 0.0201  0.1146  0.0073  25  ALA C O   
944  C CB  . ALA C 25  ? 0.8653 0.6843 0.5513 -0.0083 0.1305  -0.0116 25  ALA C CB  
945  N N   . ASN C 26  ? 0.7579 0.6530 0.5038 0.0161  0.1037  0.0100  26  ASN C N   
946  C CA  . ASN C 26  ? 0.7584 0.6774 0.5121 0.0230  0.0978  0.0164  26  ASN C CA  
947  C C   . ASN C 26  ? 0.7398 0.6513 0.5051 0.0344  0.0960  0.0267  26  ASN C C   
948  O O   . ASN C 26  ? 0.7566 0.6755 0.5215 0.0400  0.0943  0.0332  26  ASN C O   
949  C CB  . ASN C 26  ? 0.7798 0.7309 0.5346 0.0207  0.0917  0.0138  26  ASN C CB  
950  C CG  . ASN C 26  ? 0.8102 0.7824 0.5531 0.0085  0.0938  0.0025  26  ASN C CG  
951  O OD1 . ASN C 26  ? 0.8696 0.8548 0.6075 0.0140  0.0927  0.0047  26  ASN C OD1 
952  N ND2 . ASN C 26  ? 0.7861 0.7595 0.5211 -0.0102 0.0987  -0.0106 26  ASN C ND2 
953  N N   . GLY C 27  ? 0.7326 0.6291 0.5034 0.0372  0.0983  0.0269  27  GLY C N   
954  C CA  . GLY C 27  ? 0.7354 0.6316 0.5178 0.0431  0.0979  0.0324  27  GLY C CA  
955  C C   . GLY C 27  ? 0.7146 0.6126 0.5042 0.0445  0.0931  0.0367  27  GLY C C   
956  O O   . GLY C 27  ? 0.7025 0.5984 0.4951 0.0450  0.0945  0.0409  27  GLY C O   
957  N N   . ALA C 28  ? 0.6986 0.5991 0.4880 0.0434  0.0892  0.0347  28  ALA C N   
958  C CA  . ALA C 28  ? 0.6953 0.5972 0.4907 0.0471  0.0849  0.0383  28  ALA C CA  
959  C C   . ALA C 28  ? 0.6805 0.5743 0.4851 0.0484  0.0861  0.0389  28  ALA C C   
960  O O   . ALA C 28  ? 0.6867 0.5785 0.4930 0.0493  0.0885  0.0352  28  ALA C O   
961  C CB  . ALA C 28  ? 0.6885 0.5992 0.4836 0.0441  0.0818  0.0339  28  ALA C CB  
962  N N   . ASP C 29  ? 0.6835 0.5728 0.4897 0.0497  0.0856  0.0427  29  ASP C N   
963  C CA  . ASP C 29  ? 0.6830 0.5713 0.4976 0.0469  0.0875  0.0407  29  ASP C CA  
964  C C   . ASP C 29  ? 0.6721 0.5643 0.4944 0.0507  0.0833  0.0377  29  ASP C C   
965  O O   . ASP C 29  ? 0.6751 0.5637 0.4972 0.0527  0.0799  0.0393  29  ASP C O   
966  C CB  . ASP C 29  ? 0.7035 0.5768 0.5095 0.0441  0.0909  0.0442  29  ASP C CB  
967  C CG  . ASP C 29  ? 0.7484 0.6244 0.5616 0.0353  0.0943  0.0387  29  ASP C CG  
968  O OD1 . ASP C 29  ? 0.7404 0.6384 0.5668 0.0339  0.0936  0.0326  29  ASP C OD1 
969  O OD2 . ASP C 29  ? 0.8209 0.6779 0.6235 0.0310  0.0984  0.0397  29  ASP C OD2 
970  N N   . VAL C 30  ? 0.7047 0.6031 0.5297 0.0545  0.0844  0.0339  30  VAL C N   
971  C CA  . VAL C 30  ? 0.7164 0.6115 0.5403 0.0615  0.0826  0.0323  30  VAL C CA  
972  C C   . VAL C 30  ? 0.7042 0.6078 0.5380 0.0619  0.0795  0.0312  30  VAL C C   
973  O O   . VAL C 30  ? 0.7126 0.6110 0.5447 0.0666  0.0772  0.0314  30  VAL C O   
974  C CB  . VAL C 30  ? 0.7607 0.6551 0.5762 0.0721  0.0865  0.0299  30  VAL C CB  
975  C CG1 . VAL C 30  ? 0.7761 0.6975 0.6019 0.0786  0.0864  0.0263  30  VAL C CG1 
976  C CG2 . VAL C 30  ? 0.8153 0.6896 0.6157 0.0800  0.0883  0.0302  30  VAL C CG2 
977  N N   . ASN C 31  ? 0.6846 0.5988 0.5254 0.0548  0.0810  0.0290  31  ASN C N   
978  C CA  . ASN C 31  ? 0.6793 0.6010 0.5268 0.0506  0.0799  0.0253  31  ASN C CA  
979  C C   . ASN C 31  ? 0.6850 0.5846 0.5244 0.0427  0.0820  0.0288  31  ASN C C   
980  O O   . ASN C 31  ? 0.7185 0.6159 0.5566 0.0334  0.0856  0.0245  31  ASN C O   
981  C CB  . ASN C 31  ? 0.6963 0.6490 0.5528 0.0464  0.0826  0.0166  31  ASN C CB  
982  C CG  . ASN C 31  ? 0.7186 0.6924 0.5770 0.0640  0.0801  0.0146  31  ASN C CG  
983  O OD1 . ASN C 31  ? 0.7042 0.6730 0.5587 0.0766  0.0764  0.0165  31  ASN C OD1 
984  N ND2 . ASN C 31  ? 0.7300 0.7231 0.5892 0.0675  0.0833  0.0117  31  ASN C ND2 
985  N N   . ALA C 32  ? 0.6760 0.5604 0.5065 0.0476  0.0806  0.0355  32  ALA C N   
986  C CA  . ALA C 32  ? 0.6759 0.5398 0.4927 0.0496  0.0821  0.0404  32  ALA C CA  
987  C C   . ALA C 32  ? 0.7033 0.5646 0.5229 0.0519  0.0793  0.0386  32  ALA C C   
988  O O   . ALA C 32  ? 0.6576 0.5341 0.4892 0.0545  0.0744  0.0356  32  ALA C O   
989  C CB  . ALA C 32  ? 0.6685 0.5336 0.4783 0.0587  0.0789  0.0459  32  ALA C CB  
990  N N   . MET C 33  ? 0.7064 0.5443 0.5101 0.0524  0.0836  0.0407  33  MET C N   
991  C CA  . MET C 33  ? 0.7471 0.5781 0.5495 0.0541  0.0824  0.0384  33  MET C CA  
992  C C   . MET C 33  ? 0.7434 0.5566 0.5273 0.0698  0.0822  0.0457  33  MET C C   
993  O O   . MET C 33  ? 0.7516 0.5458 0.5152 0.0760  0.0873  0.0516  33  MET C O   
994  C CB  . MET C 33  ? 0.7830 0.6012 0.5788 0.0378  0.0908  0.0307  33  MET C CB  
995  C CG  . MET C 33  ? 0.8030 0.6573 0.6217 0.0282  0.0877  0.0211  33  MET C CG  
996  S SD  . MET C 33  ? 0.8878 0.7455 0.7029 0.0048  0.0968  0.0067  33  MET C SD  
997  C CE  . MET C 33  ? 0.9217 0.7479 0.7129 -0.0119 0.1119  0.0071  33  MET C CE  
998  N N   . ASP C 34  ? 0.7334 0.5591 0.5244 0.0786  0.0759  0.0456  34  ASP C N   
999  C CA  . ASP C 34  ? 0.7564 0.5723 0.5297 0.0966  0.0756  0.0509  34  ASP C CA  
1000 C C   . ASP C 34  ? 0.7913 0.5708 0.5448 0.0952  0.0832  0.0493  34  ASP C C   
1001 O O   . ASP C 34  ? 0.7847 0.5526 0.5401 0.0765  0.0887  0.0427  34  ASP C O   
1002 C CB  . ASP C 34  ? 0.7163 0.5672 0.5055 0.1039  0.0670  0.0498  34  ASP C CB  
1003 C CG  . ASP C 34  ? 0.7082 0.5645 0.5096 0.0989  0.0642  0.0449  34  ASP C CG  
1004 O OD1 . ASP C 34  ? 0.7062 0.5441 0.5058 0.0908  0.0676  0.0414  34  ASP C OD1 
1005 O OD2 . ASP C 34  ? 0.7085 0.5899 0.5199 0.1016  0.0594  0.0434  34  ASP C OD2 
1006 N N   . GLN C 35  ? 0.8391 0.6036 0.5720 0.1140  0.0845  0.0537  35  GLN C N   
1007 C CA  . GLN C 35  ? 0.9355 0.6508 0.6361 0.1158  0.0954  0.0532  35  GLN C CA  
1008 C C   . GLN C 35  ? 0.8884 0.6094 0.6048 0.1000  0.0939  0.0434  35  GLN C C   
1009 O O   . GLN C 35  ? 0.9599 0.6402 0.6506 0.0936  0.1044  0.0394  35  GLN C O   
1010 C CB  . GLN C 35  ? 1.0124 0.7123 0.6828 0.1477  0.0969  0.0616  35  GLN C CB  
1011 C CG  . GLN C 35  ? 1.0427 0.7934 0.7371 0.1619  0.0843  0.0611  35  GLN C CG  
1012 C CD  . GLN C 35  ? 1.0717 0.8755 0.7902 0.1650  0.0746  0.0622  35  GLN C CD  
1013 O OE1 . GLN C 35  ? 1.0819 0.8884 0.8049 0.1561  0.0752  0.0633  35  GLN C OE1 
1014 N NE2 . GLN C 35  ? 1.1205 0.9687 0.8531 0.1758  0.0668  0.0603  35  GLN C NE2 
1015 N N   . ASN C 36  ? 0.8040 0.5693 0.5559 0.0937  0.0830  0.0392  36  ASN C N   
1016 C CA  . ASN C 36  ? 0.7822 0.5586 0.5485 0.0815  0.0808  0.0301  36  ASN C CA  
1017 C C   . ASN C 36  ? 0.7637 0.5617 0.5498 0.0620  0.0800  0.0227  36  ASN C C   
1018 O O   . ASN C 36  ? 0.7650 0.5817 0.5640 0.0539  0.0773  0.0145  36  ASN C O   
1019 C CB  . ASN C 36  ? 0.7642 0.5702 0.5475 0.0930  0.0711  0.0315  36  ASN C CB  
1020 C CG  . ASN C 36  ? 0.7913 0.5830 0.5551 0.1123  0.0725  0.0359  36  ASN C CG  
1021 O OD1 . ASN C 36  ? 0.8574 0.6123 0.5959 0.1141  0.0805  0.0343  36  ASN C OD1 
1022 N ND2 . ASN C 36  ? 0.7693 0.5901 0.5411 0.1264  0.0662  0.0403  36  ASN C ND2 
1023 N N   . GLY C 37  ? 0.7290 0.5294 0.5170 0.0576  0.0819  0.0252  37  GLY C N   
1024 C CA  . GLY C 37  ? 0.7095 0.5353 0.5148 0.0429  0.0817  0.0183  37  GLY C CA  
1025 C C   . GLY C 37  ? 0.6708 0.5281 0.4970 0.0518  0.0725  0.0215  37  GLY C C   
1026 O O   . GLY C 37  ? 0.6612 0.5424 0.4998 0.0467  0.0713  0.0163  37  GLY C O   
1027 N N   . GLU C 38  ? 0.6587 0.5167 0.4853 0.0648  0.0676  0.0285  38  GLU C N   
1028 C CA  . GLU C 38  ? 0.6378 0.5153 0.4758 0.0694  0.0626  0.0302  38  GLU C CA  
1029 C C   . GLU C 38  ? 0.6276 0.5072 0.4660 0.0666  0.0645  0.0323  38  GLU C C   
1030 O O   . GLU C 38  ? 0.6176 0.4871 0.4474 0.0674  0.0668  0.0362  38  GLU C O   
1031 C CB  . GLU C 38  ? 0.6456 0.5263 0.4818 0.0773  0.0596  0.0338  38  GLU C CB  
1032 C CG  . GLU C 38  ? 0.6772 0.5553 0.5110 0.0821  0.0581  0.0326  38  GLU C CG  
1033 C CD  . GLU C 38  ? 0.7151 0.5973 0.5544 0.0788  0.0572  0.0271  38  GLU C CD  
1034 O OE1 . GLU C 38  ? 0.7491 0.6420 0.5931 0.0808  0.0554  0.0265  38  GLU C OE1 
1035 O OE2 . GLU C 38  ? 0.8019 0.6749 0.6365 0.0744  0.0595  0.0227  38  GLU C OE2 
1036 N N   . THR C 39  ? 0.6299 0.5213 0.4745 0.0666  0.0640  0.0303  39  THR C N   
1037 C CA  . THR C 39  ? 0.6198 0.5125 0.4630 0.0658  0.0660  0.0320  39  THR C CA  
1038 C C   . THR C 39  ? 0.6321 0.5208 0.4694 0.0680  0.0658  0.0341  39  THR C C   
1039 O O   . THR C 39  ? 0.5978 0.4853 0.4332 0.0701  0.0647  0.0339  39  THR C O   
1040 C CB  . THR C 39  ? 0.6294 0.5361 0.4769 0.0677  0.0672  0.0278  39  THR C CB  
1041 O OG1 . THR C 39  ? 0.6123 0.5214 0.4567 0.0778  0.0656  0.0275  39  THR C OG1 
1042 C CG2 . THR C 39  ? 0.6374 0.5581 0.4916 0.0595  0.0688  0.0215  39  THR C CG2 
1043 N N   . PRO C 40  ? 0.6280 0.5147 0.4603 0.0650  0.0684  0.0348  40  PRO C N   
1044 C CA  . PRO C 40  ? 0.6402 0.5218 0.4628 0.0609  0.0714  0.0333  40  PRO C CA  
1045 C C   . PRO C 40  ? 0.6491 0.5166 0.4615 0.0649  0.0749  0.0324  40  PRO C C   
1046 O O   . PRO C 40  ? 0.6696 0.5308 0.4730 0.0589  0.0781  0.0307  40  PRO C O   
1047 C CB  . PRO C 40  ? 0.6547 0.5329 0.4713 0.0572  0.0751  0.0326  40  PRO C CB  
1048 C CG  . PRO C 40  ? 0.6415 0.5288 0.4666 0.0585  0.0722  0.0353  40  PRO C CG  
1049 C CD  . PRO C 40  ? 0.6466 0.5347 0.4794 0.0624  0.0701  0.0356  40  PRO C CD  
1050 N N   . LEU C 41  ? 0.6556 0.5212 0.4672 0.0754  0.0750  0.0330  41  LEU C N   
1051 C CA  . LEU C 41  ? 0.6883 0.5388 0.4836 0.0868  0.0789  0.0337  41  LEU C CA  
1052 C C   . LEU C 41  ? 0.6898 0.5449 0.4898 0.0878  0.0754  0.0339  41  LEU C C   
1053 O O   . LEU C 41  ? 0.7093 0.5439 0.4908 0.0888  0.0810  0.0348  41  LEU C O   
1054 C CB  . LEU C 41  ? 0.6765 0.5390 0.4720 0.1028  0.0780  0.0334  41  LEU C CB  
1055 C CG  . LEU C 41  ? 0.7109 0.5568 0.4816 0.1229  0.0829  0.0356  41  LEU C CG  
1056 C CD1 . LEU C 41  ? 0.7413 0.5407 0.4777 0.1213  0.0950  0.0379  41  LEU C CD1 
1057 C CD2 . LEU C 41  ? 0.7312 0.6037 0.5036 0.1429  0.0808  0.0339  41  LEU C CD2 
1058 N N   . HIS C 42  ? 0.6782 0.5542 0.4976 0.0862  0.0684  0.0327  42  HIS C N   
1059 C CA  . HIS C 42  ? 0.6523 0.5321 0.4758 0.0864  0.0651  0.0323  42  HIS C CA  
1060 C C   . HIS C 42  ? 0.6812 0.5517 0.4970 0.0779  0.0685  0.0329  42  HIS C C   
1061 O O   . HIS C 42  ? 0.6903 0.5509 0.4949 0.0790  0.0718  0.0330  42  HIS C O   
1062 C CB  . HIS C 42  ? 0.6429 0.5360 0.4812 0.0824  0.0603  0.0303  42  HIS C CB  
1063 C CG  . HIS C 42  ? 0.6464 0.5553 0.4920 0.0847  0.0583  0.0254  42  HIS C CG  
1064 N ND1 . HIS C 42  ? 0.6291 0.5485 0.4804 0.0795  0.0596  0.0223  42  HIS C ND1 
1065 C CD2 . HIS C 42  ? 0.6373 0.5590 0.4858 0.0885  0.0556  0.0211  42  HIS C CD2 
1066 C CE1 . HIS C 42  ? 0.6389 0.5804 0.4969 0.0779  0.0584  0.0149  42  HIS C CE1 
1067 N NE2 . HIS C 42  ? 0.6274 0.5714 0.4839 0.0839  0.0555  0.0139  42  HIS C NE2 
1068 N N   . LEU C 43  ? 0.7061 0.5838 0.5263 0.0693  0.0683  0.0323  43  LEU C N   
1069 C CA  . LEU C 43  ? 0.6835 0.5709 0.5013 0.0602  0.0700  0.0298  43  LEU C CA  
1070 C C   . LEU C 43  ? 0.7228 0.5923 0.5207 0.0493  0.0800  0.0265  43  LEU C C   
1071 O O   . LEU C 43  ? 0.7349 0.6049 0.5259 0.0426  0.0839  0.0238  43  LEU C O   
1072 C CB  . LEU C 43  ? 0.6788 0.5851 0.5040 0.0584  0.0669  0.0296  43  LEU C CB  
1073 C CG  . LEU C 43  ? 0.6748 0.5844 0.5080 0.0692  0.0612  0.0334  43  LEU C CG  
1074 C CD1 . LEU C 43  ? 0.6894 0.6103 0.5211 0.0721  0.0599  0.0351  43  LEU C CD1 
1075 C CD2 . LEU C 43  ? 0.6743 0.5893 0.5094 0.0756  0.0586  0.0334  43  LEU C CD2 
1076 N N   . ALA C 44  ? 0.7215 0.5705 0.5059 0.0476  0.0860  0.0265  44  ALA C N   
1077 C CA  . ALA C 44  ? 0.7676 0.5848 0.5220 0.0363  0.0996  0.0230  44  ALA C CA  
1078 C C   . ALA C 44  ? 0.7837 0.5713 0.5174 0.0460  0.1055  0.0265  44  ALA C C   
1079 O O   . ALA C 44  ? 0.8077 0.5725 0.5168 0.0323  0.1175  0.0229  44  ALA C O   
1080 C CB  . ALA C 44  ? 0.7873 0.5846 0.5283 0.0372  0.1048  0.0230  44  ALA C CB  
1081 N N   . ALA C 45  ? 0.7749 0.5644 0.5153 0.0677  0.0987  0.0322  45  ALA C N   
1082 C CA  . ALA C 45  ? 0.7916 0.5612 0.5132 0.0837  0.1019  0.0363  45  ALA C CA  
1083 C C   . ALA C 45  ? 0.8060 0.5858 0.5337 0.0752  0.1007  0.0347  45  ALA C C   
1084 O O   . ALA C 45  ? 0.8445 0.5931 0.5425 0.0717  0.1123  0.0351  45  ALA C O   
1085 C CB  . ALA C 45  ? 0.7907 0.5818 0.5270 0.1059  0.0920  0.0391  45  ALA C CB  
1086 N N   . MET C 46  ? 0.7630 0.5806 0.5231 0.0721  0.0891  0.0328  46  MET C N   
1087 C CA  . MET C 46  ? 0.7753 0.6101 0.5449 0.0667  0.0864  0.0308  46  MET C CA  
1088 C C   . MET C 46  ? 0.8226 0.6523 0.5772 0.0456  0.0973  0.0254  46  MET C C   
1089 O O   . MET C 46  ? 0.8186 0.6458 0.5646 0.0415  0.1017  0.0242  46  MET C O   
1090 C CB  . MET C 46  ? 0.7520 0.6206 0.5502 0.0678  0.0753  0.0297  46  MET C CB  
1091 C CG  . MET C 46  ? 0.7807 0.6674 0.5855 0.0660  0.0732  0.0276  46  MET C CG  
1092 S SD  . MET C 46  ? 0.7838 0.6941 0.6091 0.0759  0.0627  0.0282  46  MET C SD  
1093 C CE  . MET C 46  ? 0.7940 0.7249 0.6232 0.0690  0.0630  0.0262  46  MET C CE  
1094 N N   . ASN C 47  ? 0.8128 0.6487 0.5669 0.0305  0.1011  0.0205  47  ASN C N   
1095 C CA  . ASN C 47  ? 0.8200 0.6713 0.5671 0.0050  0.1100  0.0108  47  ASN C CA  
1096 C C   . ASN C 47  ? 0.8726 0.6750 0.5791 -0.0123 0.1293  0.0071  47  ASN C C   
1097 O O   . ASN C 47  ? 0.9181 0.7294 0.6132 -0.0405 0.1405  -0.0042 47  ASN C O   
1098 C CB  . ASN C 47  ? 0.7975 0.6930 0.5665 -0.0013 0.1028  0.0055  47  ASN C CB  
1099 C CG  . ASN C 47  ? 0.7807 0.7184 0.5770 0.0140  0.0891  0.0079  47  ASN C CG  
1100 O OD1 . ASN C 47  ? 0.8001 0.7419 0.6001 0.0214  0.0867  0.0097  47  ASN C OD1 
1101 N ND2 . ASN C 47  ? 0.7690 0.7338 0.5794 0.0205  0.0814  0.0081  47  ASN C ND2 
1102 N N   . GLY C 48  ? 0.8947 0.6479 0.5763 0.0045  0.1344  0.0152  48  GLY C N   
1103 C CA  . GLY C 48  ? 0.9605 0.6499 0.5904 -0.0045 0.1558  0.0144  48  GLY C CA  
1104 C C   . GLY C 48  ? 1.0136 0.6861 0.6263 -0.0244 0.1664  0.0068  48  GLY C C   
1105 O O   . GLY C 48  ? 1.0651 0.6978 0.6375 -0.0499 0.1873  -0.0010 48  GLY C O   
1106 N N   . HIS C 49  ? 0.9996 0.6987 0.6385 -0.0155 0.1542  0.0081  49  HIS C N   
1107 C CA  . HIS C 49  ? 1.0156 0.7040 0.6411 -0.0331 0.1625  0.0006  49  HIS C CA  
1108 C C   . HIS C 49  ? 1.0588 0.6940 0.6544 -0.0105 0.1687  0.0088  49  HIS C C   
1109 O O   . HIS C 49  ? 1.0205 0.6778 0.6396 0.0057  0.1566  0.0129  49  HIS C O   
1110 C CB  . HIS C 49  ? 0.9696 0.7234 0.6390 -0.0381 0.1466  -0.0038 49  HIS C CB  
1111 C CG  . HIS C 49  ? 0.9764 0.7859 0.6691 -0.0552 0.1417  -0.0125 49  HIS C CG  
1112 N ND1 . HIS C 49  ? 1.0359 0.8460 0.7081 -0.0870 0.1570  -0.0256 49  HIS C ND1 
1113 C CD2 . HIS C 49  ? 0.9249 0.7925 0.6559 -0.0443 0.1249  -0.0109 49  HIS C CD2 
1114 C CE1 . HIS C 49  ? 1.0067 0.8829 0.7084 -0.0931 0.1478  -0.0321 49  HIS C CE1 
1115 N NE2 . HIS C 49  ? 0.9637 0.8722 0.6993 -0.0647 0.1282  -0.0223 49  HIS C NE2 
1116 N N   . LEU C 50  ? 1.1023 0.6682 0.6430 -0.0099 0.1890  0.0103  50  LEU C N   
1117 C CA  . LEU C 50  ? 1.1769 0.6856 0.6776 0.0218  0.1971  0.0204  50  LEU C CA  
1118 C C   . LEU C 50  ? 1.1946 0.6948 0.6898 0.0217  0.1993  0.0175  50  LEU C C   
1119 O O   . LEU C 50  ? 1.1684 0.6702 0.6670 0.0547  0.1917  0.0261  50  LEU C O   
1120 C CB  . LEU C 50  ? 1.2735 0.6992 0.7042 0.0175  0.2237  0.0212  50  LEU C CB  
1121 C CG  . LEU C 50  ? 1.3521 0.7045 0.7237 0.0500  0.2384  0.0302  50  LEU C CG  
1122 C CD1 . LEU C 50  ? 1.3248 0.7079 0.7177 0.0994  0.2201  0.0434  50  LEU C CD1 
1123 C CD2 . LEU C 50  ? 1.4602 0.7171 0.7512 0.0426  0.2693  0.0308  50  LEU C CD2 
1124 N N   . GLU C 51  ? 1.2292 0.7225 0.7132 -0.0146 0.2106  0.0047  51  GLU C N   
1125 C CA  . GLU C 51  ? 1.2658 0.7474 0.7399 -0.0190 0.2149  0.0001  51  GLU C CA  
1126 C C   . GLU C 51  ? 1.1519 0.7040 0.6860 -0.0016 0.1895  0.0049  51  GLU C C   
1127 O O   . GLU C 51  ? 1.1148 0.6568 0.6441 0.0208  0.1874  0.0102  51  GLU C O   
1128 C CB  . GLU C 51  ? 1.3545 0.8301 0.8110 -0.0665 0.2303  -0.0178 51  GLU C CB  
1129 C CG  . GLU C 51  ? 1.5041 0.9661 0.9470 -0.0739 0.2361  -0.0242 51  GLU C CG  
1130 C CD  . GLU C 51  ? 1.6473 1.0187 1.0252 -0.0539 0.2564  -0.0186 51  GLU C CD  
1131 O OE1 . GLU C 51  ? 1.8111 1.1076 1.1304 -0.0537 0.2782  -0.0168 51  GLU C OE1 
1132 O OE2 . GLU C 51  ? 1.6927 1.0661 1.0746 -0.0367 0.2516  -0.0158 51  GLU C OE2 
1133 N N   . ILE C 52  ? 1.0579 0.6756 0.6421 -0.0095 0.1723  0.0035  52  ILE C N   
1134 C CA  . ILE C 52  ? 0.9841 0.6613 0.6186 0.0034  0.1511  0.0076  52  ILE C CA  
1135 C C   . ILE C 52  ? 0.9457 0.6236 0.5900 0.0382  0.1420  0.0193  52  ILE C C   
1136 O O   . ILE C 52  ? 0.9480 0.6446 0.6089 0.0517  0.1342  0.0223  52  ILE C O   
1137 C CB  . ILE C 52  ? 0.9351 0.6712 0.6083 -0.0109 0.1388  0.0034  52  ILE C CB  
1138 C CG1 . ILE C 52  ? 0.9446 0.7013 0.6146 -0.0420 0.1448  -0.0103 52  ILE C CG1 
1139 C CG2 . ILE C 52  ? 0.8745 0.6534 0.5883 0.0087  0.1200  0.0110  52  ILE C CG2 
1140 C CD1 . ILE C 52  ? 0.9014 0.7180 0.6000 -0.0542 0.1358  -0.0164 52  ILE C CD1 
1141 N N   . VAL C 53  ? 0.9851 0.6443 0.6157 0.0513  0.1444  0.0243  53  VAL C N   
1142 C CA  . VAL C 53  ? 0.9757 0.6425 0.6122 0.0848  0.1365  0.0330  53  VAL C CA  
1143 C C   . VAL C 53  ? 1.0210 0.6605 0.6298 0.1073  0.1435  0.0362  53  VAL C C   
1144 O O   . VAL C 53  ? 0.9905 0.6674 0.6242 0.1258  0.1323  0.0387  53  VAL C O   
1145 C CB  . VAL C 53  ? 0.9744 0.6206 0.5917 0.0951  0.1406  0.0371  53  VAL C CB  
1146 C CG1 . VAL C 53  ? 0.9889 0.6358 0.5964 0.1328  0.1370  0.0445  53  VAL C CG1 
1147 C CG2 . VAL C 53  ? 0.9290 0.6160 0.5825 0.0811  0.1293  0.0350  53  VAL C CG2 
1148 N N   . GLU C 54  ? 1.0934 0.6695 0.6494 0.1051  0.1630  0.0351  54  GLU C N   
1149 C CA  . GLU C 54  ? 1.1640 0.7038 0.6827 0.1308  0.1728  0.0386  54  GLU C CA  
1150 C C   . GLU C 54  ? 1.1131 0.6872 0.6607 0.1232  0.1652  0.0344  54  GLU C C   
1151 O O   . GLU C 54  ? 1.0712 0.6692 0.6282 0.1500  0.1587  0.0381  54  GLU C O   
1152 C CB  . GLU C 54  ? 1.2859 0.7376 0.7335 0.1250  0.1990  0.0372  54  GLU C CB  
1153 C CG  . GLU C 54  ? 1.3807 0.7838 0.7803 0.1550  0.2099  0.0462  54  GLU C CG  
1154 C CD  . GLU C 54  ? 1.4924 0.8095 0.8268 0.1339  0.2367  0.0433  54  GLU C CD  
1155 O OE1 . GLU C 54  ? 1.5466 0.8550 0.8817 0.0896  0.2450  0.0316  54  GLU C OE1 
1156 O OE2 . GLU C 54  ? 1.5885 0.8494 0.8692 0.1610  0.2501  0.0518  54  GLU C OE2 
1157 N N   . VAL C 55  ? 1.1115 0.6931 0.6722 0.0883  0.1661  0.0262  55  VAL C N   
1158 C CA  . VAL C 55  ? 1.0867 0.7023 0.6746 0.0778  0.1588  0.0220  55  VAL C CA  
1159 C C   . VAL C 55  ? 1.0131 0.6898 0.6493 0.0941  0.1399  0.0270  55  VAL C C   
1160 O O   . VAL C 55  ? 1.0028 0.6933 0.6444 0.1073  0.1377  0.0280  55  VAL C O   
1161 C CB  . VAL C 55  ? 1.1110 0.7452 0.7140 0.0402  0.1583  0.0124  55  VAL C CB  
1162 C CG1 . VAL C 55  ? 1.1219 0.8017 0.7587 0.0345  0.1471  0.0104  55  VAL C CG1 
1163 C CG2 . VAL C 55  ? 1.1909 0.7700 0.7450 0.0159  0.1796  0.0028  55  VAL C CG2 
1164 N N   . LEU C 56  ? 0.9299 0.6408 0.5976 0.0905  0.1284  0.0287  56  LEU C N   
1165 C CA  . LEU C 56  ? 0.8548 0.6183 0.5642 0.0980  0.1133  0.0310  56  LEU C CA  
1166 C C   . LEU C 56  ? 0.8530 0.6266 0.5575 0.1273  0.1125  0.0340  56  LEU C C   
1167 O O   . LEU C 56  ? 0.8083 0.6151 0.5324 0.1317  0.1073  0.0327  56  LEU C O   
1168 C CB  . LEU C 56  ? 0.8194 0.6043 0.5519 0.0897  0.1048  0.0316  56  LEU C CB  
1169 C CG  . LEU C 56  ? 0.8070 0.6047 0.5538 0.0662  0.1018  0.0283  56  LEU C CG  
1170 C CD1 . LEU C 56  ? 0.8052 0.6170 0.5660 0.0630  0.0959  0.0291  56  LEU C CD1 
1171 C CD2 . LEU C 56  ? 0.7948 0.6207 0.5639 0.0616  0.0951  0.0282  56  LEU C CD2 
1172 N N   . LEU C 57  ? 0.9017 0.6495 0.5772 0.1478  0.1185  0.0372  57  LEU C N   
1173 C CA  . LEU C 57  ? 0.9357 0.7036 0.6042 0.1819  0.1169  0.0394  57  LEU C CA  
1174 C C   . LEU C 57  ? 0.9746 0.7335 0.6238 0.1971  0.1238  0.0390  57  LEU C C   
1175 O O   . LEU C 57  ? 0.9527 0.7602 0.6194 0.2148  0.1176  0.0371  57  LEU C O   
1176 C CB  . LEU C 57  ? 0.9677 0.7019 0.6001 0.2040  0.1237  0.0444  57  LEU C CB  
1177 C CG  . LEU C 57  ? 0.9309 0.6896 0.5872 0.1962  0.1144  0.0443  57  LEU C CG  
1178 C CD1 . LEU C 57  ? 1.0049 0.7132 0.6181 0.2094  0.1249  0.0497  57  LEU C CD1 
1179 C CD2 . LEU C 57  ? 0.8902 0.7169 0.5802 0.2102  0.1013  0.0410  57  LEU C CD2 
1180 N N   . LYS C 58  ? 1.0286 0.7332 0.6448 0.1872  0.1366  0.0388  58  LYS C N   
1181 C CA  . LYS C 58  ? 1.1120 0.7997 0.7044 0.2010  0.1450  0.0380  58  LYS C CA  
1182 C C   . LYS C 58  ? 1.0719 0.8086 0.7069 0.1827  0.1354  0.0335  58  LYS C C   
1183 O O   . LYS C 58  ? 1.1004 0.8455 0.7281 0.1976  0.1384  0.0325  58  LYS C O   
1184 C CB  . LYS C 58  ? 1.2055 0.8141 0.7447 0.1907  0.1639  0.0370  58  LYS C CB  
1185 C CG  . LYS C 58  ? 1.3018 0.8855 0.8112 0.2047  0.1743  0.0357  58  LYS C CG  
1186 C CD  . LYS C 58  ? 1.4345 0.9268 0.8747 0.2026  0.1978  0.0345  58  LYS C CD  
1187 C CE  . LYS C 58  ? 1.4909 0.9580 0.8971 0.2258  0.2082  0.0342  58  LYS C CE  
1188 N NZ  . LYS C 58  ? 1.6068 0.9736 0.9370 0.2214  0.2345  0.0319  58  LYS C NZ  
1189 N N   . THR C 59  ? 1.0051 0.7710 0.6788 0.1543  0.1254  0.0314  59  THR C N   
1190 C CA  . THR C 59  ? 0.9809 0.7809 0.6859 0.1359  0.1190  0.0285  59  THR C CA  
1191 C C   . THR C 59  ? 0.9123 0.7678 0.6569 0.1341  0.1075  0.0277  59  THR C C   
1192 O O   . THR C 59  ? 0.8899 0.7633 0.6579 0.1137  0.1026  0.0267  59  THR C O   
1193 C CB  . THR C 59  ? 1.0046 0.7881 0.7122 0.1066  0.1196  0.0263  59  THR C CB  
1194 O OG1 . THR C 59  ? 1.0885 0.8190 0.7554 0.1038  0.1326  0.0244  59  THR C OG1 
1195 C CG2 . THR C 59  ? 1.0136 0.8165 0.7362 0.0936  0.1172  0.0242  59  THR C CG2 
1196 N N   . GLY C 60  ? 0.8714 0.7514 0.6189 0.1543  0.1046  0.0274  60  GLY C N   
1197 C CA  . GLY C 60  ? 0.8413 0.7792 0.6215 0.1515  0.0967  0.0226  60  GLY C CA  
1198 C C   . GLY C 60  ? 0.7847 0.7328 0.5839 0.1377  0.0899  0.0221  60  GLY C C   
1199 O O   . GLY C 60  ? 0.7767 0.7646 0.5999 0.1269  0.0858  0.0165  60  GLY C O   
1200 N N   . ALA C 61  ? 0.7818 0.6953 0.5687 0.1361  0.0902  0.0264  61  ALA C N   
1201 C CA  . ALA C 61  ? 0.7491 0.6712 0.5526 0.1245  0.0839  0.0259  61  ALA C CA  
1202 C C   . ALA C 61  ? 0.7375 0.6987 0.5491 0.1395  0.0798  0.0214  61  ALA C C   
1203 O O   . ALA C 61  ? 0.7536 0.7165 0.5459 0.1661  0.0822  0.0225  61  ALA C O   
1204 C CB  . ALA C 61  ? 0.7711 0.6537 0.5586 0.1204  0.0861  0.0303  61  ALA C CB  
1205 N N   . ASP C 62  ? 0.7091 0.7015 0.5444 0.1242  0.0749  0.0155  62  ASP C N   
1206 C CA  . ASP C 62  ? 0.7199 0.7574 0.5648 0.1333  0.0707  0.0080  62  ASP C CA  
1207 C C   . ASP C 62  ? 0.7315 0.7475 0.5627 0.1469  0.0685  0.0129  62  ASP C C   
1208 O O   . ASP C 62  ? 0.7239 0.7156 0.5591 0.1316  0.0670  0.0155  62  ASP C O   
1209 C CB  . ASP C 62  ? 0.7337 0.8012 0.6015 0.1070  0.0694  -0.0016 62  ASP C CB  
1210 C CG  . ASP C 62  ? 0.7773 0.9023 0.6562 0.1111  0.0660  -0.0136 62  ASP C CG  
1211 O OD1 . ASP C 62  ? 0.7780 0.9204 0.6470 0.1398  0.0627  -0.0125 62  ASP C OD1 
1212 O OD2 . ASP C 62  ? 0.8277 0.9783 0.7212 0.0856  0.0679  -0.0247 62  ASP C OD2 
1213 N N   . VAL C 63  ? 0.7634 0.7888 0.5762 0.1772  0.0691  0.0143  63  VAL C N   
1214 C CA  . VAL C 63  ? 0.7782 0.7745 0.5683 0.1943  0.0698  0.0207  63  VAL C CA  
1215 C C   . VAL C 63  ? 0.7381 0.7652 0.5481 0.1846  0.0625  0.0145  63  VAL C C   
1216 O O   . VAL C 63  ? 0.7521 0.7506 0.5504 0.1871  0.0627  0.0196  63  VAL C O   
1217 C CB  . VAL C 63  ? 0.8233 0.8193 0.5805 0.2350  0.0738  0.0245  63  VAL C CB  
1218 C CG1 . VAL C 63  ? 0.8024 0.8768 0.5750 0.2533  0.0675  0.0145  63  VAL C CG1 
1219 C CG2 . VAL C 63  ? 0.8484 0.8030 0.5750 0.2509  0.0774  0.0323  63  VAL C CG2 
1220 N N   . ASN C 64  ? 0.7208 0.8035 0.5572 0.1720  0.0580  0.0027  64  ASN C N   
1221 C CA  . ASN C 64  ? 0.7346 0.8543 0.5873 0.1619  0.0526  -0.0071 64  ASN C CA  
1222 C C   . ASN C 64  ? 0.7111 0.8268 0.5838 0.1245  0.0539  -0.0135 64  ASN C C   
1223 O O   . ASN C 64  ? 0.7350 0.8866 0.6211 0.1088  0.0524  -0.0261 64  ASN C O   
1224 C CB  . ASN C 64  ? 0.7682 0.9620 0.6263 0.1809  0.0487  -0.0187 64  ASN C CB  
1225 C CG  . ASN C 64  ? 0.8066 0.9966 0.6357 0.2245  0.0481  -0.0105 64  ASN C CG  
1226 O OD1 . ASN C 64  ? 0.8700 1.0202 0.6815 0.2337  0.0483  -0.0019 64  ASN C OD1 
1227 N ND2 . ASN C 64  ? 0.8351 1.0643 0.6549 0.2534  0.0486  -0.0127 64  ASN C ND2 
1228 N N   . ALA C 65  ? 0.7046 0.7750 0.5743 0.1115  0.0578  -0.0055 65  ALA C N   
1229 C CA  . ALA C 65  ? 0.6844 0.7342 0.5618 0.0830  0.0606  -0.0074 65  ALA C CA  
1230 C C   . ALA C 65  ? 0.6946 0.7357 0.5724 0.0768  0.0581  -0.0096 65  ALA C C   
1231 O O   . ALA C 65  ? 0.6880 0.7120 0.5576 0.0917  0.0548  -0.0026 65  ALA C O   
1232 C CB  . ALA C 65  ? 0.6843 0.6893 0.5538 0.0795  0.0634  0.0035  65  ALA C CB  
1233 N N   . SER C 66  ? 0.6938 0.7415 0.5767 0.0537  0.0617  -0.0194 66  SER C N   
1234 C CA  . SER C 66  ? 0.7228 0.7659 0.6041 0.0438  0.0615  -0.0255 66  SER C CA  
1235 C C   . SER C 66  ? 0.7277 0.7181 0.5971 0.0304  0.0673  -0.0196 66  SER C C   
1236 O O   . SER C 66  ? 0.7203 0.6982 0.5843 0.0139  0.0751  -0.0222 66  SER C O   
1237 C CB  . SER C 66  ? 0.7347 0.8271 0.6244 0.0265  0.0642  -0.0443 66  SER C CB  
1238 O OG  . SER C 66  ? 0.7563 0.8528 0.6441 0.0204  0.0630  -0.0520 66  SER C OG  
1239 N N   . ASP C 67  ? 0.7123 0.6740 0.5748 0.0397  0.0644  -0.0115 67  ASP C N   
1240 C CA  . ASP C 67  ? 0.7250 0.6412 0.5724 0.0347  0.0694  -0.0055 67  ASP C CA  
1241 C C   . ASP C 67  ? 0.7552 0.6590 0.5908 0.0169  0.0768  -0.0166 67  ASP C C   
1242 O O   . ASP C 67  ? 0.7634 0.7016 0.6073 0.0053  0.0771  -0.0302 67  ASP C O   
1243 C CB  . ASP C 67  ? 0.7206 0.6215 0.5659 0.0520  0.0638  0.0055  67  ASP C CB  
1244 C CG  . ASP C 67  ? 0.7263 0.6371 0.5739 0.0589  0.0592  0.0027  67  ASP C CG  
1245 O OD1 . ASP C 67  ? 0.7530 0.6763 0.6011 0.0497  0.0605  -0.0078 67  ASP C OD1 
1246 O OD2 . ASP C 67  ? 0.6994 0.6069 0.5472 0.0712  0.0553  0.0100  67  ASP C OD2 
1247 N N   . PHE C 68  ? 0.7881 0.6456 0.6019 0.0161  0.0832  -0.0119 68  PHE C N   
1248 C CA  . PHE C 68  ? 0.8531 0.6798 0.6435 -0.0022 0.0950  -0.0220 68  PHE C CA  
1249 C C   . PHE C 68  ? 0.8518 0.7005 0.6492 -0.0045 0.0907  -0.0321 68  PHE C C   
1250 O O   . PHE C 68  ? 0.8735 0.7124 0.6565 -0.0268 0.1006  -0.0463 68  PHE C O   
1251 C CB  . PHE C 68  ? 0.9040 0.6698 0.6616 0.0072  0.1034  -0.0115 68  PHE C CB  
1252 C CG  . PHE C 68  ? 0.9398 0.6817 0.6837 0.0075  0.1101  -0.0035 68  PHE C CG  
1253 C CD1 . PHE C 68  ? 0.9307 0.6984 0.6886 -0.0084 0.1117  -0.0088 68  PHE C CD1 
1254 C CD2 . PHE C 68  ? 0.9966 0.6940 0.7119 0.0261  0.1148  0.0092  68  PHE C CD2 
1255 C CE1 . PHE C 68  ? 0.9728 0.7187 0.7173 -0.0081 0.1181  -0.0013 68  PHE C CE1 
1256 C CE2 . PHE C 68  ? 1.0429 0.7204 0.7435 0.0288  0.1206  0.0170  68  PHE C CE2 
1257 C CZ  . PHE C 68  ? 1.0023 0.7020 0.7178 0.0103  0.1224  0.0119  68  PHE C CZ  
1258 N N   . HIS C 69  ? 0.8159 0.6933 0.6321 0.0152  0.0781  -0.0265 69  HIS C N   
1259 C CA  . HIS C 69  ? 0.8091 0.7107 0.6316 0.0166  0.0731  -0.0350 69  HIS C CA  
1260 C C   . HIS C 69  ? 0.7776 0.7398 0.6218 0.0176  0.0658  -0.0432 69  HIS C C   
1261 O O   . HIS C 69  ? 0.7853 0.7753 0.6350 0.0236  0.0601  -0.0492 69  HIS C O   
1262 C CB  . HIS C 69  ? 0.8301 0.7189 0.6518 0.0388  0.0663  -0.0233 69  HIS C CB  
1263 C CG  . HIS C 69  ? 0.8335 0.7362 0.6553 0.0400  0.0633  -0.0312 69  HIS C CG  
1264 N ND1 . HIS C 69  ? 0.8166 0.7512 0.6516 0.0554  0.0539  -0.0284 69  HIS C ND1 
1265 C CD2 . HIS C 69  ? 0.8684 0.7545 0.6749 0.0277  0.0695  -0.0420 69  HIS C CD2 
1266 C CE1 . HIS C 69  ? 0.8387 0.7806 0.6696 0.0539  0.0530  -0.0366 69  HIS C CE1 
1267 N NE2 . HIS C 69  ? 0.8709 0.7844 0.6854 0.0360  0.0623  -0.0458 69  HIS C NE2 
1268 N N   . GLY C 70  ? 0.7331 0.7166 0.5867 0.0150  0.0661  -0.0433 70  GLY C N   
1269 C CA  . GLY C 70  ? 0.6911 0.7349 0.5615 0.0224  0.0598  -0.0502 70  GLY C CA  
1270 C C   . GLY C 70  ? 0.6682 0.7167 0.5419 0.0530  0.0508  -0.0366 70  GLY C C   
1271 O O   . GLY C 70  ? 0.6943 0.7864 0.5739 0.0676  0.0457  -0.0402 70  GLY C O   
1272 N N   . ASP C 71  ? 0.6598 0.6653 0.5260 0.0629  0.0503  -0.0220 71  ASP C N   
1273 C CA  . ASP C 71  ? 0.6559 0.6560 0.5185 0.0860  0.0460  -0.0100 71  ASP C CA  
1274 C C   . ASP C 71  ? 0.6675 0.6677 0.5306 0.0915  0.0475  -0.0044 71  ASP C C   
1275 O O   . ASP C 71  ? 0.6998 0.6858 0.5651 0.0786  0.0514  -0.0036 71  ASP C O   
1276 C CB  . ASP C 71  ? 0.6643 0.6283 0.5191 0.0895  0.0463  -0.0004 71  ASP C CB  
1277 C CG  . ASP C 71  ? 0.6961 0.6638 0.5486 0.0901  0.0442  -0.0053 71  ASP C CG  
1278 O OD1 . ASP C 71  ? 0.7002 0.6909 0.5513 0.1024  0.0406  -0.0075 71  ASP C OD1 
1279 O OD2 . ASP C 71  ? 0.6987 0.6460 0.5474 0.0802  0.0469  -0.0074 71  ASP C OD2 
1280 N N   . THR C 72  ? 0.6665 0.6789 0.5228 0.1122  0.0457  -0.0006 72  THR C N   
1281 C CA  . THR C 72  ? 0.6716 0.6787 0.5207 0.1234  0.0483  0.0054  72  THR C CA  
1282 C C   . THR C 72  ? 0.6729 0.6355 0.5043 0.1305  0.0520  0.0172  72  THR C C   
1283 O O   . THR C 72  ? 0.6805 0.6269 0.5056 0.1310  0.0519  0.0201  72  THR C O   
1284 C CB  . THR C 72  ? 0.6991 0.7478 0.5442 0.1453  0.0460  0.0007  72  THR C CB  
1285 O OG1 . THR C 72  ? 0.6910 0.7309 0.5176 0.1675  0.0451  0.0061  72  THR C OG1 
1286 C CG2 . THR C 72  ? 0.6848 0.7902 0.5489 0.1334  0.0428  -0.0152 72  THR C CG2 
1287 N N   . PRO C 73  ? 0.6845 0.6270 0.5057 0.1333  0.0568  0.0226  73  PRO C N   
1288 C CA  . PRO C 73  ? 0.7052 0.6063 0.5047 0.1356  0.0634  0.0305  73  PRO C CA  
1289 C C   . PRO C 73  ? 0.7453 0.6315 0.5202 0.1540  0.0665  0.0343  73  PRO C C   
1290 O O   . PRO C 73  ? 0.7540 0.6079 0.5129 0.1481  0.0726  0.0384  73  PRO C O   
1291 C CB  . PRO C 73  ? 0.7143 0.6026 0.5024 0.1397  0.0688  0.0328  73  PRO C CB  
1292 C CG  . PRO C 73  ? 0.6912 0.6120 0.5042 0.1302  0.0640  0.0271  73  PRO C CG  
1293 C CD  . PRO C 73  ? 0.6755 0.6335 0.5046 0.1305  0.0577  0.0198  73  PRO C CD  
1294 N N   . LEU C 74  ? 0.7811 0.6934 0.5510 0.1761  0.0634  0.0324  74  LEU C N   
1295 C CA  . LEU C 74  ? 0.8058 0.7035 0.5459 0.2004  0.0669  0.0373  74  LEU C CA  
1296 C C   . LEU C 74  ? 0.7922 0.6950 0.5419 0.1910  0.0628  0.0354  74  LEU C C   
1297 O O   . LEU C 74  ? 0.8044 0.6710 0.5282 0.1955  0.0699  0.0416  74  LEU C O   
1298 C CB  . LEU C 74  ? 0.8324 0.7703 0.5661 0.2308  0.0631  0.0345  74  LEU C CB  
1299 C CG  . LEU C 74  ? 0.8838 0.8056 0.5781 0.2651  0.0676  0.0413  74  LEU C CG  
1300 C CD1 . LEU C 74  ? 0.9289 0.7731 0.5750 0.2728  0.0836  0.0530  74  LEU C CD1 
1301 C CD2 . LEU C 74  ? 0.8905 0.8670 0.5806 0.2993  0.0622  0.0371  74  LEU C CD2 
1302 N N   . HIS C 75  ? 0.7498 0.6901 0.5317 0.1760  0.0540  0.0268  75  HIS C N   
1303 C CA  . HIS C 75  ? 0.7339 0.6763 0.5253 0.1653  0.0507  0.0242  75  HIS C CA  
1304 C C   . HIS C 75  ? 0.7391 0.6411 0.5214 0.1526  0.0570  0.0306  75  HIS C C   
1305 O O   . HIS C 75  ? 0.7653 0.6516 0.5326 0.1568  0.0602  0.0338  75  HIS C O   
1306 C CB  . HIS C 75  ? 0.7200 0.6917 0.5398 0.1462  0.0445  0.0140  75  HIS C CB  
1307 C CG  . HIS C 75  ? 0.7120 0.7326 0.5415 0.1515  0.0391  0.0029  75  HIS C CG  
1308 N ND1 . HIS C 75  ? 0.7016 0.7547 0.5421 0.1487  0.0381  -0.0043 75  HIS C ND1 
1309 C CD2 . HIS C 75  ? 0.7062 0.7551 0.5366 0.1571  0.0347  -0.0043 75  HIS C CD2 
1310 C CE1 . HIS C 75  ? 0.7224 0.8266 0.5711 0.1508  0.0336  -0.0169 75  HIS C CE1 
1311 N NE2 . HIS C 75  ? 0.7005 0.8027 0.5433 0.1559  0.0311  -0.0173 75  HIS C NE2 
1312 N N   . LEU C 76  ? 0.7173 0.6084 0.5082 0.1368  0.0591  0.0314  76  LEU C N   
1313 C CA  . LEU C 76  ? 0.7124 0.5830 0.5011 0.1216  0.0637  0.0337  76  LEU C CA  
1314 C C   . LEU C 76  ? 0.7537 0.5891 0.5103 0.1244  0.0751  0.0387  76  LEU C C   
1315 O O   . LEU C 76  ? 0.7948 0.6203 0.5436 0.1165  0.0795  0.0389  76  LEU C O   
1316 C CB  . LEU C 76  ? 0.6845 0.5585 0.4872 0.1079  0.0630  0.0326  76  LEU C CB  
1317 C CG  . LEU C 76  ? 0.6749 0.5699 0.4992 0.1033  0.0561  0.0284  76  LEU C CG  
1318 C CD1 . LEU C 76  ? 0.6813 0.5734 0.5121 0.0927  0.0569  0.0294  76  LEU C CD1 
1319 C CD2 . LEU C 76  ? 0.6647 0.5688 0.4955 0.1034  0.0521  0.0250  76  LEU C CD2 
1320 N N   . ALA C 77  ? 0.7675 0.5818 0.5027 0.1340  0.0815  0.0419  77  ALA C N   
1321 C CA  . ALA C 77  ? 0.8513 0.6169 0.5447 0.1350  0.0969  0.0464  77  ALA C CA  
1322 C C   . ALA C 77  ? 0.9039 0.6533 0.5723 0.1498  0.1012  0.0503  77  ALA C C   
1323 O O   . ALA C 77  ? 0.9157 0.6291 0.5563 0.1382  0.1142  0.0516  77  ALA C O   
1324 C CB  . ALA C 77  ? 0.8793 0.6230 0.5500 0.1494  0.1030  0.0495  77  ALA C CB  
1325 N N   . ALA C 78  ? 0.8969 0.6751 0.5737 0.1727  0.0914  0.0507  78  ALA C N   
1326 C CA  . ALA C 78  ? 0.9120 0.6829 0.5650 0.1934  0.0933  0.0545  78  ALA C CA  
1327 C C   . ALA C 78  ? 0.8946 0.6731 0.5617 0.1758  0.0915  0.0517  78  ALA C C   
1328 O O   . ALA C 78  ? 0.9284 0.6762 0.5640 0.1802  0.1013  0.0561  78  ALA C O   
1329 C CB  . ALA C 78  ? 0.9055 0.7231 0.5720 0.2187  0.0811  0.0518  78  ALA C CB  
1330 N N   . MET C 79  ? 0.8420 0.6566 0.5501 0.1584  0.0808  0.0450  79  MET C N   
1331 C CA  . MET C 79  ? 0.8399 0.6665 0.5632 0.1441  0.0783  0.0417  79  MET C CA  
1332 C C   . MET C 79  ? 0.8611 0.6630 0.5713 0.1228  0.0903  0.0421  79  MET C C   
1333 O O   . MET C 79  ? 0.8458 0.6435 0.5476 0.1166  0.0951  0.0415  79  MET C O   
1334 C CB  . MET C 79  ? 0.8123 0.6752 0.5738 0.1351  0.0663  0.0352  79  MET C CB  
1335 C CG  . MET C 79  ? 0.8220 0.6956 0.5957 0.1248  0.0643  0.0321  79  MET C CG  
1336 S SD  . MET C 79  ? 0.8775 0.7798 0.6778 0.1253  0.0529  0.0250  79  MET C SD  
1337 C CE  . MET C 79  ? 0.8788 0.7850 0.6811 0.1214  0.0534  0.0234  79  MET C CE  
1338 N N   . ALA C 80  ? 0.8622 0.6521 0.5700 0.1106  0.0956  0.0414  80  ALA C N   
1339 C CA  . ALA C 80  ? 0.8930 0.6733 0.5933 0.0847  0.1064  0.0374  80  ALA C CA  
1340 C C   . ALA C 80  ? 0.9624 0.6914 0.6144 0.0791  0.1260  0.0399  80  ALA C C   
1341 O O   . ALA C 80  ? 1.0227 0.7497 0.6663 0.0552  0.1364  0.0343  80  ALA C O   
1342 C CB  . ALA C 80  ? 0.8657 0.6534 0.5784 0.0739  0.1051  0.0346  80  ALA C CB  
1343 N N   . GLY C 81  ? 1.0068 0.6963 0.6245 0.1010  0.1322  0.0473  81  GLY C N   
1344 C CA  . GLY C 81  ? 1.0857 0.7104 0.6439 0.1020  0.1539  0.0520  81  GLY C CA  
1345 C C   . GLY C 81  ? 1.1530 0.7288 0.6758 0.0920  0.1702  0.0516  81  GLY C C   
1346 O O   . GLY C 81  ? 1.2169 0.7347 0.6890 0.0758  0.1934  0.0510  81  GLY C O   
1347 N N   . HIS C 82  ? 1.1272 0.7212 0.6712 0.0998  0.1605  0.0514  82  HIS C N   
1348 C CA  . HIS C 82  ? 1.1542 0.7056 0.6677 0.0914  0.1744  0.0502  82  HIS C CA  
1349 C C   . HIS C 82  ? 1.1832 0.6914 0.6542 0.1306  0.1801  0.0606  82  HIS C C   
1350 O O   . HIS C 82  ? 1.1165 0.6583 0.6127 0.1526  0.1657  0.0626  82  HIS C O   
1351 C CB  . HIS C 82  ? 1.0892 0.6896 0.6507 0.0756  0.1611  0.0431  82  HIS C CB  
1352 C CG  . HIS C 82  ? 1.0642 0.7039 0.6558 0.0422  0.1586  0.0330  82  HIS C CG  
1353 N ND1 . HIS C 82  ? 0.9775 0.6817 0.6231 0.0419  0.1388  0.0302  82  HIS C ND1 
1354 C CD2 . HIS C 82  ? 1.0853 0.7122 0.6577 0.0094  0.1744  0.0242  82  HIS C CD2 
1355 C CE1 . HIS C 82  ? 0.9648 0.6970 0.6232 0.0157  0.1411  0.0213  82  HIS C CE1 
1356 N NE2 . HIS C 82  ? 1.0264 0.7183 0.6439 -0.0066 0.1622  0.0163  82  HIS C NE2 
1357 N N   . LEU C 83  ? 1.2533 0.6906 0.6586 0.1409  0.2013  0.0670  83  LEU C N   
1358 C CA  . LEU C 83  ? 1.3022 0.6980 0.6578 0.1884  0.2074  0.0789  83  LEU C CA  
1359 C C   . LEU C 83  ? 1.2937 0.6667 0.6321 0.1994  0.2122  0.0796  83  LEU C C   
1360 O O   . LEU C 83  ? 1.2874 0.6943 0.6388 0.2370  0.1987  0.0843  83  LEU C O   
1361 C CB  . LEU C 83  ? 1.4117 0.7212 0.6889 0.1940  0.2341  0.0859  83  LEU C CB  
1362 C CG  . LEU C 83  ? 1.4921 0.7437 0.7009 0.2473  0.2456  0.0995  83  LEU C CG  
1363 C CD1 . LEU C 83  ? 1.4485 0.7682 0.6880 0.2928  0.2219  0.1054  83  LEU C CD1 
1364 C CD2 . LEU C 83  ? 1.6159 0.7613 0.7337 0.2467  0.2786  0.1064  83  LEU C CD2 
1365 N N   . GLU C 84  ? 1.3251 0.6457 0.6334 0.1674  0.2317  0.0737  84  GLU C N   
1366 C CA  . GLU C 84  ? 1.4092 0.6994 0.6951 0.1739  0.2393  0.0733  84  GLU C CA  
1367 C C   . GLU C 84  ? 1.3343 0.7108 0.6910 0.1843  0.2118  0.0708  84  GLU C C   
1368 O O   . GLU C 84  ? 1.3378 0.7105 0.6809 0.2166  0.2102  0.0755  84  GLU C O   
1369 C CB  . GLU C 84  ? 1.4902 0.7357 0.7530 0.1241  0.2599  0.0618  84  GLU C CB  
1370 C CG  . GLU C 84  ? 1.6551 0.7926 0.8274 0.1135  0.2952  0.0633  84  GLU C CG  
1371 C CD  . GLU C 84  ? 1.7640 0.8503 0.9020 0.0623  0.3201  0.0491  84  GLU C CD  
1372 O OE1 . GLU C 84  ? 1.7864 0.9318 0.9777 0.0320  0.3079  0.0371  84  GLU C OE1 
1373 O OE2 . GLU C 84  ? 1.9674 0.9524 1.0206 0.0522  0.3534  0.0493  84  GLU C OE2 
1374 N N   . ILE C 85  ? 1.2284 0.6775 0.6540 0.1584  0.1925  0.0633  85  ILE C N   
1375 C CA  . ILE C 85  ? 1.1514 0.6751 0.6401 0.1619  0.1694  0.0600  85  ILE C CA  
1376 C C   . ILE C 85  ? 1.1200 0.6851 0.6237 0.2023  0.1545  0.0658  85  ILE C C   
1377 O O   . ILE C 85  ? 1.0668 0.6642 0.5879 0.2199  0.1456  0.0655  85  ILE C O   
1378 C CB  . ILE C 85  ? 1.0990 0.6769 0.6442 0.1266  0.1566  0.0515  85  ILE C CB  
1379 C CG1 . ILE C 85  ? 1.1298 0.6884 0.6675 0.0903  0.1680  0.0430  85  ILE C CG1 
1380 C CG2 . ILE C 85  ? 1.0426 0.6906 0.6452 0.1357  0.1339  0.0502  85  ILE C CG2 
1381 C CD1 . ILE C 85  ? 1.0916 0.7006 0.6730 0.0596  0.1587  0.0346  85  ILE C CD1 
1382 N N   . VAL C 86  ? 1.1461 0.7152 0.6430 0.2153  0.1524  0.0695  86  VAL C N   
1383 C CA  . VAL C 86  ? 1.1404 0.7539 0.6469 0.2540  0.1393  0.0729  86  VAL C CA  
1384 C C   . VAL C 86  ? 1.1974 0.7869 0.6601 0.2951  0.1471  0.0793  86  VAL C C   
1385 O O   . VAL C 86  ? 1.1825 0.8333 0.6729 0.3172  0.1331  0.0766  86  VAL C O   
1386 C CB  . VAL C 86  ? 1.1437 0.7495 0.6341 0.2634  0.1407  0.0768  86  VAL C CB  
1387 C CG1 . VAL C 86  ? 1.1590 0.7966 0.6376 0.3104  0.1329  0.0811  86  VAL C CG1 
1388 C CG2 . VAL C 86  ? 1.0735 0.7234 0.6164 0.2311  0.1282  0.0695  86  VAL C CG2 
1389 N N   . GLU C 87  ? 1.2912 0.7944 0.6846 0.3045  0.1702  0.0864  87  GLU C N   
1390 C CA  . GLU C 87  ? 1.3809 0.8456 0.7164 0.3515  0.1816  0.0946  87  GLU C CA  
1391 C C   . GLU C 87  ? 1.3254 0.8201 0.6877 0.3487  0.1753  0.0893  87  GLU C C   
1392 O O   . GLU C 87  ? 1.3313 0.8745 0.7013 0.3862  0.1656  0.0901  87  GLU C O   
1393 C CB  . GLU C 87  ? 1.5130 0.8616 0.7602 0.3547  0.2123  0.1025  87  GLU C CB  
1394 C CG  . GLU C 87  ? 1.6200 0.9332 0.8231 0.3757  0.2211  0.1111  87  GLU C CG  
1395 C CD  . GLU C 87  ? 1.7520 0.9440 0.8686 0.3637  0.2548  0.1167  87  GLU C CD  
1396 O OE1 . GLU C 87  ? 1.8479 0.9861 0.9429 0.3313  0.2714  0.1113  87  GLU C OE1 
1397 O OE2 . GLU C 87  ? 1.8188 0.9694 0.8870 0.3847  0.2657  0.1254  87  GLU C OE2 
1398 N N   . VAL C 88  ? 1.2759 0.7510 0.6541 0.3053  0.1802  0.0829  88  VAL C N   
1399 C CA  . VAL C 88  ? 1.2345 0.7362 0.6396 0.2973  0.1747  0.0775  88  VAL C CA  
1400 C C   . VAL C 88  ? 1.1284 0.7319 0.6017 0.3048  0.1496  0.0722  88  VAL C C   
1401 O O   . VAL C 88  ? 1.1190 0.7523 0.5944 0.3306  0.1457  0.0718  88  VAL C O   
1402 C CB  . VAL C 88  ? 1.2139 0.6937 0.6338 0.2456  0.1807  0.0697  88  VAL C CB  
1403 C CG1 . VAL C 88  ? 1.2210 0.7294 0.6681 0.2384  0.1746  0.0646  88  VAL C CG1 
1404 C CG2 . VAL C 88  ? 1.2941 0.6752 0.6436 0.2311  0.2085  0.0710  88  VAL C CG2 
1405 N N   . LEU C 89  ? 1.0755 0.7293 0.5983 0.2831  0.1350  0.0676  89  LEU C N   
1406 C CA  . LEU C 89  ? 1.0267 0.7699 0.6093 0.2827  0.1145  0.0603  89  LEU C CA  
1407 C C   . LEU C 89  ? 1.0427 0.8256 0.6115 0.3296  0.1100  0.0617  89  LEU C C   
1408 O O   . LEU C 89  ? 1.0071 0.8496 0.6031 0.3380  0.1012  0.0554  89  LEU C O   
1409 C CB  . LEU C 89  ? 0.9621 0.7353 0.5841 0.2560  0.1039  0.0560  89  LEU C CB  
1410 C CG  . LEU C 89  ? 0.9316 0.6893 0.5763 0.2136  0.1046  0.0528  89  LEU C CG  
1411 C CD1 . LEU C 89  ? 0.9042 0.6846 0.5761 0.1968  0.0963  0.0500  89  LEU C CD1 
1412 C CD2 . LEU C 89  ? 0.9141 0.7032 0.5929 0.1972  0.0980  0.0474  89  LEU C CD2 
1413 N N   . LEU C 90  ? 1.0962 0.8512 0.6229 0.3593  0.1163  0.0689  90  LEU C N   
1414 C CA  . LEU C 90  ? 1.1563 0.9512 0.6616 0.4117  0.1125  0.0710  90  LEU C CA  
1415 C C   . LEU C 90  ? 1.1871 0.9736 0.6613 0.4451  0.1199  0.0739  90  LEU C C   
1416 O O   . LEU C 90  ? 1.1679 1.0356 0.6644 0.4701  0.1086  0.0673  90  LEU C O   
1417 C CB  . LEU C 90  ? 1.2166 0.9600 0.6680 0.4383  0.1225  0.0813  90  LEU C CB  
1418 C CG  . LEU C 90  ? 1.2027 0.9754 0.6865 0.4166  0.1124  0.0773  90  LEU C CG  
1419 C CD1 . LEU C 90  ? 1.2676 0.9829 0.6918 0.4440  0.1245  0.0885  90  LEU C CD1 
1420 C CD2 . LEU C 90  ? 1.1543 1.0363 0.6935 0.4204  0.0914  0.0649  90  LEU C CD2 
1421 N N   . LYS C 91  ? 1.2610 0.9568 0.6860 0.4428  0.1388  0.0814  91  LYS C N   
1422 C CA  . LYS C 91  ? 1.3639 1.0351 0.7505 0.4737  0.1492  0.0848  91  LYS C CA  
1423 C C   . LYS C 91  ? 1.2809 1.0349 0.7287 0.4587  0.1345  0.0736  91  LYS C C   
1424 O O   . LYS C 91  ? 1.2853 1.0755 0.7210 0.4977  0.1337  0.0729  91  LYS C O   
1425 C CB  . LYS C 91  ? 1.4809 1.0407 0.8154 0.4538  0.1721  0.0903  91  LYS C CB  
1426 C CG  . LYS C 91  ? 1.6194 1.0763 0.8720 0.4719  0.1948  0.1016  91  LYS C CG  
1427 C CD  . LYS C 91  ? 1.7133 1.0635 0.9155 0.4416  0.2197  0.1025  91  LYS C CD  
1428 C CE  . LYS C 91  ? 1.8320 1.0667 0.9347 0.4660  0.2483  0.1138  91  LYS C CE  
1429 N NZ  . LYS C 91  ? 1.8442 1.0766 0.9471 0.4585  0.2468  0.1170  91  LYS C NZ  
1430 N N   . HIS C 92  ? 1.1932 0.9737 0.6996 0.4058  0.1248  0.0654  92  HIS C N   
1431 C CA  . HIS C 92  ? 1.1203 0.9656 0.6811 0.3831  0.1138  0.0553  92  HIS C CA  
1432 C C   . HIS C 92  ? 1.0262 0.9733 0.6404 0.3803  0.0960  0.0445  92  HIS C C   
1433 O O   . HIS C 92  ? 1.0021 0.9995 0.6634 0.3515  0.0880  0.0348  92  HIS C O   
1434 C CB  . HIS C 92  ? 1.1212 0.9294 0.7036 0.3321  0.1162  0.0534  92  HIS C CB  
1435 C CG  . HIS C 92  ? 1.2066 0.9316 0.7402 0.3316  0.1340  0.0590  92  HIS C CG  
1436 N ND1 . HIS C 92  ? 1.2845 0.9248 0.7636 0.3329  0.1504  0.0661  92  HIS C ND1 
1437 C CD2 . HIS C 92  ? 1.2072 0.9178 0.7337 0.3281  0.1399  0.0574  92  HIS C CD2 
1438 C CE1 . HIS C 92  ? 1.3294 0.9054 0.7689 0.3278  0.1664  0.0673  92  HIS C CE1 
1439 N NE2 . HIS C 92  ? 1.2819 0.9006 0.7507 0.3262  0.1595  0.0623  92  HIS C NE2 
1440 N N   . GLY C 93  ? 1.0088 0.9835 0.6114 0.4090  0.0917  0.0452  93  GLY C N   
1441 C CA  . GLY C 93  ? 0.9835 1.0629 0.6272 0.4137  0.0768  0.0323  93  GLY C CA  
1442 C C   . GLY C 93  ? 0.9396 1.0401 0.6279 0.3694  0.0676  0.0247  93  GLY C C   
1443 O O   . GLY C 93  ? 0.9107 1.0911 0.6427 0.3511  0.0577  0.0099  93  GLY C O   
1444 N N   . ALA C 94  ? 0.9385 0.9710 0.6138 0.3518  0.0722  0.0330  94  ALA C N   
1445 C CA  . ALA C 94  ? 0.9339 0.9809 0.6440 0.3167  0.0644  0.0271  94  ALA C CA  
1446 C C   . ALA C 94  ? 0.9294 1.0461 0.6484 0.3365  0.0551  0.0188  94  ALA C C   
1447 O O   . ALA C 94  ? 0.9793 1.0978 0.6615 0.3811  0.0575  0.0246  94  ALA C O   
1448 C CB  . ALA C 94  ? 0.9469 0.9152 0.6351 0.3025  0.0721  0.0374  94  ALA C CB  
1449 N N   . ASP C 95  ? 0.8836 1.0549 0.6455 0.3056  0.0460  0.0050  95  ASP C N   
1450 C CA  . ASP C 95  ? 0.8862 1.1421 0.6643 0.3157  0.0367  -0.0091 95  ASP C CA  
1451 C C   . ASP C 95  ? 0.8842 1.1183 0.6549 0.3140  0.0343  -0.0060 95  ASP C C   
1452 O O   . ASP C 95  ? 0.8556 1.0717 0.6492 0.2759  0.0330  -0.0098 95  ASP C O   
1453 C CB  . ASP C 95  ? 0.8652 1.1874 0.6875 0.2785  0.0322  -0.0283 95  ASP C CB  
1454 C CG  . ASP C 95  ? 0.8859 1.2956 0.7290 0.2733  0.0243  -0.0477 95  ASP C CG  
1455 O OD1 . ASP C 95  ? 0.9066 1.3443 0.7313 0.3088  0.0199  -0.0466 95  ASP C OD1 
1456 O OD2 . ASP C 95  ? 0.8945 1.3409 0.7683 0.2326  0.0241  -0.0643 95  ASP C OD2 
1457 N N   . VAL C 96  ? 0.9230 1.1578 0.6592 0.3566  0.0346  0.0010  96  VAL C N   
1458 C CA  . VAL C 96  ? 0.9264 1.1298 0.6461 0.3610  0.0344  0.0071  96  VAL C CA  
1459 C C   . VAL C 96  ? 0.8869 1.1666 0.6408 0.3434  0.0234  -0.0111 96  VAL C C   
1460 O O   . VAL C 96  ? 0.8614 1.1197 0.6122 0.3357  0.0223  -0.0092 96  VAL C O   
1461 C CB  . VAL C 96  ? 1.0177 1.1884 0.6805 0.4146  0.0410  0.0217  96  VAL C CB  
1462 C CG1 . VAL C 96  ? 1.0704 1.1555 0.6924 0.4269  0.0555  0.0377  96  VAL C CG1 
1463 C CG2 . VAL C 96  ? 1.0449 1.3034 0.6995 0.4597  0.0334  0.0138  96  VAL C CG2 
1464 N N   . ASN C 97  ? 0.8890 1.2533 0.6734 0.3334  0.0172  -0.0294 97  ASN C N   
1465 C CA  . ASN C 97  ? 0.8867 1.3301 0.7030 0.3091  0.0092  -0.0518 97  ASN C CA  
1466 C C   . ASN C 97  ? 0.8365 1.2611 0.6851 0.2517  0.0119  -0.0616 97  ASN C C   
1467 O O   . ASN C 97  ? 0.8181 1.2977 0.6897 0.2233  0.0091  -0.0821 97  ASN C O   
1468 C CB  . ASN C 97  ? 0.9155 1.4703 0.7419 0.3297  0.0030  -0.0695 97  ASN C CB  
1469 C CG  . ASN C 97  ? 0.9510 1.5848 0.7803 0.3422  -0.0055 -0.0846 97  ASN C CG  
1470 O OD1 . ASN C 97  ? 1.0252 1.6226 0.8423 0.3442  -0.0066 -0.0782 97  ASN C OD1 
1471 N ND2 . ASN C 97  ? 0.9787 1.7267 0.8243 0.3505  -0.0114 -0.1059 97  ASN C ND2 
1472 N N   . ALA C 98  ? 0.8336 1.1836 0.6800 0.2358  0.0186  -0.0484 98  ALA C N   
1473 C CA  . ALA C 98  ? 0.8140 1.1353 0.6823 0.1884  0.0227  -0.0541 98  ALA C CA  
1474 C C   . ALA C 98  ? 0.7991 1.0911 0.6684 0.1701  0.0219  -0.0554 98  ALA C C   
1475 O O   . ALA C 98  ? 0.7822 1.0238 0.6333 0.1864  0.0223  -0.0404 98  ALA C O   
1476 C CB  . ALA C 98  ? 0.8257 1.0803 0.6874 0.1838  0.0289  -0.0388 98  ALA C CB  
1477 N N   . GLN C 99  ? 0.7973 1.1226 0.6839 0.1374  0.0224  -0.0744 99  GLN C N   
1478 C CA  . GLN C 99  ? 0.8366 1.1363 0.7230 0.1163  0.0233  -0.0792 99  GLN C CA  
1479 C C   . GLN C 99  ? 0.8158 1.0560 0.7044 0.0834  0.0316  -0.0768 99  GLN C C   
1480 O O   . GLN C 99  ? 0.8058 1.0613 0.7028 0.0600  0.0372  -0.0871 99  GLN C O   
1481 C CB  . GLN C 99  ? 0.8661 1.2384 0.7627 0.0997  0.0212  -0.1044 99  GLN C CB  
1482 C CG  . GLN C 99  ? 0.9027 1.3243 0.7923 0.1323  0.0122  -0.1064 99  GLN C CG  
1483 C CD  . GLN C 99  ? 0.9107 1.3954 0.8101 0.1078  0.0110  -0.1330 99  GLN C CD  
1484 O OE1 . GLN C 99  ? 0.9164 1.4443 0.8294 0.0738  0.0160  -0.1547 99  GLN C OE1 
1485 N NE2 . GLN C 99  ? 0.9537 1.4420 0.8439 0.1215  0.0060  -0.1328 99  GLN C NE2 
1486 N N   . ASP C 100 ? 0.7801 0.9575 0.6589 0.0833  0.0332  -0.0642 100 ASP C N   
1487 C CA  . ASP C 100 ? 0.7825 0.9060 0.6575 0.0573  0.0412  -0.0629 100 ASP C CA  
1488 C C   . ASP C 100 ? 0.7998 0.9350 0.6724 0.0300  0.0461  -0.0823 100 ASP C C   
1489 O O   . ASP C 100 ? 0.7944 0.9850 0.6726 0.0315  0.0416  -0.0962 100 ASP C O   
1490 C CB  . ASP C 100 ? 0.7720 0.8378 0.6373 0.0703  0.0409  -0.0442 100 ASP C CB  
1491 C CG  . ASP C 100 ? 0.7711 0.8330 0.6299 0.0835  0.0367  -0.0416 100 ASP C CG  
1492 O OD1 . ASP C 100 ? 0.7642 0.8557 0.6238 0.0768  0.0352  -0.0555 100 ASP C OD1 
1493 O OD2 . ASP C 100 ? 0.7706 0.8017 0.6225 0.0980  0.0359  -0.0272 100 ASP C OD2 
1494 N N   . THR C 101 ? 0.8284 0.9124 0.6886 0.0071  0.0561  -0.0838 101 THR C N   
1495 C CA  . THR C 101 ? 0.8740 0.9552 0.7226 -0.0253 0.0661  -0.1042 101 THR C CA  
1496 C C   . THR C 101 ? 0.8754 0.9530 0.7169 -0.0190 0.0626  -0.1077 101 THR C C   
1497 O O   . THR C 101 ? 0.9226 1.0010 0.7525 -0.0455 0.0708  -0.1267 101 THR C O   
1498 C CB  . THR C 101 ? 0.9174 0.9321 0.7440 -0.0474 0.0809  -0.1026 101 THR C CB  
1499 O OG1 . THR C 101 ? 0.9668 0.9216 0.7804 -0.0271 0.0801  -0.0829 101 THR C OG1 
1500 C CG2 . THR C 101 ? 0.9124 0.9358 0.7454 -0.0561 0.0850  -0.1012 101 THR C CG2 
1501 N N   . TRP C 102 ? 0.8453 0.9188 0.6911 0.0123  0.0524  -0.0915 102 TRP C N   
1502 C CA  . TRP C 102 ? 0.8180 0.8991 0.6594 0.0226  0.0475  -0.0941 102 TRP C CA  
1503 C C   . TRP C 102 ? 0.8053 0.9559 0.6595 0.0417  0.0367  -0.0986 102 TRP C C   
1504 O O   . TRP C 102 ? 0.7944 0.9556 0.6445 0.0550  0.0316  -0.0988 102 TRP C O   
1505 C CB  . TRP C 102 ? 0.7953 0.8255 0.6283 0.0432  0.0457  -0.0743 102 TRP C CB  
1506 C CG  . TRP C 102 ? 0.7878 0.7576 0.6017 0.0316  0.0556  -0.0728 102 TRP C CG  
1507 C CD1 . TRP C 102 ? 0.8153 0.7579 0.6119 0.0048  0.0679  -0.0860 102 TRP C CD1 
1508 C CD2 . TRP C 102 ? 0.7614 0.6890 0.5659 0.0487  0.0558  -0.0573 102 TRP C CD2 
1509 N NE1 . TRP C 102 ? 0.8304 0.7107 0.6033 0.0092  0.0757  -0.0778 102 TRP C NE1 
1510 C CE2 . TRP C 102 ? 0.7916 0.6688 0.5719 0.0370  0.0673  -0.0608 102 TRP C CE2 
1511 C CE3 . TRP C 102 ? 0.7185 0.6474 0.5295 0.0718  0.0490  -0.0422 102 TRP C CE3 
1512 C CZ2 . TRP C 102 ? 0.7887 0.6251 0.5535 0.0535  0.0699  -0.0491 102 TRP C CZ2 
1513 C CZ3 . TRP C 102 ? 0.7356 0.6303 0.5354 0.0818  0.0517  -0.0330 102 TRP C CZ3 
1514 C CH2 . TRP C 102 ? 0.7582 0.6111 0.5365 0.0756  0.0610  -0.0360 102 TRP C CH2 
1515 N N   . GLY C 103 ? 0.7805 0.9766 0.6466 0.0461  0.0338  -0.1016 103 GLY C N   
1516 C CA  . GLY C 103 ? 0.7710 1.0422 0.6447 0.0669  0.0248  -0.1088 103 GLY C CA  
1517 C C   . GLY C 103 ? 0.7658 1.0256 0.6315 0.1085  0.0180  -0.0873 103 GLY C C   
1518 O O   . GLY C 103 ? 0.8086 1.1211 0.6715 0.1341  0.0112  -0.0901 103 GLY C O   
1519 N N   . TYR C 104 ? 0.7640 0.9587 0.6223 0.1155  0.0210  -0.0674 104 TYR C N   
1520 C CA  . TYR C 104 ? 0.7660 0.9368 0.6098 0.1484  0.0191  -0.0477 104 TYR C CA  
1521 C C   . TYR C 104 ? 0.7681 0.9530 0.6110 0.1639  0.0193  -0.0420 104 TYR C C   
1522 O O   . TYR C 104 ? 0.7348 0.9139 0.5890 0.1458  0.0226  -0.0444 104 TYR C O   
1523 C CB  . TYR C 104 ? 0.7749 0.8789 0.6112 0.1440  0.0237  -0.0329 104 TYR C CB  
1524 C CG  . TYR C 104 ? 0.7802 0.8699 0.6132 0.1369  0.0236  -0.0361 104 TYR C CG  
1525 C CD1 . TYR C 104 ? 0.8170 0.9229 0.6390 0.1550  0.0200  -0.0358 104 TYR C CD1 
1526 C CD2 . TYR C 104 ? 0.7844 0.8426 0.6209 0.1150  0.0279  -0.0390 104 TYR C CD2 
1527 C CE1 . TYR C 104 ? 0.7980 0.8915 0.6165 0.1488  0.0202  -0.0391 104 TYR C CE1 
1528 C CE2 . TYR C 104 ? 0.7915 0.8346 0.6217 0.1116  0.0287  -0.0418 104 TYR C CE2 
1529 C CZ  . TYR C 104 ? 0.8069 0.8693 0.6301 0.1270  0.0245  -0.0423 104 TYR C CZ  
1530 O OH  . TYR C 104 ? 0.8231 0.8719 0.6400 0.1237  0.0254  -0.0457 104 TYR C OH  
1531 N N   . ILE C 105 ? 0.7539 0.9548 0.5791 0.1989  0.0168  -0.0347 105 ILE C N   
1532 C CA  . ILE C 105 ? 0.7727 0.9638 0.5840 0.2226  0.0196  -0.0236 105 ILE C CA  
1533 C C   . ILE C 105 ? 0.7722 0.8875 0.5586 0.2316  0.0269  -0.0041 105 ILE C C   
1534 O O   . ILE C 105 ? 0.7605 0.8459 0.5404 0.2261  0.0284  0.0002  105 ILE C O   
1535 C CB  . ILE C 105 ? 0.7857 1.0379 0.5841 0.2595  0.0148  -0.0278 105 ILE C CB  
1536 C CG1 . ILE C 105 ? 0.8233 1.0658 0.5918 0.2919  0.0140  -0.0193 105 ILE C CG1 
1537 C CG2 . ILE C 105 ? 0.7857 1.1246 0.6124 0.2427  0.0083  -0.0517 105 ILE C CG2 
1538 C CD1 . ILE C 105 ? 0.8352 1.1346 0.5827 0.3377  0.0099  -0.0207 105 ILE C CD1 
1539 N N   . PRO C 106 ? 0.7917 0.8741 0.5638 0.2408  0.0331  0.0063  106 PRO C N   
1540 C CA  . PRO C 106 ? 0.8228 0.8342 0.5685 0.2427  0.0429  0.0215  106 PRO C CA  
1541 C C   . PRO C 106 ? 0.8611 0.8456 0.5733 0.2639  0.0473  0.0299  106 PRO C C   
1542 O O   . PRO C 106 ? 0.8643 0.8080 0.5704 0.2487  0.0528  0.0350  106 PRO C O   
1543 C CB  . PRO C 106 ? 0.8438 0.8387 0.5726 0.2573  0.0487  0.0277  106 PRO C CB  
1544 C CG  . PRO C 106 ? 0.8064 0.8519 0.5710 0.2407  0.0417  0.0156  106 PRO C CG  
1545 C CD  . PRO C 106 ? 0.7735 0.8837 0.5562 0.2417  0.0325  0.0018  106 PRO C CD  
1546 N N   . PHE C 107 ? 0.9219 0.9336 0.6119 0.2994  0.0452  0.0305  107 PHE C N   
1547 C CA  . PHE C 107 ? 0.9448 0.9326 0.5967 0.3252  0.0499  0.0390  107 PHE C CA  
1548 C C   . PHE C 107 ? 0.9009 0.8938 0.5725 0.3020  0.0457  0.0337  107 PHE C C   
1549 O O   . PHE C 107 ? 0.9307 0.8724 0.5764 0.3009  0.0548  0.0430  107 PHE C O   
1550 C CB  . PHE C 107 ? 0.9861 1.0261 0.6195 0.3686  0.0442  0.0367  107 PHE C CB  
1551 C CG  . PHE C 107 ? 1.0130 1.0395 0.6108 0.3952  0.0469  0.0435  107 PHE C CG  
1552 C CD1 . PHE C 107 ? 1.0863 1.0374 0.6236 0.4219  0.0627  0.0610  107 PHE C CD1 
1553 C CD2 . PHE C 107 ? 1.0094 1.0904 0.6299 0.3900  0.0360  0.0321  107 PHE C CD2 
1554 C CE1 . PHE C 107 ? 1.1166 1.0488 0.6161 0.4461  0.0671  0.0683  107 PHE C CE1 
1555 C CE2 . PHE C 107 ? 1.0488 1.1165 0.6355 0.4146  0.0386  0.0388  107 PHE C CE2 
1556 C CZ  . PHE C 107 ? 1.1023 1.0958 0.6284 0.4436  0.0541  0.0576  107 PHE C CZ  
1557 N N   . ASP C 108 ? 0.8433 0.8936 0.5551 0.2832  0.0342  0.0183  108 ASP C N   
1558 C CA  . ASP C 108 ? 0.8212 0.8783 0.5504 0.2624  0.0302  0.0113  108 ASP C CA  
1559 C C   . ASP C 108 ? 0.8244 0.8229 0.5528 0.2396  0.0382  0.0196  108 ASP C C   
1560 O O   . ASP C 108 ? 0.8625 0.8390 0.5771 0.2404  0.0417  0.0239  108 ASP C O   
1561 C CB  . ASP C 108 ? 0.7936 0.9048 0.5608 0.2380  0.0212  -0.0074 108 ASP C CB  
1562 C CG  . ASP C 108 ? 0.8255 1.0115 0.5977 0.2544  0.0132  -0.0209 108 ASP C CG  
1563 O OD1 . ASP C 108 ? 0.8907 1.0923 0.6378 0.2879  0.0117  -0.0165 108 ASP C OD1 
1564 O OD2 . ASP C 108 ? 0.8077 1.0379 0.6061 0.2335  0.0094  -0.0366 108 ASP C OD2 
1565 N N   . LEU C 109 ? 0.7853 0.7645 0.5271 0.2207  0.0411  0.0211  109 LEU C N   
1566 C CA  . LEU C 109 ? 0.7686 0.7058 0.5120 0.1993  0.0479  0.0267  109 LEU C CA  
1567 C C   . LEU C 109 ? 0.7934 0.6815 0.4984 0.2092  0.0606  0.0387  109 LEU C C   
1568 O O   . LEU C 109 ? 0.8151 0.6826 0.5149 0.1969  0.0659  0.0407  109 LEU C O   
1569 C CB  . LEU C 109 ? 0.7539 0.6888 0.5177 0.1809  0.0477  0.0248  109 LEU C CB  
1570 C CG  . LEU C 109 ? 0.7264 0.6966 0.5202 0.1666  0.0396  0.0131  109 LEU C CG  
1571 C CD1 . LEU C 109 ? 0.7160 0.6749 0.5231 0.1502  0.0414  0.0136  109 LEU C CD1 
1572 C CD2 . LEU C 109 ? 0.7255 0.7008 0.5286 0.1560  0.0368  0.0069  109 LEU C CD2 
1573 N N   . ALA C 110 ? 0.8153 0.6824 0.4902 0.2296  0.0672  0.0457  110 ALA C N   
1574 C CA  . ALA C 110 ? 0.9052 0.7117 0.5311 0.2382  0.0838  0.0569  110 ALA C CA  
1575 C C   . ALA C 110 ? 0.9561 0.7555 0.5595 0.2510  0.0865  0.0600  110 ALA C C   
1576 O O   . ALA C 110 ? 1.0191 0.7790 0.6025 0.2361  0.0985  0.0638  110 ALA C O   
1577 C CB  . ALA C 110 ? 0.9566 0.7405 0.5470 0.2660  0.0907  0.0638  110 ALA C CB  
1578 N N   . ALA C 111 ? 0.9557 0.7980 0.5635 0.2754  0.0757  0.0566  111 ALA C N   
1579 C CA  . ALA C 111 ? 1.0000 0.8410 0.5831 0.2941  0.0770  0.0597  111 ALA C CA  
1580 C C   . ALA C 111 ? 0.9922 0.8408 0.6014 0.2659  0.0744  0.0539  111 ALA C C   
1581 O O   . ALA C 111 ? 0.9973 0.8061 0.5791 0.2612  0.0863  0.0602  111 ALA C O   
1582 C CB  . ALA C 111 ? 0.9852 0.8858 0.5734 0.3245  0.0641  0.0540  111 ALA C CB  
1583 N N   . TRP C 112 ? 0.9756 0.8685 0.6322 0.2465  0.0615  0.0423  112 TRP C N   
1584 C CA  . TRP C 112 ? 0.9484 0.8476 0.6294 0.2222  0.0592  0.0365  112 TRP C CA  
1585 C C   . TRP C 112 ? 0.9459 0.8031 0.6158 0.2026  0.0721  0.0425  112 TRP C C   
1586 O O   . TRP C 112 ? 0.9248 0.7758 0.5906 0.1944  0.0762  0.0424  112 TRP C O   
1587 C CB  . TRP C 112 ? 0.9184 0.8543 0.6411 0.2050  0.0479  0.0247  112 TRP C CB  
1588 C CG  . TRP C 112 ? 0.9041 0.8364 0.6438 0.1850  0.0480  0.0210  112 TRP C CG  
1589 C CD1 . TRP C 112 ? 0.8893 0.8353 0.6335 0.1843  0.0445  0.0152  112 TRP C CD1 
1590 C CD2 . TRP C 112 ? 0.8988 0.8142 0.6488 0.1668  0.0526  0.0231  112 TRP C CD2 
1591 N NE1 . TRP C 112 ? 0.9153 0.8527 0.6711 0.1692  0.0468  0.0142  112 TRP C NE1 
1592 C CE2 . TRP C 112 ? 0.8963 0.8189 0.6565 0.1590  0.0512  0.0187  112 TRP C CE2 
1593 C CE3 . TRP C 112 ? 0.9024 0.8013 0.6530 0.1576  0.0575  0.0273  112 TRP C CE3 
1594 C CZ2 . TRP C 112 ? 0.8943 0.8136 0.6651 0.1460  0.0541  0.0188  112 TRP C CZ2 
1595 C CZ3 . TRP C 112 ? 0.8774 0.7744 0.6401 0.1415  0.0600  0.0265  112 TRP C CZ3 
1596 C CH2 . TRP C 112 ? 0.9027 0.8124 0.6753 0.1375  0.0581  0.0225  112 TRP C CH2 
1597 N N   . ALA C 113 ? 0.9229 0.7576 0.5887 0.1937  0.0784  0.0459  113 ALA C N   
1598 C CA  . ALA C 113 ? 0.9346 0.7413 0.5946 0.1692  0.0903  0.0474  113 ALA C CA  
1599 C C   . ALA C 113 ? 0.9898 0.7471 0.6007 0.1706  0.1089  0.0548  113 ALA C C   
1600 O O   . ALA C 113 ? 1.0140 0.7568 0.6193 0.1458  0.1201  0.0527  113 ALA C O   
1601 C CB  . ALA C 113 ? 0.9192 0.7203 0.5888 0.1593  0.0911  0.0470  113 ALA C CB  
1602 N N   . GLY C 114 ? 1.0463 0.7789 0.6192 0.1985  0.1135  0.0624  114 GLY C N   
1603 C CA  . GLY C 114 ? 1.0982 0.7678 0.6106 0.2036  0.1350  0.0714  114 GLY C CA  
1604 C C   . GLY C 114 ? 1.1315 0.7484 0.6102 0.1967  0.1511  0.0755  114 GLY C C   
1605 O O   . GLY C 114 ? 1.1898 0.7512 0.6255 0.1789  0.1732  0.0779  114 GLY C O   
1606 N N   . ASN C 115 ? 1.1157 0.7494 0.6122 0.2072  0.1416  0.0749  115 ASN C N   
1607 C CA  . ASN C 115 ? 1.1507 0.7348 0.6131 0.2070  0.1557  0.0790  115 ASN C CA  
1608 C C   . ASN C 115 ? 1.2084 0.7592 0.6188 0.2526  0.1614  0.0901  115 ASN C C   
1609 O O   . ASN C 115 ? 1.1944 0.7731 0.6177 0.2762  0.1502  0.0905  115 ASN C O   
1610 C CB  . ASN C 115 ? 1.1099 0.7328 0.6202 0.1925  0.1430  0.0719  115 ASN C CB  
1611 C CG  . ASN C 115 ? 1.0634 0.7164 0.6156 0.1539  0.1391  0.0623  115 ASN C CG  
1612 O OD1 . ASN C 115 ? 1.0720 0.7018 0.6069 0.1290  0.1534  0.0597  115 ASN C OD1 
1613 N ND2 . ASN C 115 ? 1.0027 0.7086 0.6067 0.1493  0.1212  0.0563  115 ASN C ND2 
1614 N N   . GLU C 116 ? 1.3098 0.8058 0.6613 0.2662  0.1786  0.0986  116 GLU C N   
1615 C CA  . GLU C 116 ? 1.3814 0.8532 0.6796 0.3185  0.1825  0.1104  116 GLU C CA  
1616 C C   . GLU C 116 ? 1.4075 0.8353 0.6630 0.3440  0.1927  0.1174  116 GLU C C   
1617 O O   . GLU C 116 ? 1.4049 0.8705 0.6611 0.3877  0.1800  0.1205  116 GLU C O   
1618 C CB  . GLU C 116 ? 1.4867 0.8939 0.7218 0.3232  0.2036  0.1190  116 GLU C CB  
1619 C CG  . GLU C 116 ? 1.4828 0.9422 0.7564 0.3124  0.1907  0.1135  116 GLU C CG  
1620 C CD  . GLU C 116 ? 1.5794 1.0002 0.7943 0.3408  0.2027  0.1239  116 GLU C CD  
1621 O OE1 . GLU C 116 ? 1.7055 1.0419 0.8390 0.3641  0.2265  0.1365  116 GLU C OE1 
1622 O OE2 . GLU C 116 ? 1.6156 1.0868 0.8617 0.3409  0.1893  0.1197  116 GLU C OE2 
1623 N N   . ASP C 117 ? 1.4536 0.8114 0.6751 0.3166  0.2145  0.1177  117 ASP C N   
1624 C CA  . ASP C 117 ? 1.5350 0.8409 0.7119 0.3361  0.2272  0.1233  117 ASP C CA  
1625 C C   . ASP C 117 ? 1.4776 0.8653 0.7152 0.3518  0.2015  0.1178  117 ASP C C   
1626 O O   . ASP C 117 ? 1.5004 0.8779 0.7041 0.3965  0.2029  0.1250  117 ASP C O   
1627 C CB  . ASP C 117 ? 1.6027 0.8396 0.7529 0.2896  0.2511  0.1184  117 ASP C CB  
1628 C CG  . ASP C 117 ? 1.7389 0.8675 0.7995 0.2807  0.2863  0.1250  117 ASP C CG  
1629 O OD1 . ASP C 117 ? 1.7864 0.8994 0.8154 0.3043  0.2903  0.1333  117 ASP C OD1 
1630 O OD2 . ASP C 117 ? 1.8502 0.9096 0.8704 0.2486  0.3108  0.1210  117 ASP C OD2 
1631 N N   . ILE C 118 ? 1.3526 0.8154 0.6714 0.3174  0.1809  0.1054  118 ILE C N   
1632 C CA  . ILE C 118 ? 1.2649 0.8018 0.6416 0.3231  0.1590  0.0984  118 ILE C CA  
1633 C C   . ILE C 118 ? 1.2172 0.8265 0.6166 0.3597  0.1394  0.0973  118 ILE C C   
1634 O O   . ILE C 118 ? 1.1956 0.8447 0.6042 0.3866  0.1301  0.0960  118 ILE C O   
1635 C CB  . ILE C 118 ? 1.2040 0.7853 0.6488 0.2752  0.1472  0.0865  118 ILE C CB  
1636 C CG1 . ILE C 118 ? 1.2280 0.7592 0.6572 0.2438  0.1629  0.0845  118 ILE C CG1 
1637 C CG2 . ILE C 118 ? 1.0994 0.7635 0.6045 0.2813  0.1236  0.0788  118 ILE C CG2 
1638 C CD1 . ILE C 118 ? 1.1967 0.7470 0.6650 0.1965  0.1610  0.0752  118 ILE C CD1 
1639 N N   . ALA C 119 ? 1.1692 0.8037 0.5825 0.3564  0.1327  0.0954  119 ALA C N   
1640 C CA  . ALA C 119 ? 1.1962 0.9016 0.6282 0.3872  0.1153  0.0920  119 ALA C CA  
1641 C C   . ALA C 119 ? 1.2650 0.9605 0.6423 0.4447  0.1204  0.1014  119 ALA C C   
1642 O O   . ALA C 119 ? 1.2295 1.0024 0.6331 0.4694  0.1043  0.0944  119 ALA C O   
1643 C CB  . ALA C 119 ? 1.2069 0.9117 0.6370 0.3799  0.1150  0.0921  119 ALA C CB  
1644 N N   . GLU C 120 ? 1.3669 0.9694 0.6670 0.4644  0.1441  0.1157  120 GLU C N   
1645 C CA  . GLU C 120 ? 1.4741 1.0453 0.7016 0.5273  0.1543  0.1284  120 GLU C CA  
1646 C C   . GLU C 120 ? 1.4568 1.0458 0.6865 0.5473  0.1516  0.1272  120 GLU C C   
1647 O O   . GLU C 120 ? 1.4245 1.0678 0.6442 0.5983  0.1422  0.1280  120 GLU C O   
1648 C CB  . GLU C 120 ? 1.6058 1.0530 0.7439 0.5330  0.1855  0.1436  120 GLU C CB  
1649 C CG  . GLU C 120 ? 1.7423 1.1377 0.7902 0.6018  0.2005  0.1594  120 GLU C CG  
1650 C CD  . GLU C 120 ? 1.8707 1.1305 0.8197 0.6054  0.2356  0.1745  120 GLU C CD  
1651 O OE1 . GLU C 120 ? 1.9229 1.1546 0.8762 0.5650  0.2433  0.1725  120 GLU C OE1 
1652 O OE2 . GLU C 120 ? 2.0020 1.1827 0.8662 0.6484  0.2567  0.1876  120 GLU C OE2 
1653 N N   . VAL C 121 ? 1.4486 1.0027 0.6938 0.5084  0.1586  0.1239  121 VAL C N   
1654 C CA  . VAL C 121 ? 1.4234 0.9882 0.6718 0.5213  0.1576  0.1223  121 VAL C CA  
1655 C C   . VAL C 121 ? 1.3191 1.0087 0.6429 0.5244  0.1297  0.1084  121 VAL C C   
1656 O O   . VAL C 121 ? 1.3587 1.0877 0.6726 0.5652  0.1251  0.1083  121 VAL C O   
1657 C CB  . VAL C 121 ? 1.4324 0.9390 0.6867 0.4720  0.1700  0.1197  121 VAL C CB  
1658 C CG1 . VAL C 121 ? 1.4227 0.9533 0.6934 0.4793  0.1656  0.1158  121 VAL C CG1 
1659 C CG2 . VAL C 121 ? 1.5318 0.9138 0.7024 0.4676  0.2015  0.1306  121 VAL C CG2 
1660 N N   . LEU C 122 ? 1.2574 1.0061 0.6486 0.4842  0.1135  0.0964  122 LEU C N   
1661 C CA  . LEU C 122 ? 1.1847 1.0438 0.6473 0.4738  0.0904  0.0802  122 LEU C CA  
1662 C C   . LEU C 122 ? 1.1901 1.1242 0.6469 0.5190  0.0789  0.0765  122 LEU C C   
1663 O O   . LEU C 122 ? 1.1367 1.1541 0.6210 0.5345  0.0668  0.0659  122 LEU C O   
1664 C CB  . LEU C 122 ? 1.1148 0.9936 0.6356 0.4188  0.0814  0.0701  122 LEU C CB  
1665 C CG  . LEU C 122 ? 1.1154 0.9440 0.6511 0.3750  0.0891  0.0707  122 LEU C CG  
1666 C CD1 . LEU C 122 ? 1.0523 0.9017 0.6374 0.3308  0.0806  0.0621  122 LEU C CD1 
1667 C CD2 . LEU C 122 ? 1.1025 0.9531 0.6575 0.3722  0.0862  0.0663  122 LEU C CD2 
1668 N N   . GLN C 123 ? 1.2314 1.1440 0.6550 0.5379  0.0826  0.0833  123 GLN C N   
1669 C CA  . GLN C 123 ? 1.2919 1.2756 0.7023 0.5862  0.0725  0.0805  123 GLN C CA  
1670 C C   . GLN C 123 ? 1.3518 1.3391 0.7120 0.6472  0.0781  0.0885  123 GLN C C   
1671 O O   . GLN C 123 ? 1.3119 1.4057 0.7013 0.6697  0.0628  0.0756  123 GLN C O   
1672 C CB  . GLN C 123 ? 1.3342 1.2745 0.7046 0.5993  0.0794  0.0901  123 GLN C CB  
1673 C CG  . GLN C 123 ? 1.3777 1.4048 0.7445 0.6426  0.0660  0.0841  123 GLN C CG  
1674 C CD  . GLN C 123 ? 1.3994 1.3975 0.7441 0.6430  0.0693  0.0897  123 GLN C CD  
1675 O OE1 . GLN C 123 ? 1.3702 1.3404 0.7445 0.5936  0.0700  0.0864  123 GLN C OE1 
1676 N NE2 . GLN C 123 ? 1.5187 1.5262 0.8089 0.7019  0.0713  0.0982  123 GLN C NE2 
1677 N N   . LYS C 124 ? 1.4363 1.3123 0.7242 0.6692  0.1006  0.1072  124 LYS C N   
1678 C CA  . LYS C 124 ? 1.5653 1.4187 0.7876 0.7333  0.1112  0.1185  124 LYS C CA  
1679 C C   . LYS C 124 ? 1.5214 1.4445 0.7889 0.7288  0.1006  0.1066  124 LYS C C   
1680 O O   . LYS C 124 ? 1.5291 1.5033 0.7716 0.7862  0.0975  0.1072  124 LYS C O   
1681 C CB  . LYS C 124 ? 1.6810 1.3829 0.8167 0.7415  0.1416  0.1385  124 LYS C CB  
1682 C CG  . LYS C 124 ? 1.7859 1.4154 0.8569 0.7608  0.1563  0.1523  124 LYS C CG  
1683 C CD  . LYS C 124 ? 1.9362 1.4164 0.9025 0.7821  0.1902  0.1719  124 LYS C CD  
1684 C CE  . LYS C 124 ? 1.9659 1.3591 0.9382 0.7147  0.2067  0.1702  124 LYS C CE  
1685 N NZ  . LYS C 124 ? 2.1214 1.3678 0.9925 0.7190  0.2419  0.1861  124 LYS C NZ  
1686 N N   . ALA C 125 ? 1.4285 1.3583 0.7588 0.6655  0.0953  0.0960  125 ALA C N   
1687 C CA  . ALA C 125 ? 1.4075 1.3966 0.7837 0.6516  0.0866  0.0844  125 ALA C CA  
1688 C C   . ALA C 125 ? 1.3522 1.4831 0.7991 0.6416  0.0632  0.0626  125 ALA C C   
1689 O O   . ALA C 125 ? 1.3201 1.5156 0.7993 0.6391  0.0563  0.0516  125 ALA C O   
1690 C CB  . ALA C 125 ? 1.3829 1.3121 0.7876 0.5906  0.0929  0.0834  125 ALA C CB  
1691 N N   . ALA C 126 ? 1.3549 1.5317 0.8226 0.6338  0.0529  0.0553  126 ALA C N   
1692 C CA  . ALA C 126 ? 1.3171 1.6201 0.8511 0.6110  0.0332  0.0314  126 ALA C CA  
1693 C C   . ALA C 126 ? 1.3342 1.7409 0.8835 0.6394  0.0250  0.0183  126 ALA C C   
1694 O O   . ALA C 126 ? 1.3378 1.8140 0.8630 0.6940  0.0196  0.0158  126 ALA C O   
1695 C CB  . ALA C 126 ? 1.3480 1.6869 0.8733 0.6285  0.0263  0.0286  126 ALA C CB  
1696 O OXT . ALA C 126 ? 1.3267 1.7544 0.9121 0.6094  0.0238  0.0095  126 ALA C OXT 
# 
